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aspS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Magnetospirillum magneticum (strain AMB-1 / ATCC 700264)
Length
876 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
97.04 kDa
Sequence
MAATDTPWRPFRQAGALRRPMIDPAFVQGHPAYPDAFAQFFAGHGRYGHFAERVGNRNSRNGWRRRALAPGPAVGAEIVARHHEAAAQAGQGGDAARHQHRVDRLGQHHVRAAFEQVGRHFRLRGRSEHDRHRKGIVGADSPAHPPHQIARLLHAEIRVHHQKVDHFRPEVVFGIVAVVKAQQIPASQHAKGAGDDITAAEVEIAQQGAHTWGVVGHGLPSWQERTTFWPPAFRSPSDRSATSEFVAGLVNIGLSRLDKIWPGMPSSRFGFKRAYEGFMHVYRSHTCGQLKAADAGIQARLSGWVHRKRDHGNLLFVDLRDHYGITQCVIDVSSPVFAALDKARPESVITVTGKVVKRSAETINPRLPTGEIELQVAEVEIQSIADVLPIQVAGDQEYPEDMRLRYRFLDLRREDVHANMMLRSRVIAYLRQAMIGQGFTEFQTPILTASSPEGARDYLVPSRIHPGKFYALPQAPQQFKQLLMVAGFDKYFQIAPCFRDEAGRADRSPGEFYQLDFEMSYVTQDDVFAAIEPVLEGVFKEFGKGRAVTPAPFPRITYADSMLKYGSDKPDLRNPIIIADVTEPFRGSGFGLFAKLVDKGAVVRAIPAPGAAGQPRSWFDKLNDWARENGAGGLGYIQFAADGPKGPIAKNLEPARVEAIKAAANLKDGDAVFFACDKALPAAKFAGLVRTKIGNELDLLEKDVFKFCWTVDFPMYEINEETGLVEFSHNPFSMPQGGMDALLNQDPLTINAYQYDIVCNGVELSSGAIRNHRPDIMYKAFEIAGYSAAHVEEHFGGMLNAFKFGAPPHGGSAPGVDRIVMLLADQPNIREIILFPMNQQAQDLLMQAPAEIAMERLRELHIKVDLPKPKKEVKEG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100)
Length
642 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
72.343 kDa
Sequence
MPLVEGPLYRFCYGEYKNMVFDCNGTICKSGAHEQGRHMKFVKELKRTHYCGSLGVSQAGQKVVLMGWVDVRRDHGSLVFIDLRDREGIVQVVLDPNKAETASSKNLRGEFVLAVEGVVRARPDGMKNAKIKTGEVEVEAIRCEILNESAVPPFQVSDTNVNEMLRLKYRYLDLRSARLSSHLITRHKVAQLVRRFLSDNGFLEVETPILYKSTPEGARDYLVPSRVNPGHFYALPQSPQTLKQLLMISGYDRYFQIARCFRDEDLRADRQPEFSQIDMEMSYIDQEDIMEMNEKLLRTIWKEIKGIDVGAIPRMTYQEAMDRYGIDKPDTRFGVEIKDLKSIVTGSGFKVFDDVLARGGIVRGIAAPKGGSYSRGQLDKLTDMAKRAGAKGLVWIKSEADGTLSSSVSKFFSPEKLAEMFKACGGEAGDCALVVADDYDTACAALSTLRLHLGRELNLIDNSKYKFLWVVDFPLLEYSPDEKRWVARHHPFTSPKDEFAQDLVNNNEAAYGKMLAKAYDLVCNGYEMGGGSIRIYRNEIQQAMFRLLGMSEEETQHKFGFFLEALKYGTPPHGGIAWGMDRLVMLLCETDAIREVIAFPKTAKATDLMSDCPSEVNRDQLAEVGVRLSTLAEKHLEDLKKS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Salinibacter ruber (strain DSM 13855 / M31)
Length
629 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
70.304 kDa
Sequence
MERSSRADLISEDSHPARTHTCGDLRAEDNGEAVVLKGWVDTRRDHGGLVFVDLRDRYGLTQVVFSPQDNQTAYEVAGQLRREDVISVQGTVRPRGEEAVNPDLPTGAIEVSADDLAVLNTSETPPFVVSAHEERQMNTNEDLRLAHRYLDLRRPDLQENIELRHRLYQTTHRYFDAHDFLEVETPVLMKSTPEGARDFLVPSRLHPGRFYALPQSPQTYKQLLMVGGLDRYVQIVKCFRDEDLRADRQPEFTQIDVEMTFATEEQVYELTEGLMADLWDTLEDTTLETPFPRMTYDEALRTYGTDKPDLRFDLELHDVSDCFAGSGFRVFDSIVDDGGHIVALRVPGEGDRGRAAMDRLEDHVTDEIGAAGLIYFQLPSDGSGIEQNLSSDALPHEYGRAAAEQVGAEAGDLVLTLAGHSPTVFEQAGALRLHMGEELGLRPPADEGDDAFLWVTDFPLMEYDEEAGRPVSMHHPFTAPHPDDLDRLDEDPTQVQARAYDLVLNGNEIGGGSIRIHNHETQMQVFDVLGIDEEEAQDRFGFLLDALRYGAPPHGGIALGLDRLVMLLAGADSLRDVIAFPKTQSGKEPMVKSPDWVDPEQLETLALRLDLPPDVEPPARIAQRKRLAS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2)
Length
623 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
70.061 kDa
Sequence
MHRYRSHTCGDLRETDALQPTRLSGWCHRIRDHGGVLFIDLRDHYGITQCVVDPDSGAFPLAEKLRSEWVVRIDGLVRQRPAGTENIEMPTGLIEVYVTEIEVLGAAAELPLPVFGDQNYPEDMRLRYRFLDLRREKLHNNIMLRGRVIDSLRARMKGQGFFEFQTPILTASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLLMTAGFDRYFQIAPCFRDEDLRADRSLEFYQLDIEMSFVTQEDIFATVEPVLRGVFEEFGEGFAVTPEFPRIPYAETMLKYGTDKPDLRNPLVIVDVTEEFSREDVSFNAFKNVIKQGGVVRAIPAPGAGAQPRSFFDKLNDWARGEGAAGLGYVIFEGDAGALVGKGPIAKFLPADVQQAIAAKAGLKSGDAVFFACDRPDRAAKLAGAARLRIGSELKLSKTGVFELCWIVDFPMYEWNEDEKRIDFSHNPFSMPNCNLEQFLALETGVREEIVGIDRGERNRDLNESNELRKRILEITAFQYDVVCNGFELSSGAIRNHRPDIMRKAFALAGYDETVLEQKFGGMYRAFHYGAPPHGGIAPGVDRIVMLLAGEENLREIVAFPMNQRGEDLLLGAPSNVTAKQLRELSIKLNLPEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)
Length
623 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
69.423 kDa
Sequence
MHRYRSHTCGALSTAQVGEIVRLSGWCHRIRDHGGVLFIDLRDHYGLTQVVVDPDSAAFKDAEKVRAEWVIRIDGKVRLRPEGTENPDLATGAVEVYATELEVLGPSAELPLPVFGDVEYPEETRLRYRFLDLRREKLHRNIMTRGAIIDAMRSRMKGQGFFEFQTPILTASSPEGARDFLVPSRLHPGKFYALPQAPQQYKQLIMMSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVEQEDIFAAVEPVITGVFEQFAEGKPVTQKWPRIPYAESLRKYGTDKPDLRNPLVMQNVSEHFRGSGFKVFARMLEVEKNEVWAIPAPGGGSRAFCDRMNSWAQSEGQPGLGYIMWRDLSADAAAGGEKAVKDALEKSRGPGAGEGHVVEPGVVGAGPLANNIGPERTEAIRAQLDLKAGDAAFFVAGDPDKFVKFAGLARTRVGEELNLVDKDRFELAWIVDFPFYEYSEEEKKVDFSHNPFSMPQGGLDALNTQDPLSIKAFQYDIACNGYEIASGGIRNHRPEAMVKAFEIAGYDAQTVEERFGGMYRAFQYGAPPHGGMAAGVDRIVMLLCGVTNLREISLFPMNQQALDLLMGAPAEAAPKQLRELHIRPAPQAK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Cytophaga hutchinsonii (strain ATCC 33406 / NCIMB 9469)
Length
616 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
69.97 kDa
Sequence
MLRSQTCGELRISDVNKEVTLCGWVARVRDKGGMIWVDLRDRYGMTQLILEEGKSSAELLETSRKLGREFVIRATGNVIERVAKNPKMPTGDIEVKITALTILNESKTPPFLIEDETDGGDETRMKYRYLDLRRDAVRKNLELRHKVSRETRTYLDANNFLEVETPVLIKSTPEGARDFVVPSRMNPGQFYALPQSPQTFKQLLMVAGFDRYFQIVKCFRDEDLRADRQPEFTQIDCEMSFVEQEDILNMFEGLVRHLFKTVKEFDLPEVPRMLFADAMKYYGSDKPDIRFGMKFVELTDIVQSQGFQVFDEANLVVGINAEGCAEYTRKEIDALTEFVKRPQVGAKGMVWVRYAADGTLKSSVDKFYSADDLKKIAERFNAKPGDLMLILSGNGNKVRGQLNDLRLEIGSRLGLRPKDKFAALWVIDFPLLEFGEEEQRWFAMHHPFTSPKDIDAFMKLPFDQLGSVNANAYDLVINGVEVGGGSIRIYDRTVQNKMFEVLGFTEEEAKAQFGFLLEAFEYGAPPHAGLAFGFDRLCSIFGGVDSIRDFIAFPKNNSGRDVMIDSPSVIDDKQLKELSIDVKVADKGRIGIPNIIEETFNVKRDTSKDDHNITAN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Anabaena variabilis (strain ATCC 29413 / PCC 7937)
Length
614 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
70.073 kDa
Sequence
MGRLWHSLANLARKNKLTTMRTHYCGELRQKDIGETVTLYGWVDRRRDHGGVIFLDLRDRSGIVQVVSDPQRTPDSYELANSLRNEYVVEITGRVTQRPEESLNSRIPTGEVEIYADKIELLNGVRKQLPFQVSTADTETVREDLRLKYRYLDLRRDRMARNIQLRHQVVKAMRRYLEDVEGFIEVETPILTRSTPEGARDYVLPSRVNPGEWFALPQSPQLFKQILMVSGMDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFMSEEEIIQLNEKLVSYIFKTVKGVELPLPFPRLTYAEAMERYGCDKPDTRYDLQLVNVSDVMKDSGFKVFRDAVANGGIVKILPIPNGNEQISNVRIKPGGDLFREASEAGAKGLAYIRVREDGEIDTIGAIKDNLSEEQKQEILQRTGAKPGHLLLFGAGDAATVNKTLDRLRQAIAKEFGLIDPDKINLLWVVDFPMFEWNADEKRLEALHHPFTAPHPDDLHDLKTARAQAYDLVFNGFEVGGGSRRIYQREVQEQVFETIGLSPEEAQNKFGFLLEAFEYGTPPHGGIAYGLDRLVMLFAGEESIRDVIAFPKTQQARCLLTDAPSGVDVKQLKELHVASTYKPKS

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM)
Length
614 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
69.945 kDa
Sequence
MEKRTDYCGNITEKYIGQDVNLYGWVQRVRNLGNLVFIDLRDREGLVQIVVNKDSGKDLMEIANSLGNEYVIQVRGKVVKRSEANPDMKTGQVEVDATEIIILNEAKNPPFEIKDGVEISEQTRLKYRYLDLRRPEVQKAIILRSKILRATHEFFDENGFIDIETPILGKSSPEGARDYLVPSRIYPGSFYALPQSPQLFKQLLMGAGFDKYYQLARCFRDEDLRGDRQPEFTQIDMEMSFADEQTIQDYTEGLLKKIMKDVMGIDLKTPIKRMSWTDSMNKYGCDKPDTRYGMLIHDLSSIFKDSDFKVFSGAIADGGFVKGIAVKNGAKEYSRKKIDKKADFIKRFHAKGLAWVKFEDGEFSGPVARFLTDENKEALKKEFDLEGGELVVFVADKWKVVCDSLDHLRREFAKETGIIPKGVYDFVWVVDWPLFEYDEGLGRWVAAHHPFTMPDDEGVKLLTTDPHKAHARSYDIVMNGDEMGGGSIRIHKRSIQEDMFKALGFTKKRAYEQFGYLMDAFDMGFPPHAGLAIGLDRFAMMLAGKDNIRDVLAFPKNASASEPMMHAPAPVADQQLADLGIEVEKQYEDSVKATEERLEKMAAEDAEENSTWDK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Lactobacillus johnsonii (strain CNCM I-12250 / La1 / NCC 533)
Length
614 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
70.102 kDa
Sequence
MDKRTDYAGNITSKYEGQEVTLYGWVQRVRNLGNLVFIDLRDREGIVQVVVNKDSGEKLMEIADSLNNEDVIEVKGKVVKRSSVNPEMKTGEVEVDATEIDVLNKSKVPPFEIKDDINAAEQTRLKYRYLDLRRPTLQRAIILRSKILKAVHEYFDEQGFIDIETPILGKSSPEGARDYLVPSRIYPGSFYALPQSPQLFKQLLMGAGFDKYYQLARCFRDEDLRGDRQPEFTQIDMETSFLDEQGVQDYTEGLLKKIMKDVMNIDLKTPIKRITWDEAMNKYGSDKPDTRYEMYLHDLSPIFKDSDFKVFSGAIADGGVVKGIAVKNGAKEYSRKKIEEKQDYIKRYNAKGLAWVKYEDGEFSGPIARFLTDENKEALKKEFDLEGGELIVIVADKWKVVTDSLDHLRREFAHETGIIPEGVFDFVWVVDWPLFEYDEGLGRWIAAHHPFTMPDDEGIKLLDTDPHKAHARSYDIVMNGDEMGGGSIRIHKRSIQEKMFKALGFTKKRAYEQFGYLMDALDMGFPPHAGLAIGLDRLAMMLAGKDNIRDVTAFPKNASASEPMMHAPAPVADQQLADIGIEVEKQYEDSVKETEQRLEKEAQEDADKNSTWDE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rhodoferax ferrireducens (strain ATCC BAA-621 / DSM 15236 / T118)
Length
611 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.75 kDa
Sequence
MAMRSHYCGLVTDTLLGQTVTLCGWVNRRRDHGGVIFVDIRDREGYVQVVCDPDRADMFKVAEGLRNEFCIQVKGLVRARPEGTVNEGLKSGKIEVLCHELTVLNPSVTPPFQLDDDNLSETTRLTHRVLDLRRPYMQNNLMLRYRVAMEVRKFLDANGFVDIETPMLGKSTPEGARDYLVPSRVHEGHFFALPQSPQLFKQLLMVAGFDRYYQITKCFRDEDLRADRQPEFTQIDIETSFLSEQDIRDLFQEMITTVFKTTLNVDLGEFPVMAYSEAMHRYGSDKPDLRVKLEFTELTDVMTDVDFKVFSGAATMKGGRVVGLRIPGGAREVGGLSRGEIDAYAEFVKIYGAKGLAYIKVNELAKGPGDKALRWPGLQSPIVKNIHDKAIAEVLARTGAQDGDLIFFGADKAKIVNDAIGALRIKIGHSEFGKKNALFEKSWRPMWVVDFPMFEFDEEAQRYTAVHHPFTAPKEGHEDWMVTAPEKCISQGYDMVLNGWEMGGGSVRIHRADVQQKVFDALKISPEEAQDKFGFLLDALQYGAPPHGGLAFGLDRIITLMTGAESIRDVIAFPKTQRAQCLLTQAPSPVDEKQLRELHIRLRTPEPIKAA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Synechococcus sp. (strain WH7803)
Length
611 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.826 kDa
Sequence
MRSNGCGDLRKEHIDNSVQLCGWVDRRRDHGGVIFIDLRDRTGTVQITVDPDLGAEAFAVAEHLRSETVLQISGKVRARPAESLNEKLATGAVEVLASGITVLNSVKGNLPFPVSVHDEENTREELRLRHRYLDLRRKRMNDNLRLRAQTIQAARRFLEDEGFIEVETPVLTRSTPEGARDYVLPSRVCGGEWFALPQSPQLFKQLLMVGGIERYYQVARCFRDEDLRADRQPEFTQLDIEMSFMDQEEILQLNESLICSIWKAVKGIDLPRPFPRMTWHDAMERYGTDRPDTRYGMELTNVSDIVKDMGFKVFSGAVKNGGAVKCIAVPGGNEALSNVRIKPGGDVFSEAQKAGAGGLAFIRVRDGGEIDTIGAIKDNLSDEQKQELLSRTGAEPGTLLLFGAGDTATVNKALDRVRQYLAKELGMVKADRDNDQWNFLWVVDFPMFEFNSDENRYEALHHPFCAPNAEDLGSDASQWADTLPGARAQAYDLVLNGLELGGGSLRIHDSALQRQVLQTVGLPLEEAQEQFGFLMDALDVGAPPHGGLAFGVDRMVMLLAGEESIRDTIAFPKTQQARCLMTNAPGGVADKQLEELHVASTWVDPTEEDSN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Desulfovibrio vulgaris (strain Hildenborough / ATCC 29579 / DSM 644 / NCIMB 8303)
Length
610 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
69.282 kDa
Sequence
MSDQIADIQLEHQQYVAPLGDWQRTHSCCELTAADVGNDVCIMGWVQYRRDHGGLIFVDLRDRKGLTQVVFSPDFAPEAHKDAHIVRSEYVLAIRGRVRPRPEGMTNPGMKTGEIEVVVSEWKLLNTSKTPPFLIEDRTEASENLRLAWRYLDLRRPRMARNFMLRHRAAQSARRYLDELDFLEIETPYLTKATPEGARDFLVPSRLNHGMFYALPQSPQIFKQLLMVSGMDRYYQIVRCFRDEDMRADRQLEFTQIDIEMSFVDEERVMSMAEGLMSRVMKDTLGVDVTVPFPRMTYDQAMGEYGVDKPDTRFDLRLKDVTDAVRGSEFKLFAKAPLVKAMRVPGGETMTRKEIDEFTEFVKIYGAQGLAWIKIREGEWQSPIAKFLSEAERAALVAALGLEVGDIVFFQAGEPGMVNAALGNLRVKLGQHLGLIPEDTYNFLWVTDFPLFEYDEEEKRYVACHHPFTSPKDGHFDLMTSDPAAARARAYDMVLNGYELGGGSIRIHSAEVQRRMFAALGLDPQEAEEKFGFLIQALEHGAPPHGGIAFGMDRLVMLLTGSPSIRDVIAFPKTQKATCLMTQAPDAVSARQLRDLGIRLRETPQEQKPE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / JCM 7670 / NBRC 15755 / NCIMB 13165 / 161)
Length
610 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.805 kDa
Sequence
MLDFLGTKQRTHTCGELRAAHAGETITIMGWVNRRRDHGNLIFLDLRDRYGITQVVLDKDLSAEAHAKAEQARPEYVICATGKVRARSQEAINPKMPTGEIEIAATELLILNDSKVPPFSPAEEAIANEEVRLKYRYLDLRRPEMQHNFEVRHKVALAVRQYLSGQGFFEVETPFMTRSTPEGARDYLVPSRVHPGEFYALPQSPQLFKQILMISGMDRYFQIARCFRDEDLRADRQPEFTQIDLEMTFPQQETIFGVVEGFLAAAFEAVGQQITVPFPRMTYDKAIELYGIDKPDLRLPPMTDVRSVFSDEELQSLKIEPGMPIVAIVIPNKSAMSNTQKKAFGKEVEEQVGAELAYLDVERLRTSPQFALLADRIDAAAAAHCKLERVEPDHRLVVISPRLGAAAVSRDTSWVYKRAGQLRLELGKRFAAEHKAFEKKGTAADYQFLWVTDFPFFEWDEQSHTWTFAHHPFTSPHQDDLIAGRLESDQAAVRALAYDVVLNGTELGSGSIRIHRQDVQQQIFRALGMSDDEAKERFGFFLEALQYGTPPHGGIALGLDRIVMILAGASSLREVIAFPKTAKAIDLMVDAPTPVSDAQLRELHIRPTKQ

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Synechococcus sp. (strain WH8102)
Length
610 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.685 kDa
Sequence
MRSNGCGDLREQNIDQQVQLCGWVDRRRDHGGVIFIDLRDRSGTVQIKVDPDLGAEAFAVAEHLRSETVLQVAGKVRARPGESLNDKLATGAVEVLASGIIVLNNVKGNLPFPVSVHDEENTREELRLRHRYLDLRRKRMNDNLRLRAQTIQAARRFLEDEGFIEVETPVLTRSTPEGARDYVLPSRVCGGEWFALPQSPQLFKQLLMVGGIERYYQVARCFRDEDLRADRQPEFTQLDIEMSFMDQEEILQLNESLICSIWKAVKGIDLPRPFPRMTWHDAMERYGTDRPDTRYGMELTNVSDIVKDMGFKVFSGAVKSGGAVKCIAVPGGNDALSNVRIKPGGDVFSEAQKAGAGGLAFIRVRNGCEIDSIGAIKDNLSDEQKQELLSRTGAEPGTLLLFGAGDTATVNKALDRVRQYLAKELGMVKADQDNDQWNFLWVVDFPMFEFNSEENRYEALHHPFCAPNAEDLSSDASQWADTLPGARAQAYDLVLNGLELGGGSLRIHDSALQRQVLQTVGLPLEEAQEQFGFLMDALDVGAPPHGGLAFGVDRMVMLLAGEESIRDTIAFPKTQQARCLMTNAPGGVADKQLEELHVASTWVDPSGEDD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Synechococcus sp. (strain CC9902)
Length
610 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.72 kDa
Sequence
MRSNGCGDLRKDSIDAVVQLCGWVDRRRDHGGVIFIDLRDRSGTVQITVDPDLGAEAFAVAEHLRSETVLQVHGKVRARPAESLNDKLATGAVEVLASEIVVLNKVTGNLPFPVSVHDEENTREELRLRHRYLDLRRKRMNDNLRLRARTIQAARRFLEDEGFIEVETPVLTRSTPEGARDYVLPSRVCGGDWFALPQSPQLFKQLLMVGGIERYYQVARCFRDEDLRADRQPEFTQLDIEMSFMGEEQILQLNEDLICAIWKSVKGIELPRPFPRMTWHDAMERYGTDRPDTRYGMELVTVSDIVQDMGFKVFSGAVKSGGSVKVIAVPGGNDALSNVRIKPGGDVFSEAQAAGAGGLAFIRVRDGGEIDTIGAIKDNLSDEQKAELLKRTGATPGTLLLFGAGETAIVNKALDRVRQYLAKELNLVKPDRQNDAWNFLWVVDFPMFEFNSDENRYEALHHPFCAPNTDDLGSDPAQWATTLPKARAQAYDLVLNGLELGGGSLRIHDSALQRQVLQTVGLPLEEAQAQFGFLINALDMGAPPHGGLAFGVDRMVMLLAGEDSIRDTIAFPKTQQARCLMTDAPSSVAEKQLQELHVSSTWVDPAEDEN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Hyphomonas neptunium (strain ATCC 15444)
Length
609 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.648 kDa
Sequence
MHAYRTHTCGELRKSHVGETVKISGWLHRRRDHGGVMFIDLRDHYGLTQIVFNPGSPGFATVERLRAESVITVEGKVVARDAELVNANLGTGEIEVVGGAVSVQSEAAELPMPVFGDHSYPEEIRLKHRYLDLRREQLHKNMVLRSQVIASLRRRMVAEGFTEYQTPILTASSPEGARDFLVPSRLHPGEFYALPQAPQQFKQLLMVSGFDRYFQIAPCFRDEDARADRSPGEFYQLDIEMSFVTQEDVFNSIEPVMRGVFEEFADWEGKGRKVAEGPFVHIPYAEAMLKYGVDKPDLRNPILCSDVSDIMMRDDVTLAVFKKIVGGGGIVRAIPAPNSGDQPRSFFDKMDAWAKKEMQAPGLGYMRFVEENGALTATGPIAKFFEPAALAALAEKAGVKAGDALFFSAGDKTAAVRLQGQARIRVGEELGIIEPGVFRFCWIVDFPMYEWDEDNKKVDFSHNPFSMPQGGMEALLAADTVEKQLDLKAFQYDIVCNGVELSSGAIRNHRPEVMLKAFELAGYGPEVVEAKFGGMLNAFRYGAPPHGGIAPGVDRIVMLLAETDSLRDVILFPMNQQARDLLMGAPSPVDERQLKELNIRLAPVVKPQP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Synechococcus sp. (strain CC9605)
Length
609 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.598 kDa
Sequence
MRSNGCGDLREQNIDQQVQLCGWVDRRRDHGGVIFIDLRDRSGTVQITVDPDLGADAFTVAEHLRSETVLQVEGKVRARPGESLNDKLATGAVEVLASGITVLNSVKGNLPFPVSVHDEENTREELRLRHRYLDLRRKRMNDNLRLRAQTIQAARRFLEDAGFIEVETPVLTRSTPEGARDYLLPSRVCGGEWFALPQSPQLFKQLLMVGGIERYYQMARCFRDEDLRADRQPEFTQLDIEMSFMDQEQILELNESLICAIWKTVKGIELPRPFPRITWHDAMEHYGTDRPDTRYGMELTNVSDIVKDMGFKVFSGAVKAGGAVKCIAVPGGNDAVSNVRIKPGGDVFSEAQKAGAGGLAFIRVRDGGEIDTIGAIKDNLSDEQRQELLSRTGAEPGTLLLFGAGDTATVNKALDRVRQYLAKELGMVKADRDNDQWNFLWVVDFPMFEFNGDENRYEALHHPFCAPNAEDLGGDASKWSETLPGARAQAYDLVLNGLELGGGSLRIHDSTLQRQVLQTVGLTLEEAQEQFGFLMDALDVGAPPHGGLAFGVDRMVMLLAGEESIRDTIAFPKTQQARCLMTSAPGGVADKQLEELHVASTWVEPDQED

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Caulobacter sp. (strain K31)
Length
609 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.147 kDa
Sequence
MHAYRTHTCGALRASDTGASVRVSGWIHRKRDHGGLVFIDLRDHYGLTQLVLHPETPGFDVVERLRAESVIKIDGEVVARDAAAVNPNLPTGEIEIRVSAVEVLSEAAELPLPVFGEPDYPEEIRLKHRYLDLRRETLHKNIVLRSRVIQSIRSRMFAQGFNEFQTPILTASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLLMVSGFDRYFQIAPCFRDEDLRADRSLEFYQLDVEMSFVTQEDVFAAIEPVMHGVFEEFSAGKPVSPIDGVHTFTNDFGATLEHRGFERLTYAQSMAWYGSDKPDLRNPIKMQDVSEHFRDGGFGLFAKILGADPKNRVWAIPAPTGGSRAFCDRMNSWAQGEGQPGLGYAFFSKDQNGWGGPIAKNLGEGFQPIADQLGLTHDDAVFFVAGDPAVFAKFAGLARTRVGTELKLVDEEQFKFCWIVDFPMFEWNEDEKKVDFSHNPFSMPQGGLEALETQDPLTIRAYQYDIVCNGYELCSGAIRNHKPEIMLKAFEVAGYGAEVVEEQFGGMLNAFRYGAPPHGGLAPGIDRIVMLLAEQVAIREVIAFPLNQQGQDLLMNAPAEAQDRQYKELYIRSAPPIKV

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Caulobacter vibrioides (strain ATCC 19089 / CB15)
Length
609 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.988 kDa
Sequence
MHAYRTHNCGALRASDTGAAVRLSGWIHRKRDHGGLVFIDLRDHYGLTQLVLHPETPGFNVVERLRAESVIRVDGEVIARDASVVNPNLPTGEIEIRVSAVEVLSEAAELPLPVFGEPDYPEEIRLKHRYLDLRRETLHKNIVLRSRVIQSIRNRMFAQGFNEFQTPILTASSPEGARDFLVPSRLHPEKFYALPQAPQQFKQLLMVSGFDRYFQIAPCFRDEDLRADRSLEFYQLDVEMSFVTQEDVFAAIEPVMHGVFEEFSNGKPVSPINGTHTFTNDFGQSFEHKGFERLTYAQSMAWYGSDKPDLRNPIKMANVSEHFRDGGFGLFAKILGADAKNQVWAIPAPTGGSRAFCDRMNSWAQGEGQPGLGYVFWSEDQGGWGGPIAKNLGEPTQALMESLGLGAGDAAFFVAGDPAVFAKFAGLARTRVGTELKLVDENQFKFCWIVDFPMFEWNEEEKKVDFSHNPFSMPQGGLEALETQDPLTIRAYQYDIVCNGYELCSGAIRNHKPEIMLKAFATAGYGPEVVEEQFGGMLNAFRYGAPPHGGLAPGIDRIVMLLADQVAIREVIAFPLNQQGQDLLMNAPANVLDKQLKELHIRTAPPIKV

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Length
609 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.729 kDa
Sequence
MLRSHAAGLLREGDAGQQVTLAGWVARRRDHGGVIFIDLRDASGIAQVVFRDPQDTEVLAQAHRLRAEFCVSVAGVVEIRPEGNANPEIATGEIEVNATSLTVLGECAPLPFQLDEPAGEELRLKYRYLDLRRDDPAAAIRLRSRVNAAARAVLARHDFVEIETPTITRSTPEGARDFLVPARLHPGSFYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDMEMSFVDAEDIIAISEEVLTELWALIGYRIPTPIPRIGYAEAMRRFGTDKPDLRFGLELVECTDFFSDTTFRVFQAPYVGAVVMPGGASQPRRTLDGWQDWAKQRGHRGLAYVLVAEDGTLGGPVAKNLTEAERTGLADHVGAKPGDCIFFSAGPVKSSRALLGAARVEIANRLGLIDPDAWAFVWVVDPPLFEPADEATAAGEVAVGSGAWTAVHHAFTAPKPEWEDRIESDTGSVLADAYDIVCNGHEIGGGSVRIHRRDIQERVFAVMGLDKAEVEEKFGFLLEAFMFGAPPHGGIAFGWDRTTALLAGMDSIREVIAFPKTGGGVDPLTDAPAPITAQQRKESGIDAQPKRVQRHDQIFAVTTSHPSVNK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Psychrobacter arcticus (strain DSM 17307 / 273-4)
Length
608 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.231 kDa
Sequence
MTHSEYRDEYCGAVTESLIEQTISVVGWVHRRRDHGGVIFLDMRDRAGILQVVVDPDTPEAFATADAVRPEYVLKITGRVRRRYEGTENANMTSGHIELLAKEIEVLAKSETPPFPLNDEKSTVSEDLRLKYRYLDMRRPQMQDRMVFRAKATSAIRRYLDDHGFLDVETPILTRATPEGARDYLVPSRTRPGNFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQVDIETSFLNEEEIMNINEGLIKHVFKTMMDVEFEKFPRMTYAEAMRDYASDKPDLRIPLKLIDVADLMKDVDFKVFAGPANDPKGRVAALRIPGGASLSRKQIDAYTKFVGIYGARGLAYIKVNDASNINNGVDKESGLQSPIIKNMTDDVLVSLIERTGAESNDIIFFGADKASVVNDAIGALRQKIGLDLEMTTCEWAPLWVTDFPMFEETEDGRWTSMHHPFTKPKGSVEELKTNPESALSIAYDMVLNGTEVGGGSLRINTLEMQTAVFEALGIDDQEAEDKFGFLLDALKFGAPPHGGLAFGLDRLIMLMVGASSIRDVIAFPKTKTAECPLTQAPAEVNTKQLRELGIRVREKVQADTSKPAE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Psychrobacter cryohalolentis (strain K5)
Length
608 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.177 kDa
Sequence
MTHSEYRDEYCGAVTESLIEQTISVVGWVHRRRDHGGVIFLDMRDRAGILQVVVDPDTPEAFAIADAVRPEYVIKITGRVRQRYAGTENANMTSGHIELLAKEIEVLAKSETPPFPLNDEKSTVSEDLRLKYRYLDMRRPQMQDRMVFRAKATSAIRRYLDDHGFLDVETPILTRATPEGARDYLVPSRTRPGNFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQVDIETSFLNEEEIMNINEGLIKHVFKTMMDVEFEQFPRMTYAEAMRDYASDKPDLRIPLKLIDVADLMKDVDFKVFAGPANDPKGRVAALRIPGGASLSRKQIDAYTKFVSIYGARGLAYIKVNDASNINNGVDKESGLQSPIIKNMTDDVLVSLIERTGAESNDIIFFGADKASVVNDAIGALRQKIGLDLEMTTCEWAPLWVTDFPMFEETEDGRWTSMHHPFTKPKGSVEELKTNPESALSIAYDMVLNGTEVGGGSLRINTLEMQTAVFEALGIDDQEAEDKFGFLLDALKFGAPPHGGLAFGLDRLIMLMVGASSIRDVIAFPKTKTAECPLTQAPAEVNTKQLRELGIRVREKVQADTSKSAE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Corynebacterium glutamicum (strain R)
Length
608 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.053 kDa
Sequence
MLRTHLSGELRKENAGQSVTLTGWVNRRRDHGGVIFIDLRDRTGIAQVVFRNEDVAERAHALRSEFVLRVTGVVEERPEGSQNPNLASGDIEVSVTEFEVLNESAPLPFQIEDSSSAGEVGEETRLKYRYLDLRRPVQANALRLRSAANKAARTVLDSHDFTEIETPTLTRSTPEGARDFLVPARLRPGTFYALPQSPQLFKQLLQVAGMERYYQIARCYRDEDFRADRQPEFTQLDVEMSFVDQDDVIALGEEIISEVWKLIGYEIKTPIPRMTYADAMRRYGSDKPDLRFDIEITECTEFFQDTTFRVFKNEYVGAVVMTGGASQPRRQLDAWQEWAKQRGAKGLAYILVGEDGELSGPVAKNITDAERAGIAAHVGAQPGDCIFFAAGDTKSSRALLGAARGEIAKKLDLIKEGDWAFTWIVDAPMFEPAADATASGDVALGNSKWTAVHHAFTSPKPEFLDNFDTNPGDALAYAYDIVCNGNEIGGGSIRIHQRDVQERVFEVMGITGEEAREKFGFLLDAFAFGAPPHGGIAFGWDRIVSLLGGFDSIRDVIAFPKSGGGIDPLTDAPAAITPQQRKEAGIDAKPKPKAEAQAEAQAEESAEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / LMG 3730 / NCIMB 10025)
Length
608 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.01 kDa
Sequence
MLRTHLSGELRKENAGQSVTLTGWVNRRRDHGGVIFIDLRDRTGIAQVVFRNEDVAERAHALRSEFVLRVTGVVEERPEGSQNPNLASGDIEVSVTEFEVLNESAPLPFQIEDSSSAGEVGEETRLKYRYLDLRRPVQANALRLRSAANKAARTVLDSHDFTEIETPTLTRSTPEGARDFLVPARLRPGTFYALPQSPQLFKQLLQVAGMERYYQIARCYRDEDFRADRQPEFTQLDVEMSFVDQDDVIALGEEIISEVWKLIGYEIKTPIPRMTYADAMRRYGSDKPDLRFDIEITECTEFFQDTTFRVFKNEYVGAVVMTGGASQPRRQLDAWQEWAKQRGAKGLAYILVGEDGELSGPVAKNITDAERAGIAAHVGAQPGDCIFFAAGDTKSSLALLGAARGEIAKKLDLIKEGDWAFTWIVDAPMFEPAADATASGDVALGNSKWTAVHHAFTSPKPEFLDNFDTNPGDALAYAYDIVCNGNEIGGGSIRIHQRDVQERVFEVMGITGEEAREKFGFLLDAFAFGAPPHGGIAFGWDRIVSLLGGFDSIRDVIAFPKSGGGIDPLTDAPAAITPQQRKEAGIDAKPKPKAEAQAEAQAEESAEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Prosthecochloris aestuarii (strain DSM 271 / SK 413)
Length
608 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
69.789 kDa
Sequence
MSLAPGTETDLQNRFRSHFCGRLNTEYENKQVRLAGWIHRKRDHGGLIFIDLRDHTGIAQLIIQPEKQELFQKVERLHVESVIAVQGTVVKRSEETLNSRIPSGAIEVLVDDVQVESHAVALPFPVADELQTSEELRLTYRFLDLRREKIHQNIVFRSQLISKVRRYLEDHGFMEIQTPILTASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLLMVSGFPRYFQIAPCFRDEDARADRSPGEFYQVDMEMAFIEQDDLFEILEGMLRYLTETMSTKRITQFPFPRLSYRDVMNRFGSDKPDLRVPLEMQDVTELFVGSSFKVFASNTKEGSCIKAMVLKGRGTESRQFYDKAEKRARELGAPGLAYVQYREEGPKGPIVKFLSEAELSALQERLAIETGDVVFFGAGKWEKTCKIMGGIREYFSDLFELDRDELSFCWIVDFPLYEFDEKESRIDFSHNPFSMPQGEMDALDTMNPLDILAYQYDIVCNGIELSSGAIRNHRPDIMYRAFEIAGYSKEEVDKRFGHMIEAFKMGAPPHGGIAPGLDRLVMILRDEHNIREVIAFPMNQQAQDLMMSAPSDVSRLQLRELHLKLDLPVETAEQEPG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chlorobium phaeobacteroides (strain BS1)
Length
608 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
69.963 kDa
Sequence
MSAVAGTADSLQNRFRSHFCGRLHTEFENKTIAVAGWVHRIRDHGGLIFIDLRDHTGICQLIIQPEKEELFRKAEALHTESVICVSGVVVRRSEETVNPRLASGEIEVVVEDIRVESNASPLPFPVADELQTSEELRLKYRFLDLRREKIHENIHFRSRLISEVRRYLEERSFMEIQTPILTSSSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLLMVSGFSRYFQIAPCFRDEDARADRSPGEFYQIDMEMAFIEQDDLFEILEGMFKHLTEKMSNKRITQFPFPRISYKEVMNRYGSDKPDLRIPVEIEDVTELFVNSSFKVFAGNTKEGNCIKAMVLKGRGNESRQFYDKAERRAKELGSAGLAYIQYKEEGPKGPIVKFFSEDEMNDLKERLQIEAGDVVFFGAGKWERTCKIMGGMREYFSDLFELDRDELSFCWVVDFPMYEYDEAAKKIEFSHNPFSMPQGEMEALETMDPLDILAYQYDIVCNGIELSSGAIRNHRPDIMYRAFGIAGYEKAEVDKRFGHMIEAFNMGAPPHGGIAPGLDRLVMILRDEQNIREVIAFPMNQQAEDLMMAAPAEVSPLQLRELSLKLDLPKEEKKEKRS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Desulfotalea psychrophila (strain LSv54 / DSM 12343)
Length
607 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
69.037 kDa
Sequence
MSENVKKNWIKTIMESMGSLKRTHFCDALRKEDIGKQVILMGWVLRRRDHGGVIFIDLRDRRGITQVVFNPEINPEVHAKAHSLRSEWVLAIKGTVSARPGDMANTKLGTGDIEILVDELVILNTSETPPFPLDEETEVSENLRLQYRYLDLRRPAMARNLLLRHKAVQAIRNYLNDNEFLDIETPMLTRSTPEGARDYLVPSRVSAGKFYALPQSPQLFKQLLMIAGMDRYYQIVKCFRDEDLRADRQPEFTQIDMELSFVDEEQIIEVTEGMIQTLFKETLDLDLTPPFAHITYADSMERFGCDRPDMRFGMELVNLTEIAKSCSFKVFRAIAEEGGTVRAINAKACAHFSRKDLDGLTEYAALFGAKGLAWVKMKADGEWQSPIAKFFSEEERASIAEALDAQEGDLLFFGADSEKVVFQVLGELRLEMARRLDLLDKKEFNFVWVTDFPLMEYDEKEDRYQSIHHPFTAPREEDLDLLETAPDKALSRAYDLVLNGTEIGGGSIRIHQRDVQARVLTALGIDKEEADEKFGFLLRALELGAPPHGGLAFGLDRLMMLITGSDSIRNVIAFPKTQKAACLLTEAPATVARKQLTELYLRPDWKE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1)
Length
607 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.585 kDa
Sequence
MKRTHYCNDVRESQIGETVVLEGWINRRRDHGGVIFVDLRDRTGLVQVVFSPELFAEPHAQAHTLRSEYVIRATGKVTARSEGTINPNMDTGRIEVVVEDLTILNSSLPLPFQLDDEISENLRLQYRFLDLRRPDMQRNLMFRHRIMQSVRKHLDGSGFVEVETPMLTRSTPEGARDYLVPSRVNPGDFYALPQSPQLFKQLLMMAGYDRYFQIVRCFRDEDLRADRQPEFTQIDLEMSFVEPNDVMELTESVVVEAFKEALGVSIPQPVRRITYAEAMDKYGLDAPDMRITMELKDLTEVMKSSEFKVFRQAATLEGRGNEHGLVKVLKVPGGGSLTRKQIDTYTEFVGIYGAKGLAYIKVNGPWQEDGWQSPIVKFLGDAEKQAIQEATQAQVGDLLFFGADKASVVNESLGRLRVKLGKELEMLCDEKFAFVWVTDFPLLDWDNEARRNTAVHHPFTAPHPDDIIYLENADGASVEHPLEKVRSLAYDLVLNGTEVGGGSIRIHDTMLQRRMLELLEIGEEEAEGKFGFLLRALQYGAPPHGGLALGLDRLVTLMLGLDSIRDVIAFPKTQKATCLMTEAPSKVDGAQLKELHLRSTFKPKTAE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966)
Length
607 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.954 kDa
Sequence
MSSFRSHTSGELRKSHVGETVRLAGWVHRKRDHGGLLFIDLRDNYGLTQLVFDPDRAEAFALAEKLRAEYVVAIEGKVVARSAETINANLPTGDIEIAVSSMEVLSEAQDLPLPVFGEPDYPEDIRLTYRFLDLRRETLHRNILLRSKIIADIRRRMTEVGFNEFQTPILTASSPEGARDFLVPSRMHPGKFYALPQAPQQFKQLIMVAGFDRYFQIAPCFRDEDARADRSPGEFYQLDVEMSFVTQDDVFAAIEPVLHGLFEKFAEGKKVSSYPFTRIPYAEAIRKYGSDKPDLRNPIVMESVTDHFRGSGFKVFAGLIEKDSKVEVWAIPAPGGGNRAFCDRMNSWAQGEGQPGLGYIFFREEGGALEGAGPVAKNIGPERTEAIRTQLGLKAGDAVFFVAGVPAKTASFAGLARTRVGTELGLIEEDIFKFCWIVDFPMFEWNEDEKKIDFSHNPFSMPNYPLDKFLKLDKDNADEILGMTAFQYDIVCNGVELSSGAIRNHKPDVMYKAFEIAGYDKSVVETKFGGMLNAFKYGAPPHGGLAPGIDRMVMLLAGVENLREVTMFPMNQQAQDLLMQAPSEVEPKQLKELHIRVVPPLEKKKEG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Salinispora tropica (strain ATCC BAA-916 / DSM 44818 / CNB-440)
Length
607 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.462 kDa
Sequence
MIRTHDAGSLRATDAGSTVTLAGWVARRRDHGGVIFVDLRDGSGVAQVVLREEDAHVLRNEYCVRVTGEVTRRPEGNENPELATGEVEVTAEELEVLSEAAPLPLPVDDQIEAGDDVRLRYRYLDLRRSGPASALRLRSAANQIARTVLHERDFLEIETPTLTRSTPEGARDFLVPVRLQPGTWYALPQSPQLFKQLLMVGGMERYYQIARCYRDEDFRADRQPEFTQLDIEMSFVTEDDVIDLGEAIVSRLWRELAGHQITRPIPRITWHEAMARYGSDKPDLRYGVELTELTDYLRGTRFRVFAGAIEAGGYVGAVVMPGGAAQSRKELDGWQDWAKARGAKGLAYVVLDAETGEARGPVAKNLSTEHLAGLADVVGAKPGDAIFFAAGAESRAAQELLGAARVEIARRANLVDESAWAFCWVVDAPMFERVTDREEAGAGGWTAVHHPFTAPNAEWMDRFEEAPDRALAYAYDIVCNGNEIGGGSIRIHRGDVQQRVFDLLGITPEQARDKFGFLLEAFKYGPPPHGGIAFGWDRVCMLLAGADSIREVIAFPKTRGGFDPLTAAPTPITAAQRLEAGVDARPKPEARAQAGTAGPAAPVADPT

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Desulfovibrio alaskensis (strain G20)
Length
606 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.958 kDa
Sequence
MSDQNLDIQQDHQKYVESLGDWARTNTCGELNANAIGSEVCLMGWVQFRRDHGGLIFIDLRDRSGLTQVVFSPDVSVDAHERAHVLRSEYVLAVRGTVRPRPEGMVNPNMKTGEVEVYVSEWKLLNTSKTPPFQVEDRVEASENLRLEYRYLDLRRPRLARNFQLRHRATQAIRNYLDQLNFLEVETPYLTKSTPEGARDFLVPSRMNQGEFYALPQSPQIFKQLLMVAGMDRYYQIVRCFRDEDLRADRQPEFTQVDIEMSFVDEERVQSMAEGLMARVFKETLGIDVALPFPRMPYDQAIAEYGLDKPDTRFDLRLKDVTDILRGSGFRLFAKAELVKAMRVPGGAVLSRKEIDDFTEFVKVYGAQGLAWIKIKEDEWQSPIAKFLSDDERAALTTELGLETGDIVFFQAASPDVVNNSLGYLRLKVADRFGLIPENSYNFLWVTDFPLFEYSPEDKRYVACHHPFTAPQVGHEELMVSDPAKARARAYDLVLNGNEVGGGSIRIHSREAQEHMFRALGFDPQEAEEQFGFLMQALELGAPPHGGIAFGMDRLVMLLAGSASIRDVIAFPKTQKATCLMTHAPDQVAAKQLRELGIRLREKQEA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rhodospirillum rubrum (strain ATCC 11170 / ATH 1.1.1 / DSM 467 / LMG 4362 / NCIB 8255 / S1)
Length
606 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.611 kDa
Sequence
MHRYRTHTCEQLRPENVGETVRLSGWVHRKRDHGNLLFVDLRDHYGLTQVVCDVSSAVFKTLEAVRAESVVSVTGTVVARTAETANAKLPTGAIEVKAQTVEVLSQSEVLPMQVAGDQEYPEDMRLTYRFLDLRREDVHANMVLRSKVISSLRRRMTDQGFLEYQTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQFKQMLMVSGFDRYFQVAPCFRDEDSRADRSPGEFYQLDFEMSFVTQEDVFAAIEPVLVGVFEEFGGDRAVTPAPFPRIPYDEAMLKFGSDKPDLRNPLRNADVTEHFADGGFGLFSKQIALGSVVRAIPAPGAAGRPRGWYDKLNEWARESGAGGLGYVVFEEAGPKGPIAKNLEPERVEAIRQALDLKAGDSVFFACDKPLKAAKFSGLVRERICDDLGLRETGVFRFCWTVDFPMYEMNEETGQIEFSHNPFSMPQGEMEALETMDPLAIKAYQYDIVCNGIELSSGAIRNHLPEIMYKAFEIAGYPKEEVEARFGGMLRAFKFGAPPHGGSAPGIDRIVMLLADEPNIREVILFPMNGQAQDLLMQAPNTVSDKQLKELHIKLDLPKKALKVDKGEAAGDKAE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Corynebacterium urealyticum (strain ATCC 43042 / DSM 7109)
Length
606 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.637 kDa
Sequence
MLRTHLAGELRPGDIDSEVTLTGWVGRRRDHGGVIFIDLRDRSGVAQVVFRESEVAERAHALRSEYCVRVRGRVEARPEGSENPNLPSGAVEVNVSELEVLNESAALPFQIDDPSSAGEVGEETRLKYRYLDLRRASQGDALRLRSKANAAARKVLERHDFTEIETPTLTRSTPEGARDFLVPARLKPGTFYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDVEMSFVDQEDVIALAEEILTEVWSTAGYEVQTPFPRMTYADAMRLYGSDKPDLRFDIQITECTEFFKDTTFRVFQNEYVGAVVMDGGASQPRRQLDAWQEWAKQRGAKGLAYILVGEDGELSGPVAKNITDDERAGIADHVGAKPGDCIFFAAGDTKSSRALLGAARGEIAQKLGLIDDSKWAFTWVVDAPMFEPAADARAEGDVALGNSAWTAVHHAFTSPKPEFLDSFDQDPGSALAYAYDIVCNGNEIGGGSIRIHQRDVQERVFQVMGISQEEAREKFGFLLDAFAFGAPPHGGIAFGWDRIVSLLGGFDSIRDVIAFPKSGGGVDPLTDAPSEITPEQRKESGIDAKPKRAAAAQAGAAKASSK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Cutibacterium acnes (strain DSM 16379 / KPA171202)
Length
606 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.516 kDa
Sequence
MLRTHDAGTLRASDIGKGVTLAGWVGHRRDHGGVAFIDLRDASGLAQVVIRDEILESSGAHDLRNEYCIRVTGVVEARPEGNANPNLPTGEIEVAITELEVLNPSAPLPFQIDEHVSVGEDARLKYRYLDLRRPHQHEALVLRSHVTHAIREVLDRHNFYDIETPTLTRSTPEGARDFLVPARLAPGCWYALPQSPQLFKQLLMVSGMERYYQIARCYRDEDFRADRQPEFTQLDVEMSFVDQDDVIALAEETMAACWKIIGVDMPTPLPRITWHEAMDRYGSDKPDLRFGNEITEVTDFFANTAFRVFQAPYVGAVVMPGGASLPRRQFDAWQEWARTRGAKGLAYITISDEGVPEGPVAKNISEEEKAGIAEKVGAKPGDAIFFAAGSKTSSQELLGAARLEIGRRCELFDPSDWAFCWVVDAPLFKPTKEAEASGDVAVGTGAWTAVHHAFTSPTPDCLDTFDTDPGSALAYAYDFVVNGNEVGGGSIRIHRRDVQERVFNVMGIGPEEAQEKFGFLLDAFKFGAPPHGGIAFGLDRLVMLLGGFETIRDVIAFPKTGNGYDPLTAAPAPITPAQRREAGVDAKPKEPSGGQTSNAEAYKSTT

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Prochlorococcus marinus (strain MIT 9303)
Length
606 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.746 kDa
Sequence
MRSNSCGELRSKHIASNVQLCGWVDRCRDHGGVIFIDLRDRSGTIQITVDPDQGAELFASAESLRNETVLQITGLVRPRPADAINSKLSTGEIEVLADGLEVLNPVTGNLPFTVSIHDEEPVKEELRLRHRHLDLRRERMSRNLQLRHTTIKTARRFLEDEGFIEVETPVLTRSTPEGARDYLVPSRVCSGEWFALPQSPQLFKQLLMVGGLERYYQVARCFRDEDLRADRQPEFTQLDIEMSFMDQEQILKLNERLIATIWKAVKGIDLPLPFPRLTWHEAMDRYGTDRPDTRYGMELNDVSDILKDMGFKVFSGAIAAGGSVKCITVPNGNDLISNVRIKPGGDIFNEAQKAGAGGLAFIRVRDSDEIDSIGAIKDNLNSKQKTALLKQTGAKAGDLILFGAGKTATVNSALDRVRQFLGRELGLIPTDQDNKLWQFLWVVDFPMFELNAEENRLEALHHPFCAPNKDDLGNDPDAWMERLPQARAQAYDLVLNGLELGGGSLRIHNAELQRQVLQTIGLPLEEANQQFGFLIDALEMGAPPHGGLAFGMDRIVMLLTGEDSIRDTIAFPKTQQARCLMTQAPAGVSNHQLEELHVESTWVDPE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Prochlorococcus marinus (strain MIT 9211)
Length
606 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.669 kDa
Sequence
MRSNYCGALRNEHINSKVQLCGWVDRCRDHGGVIFIDLRDSSGTMQITVDPDQGTDLFNIAESLKNETVIQVTGKVRSRPEESINKKLETGQIEVLADVLKVLNPVYGNLPFAVSVHDDEPLKEEIRLKHRYLDLRRERMKKNLHLRHATIQTARNFLEEEGFIEVETPILTRSTPEGARDYLVPSRVCEGEWFALPQSPQIFKQLLMVGGIERYYQVARCFRDEDLRSDRQPEFTQLDMEMSFMSQEEILCLNERLIACIWKKIKGKDIKVPFPRLSWQESMDRYGTDRPDTRYGMELVDVSSIVKDIGFKVFSGAIQAGGSVKCIKVEEGNQSISNVRIKPGGDVFNEAQKAGAKGLAFIRVRVNNEIDTIGAIKDNLNNQQKNELLLKTKAKPGDLILFAAGDTEIVHKTLDKVRQFLAKELRLISTGKSKDQWNFLWVIDFPMFNFNKDEKRHEAMHHPFCAPNAKDIGGDPGLWEENLPKARAQAYDLVLNGLELGGGSLRIHNPELQQKVLETIGIAKDEATEQFGFLLNALEMGAPPHGGLAFGLDRIVMLLSEEDSIRDTIAFPKTQQARCLMAQAPNEVSKRQLKELHIASTWVDNE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Prochlorococcus marinus (strain MIT 9313)
Length
606 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.681 kDa
Sequence
MRSNGCGELRSKHIASNVKLCGWVDRCRDHGGVIFIDLRDRSGTIQITVDPDQGTELFASAESLRNETVLQITGLVRPRPADAINSKLSTGEIEVLANGLEVLNPVTGNLPFTVSIHDEEPVKEELRLRHRHLDLRRERMSRNLQLRHTTIKTARHFLEDEGFIEVETPVLTRSTPEGARDYLVPSRVCSGEWFALPQSPQLFKQLLMVGGLERYYQVARCFRDEDLRADRQPEFTQLDIEMSFMDQEQILKLNERLIAAIWKAVKGIDLPLPFPRLTWHEAMDRYGTDRPDTRYGMELNDVSDILKDMGFKVFSGAIAAGGSVKCITVPNGNDLISNVRIKPGGDIFNEAQKAGAGGLAFIRVRDSDEIDSIGAIKDNLNSKQKAALLKQTGAKAGDLILFGAGKTATVNSALDRVRQFLGRELGLIPTDQDNKLWQFLWVVDFPMFELNAEENRLEALHHPFCAPNKDDLGDDPDAWMERLPQARAQAYDLVLNGLELGGGSLRIHNAELQRQVLQTIGLPLEEAKQQFGFLIDALEMGAPPHGGLAFGMDRIVMLLTGEDSIRDTIAFPKTQQARCLMTQAPAGVSNHQLEELHVESTWVDPE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Prochlorococcus marinus (strain NATL2A)
Length
606 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.135 kDa
Sequence
MRNKTCGELRASAISANVQLCGWVDRRRDHGGVIFIDLRDRSGTIQITVDPDQGQDLFSIAESLRNETVLQINGLVRARPDEAINTKIPTGEVEVLAKNIKILNTVTSTLPFSVSIHDEESVKEEIRLKHRYLDLRRERMNNNLRLRHNTVKAARSFLENEGFIEVETPILTRSTPEGARDYLVPSRVCGGEFFALPQSPQLFKQLLMVGGVERYYQVARCFRDEDLRADRQPEFTQLDIEMSFMEEKEIIELNEKLIVSIWKKIKGIDLQTPFPRMTWQEAMDRFGTDRPDTRYGMELVNTSDLFSKSGFKVFSNAISSGGCVKCITIEDGNNLISNVRIKPGGDIFSEAQKAGAGGLAFIRVRDDKEVDTIGAIKDNLTTSQIKELLLKTQAKPGDLILFGAGPTNIVNRTLDRVRQFIAKDLKIISDNELKTQWNFLWVTDFPMFEFNSDENRLEAIHHPFCAPKPEDIGESESLWKDKLPNSNAQAYDLVLNGLEIGGGSLRIHNSELQKTVLEVIGLSKNEAEEQFGFLIDALAMGAPPHGGIAFGLDRIVMLLANEDSIRDTIAFPKTQQARCSMAKAPANVENKQLEDLHIASTWIDPD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chlorobium phaeobacteroides (strain DSM 266)
Length
606 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.832 kDa
Sequence
MSRAAGSTETLKNRFRTDYCGLLNPEVEHQSVKLGGWVHRKRDHGGLIFIDLRDHTGICQIVIQPEEQQLFAKAEQLHLESVICIEGTVVRRSPGAVNPRIPSGEIEVVAAGISVESSAHPLPFPVADEVQTSEELRLKYRFIDLRRDKIHENIIFRSRLTAAIRRYLEEKSFIEIQTPILTSSSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLLMVSGFPRYFQIAPCFRDEDARADRSPGEFYQLDMEMAFIEQDDLFEILEGMFSHLTGSMSTKRIREFPFPRISFRDVMNRYGTDKPDLRIPLEISDVTHLFLQSSFKVFAANTKEGCCVKAMLVKGRGNESRLFYDKAEKRAKELGSGGLAYIQFREDGPKGPLVKFLSGEELAALRELLGVEVGDVVFFGAGKWEQTCRIMGGMRTYFSDLFTLDRDELAFCWVVDFPMYEYNEDQKKIDFSHNPFSMPQGEMDALESMPPLNILAYQYDIVCNGIELSSGAIRNHRPDIMYKAFEIAGYTKEDVDSRFGHMIEAFKLGAPPHGGIAPGLDRLVMILRDEQNIREVIAFPMNQQAQDLMMGSPSEVTPIQLRELHLQVELPKKAEAKP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CN-1)
Length
606 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.878 kDa
Sequence
MLRTHLAGELRKEMAGETVTLTGWVARRRDHGGVIFIDLRDRSGVAQVVFRESEVAERAHDLRSEYCVKVTGVVEPRPEGSANANLASGEIEVNVSDLEVLNKSAALPFQIDDPSSSGEVGEETRLKYRYLDLRRERQHEALRLRSAANRAAREVLDSHDFTEIETPTLTRSTPEGARDFLVPARLKPGSWYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDVEMSFVDQDDVIALAEEIVSALWKLIGYEIKTPIPRMTYADAMKYYGSDKPDLRFDIKIVECTEFFKDTTFRVFQNEYVGAVVMEGGASQPRRQFDAWQEWAKQRGAKGLAYITIAEDGTLGGPVAKNITDAEREGIAEHVGAKPGDAIFFAAGDVKSSRALLGAARGEIAKKLDLIKDGDWAFTWVVDAPLFEPAADATASGDVALGHSKWTAVHHAFTSPKPEYLDSFDENPGEALAYAYDIVCNGNEIGGGSIRIHDQDVQKRVFDVMGIGEEEAQEKFGFLLDAFQFGAPPHGGIAFGWDRIVSLLGGFDSIRDVIAFPKSGGGVDPLTDAPGTIPAEQRKETGVDFKPEKAAKAAQGEKAGKES

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL 2338)
Length
606 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.92 kDa
Sequence
MMRTHEAGSLRAGHAGQSVTLAGWVARRRDHGGVIFIDLRDASGVAQVVFREGEMAERAHRLRSEFCLRITGEVVRRPEGNENPEIGTGDIEVTATELEVLSESAPLPFPLDEHLEVGEETRLRHRYLDLRRNGPAKAMRMRSEVNRIARDVLHGRDFVEVETPTMTRSTPEGARDFLIPARLQPGNWYALPQSPQLFKQLLMVGGLERYFQIARCYRDEDFRADRQPEFTQLDIEMSFVDQDDVIELGEEIISALWRETAGHEIPRPIQRMTYADAMARFGTDKPDLRFGLELTEMTEYFADTPFRVFRAPYVGAVVMPGGADQPRRQLDAWQDWAKQRGAKGLAYVLVGQDGTLSGPVAKNLSDGERDGLVKAVGAAPGDCVFFAAGDRSSSRALLGAARLEIGERCGLIDHDAWSFVWVVDAPMFESIDDTDDVAVGSGRWTAVHHPFTSPNADWVDNFESDPANALAWAYDIVCNGNEIGGGSIRIHRSDVQKRVFELLGISEEQAQDKFGFLLEAFKYGPPPHGGIAFGWDRICMLLAGADSLRDVIAFPKSGGGYDPLTGAPSPITVEQRKEAGVDAKPAAKVGDESISVFPPGVVEKQG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Ralstonia solanacearum (strain GMI1000)
Length
605 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.957 kDa
Sequence
MRTQYCGQVTEQLLGQSVTLSGWAHRRRDHGGVIFIDLRDREGLVQVVCDPDRPEMFKVAEGVRNEFCLQVKGIVRARPEGTTNPNLASGKIEVLCHELTVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQYNLRLRYKVAMEVRKYLDDKGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQMLMVSGFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLSEQEIRDLFEEMIRTVFQNTMSVALDAKFPVMEFREAMARFGSDKPDLRVKLEFTELTDAMKDVDFKVFSGPANAEGGRVVALRVPGGAALSRGDIDAYTKFVEIYGAKGLAWIKVNEVAKGRDGLQSPIVKNLHDAAIAEILKRSGAQDGDILFFGADRAKVVNDAMGALRLKVGHSDFAKSTGLFEDAWKPLWVVDFPMFEYDEEDARWVAMHHPFTSPKDEHLEYLETDPGKCIAKAYDMVLNGWEIGGGSVRIYREEVQSKVFRALKIGDEEARAKFGFLLDALQYGAPPHGGIAFGLDRVVTMMAGADSIRDVIAFPKTQRAQDLLTQAPSPVDEKQLRELHIRLRAAEAKVAAPAAATA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Heliobacterium modesticaldum (strain ATCC 51547 / Ice1)
Length
605 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.46 kDa
Sequence
MMIDMFTGLKRSHRGGDLRIDHAGQTVTLMGWVQRRRDHGGLIFVDLRDRSGLVQVVFSPEVGKEAFTKAEDVRNEYVLAVTGDVRPRPEGTVNANLPSGQIDVYARQLWVLNSAKTPPFYIEDGVDVDETVRLKYRYLDLRRPEMQRNLIIRHKTAKAMRDFLDRNGFLEIETPMLTKSTPEGAREFMVPSRIHPGEFFVLPQSPQLYKQILMVAGMERYFQIVRCFRDEDLRADRQPEFTQLDIEMSFTQMDDLLTLMEEMVAHIFKEALGKEISTPFRRIPYAEAMGRFGSDKPDLRFGLELIDLTETVKDVEFKVFASVVKGGGEVKAINAKGCAHFSRKEIDDLTKGVAVYGAKGLAYIQMTEEGPKSPIAKFFTDEQLNAVLDRLGAEKGDLLLFVADKPSVVAASLGFLRQELARRLNLIDSEKLEFAWVVDFPLVEYDPEEKRYNAIHHPFTAPKDEDLDLLDKEPGKVRAKAYDLVLNGVELGGGSLRIYRRDIQEKMFAILGLTAEEAYQKFGFLLDAFDYGTPPHGGIAFGLDRMIMLMTGRDTIRDVIAFPKTQSASDMMVDAPSAVTPRQLKELHIKLDLPVKAPKAEPAKK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Thermosynechococcus elongatus (strain BP-1)
Length
605 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.202 kDa
Sequence
MRTHYCGDVRLRDVGTTVTLYGWVDRRRDHGGVIFIDLRDRSGIVQIVSDPQRTPDAYPQAERLRSEYVVKVVGRVSKRPADSVNPKLATGDIEIYADGIEVLNTVRQQLPFAISSTENEEVREEVRLRYRYLDLRRERMARNLRLRHRVVQAMRRFLEDEAGFIEVETPILTRSTPEGARDYLVPSRVNPGEWFALPQSPQLFKQLLMVAGCDRYYQIAHCFRDEDLRADRQPEFTQLDMEMSFMDQEEILDLNEALICHIFKTVKGIELPRPFPRLSYQEAMDRYGTDKPDTRYGLELVDVSDILKDSGFKVFSGAIAQGGVVKILPIPNGSDRISNVRIKPGGDLFQEATTAGAKGLAYIRVRNNGEIDTIGAIKDNLSPEQKALLLERTGAQPGHLLLFGAGETATVNKTLDRLRQTIAREFNLIDPTATHLLWVVDFPMFEWNAEEKRLEALHHPFTAPHPEDLGDLKTARAQAYDLIFNGHEVGGGSLRIHQPELQRQVFEIIGIDEATAQEKFGFLLEAFEFGTPPHGGIAYGLDRLVMLLAGADSIRDTIAFPKTQQARCLLTGAPSSVEPQQLKELHVTPAKPAKTTAKTKPRPAD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Maricaulis maris (strain MCS10)
Length
605 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.259 kDa
Sequence
MHAYRSHTCAELRKAHVGQTARISGWIHRKRDHGGLLFIDLRDHYGLTQVVLEPESPHFATLERLRVESVITVTGEVIARSDETVNANLPTGEIEVRLAELAIQSEAEELPLPVFGEPDWSEEVRLKHRYIDLRRESLHKRIVLRSKIIDSLRRRMVDENFVEYQTPILTASSPEGARDFLVPSRVHPGKFYALPQAPQQFKQLIMVSGFDRYFQIAPCFRDEDARADRAPGEFYQLDMEMSFATQQDVFDVIEPVMKGLFDEFADGRTVPDEPFVQIAYKDAMSWYGSDKPDLRNPIKMSDASETFRGSGFKVFAGMLERNPKVQVWAIPAKTGGSRAFCDRMNSWAQKEGQPGMGYIFWREAEGGLEAAGPIAKNIGEERTEALRVELGLEAGDACFFAAGDPREFAGFAGRARDVVGAELDLCEKDTFRFCWIVDFPMYEWDEDNKKIDFSHNPFSMPQIDPDDFLKLDADTDADTLLALKAYQYDIVCNGVELSSGAVRNHRPDVMLKAFAFAGYDAATVEEEFGGMLNAFRYGAPPHAGVAPGVDRMIMLLAGVENLREVVMFPKDQQARDLMMNAPAEVELKQLRELHIRTVVPDAKKG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Persephonella marina (strain DSM 14350 / EX-H1)
Length
605 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
69.189 kDa
Sequence
MIDKLGDFKRDYFCGELTENNIGDEVRLLGWADSVRDHGGVIFINLRDKEGIIQVVIDPSKSPKEAYEKAKKVRSEYVLAVRGRVQRRPAGTENPKLPTGTIEIAVDELRILNTCDILPFPIEDGISAHEEVRLRYRFLDIRRPEMMKKLILRHEVYQATREYLAGHGFLEVETPMLTKSTPEGARDFLVPARLEKGKFYALPQSPQLFKQILMVSGIDRYFQIVKCFRDEDLRKDRQPEFTQIDFEMSFVDEEDVITVSEGLIHYIFKKVLGIELKLPFKRMSYTEAIERYGTDKPDLRYSLELKDITDIAKDVQFKVFKDTVEKGGIVKGINVKGGSKFSRKEIDDLTEEAKKYGAKGMAWIKINEDGSLQSPIVKFFTEEQINKIKEIMEGENGDLLIFIADSYEITHRVLGFLRKHLAEKLKLIPENVWEFVWVVDFPLVEWDEEEGRLVALHHPFTSPKEEDIDRLDEAIQDKKVALSFRSRAYDLVLNGEEIGGGSIRIHSSHIQKKVFELLGISDEEAEEKFGFLINALKYGAPPHGGLAFGLDRIVALMTGSESIRDVIAFPKTQKGICPLTDAPDFVQEDQLEELGIEVNIPEETV

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Prochlorococcus marinus (strain SARG / CCMP1375 / SS120)
Length
605 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.431 kDa
Sequence
MRSNYCGELRKKHINSNVQLCGWVDRRRDHGGVIFIDLRDRTGTIQITIDPDQGSELFTVAENLRNETVVQISGTIRARPSESCNQKLKTGEIEVLANHLEVLNQIQGNLPFSISVHDDEPIKEELRLRHRYLDLRKDRMTKNLRLRHEVLKTARNFLEQENFLEVETPILTRSTPEGARDYLVPSRVCEGDWFALPQSPQLFKQLLMVGGIERYYQIARCFRDEDLRSDRQPEFTQLDIEMSFMSQEEILGLTEKLISSIWKSVKGVDLVHPFPRLTWQESMDRFGTDRPDTRYGMELKNVSQILKGIGFKVFSGAIDAGGSVKCITITGGNQLISNVRIKPGGDIFSEAEKAGAKGLAFIRVRGNGEIDTIGAIKDNLNIAQKEELLKQTNANEGDLILFAAGDTTTVNKTLARLRQFLAKDLDLIPFKLNNEQWNFLWVVDFPMFEFNSDENRLEALHHPFCAPNQSDLGQRRLWETNLPTARAQAYDLVLNGLELGGGSLRIHNPDLQLTVLKTIGLPLQEAKKEFGFLLEALEMGAPPHGGLAFGLDRIVMLLAGEESIRDTIAFPKTQQAKCLLTEAPAEVSKKQLKELHITSTFIKNE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chlorobium chlorochromatii (strain CaD3)
Length
605 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.899 kDa
Sequence
MSNPVEQQVVCNRFRSHSCGLLNATFEQQHVRLAGWVHRKRDHGGLIFIDLRDHTGICQLVIQPEQQALFAEAEHLHNESVISVEGTVILRAENAINPRLSSGEIEVVISCMSIESNAHPLPFSVADELPTSEELRLKYRFLDLRREKLHENIIFRSRLTAAVRRYLEEKNFTEIQTPILTSSSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLLMVAGFPRYFQIAPCFRDEDARADRSPGEFYQLDMEMAFIEQENLFEILEGMLEHITSTMSKKRITQVPFPRISYRDVMNRFGTDKPDLRIPLEIQDVTSLFVDSGFKVFAKNTVPGCCVKALVVKGRGNESRLFYDKAEKRAKELGSAGLAYIQFKDEGAKGPLVKFLSEDDMNALKQHLNLEQGDVVFFGAGKWEVTCKIMGGMRNYFADLFTLDKDELSFCWIVDFPMYEYNEEAKKIDFSHNPFSMPQGEMEALETKDALDILAYQYDIVCNGIELSSGAIRNHKPEIMYKAFAIAGYSREEVDQRFGHMIEAFKLGAPPHGGIAPGLDRLVMILCDEQNIREVIAFPMNQQAQDLMMSAPSEVTLAQLRELHLKVELPKKEEKKG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chlorobium limicola (strain DSM 245 / NBRC 103803 / 6330)
Length
605 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
69.203 kDa
Sequence
MYRAEESMMPLENRFRTDYCGLLGVGSENRSVRLGGWVHRKRDHGGLIFIDLRDHTGVCQLVIQPEQQALFNAVEHLHAESVICIEGTVVLRSSETVNTRLASGEIEVVVSSVIIESDAQPLPFPVADEVPTSEELRLKYRFIDLRREKIHENIIFRSRLTAMVRRYLEEREFIEIQTPILTSSSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLLMVSGFPRYFQIAPCFRDEDARADRSPGEFYQIDMEMAFIEQNDLFEILEGMFKHLTENMSQKRITQFPFPRISYREVMNRFGSDKPDLRIPLEIQDVTSLFVNSSFKVFASNTKEGTCVKALVLKGRGGESRMFYDKAEKRARELGSAGLAYIQFREEGPKGPIVKFLGEAEMEVLKEQLGLETGDVVFFGAGKWESTCKIMGGMRIYFADLFDLDKDELSFCWIVDFPMYEYNEEAKKIDFSHNPFSMPQGEMEALETMQPLDILAYQYDIVCNGIELSSGAIRNHRPDIMYRAFEIAGYTKEEVDSRFGHMIDAFKLGAPPHGGIAPGLDRMVMILRDEQNIREVIAFPMNQQAQDLMMSAPSEVMAQQLKELHLKIDLPPVKEAK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rickettsia prowazekii (strain Madrid E)
Length
605 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.465 kDa
Sequence
MHKYRTHNCNELQLSNVGQEVKLSGWVHRRRDHGNLVFIDLRDHYGITQIVFTDQNQQLMYDASRLCYESVITVSGTVVARSLDTINNKLPTGYVEVLAMECIVESASSPLPFVINNEKEAPEESRLKHRFLDLRREKLHNNIILRSQVIAHIRHLMIARGFTELQTPILTSSSPEGARDFLVPSRIHPGKFYALPQAPQQFKQLLMVAGFDRYFQIAPCFRDEDARADRSPGEFYQLDLEMSFVTQEDIFNTIEPVLYDLFTKFTNKTVSNTPFVRIPYNESMLKYGSDKPDLRNPIIISDVTEVFRDSNFTIFRENIKKGSVVHAIPAPQAASLPRSFFDKMIEFAISKGARGLGYIQFSESGEAKGPLSKFLTGQQLEILKATANTSNGDAVFFVSDKKDEAVKLCGKVRIKLGEELNLLEKDCFKFCWITDFPFYELNEETGKIDFSHNPFSMPQGGIDALEQAKTTEELLALTAYQYDIVCNGIELSSGAIRNHKPEIMYKAFSIAGYSAEEVEQRFGAMIKAFRFGAPPHGGIAPGIDRIVMLLAEATNIREIIAFPLNQQAEDLLMNAPSYVEEKALKELSIMLSPSSRKIHKKNTNL

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rickettsia typhi (strain ATCC VR-144 / Wilmington)
Length
605 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.59 kDa
Sequence
MHKYRTHNCNELQLSNVGQEVKLSGWVHRRRDHGNLVFIDLRDHYGITQIVFTDQNQHLMDYASNLCYESVITVSGTVVARSEGTINNKLLTGHIEVLAVECIVESASSPLPFVINNEKEAPEESRLKHRFLDLRREKLHNNIILRSQVISHIRHLMIVRGFTEFQTPILTSSSPEGARDFLVPSRIHPGKFYALPQAPQQFKQLLMIAGFDRYFQIAPCFRDEDARADRSPGEFYQLDLEMSFVTQEDIFNTIEPVLYDLFTKFTDKIVSKPPFVRIPYNESMLKYGSDKPDLRNPIIISDVTEIFRDSNFTIFRENIKKGSVVRAIHAPKAASLPRSFFDKMIEFAISEGAIGLSYIQFSETGEVKGPLSKFLTKQQLEILKATSNTSNGDAVFFASDQKDKAAKLCGKVRIKLGEELNLLEKDCFKFCWITDFPFYEFNEETGKIDFSHNPFSMPQGGIDALEQAKTTEELLALTAYQYDIVCNGIELSSGAIRNHKPEIMYKAFSIAGYSAEEVDKRFGAMIRAFKFGAPPHGGIAPGIDRIVMLLAEATNIREIIAFPLNQQAEDLLMNSPSYVDEKALKELSIMLSPTSRKIHKKNTGL

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Acidovorax citrulli (strain AAC00-1)
Length
604 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.975 kDa
Sequence
MAMRSHYCGLVTEALMGQTVTLAGWVNRRRDHGGVIFIDLRDREGNVQVVCDPDRADMFKTAEGVRNEFCVQVKGLVRARPEGTTNDSLKSGRIEVLCHELNVLNPSVTPPFQMDDENLSETTRLTHRVLDLRRPYMQRNLMLRYKTAIQVRNFLDKEGFIDIETPMLGKSTPEGARDYLVPSRVHDGQFFALPQSPQLYKQMLMVAGYDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLNEEEIRAIFQRMVTEVFKTQLDVDLGEFPIMTYQDAAFRFGSDKPDLRVKLEFTELTEVMKDVDFKVFSGAANMQGGRVVALRVPGGARENGGLSRGEIDAYTEFVKIYGAKGLAYIKVNELAKGRDGLQSPIVKNIHDAAIAEILKRTGAQDGDLLFFGADKTKVVNDAIGALRLKIGHSEFGRKNGLFENVWAPLWVVDFPMFEYDEDDARWVAVHHPFTSPKDGHEDLMDTDPGKCLAKAYDMVLNGWELGGGSVRIHRAEVQSKVFAALKLTPEDARAKFGYLLDALQYGAPPHGGLAFGLDRLITLMTGAESIRDVIAFPKTQRAQDLLTQAPSPVDEKQLRELHIRLRNPDAAKAA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methylobacterium extorquens (strain CM4 / NCIMB 13688)
Length
604 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.191 kDa
Sequence
MHRYRTHTCGAIRPSDVGQTVRLSGWCHRIRDHGGVLFIDLRDHYGLTQCVIDSDSKAFKAAETARSEWVIRIDGRVRTRPAGTENAELPTGSVEVYIDDLEVLGPAGELPLPVFGDQEYPEETRLKYRFLDLRREKLHANIMKRGAIVDSLRRRMREGGFFEFQTPILTASSPEGARDYLVPSRVHPGKFYALPQAPQQFKQLTMIAGFDRYFQIAPCFRDEDARADRSPGEFYQLDIEMSFVTQEDVFQAVEPVLRGVFEEFAGGKRVTKEFPRITYADAMLKYGVDKPDLRNPLIIADVTDEFADDAVEFKAFKGVIKSGGVVRAIPATGAAGQPRSFFDKLNDWARSEGAPGLGYIVFEEEGGALTGKGPIAKFIPAAIQARIAEKAGAKAGDAVFFAAGTEAKAAGLAGKARIRIGDELKLSDTDQFAFCWVVDFPMYEWNEEDKKIDFSHNPFSMPNFDRDEFLALGEADSEKILGIKAFQYDIVCNGIELSSGAIRNHRPDVMEKAFAIAGYGRDVLEEKFGGMLNALRLGAPPHGGIAPGVDRIVMLLCEEPNIREVVLFPMNQRAEDLMMGAPAEATPKQLRELHIRLNLPEKKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060)
Length
604 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.293 kDa
Sequence
MHRYRSHTCGALRPSDVGSTVRLSGWCHRVRDHGGVLFIDLRDHYGLTQCVVDADSPAFRAAEAVRSEWVIRIDGRVRQRPAGTENPDLPTGAVEVYIADLEVLGHAVELPMPVFGDLDYPEETRLRYRFLDLRREKLHANIMKRGAIIDSLRRRMREGGFFEFQTPILTASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLTMIAGFDRYFQIAPCFRDEDARADRSPGEFYQLDIEMSFVTQEDVFQAVEPVLRGVFEEFADGWRVTQSFPRIPYAEAMLKYGVDKPDLRNPLLIVDVTEEFSAEAVTFNAFKNLIRAGGVVRAIPAPGAASQPRSFFDKLNDWARSEGAPGLGYIVFEEEGGQLIGRGPIAKFVPAEVQAAIAGKAGLKAGDAVFFSAGTEAKAAGLAGKARIRIGDDLGLSDKDQFAFCWITDFPMYEWNEDEKRIDFSHNPFSMPNYDHKAFLALDPADADTILGIKAFQYDIVCNGIELSSGAIRNHRPDVMEKAFAIAGYGRDVLEQKFGGMLNALRMGAPPHGGIAPGVDRIVMLLCHEPNIREVVLFPMNQRAEDLMMGAPSEVTAKQLRELHIRLNLPEKSA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methylobacterium populi (strain ATCC BAA-705 / NCIMB 13946 / BJ001)
Length
604 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.314 kDa
Sequence
MHRYRTHTCGALRPSDVGQTVRLSGWCHRIRDHGGVLFIDLRDHYGLTQCVIDSDSPAFKAAETARSEWVIRIDGRVRTRPAGTENAELPTGSVEVYIDDLEVLGPAGELPLPVFGDQEYPEETRLKYRFLDLRREKLHANIMKRGAIIDSLRRRMREGGFFEFQTPILTASSPEGARDYLVPSRVHPGKFYALPQAPQQFKQLTMIAGFDRYFQIAPCFRDEDARADRSPGEFYQLDIEMSFVTQEDVFQAVEPVLRGVFEEFANGKRVTKEFPRITYADAMLKYGVDKPDLRNPLIIADVTDEFADDAVEFKAFKGVIKSGGVVRAIPATGAAGQPRSFFDKLNDWARSEGAPGLGYIVFEEEGGALTGKGPIAKFIPPEIQARIAQKAGAKAGDAVFFAAGTEAKAAALAGKARIRIGDELKLSDTDQFAFCWVVDFPMYEWNEEDKKIDFSHNPFSMPNYDRDAFLALGEEDAEKILGIKAFQYDIVCNGIELSSGAIRNHRPDVMEKAFAIAGYGRDVLEEKFGGMLNALRLGAPPHGGIAPGVDRIVMLLCEEPNIREVVLFPMNQRAEDLMMGAPAEATPKQLRELHIRLNLPEKKG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methylobacterium sp. (strain 4-46)
Length
604 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.236 kDa
Sequence
MHRYRTHTCGALRPSDVGATVRLSGWCHRVRDHGGVLFIDLRDHYGVTQCVVDADSAAFRAAEAVRSEWVIRVDGRVRRRPEGTENADLPTGAVELYITDLEVLGQAVELPMPVFGELDYPEETRLRYRFLDLRREKLHANIMKRGAIIDSLRRRMREGGFFEFQTPILTASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLTMIAGFDRYFQIAPCFRDEDARADRSPGEFYQLDIEMSFVTQEDVFQAVEPVLRGVFEEFAEGWRVTGTFPRIPYAEAMLKYGVDKPDLRNPLIIVDVTQEFSAEAVTFNAFKSVIRAGGVVRAIPAPGAGAQPRSFFDRLNNWARGEGAPGLGYIVFEEEGGVLSGRGPIAKFVPPEVQAAIAAKAGLKAGDAVFFAAGVEAKAAGLAGKARIRIGDDLGLTDKDQFAFCWITDFPMYEWNEDEKRIDFSHNPFSMPNYDHDGFLGLDPADAETILGIKAFQYDIVCNGIELSSGAIRNHRPDVMEKAFAIAGYGREVLEQKFGGMLNALRMGAPPHGGIAPGVDRIVMLLCHEPNIREVVLFPMNQRAEDLMMGAPSEVTPKQLRELHIRLNLPDRSA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Micrococcus luteus (strain ATCC 4698 / DSM 20030 / JCM 1464 / NBRC 3333 / NCIMB 9278 / NCTC 2665 / VKM Ac-2230)
Length
604 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.92 kDa
Sequence
MLRTHSLGELNASLIGQTVTVTGWVARRRDHGGVAFVDLRDASGFAQVVVRDEADFDPLRNEWVLQVTGTVERRPEGNENPNLPSGEIELIAETVTVLNTAAALPFQVDEHVEVGEEARLRHRYLDLRRPQPSRIMRLRSEVNRTARELLHGEGFVEVETPTLTRSTPEGARDFLVPARLAPGSWYALPQSPQLFKQLLQVGGIEKYYQIARCYRDEDFRADRQPEFTQLDIEASFVEQDDVIALGEKIVKALWALVGVDVPTPIRRMTYAEAMEKYGSDKPDLRFGLELTDLTEYFKDTPFRVFQNEYVGAVVMPGGASQARRTLDAWQEWAKQRGAKGLAYVLIQEDGELTGPVSKNISEEEKAGLAAAVGANPGDCVFFAAGKPKESRALLGAARVEIGRRCGLFTDAGDGVAAKDADWAFVWVVDAPMFEPAADAVASGDVAVGAGAWTAVHHAFTSPKPEFADTFDADPGSALAYAYDIVCNGNEIGGGSIRIHRRDVQERVFEVMGLSPEEANEKFGFLLEGFKYGAPPHGGIAFGWDRVVALLAGTDSIREVIAFPKTGGGFDPLTGAPAPITAQQRKEAGVDAQPEPKQAEAEPEA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Verminephrobacter eiseniae (strain EF01-2)
Length
604 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.934 kDa
Sequence
MAMRTHYCGLVTQALMGQTVTLAGWVNRRRDHGGVIFIDLRDREGHVQVVCDPEREQMFKTAEGLRSEFCVQVTGLVRARPDGSSNDRIKSGQIEVLCHALNVLNPSVTPAFQIDEENLSETTRLTHRVLDLRRPYMQRNLMLRYKVAMQVRNFLDANGFIDIETPMLTKSTPEGARDYLVPSRVHDGQFFALPQSPQLFKQLLMVAGFDRYYQITKCFRDEDLRADRQPEFTQIDIETSFMQEQDIRDLFQDMIETVFRNTLGVDLGEFPVMTYQDATSRYGSDKPDLRVKLEFTELTGVMKDVDFKVFSGAAGMKGGRVVGLRVPGGARDAGGLSRGEIDAYTEFVKIYGAKGLAYIKVNARARGRDGLQSPIVKNLHDAALTEILARTGAQDGDLIFFGADKEKIVNDAIGALRTKIGHSEFGKKNGLFEERWAALWVVDFPMFEFDEQAQRYSAMHHPFTAPKDGHEDWMASAPEKCISKGYDMVLNGWEMGGGSVRIHRADVQQKVFDALQITPEEARLKFGFLLDALQYGAPPHGGMAFGLDRIVTLMTGAESIRDVIAFPKTQRAQCLLTQAPSPVDEKQLRELHIRLRNPDAAKAH

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chlorobium luteolum (strain DSM 273 / 2530)
Length
604 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.791 kDa
Sequence
MTKEAGELNALKNRFRTDYCGQLGLDGEGREVRLGGWVHRIRDHGGLVFIDLRDHTGICQLVVQPEREELFELAGRLHAESVITIEGRVVARSSETINPRLASGSIEVVVSAIGVESHARPLPFPVADEVQTSEELRLKYRFIDLRREKIHENIIFRSRISAAIRRYLEERDFIEIQTPILTSSSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLLMVAGFPRYFQIAPCFRDEDARADRSPGEFYQLDMEMAFIEQDDLFEILEGMFRHLTDTMSKKRITRFPFPRISYREVMDSYGTDKPDLRIPLKIEDVTPMFTDSGFKVFASNTKPGCAVKALVLKGRGTESRLFYDKAEKRARELGSAGLAYIQFREEGPKGPIVKFMTEPELQAMKDQLTLETGDVVFFAAGKWEAACKIMGGMRTYFGDLFTLDPDELSFCWIVDFPMFEYNEDAKKVDFSHNPFSMPQGEMEALETMDPLDVLAYQYDIVCNGIELSSGAIRNHKPEIMYKAFEIAGYSREEVDLRFGHMIEAFKLGAPPHGGIAPGLDRLVMILRDEQNIREVIAFPMNQQAQDLMMAAPSEVTGAQLRELHIRLDLPEEEKK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Salinispora arenicola (strain CNS-205)
Length
604 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.211 kDa
Sequence
MIRTHDAGSLRATDAGTTVTLAGWVARRRDHGGVIFVDLRDGSGVAQVVLREEDAHVLRNEYCVRITGEVTRRPEGNENPELATGEVEVTADELEVLSEAAPLPLPVDDQIEAGDDIRLRYRYLDLRRSGPANALRLRSRANQIARTVLHERDFLEIETPTLTRSTPEGARDFLVPVRLQPGTWYALPQSPQLFKQLLMVGGMERYYQIARCYRDEDFRADRQPEFTQLDIEMSFVTEDDVIDLGEAIVSRLWRQLAGHQITRPIPRITWHDAMARYGSDKPDLRYGVELTELTDYLRGTRFRVFAGAIEAGGYVGAVVMPGGAAQSRKELDGWQDWAKARGAKGLAYVVLDAETGEARGPVAKNLSAEHLAGLADAVGAKPGDAIFFAAGAESRAAQELLGAARVEIARRANLVDESAWAFCWVVDAPMFERVSDSEEGGWTAVHHPFTAPNAEWVDRFEEAPDRALAYAYDIVCNGNEIGGGSIRIHRGDVQQRVFDLLGITPEQARDKFGFLLEAFKYGPPPHGGIALGWDRICMLLAGADSIREVIAFPKTRGGFDPLTSAPTPITAAQRLEAGVDARPKPEARAQAGTAGPAAPVADPT

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Synechococcus sp. (strain RCC307)
Length
604 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.363 kDa
Sequence
MRSHSCGDLRSDAIDSTVLLSGWVDRRRDHGGVIFIDLRDRSGTVQITVDPDLGAEAFAVAEHLRNETVLQVEGRVRARPDESRNERLATGEVEVLAQRLKVLNAPSRNLPFAVSVHDDEQVREELRLRHRYLDLRRERMRRNLSLRHQTVQTARRFLEDEGFIEVETPVLTRSTPEGARDYLVPSRVCGGEWFALPQSPQLFKQLLMVGGLERYYQVARCFRDEDLRADRQPEFTQLDMEMSFLDQEQILDLNERLIGRIWKLVKGVELSLPLPRMTWHEAMERYGTDRPDTRYGMELVGVSDIVADMGFKVFSGAVAAGGSVKCITVPGGNDKVSNVRIKPGGDVFSEAQKAGAGGLAFIRVRDGGEIDTIGAIKDNLSDEKKAQLLQRTGAEPGSLILFGAGDTATVNKALDRVRQYLAKELEMVPAEAWNFLWVVDFPMFEFNADENRLEALHHPFCAANPEDLGDDPALWSERLPTARAQAYDLVLNGLELGGGSLRIHDAALQNQVLQTIGLAQEEAQEQFGFLLEALEMGAPPHGGIAFGLDRMVMLLAGEESIRDTIAFPKTQQARCLMTSAPGGASDKQLEELHVASTWVEPEEN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Erythrobacter litoralis (strain HTCC2594)
Length
604 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.89 kDa
Sequence
MHAYRTHNCAALSKKNVGETVRLSGWVHNKRDHGGVLFVDLRDHYGITQIVADEDSAALPVLDKLKLESVVTIDGDVKARDAEAVNPNLPTGEIEVFARSVEIQSRAEELPLIVNSAEDYPEDVRLKYRFVDLRRERLHRNIMLRSQVITSIRNRMTAQGFTEFQTPILAASSPEGARDYIVPSRLHPGTFYALPQAPQMFKQLLMVAGFDRYFQIAPCFRDEDLRADRSPEFYQLDFEMSFVTQEDVFQAIEPVLAGVFEEFANGKSVTKSGEFPRIPYAEAMLKYGTDKPDLRNPLVISDVTDHFQSSGFGLFEKIVGIGGRVRVIPAPNTQEKSRKFFDDMNDWARKEGFAGLGYVTRKQGEFGGPIAKNHGPENMQKIYDELGLGENDGLFFAAGKEKDAAKLAGAARTRVGEELGLIEQGCFKFCWIVDFPMFEYDEELKKIDFSHNPFSMPQGEMEALENKDPLEILAWQYDIVCNGYELSSGAIRNHKPEIMYKAFEIAGYDRETVDREFSGMIEAFKLGAPPHGGSAPGIDRIVMLLADEPNIREVIAFPLNQKAQDLMMGAPSQVPPKALRDVHIRTVEPPKKQQVGTHLVNDDS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Acidovorax ebreus (strain TPSY)
Length
603 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.112 kDa
Sequence
MAMRSHYCGLVTEALLGQTVTLSGWVNRRRDHGGVIFIDLRDREGYVQVVCDPDRPEMFKVAEDVRNEFCVQVKGLVRARPEGTTNDSLKSGKIEVLCQELNVLNPSVTPPFQMDDDNLSETTRLTHRVMDLRRPYMQRNMMLRYKTAIQVRNFLDKEGFIDIETPMLGKSTPEGARDYLVPSRVHDGQFFALPQSPQLYKQMLMVAGYDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLNEEEIRAIFQRMIKEVFQQQLGVDLGEFPTMTYQEAAHRFGSDKPDLRVKLEFTELTDVMKDVDFKVFSGAANMKGGRVVALRVPGGAREEGGLSRGEIDGYTEFVKIYGAKGLAYIKVNDKAKGRDGLQSPIVKNIHDAALAEVLQRTGAQDGDLLFFGADKEKIVNDAIGALRLKVGHSEFGKKNGLFENRWAPLWVVDFPMFEHDEEEDRWVAVHHPFTSPKDGHENLMDTDPGKCIAKAYDMVLNGWELGGGSVRIHRADVQAKVFAALNIGPEDQRAKFGYLLDALQYGAPPHGGLAFGLDRLITLMTGAESIRDVIAFPKTQRAQDLLTQAPSPVDEKQLRELHIRLRNPLPAAH

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Acidovorax sp. (strain JS42)
Length
603 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.112 kDa
Sequence
MAMRSHYCGLVTEALLGQTVTLSGWVNRRRDHGGVIFIDLRDREGYVQVVCDPDRPEMFKVAEDVRNEFCVQVKGLVRARPEGTTNDSLKSGKIEVLCQELNVLNPSVTPPFQMDDDNLSETTRLTHRVMDLRRPYMQRNMMLRYKTAIQVRNFLDKEGFIDIETPMLGKSTPEGARDYLVPSRVHDGQFFALPQSPQLYKQMLMVAGYDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLNEEEIRAIFQRMIKEVFQQQLGVDLGEFPTMTYQEAAHRFGSDKPDLRVKLEFTELTDVMKDVDFKVFSGAANMKGGRVVALRVPGGAREEGGLSRGEIDGYTEFVKIYGAKGLAYIKVNDKAKGRDGLQSPIVKNIHDAALAEVLQRTGAQDGDLLFFGADKEKIVNDAIGALRLKVGHSEFGKKNGLFENRWAPLWVVDFPMFEHDEEEDRWVAVHHPFTSPKDGHENLMDTDPGKCIAKAYDMVLNGWELGGGSVRIHRADVQAKVFAALNIGPEDQRAKFGYLLDALQYGAPPHGGLAFGLDRLITLMTGAESIRDVIAFPKTQRAQDLLTQAPSPVDEKQLRELHIRLRNPLPAAH

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Anaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258)
Length
603 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.148 kDa
Sequence
MPRFITELKRTHSCGELTKADIGKEVVLFGWVNNRRDHGGAVFIDLRDRAGLTQVVFEEDVRPDVHELAGQLRLEYCVGVRGKVVSRGGNVNPKLRTGEIEVHASDLEIFNRSEPAPFQIEDEIDTGEEKRLQYRYLDLRRAPLQRTLMTRAKVNHLTRNYFTDKGFLELETPFMVKYTPGGARNFLVPSRLNPGKFYALAESPQLFKQLYMMAGFDRYFQIVRCFRDEDLRLDRQPEFTQIDVEMSFVEQNDVFDVMEGLVVKLWKEVLGIEIPRPFQRMPFEESMAKYGNDKPDLRFDMPHVVLTDLVRQHDGGGVPLMHEAVKAKGIVKAMRVPASANFSRTEIDKLEEYVKGMGAKGLARAKVGEGGEWTQSPLAKTITPALRQAINEACEAKPGDLLLFQFGKESVVHTVMANLRVHLAKRMGLIPEYGSGGAWRFLWVVNPPLFEYDEESGQWAAAHHAFTRPHDSDLQFLESDPGKVNCYRYDLVLNGFEIGGGSIRLHDPEVQARVFKAMGITDEEARSKFGFLLDALKMGAPPHGGIALGMDRLVMLLTGAESLRDVVAWPKTQKGTDLMTGAPGDVDARQLRELYVKSTYEPK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Anaeromyxobacter dehalogenans (strain 2CP-C)
Length
603 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.99 kDa
Sequence
MPRFITELKRTHSCGELTKADIGKEVVLFGWVNNRRDHGGAVFIDLRDRAGLTQVVFEEDVRPDVHELAGQLRLEYCVGVRGKVVSRGGNVNPKLPTGEIEVHASDLEIFNRSEPAPFQIEDKIDTGEEKRLQYRYLDLRRAPLQQTLMTRAKVNHLTRNYFTDKGFLELETPFMVKYTPGGARNFLVPSRLNPGKFYALAESPQLFKQLYMMAGFDRYFQIVRCFRDEDLRLDRQPEFTQIDVEMSFVEQNDVFDVMEGLVVKLWKEVLGIEIPRPFQRMPFEESMAKYGNDKPDLRFDMPHVVLTDLVRQHDGGGVPLMHEAVKAKGIVKAMRVPASANFSRTEIDKLEEYVKGMGAKGLARAKVGEGGEWTQSPLAKTITPALRQAINDACEAKAGDLLLFQFGKESVVHTVMANLRVHLAKRMGLIPEYGSGGAWRFLWVVNPPLFEYDEESGQWAAAHHAFTRPHDSDLQFLESDPGKVNCYRYDLVLNGFEIGGGSIRLHDPEVQARVFKAMGISDEEARSKFGFLLDALKMGAPPHGGIALGMDRLVMLLTGAESLRDVVAWPKTQKGTDLMTGAPGDVDARQLRELYVKSTFEPK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Laribacter hongkongensis (strain HLHK9)
Length
603 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.603 kDa
Sequence
MRTDYCGLIDTRYLDQTVTVKGWVHRRRDHGGVIFIDLRDREGLVQVVIDPDTPEAFATADSARNEFVLSITGRVRRRPEGTTNAKMISGEIELLAKEIEILNAAATPPFQIDDENLSETVRLTNRVIDLRRPAMQKNLRLRYQVAMGVRRYLDAQGFIDIETPMLTRSTPEGARDYLVPSRVHPGEFFALPQSPQLFKQLLMVAGFDRYYQIVKCFRDEDLRADRQPEFTQIDLETSFLNEDDIMDITEGMARQVFHDAMDVELGDFPRMTYADAMHYYGSDKPDLRVSLKFAELTDVMKDVPFKVFNAAANLPNGRVVALRVPGGAKLSRKEIDEYTQFVGIYGAKGLAYIKVNDVSKLTTDETSGLQSPIVKNLTEGVLKSIVERTGAENGDIIFFGADKAKVVNEAIGALRIRIGHEHGEAGGYFVREWRPLWVVDFPMFEYDEDDDRWTACHHPFTSPKPGHEDLMATDPGACIARAYDMVLNGWEIGGGSIRIHRADVQEKVFGALKISPEEQQNKFGFLLDNLKFGAPPHGGLAFGLDRLVTLMAGADSIRDVIAFPKTQRAQCLLTNAPNAVDEKQLKELSLRLRQKADVAGGAA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Anaeromyxobacter sp. (strain K)
Length
603 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.035 kDa
Sequence
MPRFITELKRTHSCGELTKADIGKEVVLFGWVNNRRDHGGAVFIDLRDRAGLTQVVFEEDVRPDVHELAGQLRLEYCVGVRGKVVSRGGNVNPKLRTGEIEVHASDLEIFNRSEPAPFQIEDEIDTGEEKRLQYRYLDLRRAPLQRTLMTRAKVNHLTRNYFTDGGFLELETPFMVKYTPGGARNFLVPSRLNPGKFYALAESPQLFKQLYMMAGFDRYFQIVRCFRDEDLRLDRQPEFTQIDVEMSFVEQNDVFDVMEGLVVKLWKEVLGIEIPRPFQRMPFEESMAKYGNDKPDLRFDMPHVVLTDLVRQHDGGGVPLMHEAVKGKGIVKAMRVPASANFSRTEIDKLEEYVKGMGAKGLARAKVGEGGEWTQSPLAKTITPALRQAINEACEAKPGDLLLFQFGKDSVVHTVMANLRVHLAKRMGLIPEYGSGGAWRFLWVVNPPLFEYDEESGQWAAAHHAFTRPHDSDLQFLESDPGKVNCYRYDLVLNGFEIGGGSIRLHDPEVQARVFKAMGISDEEARSKFGFLLDALKMGAPPHGGIALGMDRLVMLLTGAESLRDVVAWPKTQKGTDLMTGAPGDVDARQLRELYVKSTYEPK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Aquifex aeolicus (strain VF5)
Length
603 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
69.729 kDa
Sequence
MLTEYGDFKRTKYCGEVSEEDIGKEVKLAGWVHRKRHHGGVIFIDLRDREGIVQVVVEEKTNPEAYEVADKLKSEYVIGVVGKVRKRPEGTENPKLKTGYVEVVADRILVFNTSEALPFPVEEETHVSEETKLKYRYIDLRRESMKNNLIFRHRVYQITRNFFTKEGFIEIETPFLTKSTPEGARDFLVPSRLHPGKFYALPQSPQLFKQILMIAGFDRYFQIVKCFRDEDLRADRQPEFTQIDYEMSFVSEEEVMDVAERLIATLFKELLGVELKTPFERISYREAMEKYGTDKPDRRFGLELIELTDIFKNTAFKVFKSVVEAGGIIKAINFKGSNLSRKEIDELTKFVQSLGAKGLAWIKVEKDKLTSPIVKFFTEEETQKLLERTKAEPGDVILFSADKKEMVYKILGNLRLHLGKKYKLIDESKWDVFWIVDFPLMEWDEEEERFVSLHHPFTMPREENIPKLKEALEEEDLEKKKEIVHSVRARAYDMVLNGEEIGGGSIRIHRRDIQEVVFKLLGIGEVEAQEKFGFLLEALKYGAPPHGGLAFGLDRVVALMLGLDSIRDTIAFPKTQRGICPLTGAPDYVDPKQLKELHIKVLE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI)
Length
603 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.944 kDa
Sequence
MIEFMDGLKRSHYCGELRVEHAGLEVVLTGWVQRRRDHGGLIFIDLRDRTGIVQVVFSPDLHEEAFLKAEAVRNEYVLAVRGTVRERPEGTANPNLATGQVEVLGCELRILNRAKTPPFYIEDGVDVDENLRLRYRYLDLRRPEMQEALIFRHRAAKSVRDFLDEHGFLEIETPMLTRSTPEGARDYLVPSRVNPGRFYALPQSPQLFKQILMVAGMDRYFQIARCFRDEDLRADRQPEFTQIDIEMSFVDVDDVLELTEGMVARLCREVAGLDIPRPFPRLSYREAMDRFGSDKPDTRFGMELKDISDIASGCGFKVFASAVAGGGQVKGINAAGCGSFSRKEIDDLTAFAAVYKAKGLAYFIVNEEGVKSAISKFFTEAELSAILERMDAKPGDLLLFVADKPEVVAASLGALRLHLGERLGLIPEGTYHFLWVVDFPLLEYNQEEGRYEAMHHPFTSPRETDIPLLESDPGRVRAKAYDLVLNGTEVGGGSIRIHRRDVQEKVFTAIGIDREEASEKFGFLLEAFEYGTPPHGGIALGFDRLVMLLAGKNTIRDVIAFPKTQSATDLMTMAPGPVAEEQLRELHIRTVLKIRERERLTAR

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chlorobaculum parvum (strain NCIB 8327)
Length
603 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.279 kDa
Sequence
MSKEPTAAAGLQNRFRTHYCGLLNRDSEGAGVKLGGWVHRIRDHGGLIFIDLRDHTGICQLVIQPESGELFRIAEGLHSESVISAEGSVVLRSDETVNPRLASGAIEVVVSAIKIESAAHPLPFPVADYMPTSEELRLKYRFLDLRRERLHENIIFRSQLTAAVRKYLTDLDFIEIQTPILTSSSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLLMVSGFPRYFQIAPCFRDEDARADRSPGEFYQVDIEMSFVEQDDLFVILEGMFKHLVETMTTKRIAQYPFPRISYKDVMNRYGSDKPDLRIPIEIQDVTELFVNSGFKVFASNTKEGCCVKAMVLKGMGNESRLFYDKAEKRARELGSAGLAYIQFKEEAPKGPVVKFLKEEEMAALKEQLGIETGDVVFFGAGKWEQTCKIMGGMRNYFADVFPLDRDELSFCWIVDFPMFEYNEEDKKIDFSHNPFSMPQGEMEALEQHSPLDILAYQYDIVCNGIELSSGAIRNHRPDIMYKAFEIAGYPHDEVDARFGHMIEAFKHGAPPHGGIAPGLDRLVMILRDEQNIREVIAFPMNQSAQDLMMAAPSEVTAQQLKELHIKVELPEEEA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
Length
603 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.599 kDa
Sequence
MSKEPTTADGLQNRFRTHYCGRLNRKSEGELVRIAGWVHRIRDHGGLIFIDLRDHTGICQLVVLPENESQFKLAETLHSESVISAEGKVVLRSDETVNPRLASGAIEVVVSSIQIESNADPLPFPVADDMPTSEELRLKYRFLDLRREKLHENIIFRSKLTAAVRKYLTDLDFIEIQTPILTSSSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLLMVAGFPRYFQIAPCFRDEDARADRSPGEFYQIDIEMSFIEQDDLFVILEGMFKHLVENMSHKRITQFPFPRISYKDVMNRYGSDKPDLRIPLEIQDVTELFVNSGFKVFASNTAEGSCVKAMVLKGMGNESRLFYDKAEKRARELGSAGLAYIQFKEEGPKGPVVKFLSEAEMNALKERLGIVTGDVVFFGAGKWEKTCKIMGGMRNYFADLFPLDKDELSFCWIVDFPMFEYNEEDKKIDFSHNPFSMPQGEMEALESKFPLDILAYQYDIVCNGIELSSGAIRNHRPDIMYKAFEIAGYSKEEVDARFGHMIEAFKHGAPPHGGIAPGLDRLVMILRDEQNIREVIAFPMNQSAQDLMMAAPSEVTAQQLKELCIRIELPEEEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Treponema pallidum (strain Nichols)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.627 kDa
Sequence
MYSAHTPWYDGQVMDYPRRTIACGELRRCHVGTVVVLNGWVHRKRSHGTVSFFNMRDRSGIVQVIVSQEENASLWSTVNRIRLECCLAVEGVVRERPPSMINRALHTGEVEVHARTLYVLSENAVLPFRVDDVVHAHEDIRLKYRYLDLRSQRMQERIALRSRVALAIRQFLSMKGFIEIETPTFICSTPEGARDFVVPSRVCPGRFYALPQSPQLYKQLLMVAGFDRYFQLARCYRDEDARGDRQPEFTQIDLEMSFVSRDDVMRVNEDMLRYVFRTSIGVELPTFFPRLTYAQALDQYGTDKPDMRFKPVLQNADFMGMLGTFTPFEEVVAQGGSIRALVLPGKARCYSRRQIEALESIARAHEAHHLFWLKATGGGLEGGIARFFAGVESEVRRRLSAQDEDLLLFVADCRHRVCCVALGAVRSALIRDESFPEKELFSFVWIVDFPLFEWNPAENKWDPAHHMFSAPQEQYLETLEQDPGSVKGDLYDLVLNGYELASGSIRIHDTQLQKRIFKIVGLDPEEAGEKFGFLTEAFKYGAPPHGGIAHGLDRLVMLMTGSESIRDVIAFPKNTLAASPLDNCPSVLDKRQLDELHLTVHV

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Treponema pallidum subsp. pallidum (strain SS14)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.627 kDa
Sequence
MYSAHTPWYDGQVMDYPRRTIACGELRRCHVGTVVVLNGWVHRKRSHGTVSFFNMRDRSGIVQVIVSQEENASLWSTVNRIRLECCLAVEGVVRERPPSMINRALHTGEVEVHARTLYVLSENAVLPFRVDDVVHAHEDIRLKYRYLDLRSQRMQERIALRSRVALAIRQFLSMKGFIEIETPTFICSTPEGARDFVVPSRVCPGRFYALPQSPQLYKQLLMVAGFDRYFQLARCYRDEDARGDRQPEFTQIDLEMSFVSRDDVMRVNEDMLRYVFRTSIGVELPTFFPRLTYAQALDQYGTDKPDMRFKPVLQNADFMGMLGTFTPFEEVVAQGGSIRALVLPGKARCYSRRQIEALESIARAHEAHHLFWLKATGGGLEGGIARFFAGVESEVRRRLSAQDEDLLLFVADCRHRVCCVALGAVRSALIRDESFPEKELFSFVWIVDFPLFEWNPAENKWDPAHHMFSAPQEQYLETLEQDPGSVKGDLYDLVLNGYELASGSIRIHDTQLQKRIFKIVGLDPEEAGEKFGFLTEAFKYGAPPHGGIAHGLDRLVMLMTGSESIRDVIAFPKNTLAASPLDNCPSVLDKRQLDELHLTVHV

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rhodococcus erythropolis (strain PR4 / NBRC 100887)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.287 kDa
Sequence
MLRTHLAGSLRPEQAEQTVTLTGWVARRRDHGGVIFIDLRDASGVAQVVFRAGDVAEQAHRLRAEYCVRVTGTVEVRPEGNQNFEIPTGAIEVNATELEVLNESAPLPFQLDDQVGEEARLKYRYLDLRREGPGSAIRLRSKVSAAARGVLAHHEFVEVETPTLTRSTPEGARDFLVPSRLQPGSFYALPQSPQLFKQLLMVGGIERYYQIARCYRDEDFRADRQPEFTQLDIEMAFVNQDDIILLAEEILTALWKLVGHEIKTPIDRMTYTEAMRRYGSDKPDLRFDIELVECMDFFKDTTFRVFQAEYVGAVVMPGGASQPRKQLDAWQEWAKQRGAKGLAYVLVGEDGTLGGPVAKNLTDAEREGLAAHVGAQPGDCVFFAAGATKPMRALLGAARGEIARKKDLIDPDAWAFVWIVDAPMFEPTADATASGDVALGHSAWTAVHHAFTSPKPEFFDTFDTDPDSALAYAYDIVCNGNEIGGGSIRIHRKDIQERVFKVMGISEEEAQEQFGFLLDAFAFGAPPHGGIAFGWDRITALLAGMDSIREVIAFPKSGGGVDPLTDAPAPISAQQRKESGIDAKPEKKSEDKKSEGDTAEAK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rhodococcus jostii (strain RHA1)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.772 kDa
Sequence
MLRTHLAGSLRAEQAQQTVTLTGWVARRRDHGGVIFIDLRDASGVSQVVFREGAAAEQAHRLRAEYCVKVTGVVEVRPEGNQNFEIPTGAIEVNVTDLEVLNESAPLPFQLDDQAGEEARLKYRYLDLRREGPGHAIRLRSKVNAAARAVLAHHEFVEVETPTLTRSTPEGARDFLVPARLQPGSFYALPQSPQLFKQLLMVGGIERYYQIARCYRDEDFRADRQPEFTQLDIEMSFVNQDDVILLAEEVLSSLWKLVGHEIKTPIARMTYAEAMRRYGSDKPDLRFGVELVECAEFFKDTTFRVFQQEYVGAVVMPGGASQPRKQLDAWQEWAKQRGAKGLAYVLVGEDGTLGGPVAKNLTDTEREGLAAHVGAKPGDCIFFAAGTTKSSRALLGAARGEIARKQNLIDPDAWAFVWVVDAPLFEPTADATASGDVALGYSAWTAVHHAFTSPKPESIDTFDTDPGSALAYAYDIVCNGNEIGGGSIRIHRKDIQERVFKVMGISHEEAEEKFGFLLDAFAFGAPPHGGIAFGWDRITALLAGVDSIREVIAFPKSGGGVDPLTNAPAPITAQQRKESGVDAKPEPKGDAASAKPDAPADK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rhodococcus opacus (strain B4)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.715 kDa
Sequence
MLRTHLAGSLRAEQAQQTVTLTGWVARRRDHGGVIFIDLRDASGVSQVVFREGAAAEQAHRLRAEYCVKVTGVVEVRPEGNQNFEIPTGAIEVNVTELEVLNESAPLPFQLDDQAGEEARLKYRYLDLRREGPGHAIRLRSKVNAAARAVLAHHEFVEVETPTLTRSTPEGARDFLVPARLQPGSFYALPQSPQLFKQLLMVGGIERYYQIARCYRDEDFRADRQPEFTQLDIEMSFVNQDDVILLAEEVLTSLWKLVGHEIKTPIARMTYAEAMRRYGSDKPDLRFGVELVECAEFFTDTTFRVFQQEYVGAVVMPGGASQPRKQLDAWQEWAKQRGAKGLAYVLVGEDGTLGGPVAKNLTDAERDGLAAHVGAKPGDCIFFAAGATKSSRALLGAARGEIARKQNLIDPDAWAFVWIVDAPLFEPTADATASGDVALGYSAWTAVHHAFTSPKPESIDTFDTDPGSALAYAYDIVCNGNEIGGGSIRIHRKDIQERVFKVMGISHEEAEEKFGFLLDAFAFGAPPHGGIAFGWDRITALLAGVDSIREVIAFPKSGGGVDPLTSAPAPITAQQRKESGVDAKPEPKGDAAAAKPQVSAEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Neisseria gonorrhoeae (strain NCCP11945)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.902 kDa
Sequence
MRTNYCGLISEQYLGQTVTVKGWVHRRRDHGGVIFIDLRDREGIVQVVIDPDTPEAFAAADSARNEYVLGITGRVRNRPEGTTNDKMISGKIEILAKEIEVLNAAATPPFQIDDENISENVRLTNRVIDLRRPVMQRNLRLRYQVAMGVRRYLDAQGFIDIETPMLTRSTPEGARDYLVPSRVHPGEFFALPQSPQLFKQLLMVAGFDRYYQITKCFRDEDLRADRQPEFTQIDLETSFLNEDEIMDITEGMAKQVFKDALNVDLGDFPRMPYSEAMFYYGSDKPDMRINLKFTELTDLMKTEEFKVFRGAADMKGGRVVALRVPNGAKFSRKEIDEYTKFVGIYGAKGLAYIKVNDAGNLSNGEDSGLQSPIVKFLSENALKEIIERTAAQNGDIIFFGADKAKVVNEAVGALRIKVGLEHGKDNGYFTDEWKPLWVVDFPMFEYDEEADRYVAVHHPFTAPKEGHEDLMVSDPANCLARAYDMVLNGWEIGGGSIRIHRADVQGKVFAALKISPEEQQEKFGFLLDNLKFGAPPHGGLAFGLDRLVTLMTGAESIRDVIAFPKTQRAQCLLTDAPNSVDDKQLRELSLRLRQKAVETKEA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Neisseria meningitidis serogroup C (strain 053442)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.047 kDa
Sequence
MRTNYCGLISEQYLDQTVTVKGWVHRRRDHGGVIFIDLRDREGIVQVVIDPDTPEAFAAADSARNEYVLSITGRVRNRPEGTTNDKMISGKIEILAKEIEVLNAAATPPFQIDDENISENVRLTNRVIDLRRPAMQRNLRLRYQVAMGVRRYLDAQGFIDIETPMLTRSTPEGARDYLVPSRVHPGEFFALPQSPQLFKQLLMVAGFDRYYQITKCFRDEDLRADRQPEFTQIDLETSFLNEDEIMDITEGMAKQVFKDALNVDLGDFPRMPYAEAMFYYGSDKPDMRINLKFTELTDLMKTEEFKVFRGAADMKGGRVVALRVPNGAKFSRKEIDEYTKFVGIYGAKGLAYIKVNDVGNLSNGEDSGLQSPIVKFLSENALKEIIERTGAQNGDIIFFGADKTKVVNEAIGALRIKVGLEHGKDNGYFTDEWKPLWVVDFPMFEYDEEADRYVAVHHPFTAPKEGHEDLMVSDPANCLARAYDMVLNGWEIGGGSIRIHRADVQEKVFAALKISPEEQQEKFGFLLDNLKFGAPPHGGLAFGLDRLVTLMTGAESIRDVIAFPKTQRAQCLLTNAPNSVDDKQLRELSLRLRQKAAETKEA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Neisseria meningitidis serogroup A / serotype 4A (strain Z2491)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.976 kDa
Sequence
MRTNYCGLISEQYLDQTVTVKGWVHRRRDHGGVIFIDLRDREGIVQVVIDPDTPEAFAAADSARNEYVLSITGRVRNRPEGTTNDKMISGKIEILAKEIEVLNAAATPPFQIDDENISENVRLTNRVIDLRRPVMQRNLRLRYQVAMGVRRYLDAQGFIDIETPMLTRSTPEGARDYLVPSRVHPGEFFALPQSPQLFKQLLMVAGFDRYYQITKCFRDEDLRADRQPEFTQIDLETSFLNEDEIMDITEGMAKQVFKDALGVDLGDFPRMPYSEAMFYYGSDKPDMRINLKFTELTDLMKTEEFKVFRGAADMKGGRVVALRVPNGAKFSRKEIDEYTKFVGIYGAKGLAYIKVNDVGNLSNGEDSGLQSPIVKFLSENALKEIIARTGAQNGDIIFFGADKTKVVNEAIGALRIKVGLEHGKDNGYFTDEWKPLWVVDFPMFEYDEEADRYVAVHHPFTAPKEGHEDLMVSDPANCLARAYDMVLNGWEIGGGSIRIHRADVQEKVFAALKISPEEQQEKFGFLLDNLKFGAPPHGGLAFGLDRLVTLMTGAESIRDVIAFPKTQRAQCLLTNAPNSVDDKQLRELSLRLRQKAAETKEA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Neisseria meningitidis serogroup B (strain MC58)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.124 kDa
Sequence
MRTNYCGLISEQYLDQTVTVKGWVHRRRDHGGVIFIDLRDREGIVQVVIDPDTPEAFAAADSSRNEYVLSITGRVRNRPEGTTNDKMISGKIEILAKEIEVLNAAATPPFQIDDENISENVRLTNRVIDLRRPVMQRNLRLRYQVAMGVRRYLDAQGFIDIETPMLTRSTPEGARDYLVPSRVHPGEFFALPQSPQLFKQLLMVAGFDRYYQITKCFRDEDLRADRQPEFTQIDLETSFLNEDEIMDITEGMAKQVFKDALNVDLGDFPRMPYSEAMFYYGSDKPDMRINLKFTELTDLMKTEEFKVFRGAADMKGGRVVALRVPNGAEFSRKEIDEYTKFVGIYGAKGLAYIKVNDVSNLSNGEDSGLQSPIVKYLSENALKEIIARTGAQNGDIIFFGADKAKVVNEAIGALRIKVGLEHGKDNGYFTDEWKPLWVVDFPMFEYDEEADRYVAVHHPFTAPKEGHEDLMVSDPANCLARAYDMVLNGWEIGGGSIRIHRADVQEKVFAALKISPEEQQEKFGFLLDNLKFGAPPHGGLAFGLDRLVTLMTGAESIRDVIAFPKTQRAQCLLTNAPNSVDDKQLRELSLRLRQKATETKEV

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM 15464 / FAM18)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.945 kDa
Sequence
MRTNYCGLISEQYLDQTVTVKGWVHRRRDHGGVIFIDLRDREGIVQVVIDPDTPEAFAAADSARNEYVLSITGRVRNRPEGTTNDKMISGKIEILAKEIEVLNAAATPPFQIDDENISENVRLTNRVIDLRRPVMQRNLRLRYQVAMGVRRYLDAQGFIDIETPMLTRSTPEGARDYLVPSRVHPGEFFALPQSPQLFKQLLMVAGFDRYYQITKCFRDEDLRADRQPEFTQIDLETSFLNEDEIMDITEGMAKQVFKDALNVDLGDFPRMPYAEAMFYYGSDKPDMRINLKFTELTDLMKTEEFKVFRGAADMKGGRVVALRVPNGAKFSRKEIDEYTKFVGIYGAKGLAYIKVNDVGNLSNGEDSGLQSPIVKFLSENALKEIIARTGAENGDIIFFGADKAKVVNEAIGALRIKVGLEHGAENGYFTDEWKPLWVVDFPMFEYDEEADRYVAVHHPFTAPKEGHEDLMVSDPANCLARAYDMVLNGWEIGGGSIRIHRADVQEKVFAALKISPEEQQEKFGFLLDNLKFGAPPHGGLAFGLDRLVTLMTGAESIRDVIAFPKTQRAQCLLTNAPNSVDDKQLRELSLRLRQKAAETKEA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 / CH34)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.186 kDa
Sequence
MSSMRTHYCGLVTEQLIGQEVALTGWVQRRRDHGGVIFIDLRDREGLVQVVCDPDRPEMFKAAEEIRNEFCIRITGKVRPRPAGTENANLTSGKIEVLCHELTVLNPSVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQYNLRLRYKVAMEVRKYLDAQGFIDIETPMLGKSTPEGARDYLVPSRVNPGHFFALPQSPQIFKQMLMVSGFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLTEQEIRDLFEDMMRTVFKNAIDVDLDAKFPVMEFREAMARFGSDKPDLRVKLEFTELTEVMKDVDFKVFSGPANSDNGRVVGLRVPGGGAISRGEIDAYTQFVAIYGAKGLAWIKVNEVAKGRDGLQSPIVKNLHDAAIAEILKRTGAQDGDIIFFGADKAKIVNDAIGALRLKVGHSEFGKSTGLFEDTWKPLWVIDFPMFEYDEEDARWVAMHHPFTSPKDEHLQYLETDPGKCIAKAYDMVLNGWEMGGGSVRIYREDVQSKVFRALKINDEEARAKFGYLLDALQYGAPPHGGLAFGLDRIVTMMAGADSIRDVIAFPKTQRAQDLLTQAPSTVDEKQLRELHIRLRAQEPKTTA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.077 kDa
Sequence
MSSMRTHYCGLVTEQFSGQEVALTGWVQRRRDHGGVIFIDLRDREGLVQVVCDPDRPEMFKAAEEIRNEFCIRVTGKVRPRPAGTENANLTSGKIEVLCHELTVLNPSVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQYNLRLRYKVAMEVRKFLDAQGFIDIETPMLGKSTPEGARDYLVPSRVNPGHFFALPQSPQIFKQMLMVSGFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLTEQEIRDLFEDMMRTVFKNAIDVDLDARFPVMEFREAMARFGSDKPDLRVKLEFTELTEVMKDVDFKVFSSPANSDNGRVVGLRVPGGGAISRGEIDAYTQFVGIYGAKGLAWIKVNEVAKGRDGLQSPIVKNLHDAAIAEILKRTGAQDGDIIFFGADKAKVVNDSIGALRLKIGHSDFGKANGLFEDTWKPLWVVDFPMFEYDEEDARWVAMHHPFTSPKDEHLEYLETDPGKCLAKAYDMVLNGWEMGGGSVRIFRSDIQSKVFRALNINDDEARAKFGYLLDALQYGAPPHGGLAFGLDRIVTMMAGADSIRDVIAFPKTQRAQDLLTQAPSSVDEKQLRELHIRLRATEPKPTA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Cupriavidus necator (strain JMP 134 / LMG 1197)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.135 kDa
Sequence
MSSMRTHYCGLVTEQLSGQEVALTGWVQRRRDHGGVIFIDLRDREGLVQVVCDPDRPEMFKAAEEIRNEYCIRITGKVRPRPAGTENTNLTSGKIEVLCYELTVLNPSVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQYNLRLRYKVAMEVRKYLDAQGFIDIETPMLGKSTPEGARDYLVPSRVNPGHFFALPQSPQIFKQMLMVSGFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLTEQEIRDLFEDMMRTVFKNAIDVDLDAKFPVMEFREAMARFGSDKPDLRVKLEFTELTDVMKDVDFKVFSGPANSDNGRVVGLRVPGGGAISRGEIDAYTQFVGIYGAKGLAWVKVNEVAKGRDGLQSPIVKNLHDAAITEILKRTGAQDGDIIFFGADKAKVVNDAIGALRLKIGHSEFGKASGLFEDVWKPLWVVDFPMFEYDEEDARWVAMHHPFTSPKDEHMQYLETDPGKCIAKAYDMVLNGWEMGGGSVRIYRSDIQSKVFRALKINDEEARAKFGYLLDALQYGAPPHGGLAFGLDRIVTMMAGADSIRDVIAFPKTQRAQDLLTQAPSAVDEKQLRELHIRLRATEPKTTV

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CIP 107171 / LMG 19424 / R1)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.03 kDa
Sequence
MSSMRTHYCGLVTEQFSGQEVALTGWVQRRRDHGGVIFIDLRDREGLVQVVCDPDRPEMFKAAEEIRNEFCIRVTGKVRPRPAGTENANLTSGKIEVLCHELTVLNPSVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQYNLRLRYKVAMEVRKFLDAQGFIDIETPMLGKSTPEGARDYLVPSRVNPGHFFALPQSPQIFKQMLMVSGFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLTEQEIRDLFEDMMRTVFKNAIDVDLDAKFPVMEFREAMARFGSDKPDLRVKLEFTELTEVMKDVDFKVFSGPANSDNGRVVGLRVPGGGAISRGEIDAYTQFVGIYGAKGLAWIKVNEVAKGRDGLQSPIVKNLHDAAIAEILKRTGAQDGDIIFFGADKAKVVNDSIGALRLKIGHSDFGKANGLFEDAWKPLWVVDFPMFEYDEEDARWVAMHHPFTSPKDEHLEYLETDPGKCLAKAYDMVLNGWEMGGGSVRIFRSDIQSKVFRALKINDEEARAKFGYLLDALQYGAPPHGGLAFGLDRIVTMMAGADSIRDVIAFPKTQRAQDLLTQAPSSVDEKQLRELHIRLRTAEPKPNA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Prochlorococcus marinus (strain MIT 9515)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.41 kDa
Sequence
MRNKICEELNKSDIGKEVNLCGWVDRRRDHGGVIFIDLRDHSGFMQITINPEDGETLFKQAEILRNETVIMVNGIVNERPKDSINKNIITGELELKVQDLQILNQIKNNLPFPVSVHDYENTKEELRLKYRYLDIRRGKLLENLKTRHKIIKAIRNYLDNSGFTEVETPLLTKSTPEGARDFLVPARLSNGDFFALPQSPQLFKQLLMVGGLDKYYQIAKCFRDEDLRADRQPEFTQLDIEMSFVSEEEIIAFNEKLIKHIWKNVLNINLNEDFPRMSWQEAMDNYGTDRPDTRYGMLLKNLGEILGNIGFNIFTKAIQMGGAIKSITIKNGNSSISNVRIKPGGDIFKVAQEAGAGGLAFIRVKGDELETIGAIKNNLNKDHISNILKITEAEDGDLILLGAGSTKIVNQSLDRVRQYIAKDLNLLENQKAQSQWNFLWITDFPMFEMNEEEKRFEALHHPFCSPKNVKFEDKKELTKKIETSTAYAYDLVLNGLELGGGSLRIHQAEMQKEVLRTVGLTDHQIDEKFGFLIEALEMGAPPHGGIAFGLDRITMLILGVDSIRETIAFPKNQQAKCLLTNAPSNVSKSQLKELDIEITIDE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chlorobium phaeovibrioides (strain DSM 265 / 1930)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.115 kDa
Sequence
MTNAAGSSSALQNRFRTHYCGSLGPVLQQEKVSLAGWVHRIRDHGGLVFIDLRDHTGICQLVIQPEEKELFEQASHLHAESVIAIEGSVVLRSPETVNARLASGAIEVVVSALTVESNARPLPFPVADELPTSEELRLKYRFIDLRREKIHENIIFRSRVSSAIRRYLEERDFVEIQTPILTSSSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLLMVAGFPRYFQIAPCFRDEDARADRSPGEFYQLDMEMAFIEQDDLFEILEGMFRHLVTSMSKKRITAFPFPRISYRDVMNRFGTDKPDLRIPLEIADVTPLFVNSGFKVFAANTKEGCAVKALVLKGRGTESRLFYDKAEKRAKELGSAGLAYIQFREEGLKGPIVKFMSEGEIASMKEQLSLETGDVVFFAAGKWEAACRIMGGMRTYFGELFTLDHDELSFCWIVDFPMYEYNEEAGKIDFSHNPFSMPQGEMEALETMDPLELLAYQYDIVCNGIELSSGAIRNHRPDIMYRAFEIAGYSKEDVDLRFGHMIEAFKLGAPPHGGIAPGLDRLVMILRDEQNIREVIAFPMNQQAEDLMMSAPSEVTTAQLRELHIKLDLPKED

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Sulfurihydrogenibium sp. (strain YO3AOP1)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.774 kDa
Sequence
MIDQLREFKRDYYCGDLNESNIGDEVRLLGWVDTVRDHGGVIFINLRDREGIVQVVFDPSKIGEELYNKAKKLKSEYVIGVRGRVYRRPAGTENPKMKTGNIEVAGEELLILNTSKALPFPIEDNIKVSEEVRLKYRYLDLRRPSMQRNIILRHEVYQAVREFLAGNGFIEVETPMLTKSTPEGARDFLVPSRLEKGKFYALPQSPQLFKQILMVAGLERYFQIAKCFRDEDLRADRQPEFTQIDLEMSFVTEDDVMTLAESLIQYVYKKVLGIDIKIPFRRMSYEEAINKYGTDKPDLRYGLELIDITDLAKEVEFKVFNDVAKSGGLVKGINIKGGSKFSRKEIDELTEYAKKFGAKGMAWVKLENGEATSPILKFFTEEQKQKLFSLMDAKDGDLLIFIADKKDITHKVLGFLRKHIAEKMNLIDNSKLEFLWVVDFPLFEWDEEENRLVAIHHPFTSPKDEDIDRLDEALNSPEIALSFKSKAYDMVLNGEEIGGGSIRIHTPYIQEKVFQLLNISEEEAKEKFGFLIEALSYGAPPHGGLAFGLDRILALMTGSESIRDVIAFPKTQKGICPLTGAPDYVSEKQLKEVGIKVEVDEE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rickettsia africae (strain ESF-5)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.029 kDa
Sequence
MHKYRTHNCNELQISDVETEVKLSGWVHRRRDHGNLVFIDLRDHYGITQIVFTDQNPQLMEDASRLRYESVITVRGTVVARSEDTINNTLPTGHVEVLAVEFSVESAADTLPFVINTEKDAPEESRFKHRFLDLRREKLHNNIILRSQIISHIRHLMTASGFTEFQTPILTASSPEGARDFLVPSRMHPGKFYALPQAPQQFKQLLMVSGFDRYFQIAPCFRDEDARADRSPGEFYQLDVEMSFVTQEDVFSTIEPVMYDLFTKFTDKKVSETPFVCIPYNESMLKYGSDKPDLRNPIIIADVTEIFRDSDFTIFRENIKKGSIVRAIPAPKAAALPRSFFDKMIEFAVSEGAGGLGYIQFSETGEAKGPVVKFLSPQQLESLKATASISNGDAVFFASDKKEKAAKLAGKVRIRLGEELDLLEKDCFKFCWITDFPFYELNEETGKIDFSHNPFSMPQGGIDALEQAKTTEELLELTAYQYDIVCNGIELSSGAIRNHKPEIMYKAFSIAGYSEEEVDKRFGGMIRAFKFGAPPHGGIAPGIDRIVMLLAEATNIREIIAFPLNQQAEDLLMNAPSYVEDKALKELSIMLSPSARKNAEKE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rickettsia akari (strain Hartford)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.112 kDa
Sequence
MHKYRTHNCSELQISDVGQEVKLSGWVHRRRDHGNLVFIDLRDHYGIIQIVFTDQNPQLMEDASRLRYESVVTVRGTVVARSEDTINNTLPTGHVEVLAVEFIVESAADTLPFVINTEKDAPEDSRLKHRFLDLRREKLHNNIILRSQIISHIRHLMMARGFTEFQTPILTASSPEGARDFLVPSRMHPGKFYALPQAPQQFKQLLMVSGFDRYFQIAPCFRDEDARADRSPGEFYQLDLEMSFVTQEDVFSTIEPVMYDLFNKFTDKKVSATPFVRIPYNESMLKYGSDKPDLRNTIIISDVTEIFRDSDFTIFRENIRKGSIVRAIPAPKAATMPRSFFDKMIEFAISEGAGGLGYIQFSETGETKGAVAKFLSTQQLDSLKATASISNGDAVFFVSDKKEKAARLAGKVRIRLGEELDLLEKDCFKFCWITDFPFYELNEETGKIDFSHNPFSMPQGGLEALENAKTTEALLELNAYQYDIVCNGIELSSGAIRNHKPDIMYKAFSIAGYSEEEVNKRFGGMIRAFKFGAPPHGGIAPGIDRIVMLLAEATNIREVIAFPLNQQAEDLLMNAPSYVEDKALKELSIMLSPSARKNAKKE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rickettsia bellii (strain OSU 85-389)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.048 kDa
Sequence
MHKYRTHNCNELKISDVGAEVKLSGWVHRRRDHGNLVFVDLRDHYGITQIVFTDQNPQLMDDASRLRYESVVTVIGKVVARSEETINNTLPTGHIEVLAGEFIVESAADTLPFVINTEKDAPEDSRLKHRFLDLRREKLHNNIMLRSQIISYIRQLMTARGFTEFQTPILTASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLLMVSGFDRYFQIAPCFRDEDARADRSPGEFYQLDIEMSFVTQEDIFSTIEPVMYELFTKFTDKKVSEAPFIRIPYNESMLKYGSDKPDLRNPIVIADVTEIFRDSDFTIFRENIKKGSIVRAIPAPYAAAQPRSFFDKMIEFAISEGAGGLGYIQFSETGEAKGPVAKFLSTQQLEDLKATANISNGDAVFFASDKKDKAAKLAGKVRIKLADELDLLEKDCFKFCWITDFPFYELNEETGKIDFSHNPFSMPQGGLEALENAKTTEELLELTAYQYDIVCNGIELSSGAVRNHKPEIMYKAFAIAGYSEEEVDKRFGGMIRAFKFGAPPHGGIAPGIDRIVMLLAEATNIREIIAFPLNQQAEDLLMNAPNYVEDKALKELNVMLSPSARKNAEKE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rickettsia bellii (strain RML369-C)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.048 kDa
Sequence
MHKYRTHNCNELKISDVGAEVKLSGWVHRRRDHGNLVFVDLRDHYGITQIVFTDQNPQLMDDASRLRYESVVTVIGKVVARSEETINNTLPTGHIEVLAGEFIVESAADTLPFVINTEKDAPEDSRLKHRFLDLRREKLHNNIMLRSQIISYIRQLMTARGFTEFQTPILTASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLLMVSGFDRYFQIAPCFRDEDARADRSPGEFYQLDIEMSFVTQEDIFSTIEPVMYELFTKFTDKKVSEAPFIRIPYNESMLKYGSDKPDLRNPIVIADVTEIFRDSDFTIFRENIKKGSIVRAIPAPYAAAQPRSFFDKMIEFAISEGAGGLGYIQFSETGEAKGPVAKFLSTQQLEDLKATANISNGDAVFFASDKKDKAAKLAGKVRIKLADELDLLEKDCFKFCWITDFPFYELNEETGKIDFSHNPFSMPQGGLEALENAKTTEELLELTAYQYDIVCNGIELSSGAVRNHKPEIMYKAFAIAGYSEEEVDKRFGGMIRAFKFGAPPHGGIAPGIDRIVMLLAEATNIREIIAFPLNQQAEDLLMNAPNYVEDKALKELNVMLSPSARKNAEKE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rickettsia canadensis (strain McKiel)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.251 kDa
Sequence
MHKYRTHNCNALQISDVGKEVKLSGWVHRRRDHGNLVFIDLRDHYGITQIVFTDQNLQLMEMASRLRYESVITVIGKVVARSGDTINDTLTTGHIEILAREFIVESAADTLPFVINTEKDAPEDLRLKHRFLDLRREKLHNNIILRSQIISHIRHLMTARGFTEFQTPILTASSPEGARDFLVPSRMHSGKFYALPQAPQQFKQLLMVSGFDRYFQIAPCFRDEDARADRSPGEFYQLDVEMSFVTQEDVFSTIEPVMYDLFTKFTDKKVSETPFIRIPYNESMLKYGSDKPDLRNPIIIADVTEIFRDSDFTIFRENIKKGSVVRAIPAPKAAAHARSFFDKMIEFAISEGAGGLGYIQFSKNDKAKGPVAKFLSPQQLESLKATVNISDGDAVFFVSDKKEKAAKLAGKVRIRISDELDLLEKDCFKFCWITDFPFYELNEETAKIDFSHNPFSMPQGGLDALKNAKTTAELLELTAYQYDIVCNGIELSSGAIRNHKPEIMYKAFSIAGYSEEEVNKRFGSMIRAFKFGAPPHGGIAPGIDRIVMLLAEATNIREIIAFPLNQQAEDLLMNAPNYVEDKALKELGIMLLPSARKNVEQE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rickettsia conorii (strain ATCC VR-613 / Malish 7)
Length
602 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.009 kDa
Sequence
MHKYRTHNCNELQISDVETEVKLSGWVHRRRDHGNLVFIDLRDHYGITQIVFTDQNPQLMEDASRLRYESVITVRGTVVARSEDTINNTLPTGHVEVLAVEFSVESAADTLPFVINTEKDAPEESRLKHRFLDLRREKLHNNIILRSQIISHIRHLMTASGFTEFQTPILTASSPEGARDFLVPSRMHPGKFYALPQAPQQFKQLLMVSGFDRYFQIAPCFRDEDARADRSPGEFYQLDVEMSFVTQEDVFSTIEPVMYDLFTKFTDKKVSETPFVCIPYNESMLKYGSDKPDLRNPIIIADVTEIFRDSDFTIFRENIKKGSIVRAIPAPKAAALPRSFFDKMIEFAISEGAGGLGYIQFSETGEAKGPVVKFLSPQQLESLKATASISNGDAVFFASDKKEKAAKLAGKVRIRLGEELDLLEKDCFKFCWITDFPFYELNEETGKIDFSHNPFSMPQGGIDALEQAKTTEELLELTAYQYDIVCNGIELSSGAIRNHKPEIMYKAFSIAGYSEEEVDKRFGGMIRAFKFGAPPHGGIAPGIDRIVMLLAEATNIREIIAFPLNQQAEDLLMNAPSYVEDKALKELSIMLSPSARKNAEKE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Psychrobacter sp. (strain PRwf-1)
Length
601 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.395 kDa
Sequence
MMRTEYCGAVTEALLEQTITITGWIHRRRDHGGVIFLDMRDRAGILQVVVDPDTPEAFVTADAARSEYVLKITGRVRKRYEGTENANMTSGNVELLAKEIVVLAKSETPPFPLNDENISVSEDLRLKYRYLDMRRPEMQERMVFRAKATSTIRRYLDDQGFLDVETPILTRATPEGARDYLVPSRTRPGNFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQVDIETSFLSEEDIMDINEGLIQNLFKTMLDVDLGKFPRMTYAEAMRDYASDKPDLRIPLKLIDVADLMQSVDFKVFAGPANDPKGRVAALRVPNGGSLTRKQIDEYTKYVGIYGARGLAYIKVNDASNINNGVDKESGLQSPIIKNMSDEVLVSLIERTGAQDGDIIFFGADKAKIVNDAMGALRVKIGLDMNMETCEWAPLWVVDFPMFEETDDGKWTSMHHPFTMPKGSVEELKNSPETALSIAYDMVLNGTEIGGGSLRINTVEMQRAVFDALGISEEEANEKFSFLLDALKFGAPPHGGLAFGLDRLIMLMVGASSIRDVIAFPKTKTADCPLTQAPAEVDSRQLRELGIRVREKAQAENKE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Agrobacterium vitis (strain S4 / ATCC BAA-846)
Length
601 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.375 kDa
Sequence
MHRYRSHTCAALRKSDVGATVRLSGWVHRVRDHGGVLFIDLRDHYGITQVVADPDSPAFKLAETVRGEWVIRIDGVVKARADETVNKAMQTGEIELYAQEIEILAVAKELPLPVFGEPDYPEDVRLKYRFIDLRRETLHKNIVKRTQIISSMRNGMSELGFAEYTTPILTASSPEGARDFLVPSRIHEGQFFALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDVEMSFVTQEDVWTTMEPMMTKVFEQFAEGKPVTKQWPRIPYDEAIRKYGSDKPDLRNPIVMQAVTEHFADSGFKIFASMIAANPKVEVWAIPVKHTEATGAIGRAVCDRMNAWAQSTGQPGLGYIFWKEEDGKVAGSGPLAKNIGEERTAAIAAQLGLGAGDACFFVAGDPAKFYKFAGEARTRAGEELNLIDRDRFEMCWIVDFPFYEWSEEEKKIDFAHNPFSMPQGGLEAFDSQDPLTLKAYQYDAVCNGFEIASGSIRNQSPELMVKAFEKVGLSQTDVEERFGGLYRAFQYGAPPHGGCAFGIDRVVMLLVGAKNLREISLFPMNQQAQDLLMGAPAPATPTQLRELALRVVPTPKKD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432)
Length
601 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.423 kDa
Sequence
MLRTSPAGSLRAEHTAQVVTLTGWVDRRRDHGGVAFIDLRDASGIAQVVIRDEAVAHPLRNEFVLQVTGEVSRRPAGNENPNLPTGEIEVVASDVVVLNSAAALPFQVSTALADTEAIGEEVRLKYRYLDLRRPAPARAIRLRAKANQAARRVLDAEEFVEIETPTLTRSTPEGARDFLVPARLAPGSWYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDVEMSFVEQDDVIALAEKVLVALWELIGFTIPTPIPRMTFDDAMRLYGTDKPDLRFGNPIVELTSYFADTPFRVFQSEYVGAVVMAGGASLPRRQFDAWQEWAKQRGARGLAYVTFPEDGSDLGGPVAKNLSDAERAGLREATGAAPGDAVFFAAGATTPSRALLGAARQEIAKRTGLIDSADQEGAWAFVWVVDAPLFKPTGDAADDGDVALGHSAWTAVHHAFTSPTPEWIDTFEQDPGSALSNAYDIVCNGNEIGGGSIRIHRRDVQERVFQVMGIDAAEAQEKFGFLLDAFSYGAPPHGGIAFGWDRILALLTGSESIREVIAFPKSGGGYDPLTQAPAPITAEQRRESGVDAVPDDETAPQA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rhodospirillum centenum (strain ATCC 51521 / SW)
Length
601 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.205 kDa
Sequence
MHAYRTHTCGQLREQNAGETVRLSGWIHRKRDHGNLLFIDLRDHYGLTQCVIDTSNPNFGTVEGLRVESVITVTGKVVARTTETVNDKLPTGRIEVQVKELEVQSAADQVPLQVNSEQDAGEELRLRYRFLDLRREKMQRNMVLRSNVIASVRRRMIEQGFTEFQTPILTASSPEGARDFLVPARNHPGKFYALPQAPQQFKQLLMVSGFDRYFQIAPCFRDEDSRADRSPGEFYQLDFEMSFVTQDDVFAAIEPVIHGIFEEFSGFTGVKKSVSPYPFVRIPFDEAMLKYGSDKPDLRNPLVIVDVTDVFRRPDVEFKAFKGVIEKGGVVRTIRVPGVADRPRSFYDKLNDWARGLGAPGLGYIVFEGGAGKGPIAKFVPEAAQAALRQATGAVDGDAVFFVCDQPGPAAKLAGQARTEIATQLDLIAKDRFEFCWIVDFPMYEYDEERKKIDFSHNPFSMPQGGLEALETQDPLTIKAFQYDIVCNGVELSSGAIRNHRPEIMYKAFEIAGYAAEDLEAKFGGMLSAFKLGAPPHGGSAPGIDRMVMLLADEPNIREVILFPLNQRAEDLLMQAPNGVAPERLKELHLKLDLPKPKIAG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Cellvibrio japonicus (strain Ueda107)
Length
601 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.027 kDa
Sequence
MRSQYCGALNASHINQEVTLCGWVDRRRDHGGVIFIDLRDREGIVQVVFDPDGKDNFALADKVRGEYVLQVTGKVRARAAATVNPNMATGEIEVYGTALTILNEAQTIPFPLDSYANVGEDVRLKYRFLDLRRTEMQNNLRFRGKVTSAIRNYLDRHGFLDVETPILTRATPEGARDYLVPSRTHDGKFFALPQSPQLFKQLLMVAGYDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFMSQDQIMAVTEGMFRELFKDLMNIEFEEIRHMPFSEAIAKYGSDKPDMRIPLELVDIKDLVTDVDFKVFAGPANDPKARVTALKVPGGNEKLTRKQIDDYTKFVGIYGAKGLAYIKVNDKSDLEEGLQSPIVKNLPVPVRAAILERVGADNGDLIFFGADKHKVVTEALGALRCKLGADLNLYTAQWAPLWVVDFPMFEEDDKGGWTSIHHPFTSPSCTPEELVANPGAALSRAYDLVLNGVELGGGSVRIHSPAMQQAVFKILGISPEEQREKFGFLLDALSYGAPPHGGLAFGLDRLVMLMVGASSIRDVIAFPKTQSAACVMTDAPGTVDELQLRELHIRLRNQKKEQPAADAPEYGM

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype gravis)
Length
601 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.474 kDa
Sequence
MHVLRTHLAGDLGKETAGQTVTLTGWVSRRRDHGGVIFIDLRDSSGLVQVVFRENDVAEQAHHLRSEFCIKVTGEVEARPEGSENPNLASGAIEVNVTDLEILNEAAPLPFQIDDVSQGGEVGEETRLKYRYLDLRRPNQGAALRLRSQANKAARNVLDSHDFVEIETPTLTRSTPEGARDFLVPARLKPGSWYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDIEMSFVDQDDVIALAEEIVSSLWKLIGYEIPTPIPRMTYADAMRLYGSDKPDLRFDIKIVECTDFFKNTTFRVFQNEYVGAVVMDGGASQPRRQLDAWQEWAKQRGAKGLAYILVGENGELTGPVSKNITDEERAGIAAHVGAKPGDCIFFAAGETKSSRALLGAARNEIAKKLDLIKEGDWAFTWVVDAPLFEPSSDATASGDVALGHSKWTAVHHAFTSPKPEWLDSFDENPGEATAYAYDIVCNGNEIGGGSIRIHRRDVQERVFKVMGITEDEAREKFGFLLDAFAFGAPPHGGIAFGWDRIVSLLGGFSSIRDVIAFPKSGGGVDPLTDAPAPIPLEQRRETGVDFKPKKKTDESAV

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1)
Length
601 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.983 kDa
Sequence
MSKAAGSTQTLKNRFRSDYCGLLCPEREHGSVRLAGWVHRKRDHGGLIFIDLRDHTGISQLVIQPEQQELFAKAEQLHVESVICIEGVVVLRAPGAINSRLASGEIEVVVSQITVESNAHPLPFPVADEVVTSEELRLKYRFIDLRREKIHENIIFRSRLTAAIRRYLEEQDFIEIQTPILTSSSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLLMVSGFPRYFQIAPCFRDEDARADRSPGEFYQLDMEMAFIEQNDLFTILEGMIEHLTRTMSHKRITQFPFPRISYKEVMNRFGTDKPDLRIPLEISDVTPLFVGSAFKVFANSTVEGSCVKALVVKGRGNESRLFYDKAEKRAKELGSGGLAYIQFREEGPKGPVVKFLSEADLATLKEHLGLETGDVVFFGAGKWESTCKIMGGMRTYFGDLFTLDKDELSFCWIVDFPMYEYNEEAKKIDFSHNPFSMPQGEMEALETMPPLDILAYQYDIVCNGIELSSGAIRNHKPEIMYKAFGIAGYSREEVDARFGHMIEAFKLGAPPHGGIAPGLDRLVMILCDEQNIREVIAFPMNQQAQDLMMGSPSEVTPVQLKELHLKVELPKK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Variovorax paradoxus (strain S110)
Length
601 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.333 kDa
Sequence
MAMRTHYCGLVTEALMGQTVTLCGWVNRRRDHGGVIFIDVRDREGYVQVVCDPDRAATFAVAENLRNEFCVQVTGLVRARPEGTTNDQLKSGKIEVLCHELKVLNPSVTPPFLLDDDNLSETTRLTHRVLDLRRPAMQRNMMLRYKVTMETRKFLDANGFIDIETPMLGKSTPEGARDYLVPSRVHDGSFFALPQSPQLFKQLLMVAGYDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFLAEEEIREMFEGMIRNVFRNAAGIDLPVFPTMTYGDAMFKYGSDKPDLRVKLEFTELTELMKRVEFKVFSNAATMQGGRVVALRVPGGGAEGGLSRGEIDAYQEFVKIYGAKGLAYIKVNDAAAGREGLQSPIVKNLDDASLAEIIARTGARNGDILFFGADKEKIVNDAIGALRVKIGHSAFGKKSGLFDDRWAPLWVVDFPMFEFDEEGQRWSAVHHPFTAPKDGHEDLMDTAPEKCIAKAYDMVLNGIEMGGGSVRIHREEVQSKVFRALKISAEDAQLKFGFLLDALQYGAPPHGGIAIGLDRLVMLMTGAESIRDVIAFPKTQRAQDLLTQAPSPVDEKQLRELHIRLRNVQQPA

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Lactobacillus casei (strain BL23)
Length
601 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.554 kDa
Sequence
MSKRTCYAGDVTAEYVDQEVTLKGWVQKRRSLGSLIFIDLRDREGIVQLVFSEEFDKDALAVANSVRSEYVIEVQGVVKKRKPQAVNKDMKTGDVEVEVHTITILNKAKTPPFYIEDGVAVTEETKLKYRYLDLRRPEMQKNIFTRAHIMRSVHHFLDDNGFIDVETPTLTASTPEGARDYLVPSRVYPGSFYALPQSPQLFKQLLMGAGFDRYYQIARCFRDEDLRGDRQPEFTQIDLETSFLTAEEIQDITEGLIAKVMHDVKGIDVKLPFDRITWQDAMDKYGSDKPDLRFDMQIQDVSELVKDSDFKVFAGAVQNGGQVRAIVLPGGADKYSRKMIDAQQDYIKRFGAKGLAWLKVTSDSISGPIAKFFGDGADLVKAVGANAGDLVLFVADKAKVVADALGYLRTHFGHDLGLIDEQAFRFCWVVDWPLFEYDEGIQRWVPAHHPFTMPNEEDVHLLDTDPHAAHAQSYDIVLNGYELGGGSIRIHNREIQGKMLKALGFTPERAQKSFGFLLNALDYGFPPHGGLAIGLDRFVMLLTGRDNIRDVIAFPKNSKASEPMTSAPYPVADAQLKDLGIEVRADVDPEKEHEGDENLTE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Lactobacillus paracasei (strain ATCC 334 / BCRC 17002 / CIP 107868 / KCTC 3260 / NRRL B-441)
Length
601 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.596 kDa
Sequence
MSKRTCYAGDVTAEYVDQEVTLKGWVQKRRSLGSLIFIDLRDREGIVQLVFSEEFDKDALAVANSVRSEYVIEVQGVVKKRKPQAVNKDMKTGDVEVEVHTITILNKAKTPPFYIEDGVAVTEETKLKYRYLDLRRPEMQKNIFTRAHIMRSVHHFLDDNGFIDVETPTLTASTPEGARDYLVPSRVYPGSFYALPQSPQLFKQLLMGAGFDRYYQIARCFRDEDLRGDRQPEFTQIDLETSFLTAEEIQDITEGLIAKVMHDVKGIDVKLPFDRITWQDAMDKYGSDKPDLRFDMQIQDVSELVKDSDFKVFAGAVQNGGQVRAIVLPGGADKYSRKMIDAQQDYIKRFGAKGLAWLKVTSDGISGPIAKFFGDGADLVKAVGANAGDLVLFVADKAKVVADALGYLRTHFGHDLGLIDEQAFRFCWVVDWPLFEYDEGIQRWVPAHHPFTMPNEEDVHLLDTDPHAAHAQSYDIVLNGYELGGGSIRIHNREIQEKMLKALGFTPERAQKSFGFLLNALDYGFPPHGGLAIGLDRFVMLLTGRDNIRDVIAFPKNSKASEPMTSAPYPVADAQLKDLGIEVRADVDPEKEHEGDENLTE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Colwellia psychrerythraea (strain 34H / ATCC BAA-681)
Length
601 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.053 kDa
Sequence
MRSLYCGEVNESHIGQEITLCGWVNKRRDLGAVIFLDLRDREGLVQVVYDPDLPEVIKKANTLRNEFCVQIKGKVRARPEGQVNKGMKTGGIEVLGLELTILNKSAPLPLDSNQVNSEELRLKYRYLDLRRVEMTERLRFRAKVTSAVRSSLESQGFLDIETPILTAATPEGARDYLVPSRTHKGQFFALPQSPQLFKQLLMMSGMERYYQIVKCFRDEDLRADRQPEFTQIDIETSFMSSDQVMEVTEKMIRELFQELLDVDLGEFPRMPYSEAMTRFGSDKPDLRNPLELIDVDDILKDVEFKVFSGPANDENGRVAVICLPQGAAKFSRKGLDELTKFVGIYGAKGMPWLKVNDIDAALSTGVEGLQSPILKFLSSDEAIALLKRTNAKTGDIIFFGADQYNVVTESLGALRLKLGEELDLLQGEWKPLWVVDFPMFEEVDGHMHAIHHPFTAPTNLTAEQLEANPVGALSDAYDMVLNGCELGGGSVRIHNQDMQAAVFRILGISDEEAEEKFGFLLEALQYGAPPHAGLAFGLDRLVMLMTGASSIRDVMAFPKTNTAACPLTNAPGKANPEQLRELGVAVLEVKKAEENKDEEQA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Synechococcus sp. (strain JA-3-3Ab)
Length
601 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.491 kDa
Sequence
MPAAIRRPPRSLYCGQVRPAHIGQTVTLYGWIDRRRDHGGVIFLDLRDRSGIVQLVADPQKTPLSYELAGQVRSEYVVRVTGTVHQRPSDSFNPRLATGEVEVYAEELEILSRVGKQLPFSVSGEEGEEVREEIRLRYRYLDLRRERLSRNLQLRHQVIKAIRRFLEDEEGFIEVETPILTRSTPEGARDYLVPSRVNPGEWFALPQSPQLFKQLLMVAGVDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFMDQEAILELNERLLCHIFKTVKGIDLPRPFPRLTYAEAMARYGSDKPDTRFGLELVDVSPLFQGSGFKVFAKALQEGGVIKVLPVPGGDEKISNTRIKPGGDLFKLVTQYGAGGLAFIRVRPGSLDTIGALKESLSPEQEQQLLQLTNAKPGDLLLFGAGPAAVVNESLGRLRLHLGQELGLIPENALNLLWITDFPLFEFNAEENRLEALHHPFTAPHPDDLADLKTARAQAYDLVWNGVEVGGGSLRIYQREIQEQVFQTIGLTPEQARDKFGFLLEAFEYGTPPHGGIAYGLDRLVMLLAGEDSIRDVIAFPKTQQARCLLTGAPSGVEAKQLKELHVASTYQPG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Synechococcus sp. (strain JA-2-3B'a(2-13))
Length
601 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.706 kDa
Sequence
MPAAIHRPARTLYCGEVRPAHIGQTVTLYGWIDRRRDHGGVIFLDLRDRSGIVQLVADPQKTPQSYPLAGEVRNEYVVRVTGTVQQRPPDSFNPRLATGEVEIYAEQLEVLSPVGKQLPFSVSGEEAEEVREEIRLRYRYLDLRRERMSRNLQLRHRVIQAIRRFLEDEEGFVEVETPILTRSTPEGARDYLVPSRVNPGEWFALPQSPQLFKQLLMVAGVDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFMDQEGILELNERLICHIFKTVKGIHLPRPFPRLTYAEAMARYGSDKPDTRFGMELVDVSEVFQGSRFKVFAKVLAEGGLIKILPVPGGDEKISNTRIKPGGDLFKLVTQYGAGGLAFIRVRPDSLDTIGALKESLSPEQEKRLLDLTQAKPGDLLLFGAGPAAVVNESLGRLRLHLGQELGLIPENALNLLWITDFPMFEFNAEENRLEALHHPFTAPHPDDLADLKTARAQAYDLVWNGVEVGGGSLRIYQREIQEQVFQAIGLTPEQARDKFGFLLEAFEYGTPPHGGIAYGLDRLVMLLAGEDSIRDVIAFPKTQQARCLLTGAPSSVEAKQLKELHVASTYQPG

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Leptospira biflexa serovar Patoc (strain Patoc 1 / Ames)
Length
601 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.694 kDa
Sequence
MNQWVTSEYKNRISATSVSDASVGKTLFLSGWAFRYRDQGGVIFIDLRDRSGILQIVARKEILGDDFSKVEKIRSEFVIAVKGKLSLRDADSINPKMETGKYELIAESVEILNSSKTPPFTLDEFDPSGEEIRLKYRYLDMRREELRDRLVLRHKLTFALREYLDSKSFLEIETPILNKSTPEGARDFLVPSRLNAGEFYALPQSPQLFKQILMIGGMERYFQIVKCFRDEDLRADRQPEFTQLDMEFSFVTEEDIRREIEAMWAFALKKVFQLEVNAPFMTMPYHVAMEEYGSDKPDIRFGMKLVNVSEHVKSCDFQVFTGAITSGGVVKAICVPGGSVISRKEIEDLTAWLSRDYRAKGLAYMKHGANGLESTITKRFSPEALEAIAKAVGSKEGDMVFFGADSSKIVNASLGALRLKLSEKYDPPKVPYSFHWVVDFPMFEIDETTKSWTFLHHPFTSPKEEDFQKLRDWKDGKEVDLSSIGAKAYDLVLNGTEIGGGSIRIHNPEIQSLVLEAIGIGEEDAKSKFGFLLDALSFGAPPHGGIAFGVDRIMMLLTGGTSIRDVIAFPKTQKGTCMMSEAPGPVEAKQLEELKLRVVTI

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris)
Length
601 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.694 kDa
Sequence
MNQWVTSEYKNRISATSVSDASVGKTLFLSGWAFRYRDQGGVIFIDLRDRSGILQIVARKEILGDDFSKVEKIRSEFVIAVKGKLSLRDADSINPKMETGKYELIAESVEILNSSKTPPFTLDEFDPSGEEIRLKYRYLDMRREELRDRLVLRHKLTFALREYLDSKSFLEIETPILNKSTPEGARDFLVPSRLNAGEFYALPQSPQLFKQILMIGGMERYFQIVKCFRDEDLRADRQPEFTQLDMEFSFVTEEDIRREIEAMWAFALKKVFQLEVNAPFMTMPYHVAMEEYGSDKPDIRFGMKLVNVSEHVKSCDFQVFTGAITSGGVVKAICVPGGSVISRKEIEDLTAWLSRDYRAKGLAYMKHGANGLESTITKRFSPEALEAIAKAVGSKEGDMVFFGADSSKIVNASLGALRLKLSEKYDPPKVPYSFHWVVDFPMFEIDETTKSWTFLHHPFTSPKEEDFQKLRDWKDGKEVDLSSIGAKAYDLVLNGTEIGGGSIRIHNPEIQSLVLEAIGIGEEDAKSKFGFLLDALSFGAPPHGGIAFGVDRIMMLLTGGTSIRDVIAFPKTQKGTCMMSEAPGPVEAKQLEELKLRVVTI

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni (strain Fiocruz L1-130)
Length
601 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
69.082 kDa
Sequence
MKHWIQENYKNRSWAGELNESQEGKQIVLFGWSFRFRDQGGVIFIDLRDRTGIIQVVARKELLGDSFTLAEKVRSEYVLAVRGTLKKRDLESINPRMQTGTIEVVLDQLEILNVAKTPPFSLDEFDEVSEELKLKYRYLDFRREELKNRMIKRHEFIFAIRNYLNKRKFVEIETPILNKSTPEGARDFLVPSRLNPNQFYALPQSPQIFKQILMVGGMERYFQIVKCFRDEDLRADRQPEFTQLDMEFSFVSQEEILSEIEGLVETIYKEVFNIQLSIPFPRMTYNTAMEEYGSDKPDLRFGMKLVDVSEIVKDCDFNVFAGAVKNGGTVKVVCVPGGSIISRKEIEDYTAWLNRDYKAKGLAYMKHGTEGLESTITKRFKKEELEAISKACGSKEGDMLFFGADEREIVNHSLGALRLKLSERFETPKENEINITWIVDFPMFEWNKDHKRWDALHHPFTSPSDESIPFFESMETLQKNAGNATAKAYDLVMNGVEIGGGSIRIHSKEIQNKVFQVLGINEEEAKEKFGFLLEALEFGAPPHGGLAFGIDRMLMLLTGGKSIRDVIAFPKTQKGLCLMSECPSPVEEKQLQELKIKLAKV

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain 56601)
Length
601 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
69.124 kDa
Sequence
MKHWIQENYKNRSWAGELNESQEGKQIVLFGWSFRFRDQGGVIFIDLRDRTGIIQVVARKELLGDSFTLAEKVRSEYVLAVRGTLKKRDLESINPRMQTGTIEVVLDQLEILNVAKTPPFSLDEFDEVSEELKLKYRYLDFRREELKNRMIKRHEFIFAIRNYLNKRKFVEIETPILNKSTPEGARDFLVPSRLNPNQFYALPQSPQIFKQILMVGGMERYFQIVKCFRDEDLRADRQPEFTQLDMEFSFVSQEEILSEIEGLVETIYKEVFNIQLSIPFPRMTYNTAMEEYGSDKPDLRFGMKLVDVSEIVKDCDFNVFAGAVKNGGTVKVVCVPGGSIISRKEIEDYTAWLNRDYKAKGLAYMKHGTEGLESTITKRFKKEELEAISKACGSKEGDMLFFGADEREIVNHSLGALRLKLSERFETPKENEINITWIVDFPMFEWNKDHKRWDALHHPFTSPSDESIPFFESMETLQKNAGNATAKAYDLVMNGVEIGGGSIRIHSREIQNKVFQILGINEEEAKEKFGFLLEALEFGAPPHGGLAFGIDRMLMLLTGGKSIRDVIAFPKTQKGLCLMSECPSPVEEKQLQELKIKLAKV

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Delftia acidovorans (strain DSM 14801 / SPH-1)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.879 kDa
Sequence
MAMRSHYCGLVTEALMGETVTLCGWVNRRRDHGGVIFIDLRDREGYVQVVCDPDRAEMFKTAEGLRNEFCVQVKGLVRARPEGTTNDKLKSGQIEVLCHELNVLNASVTPPFQLDDENLSETVRLTNRVLDLRRPYMQRNMMLRYRTAIQVRNFLDKEGFIDIETPMLGKSTPEGARDYLVPSRVHDGEFFALPQSPQLYKQMLMVAGYDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLDEEEIRAIFQRMITEVFKTQLDVDLGEFPMMTYQDAAFRFGSDKPDLRVKLEFTELTEIMKDVDFKVFSTPATTKGGRVVALRVPGGSQISRGEIDQYTEFVKIYGAKGLAWIKVNEVAKGRDGLQSPIVKNLHDAAIAEILKRTGAQDGDLIFFGADKEKIVNDSIGALRLKVGHSEFGKANGLFENRWAPLWVVDFPMFEHDEENDRWAAVHHPFTSPKDGHEELMVTDPANCLAKAYDMVLNGWELGGGSVRIHRADVQSKVFDALKISPEDARAKFGYLLDALQYGAPPHGGLAFGLDRLITLMTGADSIRDVIAFPKTQRAQDLLTQAPSPVDEKQLRELHIRLRNPLAATQG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Desulfotomaculum reducens (strain MI-1)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.306 kDa
Sequence
MSAESMNGLHRTLYCGELHKQHEGQEVTLMGWVQRRRDHGGLIFVDLRDRSGIVQVVFSPEVDQEAFKKAEGVRNEYVLAVVGRVNGRPEGTINPNMATGEVEVYAHTLRLLNRAKTPPFYIEDNIEVDENLRLRYRYLDLRRPEMHKAMMLRHRASKSIRDFLDQHGFLEIETPMLTKSTPEGARDYLVPSRVNPGKFYALPQSPQLFKQILMLAGMERYFQIVRCFRDEDLRADRQPEFTQIDLEMSFVEAEDVMGLMEQMIAEVCSDTIGVKISTPIPRLSYQEAMDRFGSDKPDTRFGLELKDITPIAAQCGFKVFNSTVAGGGQIKGINAKGCASFSRKEIDDLTAFVAVYKAKGLAYFIINEDGSVKSAIAKFFTEEEIAAIKDKMEAQPGDLLLFVADKPAVVAASLGALRVHLAERLELIPQGMWNFLWVTDFPLLEYDSEAGRFFAMHHPFTSPAEEDLPLLESNPGKVRARAYDMVLNGVEIGGGSIRIHRRDIQELMFKALGMSQEEAKEKFGFMLEAFEYGAPPHGGLAFGLDRLVMLLAGKDSIRDVIAFPKTASATCLMTQAPDVVDPAQLAELHIRSTAPVKKSN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Teredinibacter turnerae (strain ATCC 39867 / T7901)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.172 kDa
Sequence
MRSVYCGVLTAANIGEEVTLCGWVDRRRDHGGVIFVDLRDRDGIVQVVFDPDAEDNFALADKVRPEYVLQVTGKVRARSESTVNANMATGEVEIYGTGLTILNTADTPPFQLDSFTSVGEDVRLRYRYLDLRRKEMQHNLRFRSKVTNAIRNYLDEHGFLDIETPILTRATPEGARDYLVPSRTHESKFFALPQSPQLFKQLLMVSGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFMDEEQIMSVTEGMIRKLFNDVLSIDLGDFPRMPYSEAMEKYGSDKPDMRIPLEMVEIKDLMKDVEFKVFSAPANDPKSRVTAMRVPQGGEIPRKKIDAYTKFVSIYGAKGLAYIKVNDKDDLENGLQSPIVKFLPAEVCKAILERVGAENGDLIFFGADTTKVVTEALGALRCKLGEDLDLYTCEWAPLWVVDFPMFEETDEGGLTALHHPFTAPSCSPEDLQANPATALSRAYDMVLNGTELGGGSVRIHNQDMQQAVFKILGISPEEQREKFGFLLDALKFGAPPHGGLAFGLDRLIMLMTGADSIRDVIAFPKTQSAACLMTDAPGAVDAKQLQELHIRLRAKPQAAKDEAGKEEDK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 / E264)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.79 kDa
Sequence
MSMRTEYCGLVTEHLLGQTVSLCGWVQRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFATAEGVRNEFCVQVKGLVRNRPEGTVNAGLKSGKIEVLCHELTVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDEQGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLGEQEIRDLFEDMIRHIFKTTIDVELDAKFPVMPYSEAMARFGSDKPDLRVKLEFTELTDAMKDVDFKVFSTPANTKDGRVAALRVPKGAELTRGDIDGYTEFVRIYGAKGLAWIKVNERAKGRDGLQSPIVKNLHDASIAAILERTGAQDGDIVFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVESGWKPLWVVDFPMFEYDDEEARYVAAHHPFTSPKDEHLEYLETDPGRCLAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGPEEAQAKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQCLLTQAPSPVDERQLRELHIRLRQPEQPKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Burkholderia vietnamiensis (strain G4 / LMG 22486)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.687 kDa
Sequence
MSMRTEYCGLVTEHLLGQTVSLCGWVQRRRDHGGVIFIDLRDREGLVQVVCDPDRGEMFATAEGVRNEFCVQIKGLVRNRPEGTVNAGLKSGKIEVLCHELIVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDEQGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLGEQEIRDLFEDMIRHIFKTTIDVELDAKFPVMPYSEAMARFGSDKPDLRVKLEFTELTDAMKDVDFKVFSTPANAKDGRVAALRVPKGGELSRGDIDGYTEFVRIYGAKGLAWIKVNEKAKGRDGLQSPIVKNLHDASIAAILERTGAEDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVEAGWKPLWVVDFPMFEYDDEDARYVAAHHPFTSPKDEHLEYLETDPGRCLAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGAEEAQAKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQDLLTQAPSPVDERQLRELHIRLRQPEQPKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methylacidiphilum infernorum (isolate V4)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.408 kDa
Sequence
MKKSEMKGYRTHHCNELNLALVGHKAKLCGWVHSKRDHGGLLFIDLRDREGITQVVFHPEKDPPLFAKAKQLKNEFVVKVEGKVVERPAGTKNASIPTGEIELEAESLEILNPSQPLPFNLDEDIENEELRLSFRFLDLRRKKILNCLKVRHLVSSVVREYLSREGFLEVETPILSKSTPEGARDFLVPSRLSPGKFYALPQAPQQYKQLLMVAGIDKYFQIARCFRDEDLRSDRQPEFTQIDLEASFVEVEDIMKWVEEMIQLIFLKVLGIELSLPFVRLTYSEALDNYGSDKPDLRIEWQIQDVGTVFKNTQFKLFRDVIEKGGVIKALNAKGRAPMVNSSALEELVGIATSMGAKGLAHIRVENQEWKSPIVKFFSSEERKELERLLRMEPSDLVLFSAGPREQACLILGKIRLHLAEMTQGIPGNQWKFAWITDFPLFEYSPLEQKWNSVHHPFTRPHPEDLTKLNEGKYDAIRALAYDIVLNGVELGGGSLRIYEKELQEKVFSILGIGKERQELLFGHLLKAFQYGAPPHGGIALGLDRFVMLLTGSESLREVIAFPKNRHGVDLLTQSPSEVDYQQLKELNIQLSFPSIKIEP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.237 kDa
Sequence
MLRTHLSGELRKENAGQSVTLTGWVARRRDHGGVIFIDLRDRSGIAQVVFRNEDVAERAHALRSEFVLQVTGVVEKRPEGSENPNLASGDVEVSVTDFTVLNESAPLPFQIEDASSAGEVGEETRLKYRYLDLRRPVQANALRLRSAANKAARTVLDSHDFTEIETPTLTRSTPEGARDFLVPARLKPGTFYALPQSPQLFKQLLQVAGMERYYQIARCYRDEDFRADRQPEFTQLDVEMSFVDQEDVIALAEEILTEVWKLIGYEISTPIPRITYADAMRLYGSDKPDLRFDIQITECTDFFADTTFRVFKNEYVGAVVMKGGASQPRRQLDAWQEWAKQRGAKGLAYILVGEDGELGGPVAKNITDAEREGIAAHVGAEPGDCIFFAAGDTRSSRALLGAARDEIARKLDLIRDGEWSFVWVVDAPMFESAADATASGDVALGNSKWTAVHHAFTSPKPEFLDTFDENPGEALAYAYDIVCNGNEIGGGSIRIHQRDVQERVFKVMGISEEEARDKFGFLLDAFAFGAPPHGGIAFGWDRIVSLLGGFDSIRDVIAFPKSGGGVDPLTDAPAPITPLQRKESGIDAKPKAAENKPEEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Corynebacterium jeikeium (strain K411)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.196 kDa
Sequence
MLRTHLAGELRPDNIGDEVTLTGWVGRRRDHGGVIFIDLRDRSGVAQVVFRESEVAERAHDLRSEYCLKVTGVVEARPEGSENPNLASGGIEVNVSALEVLNEAAALPFQIDDPSTSGEVGEETRLKYRYLDLRRKTQGDALRLRSRVNQAARGVLAEHDFTEIETPTLTRSTPEGARDFLVPARLRPGTFYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDVEMSFVDQEDVISLAEEILVAIWKEIGYEISTPIPRMTYADAMKYYGSDKPDLRFDIQITECTDFFKNTTFRVFQNEYVGAVVMEGGADQPRRQLDAWQEWAKQRGAKGLAYILVGEDGELSGPVAKNITDEERAGIAEHVGAKPGDCIFFAAGETKPSRALLGAARGEIANKLGLIKEGDWAFTWVVDAPLFEPAADATASGDVALGHSAWTAVHHAFTSPKPEYLDNFDENPGEALAYAYDIVCNGNEIGGGSIRIHQPDVQERVFKVMGITEEEAREKFGFLLDAFAFGAPPHGGIAFGWDRIVSLLGGFDSIRDVIAFPKSGGGVDPLTDAPGEISAAQRKESGIDFKPKKGPQGQKEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Moorella thermoacetica (strain ATCC 39073 / JCM 9320)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.678 kDa
Sequence
MVVVEGLAGLHRSHGCGELTAADAGKEVTLMGWVHRRRDHGGLIFIDLRDRSGLVQVVCDPKSGPAFQKAEEVRNEYVVAVRGLVRRRPEGTVNPKLPTGEIEVVAEEFRLLNRAKTPPFYIDDGIDVDEALRLRYRYLDLRRPEMQRLLYLRYRTTRAIRDFLDARGFWEIETPMLTRSTPEGARDFLVPSRLRPGEFFALPQSPQLFKQILMVAGVERYFQIVRCFRDEDLRADRQPEFTQLDMEMSFVQREDILKLVEELMAYVFRETLGVELALPLPRLTYREAMDRYGSDKPDIRFGMEIVDVSDLVAGCGFKVFAEAVARGGVVRGLCAPGCAGYSRRELDELTRQAAVFGAKGLAWMAVTPEGIRSPIAKFFTSGELEGLVARLAGKPGDLLLFVADTETTAATALGALRLEMGRRLHLYDPEQLAFTWVTEFPLLEYSAEEKRYVAVHHPFTMPMEEDWPLLDSDPLRVRALAYDLVLNGVELGGGSIRIHRRDIQEKMFNLLGFTPEAARDKFGFLLDAFEYGTPPHGGIAFGLDRMLMLMARRDTIRDCIPFPKTQSGTCLMTAAPSGVSPEQLQELHLRSTARKSTNPA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Wolbachia pipientis wMel
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.838 kDa
Sequence
MNCYKTHTCEELRKNDVEKEVTLSGWLYRKRDHGNLIFVDLRDFYGITQLVFNNDKDFFDEISNLKLESVITVTGIVEARTEDTVNSSISTGEIEVIVNNLRVESEVEFHFDEEIAKEERSILVSITGEQEYPENMRFKYRFLDLRREKVRNNIILRSQIIAELRKLMIERGFLEIQTPILTASSPEGARDYLVPSRLNPGKFYALPQAPQIFKQLLMVSGFDKYFQIAPCFRDEDARADRSPGEFYQLDLEMSFVTQEDIFQIIESTLYRVFAKFSRKSVDKDFPRITYKEAMLKYGSDKPDLRNPLLISDVTEIFRDSGFNIFKSNIERGMVVRAIPAPKTAEEPRSFFDKKIEHAQKEFGAKGLGYITFDKDGTAKGPIAKFLDENRLNHIREATNIEPGDSVFFASDKENEAANIAGKVRTLLGSELSLIDDNIFRFCWIIDFPYFVYDDKSKKIDFFHNPFSMPHGGLKDLEDKNPLDILAYQYDLVCNGIELSSGAIRNNKLDIMYKAFAIAGYSRGEVDTRFGALVRAFRFGVPPHGGIAPGVDRIVMLLADEPNIREVICFPMNQQGEDVLMGAPSKVEDKHLRELSLKVIE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Wolbachia pipientis subsp. Culex pipiens (strain wPip)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.57 kDa
Sequence
MNCYKTHECNELRKNDVEKEVTLSGWLYRKRDHGNLIFVDLRDFHGITQLVFNNDKDFFDEISNLKSESVITVTGIVKARTEDTVNSSISTGEIEVIVSNLQVESEVEFHCDEEIAKEERSILASIAGEQEYPENMRFKYRFLDLRREKVRNNIILRSQIISELRRLMIEQGFLDIQTPILTASSPEGARDYLVPSRLNPGKFYALPQAPQIFKQLLMVSGFDKYFQIAPCFRDEDARADRSPGEFYQLDLEMSFVTQEDIFQVIESTLYKVFAKFSRKSVDKDFPRITYKEAMLKYGSDKPDLRNPLLISDVTEIFRDSEFNIFKSNIERGMVVRAIPAPKTAEEPRSFFDKKIEHAQKEFGAKGLGYITFDKDGIAKGPIAKFLDDNRLNSIKEITNVKPGDSVFFASDKENEAATIAGKVRTLLGSELGLIDDDIFKFCWIIDFPYFVYDDKSKKIDFFHNPFSMPHGGLKDLEEKDPLDILAYQYDLVCNGIELSSGAIRNNKLNIMYRAFAIAGYSKEEVDTKFGALVRAFRFGAPPHGGIAPGVDRMVMLLADEPNIREVICFPMNQQGEDVLMGAPSKVDDKHLRELSLKVVE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Wolbachia sp. subsp. Brugia malayi (strain TRS)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.776 kDa
Sequence
MNYYKTHTCNELRKNDVEKEVTLSGWMYRKRDHGNLIFVDLRDFYGITQLVFNNDKDFFCKISDLKPESVITVTGIVKARTEDTINISISTGEIEVTVNNLQIESEVEFHHNEETAKEERSILASIADDQEYPENMRFKYRFLDLRREKVRNNIVLRSQIIAELRKFMIEQGFLEIQTPILTASSPEGARDYLVPSRLNPGKFYALPQAPQIFKQLLMISGFDKYFQIAPCFRDEDARADRSPGEFYQLDLEMSFVTQEDVFQVIESTLYKVFAKFSRKSVDKGFSRITYKEAMLKYGSDKPDLRNPLLISDVTEIFRDSEFNIFKSNIERGMVVRAIPAPKTAEEPRSFFDKKIEHTQKEFGAKGLGYITFNKDGTAKGPIAKFLDDNRLNHIREATNIKPGDSVFFASDKENEAATIAGKVRTLLGSELGLIDNNIFKFCWVVDFPYFVYDDKSKKIDFFHNPFSMPHGGLKDLEEKNPLDILAYQYDLVCNGIELSSGAIRNNKLDIMYKAFATAGYNKEEVNKKFGALVRAFRFGVPPHGGIAPGIDRIVMLLADAPNIREITCFPMNQQGEDVLMDAPSKVDNKHLRELSLKVVE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Wolbachia sp. subsp. Drosophila simulans (strain wRi)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.767 kDa
Sequence
MNCYKTHTCNELRKNDVEKEVTLSGWLYRKRDHGNLIFVDLRDFYGITQLVFNNDKDFFDEISNLKLESVITVTGIVEARTEDTVNSSISTGEIEVIVNNLRVESEVEFHFDEEIAKEERSILASITGEQEYPENMRFKYRFLDLRREKVRNNIILRSQIIAELRKLMIERGFLEIQTPILTASSPEGARDYLVPSRLNPGKFYALPQAPQIFKQLLMVSGFDKYFQIAPCFRDEDARADRSPGEFYQLDLEMSFVTQEDIFQIIESTLYRVFAKFSRKSVDKDFPRITYKEAMLKYGSDKPDLRNPLLISDVTEIFRDSGFNIFKSNIERGMVVRAIPAPKTAEEPRSFFDKKIEHAQKEFGAKGLGYITFDKDGTAKGPIAKFLDENRLNHIREATNIEPGDSVFFASDKENEAANIAGKVRTLLGSELSLIDDNIFKFCWIIDFPYFVYDDKSKKIDFFHNPFSMPHGGLKDLEDKNPLDILAYQYDLVCNGIELSSGAIRNNKLDIMYKAFAIAGYSRGEVDTRFGALVRAFRFGVPPHGGIAPGVDRIVMLLADEPNIREVICFPMNQQGEDVLMGAPSKVEDKHLRELSLKVIE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Lactobacillus reuteri (strain DSM 20016)
Length
600 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.431 kDa
Sequence
MKRTNYAGDTNEQQVGQEVVLKGWVAKRRNLGGLIFIDLWDREGIVQLVFNEKENPEAFEIANAVRNQYVLEVQGKVQLRAEKEINPDMKTGKVEVAVDEVKVLAKSETTPFDITDGVDASEDLRMKYRYLDLRRPEMMRNLKLRSKVASIVHNYYDNEGFMDVETPDLTRSTPEGARDYIVPSRVYPGHFYALPQSPQLFKQLLMAAGVDKYYQLARCFRDEDLRGDRQPEFTQIDTEMSFATPEDIQTVTEGLIKRVMKEIVGVDVKTPFPRMEWQEAMDKYGSDKPDTRFGMLIHDLSDIVKDSSFKVFANTVADGNYVRAIRVPGGADKYSRKDISKYEEYIKRFGAKGLAWVKVTADGYNGPVAKFLNDQVAQINEEMDAKEGDLILFVAGSFHVVSDSLGYLRRAIAEELDMIKPDQWNYLWVVNWPMFEYDEGFGKWIAAHHPFTMLNEEDLHYLEDGEDPHKAHAQSYDIILNGNEIGGGSIRIHDPKIQEKVLKALGYTKERAEARFGFLLKALTMGMPPEGGLAFGLDRWVMLLAQADSIRDVIPFPKNSKAVEPLTAAPGKVSEQQLDDLKIEFDEKIDYKLDQDPDEQ

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Lactobacillus reuteri (strain JCM 1112)
Length
600 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.431 kDa
Sequence
MKRTNYAGDTNEQQVGQEVVLKGWVAKRRNLGGLIFIDLWDREGIVQLVFNEKENPEAFEIANAVRNQYVLEVQGKVQLRAEKEINPDMKTGKVEVAVDEVKVLAKSETTPFDITDGVDASEDLRMKYRYLDLRRPEMMRNLKLRSKVASIVHNYYDNEGFMDVETPDLTRSTPEGARDYIVPSRVYPGHFYALPQSPQLFKQLLMAAGVDKYYQLARCFRDEDLRGDRQPEFTQIDTEMSFATPEDIQTVTEGLIKRVMKEIVGVDVKTPFPRMEWQEAMDKYGSDKPDTRFGMLIHDLSDIVKDSSFKVFANTVADGNYVRAIRVPGGADKYSRKDISKYEEYIKRFGAKGLAWVKVTADGYNGPVAKFLNDQVAQINEEMDAKEGDLILFVAGSFHVVSDSLGYLRRAIAEELDMIKPDQWNYLWVVNWPMFEYDEGFGKWIAAHHPFTMLNEEDLHYLEDGEDPHKAHAQSYDIILNGNEIGGGSIRIHDPKIQEKVLKALGYTKERAEARFGFLLKALTMGMPPEGGLAFGLDRWVMLLAQADSIRDVIPFPKNSKAVEPLTAAPGKVSEQQLDDLKIEFDEKIDYKLDQDPDEQ

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Burkholderia ambifaria (strain MC40-6)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.743 kDa
Sequence
MSMRTEYCGLVTEHLLGQTVSLCGWVQRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFATAEGVRNEFCVQIKGLVRNRPEGTVNAGLKSGKIEVLCHELNVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDEQGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLGEQEIRDLFEDMIRHIFKTTIDVELDAKFPVMPYSEAMARFGSDKPDLRVQLEFTELTDAMKDVDFKVFSTPANAKDGRVAALRVPKGGELSRGDIDGYTEFVRIYGAKGLAWIKVNEKAKGRDGLQSPIVKNLHDASIAAILERTGAEDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVQAGWKPLWVVDFPMFEYDDEDARYVAAHHPFTSPKDEHLEYLETDPGRCLAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGAEEAQLKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQDLLTQAPSPVDERQLRELHIRLRQPEQPKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Burkholderia cenocepacia (strain AU 1054)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.757 kDa
Sequence
MSMRTEYCGLVTEHLLGQTVSLCGWVQRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFATAEGVRNEFCVQIKGLVRNRPDGTVNAGLKSGRIEVLCHELNVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDEQGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLGEQEIRDLFEDMIRHIFKTTIDVELDAKFPVMPYSEAMARFGSDKPDLRVQLEFTELTDAMKDVDFKVFSTPANAKDGRVAALRVPKGGELSRGDIDGYTEFVRIYGAKGLAWIKVNEKAKGRDGLQSPIVKNLHDASIAAILERTGAEDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVQAGWKPLWVVDFPMFEYDDEDARYVAAHHPFTSPKDEHLEYLETDPGRCLAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGAEEAQLKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQDLLTQAPSPVDERQLRELHIRLRQPEQPKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Burkholderia cenocepacia (strain MC0-3)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.743 kDa
Sequence
MSMRTEYCGLVTEHLLGQTVSLCGWVQRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFATAEGVRNEFCVQIKGLVRNRPEGTVNAGLKSGKIEVLCHELNVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDEQGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLGEQEIRDLFEDMIRHIFKTTIDVELDAKFPVMPYSEAMARFGSDKPDLRVQLEFTELTDAMKDVDFKVFSTPANAKDGRVAALRVPKGGELSRGDIDGYTEFVRIYGAKGLAWIKVNEKAKGRDGLQSPIVKNLHDASIAAILERTGAEDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVQAGWKPLWVVDFPMFEYDDEDARYVAAHHPFTSPKDEHLEYLETDPGRCLAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGAEEAQLKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQDLLTQAPSPVDERQLRELHIRLRQPEQPKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Burkholderia cenocepacia (strain HI2424)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.757 kDa
Sequence
MSMRTEYCGLVTEHLLGQTVSLCGWVQRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFATAEGVRNEFCVQIKGLVRNRPDGTVNAGLKSGRIEVLCHELNVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDEQGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLGEQEIRDLFEDMIRHIFKTTIDVELDAKFPVMPYSEAMARFGSDKPDLRVQLEFTELTDAMKDVDFKVFSTPANAKDGRVAALRVPKGGELSRGDIDGYTEFVRIYGAKGLAWIKVNEKAKGRDGLQSPIVKNLHDASIAAILERTGAEDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVQAGWKPLWVVDFPMFEYDDEDARYVAAHHPFTSPKDEHLEYLETDPGRCLAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGAEEAQLKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQDLLTQAPSPVDERQLRELHIRLRQPEQPKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.701 kDa
Sequence
MSMRTEYCGLVTEHLLGQTVSLCGWVQRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFATAEGVRNEFCVQIKGLVRNRPEGTVNAGLKSGKIEVLCHELNVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDEQGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLGEQEIRDLFEDMIRHIFKTTIDVELDAKFPVMPYSEAMARFGSDKPDLRVQLEFTELTDAMKDVDFKVFSTPANAKDGRVAALRVPKGGELSRGDIDGYTEFVRIYGAKGLAWIKVNEKAKGRDGLQSPIVKNLHDASIAAILERTGAEDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVQAGWKPLWVVDFPMFEYDDEDARYVAAHHPFTSPKDEHLEYLETDPGRCLAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGAEEAQAKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQDLLTQAPSPVDERQLRELHIRLRQPEQPKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Burkholderia ambifaria (strain ATCC BAA-244 / AMMD)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.716 kDa
Sequence
MSMRTEYCGLVTEHLLGQTVSLCGWVQRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFATAEGVRNEFCVQIKGLVRNRPEGTVNAGLKSGKIEVLCHELNVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDEQGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLGEQEIRDLFEDMIRHIFKTTIDVELDATFPVMPYSEAMARFGSDKPDLRVQLEFTELTDAMKDVDFKVFSTPANAKDGRVAALRVPKGGELSRGDIDGYTEFVRIYGAKGLAWIKVNEKAKGRDGLQSPIVKNLHDASIAAILERTGAEDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVQAGWKPLWVVDFPMFEYDDEDARYVAAHHPFTSPKDEHLEYLETDPGRCLAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGAEEAQLKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQDLLTQAPSPVDERQLRELHIRLRQPEQPKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.757 kDa
Sequence
MSMRTEYCGLVTEHLLGQTVSLCGWVQRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFATAEGVRNEFCVQIKGLVRNRPEGTVNAGLKSGKIEVLCHELNVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDEQGFIDIETPMLTKSTPEGARDYLVPSRTNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLGEQEIRDLFEDMIRHIFKTTIDVELDATFPVMPYSEAMARFGSDKPDLRVQLEFTELTDAMKDVDFKVFSTPANAKDGRVAALRVPKGSELSRGDIDGYTEFVRIYGAKGLAWIKVNEKAKGRDGLQSPIVKNLHDASIAAILERTGAEDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVHAGWKPLWVVDFPMFEYDDEDARYVAAHHPFTSPKDEHLEYLETDPGRCLAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGAEEAQLKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQDLLTQAPSPVDERQLRELHIRLRQPEQPKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Burkholderia multivorans (strain ATCC 17616 / 249)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.672 kDa
Sequence
MSMRTEYCGLVTEHLLGQTVSLCGWVQRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFATAEGVRNEFCVQVKGLVRNRPEGTVNAGLKSGKIEVLCHELNVLNPSITPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDEQGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLGEQEIRDLFEDMIRHIFKTTINVELDAKFPVMPYSEAMARFGSDKPDLRVKLEFTELTDAMKDVDFKVFSTPANAKDGRVAALRVPKGAELSRGDIDGYTEFVRIYGAKGLAWIKVNEKAKGRDGLQSPIVKNLHDASIAAILERTGAEDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVEAGWKPLWVVDFPMFEYDDEDARYVAAHHPFTSPKDEHLEYLESDPGRCLAKAYDMVLNGWEIGGGSVRIHREDVQSKVFRALKIGAEEAQAKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQDLLTQAPSPVDERQLRELHIRLRQPEQPAS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Burkholderia mallei (strain NCTC 10247)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.68 kDa
Sequence
MSMRTEYCGLVTEHLLGQTVSLCGWVHRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFAAAEGVRNEFCIQVKGLVRGRPEGTINAGLKSGRIEVLCHELNVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDEQGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLGEQEIRDLFEDMIRHIFKTTIGVELDATFPVMPYSEAMARFGSDKPDLRVKLEFTELTDAMKDVDFKVFSTPANTKDGRVAALRVPKGGELTRGDIDGYTEFVRIYGAKGLAWIKVNERAKGRDGLQSPIVKNLHDASIAAILERTGAQDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVEAGWKPLWVVDFPMFEYDDEEARYVAAHHPFTSPKDEHLEYLETDPGRCLAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGPEEAQAKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQCLLTQAPSPVDERQLRELHIRLRQPEQPKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Burkholderia mallei (strain NCTC 10229)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.68 kDa
Sequence
MSMRTEYCGLVTEHLLGQTVSLCGWVHRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFAAAEGVRNEFCIQVKGLVRGRPEGTINAGLKSGRIEVLCHELNVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDEQGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLGEQEIRDLFEDMIRHIFKTTIGVELDATFPVMPYSEAMARFGSDKPDLRVKLEFTELTDAMKDVDFKVFSTPANTKDGRVAALRVPKGGELTRGDIDGYTEFVRIYGAKGLAWIKVNERAKGRDGLQSPIVKNLHDASIAAILERTGAQDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVEAGWKPLWVVDFPMFEYDDEEARYVAAHHPFTSPKDEHLEYLETDPGRCLAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGPEEAQAKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQCLLTQAPSPVDERQLRELHIRLRQPEQPKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Burkholderia mallei (strain SAVP1)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.68 kDa
Sequence
MSMRTEYCGLVTEHLLGQTVSLCGWVHRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFAAAEGVRNEFCIQVKGLVRGRPEGTINAGLKSGRIEVLCHELNVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDEQGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLGEQEIRDLFEDMIRHIFKTTIGVELDATFPVMPYSEAMARFGSDKPDLRVKLEFTELTDAMKDVDFKVFSTPANTKDGRVAALRVPKGGELTRGDIDGYTEFVRIYGAKGLAWIKVNERAKGRDGLQSPIVKNLHDASIAAILERTGAQDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVEAGWKPLWVVDFPMFEYDDEEARYVAAHHPFTSPKDEHLEYLETDPGRCLAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGPEEAQAKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQCLLTQAPSPVDERQLRELHIRLRQPEQPKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Burkholderia pseudomallei (strain 1106a)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.68 kDa
Sequence
MSMRTEYCGLVTEHLLGQTVSLCGWVHRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFAAAEGVRNEFCIQVKGLVRGRPEGTINAGLKSGRIEVLCHELNVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDEQGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLGEQEIRDLFEDMIRHIFKTTIGVELDATFPVMPYSEAMARFGSDKPDLRVKLEFTELTDAMKDVDFKVFSTPANTKDGRVAALRVPKGGELTRGDIDGYTEFVRIYGAKGLAWIKVNERAKGRDGLQSPIVKNLHDASIAAILERTGAQDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVEAGWKPLWVVDFPMFEYDDEEARYVAAHHPFTSPKDEHLEYLETDPGRCLAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGPEEAQAKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQCLLTQAPSPVDERQLRELHIRLRQPEQPKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Burkholderia pseudomallei (strain 668)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.738 kDa
Sequence
MSMRTEYCGLVTEHLLGQTVSLCGWVHRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFAAAEGVRNEFCIQVKGLVRGRPEGTINAGLKSGRIEVLCHELNVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDEQGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLGEQEIRDLFEDMIRHIFKTTIDVELDATFPVMPYSEAMARFGSDKPDLRVKLEFTELTDAMKDVDFKVFSTPANTKDGRVAALRVPKGGELTRGDIDGYTEFVRIYGAKGLAWIKVNERAKGRDGLQSPIVKNLHDASIAAILERTGAQDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVEAGWKPLWVVDFPMFEYDDEEARYVAAHHPFTSPKDEHLEYLETDPGRCLAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGPEEAQAKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQCLLTQAPSPVDERQLRELHIRLRQPEQPKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rickettsia felis (strain ATCC VR-1525 / URRWXCal2)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.976 kDa
Sequence
MHKYRTHNCNELQISDVRKEVKLSGWVHRRRDHGNLVFIDLRDHYGITQIVFTDQNQQLMEDASRLRYESVITVRGTIVARSNDTINDTLPTGHIEVLAGEFIVESAADTLPFVINTEKDAPEETRLKHRFLDLRREKLHNNIILRSQIISHIRHLMTGRGFTEFQTPILTASSPEGARDFLVPSRMHPGKFYALPQAPQQFKQLLMVSGFDRYFQIAPCFRDEDARADRSPGEFYQLDVEMSFVTQEDIFSTIEPVMYDLFTKFTAKKVSETPFVRIPYNESMLKYGSDKPDLRNPIIIADVTEIFRDSDFTIFRENIKKGSIVRAIPAPKAAALPRSFFDKMIEFAISEGAGGLGYIQFSETGEAKGPVAKFLSPQQLESLKATASISNGDAVFFASDKKEKAAKLAGKVRIRLGEELDLLEKDCFKFCWITDFPFYELNEDTGKIDFSHNPFSMPQGGLEALEQAKTTEELLELTAYQYDIVCNGIELSSGAIRNHKPEIMYKAFSMAGYSEEEVDKRFGGMIRAFKFGAPPHGGIAPGIDRIVMLLAEATNIREIIAFPLNQQAEDLLMNAPSYVEDKALKELSIMLSPSILKNMK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129)
Length
600 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.753 kDa
Sequence
MHGTATNPYRTHTAGELRASNVGQRVRLAGWVHRRRDHGGLIFVDLRDRWGITQVTFDPERGEVFSAAERLRPEWSVSVEGEVVRRPEGNENPELPTGEIEVEASSLRVLNASETPPFEIDRERPVDELTRLRYRYLDLRRERMRENILFRDRVVRYIRRYLAERDFVEVETPLLTKSTPEGARDYLVPSRLYPGQFYALPQSPQQFKQLLMVAGLERYFQIARALRDEDQRGDRQPEHTQLDLEMSYTTQDEVLQLIEGLYTEIVERLTEKRVLFKPFPRLTYAEAMERFGSDKPDLRFGLELRDVSDLARSSEFKVFRNAVEAGGSVRGLAAGGLGDLSRRELDGLTEVAREGGARGLAHLRAEGKALKGPVAKFFSAEEQAALREALGARPGDWMFFVADRDPVVFESLNRLRLHLRDRLGLADRDALAFCWITDFPLFEYNEEEGRIEPMHHMFTMPREEDIPLLDTDPLAVTGQLYDLVANGVELASGSIRIHRPDLQQKVFSIIGIDEEEAERRFGTLLRAFRYGAPPHGGIAPGIDRLVMLLRDEPNIREVMAFPKTQAARDEMMDAPSPVSEEQLRELHISLCLPPEERRNP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6)
Length
599 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.835 kDa
Sequence
MLRTHDLGSLRSEHIGQTVTLAGWVGRRRDHGGVAFVDLRDASGVAQIVVREEEVFHGLRNEYVLQVTGTVSKRPEGNENPALGTGEIEVIAEDVTVLNTSDPLPFQIDEHVEVGEEARLKHRYLDLRRPGPSRNIRLRSEANRVARDLLHHEGYVEIETPTLTRSTPEGARDFLVPARLAPGSWYALPQSPQLFKQLLQVGGFEKYYQIARCYRDEDFRADRQPEFTQLDIEASFVDQDDVIRLGENIVKAVWKLIDVEIPTPIQRITYADAMARYGSDKPDLRFGQELTELTEFFKDTNFGVFKAPYVGAVVMPGGASQARRALDAWQEWAKQRGAKGLAYVLYKEDGELAGPVAKNLTDTERAGLADAVGAKPGDCIFFAAGEKTPSRALLGAARVEIGHRTGLIDPTDWAFCWVVDAPMFEPAAAAVASGDVAVGAGQWTAVHHAFTSPKPEFLDTFDKDPESALSYAYDIVCNGNEIGGGSIRIHQRDVQERVFELMGLDKEDAQTKFGFLLEGFKYGAPPHGGIAFGWDRVVSLLAGVESIRDVIAFPKSGGGFDPLTAAPAPITAQQRKEAGVDFKPEAVKPVEARKAEAVK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Herminiimonas arsenicoxydans
Length
599 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.553 kDa
Sequence
MRTQYCGLTSEALLDQTVSLCGWVHRRRDHGGVIFIDLRDREGLVQVVCDPDRVDVFKAAEAVRNEFCLRITGIVRHRPEGTTNSNLTSGKIEVLAHELEVLNPSVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQNNLRLRYKVTMEVRKFLDAQGFIDIETPMLTKSTPEGARDYLVPSRVNAGHFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFMNEQEIRDLFEGMIRLVFKNCLNVELPNPFPVMDYATAMGMYGSDKPDMRVKLEFTDLTSIMKDVEFKVFSGAANMENGRVVGLRVPGGGAMPRSEIDAYTQFVAIYGAKGLAYIKVNEKAKGRDGLQSPIVKNIHDEALAKIIEATGAQDGDLIFFGADKAKVVNDAIGALRVKVGHSDFGKKNGLFDDEWRPLWVVDFPMFEYDEDSQRWSATHHPFTAPKDGHEDLMETNPGKCLSKAYDMVLNGWELGGGSVRIHRAEVQSKVFRALKISAEEAQLKFGFLLDALQYGAPPHGGLAFGLDRIVTMMTGAESIRDVIAFPKTQRAQCLLTQAPSEVDEKQLRELHIRLRNVEPVVKG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Length
599 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.209 kDa
Sequence
MRTHYCGDLRTTHLGETVTLYGWVDRRRDHGGVIFLDLRDRQGIVQIASSPDQTPASYPVAEGLRNEYVVQVTGVVSKRPPESLNEKIPTGEIEIYADSIILLNGVNQQLPFVVSSHEAEQVREDVRLKYRYLDLRRARLSQNLQLRHQVVKAMRRFLEDQENFLEIETPILTRSTPEGARDYLVPSRVNPGEWYALPQSPQLFKQLLMVAGMDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFMGQEEILDLNEALICHIFKVVKNIDLPRPFPRLTYQESMAKYGNDRPDTRFGLELVDVSDLLGNTGFKVFSAAVSSGGSIKAIRVPGGNETISNVRIKPGGDLFKEATEAGAKGIAYIRVRDNGEIDTIGAIKENLDEAQVKTLLQLTQAEAGDLLLFGAGDTATVDKSLSRLRLVLGEQLGLIDPDAINLLWITDFPMFEWNSDEKRFEALHHPFTAPHPDDLGDLKTARAQAYDLVMNGVEIGGGSLRIYQREVQEKVFATIGLSPEEAHEKFGFLLDAFEYGTPPHGGIAYGLDRLVMLLAKEDSIRDVIAFPKTQQASCLLTEAPAAVDKKQLKELSVASTYVPKVKVDD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bifidobacterium longum (strain DJO10A)
Length
599 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.91 kDa
Sequence
MSQTAYRTHHATEVTEALVGQKVTLAGWVDRRRDHGGVAFIDLRDSTGLVQVVIYDEDMARPLRSEFVIQITGEVRLRPDGNENTHLATGKIEVVAETIEILAKSDALPFQVSTALENESENKLPGEDVRLKYRYLDLRRPSMQHNLKLRSDMAKAARHALEDMDFTEVETPTFIKSTPEGARDFVVPARLVPGSWYALPQSPQLLKQLLMVSGVERYYQLARCYRDEDFRADRQPEFTQLDMEMAYVDQEDVMAMTEKVIAAIWKSAGYEVQLPLPRITWKDAMDKYGSDKPDLRFGNPLVELTEYFKNTPFRVFQAPYVGAVVFKGGAATPRRQFDAWQDWARQRGAKGLAYVVFGENGELKGPVAKNLSDEERNGLREAVGAEEGDAVFFAAGSRESAQLLLGAVRVELASREGLLDPKKFAFTWVVDFPLFKPTDDPDDDDVAVGHSKWTSMHHPFTMPSKDWIDKFDKDPEHAMSDSYDIVCNGEEMGGGSVRIHRDDIQARVLDVLGITKEEADEKFGFLLEAFKYGAPPHAGLALGWDRTVSILAGADSIRDVIAFPKAGGGRDPLTGAPAPISDEQRAETGVDYDPDADEN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bifidobacterium longum (strain NCC 2705)
Length
599 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.936 kDa
Sequence
MSQTAYRTHHATEVTEALVGQKVTLAGWVDRRRDHGGVAFIDLRDSTGLVQVVIYDEDMARPLRSEFVIQITGEVRLRPDGNENTHLATGKIEVVAETIEILAKSDALPFQVSTALENESENKLPGEDVRLKYRYLDLRRPSMQYNLKLRSDMAKAARHALEDMDFTEVETPTFIKSTPEGARDFVVPARLVPGSWYALPQSPQLLKQLLMVSGVERYYQLARCYRDEDFRADRQPEFTQLDMEMAYVDQEDVMAMTEKVIAAIWKSAGYEVQLPLPRITWKDAMDKYGSDKPDLRFGNPLVELTEYFKNTPFRVFQAPYVGAVVFKGGAATPRRQFDAWQDWARQRGAKGLAYVVFGENGELKGPVAKNLSDEERNGLREAVGAEEGDAVFFAAGSRESAQLLLGAVRVELASREGLLDPKKFAFTWVVDFPLFKPTDDPDDDDVAVGHSKWTSMHHPFTMPSKDWIDKFDKDPEHAMSDSYDIVCNGEEMGGGSVRIHRDDIQARVLDVLGITKEEADEKFGFLLEAFKYGAPPHAGLALGWDRTVSILAGADSIRDVIAFPKAGGGRDPLTGAPAPISDEQRAETGVDYDPDADEN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bifidobacterium longum subsp. infantis (strain ATCC 15697 / DSM 20088 / JCM 1222 / NCTC 11817 / S12)
Length
599 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.91 kDa
Sequence
MSQTAYRTHHATEVTEALVGQKVTLAGWVDRRRDHGGVAFIDLRDSTGLVQVVIYDEDMARPLRSEFVIQITGEVRLRPDGNENTHLATGKIEVVAETIEILAKSDALPFQVSTALENESENKLPGEDVRLKYRYLDLRRPSMQHNLKLRSDMAKAARHALEDMDFTEVETPTFIKSTPEGARDFVVPARLVPGSWYALPQSPQLLKQLLMVSGVERYYQLARCYRDEDFRADRQPEFTQLDMEMAYVDQEDVMAMTEKVIAAIWKSAGYEVQLPLPRITWKDAMDKYGSDKPDLRFGNPLVELTEYFKNTPFRVFQAPYVGAVVFKGGAATPRRQFDAWQDWARQRGAKGLAYVVFGENGELKGPVAKNLSDEERNGLREAVGAEEGDAVFFAAGSRESAQLLLGAVRVELASREGLLDPKKFAFTWVVDFPLFKPTDDPDDDDVAVGHSKWTSMHHPFTMPSKDWIDKFDKDPEHAMSDSYDIVCNGEEMGGGSVRIHRDDIQARVLDVLGITKEEADEKFGFLLEAFKYGAPPHAGLALGWDRTVSILAGADSIRDVIAFPKAGGGRDPLTGAPAPISDEQRAETGVDYDPDADEN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Aromatoleum aromaticum (strain EbN1)
Length
599 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.17 kDa
Sequence
MRTHYCGQVTAADLDQTVTLCGWVHRRRDHGGVIFIDLRDREGLVQVVCDPDRAETFHTAESIRNEFVIELTGKVRRRPAGTENPNLVSGEIEVLCHTLEVLNASATPPFQLDDDNLSENVRLTHRVIDLRRPQMQKNLMLRYKVAMAFRRFLDAQGFIDVETPMLTKSTPEGARDYLVPSRVHPGQFFALPQSPQLFKQLLMVAGFDRYYQITKCFRDEDLRADRQPEFTQVDIETSFLDEAEITAIMEDMIRYVFREALAVELPNPFPRMTHAEAMRRYGSDKPDLRVTLELTDVTDAVQDVAFKVFSGPATSGGRVAALRVPGGASLTRGEIDEYTKFVGIYGARGLAYIKVNDVTKPNDEGLQSPIVKNLHEEALRTILERTGAESGDLIFFGADKTKVVNDALGALRTKLGHEKGYVSGAAWTPVWVVDFPMFEYDDESKRWVACHHPFTAPKDEHVELLESAPGECLAKAYDLALNGWEIGGGSVRIHRADMQSKVFRALNIGDEEAQLKFGFLLDALKYGAPPHGGLAFGLDRVVTLMTGAESIRDVIAFPKTQRAQCLLTDAPGEVDDKQLRELHIRLRQKIETQVEVAKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Azoarcus sp. (strain BH72)
Length
599 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.094 kDa
Sequence
MRTQYCGQVTAAHLDQIVTLCGWVHRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFKTAESVRNEFVLKMTGKVRRRPAGTENANLTSGEIEVLCHEIEVLNTSATPPFQLDDENLSETVRLTNRVIDLRRPQMQKNLMLRYKVAMAFRRFLDGAGFIDVETPMLTKSTPEGARDYLVPSRVHPGQFFALPQSPQLFKQLLMVAGFDRYYQITKCFRDEDLRADRQPEFTQVDIETSFLNETEITALMEEMIRFVFKESLGVDLPSPFPRMTYAEAMRRYGSDKPDLRVTLELTEVTDLMKDVAFKVFSGPANSGGRVAAMRVPGGATLTRGEIDEYTKFVGIYGAKGLAYIKVNDASQPNETGLQSPIVKNLSEAALRGVIERTGAQSGDLIFFGADKAKVVNDAIGALRIKLGHEKGYVTGDAWRPLWVVDFPMFEYDEDDKRWTACHHPFTSPKDEHVELLKTNPGECLAKAYDLALNGWEIGGGSVRIHRADVQATVFEALNIGAEEQQVKFGFLLDALKFGAPPHGGLAFGLDRVVTMMAGAESIRDVIAFPKTQRAQCLLTNAPGEVDEKQLRELHIRLRQKVETQVEVGKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Marinobacter hydrocarbonoclasticus (strain ATCC 700491 / DSM 11845 / VT8)
Length
599 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.005 kDa
Sequence
MRSHYCGGINESHIDQEVTLCGWVHRRRDHGGVIFLDLRDRDGMSQVVVDPDTPESFALAEKVRSEFVIKVTGRVRRRPAGTENNNMPTGQVELLGKELVILNAAATPPFPLDEHVDVGEDVRLRYRFVDLRRPEMINRLRFRSRVTSYIRNFLDSRGFMDVETPILTRATPEGARDYLVPSRTHEGSFFALPQSPQLFKQLLMVSGVDRYYQIAKCFRDEDLRADRQPEFTQVDIEASFIDEETLMGLNEEMIRSLFKDVLDVELPEFPRMPYSEAMQRYGSDKPDLRIPLELQDVGDLVESVDFKVFAGPAKDPKGRVAALRVPKGAELTRKQIDDYTRFVGIYGAKGLAYIKVNELTKGAEGLQSPIVKFLGDDVALAIMERVGAEDGDIVFFGADKATVVNEALGALRIKVGHDLNMLTCEWAPMWVVDFPMFEELPDGNLTAIHHPFTAPSCSPEDLAADPANALSRAYDMVLNGTELGGGSIRIHDEKMQEAVFRILGIGEEEARAKFGFLLDALKFGCPPHGGLAFGLDRLVMLMTGSSSIRDVIAFPKTQSATCLMTQAPGEVDEKQLKELHIRLRRSAKAVEGNKAENKE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methylococcus capsulatus (strain ATCC 33009 / NCIMB 11132 / Bath)
Length
599 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.957 kDa
Sequence
MRSHRCGEVNESLLGQEVGLCGWVHRRRDHGGVIFVDLRDREGLVQVVFDPDHPEPFSLAETVRSEYVIRVVGQVRARPEGTENPNLKSGRVEVLATSLEILNRSETPPFPIESDIEVNEEMRLRYRYIDLRRPVMQQRMRLRRDITRFLRNFLDHHGFYEIETPFLTKATPEGARDYLVPSRTHPHSFFALPQSPQLYKQLLMISGMDRYYQVVRCFRDEDLRADRQPEFTQLDIETSFMNEDQIMTLMEAMIRDLFRETLNEELPDPFPRMTYAEAMRRYASDKPDLRIPLELVDIADLMAGVEFKVFAGPAADPEGRVVALKLPGGGDLSRKDIDDLTRFVGIYGAKGLAYVKVNDLGAGLEGLQSPILKFMPESTIRGILERTEAQTGDLIFFGADKARIVNESMGALRVKLGQDRGLVEKGWRPLWVTDFPMFEWDEKSGRWVALHHPFTAPKCSEEQLRQNPGRALSRAYDMVLNGTEIGGGSVRIHRTEMQQTVFDLLGIGEEEAQQKFGFLLNALRYGCPPHGGLAFGLDRLVMLMSGASSIREVMAFPKTQSAWCPLIDAPAQVNDAQLHELGIRLRKNPAVEGGTVPST

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052)
Length
599 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.011 kDa
Sequence
MGESLNGLKRTMMCGEPREEHVGKKITLMGWVQRNRKLGALEFVDLRDKTGIMQVVFGEEINAEAFEKAKGVRSEYCVAVTGEVVKRESVNENMPTGFVELKCENIKILSESETPPIYIKEDLDAAENIRLKYRYLDLRRSDMHKIFEIRSKTTKAIRDYLEENNFLDVETPILSKSSPEGARDYLVPSRNYPGMFYALPQSPQIFKQLLMVSGFDRYYQIAKCFRDEDLRANRQPEFTQVDMELSFVEQEDIMAVNEGLIAHVFKKVAGVDVQLPIKRMTFKDAMEKYGSDKPDLRFGMEITNITEDVKDLDFVVFKSAIEAGGSVRALCLKCGADLGRKPLDKLGEFVKTYKAKGLAWIQIKEDGVKSSIAKFLTDDVTNSIVKTMNAETGDAILIVADKNSVVFQSLGALRLELAKQFDLIKDKNEFNFTWITEFPLFEYSEEEERYKACHHPFTAPMDEDLDFIESDPGNVRSKAYDLVLNGEELGGGSIRIHDTALQERMFRALGLTDEVVNERFGYLLQAFKFGPPPHGGLAFGLDRMIMFLAGTENIKDVIAFPKNQNAYCYLSEAPNIVDEKQLTELGIAILPKEEKNDKE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Clostridium botulinum (strain Alaska E43 / Type E3)
Length
599 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.098 kDa
Sequence
MGEALNGLKRTMMCGEPREEHVGQKITLMGWVQRNRKLGGLDFIDLRDKTGIMQVVFGEEINAEAFEKAKGVRPEYCIAVTGEVVKRESVNENMPTGFVELKCQSLKILSESETPPIYIKENLDAAENIRLKYRYLDLRRPDMHRIFEIRSKTTKSIRDYLEKNDFLDVETPMLTKSTPEGARDYLVPSRNYPGMFYALPQSPQIFKQLLMVSGFDKYYQIVKCFRDEDLRANRQPEFTQVDMELSFVEQDDIMALNEGLIAHVFKEVAGVDVKLPIKRMTFKDAMEKYGSDKPDLRFGMEITNITEDVKDMDFVVFKSAIEAGGSVRALCLKGGAALGRKPLDKLGEFVKTYKAKGLAWIQLKEDGVKSSIAKFLTDDVTNSIIETMGAETGDAILIVADKESVVFQSLGALRLELAKQFELIKDKNEFNFTWITEFPLFEYSEEEERYTACHHPFTAPMEEDLDFLESAPGKVRSKAYDLVLNGEELGGGSIRIHDMELQQRMFKALGFTEEQAWERFGFLLQAFKFGPPPHGGLAFGLDRMIMFLAGTENIKDVIAFPKNQNAYCYLSEAPNIADEKQLTELGIGILPKQEKQEQE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Clostridium botulinum (strain Eklund 17B / Type B)
Length
599 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.248 kDa
Sequence
MGEALNGLKRTMMCGEPREEHVGQKITLMGWVQRNRKLGGLDFIDLRDKTGIMQVVFGEEINSEAFEKAKSVRPEYCIAVTGEVVKRESVNENMPTGFVELKCESLKILSESETPPIYIKENLDAAENIRLKYRYLDLRRPDMHRIFEIRSKTTKSIRDYLEKNDFLDVETPMLTKSTPEGARDYLVPSRNYRGMFYALPQSPQIFKQLLMVSGFDKYYQIVKCFRDEDLRANRQPEFTQVDMELSFVEQDDIMALNEGLIAHVFKEVAGVDVKLPIKRMTFKDAMEKYGSDKPDLRFGMEITNITEDVKDMDFVVFKSAIEAGGSVRALCLKGGATLGRKPLDKLGEFVKTYKAKGLAWIQLKEDGVKSSIAKFLTDDVTNSIIETMGAETGDAILIVADKESVVFQSLGALRLELAKQFELIKDKNEFNFTWITEFPLFEYSEEEERYTACHHPFTAPMEEDLEFLESAPGKVRSKAYDLVLNGEELGGGSIRIHDMELQQRMFKALGFTEEQAWERFGFLLQAFKFGPPPHGGLAFGLDRMIMFLAGTENIKDVIAFPKNQNAYCYLSEAPNIADEKQLTELGIGILPKQEKQEQE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Dechloromonas aromatica (strain RCB)
Length
599 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.956 kDa
Sequence
MRTHYCGQLNAALDGQIVTLCGWAHRRRDHGGVIFIDLRDREGLAQVVCDPDRADTFKIAESVRNEFCLKITGKVRPRPAGTTNANLASGEIEILCHEIEVLNPSVTPPFQLDEDNLSENVRLLHRVIDLRRPQMQNNLMLRYKTSRAFRRFLDDNGFIDIETPMLTKSTPEGARDYLVPSRVHPGQFFALPQSPQLFKQLLMVAGYDRYYQIVKCFRDEDLRADRQPEFTQVDIETSFMSEAEIMALTEKLIRTVFKEAIDVDLPDFPRMTYAEAMHRFGSDKPDLRVTLELTEVTDAFKDVAFKVFAGVANSEGGRIAAMRIPGGATLTRGEIDAYTQFVGIYGAKGLAYIKVNDASQINETGLQSPIVKNLSEASLKAVIERTGAQSGDLIFFGADKAKIVNDALGALRIKIGHEKGFVTGAKWAPLWVIDFPMFEYDDESKRWTACHHPFTSPKDEHLDLLVSDPGKCLAKAYDLALNGWELGGGSVRIHRSDVQEKVFSALNIGPEEQQAKFGFLLDALKYGAPPHGGLAFGLDRIVTMMTGAESIRDVIAFPKTQRAQCLLTDAPSGVDEKQLRELHIRLRQKVETQVEVGQP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1)
Length
599 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.943 kDa
Sequence
MRTTYCGLVSEMLLGQTVTLMGWAHRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFKAAEGVRNEFCLKIVGKVRARPAGTENANLVSGKVELLCHELEVLNPSVTPPFQLDDDNLSETTRLTHRVLDLRRPAMQKNLILRYRVAMEVRKFLDANGFIDIETPMLTKSTPEGARDYLVPSRVNEGMFFALPQSPQLFKQLLMVSGFDRYYQITKCFRDEDLRADRQPEFTQIDIETSFLDEEEIRGMFEGMIRTVFRAVMNVELPGYPVMKYAEAMHRFGSDKPDLRVKMEFTELTEVMKDVDFKVFSAPAQAKGGRVVALRVPGGGEMSRSEIDGYTEFVKIYGAKGLAWIKVNDASKGREGLQSPIVKNLHDAAIAEIIARSGARNGDLLFFGADKAKVVNDAIGALRVKIGHSDFGKSGGLFEDKWAPLWVVDFPMFEHDEEGDRWAAVHNPFTAPKDGHEDLMDTDPGKCIAKAYDMVLNGWELGGGSVRIHRAEVQSKVFSALKIGPDEAQLKFGFLLDALQYGAPPHGGLAFGLDRLVTLMTKADSIRDVIAFPKTQRAQDLLTHAPSPVDEKQLRELHIRLRNPAAGQSGV

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptomyces griseus subsp. griseus (strain JCM 4626 / NBRC 13350)
Length
599 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.773 kDa
Sequence
MHRYRSHTCGELRASDVGTDVRLSGWLHNRRDLGGILFIDLRDHYGLVQLVARPGTPGNDALAKLTKETVVRIDGKVSARGADNVNPELPTGEIEIEVTEVEVLGEAGPLPFTINTEDGVNEERRLEYRFLDLRRERMHRNIMLRSAVIASIRSKMVALGFNEMATPILTATSPEGARDFVVPSRLNPGKFYALPQAPQQFKQLLMISGFDRYFQIAPCFRDEDARADRSPGEFYQLDVEMSFVEQEDVFQPIEKLMTELFTEFGNGREVTSPFPRIPFRESMLKYGNDKPDLRAKLELVDISDVFADSGFKAFAGKHVRALPVPDTAGQSRKFFDGLGEYAVEHGAKGLAWVRVGEDGTLAGPIAKFLTETDVKTLTERLSLVPGHAVFFGAGEFDEVSKIMSAVRVEAAKRAGHFEEGVFRFCWIVDFPMYEKDEETGKIDFSHNPFSMPQGGLADLEEKDPLDILAWQYDIVCNGIELSSGAIRNHEPELMLKAFEIAGYDRETVEHEFAGMLRAFRLGAPPHGGIAPGVDRIVMLLADEPNIRETIAFPLNGNAQDLMMGAPTELDESRLRELNIQLRKPVAAKGANAPEKTAEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 / STM815)
Length
599 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.728 kDa
Sequence
MSMRSEYCGLVTEHLLGQTVSLCGWVSRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFKTAEGVRNEFCVQVKGVVRNRPEGTTNAGLKSGKIEVLCHELNVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAMEVRKYLDSRGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLSEQEIRDLFEDMTRHVFKETIGVELDAKFAVMPYSEAMSRFGSDKPDLRVKLEFTELTDAMKDVDFKVFSTPANTKDGRVAALRVPKGGELSRGDIDSYTEFVRIYGAKGLAWIKINEVAKGRDGLQSPIVKNLHDAAIAAIIERTGAQDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVEAGWKPLWVVDFPMFEYDEEENRYVAAHHPFTSPKDEHLEYLETDPGRCLAKAYDIVLNGWEIGGGSVRIFQEDVQSKVFRALKIGAEEARLKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQDLLTQAPSEVDERQLRELHIRLRQPEQKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
Length
599 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.911 kDa
Sequence
MSMRSQYCGLVTEELLGQSVSLCGWVSRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFKAAEGVRNEFCLQIKGVVRGRPEGTTNAALKSGKIEVLCHELIVLNPSITPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDSLGFIDIETPMLTKSTPEGARDYLVPSRTNPGQFFALPQSPQLFKQLLMVANFDRYYQIVKCFRDEDLRADRQPEFTQIDCETSFLSEQEIRDLFEDMIRHVFKETIGVTLDEKFPVMLYSEAMRRFGSDKPDLRVKLEFTDLTDAVRDVDFKVFSTPANTKDGRVAAIRVPKGGELSRGDIDSYTEFVRIYGAKGLAWIKVNEVAKGRDGLQSPIVKNLHDEAVKAIIERTGAQDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVETGWKPLWVVDFPMFEYDEEDNRYVAAHHPFTSPKDEHLEYLETDPARCLAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKINAEEAQAKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQCLLTQAPSEVDERQLRELHIRLRQPEPKV

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Protochlamydia amoebophila (strain UWE25)
Length
599 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
69.12 kDa
Sequence
MNLMMFDYRRSHTCGQLRKEKVNSQVTLSGWVNRRRDHGGLIFIDLRDRFGLTQLVFDPIKSPTAHLAAEKLRSEWVISVKGTVIPRQEGMTNPKLPTGEIEIMVHEMDILSKSKTPPFSVSDDLIEVNEELRLKYRYLDIRRGDVAKKLITRHQAMLAVRNYLNNQGFLEISTPILGKSTPEGARDYLVPSRVYPGNFYALPQSPQIFKQLLMISGMDRYFQIAQCFRDEDLRADRQPEFTQIDMEMSFGTPEDLMNIVEDLIKTVFKTCSNIDVPTPFKRLSHAICMEEYGCDRPDLRFGMKLHNLNHLAAQTTFSVFLDQIRENGLVKGFCIKGGADFSRKTIDEYTEFVGRLGVKGLAWIKRQENGLNSSIVKFFPESIHQQLIEEMEMEVGDIIFMIANTPSKTNQALDHLRRKIARDRNLVDPHHYEFLWVTDFPLFSWNEEEKRLQSEHHPFTSPHLEDLHLMETNPLKMRSSGYDIVLNGYEIGGGSQRIHNSDLQQKIFERLKFSPEELETKFGFFLEALNYGTPPHLGIALGLDRIIMILTQTENIRDVIAFPKTQKASDLMIECPSPVANEQLKELEIRVPDSQFSWT

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Paraburkholderia xenovorans (strain LB400)
Length
599 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.881 kDa
Sequence
MSMRSEYCGLVTEELLGQSVSLCGWVSRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFKAAEGVRNEFCLQIKGVVRARPEGTTNAALKSGKIEVLCHELIVLNPSITPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEVRKYLDAQGFIDIETPMLTKSTPEGARDYLVPSRTNPGQFFALPQSPQLFKQLLMVANFDRYYQIVKCFRDEDLRADRQPEFTQIDCETSFLSEQEIRDLFEAMIRHVFKETIGVTLDEKFPVMLYSEAMRRFGSDKPDLRVKLEFTDLTDAVRDVDFKVFSTPANTKDGRVAAIRVPKGGELSRGDIDSYTEFVRIYGAKGLAWIKVNEVAKGRDGLQSPIVKNLHDEAVKAIIERTGAQDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVESGWKPLWVIDFPMFEYDEEDNRYVAAHHPFTSPKDEHLEYLETDPARCLAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKINAEEAQAKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQCLLTQAPSEVDERQLRELHIRLRQPEPKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Synechococcus elongatus (strain PCC 7942)
Length
599 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.095 kDa
Sequence
MRTHYCGELRAEQVGTSVTLYGWVDRRRDHGGVIFVDLRDRTGTVQIVSDPERTPESYHQAEGLRNEYVVKITGRVSGRPAESLNPKLPTGEVEIYADRIEILNAVRRQLPFQVSSADEETVREDLRLRYRYLDLRRDRMNRNLQLRHQVVKAIRRFLEDEEQFIEIETPVLTKSTPEGARDYLVPSRVNPGEWFALPQSPQLFKQLLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFLSQEEIIDLNERLIAHIFKTVKGIELPRPFPRLTYAEAMDRYGSDRPDTRFGLELVDVSDVVADMGFKVFSGAVKSGGKVKILPIPDGNDRISNVRIKPGGDIFKEATEAGAAGLAYIRVRENGEIDTIGAIKDNLSDEQKAEILRRTQAQPGTLLLFGAGSTDIVNKSLDRVRQFLGKELGLIDPEALNLLWVVDFPMVEWNADEKRYEALHHPFTAPNPQDLEDLTTARAQAYDIVLNGLEIGGGSLRIYQRDIQERVFETIGLSHEEAQAKFGFLLEAFDFGTPPHGGIAYGLDRLVMLLTGEESIRDAIAFPKTQQARCLLTEAPADVSDRQLKELYVASTWQPPIKERD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
Length
599 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.094 kDa
Sequence
MRTHYCGELRAEQVGTSVTLYGWVDRRRDHGGVIFVDLRDRTGTVQIVSDPERTPESYHQAEGLRNEYVVKITGRVSGRPAESLNPKLPTGEVEIYADRIEILNAVRRQLPFQVSSADEETVREDLRLRYRYLDLRRDRMNRNLQLRHQVVKAIRRFLEDEEQFIEIETPVLTKSTPEGARDYLVPSRVNPGEWFALPQSPQLFKQLLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFLSQEEIIDLNERLIAHIFKTVKGIELPRPFPRLTYAEAMDRYGSDRPDTRFGLKLVDVSDVVADMGFKVFSGAVKSGGKVKILPIPDGNDRISNVRIKPGGDIFKEATEAGAAGLAYIRVRENGEIDTIGAIKDNLSDEQKAEILRRTQAQPGTLLLFGAGSTDIVNKSLDRVRQFLGKELGLIDPEALNLLWVVDFPMVEWNADEKRYEALHHPFTAPNPQDLEDLTTARAQAYDIVLNGLEIGGGSLRIYQRDIQERVFETIGLSHEEAQAKFGFLLEAFDFGTPPHGGIAYGLDRLVMLLTGEESIRDAIAFPKTQQARCLLTEAPADVSDRQLKELYVASTWQPPIKERD

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672)
Length
599 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.963 kDa
Sequence
MMRTNYCGQLNSSHVGQEVTLCGWVNRRRDLGGLIFIDMRDREGLVQVFFDPDRQDAFKLASELRNEFCIQLTGVVRARPESQINKDMATGEVEIFANALTIVNRSEALPLDSNQTNTEEARLKFRYLDLRRPEMAQRLKTRARITSFVRRFMDDHGFMDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEQLVRELWLDVKGVDLGDFPVMTFAEAMRRFGSDKPDLRNPLELVDVADLLKDIEFKVFSGPANDAKGRVAAIRVPGGSQLSRKQIDEYGKFIEIYGAKGLAYIKVNERAKGLEGVQSPVAKFLSEDVLSALLDRTAAQDGDILFFGADSAKVVTDALGALRLKLGRDLNLTKNNSWEPLWVVDFPMFEEDGEGGLSAMHHPFTAPRDMLPSELAANPVSAIANAYDMVINGYEVGGGSVRIHSGEMQQTVFRILGITEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLVMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPASLEELAIAVVVKGKAAQDGKSENE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
Length
598 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.855 kDa
Sequence
MLKTHSCALTQENIGTEVTLAGWVHRRRDHGGVIFIDLRDREGIVQVVFNPEQSAACLDIGKELRSEYVLQVKGTVSHRPAGTENSRMLSGLVEVVAEGAKILNTAKTPPFYINEEVEVDESLRLKYRYLDIRRQGMKNNLIIRHKTVSFMRQFLNDRGFIEIETPILIKSTPEGARDYLVPSRLFPGQFFALPQSPQQLKQLLMVAGMEKYYQVARCFRDEDLRADRQPEFTQLDMEMSFVDENDMMQLMEDLFTGLVASVRPDMKYNKKFPRISFADAMEKYGCDKPDLRFGMELADITDIGASSAFGVFKNVAAQGGAIKAISAPGCGGYNKSQQEELINLAKKYGAAGLVPISLGAESGELKDLTMEMVKSVSAKYLTLEEIKTIAERSGAKPGGLILIVAGARKMVNSVLGEMRNHLAAKLDLCDKNELSFAFVVDFPLFQWDEEGKRWDSVHHPFTAPLESDLPLMDTDPARVGSRAYDVVCNGYEIAGGSIRIHQADLQRKVFHLLGYNNEQIDERFGHLLEAFEFGAPPHGGVAPGIDRFVMLLAGETSIREVIPFPKNQAAQDLLFGAPSVVDDKQIRDLHIRIQTEKE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Dehalococcoides mccartyi (strain ATCC BAA-2100 / JCM 16839 / KCTC 5957 / BAV1)
Length
598 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.976 kDa
Sequence
MLKTHSCALTQENVGTEVTLAGWVHRRRDHGGVIFIDLRDREGIVQVVFNPEQSAACLDIGKELRSEYVLQVKGVVSHRPAGTENNRMPSGMVEVVAVHAKILNAAKTPPFYINEEVEVDESLRLKYRYLDIRRQGMKNNLIIRHKAVRFMREFLNDQGFIEIETPILIKSTPEGARDYLVPSRLFPGKFFALPQSPQQLKQLLMVAGMEKYYQVARCFRDEDLRADRQPEFTQLDMEMSFVDEEDMMKLMEDLFTGLVANVRPDMKYNKKFPRISFADATEKYGCDKPDLRFGMELADITDIGASSAFGVFKNVAAQGGAIKAISAPGCGGYNKSQQEELINLAKKYGAAGLVPISLGVENGELKDLTMEMVKSVAAKYLALEEIKTIAERSGAKPGDLILIVAGARKMVNTVLGEMRNQLAVKLNLCDKNELSFAFVVDFPLFQWDEEGKRWDSVHHPFTAPLESDMPLMDTDPGRVGSRAYDVVCNGYEIAGGSIRIHQADLQRKVFHLLGYNDEQIDERFGHLLEAFEFGAPPHGGVAPGIDRFVMLLAGETSIREVISFPKNQAAQDLLFGAPSVVDDKQIRDLHIRIQAEKE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Dehalococcoides mccartyi (strain CBDB1)
Length
598 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.939 kDa
Sequence
MLKTHSCALTQENVGTEVTLAGWVHRRRDHGGVIFIDLRDREGIVQVIFNPEQSAACLDIGKELRSEYVLQVKGVVSHRPAGTENNRMPSGMVEVVAVNAKILNAAKTPPFYINEEVEVDESLRLKYRYLDIRRQGMKNNLIIRHKAVRFMREFLNDQGFIEIETPILIKSTPEGARDYLVPSRLFPGKFFALPQSPQQLKQLLMVAGMEKYYQVARCFRDEDLRADRQPEFTQLDMEMSFVDEEDMMKLMEDLFTGLVANVRPDMKYNKKFPRISFADAMEKYGCDKPDLRFGMELADITDIGASSAFGVFKNVAAQGGAIKAISAPGCGGYNKSQQEELINLAKKYGAAGLVPISLGVENGVLKDLTMEMVKSVAAKYLALEEIKTIAERSGAKPGDLILIVAGARKMVNTVLGEMRNQLAVKLNLCDKNELSFAFVVDFPLFQWDEEGKRWDSVHHPFTAPLESDMPLMDTDPGRVGSRAYDVVCNGYEIAGGSIRIHQADLQRKVFHLLGYNDEQIDERFGHLLEAFEFGAPPHGGVAPGIDRFVMLLAGETSIREVISFPKNQAAQDLLFGAPSVVDDKQIKDLHIRIQAEKE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Anaplasma phagocytophilum (strain HZ)
Length
598 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.205 kDa
Sequence
MNMYRTHLCNALNLSHVGEEVTLSGWIFRKRDHGGILFIDLRDFYGITQLVLNESSDQELFNYARSIGLESVITVKGTVAARSEDTINTSLSTGHVEVAVHTLVTESAADALPIHVPTSTNHPEDLRLKYRFLDLRCDKVKSNMLLRSAVISEMRKAMESRGFIEVQTPILTASSPEGARDYLVPSRVHAGKFYALPQAPQIFKQLLMASGFDKYFQIAPCFRDEDARADRSPGEFYQLDVEMSFVTQEDVFSVMEPVLRDIFTKFAGNRSVSPTFPRITYKDAMLRYGTDKPDLRNPIIIADVSEVFLRSNFKTFQEGVARGMVVRAIPAPKTSEHPRSFFDSKVEYAKKIGARGLGYITFSTDNTVKGPVAKFLSDTELANIQTLAGVGPGDSVFFVSDAADKAAELSGSVRELLGTELNLIEKDTFKFCWIVDFPYFQYENGKLAFSHNPFSMPQGGLDALSSSNPLDIVAYQYDIVCNGIEISSGAIRNHKLDILYKAFSMVGYSPEAVDAEFGALTRAFRFGVPPHGGIAPGVDRIVMLLADVPNIREIIYFPLTQMGEDLLMGAPSEVNQSHLKELSLALNITPKAAGKTSS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216)
Length
598 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.725 kDa
Sequence
MLRTHEAGSLRADHAGQTVTLTGWVARRRDHGGVAFLDLRDASGVVQVVARDEILDAGGARELRNEYCIRITGDVRLRPEGNDNANIPTGAVEVDTTALEVLSEAAPLPFQIDDHLNVGEEARLKHRYLDLRRTGPANALKLRSAANRAARAVLEEHAFTEIETPTLTRSTPEGARDFLVPARLAPGSWYALPQSPQLFKQLLMVAGMERYYQLARCYRDEDFRADRQPEFTQLDIEMSFVEQDDVIALGEQIVAALWKLIGHDVPLPLPRMTYEEAMRRYGSDKPDLRFGLELVECAGFFADTTFRVFQAPYVGAVVMPGGASQPRKTLDAWQEWAKQRGARGLAYVLVGQDGELSGPVAKNLSDTERAGLAAHVGANPGDCIFFAAGAVNPSRALLGAARAEIARRTGAIDESAWSFLWVVDAPMFKSAAEDDDVSIGEGSWNAVHHAFTAPKPEVVDTFDTDPGSALSNAYDIVCNGNEIGGGSIRIHRRDVQERVFAVMGISEADAREKFGFLLDAFSFGAPPHGGIAFGWDRVVALLAGVDSIREVIAFPKSGGGYDPLTAAPAPITAQQRKEAGVDAKPETKKAAAGEPAGA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg)
Length
598 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.521 kDa
Sequence
MAESMKGLHRTHRCTELSNSNVGEIVTVMGWVQKSRNKGGIIFVDLRDRSGLLQIIFEEGDIGTEMFEKASKLRSEFVVAVVGKVETRSGAVNENLLTGTIEVRATELRILSESETPPFPIEEGSKTKEELRLKYRYLDLRRPDLVRNLMLRSKVATLTRQFLSDEGFLEIETPMLTKSTPEGARDYLVPSRVHPGNFYALPQSPQIFKQLLMVSGYDRYFQIVKCFRDEDLRADRQPEFTQIDMELSFVDVDDVISVNERLLQKMFKESIGIDVSLPIQRMTWREAMDRYGSDKPDTRFGMELKNVSELVKDCGFAVFTGALENGGSVRGINANGQGEMPRKKIDALIEFAKGYGAKGLAYLSINEDGTYKSSFSKFMTEEELSALVAAMEAKPGDLLFFAADKDKVVFDVLGNLRLEIARNLELLDKNTYNFLWVTEFPLLEYSEEEGRYTAMHHPFTMPMDEDLPLLETDPGKVRAKAYDIVLNGTEVGGGSVRIFQNNVQEKMFEVLGFTKEEAYERFGFLLNAFKYGVPPHAGLAYGLDRLVMLMAKEDSIRDVIAFPKVKDASCLLTDAPNVVDDKQLEELSIALAKKATEE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Burkholderia pseudomallei (strain K96243)
Length
598 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.462 kDa
Sequence
MRTEYCGLVTEHLLGQTVSLCGWVHRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFAAAEGVRNEFCIQVKGLVRGRPEGTINAGLKSGRIEVLCHELNVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDEQGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLGEQEIRDLFEDMIRHIFKTTIGVELDATFPVMPYSEAMARFGSDKPDLRVKLEFTELTDAMKDVDFKVFSTPANTKDGRVAALRVPKGGELTRGDIDGYTEFVRIYGAKGLAWIKVNERAKGRDGLQSPIVKNLHDASIAAILERTGAQDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVEAGWKPLWVVDFPMFEYDDEEARYVAAHHPFTSPKDEHLEYLETDPGRCLAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGPEEAQAKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQCLLTQAPSPVDERQLRELHIRLRQPEQPKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Length
598 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.17 kDa
Sequence
MLRTHAAGSLRPADAGQTVTLAGWVARRRDHGGVIFIDLRDASGVSQVVFREGDVLAAAHRLRAEFCVAVTGVVEVRPEGNENPEIPTGQIEVNATELTVLGESAPLPFQLDEQAGEEARLKYRYLDLRREGPGNALRLRSKVNAAARSVLAEHDFVEIETPTLTRSTPEGARDFLVPARLQPGSFYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDMEMSFVEADDVIAISEQVLKAVWATIGYDLPLPLPRISYEEAMRRFGSDKPDLRFGIELVECTEYFKDTTFRVFQAPYVGAVVMPGGASQPRRTLDGWQEFAKQRGHKGLAYVLVGEDGTLGGPVAKNLSDAERDGLVAHVGANPGDCIFFAAGPAKGARALLGATRIEIAKRLDLIDPNAWAFTWVVDFPMFEAADEATAAGDVAVGSGAWTAMHHAFTAPKPDSVDTFDSDPGNALSDAYDIVCNGNEIGGGSIRIHRRDIQERVFAMMGIDHDEAQEKFGFLLDAFSYGAPPHGGIAFGWDRITALLAGVDSIREVIAFPKSGGGVDPLTDAPAPITPQQRKESGIDAKPREDKPKEDAKSKA

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Agathobacter rectalis (strain ATCC 33656 / DSM 3377 / JCM 17463 / KCTC 5835 / VPI 0990)
Length
598 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.49 kDa
Sequence
MAESMQGLHRSHRCTEVSNANIGEKVTVMGWVQKRRNLGSLIFVDLRDRSGILQIVFGEENVGAEGFEKAGTLRSEFVIAVEGTVQKRTAAVNESLKTGDIEVIATSIRVLSEAQTPPFHIEENSKTSEDIRLKYRYLDLRRPDIQRNLMLRSNVLRVMRDFMANEGFLEIETPILCKSTPEGARDYLVPSRIHHGHFYALPQSPQLFKQLLMASGYDRYFQIARCFRDEDLRADRQPEFTQADMELSFVDIDDVIEVNERLLKHLFKEVINVDVEIPFKRMPWQEAMDRFGSDKPDTRFGMELCDVSEVVKDCGFGVFTGALENGGSVRGINVEGQAKMPRKKIDKLVEHAKGCGAKGLAYLCINEDGTYKSSFAKFMTEAELDALVAKMNGKPGDLLLFAADKNKIVWNVLGALRLMLGAELGLIDENKYNFLWVTEFPLLEWSDEENRFMAMHHPFTMPMEEDWDKIDSDPGAVRAKAYDIVLNGTELGGGSVRIHQDDIQEKMFEVLGFTKERAHEQFGFLLDAFSYGVPPHAGLAFGVDRICMHMLHTDNIKEVIAFPKVKDASDLMSEAPGTVDPKQLEELGIAVAAEEDEE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shewanella halifaxensis (strain HAW-EB4)
Length
598 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.589 kDa
Sequence
MRSHYCGDVNKSHVGQEVTLVGWVNRSRDLGGVVFLDLRDREGIVQVVYDPDLPEVFDVASTLRSEFCVQIKGLVRARPDSQINADMRTGEVEILGLELTILNSSAPLPINMDKNQHNTEEQRLKYRYLDLRRPEMADRIVFRSKVTSAVRRFLDGNGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMSSDQVMAKTEEMVRGLFQELLNVDLGEFPKMTFEEAMRRFGSDKPDLRNPLELIDVADIVKEVEFAVFNGPANDPEGRVAVLSIPGGAKLSRKQLDEYAKYVTIYGAKGLAWMKVNDLDKGMEGIQSPVLKFLSEDVVKALLERTGAQTGDLILFGADKANIVAESMGALRLKAGEDFDLLQGEWKPLWVVDFPMFERTSDGGLHAMHHPFTAPSNMTPEELEANPIAAISDAYDMVLNGCELGGGSVRIHDSKMQSAVFRILGINDEEATEKFGFLLEALRYGTPPHAGLAFGLDRIIMLMTGASSIRDVMAFPKTTTAACPLTNAPGFANPVQLAELGVSVVEAETKDSETKDAE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6)
Length
598 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.961 kDa
Sequence
MRSSYAGQVSEKLMGQTVTLMGWAHRRRDHGGVIFIDLRDREGLVQIVCDPDRAEMFKTAEGVRNEFCLKIVGLVRARPSGTENANLVSGKVEVLCHELEVLNPSVTPPFQIDDENLSETTRLTHRVLDLRRPQMQKNLMLRYRVSMEVRKFLDANGFIDIETPMLTKSTPEGARDYLVPSRVNDGHFFALPQSPQLFKQLLMVAGFDRYYQITKCFRDEDLRADRQPEFTQIDIETSFLSEEEIRGMFEGMIRTVFRNTIGVDLPGYPVMTYADAMHKYGSDKPDLRVKLQFTELTDVMRDVDFKVFSAPAQSKNGRVVALRVPGGADMSRGEIDGYTEFVKIYGAKGLAWIKVNDVAKGREGMQSPIVKNLHDAAIAEIIARTGVCNGDLIFFGADKAKVVNDAIGALRVKVGHSDFGKKNGLFEDKWAPLWVVDFPMFEHDDEGDRWNAVHHPFTAPKDGHEDYMDTDPGKCIAKAYDMVLNGWELGGGSVRIHKAEVQSKVFSALKIGKEDAQVKFGFLLDALQYGAPPHGGLAFGLDRIVTMMTRAESIRDVIAFPKTQRAQCLLTGAPSLVDEKQLRELHIRLRNAGAAGNA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Cyanothece sp. (strain ATCC 51142)
Length
598 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.799 kDa
Sequence
MRTHYCNHISATDIDKTVTLFGWVDRRRDHGGVIFIDLRDRTGIVQIVSDPQRTPTSYPIAETLRNEYVVKIIGQVSQRPPESLNPKIPTGEVEIYAESIELLNGVNKQLPFVVSSLEAELVKEETRLKYRYLDLRRDRMAKNLQLRHAVVKAMRRYLEDEQQFMEIETPILTRSTPEGARDYLVPSRVNPGQWYALPQSPQLFKQLLMVSGCDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFMSEEEILDLNEGLVCHIFKAVKNIELPRPFPRLTYQDAMAKYGTDRPDTRFDLTLVDVSDIVKDSGFKVFSGAVKNGGKVKVLPIPGGNDIISNVQIKPGGDLFKEATDAGAKGIAYIRVKENNKLDTIGAIKDNLTEEQKRELLARTGAKPGYLLLFGAGDTDTVNKSLSRLRLVIGQRMNLIDPEKINLLWITEFPMFEWNADEKRLEALHHPFTAPNLADLNDLATARAQAYDLVYNGVEIGGGSLRIYQKEIQEKVFETIGLSLEEAYNKFGFLLEAFEYGTPPHGGIAYGLDRLVMLLAGEESIRDVIAFPKTQQASCLLTEAPASVDTKQLKELQVKSTYKPKVKEE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Cyanothece sp. (strain PCC 8801)
Length
598 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.802 kDa
Sequence
MRTHYCGDLRATDIEQTVTLFGWVDRRRDHGGVIFIDLRDRTGIVQIVSDPQRTPDSYPDAETLRNEYVVKIVGRVSQRPPESLNPKIPTGEVEIYANSIELLNGVNKQLPFVISSLEAELVREDVRLKYRYLDLRRDRMAKNLQLRHAVVKAMRRYLEDEQQFMEIETPILTRSTPEGARDYLVPSRANPGQWYALPQSPQLFKQLLMVAGCDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFMSEEEILRLNEGLVCHIFKSVKNLDIPRPFPRLTYAKAMEKYGNDRPDTRFGLELVDVSDIVKDSGFKVFSEAVKTGGKVKILPVPGGNETISNVRIKPGGDLFREATEAGAKGIAYIRVKEDNKLDTIGAIKDNLTEDQKLELLARTGAKSGDLLLFGAGDTDTVNKSLSRLRLVIGEQLGLIDPEKINLLWITEFPMFEWNADEKRLEALHHPFTAPNPEDLDDLKTARAQAYDLVYNGVEVGGGSLRIYQKDVQEKVFATIGLSMEEAYNKFGFLLEAFEYGTPPHGGIAYGLDRLVMLLAGEDSIRDVIAFPKTQQASCLLTEAPATVDEKQLKELQVKSTYKPKTKEE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Prochlorococcus marinus (strain MIT 9301)
Length
598 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.656 kDa
Sequence
MRNKICKELNNTDIGKLVNLCGWVDRRRDHGGVIFIDLRDHSGFLQITINPDDGAALFKQAETLRNETVIMVSGIINERPKDSINTNLSTGELELKVKDLQILNQIKKNLPFPVSIHDYENTKEELRLKYRYLDLRRGKLLENLKTRHKIIKVAREFLDNFGFTEVETPLLTKSTPEGARDFLVPARLSNGEFFALPQSPQLFKQLLMVGGLDKYYQIAKCFRDEDLRADRQPEFTQLDIEMSFISEEEIISFNESLIKKIWKEVLNIKFNNAFPRMSWQEAMDNYGTDRPDTRYQMLLKDLGGILGDIGFNIFTKAIKSGGYIKSITVKGGNSSISNVRIKPGGDIFQVAKDAGAGGLAFIRVKGDELETIGAIKNNLSEEHIADILKITEAKDGDLILLGAGDKLIVNQSLDRVRQYIAKDLNLIDKSKWNFLWVTDFPMFERNEEENRYEALHHPFCSPKNIKSKDSENLKKEIESSTANAYDLVLNGLELGGGSLRIHEANLQREVLKMVGLTDKEIDEKFGFLIEALEMGAPPHGGIAFGLDRITMLIIGTDSIRETIAFPKNQQAKCLLTNAPSNVSESQLKELDIEITIDE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Prochlorococcus marinus (strain MIT 9215)
Length
598 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.588 kDa
Sequence
MRNKICKELNNTDIGKLVNLCGWVDRRRDHGGVIFIDLRDHSGFLQITINPDDGADLFKQAETLRNETVIMVSGIINERPKDSINTNLSTGELELKVKDLQVLNQIKNNLPFPVSIHDYENTKEELRLKYRYLDLRRGKLLENLKTRHKIIKVSREFLDNFGFTEVETPLLTKSTPEGARDFLVPARLSNGEFFALPQSPQLFKQLLMVGGLDKYYQIAKCFRDEDLRADRQPEFTQLDIEMSFVSEEEIISFNESLIKKIWKEVLNINFNNAFPRMSWQAAMDNYGTDRPDTRYEMLLKDLGGVLGDIGFNIFTKAIKAGGYIKSITVKGGNSSISNVRIKPGGDIFQVAQDAGAGGLAFIRVKGDELETIGAIKNNLSEEHIADILKITEAKDGDLILLGAGDKQIVNQSLDRVRQYIAKDLNLIDKSKWNFLWVTDFPMFERNEDENRYEALHHPFCSPKNIKSKDSDKMQKEIENSIANAYDLVLNGMELGGGSLRIHEANLQREVLKTVGLTDKEIDEKFGFLIEALEMGAPPHGGIAFGLDRITMLLIGADSIRETIAFPKNQQAKCLLTNAPSNVSESQLKELDIEITIDE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Prochlorococcus marinus (strain MIT 9312)
Length
598 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.614 kDa
Sequence
MRNKICDELNNTDIGKLVNLCGWVDRRRDHGGVIFIDLRDHSGFLQITINPDDGANLFKQAETLRNETVIMVSGIINERPKDSINKNLSTGKLELKVKDLQILNQIKNNLPFPVSIHDYENTKEELRLKYRYLDLRRGKLLKNLKTRHKIIKVAREFLDNFGFTEVETPLLTKSTPEGARDFLIPSRLSNGEFFALPQSPQLFKQLLMVGGLDKYYQIAKCFRDEDLRADRQPEFTQLDIEMSFISEEEIISFNESLIKKIWKEVLNINFDNAFPRMKWQAAMDNYGTDRPDTRYQMLLKDLGEVLGDIGFNIFTKAIKSGGSIKSITVKGGNSSISNVRIKPGGDIFQVAQDAGAGGLAFIRVKGDELETIGAIKNNLSEEHISDILRITEAEDGDLILLGAGDKQIVNQSLDRVRQYIAKDLNLIDTSKWNFLWVTDFPLFERNEEENRYEALHHPFCSPKNIKSKDSENLKKAIENSIANAYDLVLNGLELGGGSLRIHEANLQREVLKTVGLTDKEIDEKFGFLIEALEMGAPPHGGIAFGLDRITMLIIGADSIRETIAFPKNQQAKCLLTNAPSNVSESQLKELDIEITIDE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Prochlorococcus marinus subsp. pastoris (strain CCMP1986 / NIES-2087 / MED4)
Length
598 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.994 kDa
Sequence
MRNKICEELNKSDIGKVVNLCGWVDRRRDHGGVIFIDLRDHSGFMQITINPEDGETLFKQAEILRNETVIMVNGIVNERPKDSINKNILTGELELKVKDLQILNQIKNNLPFPISVHDYENTKEELRLKYRYLDLRRGKLLKNLKTRHKIIKAVREYLDNSGFTEVETPLLTKSTPEGARDFLVPARLSNGEFFALPQSPQLFKQLLMVGGLDKYYQIAKCFRDEDLRADRQPEFTQLDIEMSFISEEEIISFNEKLIKNVWKNVLNINFNEEFPRMTWQEAMDNYGTDRPDTRYEMLLKNLGGILGNIGFNIFTKAIQNGGAIKSITIKDGNTSISNVRIKPGGDIFKVAQDAGAGGLAFIRVKGDELETIGAIKNNLNKDHISTILKITEAKDGDLILLGAGNTQIVNQSLDRVRQYIAKDLKLIEKDKWNFLWVTDFPMFEMNEEEKRFEALHHPFCSPKNIKLEDSKELKEKIESSTAHAYDLVLNGLELGGGSLRIHQAEMQREVLRTVGLTDNQINEKFGFLIEALEMGAPPHGGIAFGVDRITMLILGEDSIRETIAFPKNQQAKCLLTNAPSNVSKSQLKELDIEITIDE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Prochlorococcus marinus (strain AS9601)
Length
598 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.594 kDa
Sequence
MRNKICEELNNTDIGKLVNLCGWVDRRRDHGGVIFIDLRDHSGFLQITINPDDGADLFKQAETLRNETVIMVSGIINERPKDSINTNLSTGELELKVKDLQILNQIKNNLPFPVSIHDYENTKEELRLKYRYLDLRRGKLLENLKKRHKIIKVAREFLDNFGFTEVETPLLTKSTPEGARDFLVPARLSNGEFFALPQSPQLFKQLLMVGGLDKYYQIAKCFRDEDLRADRQPEFTQLDIEMSFISEEEIISFNESLIKKIWKEVLNINFNNAFPRMTWQAAMDNYGTDRPDTRYQMLLKDLGGVLGNIGFNIFTKAIKSGGYIKSITVKGGNSSISNVRIKPGGDIFKVAQDAGAGGLAFIRVKGDELETIGAIKNNLSEEHIADILKITEAKDGDLILLGAGDKQIVNQSLDRVRQYIAKELNLIDKSKWNFLWVTDFPMFERNEDENRYEALHHPFCSPKNIKSKDSENLKKEIESSTANAYDLVLNGLELGGGSLRIHEANLQRQVLKTVGLTDKEIDEKFGFLIEALEMGAPPHGGIAFGLDRITMLIIGADSIRETIAFPKNQQAKCLLTNAPSNVSESQLKELDIEITIDE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Lactobacillus plantarum (strain ATCC BAA-793 / NCIMB 8826 / WCFS1)
Length
598 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.603 kDa
Sequence
MKRTTYAGLINEDYLGQTVTLQGWVQKRRDLGSLIFIDLRDREGIVQLVFSQEFSADALAVADQLRGEYVIEVQGTVVNRNADAVNDRMKTGKVEVEIHDAKILNKAKTPPFYIQDDINVSDELRLKYRYLDLRRPEMQRGLKIRNGITQAVHSYFDANGFYDIETPFLTKSTPEGARDYLVPSRVYQGHFYALPQSPQLFKQLLMGAGFDRYYQIARCFRDEDLRGDRQPEFTQIDMETSFLTAEEIQSYTEGLIKQVMKDVKGVDIKTPFTRMTWQEAMDRFGSEKPDVRFGMELKDMGVAVSNAGFKVFDNALANGGLVKAIAVPGGADQYSRKQIDAYTEYVKRFGAKGLAWMKVTDDGFSGPVAKFFKNDGDFEAITSAAAAKPGDLLLFAADSFKVVSDTLGYLRTAIAKELDLIDQDQYAYLWVVDWPLFEYDEGIERWVPAHHPFTMPNEEDVHYLNDGEDPHKAHAQSYDIILNGYELGGGSIRIHTRELQEKMFKALDFTKERAQEQFGFLLDALDMGFPPHGGLAIGLDRFAMLLSGNDNIREVIAFPKNSKASEPMTNAPSRVSDQQLADLDLNITNPVTDDEPTE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081)
Length
598 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.803 kDa
Sequence
MRTEYCGQLNLSHVGQEVTLCGWVNRRRDLGGLIFIDMRDREGIVQVFFDPDHKAAYEQASELRNEFCIQITGTVRARPDSQINKDMSTGEVEIFANTLNIINRSEPLPLDSNQTNSEEQRLKYRYLDLRRPEMADRLKTRAKITSFVRRFMDSHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTADQVREVMEKLVRELWQETKGVDLGDFPVMTFAEAMRRYGSDKPDLRNPMELVDVADLVKDVEFKVFSGPANDAKGRVAALRVPGGAQVTRKQIDEYGQFVGIYGAKGLAWLKVNDRAAGVEGVQSPIAKFLSAEVLEAILARTQAESGDILFFGADSFKVVTDAMGALRLKVGRDLALTKLDSWAPLWVVDFPMFEDDSEGGLSAMHHPFTAPKDMSPEQLAAAPTTAIANAYDMVINGYEVGGGSVRIHRTEMQQQVFGILGINEEEQREKFGFLLDALKFGTPPHAGLAFGLDRLVMLLTGTDNIRDVIAFPKTTAAACLMTDAPSFANPASLQELSISVVAKKGATDSSVEENQ

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Yersinia pseudotuberculosis serotype O:1b (strain IP 31758)
Length
598 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.642 kDa
Sequence
MRTEYCGQLNLSHVGQSVTLCGWVNRRRDLGGLIFIDMRDREGIVQVFFDPDHKAAFEQASELRNEFCIQITGTVRARPDSQINKDMSTGEVEIFANTLNIINRSEPLPLDSNQINSEEQRLKYRYLDLRRPEMADRLKSRAKITSFVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMSADQVREVMEKLVRELWQETKGVDLGDFPVMTFAEAMRRYGSDKPDLRNPLELVDVASLVKDVEFKVFSGPANDAKGRVAALRVPGGAQLSRKQIDEYGQFVGIYGAKGLAWLKVNDRAAGLEGVQSPIAKFLSAEVLDAILVATQAESGDILFFGADSYKIVTDAMGALRLKVGRDLELTRLGTWAPLWVVDFPMFEDDSEGGLTAMHHPFTAPKDMSPEQLAAAPTTAIANAYDMVINGYEVGGGSVRIHRTEMQQTVFGILGITEDEQREKFGFLLDALKFGTPPHAGLAFGLDRLVMLLTGTDNIRDVIAFPKTTAAACLMTDAPSFANPASLQELSISVVAKKGTTDAGAEENQ

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Yersinia pestis bv. Antiqua (strain Antiqua)
Length
598 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.642 kDa
Sequence
MRTEYCGQLNLSHVGQSVTLCGWVNRRRDLGGLIFIDMRDREGIVQVFFDPDHKAAFEQASELRNEFCIQITGTVRARPDSQINKDMSTGEVEIFANTLNIINRSEPLPLDSNQINSEEQRLKYRYLDLRRPEMADRLKSRAKITSFVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMSADQVREVMEKLVRELWQETKGVDLGDFPVMTFAEAMRRYGSDKPDLRNPLELVDVASLVKDVEFKVFSGPANDAKGRVAALRVPGGAQLSRKQIDEYGQFVGIYGAKGLAWLKVNDRAAGLEGVQSPIAKFLSAEVLDAILVATQAESGDILFFGADSYKIVTDAMGALRLKVGRDLELTRLGTWAPLWVVDFPMFEDDSEGGLTAMHHPFTAPKDMSPEQLAAAPTTAIANAYDMVINGYEVGGGSVRIHRTEMQQTVFGILGITEDEQREKFGFLLDALKFGTPPHAGLAFGLDRLVMLLTGTDNIRDVIAFPKTTAAACLMTDAPSFANPASLQELSISVVAKKGTTDAGAEENQ

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Yersinia pseudotuberculosis serotype IB (strain PB1/+)
Length
598 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.642 kDa
Sequence
MRTEYCGQLNLSHVGQSVTLCGWVNRRRDLGGLIFIDMRDREGIVQVFFDPDHKAAFEQASELRNEFCIQITGTVRARPDSQINKDMSTGEVEIFANTLNIINRSEPLPLDSNQINSEEQRLKYRYLDLRRPEMADRLKSRAKITSFVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMSADQVREVMEKLVRELWQETKGVDLGDFPVMTFAEAMRRYGSDKPDLRNPLELVDVASLVKDVEFKVFSGPANDAKGRVAALRVPGGAQLSRKQIDEYGQFVGIYGAKGLAWLKVNDRAAGLEGVQSPIAKFLSAEVLDAILVATQAESGDILFFGADSYKIVTDAMGALRLKVGRDLELTRLGTWAPLWVVDFPMFEDDSEGGLTAMHHPFTAPKDMSPEQLAAAPTTAIANAYDMVINGYEVGGGSVRIHRTEMQQTVFGILGITEDEQREKFGFLLDALKFGTPPHAGLAFGLDRLVMLLTGTDNIRDVIAFPKTTAAACLMTDAPSFANPASLQELSISVVAKKGTTDAGAEENQ

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Yersinia pestis
Length
598 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.642 kDa
Sequence
MRTEYCGQLNLSHVGQSVTLCGWVNRRRDLGGLIFIDMRDREGIVQVFFDPDHKAAFEQASELRNEFCIQITGTVRARPDSQINKDMSTGEVEIFANTLNIINRSEPLPLDSNQINSEEQRLKYRYLDLRRPEMADRLKSRAKITSFVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMSADQVREVMEKLVRELWQETKGVDLGDFPVMTFAEAMRRYGSDKPDLRNPLELVDVASLVKDVEFKVFSGPANDAKGRVAALRVPGGAQLSRKQIDEYGQFVGIYGAKGLAWLKVNDRAAGLEGVQSPIAKFLSAEVLDAILVATQAESGDILFFGADSYKIVTDAMGALRLKVGRDLELTRLGTWAPLWVVDFPMFEDDSEGGLTAMHHPFTAPKDMSPEQLAAAPTTAIANAYDMVINGYEVGGGSVRIHRTEMQQTVFGILGITEDEQREKFGFLLDALKFGTPPHAGLAFGLDRLVMLLTGTDNIRDVIAFPKTTAAACLMTDAPSFANPASLQELSISVVAKKGTTDAGAEENQ

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Yersinia pestis bv. Antiqua (strain Angola)
Length
598 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.642 kDa
Sequence
MRTEYCGQLNLSHVGQSVTLCGWVNRRRDLGGLIFIDMRDREGIVQVFFDPDHKAAFEQASELRNEFCIQITGTVRARPDSQINKDMSTGEVEIFANTLNIINRSEPLPLDSNQINSEEQRLKYRYLDLRRPEMADRLKSRAKITSFVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMSADQVREVMEKLVRELWQETKGVDLGDFPVMTFAEAMRRYGSDKPDLRNPLELVDVASLVKDVEFKVFSGPANDAKGRVAALRVPGGAQLSRKQIDEYGQFVGIYGAKGLAWLKVNDRAAGLEGVQSPIAKFLSAEVLDAILVATQAESGDILFFGADSYKIVTDAMGALRLKVGRDLELTRLGTWAPLWVVDFPMFEDDSEGGLTAMHHPFTAPKDMSPEQLAAAPTTAIANAYDMVINGYEVGGGSVRIHRTEMQQTVFGILGITEDEQREKFGFLLDALKFGTPPHAGLAFGLDRLVMLLTGTDNIRDVIAFPKTTAAACLMTDAPSFANPASLQELSISVVAKKGTTDAGAEENQ

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Yersinia pestis bv. Antiqua (strain Nepal516)
Length
598 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.642 kDa
Sequence
MRTEYCGQLNLSHVGQSVTLCGWVNRRRDLGGLIFIDMRDREGIVQVFFDPDHKAAFEQASELRNEFCIQITGTVRARPDSQINKDMSTGEVEIFANTLNIINRSEPLPLDSNQINSEEQRLKYRYLDLRRPEMADRLKSRAKITSFVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMSADQVREVMEKLVRELWQETKGVDLGDFPVMTFAEAMRRYGSDKPDLRNPLELVDVASLVKDVEFKVFSGPANDAKGRVAALRVPGGAQLSRKQIDEYGQFVGIYGAKGLAWLKVNDRAAGLEGVQSPIAKFLSAEVLDAILVATQAESGDILFFGADSYKIVTDAMGALRLKVGRDLELTRLGTWAPLWVVDFPMFEDDSEGGLTAMHHPFTAPKDMSPEQLAAAPTTAIANAYDMVINGYEVGGGSVRIHRTEMQQTVFGILGITEDEQREKFGFLLDALKFGTPPHAGLAFGLDRLVMLLTGTDNIRDVIAFPKTTAAACLMTDAPSFANPASLQELSISVVAKKGTTDAGAEENQ

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Yersinia pestis (strain Pestoides F)
Length
598 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.642 kDa
Sequence
MRTEYCGQLNLSHVGQSVTLCGWVNRRRDLGGLIFIDMRDREGIVQVFFDPDHKAAFEQASELRNEFCIQITGTVRARPDSQINKDMSTGEVEIFANTLNIINRSEPLPLDSNQINSEEQRLKYRYLDLRRPEMADRLKSRAKITSFVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMSADQVREVMEKLVRELWQETKGVDLGDFPVMTFAEAMRRYGSDKPDLRNPLELVDVASLVKDVEFKVFSGPANDAKGRVAALRVPGGAQLSRKQIDEYGQFVGIYGAKGLAWLKVNDRAAGLEGVQSPIAKFLSAEVLDAILVATQAESGDILFFGADSYKIVTDAMGALRLKVGRDLELTRLGTWAPLWVVDFPMFEDDSEGGLTAMHHPFTAPKDMSPEQLAAAPTTAIANAYDMVINGYEVGGGSVRIHRTEMQQTVFGILGITEDEQREKFGFLLDALKFGTPPHAGLAFGLDRLVMLLTGTDNIRDVIAFPKTTAAACLMTDAPSFANPASLQELSISVVAKKGTTDAGAEENQ

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Yersinia pseudotuberculosis serotype I (strain IP32953)
Length
598 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.642 kDa
Sequence
MRTEYCGQLNLSHVGQSVTLCGWVNRRRDLGGLIFIDMRDREGIVQVFFDPDHKAAFEQASELRNEFCIQITGTVRARPDSQINKDMSTGEVEIFANTLNIINRSEPLPLDSNQINSEEQRLKYRYLDLRRPEMADRLKSRAKITSFVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMSADQVREVMEKLVRELWQETKGVDLGDFPVMTFAEAMRRYGSDKPDLRNPLELVDVASLVKDVEFKVFSGPANDAKGRVAALRVPGGAQLSRKQIDEYGQFVGIYGAKGLAWLKVNDRAAGLEGVQSPIAKFLSAEVLDAILVATQAESGDILFFGADSYKIVTDAMGALRLKVGRDLELTRLGTWAPLWVVDFPMFEDDSEGGLTAMHHPFTAPKDMSPEQLAAAPTTAIANAYDMVINGYEVGGGSVRIHRTEMQQTVFGILGITEDEQREKFGFLLDALKFGTPPHAGLAFGLDRLVMLLTGTDNIRDVIAFPKTTAAACLMTDAPSFANPASLQELSISVVAKKGTTDAGAEENQ

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Yersinia pseudotuberculosis serotype O:3 (strain YPIII)
Length
598 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.658 kDa
Sequence
MRTEYCGQLNLSHVGQSVTLCGWVNRRRDLGGLIFIDMRDREGIVQVFFDPDHKAAFEQASELRNEFCIQITGTVRARPDSQINKDMSTGEVEIFANTLNIINRSEPLPLDSNQINSEEQRLKYRYLDLRRPEMADRLKSRAKITSFVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMSADQVREVMEKLVRELWQETKGVDLGDFPVMTFAEAMRRYGSDKPDLRNPLELVDVASLVKDVEFKVFSGPANDAKGRVAALRVPGGAQLSRKQIDEYGQFVGIYGAKGLAWLKVNDRAAGLEGVQSPIAKFLSSEVLDAILVATQAESGDILFFGADSYKIVTDAMGALRLKVGRDLELTRLGTWAPLWVVDFPMFEDDSEGGLTAMHHPFTAPKDMSPEQLAAAPTTAIANAYDMVINGYEVGGGSVRIHRTEMQQTVFGILGITEDEQREKFGFLLDALKFGTPPHAGLAFGLDRLVMLLTGTDNIRDVIAFPKTTAAACLMTDAPSFANPASLQELSISVVAKKGTTDAGAEENQ

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Burkholderia mallei (strain ATCC 23344)
Length
598 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.462 kDa
Sequence
MRTEYCGLVTEHLLGQTVSLCGWVHRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFAAAEGVRNEFCIQVKGLVRGRPEGTINAGLKSGRIEVLCHELNVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDEQGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLGEQEIRDLFEDMIRHIFKTTIGVELDATFPVMPYSEAMARFGSDKPDLRVKLEFTELTDAMKDVDFKVFSTPANTKDGRVAALRVPKGGELTRGDIDGYTEFVRIYGAKGLAWIKVNERAKGRDGLQSPIVKNLHDASIAAILERTGAQDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVEAGWKPLWVVDFPMFEYDDEEARYVAAHHPFTSPKDEHLEYLETDPGRCLAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGPEEAQAKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQCLLTQAPSPVDERQLRELHIRLRQPEQPKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Burkholderia pseudomallei (strain 1710b)
Length
598 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.462 kDa
Sequence
MRTEYCGLVTEHLLGQTVSLCGWVHRRRDHGGVIFIDLRDREGLVQVVCDPDRAEMFAAAEGVRNEFCIQVKGLVRGRPEGTINAGLKSGRIEVLCHELNVLNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLRLRYRVAIEARKYLDEQGFIDIETPMLTKSTPEGARDYLVPSRVNAGQFFALPQSPQLFKQLLMVANFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLGEQEIRDLFEDMIRHIFKTTIGVELDATFPVMPYSEAMARFGSDKPDLRVKLEFTELTDAMKDVDFKVFSTPANTKDGRVAALRVPKGGELTRGDIDGYTEFVRIYGAKGLAWIKVNERAKGRDGLQSPIVKNLHDASIAAILERTGAQDGDIIFFAADRAKVVNDSLGALRLKIGHSEFGKANGLVEAGWKPLWVVDFPMFEYDDEEARYVAAHHPFTSPKDEHLEYLETDPGRCLAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGPEEAQAKFGFLLDALQYGAPPHGGIAFGLDRIVTMMAGADSIRDVIAFPKTQRAQCLLTQAPSPVDERQLRELHIRLRQPEQPKA

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Pectobacterium carotovorum subsp. carotovorum (strain PC1)
Length
598 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.73 kDa
Sequence
MRTNYCGQLNSSHVGQEVTLCGWVNRRRDLGGLIFIDMRDREGLVQVFFDPDRQDAFKLASELRNEFCIQLTGVVRARPESQINKDMATGEVEIFANALTIVNRSEALPLDSNQTNTEEARLKYRYLDLRRPEMAQRLKTRARITSFVRRFMDEHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEKLVRELWLDVKGVDLGDFPIMTFAEAMRRFGSDKPDLRNPLELVDVADLVKNIDFKVFSGPANDAKGRVAAIRVPGGAQLSRKQIDEYGKFIEIYGAKGLAYIKLNERAKGLEGVQSPVAKFLNADMLSALLDRTAAQDGDILFFGADSAKVVTDALGALRLKLGRDLSLTKDDSWEPLWVVDFPMFEEDGEGGLAAMHHPFTAPRDMLPSELAANPVSAIANAYDMVINGYEVGGGSVRIHNGDMQQTVFSILGITEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLVMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPASLEELAIAVVVKGKAAQDGKSENE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Gluconobacter oxydans (strain 621H)
Length
598 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.287 kDa
Sequence
MHPYRTHDCSALREENAGQVVRLSGWVHSKRDHGGLLFIDLRDHYGVTQIVIPAGTDLLEKAERLRVESVITVTGKVVVRHGSQRNPNLPTGDVEVLADALEVRSSAEVLPFQVAGNENYPEDLRLKYRYIDLRRDKMHQNIMLRSKVITSLRQRMIEQGFTEFQTPILTASSPEGARDFLVPARLHPGKFYALPQAPQQFKQLAMVAGFDRYFQIAPCFRDEASRADRSPGEFYQLDFEMSFVTQEDVFTVLEPVLAGVFNEFTPEGWKITDGAFPRIPYADAMRDYGSDKPDLRNPLIIKDVTDAFRDSGFGLFAKIAASGGQIRAIPAPGAGDRPRGFFDKLNSWARENGAGGLGYIIFGEEGGKGPIVKNLEADRVESIREICGLKAGDAVFFAAGKGDEVAKFSGVVRTKVATELDLIEKNAFRFCWVVDFPMYELNEETGKVDFSHNPFSMPQGGLEALNTQDPLTINAYQYDIVCNGVELSSGAIRNHLPDVMLRAFEIAGYGPEVVEERFGGMLNAFRYGAPPHGGAAPGVDRIVMLLADEPNIREVILFPLNQSGEDLMMEAPAPVEPARLKELHLALDLPKPKPTASK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Desulfatibacillum aliphaticivorans
Length
597 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.405 kDa
Sequence
MADLLGSMRRTHNCGVLRKEDTGKTVTLMGWAQRWRDHGGVIFIDLRDRYGVTQVVFNPENNAEVHKLADSIRSEWVIAVQGEVLERPDGMVNPKMETGEIEVMVSDLKILNKSKTPPFMVEDNAEVSENLRLEYRYLDLRRPRIAKNIMLRHQVGACVRAFLNENEFLDIETPVLTKSTPEGARDYLVPSRVNTGLFYALPQSPQLFKQLLMVAGYDRYYQIVRCFRDEDLRADRQPEFTQIDLEMSFVGEEDVMGIAEQMIAKVFKDVMGKEVKTPFDRLTYKDAMDRYGLDKPDLRFDLELKEVSSIVEGSDFKVFASVVKKGGMVKAMNAKGCAHFSRKVIDDLTAFVAVYGAKGLAWIKVKEDGSWQSPIAKFFTDDEKAAMAQTLDMAPGDLIFFVADNVKVTNDALGHLRNRVAKELGLIDENEFRFVWVTEFPLVEYDETDKRYVALHHPFTAPMEEDLDLLESDPGAVRSRAYDMVLNGTELGGGSIRIHQPEMQEKVFNMLGLGQEEAEEKFGFLLKALAFGAPPHGGLAFGFDRLIMLLSGENSIRDIIPFPKTQKAACLLTDAPSEVAFEQLAELALRIKKDPAS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Desulfococcus oleovorans (strain DSM 6200 / Hxd3)
Length
597 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.838 kDa
Sequence
MVDTLGNMRRTHTCNELSAASAGTEVVLAGWVQRRRDHGGVIFVDLRDREGITQVVFNPDREPAVHAKAHDIRNEYVICVKGKVEKRPDDMVNPKLTTGEIEVAASELAILNTAKTPPFMVEDRIDVSESIRLKHRFVDLRRPAMQKNLLARHRAGMAAREFLNSQGFLDIETPFLTRNTPEGARDYLVPSRVNPGAFYALPQSPQLFKQMLMVAGFDRYYQIVRCFRDEDLRADRQPEFTQIDLEMSFVGEEDVMAIGEGLVANVVRQVTGEAVDLPFSRMTYDQAMADYGLDKPDLRFDMKLVDITDIAAGCGFQVFSGAVKNGGIVKALNAKGCADFTRKELDDYTEFVAIYKARGLAWVKVREDGWQSPIAKFFTDDEKASMAQRLNMAVGDLVFFGADAASVVNDSLGNLRNRIGERLGLVDKNRMCFLWVTDFPFFEYDETEKRYQAKHHPFTAPHEADMEHLHTDPEAVRSRAYDLVLNGTEIGGGSIRIHNRQVQEKMFEALGLAPEDYTAKFGFLLDALDSGAPPHGGMAFGFDRLVMLLCGESSIREVIAFPKTQKAACALTDAPSPADKKQLDELFIKVTADINKE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Thiobacillus denitrificans (strain ATCC 25259)
Length
597 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.893 kDa
Sequence
MRTHYCGAVTAADVGNTVTLCGWAHRRRDHGGVIFIDLRDREGMVQVVVDPDTPAAFKLAEDVRAEFVLKIEGKVRPRPAGTENPHLPTGMVEVLTLDLDVLNPSLTPPFQIDDETINENIRLQYRYLDLRREPMQKNLKLRYRVSKIMRDYLDTHGFMEVETPMLTRSTPEGARDYLVPSRVHDGMFYALPQSPQLFKQLLMVSGVDRYFQITKCFRDEDLRADRQPEFTQVDLETSFMGEEAIMGLVEGMIRDMMQKAQGIELPAAFPRMSYAEAMNRYGSDKPDLRVTLEIVDVGDVMRDVAFKVFATPANDPKGRVAALRIPGGATLSRSEIDGYTEFVKIYGAKGLAYIKVNDVGQLNEAGLQSPIVKNLSEAALHAVMERTGAQNGDLIFFGADRAKVVNDALGALRLKIGHEKGHVDGRAWAPLWVVDFPMFEYNEDENRWDALHHPFTAPKDGHEDWLATDPGKCLSKAYDMVLNGWEVGGGSVRIHREKVQEKVFAALNIGEEERREKFGFLLDALQYGAPPHGGLAFGLDRLVTLMAGAESIRDVIAFPKTQRASCLMTNAPNVVDEKQLRELHIRLRNPIAADKAA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bartonella quintana (strain Toulouse)
Length
597 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.815 kDa
Sequence
MHRYRSHNCAALRKHDVGKHVRLSGWVHRVRDHGGILFVDLRDHFGITQIVANPASPAFEIIEKVRSEWVIRVDGEVCARSDEVINTVLPTGEIEIFVKEVEILSKSDELPLPVFGEPDYPEDIRLKYRFLDLRRETMHKNIMRRTEIITAIRRSMQNNGFTEFTTPLLTASSPEGARDFLVPSRIHQGKFYALPQAPQQYKQLLMMSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDVEMSFVEQEDVFVTMEPIMRSIFEEFANGKPVTQNFPRISYDEAIKKYGSDKPDLRNPIIMQDVSQHFYDSCFKIFAQILTNDENAQVWAIPAKTGGSRAFCDRMNLWAQSEGQPGLGYIFWREEEGKFEGAGPIAKNIGEQRTEALRIQLGLESGDACFFIAGNPKKFSTFAGAVRTRIGEELDLIDRECFSLAWIVDFPFFEWNEDEKKLDFAHNPFSMPQGGKNALECQDPLTLKAFQYDLVCNGYEIASGGIRNHSPEMMLKVFNLAGLSREVVEDRFGALYRAFHYGAPPHGGMAAGVDRIIMLLQGVKNLREIALFPMNQQALDLLMSAPSDVSSAQLRDLGIRVAPAAKNGS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bartonella tribocorum (strain CIP 105476 / IBS 506)
Length
597 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.738 kDa
Sequence
MHRYRSHHCAALRKCDVGTKVRLSGWVHRVRDHGGILFVDLRDHFGITQIVADPASPAFKVIEKVRSEWVIRVDGEVCARSDEVINATLPTGEIEIFVQEVEILSKSEELPLPVFGEPDYPEDIRLKYRFLDLRRETMHKNIMRRTEIIAAMRRAMQNNGFTEFSTPLLTASSPEGARDFLVPSRVHQGKFYALPQAPQQYKQLLMMSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDVEMSFVEQEDVLATMEPIMRSIFEEFANGKTVTQNFPRISYDEAIQKYGSDKPDLRNPIIMEDVSQHFYNSGFKVFAQILADDENAQVWAIPAKTGGSRAFCDRMNVWAQGEGQPGLGYIFWRKEEEKFEGAGPIAKNIGEQRTEALRIQLGLENGDACFFVAGDPKKFASFAGAARTRVGEELDLVDRECFSLAWIVDFPFFEWNEDEKKIDFAHNPFSMPQGGENALECQDPLTLKAFQYDLVCNGYEIASGGIRNHLPEMMLKVFELVGLSKKVVKDRFGALYRAFHYGAPPHGGMAAGIDRIIMLLQGVKNLREVALFPMNQQALDLLMNAPSDVSSTQLRDLGIRMAPTQKNSS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Beijerinckia indica subsp. indica (strain ATCC 9039 / DSM 1715 / NCIB 8712)
Length
597 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.892 kDa
Sequence
MHRYRTHTCGDLREAQADETTRLSGWCHRIRDHGGVLFIDLRDHYGITQCVVDPDSKAFPLAEKLRSEWVVRIDGLVRKRPSGTENPEMPTGFIEIYVTEIEVLGAAAELPMPVFGDIDYPEDIRLKYRFLDLRREKLHKNIMLRGQVIDSLRRRMKEQGFFEFQTPILTASSPEGARDFLVPSRIHAGKFYALPQAPQQYKQLLMMAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDVEMSFITQEDVFAAMEPVIRGAFEEFGNGQPVTQTFPRIPYAEAMLKYGSDKPDLRNPLVIADVTDLFARDDVSFNAFKNVIKKGGVVRAIPATGAASQPRSFFDKLNDWAKSEGAAGLGYVIFEGSDEAPVGKGPIAKFLPAEVQAAIVTRADLKAGDAVFFACDIEEKAAKLAGAARLRIGHELGLSKTGVFELCWIVDFPMYEWNEDDKTVDFSHNPFSMPQGGLEALQTQDPLTIKAFQYDIACNGYEIASGGIRNHRPEAMVKAFEIAGYGEETVVERFGGMYRAFQYGAPPHGGMAAGVDRIIMLLAGVQNLREISLFPMNQKAEDLLMGAPSEATTKQLRELHIRLNLPEPK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Mycobacterium abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC 1543)
Length
597 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.82 kDa
Sequence
MLRTHDAGSLRESNAGQRVTLAGWVARRRDHGGVIFIDLRDASGVAQVVFREDAVLEQAHRLRAEFCVEVSGVVEVRPEGNANDEIATGQIEVNAAELKVLNESAPLPFQLDETAGEEARLRYRYLDLRREGPGNAIRLRSKANAAARSVLSGHEFVEVETPTLTRSTPEGARDFLVPARLQPGSFYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDIEMSFVDQDDVIALAEEILVALWDLVGYRVPTPIDRITYAEAMRRYGSDKPDLRFGLELVECTDYFSETSFRVFQAPYVGAVVMPGGADQPRRTLDGWQEFAKQRGHKGLAYVLVGEDGTLGGPVAKNLSDAERDGLAAHVGANPGDCIFFSAGAAKSSRALLGSVRGEVAQRLGLIDPDAWAFTWVVDAPLFEPADDATAAGDVAVGSGAWTAVHHAFTSPKPESENTFDTDPGSALAYAYDIVCNGHEIGGGSIRIHRRDIQERVFQVMGISNEDAQEKFGFLLDAFAFGAPPHGGIAFGWDRVTALLAGTSSIREVIAFPKSGGGVDPLTDAPAPITAAQRKESGIDAKPEKAEKAGKPADA

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shewanella pealeana (strain ATCC 700345 / ANG-SQ1)
Length
597 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.352 kDa
Sequence
MRSHYCGDVNKSHVGQEVTLVGWVNRSRDLGGVVFLDLRDREGIVQVVYDPDLPEVFDVASTLRSEFCVQIKGLVRARPDSQINADMRTGEVEILGLELTILNSSAPLPINMDKNQHNTEEQRLKYRYLDLRRPEMADRIVFRSKVTSAVRRFLDGNGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTSAQVMDKTEEMVRGLFKELLNVDLGEFPKMTFEEAMRRFGSDKPDLRNPLELIDVADIVKEVEFAVFNGPANDPEGRVAVLSIPGGAKLSRKQLDEYAKYVTIYGAKGLAWMKVNDLAQGMEGIQSPVLKFLSEDVVNALLERTGAQTGDLILFGADKANIVAEAMGALRLKAGEDFDLLQGEWKPLWVVDFPMFERTSDGGLHAMHHPFTAPSNMTPEELEANPIGAISDAYDMVLNGCELGGGSVRIHDSKMQSAVFRILGINDEEASEKFGFLLEALRYGTPPHAGLAFGLDRIIMLMTGASSIRDVMAFPKTTTAACPLTNAPGFANPVQLAELGVSVVEAEPKADAKDTE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / Type A)
Length
597 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.026 kDa
Sequence
MGEALNGLKRNIMCGDARESHIGQKVTVMGWVQRNRNLGGLQFIDLRDREGILQVVFNDDLGEEILEKAKSIRPEYCIAVTGEIVKRESVNPNMPTGMVELKAEELKILSESDTPPIYIKEDLDAAESIRLKYRYLDLRRPDMQNIFKIRHKTTKAIRDYLDQNGFLEMETPILTKSTPEGARDYLVPSRNYPGMFYALPQSPQLFKQLLMVSGFDRYFQIVKCFRDEDLRANRQPEFTQVDLEMSFVEQDDVMALNEGLIKHVFKEVLGVDVKTPIKRMTFKDAMEKYGSDKPDLRFGMEITNLSDVVKECGFKVFTDAVANGGSVRGLCLEGGASMGRKDIDRLGEFVKTFKAKGLAWIQLKEEGVKSPIAKFFSEEELNKIIETMGAKTGDLILIVADKNSVVLKALGELRLELSRKFDLVKDKSEFNFTWITEFDLLEYDEEEGRYFAAHHPFTMPMDEDIKYLDTDPGRVRAKAYDLVLNGEELGGGSIRIHDTKLQEKMFEVLGFTQESAWERFGFLLEAFKFGPPPHGGLAFGLDRMIMFLAGTENIKDVITFPKNQNAFCYLTEAPNIVDEEQLKELGIETIKKEDTAE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Clostridium perfringens (strain 13 / Type A)
Length
597 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.026 kDa
Sequence
MGEALNGLKRNIMCGDARESHIGQKVTVMGWVQRNRNLGGLQFIDLRDREGILQVVFNDDLGEEILEKAKSIRPEYCIAVTGEIVKRESVNPNMPTGMVELKAEELKILSESDTPPIYIKEDLDAAESIRLKYRYLDLRRPDMQNIFKIRHKTTKAIRDYLDQNGFLEMETPILTKSTPEGARDYLVPSRNYPGMFYALPQSPQLFKQLLMVSGFDRYFQIVKCFRDEDLRANRQPEFTQVDLEMSFVEQDDVMALNEGLIKHVFKEVLGVDVKTPIKRMTFKDAMEKYGSDKPDLRFGMEITNLSDVVKECGFKVFTDAVANGGSVRGLCLEGGASMGRKDIDRLGEFVKTFKAKGLAWIQLKEEGVKSPIAKFFSEEELNKIIETMGAKTGDLILIVADKNSVVLKALGELRLELSRKFDLVKDKSEFNFTWITEFDLLEYDEEEGRYFAAHHPFTMPMDEDIKYLDTDPGRVRAKAYDLVLNGEELGGGSIRIHDTKLQEKMFEVLGFTQESAWERFGFLLEAFKFGPPPHGGLAFGLDRMIMFLAGTENIKDVITFPKNQNAFCYLTEAPNIVDEEQLKELGIETIKKEDTAE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Clostridium perfringens (strain SM101 / Type A)
Length
597 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.072 kDa
Sequence
MGEALNGLKRNIMCGDARESHIGQKVTVMGWVQRNRNLGGLQFIDLRDREGILQVVFNDDLGEEILEKAKSIRPEYCIAVTGEIVKRESVNPNMPTGMVELKAEELKILSESDTPPIYIKEDLDAAESIRLKYRYLDLRRPDMQNIFKIRHKTTKAIRDYLDQNGFLEMETPILTKSTPEGARDYLVPSRNYPGMFYALPQSPQLFKQLLMVSGFDRYFQIVKCFRDEDLRANRQPEFTQVDLEMSFVEQDDVMALNECLIKHVFKEVLGVDVKTPIKRMTFKDAMEKYGSDKPDLRFGMEITNLSDVVKECGFKVFTDAVANGGSVRGLCLEGGASMGRKDIDRLGEFVKTFKAKGLAWIQLKEEGVKSPIAKFFSEEELNKIIETMGAKTGDLILIVADKNSVVLKALGELRLELSRKFDLVKDKSEFNFTWITEFDLLEYDEEEGRYFAAHHPFTMPMDEDIKYLDTDPGRVRAKAYDLVLNGEELGGGSIRIHDTKLQEKMFEVLGFTQESAWERFGFLLEAFKFGPPPHGGLAFGLDRMIMFLAGTENIKDVITFPKNQNAFCYLTEAPNIVDEEQLKELGIETIKKEDTAE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Corynebacterium kroppenstedtii (strain DSM 44385 / JCM 11950 / CIP 105744 / CCUG 35717)
Length
597 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.981 kDa
Sequence
MHRTHLAGELRSHHVGQTVTLSGWVARRRDHGGVIFIDLRDRSGLAQVVFRDSDVAAQAHHLRSEYCIRVTGVVDARPEGSENPNLDSGAIELNVNELTILNSSEALPFQIDDQSSSGEVGEETRLKYRYLDLRRKTQHDALVLRSNVNQAARSVLLKHDFHEIETPTLTRSTPEGARDFLVPARLRPGSFYALPQSPQLFKQLLMVGGMERYFQIARCYRDEDFRADRQPEFTQLDVEMSFVDQDDVISVAEEILTAIWKEIGYDIPTPIPRMTYADAMKYYGSDKPDLRFDIKIVECTEFFANTTFRVFQNPYVGAIVMEDGASQPRRQLDAWQDWAKQRGAKGLAYILVGDDGQLSGPVAKNITDAEREGIADHVGAKPGDCIFFAAGDAKSSRALLGAARGEVARKLGLIKEGDWAFTWVVDAPLFEPAADATAEGDVALGHSAWTAVHHAFTSPKPECMDSFDKDPGSALSYAYDIVCNGNEIGGGSIRIHRSDVQQRVFNVMGISDEEAQEKFGFLLEAMKFGAPPHGGIAFGWDRIVSLLGGFESIRDVIAFPKSGGGVDPLTDAPAPITPEQRKESGIDAKPKKKETKN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Cyanothece sp. (strain PCC 7425 / ATCC 29141)
Length
597 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.345 kDa
Sequence
MRTHYCGDVRSHDVGTTVTLFGWVDRRRDHGGVIFLDLRDRSGVVQIVSDPERTPNSYAKAEQLRNEYVVKVTGRVSARPEESLNPRLPTGEVEIYADQIELLNAVRKQLPFQVSTTESESVREDLRLKYRYLDLRRETMAANLQLRHQVVKAMRRYLEDEQNFVEIETPVLTRSTPEGARDYLVPSRVNPGEWFALPQSPQLFKQLLMVAGYDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFMSQEEILELNEALVCHIFKQVKGIELPRPFPRLTYAEAMDRYGSDKPDTRFGLELVNVSDLMKDSGFKVFSGAVASGGLVKVLPIPNGNDLISNVRIKPGGDLFKEATDAGAKGLAYIRVREGGEIDTIGAIKDNLTEAQKAELLQRTGAKPGHLLLFGAGTAAIVNKTLDRLRQVLGRELNLIDPAKINLLWIVEFPMFEWNADEKRLEALHHPFTAPYPEDVQDLKTAQAQAYDLVYNGFEVGGGSLRIYQTELQKQVFETIGLSPEEAQNKFGFLLEAFEYGTPPHGGIAYGLDRLVMLLAGEESIRDVIAFPKTQQARCLLTSAPAEVDLRQLKELHVASTSQPKVNG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Length
597 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.298 kDa
Sequence
MRTDYCGLIDKKYLGQTVTVKGWAHRRRDHGGVIFIDLRDREGLVQVVIDPDTPEAFKLADSSRGEYVLSITGIVRERPAGTANSKMISGEIEILAKEIEILNAAATPPFQIDDENLSENVRLTNRVIDLRRPAMQKNLRLRYKVAMGVRNHLDKQGFIDIETPMLTRSTPEGARDYLVPSRVHPGEFFALPQSPQLFKQLLMVAGFDRYYQITKCFRDEDLRADRQPEFTQIDIETSFLNEDEIMDITEGMTKEIFQDVLGVTLPTFPRMTYGDAMFYYGSDKPDMRVALKFTELTDVMKSEEFKVFRGAADMANGRVVALRVPNGASFSRKEIDDYTQFVAIYGAKGLAYIKVNDVTKLNEEGLQSPIVKFLSANGLKEIIARTGAQNGDIIFFGADKAKVVNEAIGALRIKIGHEHGLENGYFVKEWRPLWVVDFPMFEHDEEEDRWTACHHPFTSPKPGHEDLMATDPGKCLARAYDMVLNGWEIGGGSIRIHRADIQEKVFGALKISPEEQQNKFGFLLDNLKFGAPPHGGLAFGLDRLVTLMCGAESIRDVIAFPKTQRAQCLLTNAPNAVDDKQLRELNLRLRQKAEPSA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Nocardia farcinica (strain IFM 10152)
Length
597 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.559 kDa
Sequence
MLRTHLAGSLRSEHAGQTVTLTGWVARRRDHGGVIFIDLRDASGVSQAVFREGEAAEQAHRLRAEYCVRVTGVVEQRPDGNENPELPTGQIEVNVRELEVLNESAPLPFQLDEQPGEEARLKHRYLDLRREGPAHAIRLRSKVNAAAREVLARHEFVEVETPTLTKSTPEGARDFLVPARLQPGNFYALPQSPQLFKQLLMVGGIERYFQIARCYRDEDFRADRQPEFTQLDIEMSFVEQADVILLAEEILVALWKLIGYEIPTPIPHMTYAEAMRRFGSDKPDLRFGVEITECTEYFKNTPFRVFQAPYVGAVVMPGGASQPRRQLDAWQEWAKQRGAKGLAYVLVNEDGSLGGPVAKNLSDAEREGLAKHVGAEPGDCVFFAAGPAKAQRALLGAARGEIARKVGLIDENAWSFVWIVDAPLFEPADDATASGDVALGHSAWTAVHHAFTSPKPESLDTFDTDPGSALAYAYDIVCNGNEIGGGSIRIHRRDVQERVFKVMGIGEQEAQEKFGFLLDAFAYGAPPHGGIAFGWDRIVALLAGLDSIREVIAFPKTGGGVDPLTDAPAPITAQQRKEAGLDAKPEQAEVKKAEQAG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Orientia tsutsugamushi (strain Boryong)
Length
597 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.432 kDa
Sequence
MHKYRTHTCGELSLAHVGLQVKLSGWLYRRRDHGGLLFIDLRDHYGIIQLVFNDDCSAVQAEISKIKFETVITVEGAVVARSNETINKNISTGDVEVVVSSYVVESFAEELPLQINGEYEAPEETRLKYRFLDLRGARLHQNIVLRSKVIQELRNQMLSNGFIEFQTPILTASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLIMMSGFDKYFQIAPCFRDEDARADRSPGEFYQLDIEMAFVTQEDVFGLVEPVLYNTFKKFSNYSITNIPFPRITYDESMLRYGSDKPDLRNPIQISDVTDIFQCSEFTTLKDSINCGAVVRAIPAPMSANKPRSFFDKMIEYAKHLGASGLAYIQFTNDGVKGSIAKFFDEALLARIKKLVKCQDGDAIFFICDKENDATKVAAKIRAKVGEELNIIKTDCYKFCWVIDFPFYQLDSEINKITFSHNPFSMPQGGIEAFNKAKTVEDLLSIKAFQYDIVCNGVELSSGAIRNHKPDLMYKAFAIVGYSKDEVDKQFGAMIRAFCYGAPPHGGIAPGIDRILMLLTNSVNIREVIAFPMNQQAEDLLMGCPAAVTDKQLHELQLKLISKERIK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Orientia tsutsugamushi (strain Ikeda)
Length
597 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.52 kDa
Sequence
MHKYRTHTCGELNLAHVGLQVKLSGWLYRRRDHGGLLFIDLRDHYGIIQLVFNDDCSIIQAEISKIKFETVITVEGTVIARSNETINKNISTGDVEVVVSSYVVESFAEELPLQINGEYEAPEETRLKYRFLDLRGARLHQNIVLRSKVIQELRNQMLSNGFIEFQTPILTASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLIMMSGFDKYFQIAPCFRDEDARADRSPGEFYQLDIEMAFVTQEDVFGLVEPVLYNTFKKFSNYSITDIPFPRITYDESMLRYGSDKPDLRNPIQISDVTDIFQCSEFTTLKDSINCGAVVRAIPAPMSANRPRSFFDKMIEYAKHLGASGLAYIQFTNDGVKGSIAKFFDEALLARIKKLVKCQDGDAIFFICDKEDDATKVAAKIRAKVGEELNIIKTDCYKFCWVIDFPFYQLDSEVNKITFSHNPFSMPQGGIEAFNKAKTVEDLLSIKAFQYDIVCNGVELSSGAIRNHKPDLMYKAFAIAGYSKDEVDKQFGAMIRAFSYGAPPHGGIAPGIDRILMLLTNSVNIREVIAFPMNQQAEDLLMGAPSAVTEKQLQELQLKLISKERIK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Photobacterium profundum (strain SS9)
Length
597 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.926 kDa
Sequence
MRTQYCGHLNKSLEGQTVELCGWVNRRRDLGGLIFIDMRDREGIVQVVVDPDMKDVFELANQLRNEFCIRLIGEVRVRPESQVNKKMATGEVEILATGLEIINRSDVLPLDFNQNNSEEQRLKFRYLDLRRPEMSDRIKLRAKASSFVRRFLDENAFLDIETPVLTKATPEGARDYLVPSRVHKGSFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMSAEQVREITEKMITEMWKELLNVDLGTFPIMQFEEALRRFGSDKPDLRNPLELVDVADILKDVDFKVFSGPANDEKGRVAVIRVPGGASLSRKQIDEYTKFVGIYGAKGLAWMKVNDREAGFAGVQSPVAKFLNEDVVANLLDRTQAETGDIILFGADSKRVVTEALGALRLKLGEDLELTDKSIWKPLWVIDFPMFEEDGEGNLHAMHHPFTSPLGITAEELAVNPAAANSNAYDMVINGYEVGGGSVRIHNADMQSAVFNILGIEEGEQQSKFGFLLEALKYGTPPHAGLAFGLDRLVMLLCGTDNIRDVIAFPKTTAASCLLTNAPSLANPDSLKELSIAVAIAKKETAKEESAE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Desulfobacterium autotrophicum (strain ATCC 43914 / DSM 3382 / HRM2)
Length
596 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.02 kDa
Sequence
MTDLLGDMRRTHTCGELRVTDVDTEVTLMGWVQRRRDHGGVIFIDFRDKEGITQIVFNPEVNPEVHAKAQTIRSEYVLGVKGRVVNRPDDMVNPKMVTGGIEILVDELKILSRAETPAFQIEDRIEASETVRLKYRHLDLRRPKLQQNIIARHTASRAVRDYLNDLGFLDIETPFLTRSTPEGARDYLVPSRVNHGQFYALPQSPQLFKQMLMISGFDRYYQIVRCFRDEDLRADRQPEFTQIDMEMSFVGEDEIMEITEGLIKTVFKRVRDIDLELPFQRITYAESIDRFGIDRPDMRFGLELNDLSDLVENTGFKVFASVVKKGGLVKAINAKGCANFTRKQIDELTDFAAIYKAKGLAWVKVKADGTWQSPIAKFFTDDEKKAIEVRLDMEKDDIVFFVADNPKITNEALGQLRNELARRLELIDNNTYRFVWVTHFPLVEYDEGEKRYQAIHHPFTAPLEEDLEKLDTDPLNVRSRAYDMVLNGIEIGGGSIRIHSTELQEKVLNTLGIGKEEANDKFGFLLNALGSGTPPHGGLAFGFDRLVMLLCQEESIRDVIAFPKTQRATCLLTEAPSKAAPAQLQELSIRVVNIEE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455)
Length
596 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.372 kDa
Sequence
MRTHYCNGIHEGLIGQTVTLCGWAQRRRDHGGVIFIDLRDREGLVQIVADPDQVDAFAAANECRSEFVLQVEGVLRARPAGTENPHMPSGKVELAAARIRILNRSEPVPFPLDEEDIAENLRLKYRYLDLRRPEMLHRLRLRHQVTRFVRGYLDNAGFIDVETPVLTRSTPEGARDYLVPSRTQPGHFFALPQSPQLFKQLLMVAGLDRYYQITKCFRDEDLRADRQPEFTQIDIEASFVDEEAVMGTAEPMIRGLFAEVLGVQLPDPFPRMTYRDAMHRFGVDRPDLRNPLELTELTDLMRAVDFKVFREAAERPHGRVACLRVPGGAQLSRAQIDAYTQFTAIYGARGLAWIKVNALDQGNEGLQSPIVKFLPEMVLSEILRRSGAAAGDILFFGADTAKIVNEALGNLRNRVAADLGLLEGEWCPVWITDFPMFDYDDKEDRWTSTHHPFTAPQTEHLETLGQDPGNALARAYDLVLNGNEIGGGSIRIHQEAVQEKVFAALGIGAEEARDKFGFLLDALHYGAPPHGGLAFGLDRLVMLLCGAETIRDVIAFPKTQKAGCLLTEAPGTVADKQLQELGIRLRPGVGGGVPNP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Acidithiobacillus ferrooxidans (strain ATCC 53993)
Length
596 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.372 kDa
Sequence
MRTHYCNGIHEGLIGQTVTLCGWAQRRRDHGGVIFIDLRDREGLVQIVADPDQVDAFAAANECRSEFVLQVEGVLRARPAGTENPHMPSGKVELAAARIRILNRSEPVPFPLDEEDIAENLRLKYRYLDLRRPEMLHRLRLRHQVTRFVRGYLDNAGFIDVETPVLTRSTPEGARDYLVPSRTQPGHFFALPQSPQLFKQLLMVAGLDRYYQITKCFRDEDLRADRQPEFTQIDIEASFVDEEAVMGTAEPMIRGLFAEVLGVQLPDPFPRMTYRDAMHRFGVDRPDLRNPLELTELTDLMRAVDFKVFREAAERPHGRVACLRVPGGAQLSRAQIDAYTQFTAIYGARGLAWIKVNALDQGNEGLQSPIVKFLPEMVLSEILRRSGAAAGDILFFGADTAKIVNEALGNLRNRVAADLGLLEGEWCPVWITDFPMFDYDDKEDRWTSTHHPFTAPQTEHLETLGQDPGNALARAYDLVLNGNEIGGGSIRIHQEAVQEKVFAALGIGAEEARDKFGFLLDALHYGAPPHGGLAFGLDRLVMLLCGAETIRDVIAFPKTQKAGCLLTEAPGTVADKQLQELGIRLRPGVGGGVPNP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Agrobacterium radiobacter (strain K84 / ATCC BAA-868)
Length
596 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.037 kDa
Sequence
MHRYRSHTCAALRKSDVGSTVRISGWVHRVRDHGGVLFIDLRDHYGITQVVADPDSPAFKLAETVRGEWVIRIDGLVKARTEDTVNKTMPTGEIELYAQEIEVLSAAKELPLPIFGEPDYPEDVRLKYRFLDLRRDTLHKNIVKRTQVISSMRRHMGEVGFTEYTTPILTASSPEGARDFLVPSRIHPGTFYALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVTQEDVWNTMAPLMTSIFEEFAEGKPVTKEWPRIPYDVAIRKYGSDKPDLRNPIVMEAVTEHFAGSGFKVFANMIASNPKVEVWAIPAKTGGSRAFCDRMNAWAQSQGQPGLGYIFWRKEGEKLEGAGPLAKNIGEERTDAIRTQLGLDDGDACFFVAGDPAKFYKFAGEARTRAGDELNLIDRDRFELCWIVDFPFFEWSEEEKKVDFAHNPFSMPQGGLEALQNQDPLTIKAYQYDAVCNGFEIASGSIRNQSPETMVAAFEKVGLSQADVEERFGGLYRAFQYGAPPHGGAAFGIDRIVMLLVGAKNLREISLFPMNQQAQDLLMGAPSVATPTQLRELAIRPVPPVKKD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Hydrogenovibrio crunogenus (strain XCL-2)
Length
596 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.745 kDa
Sequence
MMRTHYCGQVTEILENQQVTVSGWVHRRRDHGGVIFIDLRDREGLVQVVVNPDNAEMFAIAERVRSEYVLKVEGKVCARTPETINPKMNTGKIEIVAESLEVLSSAEPIPFQLDDKHISEEVRLTYRYLDLRREEMQSTMRTRYRVTRSMRRYLDDNGFMDMETPILTKSTPEGARDYLVPSRTHPNKFFALPQSPQLFKQLLMMSGFDRYYQITRCFRDEDLRADRQPEFTQLDIETSFMTEEEVMNMMEGLTKTIFREGVDVNFEDDFPRMTYAEAIEKYGIDRPDLRIPLQLVDVADLLQDIDFKVFAGPAKDPMGRVAALRVPQGGKLSRKEIDDYTKYVGIYGAKGLAYIKVNDLSAGLDGLQSPIVKFFPDQAMEIMQRVGAEDGDIVFFGADNAKIVNEALGALRCKIGEDLDMIEKEWAPVWVVDFPMFEMDEKTAKMTAIHHPFTQPKATTEEILNHDEPHQMLSRAYDLVINGIEVGGGSVRIHDTHMQAAVLKMLGISDEDAQEKFGFLLNALKYGCPPHAGMAFGLDRLVMLMAKRDSIRDVIAFPKTQSAACMLTDAPGNVDNTQLADLELRFRKSLVAKDAS

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Sodalis glossinidius (strain morsitans)
Length
596 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.488 kDa
Sequence
MRTVYCGQLNLSHVGQEVMLCGWVNRRRDLGGLIFIDMRDREGLVQVFFDPDRQDAFARAAELRNEFCLQLTGIVRARPDSQVNSEMATGAVEVLATELSIINCSEPLPLDSNQNNTEEQRLKFRYLDLRRPVMAQRLKTRARISSFVRRFMDAEGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTATQVREVMERLIRDLWREITGVDLGIFPQMTYADAMRRFGSDKPDLRNPMELVDVADLVKDVQFKVFSIPANDSQGRVAALRVPGGAQLSRKQIDEYGKYSEIYGAKGLAWMKVNQRAAGVEGVQSPVAKFLGPQVIEQILVRTGAADSDIIFFSADRKNVVTDALGALRLKLGLDLQLTVTDRWAPLWVVDFPMFEEDGEGGLAAMHHPFTAPKDVDAQMLAASPTSAVANAYDMVINGYEVGGGSVRIHRGDMQQTVFGILAINEQEQQEKFGFLLDALKYGTPPHAGLAFGLDRLVMLLTGTDNIRDVIAFPKTTAAADLMTEAPSFGNADALADLSIAVVGKGREAMENGRS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bartonella bacilliformis (strain ATCC 35685 / NCTC 12138 / KC583)
Length
596 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.562 kDa
Sequence
MHRYRSHNCAALRKCDVGTQVRLSGWVHRVRDHGGILFVDLRDHFGITQIVVNPDSSAFQIMEKVRSEWVICVDGKVCARSDEVINTTLPTGEIEIFADEIEILSKSDELPLPVFGEPDYPEDIRLKYRFLDLRRVTMHKNIMRRTEIISSIRRHMQDSGFTEFTTPLLTASSPEGARDFLVPSRIHQGKFYALPQAPQQYKQLLMMSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDIEMSFVEQEDVLATMEPIIRSVFEEFSDGKLVTQSFPRISYDEAMRKYGSDKPDLRNPIIIEDVSQHFYDSDFKVFAQILANNENAQVWAIPAKTGGNRAFCDRMNGWAQGEGQPGLGYIFWRKEGENFEGAGPIAKNIGEQRTEAIRTQLGLKEGDACFFVAGDPKKFASFAGASRTRIGEELDLIDSKCFSFAWIVDFPFFEWNEDEKKIDFAHNPFSMPQGGMNAVDSQDPLTIKAFQYDLVCNGYEIASGGIRNHSPEMMLKVFNLAGLSREIVEERFGGLYRAFHYGAPPHGGMAAGVDRIVMLLQGVKNLREISLFPMNQQALDLLMSAPSDVSATQLNDLGIRIFPKVNNA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bartonella henselae (strain ATCC 49882 / DSM 28221 / Houston 1)
Length
596 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.626 kDa
Sequence
MHRYRSHHCAALRKCDVGIKARLSGWVHRVRDHGGILFVDLRDHFGITQIVADPASPAFKIIEKVRSEWVIRVDGEVRARSDEVINTSLPTGEIEIFAKEVEILSKSDELPLPVFGEPDYPEDIRLKYRFLDLRRETMHRNIMRRTEIIAAIRRSMQENGFTEFTTPLLTASSPEGARDFLVPSRIHQGKFYALPQAPQQYKQLLMMSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDVEMSFVEQEDVLVTMEPIMRSLFEEFADGKPVTQSFPRLSYEEAMRKYGSDKPDLRNPIIMEDVSQHFYDSGFKVFAQILANDENARVWAIPAKTGGSRAFCDRMNGWAQSEGQPGLGYIFWREEQGKFEGAGPIAKNIGEQRTEALRMQLGLENGDACFFVAGDPKKFLPFAGAARTRVGEELDLVDRDCFSLAWIVDFPFFEWNEEEKKLDFAHNPFSMPQGGKDALECQDPLTLKAFQYDLVCNGYEIASGGIRNHSPEMMLKVFNLAGLSKEVVEDRFGGLYRAFHYGAPPHGGMAAGVDRIIMLLQGVKNLREVALFPMNQQALDLLMSAPSDVSPVQLRDLGIRIAPAAKND

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bordetella avium (strain 197N)
Length
596 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.155 kDa
Sequence
MRTCYTGQVCRDHLGQTVTLYGWVNRRRDHGGVIFIDLRDRTGLAQIVFDPDNAGAFGTAERLRNEFCVRVTGLVRERPQGTTNAELASGEVEVLCRDVEILNPSVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQRNLMLRYRVSIEVRKFLDQLGFIDIETPMLTKSTPEGARDYLVPSRVNAGHFFALPQSPQLFKQMLMVSGFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLTETEIRAVFESMIRHVFKVVQNVDLPDPFPIMTWTEAMARFGSDKPDMRVNLEFTDVADIMRDVDFKVFASAATTQGSRVVALRVPGGGELSRSEIDAYTQFVGIYGAKGLAYIKVNDVAKGREGLQSPIVKNLHDAALAELVKRTGAQDGDIIFFGADRAKVVNDALGALRVKIGHSEFGKKTGLFSGGWRPLWVVDFPMFEYDEEEGRYTAAHHPFTSPKDGHEDFLETDPSQAFAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGPDEAREKFGFLLDALQYGAPPHGGIAFGLDRIVTMMTGADSIRDVIAFPKTQRAQDLLTQAPSSVDDKQLRELHIRLRNTEVK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rhizobium leguminosarum bv. viciae (strain 3841)
Length
596 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.918 kDa
Sequence
MHRYRSHTCAALRKSDVGSTVRISGWVHRVRDHGGVLFIDLRDHYGITQVVADPDSPAFQMAETVRGEWVIRIDGLVKARTEDTVNKTMATGEIELYAQEIEVLSAAKELPLPVFGEPDYPEDVRLKYRFLDLRRETLHRNIVKRTQVISAMRREMGNVGFTEYTTPILTASSPEGARDFLVPSRIHPGTFYALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVTQEDVWNTMGPLMTSIFEEFAEGKPVTKEWPRIPYDEAIRKYGSDKPDLRNPIVMQAVTEHFAGSGFKVFAGMIASNPKVEIWAIPAKTGGSRAFCDRMNAWAQSTGQPGLGYIFWRKEGDKLEGAGPLAKNIGEERTDAIRTQLGLDDGDACFFVAGDPAKFYKFAGEARTKAGEELNLVDRDRFELCWIVDFPFFEWSEEDKKVDFAHNPFSMPQGGLDALQNQDPLTIKAFQYDAVCNGFEIASGSIRNQSPETMVAAFEKVGLSQQDVEDRFGGLYRAFQYGAPPHGGAAFGIDRIVMLLVGAKNLREISLFPMNQQAQDLLMGAPSPAAPTQLRELSIRPIPPVKKD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
Length
596 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.001 kDa
Sequence
MHRYRSHTCAQLRKSDVGSSVRLSGWVHRVRDHGGLLFIDLRDHYGLTQIVADPDSPAFKVAETVRGEWVIRVDGEVKARLSETVNANLPTGEIEIFAREIEVLSAAKELPLPVFGEPDYPEDIRLKYRFLDLRRDTLHKNIVARTKIIAEMRKRMGDVGFTEFSTPILTASSPEGARDFLVPSRIHPGTFYALPQAPQQYKQLIMVSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVEQDDVLNTMEPVLRGVFETFANGKPVTQKFQRIPYDVAMRKYGSDKPDLRNPIEMQAVSDHFRDSGFKVFANILANDPKAEVWGIPAKTGGSRAFCDRMNSWAQGEGQPGLGYIFWRKEGDKLEGAGPLAKNIGEERTEAIRQQLGLADGDAAFFVAGDPKKFVSFAGAARTRAGEELNLVDRERFELCWIVDFPFFEWNEEEKKIDFAHNPFSMPQGGIDALNGEDLLGIKAFQYDMVCNGFEIASGGIRNHLPETMVKAFETVGLDRATVEERFGGLYRAFQYGAPPHGGMAAGIDRVVMLLVGAKNLREVTMFPMNQQAYDLLMNAPSEASPQQLRELALRVAPTKKDA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rhizobium leguminosarum bv. trifolii (strain WSM2304)
Length
596 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.934 kDa
Sequence
MHRYRSHTCAALRKTDVGSTVRISGWVHRVRDHGGVLFIDLRDHYGITQVVADPDSPAFKMAETVRGEWVIRIDGLVKARTEDTVNKAMATGEIELYAQEIEVLSAAKELPLPVFGEPDYPEDVRLKYRFLDLRRETLHKNIVKRTQVISAMRREMGNVGFTEYTTPILTASSPEGARDFLVPSRIHPGTFYALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVTQEDVWDTMGPLMTSVFEEFAEGKPVTKEWPRIPYDEAIRKYGSDKPDLRNPIVMEAVTEHFAGSGFKVFAGMIASNPKVQIWAIPAKTGGSRAFCDRMNAWAQSQGQPGLGYIFWRSENDKLEGAGPLAKNIGEERTDAIRTQLGLGDGDACFFVAGEPEKFYKFAGEARTKAGEELNLVDRDRFELCWIVDFPFFEWSEEDKKVDFAHNPFSMPQGGLDALQNQDPLTIKAFQYDAVCNGFEIASGSIRNQSPETMVAAFEKVGLSQQDVEDRFGGLYRAFQYGAPPHGGAAFGIDRIVMLLVGAKNLREISVFPMNQQAQDLLMGAPSPATPTQLRELSIRPIPPVKKD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Arthrobacter sp. (strain FB24)
Length
596 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.331 kDa
Sequence
MLRTHDLGSLRSEHIGQTVTLAGWVGRRRDHGGVAFVDLRDASGVSQVVVREEEVFHGLRNEYVLQVIGTVSQRPEGNENPALATGQIEVIAEKVTILNTSDPLPFQIDEHVEVGEEARLKHRYLDLRRPGPARNMRLRSEANRVARELLHRDGYVEIETPTLTRSTPEGARDFVVPARLAPGSWYALPQSPQLFKQLLQVGGFEKYYQIARCYRDEDFRADRQPEFTQLDIEASFVEQDDIISLGESIVKALWQLIDVEIPTPIQRITYADAMARYGSDKPDLRFGLELTELTEFFKDTNFGVFKAPYVGAVVMPGGASQARRALDAWQEWAKQRGAKGLAYVLFKEDGELAGPVAKNLTDTERAGLADAVGAKPGDCIFFAAGEKTPSRALLGAARVEIGHRTGLINPADWAFCWVVDAPMFEPAAAAVASGDVAVGAGQWTAVHHAFTSPKPEFMDSFDKDPESALSYAYDIVCNGNEIGGGSIRIHERDVQERVFELMGLDKADAETKFGFLLEGFKFGAPPHGGIAFGWDRVVALLAGVESIRDVIAFPKSGGGYDPLTQAPAPITAQQRKEAGVDFKPEAKKADPGATKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pelobacter carbinolicus (strain DSM 2380 / NBRC 103641 / GraBd1)
Length
596 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.661 kDa
Sequence
MIDILGDWKRSHFCGSITAADTGKEVCLMGWVQRRRDHGGLIFIDLRDRQGIAQLALDPDRDPEAHAKAERVRNEYVVAVRGIVSARPEGTVNPKMATGEVEVEVKELRMLNGAETPPFLIEDNVDVAENIRLKHRYLDLRRPALQSNLVLRHKVAQIVRNYLNDTGFIEVETPVLTKSTPEGARDYLVPSRVNPGMFYALPQSPQLFKQLLMVSGFDRYYQIVKCFRDEDLRADRQPEFTQIDCELSFVDRQDIMDIMEAMIATVFQQILGIELSLPMPRITYTESMARFGVDNPDMRFDLELVEISNIAKDCGFKVFADAVKKGGIVKLLNAKQCASFSRKEIDDLTDFVKIYGAKGLAYVKIQEDGSWQSPIAKFFTEKEIALIDEAAGSEPGDLLLFAADTFKVANESLGRLRGHLGQKLGLARKDDFRFAWVTDFPLLEWDGEARRHVAVHHPFTAPLDEDIALLDGDPGSARAKAYDLVLNGSEIGGGSIRIHNREIQNKMFSLMGITAEEAEEKFGFLLGALSYGAPPHGGIAFGLDRLMMILTGSDSIRDVIAFPKTQKATCLLSEAPGAVDDKQLRELSIRRAVRNN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
Length
596 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.165 kDa
Sequence
MRTCYTGQVCRDHLGQTVTLYGWVNRRRDHGGVIFIDLRDRTGLAQIVFDPDNAEAFGTAERLRNEFCISITGLVRLRPEGTANAELASGEVEVLCQQVEILNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLMLRYRVSIEVRKYLDQLGFIDIETPMLTKSTPEGARDYLVPSRVNAGYFFALPQSPQLFKQMLMVSGFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLNEVEIREIFEGMIRHVFKVVQDVDLPTPFPIMSWTEAMQRYGSDKPDLRVNLEFTDMTDVMRDVDFKVFASAATTAGSRVVALRVQGGGEMSRSEIDAYTQFVGIYGAKGLAYIKVNDVAKGREGLQSPIVKNLHDAALAELVKRTGAQNGDIIFFGADRAKVVNDAIGALRVKIGHSEFGKKAGLFSGGWKPLWVVDFPMFEYDEEENRYTAAHHPFTSPKDGHEDFLESDPGKAVAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIDAEEAREKFGFLLDALQYGAPPHGGIAFGLDRIITMMAGAESIRDVIAFPKTQRAQCLLTGAPSEVDEKQLRELHIRLRNVEVK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253)
Length
596 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.165 kDa
Sequence
MRTCYTGQVCRDHLGQTVTLYGWVNRRRDHGGVIFIDLRDRTGLAQIVFDPDNAEAFGTAERLRNEFCISITGLVRLRPEGTANAELASGEVEVLCQQVEILNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLMLRYRVSIEVRKYLDQLGFIDIETPMLTKSTPEGARDYLVPSRVNAGYFFALPQSPQLFKQMLMVSGFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLNEVEIREIFEGMIRHVFKVVQDVDLPTPFPIMSWTEAMQRYGSDKPDLRVNLEFTDMTDVMRDVDFKVFASAATTAGSRVVALRVQGGGEMSRSEIDAYTQFVGIYGAKGLAYIKVNDVAKGREGLQSPIVKNLHDAALAELVKRTGAQNGDIIFFGADRAKVVNDAIGALRVKIGHSEFGKKAGLFSGGWKPLWVVDFPMFEYDEEENRYTAAHHPFTSPKDGHEDFLESDPGKAVAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIDAEEAREKFGFLLDALQYGAPPHGGIAFGLDRIITMMAGAESIRDVIAFPKTQRAQCLLTGAPSEVDEKQLRELHIRLRNVEVK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
Length
596 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.165 kDa
Sequence
MRTCYTGQVCRDHLGQTVTLYGWVNRRRDHGGVIFIDLRDRTGLAQIVFDPDNAEAFGTAERLRNEFCISITGLVRLRPEGTANAELASGEVEVLCQQVEILNASVTPPFQLDDDNLSETTRLTHRVLDLRRPQMQHNLMLRYRVSIEVRKYLDQLGFIDIETPMLTKSTPEGARDYLVPSRVNAGYFFALPQSPQLFKQMLMVSGFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLNEVEIREIFEGMIRHVFKVVQDVDLPTPFPIMSWTEAMQRYGSDKPDLRVNLEFTDMTDVMRDVDFKVFASAATTAGSRVVALRVQGGGEMSRSEIDAYTQFVGIYGAKGLAYIKVNDVAKGREGLQSPIVKNLHDAALAELVKRTGAQNGDIIFFGADRAKVVNDAIGALRVKIGHSEFGKKAGLFSGGWKPLWVVDFPMFEYDEEENRYTAAHHPFTSPKDGHEDFLESDPGKAVAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIDAEEAREKFGFLLDALQYGAPPHGGIAFGLDRIITMMAGAESIRDVIAFPKTQRAQCLLTGAPSEVDEKQLRELHIRLRNVEVK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Length
596 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.458 kDa
Sequence
MHAYRTHNCSALRRANVGEKVRLSGWVHRKRDHGGLLFVDLRDHYGLTQIVADSDSAVFEKLDQLRLESVITVTGEVVERAPEVVNPNLATGEIEIRASEVDVQSFAQELPLPVAGEADYPEDIRLRYRYLDLRRDRLHRNIVLRSNVIASLRRRMIEQGFNEYQTPILTASSPEGARDYLVPSRVHPGKFYALPQAPQMFKQLMMVAGFDRYFQIAPCFRDEDARADRSPGEFYQLDFEMSFVTQEDVFATIEPVLAGVFEEFGGGKTVTPAPFPRIAYRDAMLYYGSDKPDLRNPLKISDVTEHFRDSGFGLFAGMVAKGGVVRAIPAPEAGKNSRKFFDDMNNWAREEGFAGLGYINIKNGEAGGPIARNLGEDATQKLLADLGLGENDGVFFAAGKEGEAARLAGLARNRVGELLDLIEKDSFRFCWVVDFPMFEYDEEAKQVIFSHNPFSMPQGGMEALETKDPLDILAYQYDIVCNGIELSSGAIRNHRPEIMYKAFEIAGYDQAMVDENFAGMINAFKYGAPPHGGAAPGVDRMVMLLAGEPNIREVVLFPMNQKAEDLMMGAPAAVSERQLKELSLRIAVKPTQKSAS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6)
Length
596 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.911 kDa
Sequence
MRTHYCGDLRSEHIDQTVTLYGWVDRRRDHGGVIFIDLRDRTGIVQIVSDPQRTPDSYNDADASRSEYVVKIVGKVSARQEGAKNPKLPTGEVEIYADTIEILNGVHKQLPILVSSSADGDQVKEDLRLKYRYLDLRRETMAKNLQLRHTVVKSMRRFLEDDENFMEVETPILTRSTPEGARDYLVPSRVNPGDWYALPQSPQLFKQLLMVAGCDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFMSFDEIIDLNERLICRIFQDAQGIELERPFPRITYAESMEKYGCDRPDTRFGLELVNVSDIVADMGFKVFSGAVKSGGQVKVLPIPNGNDAISNVRIKPGGDLFNAAVEMGAKGLAFIRVREDGAIDTIGAIKDNLSDAQKQELLSRTGAEAGTLLLFGAGATDIVNKSLDRVRQLVGAEMGLINENQLNFVWVTDFPMFEYNSDEKRLEALHHPFTAPNPEDLEDLATARALAYDIVLNGIEIGGGSLRIYQREVQEKVFQTIGLSETEAQEKFGFLLEAFEYGTPPHGGIAYGLDRLVMLMAQEDSIRDVIAFPKTQQASCLLTDAPAGVDQKQLKELFVASTAPEKD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Acaryochloris marina (strain MBIC 11017)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.537 kDa
Sequence
MRTHYCSELRNDHVGERVTLCGWVDRRRDHGGVIFLDVRDRTGLIQIVSDPERTPEAYPQADALRNEYVVRIHGEVSRRPDDSLNPRLPTGEVEIYADQIELLNAVHQQLPFQVSTADVESVKEELRLKYRYLDLRRDRMHQNIMMRHRLIQSIRRYLEDQQNFVDIETPVLTRSTPEGARDYLVPSRANPGEWFALPQSPQIFKQLLMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFMSQEEIIQLNEDLMRHVFKTLKDIDLPKTFPQMTYAEAMERFGTDRPDTRFDLELVNVSDLLEDSGFKVFSGAIKKGGQVKVLPIPDGNAKISNVRIKPGGDLFSEASAGGAKGLAYIRVKDDGAIDTIGAIKDNLSPEQTAELLERTGAKPGHLLLFGAGPTEIVNASLSRLRLALGAEMKLIDPDQIDLLWITEFPMFEWNADEKRLEALHHPFTAPYPEDEADLKTARAQAYDLVYNGLEIGGGSLRIYQADLQRRVFDAIGLSEEEAQDKFGFLLNAFNFGAPPHGGIAYGIDRLAMLLSGEESIRDTIAFPKTQQARCLLTQAPSSVDQKQLKELQIKSTAEPKN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Acidiphilium cryptum (strain JF-5)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.858 kDa
Sequence
MHEYRTHDCGALRAADAGITARLSGWVNVKRDHGGLLFIDLRDHYGITQCVFPAGSPVFAAAEALRAESVITVTGRVVKRDADTVNPRLPTGEIELVAETVEVQSTADVLPIQVAGEAQFPEELRLRYRFLDLRREKLHRNIMLRANVIAWLRREMTARGFTEFTTPILTASSPEGARDFLVPSRVHPGQFYALPQAPQQFKQLLMVAGFDRYFQIAPCFRDEASRADRAPGEFYQLDFEMSFVTQEDVFATIEPVLGGLFREFGGGRGVTQWPFPRIAYDEALLKYGSDKPDLRNPLLITDVTEAFRDSGFGLFAKIVAGGGVVRAIPAPGTGGNPRSFFDKLNDWARSEGAGGLGYIIFAPDGAKGPIAKNLEPARAEAIREATGASVGDAVFFAAGKPLEAAKFAGTVRTKLGTDLGLIDGAKFEFCWIVDFPMYERDEETGQIVFSHNPFSMPQGGLEALNGQDPLTIKAFQYDIVCNGVELSSGAIRNHRPDIMLRAFEIAGYGAEEVEARFGGMLNAFRYGAPPHGGSAPGVDRMVMLLADEPNLREVIAFPLNQQGQDLLMGAPAPVPAARLKELSLAIALPPAPKKG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Agrobacterium fabrum (strain C58 / ATCC 33970)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.035 kDa
Sequence
MHRYRSHTCAALRKSDVGETVRLSGWVHRVRDHGGVLFIDLRDHYGITQVVADPDSPAFKVAETVRGEWVIRIDGLVKARSEDTINKGMATGEIELYAQEIEVLGVAKELPLPVFGEPEYPEDVRLKYRFLDLRRETLHRNIVKRTQIISSMRKGMGDLGFAEYTTPILTASSPEGARDFLVPSRIHEGQFFALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDVEMSFVTQEDVWTTMEPMMTAVFEQFAEGKPVTKQWPRIPYDESIRKYGSDKPDLRNPIVMEAVTEHFDGSGFKVFANMIASNPKVQVWAIPAKTGGSRAFCDRMNAWAQSQGQPGLGYIFWKEEEGKVAGSGPLAKNIGEERTEALRQQLGLEAGDACFFVAGDPAKFYKFAGEARTRAADELNLIDRDRFEMCWIVDFPFFEYNEEEKKIDFAHNPFSMPQGGMEALEGQDPLSIKAFQYDAVCNGFEIASGSIRNQSPELMVKAFEKVGLSQSDVEERFGGLYRAFQYGAPPHGGCAFGIDRVVMLLVGAKNLREITLFPMNQQAQDLLMNAPSPATPTQLRELALRVVPSKKD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Trichodesmium erythraeum (strain IMS101)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.499 kDa
Sequence
MRTHYCGQVNSNNIEETVNLCGWVDRRRDHGGVIFLDLRDRSGLIQIVSDPERTPDSYQIAGDIRNEYVVQITGRVSRRPEESLNPKLPTGEIEIYADDIQLLNGLGKQLPFQVSTAETEAVREELRLKYRYLDLRRERMTRNLLLRHEVIKAIRRFLEDEQNFVEIETPILTRSTPEGARDYLVPSRVHPGEWFALPQSPQLFKQILMVSGFDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFMSQEEILQLNEKLVAYIFQKVKGIDLPLPFPRLTYTEAMERYGSDKPDVRFGLELVDVSDLMKDSGFKVFSGAIAKGGIVKVLPIPGGNDAISNVRIKPGGDLFKEASEVGAKGLAYVRVKEGGKIDTIGAIKDNLTDEQKQELLKRTNAQPGHLLLFAADDANTVNKTLDRLRLVIGEQLGLIDQDKISLLWVTDFPMFEWNEDEQRLEALHHPFTAPHPDDINDLKTARAQAYDLVFNGYEVGGGSLRIYQRDVQEKVFEAIGLSAQEADNKFGFLLEAFEYGTPPHGGIAYGLDRLVMLLAVEESIRDVIAFPKTQQAKCLLANAPSEVDKKQLKELHVSSISKAKS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rhizobium meliloti (strain 1021)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.189 kDa
Sequence
MHRYRSHTCAALRKSDVGSTVRLSGWVHRVRDHGGVLFIDLRDHYGMTQVVADPDSPAFKTAETVRGEWVIRVDGAVKARTDDTVNKNMPTGEVELYAREIEVLSAAKELPLPVFGEPDYPEDVRLKYRFLDLRRETLHKNIVRRTEIIAAMRRRMGDIGFTEYTTPILTASSPEGARDFLVPSRIHPGNFYALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVEQEDVWDAMEPMIRAIFSDFAGGKPVTDKFPRIPYDTAIRKYGSDKPDLRNPIEMQEVTEHFAGSGFKVFANMIASNPKVEIWAIPAKTGGSRAFCDRMNAWAQSQGQPGLGYIFWRKEGEKLEGAGPLAKNIGEERTDAIRTQLGLEDGDACFFVAGEPAKFYKFAGEARTRAGEELNLVDRDRYELCWIVDFPFYEWNEEEKRVDFAHNPFSMPQGGLTALSSDDLLSIKAFQYDMVCNGFEIASGSIRNQSPELMVKAFENVGLSQADVEERFGGLYRAFQYGAPPHGGMAFGIDRIVMLLVGAKNLREISLFPMNQQAQDLLMGAPSQATPAQLRELSIRPIPQKKD

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shewanella sediminis (strain HAW-EB3)
Length
595 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.287 kDa
Sequence
MRSQYCGDVNKSHVGQEVTLVGWVNRSRDLGGVVFLDLRDREGIVQVVYDPDLPEVFDVASTLRSEFCVQVTGLVRARPDSQVNKDMRTGEIEILGKGLTILNSAAPLPINMDKNQHNTEEQRLKYRYLDLRRPEMADRIVFRSKVTSAVRRFLDDSGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMSSAEVMAKTEEMTRGLFKDLLNVDLGEFPKMTFAEAMRRFGSDKPDLRNPLELIDVADILKDVEFKVFQEPANDPAGRVAVLCIPGGAKLSRKQLDEYAKYATIYGAKGLAWMKVNDLDKGLEGIQSPVLKFLNEDVVNGLLERTNAKTGDLILFGADKANIVAEAMGALRLKAGEDFDLLNGEWKPLWVVDFPMFEPTSDGGLHAMHHPFTAPMGITPEQLEADPTAAISDAYDMVLNGCELGGGSVRIHNSEMQSAVFRILGIEEEEANEKFGFLLEALRYGTPPHAGLAFGLDRIVMLMTGATSIRDVMAFPKTTTAACPLTNAPGFANPAQLVELGVNVIESEDNKEEQE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shewanella woodyi (strain ATCC 51908 / MS32)
Length
595 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.187 kDa
Sequence
MRSQYCGDVNKSHVGQEVTLVGWVNRSRDLGGVVFLDLRDREGIVQVVYDPDLPEVFDVASTLRSEFCVQVTGLVRARPDSQVNQDMRTGGIEILGKGLTILNSSAPLPINMDKNQHNTEEQRLKYRYLDLRRPEMADRIVFRSKVTSAVRRFLDDSGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMSSEQVMAKTEEMVRGLFNDLLNVDLGEFPKMTFAEAMRRFGSDKPDLRNPLELIDIADIVKEVEFAVFNGPANDPEGRVAVLSIPGGAKLSRKQLDEYAKYVTIYGAKGLAWMKVNDLDQGMEGIQSPVLKFLSEDVVKALLDRTGAQTGDLILFGADKANIVAEAMGALRLKAGEDFDLLQGEWKPLWVVDFPMFERTSDGGLHAMHHPFTAPTGISPEQLEADPTAAISDAYDMVLNGCELGGGSVRIHNSEMQSAVFRILGIEEEEANEKFGFLLEALRYGTPPHAGLAFGLDRIIMLMTGASSIRDVMAFPKTTTAACPLTNAPGFANPAQLIELGIEVIENQESKEEQA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Cyanothece sp. (strain PCC 7424)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.695 kDa
Sequence
MRTHYCGDLRASDIDKTVTLFGWVDRYRDHGGVIFADLRDRTGRVQIVSDPQRTPESYQAAANLRNEYVIKVEGRVSKRPKESLNPKIPTGEVEIYADSIEILNGVNKQLPFVISSEDAELVREEVRLKYRYLDLRRDRMRKNLQLRHQVVQAMRRYLEDQQNFMEVETPILTRSTPEGARDYLVPSRTNPGKWYALPQSPQLFKQLLMVSGVDRYYQIARCFRDEDNRADRQPEFTQLDMEMSFMSFDEILDLNEGLIAHVFKTVKNIDIPRPFPRLTYAEAMEKYGIDRPDTRFGLELVDVSEIVKDSGFKVFSGAVKSGGIVKVLPIPEATNIISNVQIKPGGELFKEATEAGAKGIAYIRIKDNNELDTIAAIKDNLTDEQKQELIEKTGAKPGHLLLFGAGDTDTVNKSLARLRLVVGEKLGLIDEDKINLLWVTDFPMFEWNAEEKRLEALHHPFTAPKPEDINDLPHARALAYDMIFNGIELGGGSLRIYQRDIQEKVFSTIGLSMEEAYNKFGFLLEAFEYGTPPHGGIAYGLDRFVMLLAKEESIRDVIAFPKTQQASCLLTEAPSTVEPKQLKELHIASTFKPKS

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Erwinia tasmaniensis (strain DSM 17950 / CIP 109463 / Et1/99)
Length
595 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.66 kDa
Sequence
MRTEYCGQINLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRQEAFTLASELRNEFCIQIVGTVRARDEKNKNGDMATGEIEIFATELTIINRSEPLPLDSNHINSEEARLKYRYLDLRRPDMANRLKTRAKITSFVRRFMDDQGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMERLVRELWQDVKSVDLGAFPSMTFAEAMRRYGSDKPDLRNPMELVDVADLLKNVEFKVFSGPANDVKGRVAALRVPGGAALSRKQIDDYAKFIETYGAKGLAYIKVNERAKGIEGITSPVAKFLNAEIVESILQRTAAADGDLIFFGADSAKVVADALGALRLKLGRDLNITNGSVWAPLWVLDFPMFEDDGEDGLTAMHHPFTAPKEMSPEQLKNAPETAIANAYDMVINGYEVGGGSVRIHNGQMQQTVFGILGITEQEQREKFGFLLDALKFGTPPHAGLAFGLDRLVMLLTGTDNIRDVIAFPKTTAAACLMTEAPNFANPASLTELGIEVVKKAKDRPSEND

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.058 kDa
Sequence
MRTCYTGEVCRDHLGQTVTLYGWVNRRRDHGGVIFIDLRDRAGLAQIVFDPDNAAFATAERLRNEFCIRVTGLVRPRPEGTANPELASGEVEVLCKEVEILNASITPPFQLDDDNLSETTRLTHRVLDLRRPQMQRNLMLRYRVSIEVRKFLDQLGFIDIETPMLTKSTPEGARDYLVPSRVNAGHFFALPQSPQLFKQMLMVSGFDRYYQITKCFRDEDLRADRQPEFTQIDCETSFLNEVEIRQIFEDMIRHVFKTVQNVELPAPFPQMTWTEAMQRYGSDKPDLRVSLEFTDVTDVMRDVDFKVFAAAATAPGSRVVALRVPGGAELSRSEIDAYTQFVGIYGAKGLAYIKVNDASKGREGLQSPIVKNLHDAALAELLKRSGAQSGDIIFFGADRAKIVNDAIGALRVKIGHSEFGKKAGLASSDWKPLWVVDFPMFEYDEEDGRYTAAHHPFTSPKDGHEDFLESDPSKAFAKAYDMVLNGWEIGGGSVRIHREEVQSKVFRALKIGAEEAREKFGFLLDALQYGAPPHGGIAFGLDRIVTMMTGAESIRDVIAFPKTQRAQCLLTQAPSEVDEKQLRELHIRLRNVEVK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Brucella abortus (strain S19)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.255 kDa
Sequence
MHRYRSHTCAALRKTDVGSNVRLSGWVHRVRDHGGILFIDLRDHYGITQIVADPDSPAFKVAETVRGEWVIRVDGEVKARADDAVNTNLPTGEVEIFATEIEVLSPAKELPLPVFGEPDYPEDIRLKYRFLDLRRETLHKNIMSRTKIIAAMRRRMTEIGFNEFSTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVTQEEVWETMEPVMRGIFEEFAEGKPVTKVFRRIAYDDAIRTYGSDKPDLRNPIEMQAVTDHFAGSGFKVFANMIANDAKVEVWAIPAKTGGSRAFCDRMNSWAQSEGQPGLGYIFWRKEGDKLEGAGPIAKNIGEERTEAIRKQMGLEDGDACFFVAGLPSKFYKFAGDARTRAGEELNLVDRDRFELAWIIDFPFYEWDEDNKKIDFAHNPFSLPQGGMDALENMDPLEIKAYQYDLVCNGFEIASGSIRNQLPEVMVKAFEKVGLSQQDVEERFGGLYRAFQYGAPPHGGMAAGIDRVIMLLVGAKNLREISLFPMNQQALDLLMGAPSEVSPAQLRDLHVRLAPVQKS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Brucella abortus (strain 2308)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.255 kDa
Sequence
MHRYRSHTCAALRKTDVGSNVRLSGWVHRVRDHGGILFIDLRDHYGITQIVADPDSPAFKVAETVRGEWVIRVDGEVKARADDAVNTNLPTGEVEIFATEIEVLSPAKELPLPVFGEPDYPEDIRLKYRFLDLRRETLHKNIMSRTKIIAAMRRRMTEIGFNEFSTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVTQEEVWETMEPVMRGIFEEFAEGKPVTKVFRRIAYDDAIRTYGSDKPDLRNPIEMQAVTDHFAGSGFKVFANMIANDAKVEVWAIPAKTGGSRAFCDRMNSWAQSEGQPGLGYIFWRKEGDKLEGAGPIAKNIGEERTEAIRKQMGLEDGDACFFVAGLPSKFYKFAGDARTRAGEELNLVDRDRFELAWIIDFPFYEWDEDNKKIDFAHNPFSLPQGGMDALENMDPLEIKAYQYDLVCNGFEIASGSIRNQLPEVMVKAFEKVGLSQQDVEERFGGLYRAFQYGAPPHGGMAAGIDRVIMLLVGAKNLREISLFPMNQQALDLLMGAPSEVSPAQLRDLHVRLAPVQKS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Brucella abortus biovar 1 (strain 9-941)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.255 kDa
Sequence
MHRYRSHTCAALRKTDVGSNVRLSGWVHRVRDHGGILFIDLRDHYGITQIVADPDSPAFKVAETVRGEWVIRVDGEVKARADDAVNTNLPTGEVEIFATEIEVLSPAKELPLPVFGEPDYPEDIRLKYRFLDLRRETLHKNIMSRTKIIAAMRRRMTEIGFNEFSTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVTQEEVWETMEPVMRGIFEEFAEGKPVTKVFRRIAYDDAIRTYGSDKPDLRNPIEMQAVTDHFAGSGFKVFANMIANDAKVEVWAIPAKTGGSRAFCDRMNSWAQSEGQPGLGYIFWRKEGDKLEGAGPIAKNIGEERTEAIRKQMGLEDGDACFFVAGLPSKFYKFAGDARTRAGEELNLVDRDRFELAWIIDFPFYEWDEDNKKIDFAHNPFSLPQGGMDALENMDPLEIKAYQYDLVCNGFEIASGSIRNQLPEVMVKAFEKVGLSQQDVEERFGGLYRAFQYGAPPHGGMAAGIDRVIMLLVGAKNLREISLFPMNQQALDLLMGAPSEVSPAQLRDLHVRLAPVQKS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Brucella canis (strain ATCC 23365 / NCTC 10854)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.273 kDa
Sequence
MHRYRSHTCAALRKTDVGSNVRLSGWVHRVRDHGGILFIDLRDHYGITQIVADPDSPAFKVAETVRGEWVIRVDGEVKARADDAVNTNLPTGEVEIFATEIEVLSPAKELPLPVFGEPDYPEDIRLKYRFLDLRRETLHKNIMSRTKIIAAMRRRMTEIGFNEFSTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVTQEEVWETMEPVMRGIFEEFAEGKPVTKVFRRIAYDDAIRTYGSDKPDLRNPIEMQAVTDHFAGSGFKVFANMIANDAKVEVWAIPAKTGGSRAFCDRMNSWAQSEGQPGLGYIFWRKEGDKLEGAGPIAKNIGEERTEAIRKQMGLEDGDACFFVAGLPSKFYKFAGDARTRAGEELNLVDRDRFELAWIIDFPFYEWDEDNKKIDFAHNPFSMPQGGMDALENMDPLEIKAYQYDLVCNGFEIASGSIRNQLPEVMVKAFEKVGLSQQDVEERFGGLYRAFQYGAPPHGGMAAGIDRVIMLLVGAKNLREISLFPMNQQALDLLMGAPSEVSPAQLRDLHVRLAPVQKS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Microcystis aeruginosa (strain NIES-843)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.811 kDa
Sequence
MRTHYCGDLSAIEIEKSVTLFGWVDRRRDHGGVIFIDLRDRSGIVQIVSDPQRTPASYPIAETVRNEYVLKVTGTVSQRPTESLNPRIATGEIEIYATSIEILNGVTKQLPFVVSSSESESVREDVRLRYRYLDLRRERMSQNLQLRHQVVKEMRRFLEDEQHFIEVETPILTRSTPEGARDYLVPSRVNPGQWYALPQSPQLFKQLLMVSGMDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFLSLPEILALNEALIAHIFKKVKNIDISLPLPRLTYAEAMDRYGIDRPDTRFGLELVNVAEIFADSGFKVFSGAIASGGTVKVLPIPNGNEAISNVRIKPGGDLFKEATDAGAKGIAYIRVREDYDFDTIGAIKDNLTEAQKQALIEKTGAKPGHLLLFGAGDTDTVNKSLSRLRLVLGEQLGLIDPEKINLLWVTDFPMFEYNAEEKRLEALHHPFTAPNPEDLEDLAQARALAYDMIFNGIEIGGGSLRIYQREVQEKVFATIGLSPEEAYNKFGFLLEAFEYGTPPHGGIAYGLDRLVMLLAGEESIRDVIAFPKTQQASCLLTSAPSTVAAKQLKELSVASTYKPPS

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Klebsiella pneumoniae (strain 342)
Length
595 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.418 kDa
Sequence
MRTEYCGQLRQSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRAREEKNINADMATGAIEVLASDLTIINRSESLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKIRAKITSFVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREIMEAMVRQLWLEIKGVDLGDFPIMTFAEAERRYGSDKPDLRNPIELVDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKLIDEYGNFVKIYGAKGLAYIKVTERAKGMDGINSPVAKFLTAEIVEAILERTGAQDGDMIFFGADNKKVVADALGALRLKLGKDLSLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTADELKAAPEEAVANAYDMVINGYEVGGGSVRIHRGDMQQTVFGILGINEHEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPAALGELGIQVVEKEAKASLENK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578)
Length
595 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.415 kDa
Sequence
MRTEYCGQLRQSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRAREEKNINADMATGAIEVLASDLTIINRSESLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSFVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREIMEAMVRQLWLEVKGVDLGEFPIMTFAEAERRYGSDKPDLRNPMELVDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKLIDEYGNFVKIYGAKGLAYIKVTERAKGMDGINSPVAKFLTAEIVEAILDRTGAQDGDMIFFGADNKKVVADALGALRLKLGKDLSLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTADELKAAPEEAVANAYDMVINGYEVGGGSVRIHRGEMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPAALGELGIQVVEKEAKASLENK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Nitrosococcus oceani (strain ATCC 19707 / BCRC 17464 / NCIMB 11848 / C-107)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.281 kDa
Sequence
MRSHYCGELSEAHLDQSVTLCGWVNRRRDHGGVIFIDLRDREGLIQLVFDPEYSPESFRHAEQIRSEYVLQVKGRVQHRPEGTENPDLKTGQVEVLGQELILLNASETPPFPVDEKLEVGEDIRLRYRYIDLRRPESLQRLRFRSAIIRQLRKFLDERGFLDIDTPILTQSTPEGARDFLVPSRTHPGQFFALPQSPQLFKQLLMVAGVDRYYQVVRCFRDEDLRADRQPEFTQLDIEASFLHEETLMALMEEMFKELFATVLEVPLHTPFVRMPYAEALACFGLDKPDLRIPLRLVEVGDLMKTVDFKVFAQPAQDRDGRVAALRLPGGGKLSRKEIEEYTQFVAIYGAKGLAYIKVVERSRGREGLQSPILKFLPDEVIGAMLERTEAENGDIVFFGADKASIVNESLGALRVKLGHDHGLVEHGWSPLWVIDFPMFEWDEDDHRWHALHHPFTSPKEEDLSLLEQNPGACRSRAYDLVLNGTEVGGGSIRISQSQVQSQVFRLLGIGDEEAQDKFGFLLDALKYGCPPHGGIAFGLDRLVMLMTGSASIREVIPFPKTQTAACPLTGAPGQVAEAQLRELGIGVRRLASDKV

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Nostoc punctiforme (strain ATCC 29133 / PCC 73102)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.664 kDa
Sequence
MRTHYCGELRKEHIGETVTFYGWVDRRRDHGGVVFLDLRDRSGIVQIVSDPQRTPDSYEQANALRNEYVVEITGRVTQRPEESLNTRIPTGEVEIYADKIKLLNAVGKQLPFQVSVADTETVREDLRLKYRYLDLRRERMAQNLQLRHQIVKAMRRYLEDLEGFIEVETPILTRSTPEGARDYVLPSRVNPGEWYALPQSPQLFKQLLMVSGLDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFMSQEEIIELNESLVCHIFKTVKGIELQRPFLRLTYAEGMERYGSDKPDTRYGLELVDVSDIVKDSGFKVFRDTVTNGGIVKILPIPNGNDVISNVRIKPGGDLFKEASEAGAKGLAYIRVRDDGEIDTIGAIKDNLSEEQKQEILRRTGAKAGHLLLFGAGEAATVNKTLDRLRQAIAREFNLIDPDKINLLWITDFPMFEWNADEKRLEALHHPFTAPHPDDLSDLKTARAQAYDLVLNGVEVGGGSLRIYQREIQQQVFEAIGLSPEEAQSKFGFLLEAFEYGTPPHGGIAYGLDRLVMLLAGEESIRDVIAFPKTQQARCLLTDAPSSVDAKQLKELHVASTYKPKS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.905 kDa
Sequence
MRTHYCGELRQKDIGETVTLYGWVDRRRDHGGVIFLDLRDRSGIVQVVSDPQRTPDSYELANSLRNEYVVEITGRVTQRPEESLNTRIPTGEVEIYADKIELLNGVRKQLPFQVSTADTETVREDLRLKYRYLDLRRDRMARNIQLRHQVVKAMRRYLEDVEGFIEVETPILTRSTPEGARDYVLPSRVNPGEWFALPQSPQLFKQILMVSGLDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFMSEEEIIELNEKLVSYIFKTVKGVELPLPFPRLTYAEAMERYGCDKPDTRYDLQLVNVSDVMKDSGFKVFRDAVANGGIVKILPIPNGNEQISNVRIKPGGDLFREASEAGAKGLAYIRVREDGEIDTIGAIKDNLSEEQKQEILQRTGAKPGHLLLFGAGDAVTVNKTLDRLRQAIAKEFGLIDPDKINLLWVVDFPMFEWNADEKRLEALHHPFTAPHPDDLHDLKTARAQAYDLVFNGFEVGGGSRRIYQREVQEQVFETIGLSPEEAQNKFGFLLEAFEYGTPPHGGIAYGLDRLVMLFAGEESIRDVIAFPKTQQARCLLTDAPSGVDVKQLKELHVASTYKPKS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Ochrobactrum anthropi (strain ATCC 49188 / DSM 6882 / JCM 21032 / NBRC 15819 / NCTC 12168)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.242 kDa
Sequence
MHRYRSHTCAALRKTDVGSNVRLSGWVHRVRDHGGILFIDLRDHYGITQIVADPDSPAFKVAETVRGEWVIRVDGEVKARAGDAVNTNLPTGEVEIFATEIEVLAAAKELPLPVFGEPDYPEDIRLKYRFLDLRRETLHKNIMSRTKIIAAMRRRMTEIGFNEFTTPILTASSPEGARDFLVPSRIHEGKFYALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVTQEEVWETMEPVMRGIFEEFAEGKPVTQQFRRIAYDDAIRTYGSDKPDLRNPIEMQAVTEHFAGSGFKVFANMIANDPKVEVWAIPAKTGGSRAFCDRMNSWAQSEGQPGLGYIFWRKEGDKLEGAGPIAKNIGEERTEAIRTQMGLEDGDACFFVAGLPSKFYKFAGDARTRAGEELNLVDRDRFELAWIIDFPFYEWDEDNKKLDFAHNPFSMPQGGMDALENQDPLAIKAYQYDLVCNGFEIASGSIRNQLPDVMVKAFEKVGLSQQDVEERFGGLYRAFQYGAPPHGGMAAGIDRVIMLLVGAKNLREISLFPMNQQALDLLMNAPSDVSPAQLRDLHIRLAPVQKS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Opitutus terrae (strain DSM 11246 / JCM 15787 / PB90-1)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.028 kDa
Sequence
MHRTHHCAQLTTSQLGATVSLLGWVDTIRDQGGIIFVDLRDRKGITQIQLEPHENAKLAEQVKQLKPESVIGITGKVVRRPAGTENPALPTGEVEVVASSLEIHNISDTPPFPLDDAGGDKVNEDLRLTYRYLDLRRPKMRKNLQVRHRAAKSIRDYFDAQEFIEVETPALFKSTPEGAREYLVPSRIHPGQFYALSQSPQQFKQILMVAGVEKYFQIARCFRDEDLRADRQMEFTQVDVEASFVTREDIYALFEGMLKKVWKDVLDVDIPTPFPRMAFHDAMNRYGVDKPDVRFALELADFSELFKNSAFKVFQSTVAGGGVVKALNAKGLADLTQGELKSMEDTAKSLGAKGLAFIKVEGGEWKSPIVKFFTEPEKAELTKRLNIEEGDIIFFAAAPWEKACAILGRLRLESAAFLQKRGKLTIRHDDWQFLWVIDFPLMTYDEAENRYVATHHPFTAPVPDDTQYLDSDPKKVRGQHYDVVLNGMELGGGSIRIHQPVLQKKVFEDVLKIPQDVVESRFGYMLKAFTYGAPPHGGIAFGLDRMVALLCGTTSIRDVIAFPKTQKGQDLMAQSPTPVTPRQLKDLHIQTVMPE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Length
595 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.222 kDa
Sequence
MIGRTHHCGQLSEEQVNERVQLKGWVQRRRDLGQVIFVDLRDRSGVVQLVFNSDISQEALETAEKVRNEYVLDVEGVVLKRDPSTVNDKIATGTIEVHVERLTILNKAKSLPFQIEANTDASEDIRLKYRYLDLRRPDMQETMKLRHQTTKLIRDFLDGQEFFEIETPMLTKSTPEGARDYLVPSRVHHGEFYALPQSPQIFKQLLMVSGFERYYQIVRCFRDEDLRADRQPEFTQIDIETSFMDKEDLLTMTENMMAKIMKEVKGLDVALPFPRMTYDDAMNRYGSDKPDTRFEMELIELSDIVKDSDFKVFSSAIKSGGIVKGLNLKGGAGSLSRKEIDGLAEFVKPYGAKGLAWLKVEEGELKGPIAKFFAGETGAELQQAMGAEDGDLLFFAADKKEVVFDSLGALRLKLGKDFNLIDESKFNFLWVVDFPLVEYDEEAKRFVALHHPFTSPKQEDLTKLETDPASVRADAYDLVLNGYELGGGSQRIYQRPVQEKMFAALGFTEEAAQKEFGFLLEAFEYGTPPHGGIALGLDRLVMLLAGRLNLRDTIAFPKTASASCLLTEAPGEVSLEQLLDLNLSIIGHKPDKVNV

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787)
Length
595 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.243 kDa
Sequence
MGESLNGLKRTIMCGEIRENHIGNRVVVMGWVQRKRNLGGLVFVDLRDREGILQVVFGEEINKDAFMKADLVKSEYCISVSGTLVKRESPNPNMPTGMVELKGEEIKILSESETPPIYIKENLDAAENIRLRYRYLDLRRPDMQKIFKIRHKTTKIIRDFMDEENFLEMETPILTKSTPEGARDYLVPSRNYNGKFYALPQSPQLFKQLLMVSGYDKYFQIAKCFRDEDLRANRQPEFTQVDMEMSFVEEDDVIELNERLIQKVFKEMAGVEVKLPIERMTWKTAMEKYGSDKPDLRFGMEINDISEAVSTSDFKVFKSAIEEGGSVRAIKAPNSADMPRKKIDKLGEFVKTYKAKGLAWIALKEDGIKSPIAKFLKEEELKAIIDKVQGKTGDLILIVADKNSVVFQSLGALRLEIAKELEILKDNKEFRFVWITEFPLLSYNEEEERFQAEHHPFTMPMDEDIEYLESDPGRVRAKAYDIVLNGEELGGGSVRIHDTALQERMFKVLGFTKESAWERFSFLLEAFKFGPPPHAGLAYGLDRLIMFLAGTENIKDVIAFPKNQNAFCPLTEAPNVVDENQIEELGIKVESKEEE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Brucella melitensis biotype 2 (strain ATCC 23457)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.273 kDa
Sequence
MHRYRSHTCAALRKTDVGSNVRLSGWVHRVRDHGGILFIDLRDHYGITQIVADPDSPAFKVAETVRGEWVIRVDGEVKARADDAVNTNLPTGEVEIFATEIEVLSPAKELPLPVFGEPDYPEDIRLKYRFLDLRRETLHKNIMSRTKIIAAMRRRMTEIGFNEFSTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVTQEEVWETMEPVMRGIFEEFAEGKPVTKVFRRIAYDDAIRTYGSDKPDLRNPIEMQAVTDHFAGSGFKVFANMIANDAKVEVWAIPAKTGGSRAFCDRMNSWAQSEGQPGLGYIFWRKEGDKLEGAGPIAKNIGEERTEAIRKQMGLEDGDACFFVAGLPSKFYKFAGDARTRAGEELNLVDRDRFELAWIIDFPFYEWDEDNKKIDFAHNPFSMPQGGMDALENMDPLEIKAYQYDLVCNGFEIASGSIRNQLPEVMVKAFEKVGLSQQDVEERFGGLYRAFQYGAPPHGGMAAGIDRVIMLLVGAKNLREISLFPMNQQALDLLMGAPSEVSPAQLRDLHVRLAPVQKS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.273 kDa
Sequence
MHRYRSHTCAALRKTDVGSNVRLSGWVHRVRDHGGILFIDLRDHYGITQIVADPDSPAFKVAETVRGEWVIRVDGEVKARADDAVNTNLPTGEVEIFATEIEVLSPAKELPLPVFGEPDYPEDIRLKYRFLDLRRETLHKNIMSRTKIIAAMRRRMTEIGFNEFSTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVTQEEVWETMEPVMRGIFEEFAEGKPVTKVFRRIAYDDAIRTYGSDKPDLRNPIEMQAVTDHFAGSGFKVFANMIANDAKVEVWAIPAKTGGSRAFCDRMNSWAQSEGQPGLGYIFWRKEGDKLEGAGPIAKNIGEERTEAIRKQMGLEDGDACFFVAGLPSKFYKFAGDARTRAGEELNLVDRDRFELAWIIDFPFYEWDEDNKKIDFAHNPFSMPQGGMDALENMDPLEIKAYQYDLVCNGFEIASGSIRNQLPEVMVKAFEKVGLSQQDVEERFGGLYRAFQYGAPPHGGMAAGIDRVIMLLVGAKNLREISLFPMNQQALDLLMGAPSEVSPAQLRDLHVRLAPVQKS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.273 kDa
Sequence
MHRYRSHTCAALRKTDVGSNVRLSGWVHRVRDHGGILFIDLRDHYGITQIVADPDSPAFKVAETVRGEWVIRVDGEVKARADDAVNTNLPTGEVEIFATEIEVLSPAKELPLPVFGEPDYPEDIRLKYRFLDLRRETLHKNIMSRTKIIAAMRRRMTEIGFNEFSTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVTQEEVWETMEPVMRGIFEEFAEGKPVTKVFRRIAYDDAIRTYGSDKPDLRNPIEMQAVTDHFAGSGFKVFANMIANDAKVEVWAIPAKTGGSRAFCDRMNSWAQSEGQPGLGYIFWRKEGDKLEGAGPIAKNIGEERTEAIRKQMGLEDGDACFFVAGLPSKFYKFAGDARTRAGEELNLVDRDRFELAWIIDFPFYEWDEDNKKIDFAHNPFSMPQGGMDALENMDPLEIKAYQYDLVCNGFEIASGSIRNQLPEVMVKAFEKVGLSQQDVEERFGGLYRAFQYGAPPHGGMAAGIDRVIMLLVGAKNLREISLFPMNQQALDLLMGAPSEVSPAQLRDLHVRLAPVQKS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Brucella suis (strain ATCC 23445 / NCTC 10510)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.273 kDa
Sequence
MHRYRSHTCAALRKTDVGSNVRLSGWVHRVRDHGGILFIDLRDHYGITQIVADPDSPAFKVAETVRGEWVIRVDGEVKARADDAVNTNLPTGEVEIFATEIEVLSPAKELPLPVFGEPDYPEDIRLKYRFLDLRRETLHKNIMSRTKIIAAMRRRMTEIGFNEFSTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVTQEEVWETMEPVMRGIFEEFAEGKPVTKVFRRIAYDDAIRTYGSDKPDLRNPIEMQAVTDHFAGSGFKVFANMIANDAKVEVWAIPAKTGGSRAFCDRMNSWAQSEGQPGLGYIFWRKEGDKLEGAGPIAKNIGEERTEAIRKQMGLEDGDACFFVAGLPSKFYKFAGDARTRAGEELNLVDRDRFELAWIIDFPFYEWDEDNKKIDFAHNPFSMPQGGMDALENMDPLEIKAYQYDLVCNGFEIASGSIRNQLPEVMVKAFEKVGLSQQDVEERFGGLYRAFQYGAPPHGGMAAGIDRVIMLLVGAKNLREISLFPMNQQALDLLMGAPSEVSPAQLRDLHVRLAPVQKS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Brucella suis biovar 1 (strain 1330)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.273 kDa
Sequence
MHRYRSHTCAALRKTDVGSNVRLSGWVHRVRDHGGILFIDLRDHYGITQIVADPDSPAFKVAETVRGEWVIRVDGEVKARADDAVNTNLPTGEVEIFATEIEVLSPAKELPLPVFGEPDYPEDIRLKYRFLDLRRETLHKNIMSRTKIIAAMRRRMTEIGFNEFSTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVTQEEVWETMEPVMRGIFEEFAEGKPVTKVFRRIAYDDAIRTYGSDKPDLRNPIEMQAVTDHFAGSGFKVFANMIANDAKVEVWAIPAKTGGSRAFCDRMNSWAQSEGQPGLGYIFWRKEGDKLEGAGPIAKNIGEERTEAIRKQMGLEDGDACFFVAGLPSKFYKFAGDARTRAGEELNLVDRDRFELAWIIDFPFYEWDEDNKKIDFAHNPFSMPQGGMDALENMDPLEIKAYQYDLVCNGFEIASGSIRNQLPEVMVKAFEKVGLSQQDVEERFGGLYRAFQYGAPPHGGMAAGIDRVIMLLVGAKNLREISLFPMNQQALDLLMGAPSEVSPAQLRDLHVRLAPVQKS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Sinorhizobium fredii (strain NBRC 101917 / NGR234)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.145 kDa
Sequence
MHRYRSHTCAALRKSDVGSTVRLSGWVHRVRDHGGVLFIDLRDHYGMTQVVADPDSPAFKMAETVRGEWVIRIDGTVKARTDDTVNKNMPTGEIELYAREIEVLSAAKELPLPVFGEPDYPEDVRLKYRFLDLRRETLHRNIVKRTEVISAMRRGMSDIGFTEYTTPILTASSPEGARDFLVPSRIHPGTFYALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVEQEDVWDTMEPMIRAIFADFADGKPVTDKFPRIPYDTAIRKYGSDKPDLRNPIEMQEVTQHFAGSGFKVFANMIATNPKVEIWAIPAKTGGSRAFCDRMNAWAQSQGQPGLGYIFWRKEGEKLEGAGPLAKNIGEERTDAIRTQLGLEDGDACFFVAGEPAKFYKFAGEARTRAGEELNLVDRDRFELCWIVDFPFYEWNEDEKRVDFAHNPFSMPQGGLKALSGDDLLSIKAFQYDMVCNGFEIASGSIRNQSPELMVKAFENVGLSQADVEEQFGGLYRAFQYGAPPHGGMAFGIDRIVMLIVGAKNLREISLFPMNQQAVDLLMGAPSPATPAQLRELAIRPIPQKKD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Sinorhizobium medicae (strain WSM419)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.094 kDa
Sequence
MHRYRSHTCAALRKSDVGSTVRLSGWVHRVRDHGGVLFIDLRDHYGMTQVVADPDSPAFKAAETVRGEWVIRVDGAVKARTDETVNRNMPTGEVELYAREIEVLSAAKELPLPVFGEPDYPEDVRLKYRFLDLRRETLHKNIVRRTEIIAAMRRRMSDIGFTEYTTPILTASSPEGARDFLVPSRIHPGNFYALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVEQEDVWDAMEPMIRAIFADFAGGKPVTDKFPRIPYDAAIRKYGSDKPDLRNPIEMQEVTEHFAGSGFKVFANMIASNPKVEIWAIPAKTGGSRAFCDRMNAWAQSQGQPGLGYIFWRKEGEKLEGAGPLAKNIGEERTDAIRTQLGLGDGDACFFVAGEPAKFYKFAGEARTRAGEELNLVDRERYELCWIVDFPFYEWNEEEKRVDFAHNPFSMPQGGLTALSSDDLLSIKAFQYDMVCNGFEIASGSIRNQSPELMVKAFENVGLSQADVEERFGGLYRAFQYGAPPHGGMAFGIDRIVMLLVGAKNLREISLFPMNQQAQDLLMGAPSPAEPAQLRELAIRPVPQKKD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Gloeobacter violaceus (strain ATCC 29082 / PCC 7421)
Length
595 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.973 kDa
Sequence
MRSDYCGTLRSEHIGKTVSLYGWIDGWRDHGGVIFLDLRDYTGIVQIVADPQRTPESYHLASSLRNEYVVRVEGRVSARPEHSLNPRLSTGTVEVYADTLAVLNRAETPPFAISKDEEVDEKLRLKFRYLDLRRGRMQKLLRLRHRVMQIMRRHLDERGFTEIETPVLVKSTPEGARDYLVPSRVNPGDWFALPQSPQLFKQLLMVAGFDRYYQIARCFRDEDLRADRQPEFTQLDMEMSFLSMEEIIALNEGLVAAILQETMGLELSLPLPRLTYAEAMVRYGSDKPDTRFGLELVEVSEVFRESSFQVLSGAVAAGGKVVCLPVPGAEGITNTRVKPGGDLFEFVTQFGARGLLFARVREGGQVDTIGAFSKSLTPEIAAGMIEKTGAQPGHLLLFGAGDRTAVPTVLDYMGRLRLKMGEELGLIDPNRHNLLWVTDFPMFEWNAEEKRLEALHHPFTAPRPEDEHDLKTARALAYDIIWNGVEVGGGSLRIYRRALQERVFETIGLTEEEARAKFGFLLDAFEYGTPPHGGIAYGFDRFVMLIAGEQSIREVIAFPKTQRAQDLMLGAPSAVAERQLKELNVRSTLPPKTQG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Herpetosiphon aurantiacus (strain ATCC 23779 / DSM 785 / 114-95)
Length
594 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.263 kDa
Sequence
MLRTHTCGELRRDHIDQTVTLAGWVHRRRDHGTVLFLDLRDRYGLTQVIVDPSSNPEARAMLDSIKNEYVIQVTGRVRSRLEGAENANLATGAIELEVQSAKILNTAKTPPILVNRDGGEDEALRLKYRYIELRRERQQHILGLRHRTIKFMRDWMDREGFWEIETPILMKSTPEGARDYLVPSRLHPGEFYALPQSPQQLKQLLMVSGIDKYFQIARCMRDEDLRADRQPEFTQLDIEMSFVEQDDVLDVVERLMTELVANVTPHKRLVSPFPRLTYADAIEYYGSDKPDLRYDLKFVNVGEIVKDSQFGVFTGALSSGGKVQAIRLPGCGSYSRKQIDDLQEVAKIGGAKGMAWMAIEADGSVRSPIAKFFEQAQLDQLKSATAAEAGDLIVYVADKPAVVAASLDKVRREMAKRLDLADKDLMHFAWVIDFPMFEYNAESGEWDAAHHPFCMVNPADVEKMQRGEFEGVRAASYDLVCNGYELASGSIRIHDRSIQQYIFDRLPYSPEEIQKRFGHMLEAFEYGAPPHGGMAPGIDRLVMLLADTDNIRDVIAFPKTQRAEDLMMNAPSSVDAKQLRELGLRLADGVEPRG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Hydrogenobaculum sp. (strain Y04AAS1)
Length
594 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.135 kDa
Sequence
MLRDTYIGLVDDSFIGKHVKLAGWIDSIRDHGGVLFIDLRDKEGKLQAVLEESGNKELYDIAKHFKEESVVLVEGLVRRRPSGTENPKIKSGNVELLIERIELLNASETLPFPIDDNVDISEELRLKYRYLDLRRPKFQKAIKTRSKALKITRDFFEENGFYEIETPFLIKSTPEGARDFLVPSRLHPGKFYALPQSPQLFKQILMISGFDRYFQIARCFRDEDLRSDRQPEFTQIDFEMSFVEEQDIMEISEKLLSKLFLELLDIELSTPFKRITYKEAMERYGSDKPDTRFGLELVDLSDIFKNTNFNVFKSAIEQKGIIKAIKINKILSRKEIDNLTEYVKGLGAKGLAWGKIENGEFSSPIAKFLTEEEIKAMLSRLEAKDQDMIFFSADKPKNVYKILGNLRLQLGKMLNLIDESKFAFLWVVDFPMFEYNEEEGRLEAMHHPFTSPKTEDLDKIKYIVDKSDKEDIINIGENIGARAYDIVLNGVEIGGGSIRIHKQDIQKLVFKILNITDEEAAMKFGFLLEALKYGAPPHGGLAFGFDRLMAMMLGFDSIRDVIAFPKTQKGTCLLTGAPDVVSDKQLKELHIKIT

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Thermodesulfovibrio yellowstonii (strain ATCC 51303 / DSM 11347 / YP87)
Length
594 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.347 kDa
Sequence
MFRDKYCAEVKEEEIGKEISLCGWVFRRRDHGGLIFIDLRDRTGIIQVVFSPEISIEMHQKAHGLRSEYVIAVKGILKKRPEGTENPELITGNVELWAKELEILSFSKPLPFQLDEMAEVSELLRLKYRYLDLRRAEMQKNFLLRHRITMAVRNFLDSKGFVEVETPMLTKSTPEGARDFLVPSRLNPGTFYALPQSPQLFKQILMMSGFDRYFQIVRCFRDEDLRADRQPEFTQIDFEMSFVKPEDIIEIVEEMLFKCFKEVLEVDIEIPFKRLTYEEAINKYGSDKPDLRFALEIQDVSELVKNSQFKVFLDTIEKGGVVKAICGKGLASLSRSEIDKLTALAQSFGAKGLAWIKVKNGFESPIVKFFSESLLREIAEKVGVEDGDMILFVADKKSLANEVLGRLRLEIAERAQIKKEGFYFAWVLDFPLFEWDEEEKRFVSMHHPFTSPKDEDIDKLLKIPQEAFYDPQSSVKDIKAKAYDIVLNGYELGGGSIRIHKADIQEHIFRILAISEEEIKRRFGFFVEALRYGAPPHGGIALGLDRLVMVMTGANSLRDVIAFPKTQKAFCPLSEAPSEVNLKQLRELHIKLDI

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chelativorans sp. (strain BNC1)
Length
594 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.143 kDa
Sequence
MHRYRSHTCEELRPSDVGGTVRLSGWVHRVRDHGGLLFIDLRDHYGITQIVADPDSPSFSTAEKLRSEWVIRVDGEVKARTPETVNPNLATGGVEVFAREIEVLSQAKELPLPVFGEPDYPEDIRLKYRFLDLRRETLHRNILARTKIIAEMRKRMAESGFTEFSTPILTASSPEGARDFLVPSRLHQGKFYALPQAPQIYKQLIMVSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVTQEDVFSTMEPVMRGIFEAFAEGKPVTQKLPRIPYDEAMRKYGSDKPDLRNPIVMEEVSEHFRGSGFKVFANILANDPKAEVWAIPAKTGGSRAFCDRMNSWAQGEGQPGLGYIFWRKEGDTLEGAGPIAKNIGPERTDAIRTQLGLGDGDACFFVAGDPKKFVAFAGAARTRAGEELNLVDRDRFELAWIVDFPFYEWNEDEKRIEFGHNPFSMPQGGMEALENQEPLSIKAFQYDLVCNGFEIASGGIRNHMPELMVKAFEVAGFDRQMVEERFGGLYRAFQYGAPPHGGMAAGIDRIVMLLRGAKNLREITMFPMNQQAMDLLMGAPSEATPQQLRELHIRLAPKQD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Length
594 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.981 kDa
Sequence
MLRSHAAGLLREGDAGQQVTLAGWVARRRDHGGVIFIDLRDASGIAQVVFRDPQDTEVLAQAHRLRAEFCVSVAGVVEIRPEGNANPEIATGEIEVNATSLTVLGECAPLPFQLDEPAGEELRLKYRYLDLRRDDPAAAIRLRSRVNAAARAVLARHDFVEIETPTITRSTPEGARDFLVPARLHPGSFYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDMEMSFVDAEDIIAISEEVLTELWALIGYRIPTPIPRIGYAEAMRRFGTDKPDLRFGLELVECTDFFSDTTFRVFQAPYVGAVVMPGGASQPRRTLDGWQDWAKQRGHRGLAYVLVAEDGTLGGPVAKNLTEAERTGLADHVGAKPGDCIFFSAGPVKSSRALLGAARVEIANRLGLIDPDAWAFVWVVDPPLFEPADEATAAGEVAVGSGAWTAVHHAFTAPKPEWEDRIESDTGSVLADAYDIVCNGHEIGGGSVRIHRRDIQERVFAVMGLDKAEAEEKFGFLLEAFMFGAPPHGGIAFGWDRTTALLAGMDSIREVIAFPKTGGGVDPLTDAPAPITAQQRKESGIDAQPKRVQQA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Length
594 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.981 kDa
Sequence
MLRSHAAGLLREGDAGQQVTLAGWVARRRDHGGVIFIDLRDASGIAQVVFRDPQDTEVLAQAHRLRAEFCVSVAGVVEIRPEGNANPEIATGEIEVNATSLTVLGECAPLPFQLDEPAGEELRLKYRYLDLRRDDPAAAIRLRSRVNAAARAVLARHDFVEIETPTITRSTPEGARDFLVPARLHPGSFYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDMEMSFVDAEDIIAISEEVLTELWALIGYRIPTPIPRIGYAEAMRRFGTDKPDLRFGLELVECTDFFSDTTFRVFQAPYVGAVVMPGGASQPRRTLDGWQDWAKQRGHRGLAYVLVAEDGTLGGPVAKNLTEAERTGLADHVGAKPGDCIFFSAGPVKSSRALLGAARVEIANRLGLIDPDAWAFVWVVDPPLFEPADEATAAGEVAVGSGAWTAVHHAFTAPKPEWEDRIESDTGSVLADAYDIVCNGHEIGGGSVRIHRRDIQERVFAVMGLDKAEAEEKFGFLLEAFMFGAPPHGGIAFGWDRTTALLAGMDSIREVIAFPKTGGGVDPLTDAPAPITAQQRKESGIDAQPKRVQQA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875)
Length
594 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.88 kDa
Sequence
MRTHYCGHLNREHIGQTVTLCGWAHRRRDHGGVIFIDLRDREGMAQIVIDPDTPEAFKIAESVRNEFVLKVVCKVRARPEGTVNLNIPTGEVEMLASEIEILNPSLTPPFMLDDDNLSEMVRLEHRYIDLRRPAMQKNLMLRYRVAKVLRDQLDSQGFIEVETPMLTRSTPEGARDYLVPSRVHHGQFFALPQSPQLFKQLLMVSGFDRYFQITKCFRDEDLRADRQPEFTQVDIETSFLNEEEIMTIVEGMIRTMFKQVQDIDLPNPFPRISFAEAMNRYGSDKPDMRVTLEITELTDVMKDVDFKVFAGAANSAGGRVAAIRVPNGAALSRSEIDAYTEFVKIYGAKGLAYIKVNDASKLNEEGLQSPIVKNIHEPALKAIIERTGAQSGDIVFFGADKAKIVNEALGALRTKIGHEKGHVDGRAWAPLWVVDFPMFEHDEENDRWVALHHPFTSPKDGHEDLLASNPGAALSKAYDMVLNGWEVGGGSVRIHKQEVQSKVFDALKISKEEAQEKFGFLLDALQYGAPPHGGLAFGLDRLVTLMAGAESIRDVIAFPKTQRAQCLMTKAPNEVDEKQLRELHIRVRQQNPAA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pelagibacter ubique (strain HTCC1062)
Length
594 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.157 kDa
Sequence
MNKYRTHTCSELTIDSRGKDVVLSGWINKKRDHGNLLFIDLRDNYGMTQCIIDKSNQNFNSLEKIQLESVIKINGKVVERTKETINTDLQTGEIEVNINSFEVLGTCKELPMPVFSDQEYAEEIRLKYRFLDLRRKKIHDNIILRSKVISFIRSEMSKLGFLEFQTPILTSSSPEGARDFLVPSRLNPGKFYALPQAPQQFKQLIMVSGFDKYFQIAPCFRDEDARADRSPGEFYQLDLEMSFVEQEDVFQVVEKLIVNVFKKFSEKKLMYEKFPRIPYEESMLKYGSDKPDLRNPLIISDLSNIFIRDDVTFEIFKKLVKSGSKVRCIVTKNTKDKPRSFFDNIDKWAKEQGASGLAYFTIEKEENISARGPVGKFFSKEALEEIMKITGAEIGDSIFFACGKINDVEKITSLARDKIAKDLKLIDENTFAFCWVVDYPMFEKNEVTNKIEFSHNPFSMPQGDLKDIDFDNPLNIKAYQYDIVCNGIELSSGAIRNHVPELMYKLFSIAGYQKEQVDEKFSGMINALSYGAPPHGGIAPGIDRIVMLLANEKNIREVTMFPMNQNAQDLMMNAPSNVNEEQLKELGLALKLKK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Proteus mirabilis (strain HI4320)
Length
594 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.599 kDa
Sequence
MRTNYCGQLNSAHVGQKVTLCGWVNRRRDLGGLIFIDMRDREGIVQVFFDPEQKEAFSQASELRNEFCIQVTGTVRARPDSQVNKNMATGEIELAAESLSIFNRSEALPLDSNQTNTEERRLTYRYLDLRRPEMSQRLKTRAKITSFVRRFMDGEGFLDVETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAEQVREVMERMIHALWLDILNVDLGAFPVMTFAEAMRRYGSDKPDLRNPMELIDIADLVKNVEFSVFAQAANDEKCRVIALRVPGGASLTRKNIDEYTQFVSIYGAKGLAWMKVNEKAKGIEGVQSPIAKFLTNDVVNSILAATNATDGDLIFFGAGRQGTMSDAMGALRLKVGRDLELTDLNAWKPLWVIDFPMFEEDEDTGSLSAMHHPFTSPKDLTPAELTAHPVGAVANAYDMVINGYEVGGGSVRIHRNEMQQAVFSILGITPDEQREKFGFLLDALKFGTPPHAGLAFGLDRLVMLLTGTDNIRDVIAFPKTTAAACLMTNAPSFANEDALKELAIQVTEKEVSTDNE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Geobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210)
Length
594 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.613 kDa
Sequence
MEDILGEWKRSHYCGNLTKADVGREVILMGWILRRRDHGGLIFADLRDREGLAQIVFDPAKNTDAHHKAEAIRNEYVVAVKGEVIPRPEGTVNSAMKTGEVEVLVTECKILNRSKALPFTLDDYVDVAENIRLKYRYLDLRRPVLQQNLILRSMVAQITRQYLSENGFLEIETPFLTKSTPEGARDFLVPSRINQGNFYALPQSPQIFKQILMISGFDRYFQIVRCFRDEDLRADRQPEFTQIDCEMSFIDREDIISVMEGLIAKIFTVAKGVDVPLPMPRMTYAEAIRRFGVDNPDVRFGLELVELTDIVKGAGFKVFADVAASGGIIKGLNAKGCARFSRKEIDDLTEFAKIYGAKGLAYVKIEEGQWHSPIAKFFSAEEIATMNQAFGAEDGDLLLFVADKPKVVNDSLGKLRNHLAGILGLADKNTFRFVWITDFPLLEWDEDEKRWAAVHHPFTAPMDEDLEKVESDPGSCRAKAYDLVLNGNEIGGGSIRIHQQHVQSLMFSMLGLSDDETRAKFGFLLDALECGTPPHGGIAFGMDRLIMLLTGSDSIRDVIAFPKTQKGACLMSEAPSPVDAKQLRELALKVTVKQ

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA)
Length
594 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.825 kDa
Sequence
MTDMLGDWKRSHLCGTLTKADVGKQVTLMGWVMRRRDHGGLIFIDLRDREGLAQIVFDPAKAPEAHREAEAVRNEYVVAIKGEVVPRPEGTVNPNMKTGEVEILVTQCKLLNRSKALPFTLDDYVDVAENLRLKHRYLDLRRTPLQQNLILRSRVSQVTRQYLTENGFLEIETPFLTKSTPEGARDFLVPSRINQGNFYALPQSPQIFKQILMISGFDRYFQVVRCFRDEDLRADRQPEFTQIDCELSFVDRDDVIAVMEGLIARIFKEAKEIDVQLPIPRMTYAEAIRRYGVDNPDVRFGLELVELTDIVKGSGFKVFADVAAGGGIIKGLNAKGCARFSRKEIDDLTEFVKIYGAKGLAYVKIEGGEWHSPIAKFFTAQEIADMNRAFGAEEGDLLLFVADKPKVVNDSLGKLRNQLAQILGLVDKGTFKFVWITDFPLLEWDEEEKRWAAVHHPFTAPMDEDLDKVESDPGACRAKAYDLVLNGNEIGGGSIRIHQQHIQSLMFRMLGLSEEEARAKFGFLLDALEFGTPPHGGIAFGMDRLIMLLTGSDSIRDVIAFPKTQKGACLMSDAPSPVDSKQLRELAIKVTVKQ

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Geobacillus sp. (strain WCH70)
Length
594 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.321 kDa
Sequence
MFGRTYYCGEITEKAIGEKVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFSPEVSKEALNVAEKVRNEYVLSVEGTVVAREEGTINPNLPTGKIEIQAERITIINEAKTPPFVITDQTDVAEEVRLKYRYLDLRRPVMFRTLQLRHRVTKAIRDFLDGEGFLEVETPILTKSTPEGARDYLVPSRVHPGEFYALPQSPQIFKQLLMVAGFERYYQIARCFRDEDLRADRQPEFTQIDIETSFMSQEEIMQLTERMMAYVMKMAKGIDISLPFPRMSYDEAISRYGSDKPDTRFGLELVDVSEIVKNSSFKVFAGAIANGGQVKAINVKGAADQYSRKDIDALAEFVARYGAKGLAWLKVEEDGLKGPIAKFFTEEEQNGLIRTLEAEAGDLLLFVADHKTVVANALGALRVKLGKDLNLIDETKFNFLWITDWPLLEYDEEDGRYYAAHHPFTMPVREDLPQLETNPEKVRAQAYDLVLNGYELGGGSMRIFEREVQEKMFRALGFTEEEARKQFGFLLEAFEYGTPPHGGIALGLDRLVMLLAGRTNLRDTIAFPKTASASCLLTEAPSPVSEQQLEELHLVVNSEKKSEQY

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Ruegeria sp. (strain TM1040)
Length
594 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.164 kDa
Sequence
MHAFRSHTCAELNKSHVGETVRLSGWVHRVRDHGGLLFIDLRDHYGVTQVMADPDSPVFAEIEKVRSEWCIRIDGEVKARDESLVNAKIPTGEIEVFIRDIEVLGKSEELPLMVFGEQEYPEETRLRYRYLDLRREKMQRNMVLRSNMIRSIRNRMWDQGFNEYQTPIITASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLMMVSGFDKYFQIAPCFRDEDPRADRSPTDFYQLDMEMSFVTQQDVFDTIAPVIAGVFEEFGQGRKVDAPNEWPQISYKDAALWYGSDKPDLRNPIKMQVVSEHFRGSGFAIFAKLLEQEGTEIRAIPAPTGGSRKFCDRMNAFAQKEGLPGMGYIFWREGADGMEAAGPLAKNIGPERTEAIRQQLGLGVGDAAFFLGGKPKTFEAVAGRARNVIGEELNLTDKDRFAFAWIVDFPIYEKDEETGKIDFEHNPFSMPQGGMDALNGDPLDVRGNQYDLACNGYELVSGAIRNHKPEIMFKAFEIAGYGKEEVEKRFGGMVNAFQYGAPPHGGCAAGIDRMVMLLADEANIREVIMFPMNQRAEDLMMAAPSEPMSEQLMELGLRVIPQDD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Saccharophagus degradans (strain 2-40 / ATCC 43961 / DSM 17024)
Length
594 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.508 kDa
Sequence
MRSVYCGVVNTSNIDQEITLCGWVDRRRDHGGVIFIDLRDREGIVQVVFDPDAADKFALADKVRPEYVLRVTGKVRARSEATVNANMATGQIEVYGTDLEILNSAETPPFQLDEHTNVGEDVRLKYRYLDLRRDAMQQRLKFRSKVTNAIRNYLDDNDFLDIETPILTRATPEGARDYLVPSRTHDGKFFALPQSPQLFKQLLMVSGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFMDEEQIMSVTEGMISKLFRELKGVELGEFPRMPYAEAMEKYGSDKPDMRIPLEMVEIKDLMASVDFKVFSGPASDPKGRVTAMKVPGGGEIPRKKIDAYTKFVSIYGAKGLAYIKVNDKTDLEGGLQSPIVKFLPQDVLQALLDRLEVENGDLIFFGADSAKVVTEALGALRCELGKDLNLYTCEWAPLWVVDFPMFEELEDGSLTALHHPFTAPSCSPEELSANPATALSRAYDMVLNGTELGGGSIRIHDQSMQQEVFRVLGIGEEEQREKFGFLLDALKYGAPPHGGLAFGLDRLIMLMTGASSIRDVIAFPKTQSAACVMTDAPGAVDKKQLEELHIRLRPVVAQPKEQG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Dictyoglomus thermophilum (strain ATCC 35947 / DSM 3960 / H-6-12)
Length
593 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.64 kDa
Sequence
MRRTHYCGEINIKNVGEKVSLSGWVHRIRHHGGLIFIDLRDRSGIVQLVVDPAISQESYNIADTLGNEWVISVEGKVRKRPEGMENPKIPTGEIEIEVEKINIENPSKPLPFNLWSNKEIDETVRLKYRYLDLRRDKMQSNIIFRHNFILAIRNFLAQNGFIEIETPYLIVSTPEGARDFIIPSRLQPGKFYALPQSPQLFKQILMVSGFDRYFQIARCFRDEDLRADRQPEFTQLDMEMSFVEIEDIFNIIENLFKTTLKNLMNIDITVPFPRITYEEAMNTYGSDKPDLRYDLKISDVTEIFKNLPLEFIRSTLEKNGVIKGIILKNIVPSRREWSIIENKVRELKGKGIMWFTYTDGELKSSISKYLDENTKNKLIENLNLREGDSFFCIAGEWKEVVKILGTLRLEIAELFNIEKKEGLYFLWVTDFPLFEYDEEERRIVAEHHPFTSPKDEDIPLLDTDPLKVKAKCYDLVLNGTELGSGSIRIHKKEIQEKVFNILNITPEDAKKKFGFLLEAFEYGAPPHGGIALGIDRIIAILTKSNSLRDVIAFPKTQSGTCLLTGAPSEVDSKQLEEVHIRVVYPEEKRKEEE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Serratia proteamaculans (strain 568)
Length
593 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.483 kDa
Sequence
MRTEYCGQLNLSHVGQEVTLCGWVNRRRDLGGLIFIDMRDREGIVQVFFDPDQKAAFDKAYDLRNEFCIQIVGTVRARPDSQINKDMATGEVEVFAHALEIINRSEPLPLDSNQVNSEEARLKYRYLDLRRPEMADRLKTRAKITSFVRRFMDSHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAEQVREVMEKLARELWLDVKNVDLGDFPIMTFEEAMRRYGSDKPDLRNPLELVDVADLVKDVEFKVFSGPANDAKGRVAAICVPGGAQLTRKLIDEYGAFVNIYGAKGLAWLKVNDRAAGMEGVQSPIAKFLSAEVLEAILARTNAQSGDILFFGADSFKIVTDAMGALRLKLGRDLELTKLDSWAPLWVVDFPMFEEDGEGGLAAMHHPFTAPRDMSPEELAGTPTNAIANAYDMVINGYEVGGGSVRIHRSEMQQTVFSILGINEHEQREKFGFLLDALKYGTPPHAGLAFGLDRLVMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPASLQELAICVVKKASEQESE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Nitrosomonas eutropha (strain DSM 101675 / C91)
Length
593 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.311 kDa
Sequence
MRTDYCGAINTRHLGRTITLCGWVHRRRDHGGVIFIDLRDREGIVQIVCDPDNVAAFPIAEKIRNEFVLEITGLVRHRPEGTVNRGIPSGEIEVLVSTIEILNPSLTPPFQMDDDNLSEAIRLEYRYLDLRRPAMQHNIRLRHKVTMATRVFLDQHGFIDVETPMLTKSTPEGARDYLVPSRVNVGCFFALPQSPQLFKQLLMVSGFDRYYQITRCFRDEDLRADRQPEFTQIDIETSFLQENDIMDLMEDMIRRLFADVINVSLPDPFPRISYADAMFRYGSDKPDLRVPLELTELTDLMQDVPFQVFRDAAQKPGGRVAALRVPGGGELSRKEIDEYTRFVGIYGAKGLAYIKINDLTKGMEGLQSPILKFLPEPVVQSMLERTQAQNGDLVFFGADKVKTVNDALGALRVKIGHERGLATNLWQPLWVVDFPMFEWDEEEKRWQALHHPFTAPSQGHEDFLATDPGKALSRAYDMVLNGMEIGGGSIRIHRQDVQSKVFQALNIADDEAKLKFGFLLDALQYGAPPHGGIAFGLDRIVAMMTGTDSIRDVIAFPKTQRAQCLLTQAPSTVEEKQLRELHIRLRKTDITTD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Nitrosomonas europaea (strain ATCC 19718 / CIP 103999 / KCTC 2705 / NBRC 14298)
Length
593 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.12 kDa
Sequence
MRTDYCGAINTRHLDKTITLCGWVHRRRDHGGVIFIDLRDREGIVQIVCDPDNVAAFQIAEKIRSEFVLAITGTVRHRPEGTVNHGILSGEIEVLVNAIEILNPSLTPPFQMDDDNLSEAIRLEYRYLDLRRPVMQRNIRLRHQVTMAVRIFLDQHGFIDVETPMLTKSTPEGARDYLVPSRVNAGHFFALPQSPQLFKQLLMVSGFDRYYQITRCFRDEDLRADRQPEFTQIDIETSFLPENEIMGMMEDMIRRLFASVLDISLPDPFPRLSYADAMFLYGSDKPDLRVPLVLTELTDLMQDVPFQVFRDAAQKAGGRVAALRVPGGGELSRKEIDEYTQFVGIYGAKGLAYIKINDLTKGIEGLQSPILKFLPESVVQSILERTQAQNGDLVFFGADKAKVVNDALGALRVKIGHERNLATDSWQPLWVVDFPMFEWDEEEKRWQALHHPFTSPSQGHEDFLTSDPGKALSRAYDMVLNGMEIGGGSIRIHRQDIQSKVFQALNISDDEAKLKFGFLLDALQYGAPPHGGIAFGLDRIVAMMTGADSIRDVIAFPKTQRAQCLLTQAPGAVEEKQLRELHIRLRRTENTNN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013)
Length
593 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.08 kDa
Sequence
MRSHYCGDINRSHLGQEVTLVGWVNRSRDLGGVVFLDLRDREGLVQVVYDPDLKDVFDVASSLRGEFCVQVTGLVRARPDSQINSQMKTGEIEVLGKGLTIINASAPLPLSMDNHQNNSEEQRLKYRYLDLRRPEMAERLIFRAKVTSAVRRFLDSNGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTSEEVMVKTEEMMRGLFLELLNVDLGEFPRMTYNEAMRRFGSDKPDLRNPLELVDVADLLKEVEFAVFNGPANDEEGRVAALRIPNGATLSRKQIDDYTKFVGIYGAKGLAWMKINDLAAGMEGIQSPVLKFLTESIVNDIISRTGAQTGDIILFGADKANVVAEAMGALRLKAGEDFELLEGQWRPLWVIDFPMFEKINGGFHAVHHPFTAPRGVTAAELEANPANRVSDAYDMVLNGCELGGGSVRIHNAEMQSAVFRILGIEEEEAKEKFGFLLEALRYGTPPHAGLAFGLDRIIMLMTGATSIRDVMAFPKTTTAACPLTNAPGFANPAQLTELGIKVVEKVKVADGE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shewanella piezotolerans (strain WP3 / JCM 13877)
Length
593 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.014 kDa
Sequence
MRSHYCGDVNKSHVGQEVTLVGWVNRSRDLGGVVFLDMRDREGIVQVVYDPDLPEVFEVASSLRSEFCVQIKGLVRARPDSQVNADMRTGEIEILGLELTVLNSSAPLPINMDKNQHNTEEQRLKYRYLDLRRPEMADRIVFRSKVTSAVRRFLDGNGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTSEQVMAKTEEMTRGLFKELLDVDLGEFPRMTFAEAMRRYGSDKPDLRNPLELIDIADLVKEVEFAVFNGPANDPEGRVAVLSIPGGAKLSRKQLDEYAKYVTIYGAKGLAWMKVNDLDKGMEGIQSPVLKFLTEDVVKALLERTGAQTGDVILFGADKANVVAEAMGALRLKAGEDFDLLKGDWKPLWVVDFPMFERTSDGGLHAMHHPFTAPSNMTPAELEANPTAAISDAYDMVLNGCELGGGSVRIHNSEMQSAVFRILGINDEEANEKFGFLLEALRYGTPPHAGLAFGLDRIIMLMTGASSIRDVMAFPKTTTAACPLTNAPGFANPVQLVELGVSVIEPEVKDGE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Legionella pneumophila (strain Paris)
Length
593 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.922 kDa
Sequence
MRTHYCSAVNELSLDKQITVCGWVHNRRDHGGVIFLDIRDRSGLLQVVYEPENKEIFAIAEKLRSEFVVRVTGIVRKRPEGMINDKMETGRVEVIGIQLEILNQSPTPPFLPDDHQIINEDLRYKYRYIDLRRAVMQKKLTLRHKLNSCIRNYLNEQNFLDIETPMLTKATPEGARDYLVPSRVHPGQFYALPQSPQLFKQLLMMSGFDKYYQIVRCFRDEDLRADRQPEFTQLDIEMAFINEEDILQLIEGLLKVVFKEILNITLPDKLPRMSYKEAMTRYGSDKPDLRNPLELIDIADLVKDCDFNVFASAANDNSGRVVALKLPNGCDLSRKDLDNYGQFVTIYGAKGLAYIKVNDLSAGMAGLQSPILKFLSETAVQSILNRVEAQTGDVIFFGADKAHVVNESMGALRNKLGHDRNLINPGWQLLWVIDWPMFELDPQSNKLQPMHHPFTSPQELSAEALRSKPTQTLAKAYDIVINGYEIGGGSIRIHQPELQKTVFDLIGIDEQEAHEKFGFLLDALQYGAPPHGGIALGIDRLAMLLTDSTSIRDVIAFPKTQTASCPLTSAPSPAGNAQLTELGIRLAPTITTK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Legionella pneumophila (strain Corby)
Length
593 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.844 kDa
Sequence
MRTHYCSAVNELSLDKQITVCGWVHNRRDHGGVIFLDIRDRSGLLQVVYEPENKEIFAIAEKLRSEFVVRVTGIVRKRPEGMINDKMETGRVEVIGTQLEILNQSPTPPFLPDDHQIINEDLRYKYRYIDLRRAVMQKKLTLRHKLNSCIRNYLNEQNFLDIETPMLTKATPEGARDYLVPSRVHPGQFYALPQSPQLFKQLLMMSGFDKYYQIVRCFRDEDLRADRQPEFTQLDIEMAFINEEDILQLIEGLLKIVFKEILNITLPDKLPRMSYKEAMTRYGSDKPDLRNPLELIDIADLVKDCDFNVFSSAANDNSGRVVALKLPNGCDLSRKDLDNYGQFVTIYGAKGLAYIKVNDLSAGMAGLQSPILKFLSETAVQSILNRVEAQTGDVIFFGADKAHVVNESMGALRNKLGHDRNLINSGWQLLWVVDWPMFELDPQSNKLQPMHHPFTSPQELSAEALRSKPTQTLAKAYDIVINGYEIGGGSIRIHQPELQKTVFDLIGIGDQEAHEKFGFLLDALQYGAPPHGGIALGIDRLAMLLTDSTSIRDVIAFPKTQTASCPLTSAPSPAGNAQLTELGIRLAPTITTK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Length
593 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.909 kDa
Sequence
MRTHYCSAVNELSLDKQITVCGWVHNRRDHGGVIFLDIRDRSGLLQVVYEPENKEIFAIAEKLRSEFVVRVTGIVRKRPEGMINDKMETGRVEVIGTQLEILNQSPTPPFLPDDHQIINEDLRYKYRYIDLRRAVMQKKLTLRHKLNSCIRNYLNEQNFLDIETPMLTKATPEGARDYLVPSRVHPGQFYALPQSPQLFKQLLMMSGFDKYYQIVRCFRDEDLRADRQPEFTQLDIEMAFINEEDILQLIEGLLKIVFKEILNITLPDKLPRMSYKEAMTRYGSDKPDLRNPLELIDIADLVKDCDFNVFASAANDNSGRVVALKLPNGCDLSRKDLDNYGQFVTIYGAKGLAYIKVNDLSAGMAGLQSPILKFLSETAVHSILNRVEAQTGDVIFFGADKAHVVNESMGALRNKLGHDRNLINSGWQLLWVVDWPMFELDPQSNKLQPMHHPFTSPQELSAEALRSKPTQTLAKAYDIVINGYEIGGGSIRIHQPELQKTVFDLIGIDEQEAHEKFGFLLDALQYGAPPHGGIALGIDRLAMLLTDSTSIRDVIAFPKTQTASCPLTSAPSPAGNAQLTELGIRLAPTITTK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Legionella pneumophila (strain Lens)
Length
593 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.923 kDa
Sequence
MRTHYCSAVNELSLDKQITVCGWVHNRRDHGGVIFLDIRDRSGLLQVVYEPENKEIFAIAEKLRSEFVVRVTGIVRKRPEGMINDKMETGRVEVIGTQLEILNQSPTPPFLPDDHQVINEDLRYKYRYIDLRRAVMQKKLTLRHKLNSCIRNYLNEQNFLDIETPMLTKATPEGARDYLVPSRVHPGQFYALPQSPQLFKQLLMMSGFDKYYQIVRCFRDEDLRADRQPEFTQLDIEMAFINEEDILQLIEGLLKIVFKEILNITLPDKLPRMPYKEAMTRYGSDKPDLRNPLELIDIADLVKNCDFNVFASAANDNSGRVVALKLPNGCDLSRKDLDNYGQFVTIYGAKGLAYIKVNDLSAGMAGLQSPILKFLSETAVQSILNRVEVQTGDVIFFGADKAHVVNESMGALRNKLGHDRNLINSGWQLLWVVDWPMFELDPQSNKLQPMHHPFTSPQELSAEALRSKPTQTLAKAYDIVINGYEIGGGSIRIHQPELQKTVFDLIGIDEQEAHEKFGFLLDALQYGAPPHGGIALGIDRLAMLLTDSTSIRDVIAFPKTQTASCPLTSAPSPAGNAQLTELGIRLAPTITTK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Clostridium botulinum (strain 657 / Type Ba4)
Length
593 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.788 kDa
Sequence
MGEALRGLKRTIMCGEPRENNIGEKVTVMGWVQRKRNLGGLIFVDLRDRTGIMQIVFGEEINKEAFEKSDNVKSEYCIAVTGEIVKRQSPNNDMETGAVELKGEDIKILSESETPPIYIKEGLDASENVRLKYRYLDLRRPDMQKIFMIRHKTCKVVRDFLDENGFLEMETPILTKSTPEGARDYLVPSRNYKGMFYALPQSPQIFKQLLMVSGYDKYFQITKCFRDEDLRANRQPEFTQIDMELSFVEEDDVIDLNEKLLAKVFKEVAGIDVKLPIERMPYKIAMEKYGSDKPDLRFGMEINDLTEAVKNSEFKVFKGAIEAGGSVRAIKAENCATMGRKQIDKLQDFVKTYKAKGLAWIAYKEDEIKSPIAKFLTEEEMKAILEKMDAKVGDLILIVGDKNNVVFESLGALRLHLAKELDIINKDEFRFVWITEFPLLAYNEEEGRYQAEHHPFTAIMDEDIDLLDTDPGKVRAKAYDIVLNGEELGGGSIRIHDSKLQEKMFSVLGFTKEKAWERFGFLLEAFKFGPPPHGGLAYGLDRMIMFLAGTENIKDVITFPKNQNAFCPLTEAPNVVDENQLEELGIKKIEKED

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A)
Length
593 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.808 kDa
Sequence
MGEALRGLKRTIMCGESRENNIGQKVTVMGWVQRKRNLGGLIFVDLRDRTGIMQIVFGEEINKEAFEKSDNVKSEYCIAVTGEIVKRQSPNNDMETGAVELKGEDIKILSESETPPIYIKEGLDASENIRLKYRYLDLRRPDMQKIFMIRHKTCKVVRDFLDENGFLEMETPILTKSTPEGARDYLVPSRNYKGMFYALPQSPQIFKQLLMVSGYDKYFQITKCFRDEDLRANRQPEFTQIDMELSFVEEDDVIELNERLLAKVFKEVGGIDVKLPIERMPYKIAMEKYGSDKPDLRFGMEINDLTEAVKNSEFKVFKGAIEAGGSVRAIKAENCATMGRKQIDKLQDFVKTYKAKGLAWIAYKEDEIKSPIAKFLTEEEMKAILEKMDAKAGDLILIVADKNNVVFESLGALRLHIAKELDIINKNEFRFVWITEFPLLAYNEEEGRYQAEHHPFTAIMDEDIELLGTEPGKVRAKAYDIVLNGEELGGGSIRIHDSKFQEKMFSVLGFTKEKAWERFGFLLEAFKFGPPPHGGLAYGLDRMIMFLAGTENIKDVITFPKNQNAFCPLTEAPNVVDENQLEELGIKKIEKED

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Clostridium botulinum (strain Kyoto / Type A2)
Length
593 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.802 kDa
Sequence
MGEALRGLKRTIMCGEPRENNIGEKVTVMGWVQRKRNLGGLIFVDLRDRTGIMQIVFGEEINKEAFEKSDNVKSEYCIAVTGEIVKRQSPNNDMETGAVELKGEDIKILSESETPPIYIKEGLDASENVRLKYRYLDLRRPDMQKIFMIRHKTCKVVRDFLDENGFLEMETPILTKSTPEGARDYLVPSRNYKGMFYALPQSPQIFKQLLMVSGYDKYFQITKCFRDEDLRANRQPEFTQIDMELSFVEEDDVIDLNEKLLAKVFKEVAGIDVKLPIERMPYKIAMEKYGSDKPDLRFGMEINDLTEAVKNSEFKVFKGAIEAGGSVRAIKAENCATMGRKQIDKLQDFVKTYKAKGLAWIAYKEDEIKSPIAKFLTEEEMKAILEKMDAKVGDLILIVADKNNVVFESLGALRLHLAKELDIINKDEFRFVWITEFPLLAYNEEEGRYQAEHHPFTAIMDEDIDLLDTDPGKVRAKAYDIVLNGEELGGGSIRIHDSKLQEKMFSVLGFTKEKAWERFGFLLEAFKFGPPPHGGLAYGLDRMIMFLAGTENIKDVITFPKNQNAFCPLTEAPNVVDENQLEELGIKKIEKED

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Clostridium botulinum (strain Okra / Type B1)
Length
593 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.833 kDa
Sequence
MGEALRGLKRTIMCGESRENNIGEKVTVMGWVQRKRNLGGLIFVDLRDRTGIMQIVFGEEINKEAFEKSDNVKSEYCIAVTGEIVKRQSPNNDMETGAVELKGEDIKILSESETPPIYIKEGLDASENIRLKYRYLDLRRPDMQKIFMIRHKTCKVVRDFLDENGFLEMETPILTKSTPEGARDYLVPSRNYKGMFYALPQSPQIFKQLLMVSGYDKYFQITKCFRDEDLRANRQPEFTQIDMELSFVEEDDVIELNERLLAKVFKEVGGIDVKLPIERMPYKIAMEKYGSDKPDLRFGMEINDLTEAVKNSEFKVFKGAIEAGGSVRAIKAENCATMGRKQIDKLQDFVKTYKAKGLAWIAYKEDEIKSPIAKFLTEEEMKAILEKMDAKAGDLILIVADKNNVVFESLGALRLHIAKELDIINKNEFRFVWITEFPLLAYNEEEGRYQAEHHPFTAIMDEDIELLDTEPGKVRAKAYDIVLNGEELGGGSIRIHDSKLQEKMFSVLGFTKEKAWERFGFLLEAFKFGPPPHGGLAYGLDRMIMFLAGTENIKDVITFPKNQNAFCPLTEAPNVVDENQLEELGIKKIEKED

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Clostridium botulinum (strain Langeland / NCTC 10281 / Type F)
Length
593 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.833 kDa
Sequence
MGEALRGLKRTIMCGESRENNIGEKVTVMGWVQRKRNLGGLIFVDLRDRTGIMQIVFGEEINKEAFEKSDNVKSEYCIAVTGEIVKRQSPNNDMETGAVELKGEDIKILSESETPPIYIKEGLDASENIRLKYRYLDLRRPDMQKIFMIRHKTCKVVRDFLDENGFLEMETPILTKSTPEGARDYLVPSRNYKGMFYALPQSPQIFKQLLMVSGYDKYFQITKCFRDEDLRANRQPEFTQIDMELSFVEEDDVIELNERLLAKVFKEVGGIDVKLPIERMPYKIAMEKYGSDKPDLRFGMEINDLTEAVKNSEFKVFKGAIEAGGSVRAIKAENCATMGRKQIDKLQDFVKTYKAKGLAWIAYKEDEIKSPIAKFLTEEEMKAILEKMDAKAGDLILIVADKNNVVFESLGALRLHIAKELDIINKNEFRFVWITEFPLLAYNEEEGRYQAEHHPFTAIMDEDIELLDTEPGKVRAKAYDIVLNGEELGGGSIRIHDSKLQEKMFSVLGFTKEKAWERFGFLLEAFKFGPPPHGGLAYGLDRMIMFLAGTENIKDVITFPKNQNAFCPLTEAPNVVDENQLEELGIKKIEKED

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Clostridium botulinum (strain Loch Maree / Type A3)
Length
593 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.842 kDa
Sequence
MGEALRGLKRTIMCGEPRENNIGQKVTVMGWVQRKRNLGGLIFVDLRDRTGIMQIVFGEEINKEAFEKSDNVKSEYCIAVTGEIVKRQSPNNDMETGAVELKGEDIKILSESETPPIYIKEGLDASENIRLKYRYLDLRRPDMQKIFMIRHKTCKVVRDFLDENGFLEMETPILTKSTPEGARDYLVPSRNYKGMFYALPQSPQIFKQLLMVSGYDKYFQITKCFRDEDLRANRQPEFTQIDMELSFIEEDDVIELNERLLAKVFKEVAGIDVKLPIERMPYKIAMEKYGSDKPDLRFGMEINDLTEAVKNSEFKVFKGAIEAGGSVRAIKAGNCATMGRKQIDKLQDFVKTYKAKGLAWIAYKEDEIKSPIAKFLTEEEMKAILEKMDAKVGDLILIVADKNNVVFESLGALRLHLAKELDIINKDEFRFVWITEFPLLSYNEEEGRYQAEHHPFTALMDEDVELLDTDPGKVRAKAYDIVLNGEELGGGSIRIHDSKLQEKMFNVLGFTKEKAWERFGFLLEAFKFGPPPHGGLAYGLDRMIMFLAGTENIKDVITFPKNQNAFCPLTEAPNVVDENQLEELGIKKIEKED

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Clostridium cellulolyticum (strain ATCC 35319 / DSM 5812 / JCM 6584 / H10)
Length
593 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.256 kDa
Sequence
MGESIHGLERSHKCTELSSSNIGEKVTVMGWVQKQRNLGSLVFIDLRDRTGIVQLVFTDKDGEMFDKAKTIRSEYVIATVGTVAARSAEAVNKKMATGEIEIIASELRILSSSETPPMYIEENSDVNEQTRLKYRFLDLRRPDMQRNLILRHRVAKVARDYYDQNGFLEIETPILIKSTPEGARDYLVPSRVHPGKFFALPQSPQLYKQLLMVSGYDRYFQIAKCFRDEDLRADRQPEFTQIDIEMSFVNVDDVLEVNEGFVKKAFKEALGVDVETPFTRMPYAEAMERFGSDKPDIRFGMELVNMSDLVANCGFKVFTDAVAMGGSVRAINAKGCAKFSRKEIDALVDLVKTYKAKGMAWISISQENEIKSSFAKFMSEDEMKAILNRAQAEAGDLICFVADKNNVVFDALGQLRLEIARKLDILNPDEFKFLWVTEFPLFEYDEEDQRWAAKHHPFTSPMDEDLQYLDTDPGRVRAKAYDMVLNGVELGGGSIRIHIQELQAKMFKMLGFTEEDANRKFGFLLEAFKYGTPPHGGMAFGLDRLVMLMAKRNSIRDVIAFPKVQNASCPMSNAPDVVDETQIEELHISIAKE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Clostridium novyi (strain NT)
Length
593 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.746 kDa
Sequence
MAESLNGLKRTVMCGELRESHIGQKHVVMGWVQRKRNLGGLVFVDLRDREGILQVVFGEEINKEAFEKADLVKPEYCIAVEGELVRRESPNEAMPTGMVELKGQNIKILSESETPPIYIKEDLDTDEAVRLKYRYLDLRRPDMQKIFKVRHKTAKVIRDFLDENGFLEMETPMLTKSTPEGARDYLVPSRNYPGMFYALPQSPQLFKQLLMVSGYDKYFQITKCFRDEDLRANRQPEFTQVDMELSFVDMEDVIALNEKLIQKVFKEVANVDVQLPIQRITYKEAMDKYGSDKPDLRFGMEINDITDAVKDVDFKVFKDAIENGGSVRAIKAPNCATMGRKQIDKLGEFVKTYKAKGLAWIAYKEDEIKSPIAKFLGEEGINKVIESLDAKVGDLILIVADKDSVVLQSLGALRLEMAKRLEILKDNKEFRFAWVTEFPLLSYNEEEDRYQAEHHPFTMPMDEDIEYLESDPGRVRAKAYDIVLNGEELGGGSIRIHDTKLQEKMFNVLGFTSESAWERFGFLLEAFKFGPPPHGGLAYGFDRMIMFLAGTENIKDVIAFPKNQNAYCPLTEAPNVVDEKQLGELGIGVQKQK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CIP 105152 / NBRC 16084 / F199)
Length
593 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.745 kDa
Sequence
MHLYRSHTCGALSRGDVGQTVRLSGWVHRKRDHGGVLFVDLRDHYGMTQIVADADSPALPILEALRVESVVTIDGEVKARSEGTVNANLSTGEIEVFARVATVLSAAEELPMPVAGEQEYPEDIRLRYRFLDLRRETLHANIVKRTKVISDMRRRMEGAGFTEYSTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMVAGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVTQEEVWETMEPVIGGVFEAFADGRKVTPIGSFPRIPYAEAMLKYGSDKPDLRNPIIISDVSEEFAQSGFGLFEKIVGTGGVVRLIPAPNTADKSRKFFDEMNDWARAEGHAGLGYVTRKQGEFGGPIAKNHGADKMAALFDRLGLGPDDGCFFAAGKAEQAAKLAGAARTRVADQLGLIDKDRFELCWIVDFPFYEWDEENKKVEFSHNPFSMPQGGLDALNTQDPLTINAFQYDLVCNGFEIASGSIRNQSPETMVKAFEIVGLSKADVEERFGGLYRAFQYGAPPHGGMAAGVDRIVMLICGAQNLREITLFPMNQRAEDLLMGAPSPAALKQLRELNIRVVEQTKG

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Clostridium botulinum (strain ATCC 19397 / Type A)
Length
593 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.808 kDa
Sequence
MGEALRGLKRTIMCGESRENNIGQKVTVMGWVQRKRNLGGLIFVDLRDRTGIMQIVFGEEINKEAFEKSDNVKSEYCIAVTGEIVKRQSPNNDMETGAVELKGEDIKILSESETPPIYIKEGLDASENIRLKYRYLDLRRPDMQKIFMIRHKTCKVVRDFLDENGFLEMETPILTKSTPEGARDYLVPSRNYKGMFYALPQSPQIFKQLLMVSGYDKYFQITKCFRDEDLRANRQPEFTQIDMELSFVEEDDVIELNERLLAKVFKEVGGIDVKLPIERMPYKIAMEKYGSDKPDLRFGMEINDLTEAVKNSEFKVFKGAIEAGGSVRAIKAENCATMGRKQIDKLQDFVKTYKAKGLAWIAYKEDEIKSPIAKFLTEEEMKAILEKMDAKAGDLILIVADKNNVVFESLGALRLHIAKELDIINKNEFRFVWITEFPLLAYNEEEGRYQAEHHPFTAIMDEDIELLGTEPGKVRAKAYDIVLNGEELGGGSIRIHDSKFQEKMFSVLGFTKEKAWERFGFLLEAFKFGPPPHGGLAYGLDRMIMFLAGTENIKDVITFPKNQNAFCPLTEAPNVVDENQLEELGIKKIEKED

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Symbiobacterium thermophilum (strain T / IAM 14863)
Length
593 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.824 kDa
Sequence
MKRTVYCGEVTDALVGQEVTVNGWVQRRRDHGSLIFVDLRDRTGLVQVVFDVEECGADLFRKAEQVRSEYVLAVRGRLVHRTPEAVNPNIPTGRFEIRALDLRILSPAKTPPFYIQDDLDVDETVRLKYRYLDLRRPEMQRNLILRHRVTKAVRDFFDEHGFLEIETPMLTKSTPEGARDYLVPSRVNPGKFYALPQSPQIFKQLCMVSGLERYVQIVRCFRDEDLRADRQPEFTQIDVEMSFVERDDVLSMMEQMVARVFRDALGVEVPTPFKRLTYAEAMARYGSDKPDLRFGMELVDVSDVAAGCGFGVFKGAVEAGGQVKGINAKGCGGYSRKQIDELTEFVKTYKAKGLAYIALGEGGEVRSSFTKFLTEAETAEIVRRLEGEPGDLLLFVADQPDVVAAALGALRVEMGNRLGLRKPGEFNLLWVIDFPLLEWDEEENRFVAVHHPFTSPHPEDLDKVFKEGATREELAAIRANAYDLVLNGVELGGGSIRIHQRPLQNRMFELLGFTPEEAQAKFGFLLEAFEYGAPPHGGIAFGLDRFVMLLAGRQSIRDVIAFPKTAKATDLMTDAPSEVAPKQLQELHIRTTV

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w)
Length
593 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.136 kDa
Sequence
MKRTTYAGLVNEQYTGQTVTLKGWVQKRRDLGQLIFIDLRDREGIVQLVFSSEFSADALKIADQLRNEYVLEITGIVKQRKEKDVNPKMKTGQIEVEVQQAKILNSAKTPPFDIEDGVSASDELKMKYRYLDLRRPEMLKGLKIRNRITQAVHSYLDEQGFLDIETPDLTKSTPEGARDYLVPSRVYPGHFYALPQSPQLFKQLLMGAGIDRYYQLARCFRDEDLRGDRQPEFTQIDLETSFLTAEEIQDITEGLIARVMKDTLDIDVKLPFDRISWKESMDRFGTDQPDVRFGMELKDISSIVADSEFKVFSGAVANGGVVKAIAVPDGANNLSRKDIDKLGKYVERFGAKGLAWLKITDDGFSGPVAKFFNAETEKQIMEQTGAQVGDLLLFAADRAKVVGDTLGYLRVELAKRFDMIDEDQFAFLWVVDWPLFDYDEGDQRWVAAHHPFTMPNEEDVHYLDEGEDPHQAHAQSYDIILNGLELGGGSIRINTRELQEKMLKALGFSLESANDQFGYLLTALDYGFPPHGGLAIGLDRFARLLVKRDNIRDVIAFPKNSKASEPMTEAPTMVSEEQLAELSLDIDVRKPED

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Geobacter bemidjiensis (strain Bem / ATCC BAA-1014 / DSM 16622)
Length
593 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.559 kDa
Sequence
MIDFLGDWKRSSYCGELRGGHIGQEVTLMGWVSKRRDHGGLIFVDLRDRDGISQIVFDPERCPEAHAKAESARNEYVLAIRGTVAARPEGTVNPKMKTGEIEVLVTECKLLNPSKALPFTLDGFVDVNENIRLKYRYLDLRTGTLQQNLMLRSKVAQLTRSYLSDNGFIELETPFLTKSTPEGARDFLVPSRINKGEFYALPQSPQLFKQILMVSGFDRYFQIVRCFRDEDLRADRQPEFTQIDCEMSFIDREDIITVMEGLMARIFTEARGVKVELPIERMTYQEAIRRFGVDNPDLRFGLELVELSDIVKNSGFKVFADVVNGGGIVKGMNVKGAGAMSRKEIDDLTEFAKIYGAKGLAYVKMTAEGWQSPIAKFFTPEEIATMDKAFDAKEGDLLLFVADKPKVVNDSLGKLRNHLAAKMGLTDPNVFRFVWITDFPLLEWDEEAKRWAAVHHPFTAPMDEDLQYVESDPGRCRAKAYDLVLNGNEIGGGSIRIHQEEVQSLMFKMLGLSEENARSKFGFLLDALEYGTPPHGGIAFGLDRLMMLITGSDSIRDVIAFPKTQKGACLMSDAPSGVDALQLRELGIRLAAK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Geobacter daltonii (strain DSM 22248 / JCM 15807 / FRC-32)
Length
593 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.5 kDa
Sequence
MIDFLGDWKRTHYCGTLTADDTGKEVVLMGWAHRRRDHGGLIFVDLRDREGLAQIVFDPDNSAEAHHKAEAIRNEYVVAVKGKVIPRPQGTVNTNLRTGAVEILVSACKILSRSKALPFTLDDYVDVAENLRLKHRYLDLRRPVLQDNLILRSKVAQVTRQYLTGNGFLELETPFLTKSTPEGARDFLVPSRINRGEFYALPQSPQLFKQILMISGFDRYFQIVRCFRDEDLRADRQPEFTQIDCEMSFIDREDIITVMEGLIARIFADVKDMSVSLPIKRMTYAESINRFGVDNPDLRFGLELVELSDIVKGSGFKVFADVVAGGGIVKGLNAKGCGGMSRKEIDDLTEFVKIYGAKGLAYVKVTEDGWQSPITKFFTGEEISAMTKTFAAEQGDLLLFVADKPKVVNDSLGKLRNQLAKILGLLDKNTFNFVWITDFPLLEWDEEEKRWAAVHHPFTAPMDEDLEYVENDPGRCRAKAYDLVLNGNEIGGGSIRIHQEKVQSLMFKMLGLSEEDAKAKFGFLLDALEYGTPPHGGIAFGLDRLIMLLTGSDSIRDVIAFPKTQKGACLMSEAPSPVDLKQLRELGLKTTGK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Geobacter sp. (strain M21)
Length
593 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.443 kDa
Sequence
MIDFLGGWKRTSYCGELRGGHIGQEVTLMGWVSKRRDHGGLIFVDLRDRDGISQIVFDPERCAEAHAKAESVRNEYVLAIKGTVAARPEGTVNPKMKTGEIEVLVTECKLLNPSKALPFTLDGFVDVNENIRLKYRYLDLRTGTLQQNLILRSKVAQLTRSYLSDNGFIELETPFLTKSTPEGARDFLVPSRINKGEFYALPQSPQLFKQILMVSGFDRYFQIVRCFRDEDLRADRQPEFTQIDCEMSFIDREDIITVMEGLMARIFTEAKGVKVELPIERMTYQEAIRRFGVDNPDLRFGLELVELSDIVKNSGFKVFADVVNGGGIVKGMNVKGAGAMSRKEIDDLTEFAKIYGAKGLAYVKMTAEGWQSPIAKFFTPEEIATMDKAFDAKEGDLLLFVADKPKVVNDSLGKLRNHLAAKMGLTDPNVFRFVWITDFPLLEWDEEAKRWAAVHHPFTAPMDEDLQYVESDPGRCRAKAYDLVLNGNEIGGGSIRIHQEEVQSLMFKMLGLSEENARSKFGFLLDALEYGTPPHGGIAFGLDRLMMLITGSDSIRDVIAFPKTQKGACLMSDAPSGVDALQLRELGIRLAAK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Geobacter uraniireducens (strain Rf4)
Length
593 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.481 kDa
Sequence
MIDFLGGWKRTHYCGALTAGDIGKEVVLMGWAHRRRDHGGLIFVDLRDREGLAQVVFDPDNSPAAHKKAEAIRNEYVVAIRGKVIPRPDGTVNANLKTGEVEVLVSECKMLNRSKALPFTLDDYVDVAENLRLKHRYLDLRRPVLQENLILRSKVAQITRQYLTGNGFLELETPFLTKSTPEGARDFLVPSRINRGEFYALPQSPQLFKQILMVSGFDRYFQVVRCFRDEDLRADRQPEFTQIDCEMSFIDREDIITVMEGLIARIFTETKGATVNLPIPRMTYAESIRRFGVDNPDLRFGLELVELSDIVKNAGFKVFADVVAGGGIVKGLNAKGCGGMSRKEIDDLTEFAKIYGAKGLAYVKMTAEGWQSPIAKFFTAEEISAMDKAFDAKEGDLLLFVADKPKVVNDSLGKLRNHLAKSLGLLDKDTFNFVWITDFPLLEWDEEEKRWAAVHHPFTAPMDEDLEYVESDPGRCRAKAYDLVLNGNEIGGGSIRIHQEKIQSLMFKMLGHSEEDARTKFGFLLDAMDYGAPPHGGIAFGLDRLIMLLTGSDSIRDVIAFPKTQKGACLMSEAPSAVDMKQLRELGLKTVVK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
Length
593 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.354 kDa
Sequence
MHAYRSHTCAALTAANVGETVRLSGWVHRVRDHGGVLFIDLRDHYGVTQVLCDGDSAAFAALEKVRSEWCIRIDGTVKARDADLVNPKLPTGEIEVYVRELEVLGRAEELPLMVFGDQEYPEETRLRYRYLDLRREAMQANMTLRSDVVASMRRRMWDKGFREYQTPIITASSPEGARDFLVPSRLHPGRFYALPQAPQQFKQLIMVSGFDKYFQIAPCFRDEDPRADRSPTDFYQLDLEMSFVTQQDVFDTIAPVLAGVFEEFGGGRKVDAPQDWPQIAYADAAKWYGTDKPDLRNPIKMQDCSEHFRGSGFAIFAKLLEQEGTEIRAIPAPTGGSRKFCDRMNAFAQKEGLPGMGYIFWRDQGEGLEAAGPLAKNIGPERTEAIRQQLGLGVGDAAFFLGGKPKSFEKVAGKARDVIGAELGLTETDRFAFAWIVDFPIYERDEETGEIDFEHNPFSMPQGGMEALNGDPMAVRGYQYDLACNGYELVSGAIRNHKPEIMLKAFELAGYGADEVKARFGALFNAFHYGAPPHGGCAAGIDRIVMLLADEANIREVMMFPMNQRAEDLMMQAPSEPSSDQLMELGLRVILQD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.646 kDa
Sequence
MMRTHYCGSLTEAQIDQTVTLCGWVHRRRDHGGVIFLDMRDRDGLVQVVIDPDTPEAFATADKVRSEFVLKITGRVRRRYEGTENSNMVSGQIEVLGKEIEVLAQSETPPFPLNDDNINISEEHRLKYRFLDIRRPEMLDRLRFRSKVTNLIRNYLDDHGFLDVETPILTRATPEGARDYLVPSRVQNGSFYALPQSPQLFKQLLMVGGIDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLNDDDIMDLMEGMTVKLFDELLGIKFDKFQRMPYSEAMRDYASDKPDLRIPLKLVDVADLMQDVEFKVFAGPAKDPKGRIAALRVPGAGALPRSAIDEYTKFVGIYGAKGLAYIKVNEIEKGVEGLQSPIVKFIEPIVMQLLERVGAENGDIVFFGADKAKVVNDAMGALRVKIGHDLKLVTCEWAPLWVVDFPMFEETDDGKWTSVHHPFTLPKSSVEDVKANPGEALSVAYDMVLNGTEVGGGSLRIYTLEMQKAIFEALGISDEEAEEKFSFLLNALRYGAPPHGGLAFGLDRLIMLMTGASSIRDVIAFPKTKTAECPLTQAPAPVEANQLRDLGIRLREQPKKED

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Acinetobacter baumannii (strain AB307-0294)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.667 kDa
Sequence
MMRTHYCGSLTEAQIDQTVTLCGWVHRRRDHGGVIFLDMRDRDGLVQVVIDPDTPEAFATADKARSEYVLKITGRVRRRYEGTENPNMVSGQIEVLGKEIEVLAASETPPFPLNDDTINVSEEHRLKYRFLDIRRPEMLERLRFRSKVTNLIRNYLDDHGFLDVETPILTRATPEGARDYLVPSRVQNGSFYALPQSPQLFKQLLMVGGIDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLNDDDIMDLMEGMTVKLFNDLLGVKFEKFRRMPYSEAMRDYASDKPDLRIPLKLVDVADLMQEVEFKVFAGPAKDPKGRIAALRVPGAGSLTRSQIDEYTKFVGIYGAKGLAYIKVNEIEKGIEGLQSPIVKFIEPIVMQLLERVGAENGDIVFFGADKAKIVNDAMGALRVKIGHDLNLATCEWAPLWVVDFPMFEETDDGKWTSVHHPFTLPKSSVEDVKSNPGEALSVAYDMVLNGTEVGGGSLRIYTLEMQKAIFEALGISDEEAEEKFSFLLNALRYGAPPHGGLAFGLDRLVMLMTGATSIRDVIAFPKTKTAECPLTQAPAPVEANQLRDLGIRLREQQKKEA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Acinetobacter baumannii (strain AB0057)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.667 kDa
Sequence
MMRTHYCGSLTEAQIDQTVTLCGWVHRRRDHGGVIFLDMRDRDGLVQVVIDPDTPEAFATADKARSEYVLKITGRVRRRYEGTENPNMVSGQIEVLGKEIEVLAASETPPFPLNDDTINVSEEHRLKYRFLDIRRPEMLERLRFRSKVTNLIRNYLDDHGFLDVETPILTRATPEGARDYLVPSRVQNGSFYALPQSPQLFKQLLMVGGIDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLNDDDIMDLMEGMTVKLFNDLLGVKFEKFRRMPYSEAMRDYASDKPDLRIPLKLVDVADLMQEVEFKVFAGPAKDPKGRIAALRVPGAGSLTRSQIDEYTKFVGIYGAKGLAYIKVNEIEKGIEGLQSPIVKFIEPIVMQLLERVGAENGDIVFFGADKAKIVNDAMGALRVKIGHDLNLATCEWAPLWVVDFPMFEETDDGKWTSVHHPFTLPKSSVEDVKSNPGEALSVAYDMVLNGTEVGGGSLRIYTLEMQKAIFEALGISDEEAEEKFSFLLNALRYGAPPHGGLAFGLDRLVMLMTGATSIRDVIAFPKTKTAECPLTQAPAPVEANQLRDLGIRLREQQKKEA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Acinetobacter baumannii (strain ACICU)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.667 kDa
Sequence
MMRTHYCGSLTEAQIDQTVTLCGWVHRRRDHGGVIFLDMRDRDGLVQVVIDPDTPEAFATADKARSEYVLKITGRVRRRYEGTENPNMVSGQIEVLGKEIEVLAASETPPFPLNDDTINVSEEHRLKYRFLDIRRPEMLERLRFRSKVTNLIRNYLDDHGFLDVETPILTRATPEGARDYLVPSRVQNGSFYALPQSPQLFKQLLMVGGIDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLNDDDIMDLMEGMTVKLFNDLLGVKFEKFRRMPYSEAMRDYASDKPDLRIPLKLVDVADLMQEVEFKVFAGPAKDPKGRIAALRVPGAGSLTRSQIDEYTKFVGIYGAKGLAYIKVNEIEKGIEGLQSPIVKFIEPIVMQLLERVGAENGDIVFFGADKAKIVNDAMGALRVKIGHDLNLATCEWAPLWVVDFPMFEETDDGKWTSVHHPFTLPKSSVEDVKSNPGEALSVAYDMVLNGTEVGGGSLRIYTLEMQKAIFEALGISDEEAEEKFSFLLNALRYGAPPHGGLAFGLDRLVMLMTGATSIRDVIAFPKTKTAECPLTQAPAPVEANQLRDLGIRLREQQKKEA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Dictyoglomus turgidum (strain Z-1310 / DSM 6724)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.344 kDa
Sequence
MRRTHYCGELNAKNIGEKVYLSGWVHRIRHHGGLIFIDLRDRSGIVQLVFDPSISKESYDIADTVGNEWVISVEGKVRKRPEGMENPKIPTGEIEIEVEKIKIENTAKPLPFNLWTNKEIDEIVRLKYRYLDLRRDKMQSNIIFRHNFILSIRNFLAKNGFIEIETPYLIVSTPEGARDFIIPSRLQPGKFYALPQSPQLFKQILMVAGFDRYFQIARCFRDEDLRADRQPEFTQLDMEMSFIEVEDVFTIIEELFKTVLKEVMNIEINTPFPRLSYEDAMNTYGSDKPDLRYDLKIVDVTNILKDLPLEFIRSTIEKDGVIKGIVLKNIVPSRREWSIIENKVRELKGKGIMWFTYADGELKSSISKYLDENIKDKLIKNLNLKSGDSFFCIAGTWKDVVKILGILRLEVAELFNMEKKEGLFFLWITDFPLFEYDEEERRIVAEHHPFTSPKDEDIPLLDTNPLKVKAKCYDLVLNGTELGSGSIRIHKKEIQEKVFNILGITPEDAKKKFGFLLEAFEYGAPPHGGIALGIDRIIAILTNSNSLREVIAFPKTQSGTCLLTGAPSEVDPKQLEEVHIKVVYPEEKKEED

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Psychromonas ingrahamii (strain 37)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.992 kDa
Sequence
MRTMYCGEVTEAVLGQEIQLVGWINKQRDLGGVIFLDMRDRAGIVQVFFDADTPIATALATTVRNEFCIQIKGLVRARPEGQVNKDMTTGGIEILGLELEILNRSEPLPLDSNQQNSEEQRLRYRYLDLRRPEMAKRMQFRAKVSSFVRRFLDDQDFLDVETPILTKATPEGARDYLVPSRTHKGKFFALPQSPQLFKQLLMMSGMDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMNADQVMEISEEMIVKLFKEMLNVDLGNFPKMTYAEALRRFGSDKPDLRIDFELYDVADLMKDVEFNVFSGPANDPDSRVAVICVPGGAKLSRKNIDEYGKFVTIYGAKGLAWMKVNEVAKGLEGVQSPVAKFLNEEIVTELLIRTGAKDGDIILFGADKSNIVSEAIGALRLKVAQDLGLVKDQWKPLWVIDFPMFEPLDDGGLTPLHHPFTAPIGLTVEELEANPVGAISNAYDMVLNGCELGGGSVRIHKQDMQAAIFRILKISDEEAEDKFGFLLEALKYGAPPHAGLAFGLDRLVMLMTGTSSIRDVIAFPKTASAACPLTNAPSFANPAVLAELNVAVVADPKKVISE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Acinetobacter baumannii (strain SDF)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.623 kDa
Sequence
MMRTHYCGSLTEAQIDQTVTLCGWVHRRRDHGGVIFLDMRDRDGLVQVVIDPDTPEAFATADKARSEYVLKITGRVRRRYEGTENPNMVSGQIEVLGKEIEVLAASETPPFPLNDDTINVSEEHRLKYRFLDIRRPEMLDRLRFRSKVTNLIRNYLDDHGFLDVETPILTRATPEGARDYLVPSRVQNGSFYALPQSPQLFKQLLMVGGIDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLNDDDIMDLMEGMTVKLFNDLLGVKFEKFRRMPYSEAMRDYASDKPDLRIPLKLVDVADLMQEVEFKVFAGPAKDPKGRIAALRVPGAGSLTRSQIDEYTKFVGIYGAKGLAYIKVNEIEKGIEGLQSPIVKFIEPIVMQLLERVGAENGDIVFFGADKAKIVNDAMGALRVKIGHDLNLATCEWAPLWVVDFPMFEEADDGKWTSVHHPFTLPKSSVEDVKSNPGEALSVAYDMVLNGTEVGGGSLRIYTLEMQKAIFEALGISDEEAEEKFSFLLNALRYGAPPHGGLAFGLDRLVMLMTGATSIRDVIAFPKTKTAECPLTQAPAPVEANQLRDLGIRLREQQKKEA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.681 kDa
Sequence
MMRTHYCGSLTEAQIDQTVTLCGWVHRRRDHGGVIFLDMRDRDGLVQVVIDPDTPEAFATADKARSEYVLKITGRVRRRYEGTENPNMVSGQIEVLGKEIEVLAASETPPFPLNDDTINVSEEHRLKYRFLDIRRPEMLERLRFRSKVTNLIRNYLDDHGFLDVETPILTRATPEGARDYLVPSRVQNGSFYALPQSPQLFKQLLMVGGIDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLNDDDIMDLMEGMTIKLFNDLLGVKFEKFRRMPYSEAMRDYASDKPDLRIPLKLVDVADLMQEVEFKVFAGPAKDPKGRIAALRVPGAGSLTRSQIDEYTKFVGIYGAKGLAYIKVNEIEKGIEGLQSPIVKFIEPIVMQLLERVGAENGDIVFFGADKAKIVNDAMGALRVKIGHDLNLATCEWAPLWVVDFPMFEETDDGKWTSVHHPFTLPKSSVEDVKSNPGEALSVAYDMVLNGTEVGGGSLRIYTLEMQKAIFEALGISDEEAEEKFSFLLNALRYGAPPHGGLAFGLDRLVMLMTGATSIRDVIAFPKTKTAECPLTQAPAPVEANQLRDLGIRLREQQKKEA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Acinetobacter baumannii (strain AYE)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.667 kDa
Sequence
MMRTHYCGSLTEAQIDQTVTLCGWVHRRRDHGGVIFLDMRDRDGLVQVVIDPDTPEAFATADKARSEYVLKITGRVRRRYEGTENPNMVSGQIEVLGKEIEVLAASETPPFPLNDDTINVSEEHRLKYRFLDIRRPEMLERLRFRSKVTNLIRNYLDDHGFLDVETPILTRATPEGARDYLVPSRVQNGSFYALPQSPQLFKQLLMVGGIDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLNDDDIMDLMEGMTVKLFNDLLGVKFEKFRRMPYSEAMRDYASDKPDLRIPLKLVDVADLMQEVEFKVFAGPAKDPKGRIAALRVPGAGSLTRSQIDEYTKFVGIYGAKGLAYIKVNEIEKGIEGLQSPIVKFIEPIVMQLLERVGAENGDIVFFGADKAKIVNDAMGALRVKIGHDLNLATCEWAPLWVVDFPMFEETDDGKWTSVHHPFTLPKSSVEDVKSNPGEALSVAYDMVLNGTEVGGGSLRIYTLEMQKAIFEALGISDEEAEEKFSFLLNALRYGAPPHGGLAFGLDRLVMLMTGATSIRDVIAFPKTKTAECPLTQAPAPVEANQLRDLGIRLREQQKKEA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Acidothermus cellulolyticus (strain ATCC 43068 / 11B)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.481 kDa
Sequence
MIRTHEAGTLRPADAGSRVVLAGWVARRRDLGGVVFLDLRDASGIVQVVAREGVAGQVASRVRAEFCLRVAGEVRLRPAGNENPELETGDVEVVADEIEVLSEAAPLPFPVTGPVEVNEETRLKYRYLDLRRPGPARALRLRSEMNRLAREVMARHRFVEVETPYLTRSTPEGARDFLVPARLQPGHWYALPQSPQLFKQLLMVAGLERYYQLARCFRDEDFRADRQPEFTQLDIEMSFVTEDDVMALAEDVIATLWSQLAGVELALPLPRLTYAEAMRRFGSDKPDLRFGQEIVDLTKFFAGTSLRIFQAPYVGAVVMPGGAGQSRSELDEWTTFARSRGAKGLAYVLVGAELTGPIAKNLSDAERAGLPAATGARPGDAIFFAAGEQRASQELLGAVRLEIARRCRLTDPASGAPAWSLCWIVDPPLFEPDGAGGWTSVHHPFTAPKPEWMDRFADKPGEALAAAYDIVANGNEIGGGSIRIHRADVQQRVFEVLGISEAEANAKFGFLLEAFRYGPPPHGGIAFGWDRIAALLAGVESIRDVIAFPKTASGTDPLTGAPTPITPEQRKEAGIDADPYAAAGRPPGRQSA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.792 kDa
Sequence
MRTHYCGHVSETDLDQEVTLCGWAHRRRDHGGVIFIDLRDREGLVQVVFDPDRPETFALAERVRSEFVLKVRGRVRRRPAGTENPDLPTGQVEVLGLELDLLNPAKTPPFQLDEHEQAGEDVRLRYRYVDLRRPEMLQRLRARARITSNLRRFLDEHGFLDIETPMLTRATPEGARDYLVPSRTHPGSFFALPQSPQLFKQLLMMAGMDRYYQIVRCFRDEDLRADRQPEFTQLDIETSFMDEEGIMHLTERMMRRLFADVLQVDLPDPFPRMGYAEAMARFGSDKPDLRIPLELVEVADLMGGVEFKVFAGPAADPRGRVAALHVPGGAGLTRKQIDDYTQFVGRYGAKGLAYIKVNDPAQGREGLQSPILKFLTDEAVDGILRRTEARAGDLIFFGADKAKVVNDALGALRVKLGHDLAMVEDEWRPLWVVDFPMFEYDEKDGRLYALHHPFTAPNVDDPAELADKDPEQLVSRAYDMVLNGTELGGGSVRIHRQDMQQAVFRLLGIDEDEARAKFGFLLDALEYGAPPHGGIAFGLDRLVMLMTGASSIREVMAFPKTQTAACLLTDAPAEVDIAQLQELALRITKPQA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Anaplasma marginale (strain Florida)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.012 kDa
Sequence
MNIYRTHVCNELGVAHVGNEVALSGWVYRKRDHGGLLFVDLRDFYGITQLIFNESENPELFNRMATIGLESVITVRGIVAERSEDNVNASIETGHVEVKVSTLTVVSEAAPLPLHVPTSFSYPEDIRLQHRFLDLRCDKVKNSILLRSMVVSELRRAMEALGFIEVHTPILTSSSPEGARDYIVPSRTHAGKFYALPQAPQIFKQLLMVGGFDKYFQIAPCFRDEDSRADRSPGEFYQLDMEMSFVTQEDVFAAIEPVLYGLFAKFAGADKKVDRQFPRITYRDSMIRYGSDKPDLRNPLVISDVTEIFRNSGFRTFQAGVEAGEVVRAIPAPNTSGKPRSFFDDKIERAKEFGARGLGYVTYEADGTAKGPIAKFLSEDELARIRSAAGVGNGDSVFFMSDTADKAADFAGKIRELLGLELGLIEHDTFKFCWIVDFPYFKCEDGELDFCHNPFSMPQGEMEALEQQNPLDIIAYQYDIVCNGIEISSGAIRNHRLDVMYKAFSMVGYDEQTVNSKFGALVRAFKFGAPPHGGLAPGIDRIVMLLADAPNIREVICFPLNQTGEDLLMGAPSEVSPAHLQELSIALNIKRK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Thermoanaerobacter pseudethanolicus (strain ATCC 33223 / 39E)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.874 kDa
Sequence
MGEQLNGLKRTHMCGELTVEDVDKSVVVMGWVQRRRDHGGLVFIDLRDRTGIVQVVFSNEVSSEAFEKVQSVRSEYVLAIEGKVVKRAPENVNPKISTGEIEIYANTLKILSKSETPPFPIEDRSNVSEAIRLKYRYLDLRRPSMQQNLMTRFKITKVVRDFLNRNGFIEIETPLLIKSTPEGARDYLVPSRIYPGKFYALPQSPQIFKQLLMISGFDKYYQIAKCLRDEDLRADRQPEFTQIDIEMSFVEVEDVLKINEKMIAEIFKETLGIDVPIPFKRLSYQESMERFGTDKPDLRFGMELKDLSDIVAQSEFNVFKTALKNNGSVRGINVKGAASMPRRQLDELVEFAKTYGAKGLLWIQVFEKEVKSPATKFLSEEEMKKILERLEAEAGDLLLIVADKDEIVFDTLAHLRLELGKRFNLIDENKYEFVWIVDFPLLEYDEGEKRYVAKHHPFTAPKDEDIELLEKEPLKVRAKAYDIVLNGTEIGGGSIRIHDTELQKRMFKVLGFSEEKAWERFGFLMEAFKYGAPPHGGIAYGLDRLAMIITGSDTIRDVIAFPKTQNAVCLMTDAPSEVSEEQLKELHIKVDL

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Thermoanaerobacter sp. (strain X514)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.924 kDa
Sequence
MGEQLNGLKRTHMCGELTVEDVDKYVVVMGWVQRRRDHGGLVFIDLRDRTGIVQVVFSNEVSSEAFEKVQSVRSEYVLAIEGKVVKRSPENVNPKISTGEIEIYANTLKILSKSETPPFPIEDRSNVSEAVRLKYRYLDLRRPSMQKNLMTRFKITKVVRDFLNKNGFIEIETPLLIKSTPEGARDYLVPSRIYPGKFYALPQSPQIFKQLLMISGFDKYYQIAKCLRDEDLRADRQPEFTQIDIEMSFVEVEDVLKINEKMIAEIFKETLGIDVPIPFKRLSYQESMERFGTDKPDLRFGMELKDLSDIVAQSEFNVFKTALKNNGSVRGINVKGAASMPRRQLDELVEFAKTYGAKGLLWIQVFEKEVKSPATKFLSEEEMKKILERLEAEAGDLLLIVADKDEIVFDTLAHLRLELGKRFNLIDENKYEFVWIVDFPLLEYDEGEKRYVAKHHPFTAPKDEDIELLEKEPLKVRAKAYDIVLNGTEIGGGSIRIHDTELQKRMFKVLGFSEEKAWERFGFLMEAFKYGAPPHGGIAYGLDRLAMIITGSDTIRDVIAFPKTQNAVCLMTDAPSEVSEEQLKELHIKVDL

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Thioalkalivibrio sulfidiphilus (strain HL-EbGR7)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.68 kDa
Sequence
MRSHYCGSVNESHLDQEVTLCGWVNRRRDHGGVIFIDLRDREGLVQVVFDPDLPEVFATAERVRSEYVLKVKGRVRRRPAGTENPDLPTGAIEVLGRELTVLNSAETPPFQLDEDEVNEETRLRYRYVDLRRPAMQKRLQMRARVSRTLRRFLEDNGFLDIETPMLTKATPEGARDYIVPSRTHPGSFFALPQSPQLFKQLLMMGGMDRYYQIVRCFRDEDLRADRQPEFTQLDIETSFMDEEGIMGLMEEMVRELFAQVLEVPLHTPFQRMSYAEAMARYGSDKPDLRIPLELTELTDIMGEVDFKVFSGPARDPAGRVAALRVPKGGELSRKDIDDYTHFVGRYGAKGLAYIKVNDLNAGREGLQSPILKFMPDTVVVEILGRTGAEDGDLIFFGADKARIVNEALGALRVKLGHDLGLVERGWRPLWVVDFPMFEHDEKEGRWVALHHPFTAPRVERPEELTGNPGEMISRAYDMVLNGTEVGGGSVRIHTTAMQQAVFNLLGIGEAEARDKFGFLLDALKYGCPPHGGIAFGLDRLVMLMTGSQSIRDVMAFPKTQTAHCPLTDAPAEVSDAQLKELSIRVKKQTASG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bacillus subtilis (strain 168)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.975 kDa
Sequence
MFGRTYYCGDITEKAIGESVTLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPDVSKEALAIAEGIRNEYVLDIQGKVVAREEGTVNPNLKTGAIEIHADGVNVLNAAKTPPFAISDQAEEVSEDVRLKHRYLDLRRPAMFQTMQLRHNVTKAVRSFLDENGFLDIETPILTGSTPEGARDYLVPSRVHEGEFYALPQSPQLFKQLLMVSGIERYYQIARCFRDEDLRADRQPEFTQIDIEMSFMSQEDIMSLAEEMMAKVMRETKGEELQLPLPRMTYDEAMNKYGSDKPDTRFDMLLTDVSDIVKDTEFKVFSSAVANGGVVKAINVKGGAGDYSRKDIDALGAFAANYGAKGLAWVKVEADGVKGPIAKFFDEEKQSKLIEALDAAEGDLLLFGADQFEVVAASLGALRLKLGKERGLIDEKLFNFLWVIDWPLLEHDPEEGRFYAAHHPFTMPVREDLELIETAPEDMKAQAYDLVLNGYELGGGSIRIFEKDIQEKMFALLGFSPEEAAEQFGFLLEAFEYGAPPHGGIALGLDRLVMLLAGRTNLRDTIAFPKTASASCLMTEAPGEVSDAQLDELHLSIKKKVKN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / FZB42)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.058 kDa
Sequence
MFGRTYYCGEITEKAIGETVKLKGWVQKRRDLGGLIFIDLRDRSGIVQVVFNPDVSKEALAAAEAIRNEYVLDIEGTVSAREEGTVNPNLKTGKIEIKAEAVTVLSTAKTPPFPISDQAADVSEDVRLKHRYLDLRRPAMFQTLQMRHQVTKSIRHFLDENGFLDIETPILTKSSPEGARDYLVPSRVHEGEFYALPQSPQIFKQLLMVSGFERYYQVARCFRDEDLRADRQPEFTQIDIEMSFMSQEDIMALAEEMMAKVMLETKGVEVPLPLPRMTYEEAMNSYGSDKPDTRFGMLLTDVSDIVKDTEFKVFSSAVANGGVVKAINVKGAAGDYSRKDIDALGVFAGNYGAKGLAWVKVEADGVKGPIAKFFDEEKQAKLAEALEASEGDLLLFGADKFEVVAQSLGALRLKLGKERGLIDESLFNFLWVVDWPLLEHDEEEGRFYAAHHPFTMPVREDLDLIETAPEDMKAQAYDLVLNGYELGGGSIRIFEKDVQEKMFGLLGFTKEEAEEEFGYLLEAFEYGAPPHGGIALGLDRLVMLLAGRTNLRDTIAFPKTASASCLLTEAPGEVSDAQLEELHLSVKRKVKQ

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rhodopirellula baltica (strain DSM 10527 / NCIMB 13988 / SH1)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.228 kDa
Sequence
MLRTHTCGALRKSDVGSPVTLCGWVDSKRDHGGAVFIDLRDRYGLTQVVIGPPEANEALIKQAGHVPNESVILIRGVVADRLEGKTNAKLETGEIEVRSEHFEILSASETPPFTPGQSDLPGEDLRLKYRFLDLRRKEMQQALIRRSEIIKCMRDYFAEHDFIDVETPILGRSTPEGARDYLVPSRVHPSNFYALPQSPQLYKQILMVAGFDRYVQVAKCFRDEDLRADRQPEFTQLDLEMSFVDSEDIIGLIDGLVAKTAKQVLGKDITLPLPRMTYEEAMRRFGSDAPDLRFGLEIVDVTSVAAKTDFRVFRGTADAGNFVRGINVKDSALKFSRRQIDELTAFVQQDFGAKGLAWFRVEDDGTLWSPIAKNFDEEHLAEIKALMGGEPGDLLMFLADTWEVTCKGLSGLRKRLAVELKLYEDGELNCSWVTEFPMFEKDEEAGRYVAMHHPFTAPLEEDLPLLKESPEKCRAQAYDLVINGSEAGGGTIRIHDSKVQSQVFELLGMDEETARDRFGFLLDALRFGAPPHGGIALGVDRWVMLFAGLENIREVIAFPKTQKAADMMTGAPGEVDADQLNELHLRTVSAKT

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shewanella baltica (strain OS223)
Length
592 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.988 kDa
Sequence
MRSHYCGDVNKSHVGQEVTLVGWVNRSRDLGGVVFLDLRDREGLIQVVYDPDLPEVFNVASTLRAEFCVQVKGLVRARPDSQVNGQMKTGEIEVLGQALTIINAADPLPLSMDNYQNNSEEQRLKYRYLDLRRPEMAQRLIFRAKVTSSVRRFLDSNGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMSSEQVMAKTEEMMRGLFLEMLNVDLGEFPRMTYNEAMRRFGSDKPDLRNPLELVDIADLLKEVEFAVFSGPANDEEGRVAALRIPGGAALSRKQIDDYTKFVGIYGAKGLAWMKINDLSLGLEGIQSPVLKFLNESIVNEIVSRTGAQTGDIILFGADQATVVAESMGALRLKAGEDFNLLQGEWRPLWVVDFPMFEKINGNFHAVHHPFTAPRGVTAAELEANPANRVSDAYDMVLNGCELGGGSVRIHNQEMQSAVFRILGITDEEAKEKFGFLLEALRYGTPPHAGLAFGLDRIIMLMTGASSIRDVMAFPKTTTAACPLTNAPGFANPQQLAELGIAVVEKAVKTED

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shewanella baltica (strain OS155 / ATCC BAA-1091)
Length
592 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.947 kDa
Sequence
MRSHYCGDVNKSHVGQEVTLVGWVNRSRDLGGVVFLDLRDREGLIQVVYDPDLPEVFNVASTLRAEFCVQVKGLVRARPDSQVNGQMKTGEIEVLGQALTIINAADPLPLSMDNYQNNSEEQRLKYRYLDLRRPEMAQRLIFRAKVTSSVRRFLDSNGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMSSEQVMAKTEEMMRGLFLEMLNVDLGEFPRMTYNEAMRRFGSDKPDLRNPLELVDIADLLKEVEFAVFSGPANDEEGRVAALRIPGGAALSRKQIDDYTKFVGIYGAKGLAWMKINDLSLGLEGIQSPVLKFLNDSIVNEIVSRTGAQTGDIILFGADQATVVAESMGALRLKAGEDFSLLQGEWRPLWVVDFPMFEKINGNFHAVHHPFTAPRGVTAAELEANPANRVSDAYDMVLNGCELGGGSVRIHNQEMQSAVFRILGITDEEAKEKFGFLLEALRYGTPPHAGLAFGLDRIIMLMTGASSIRDVMAFPKTTTAACPLTNAPGFANPQQLAELGIAVVEKAVKTED

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shewanella baltica (strain OS185)
Length
592 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.988 kDa
Sequence
MRSHYCGDVNKSHVGQEVTLVGWVNRSRDLGGVVFLDLRDREGLIQVVYDPDLPEVFNVASTLRAEFCVQVKGLVRARPDSQVNGQMKTGEIEVLGQALTIINAADPLPLSMDNYQNNSEEQRLKYRYLDLRRPEMAQRLIFRAKVTSSVRRFLDSNGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMSSEQVMAKTEEMMRGLFLEMLNVDLGEFPRMTYNEAMRRFGSDKPDLRNPLELVDIADLLKEVEFAVFSGPANDEEGRVAALRIPGGAALSRKQIDDYTKFVGIYGAKGLAWMKINDLSLGLEGIQSPVLKFLNESIVNEIVSRTGAQTGDIILFGADQATVVAESMGALRLKAGEDFNLLQGEWRPLWVVDFPMFEKINGNFHAVHHPFTAPRGVTAAELEANPANRVSDAYDMVLNGCELGGGSVRIHNQEMQSAVFRILGITDEEAKEKFGFLLEALRYGTPPHAGLAFGLDRIIMLMTGASSIRDVMAFPKTTTAACPLTNAPGFANPQQLAELGIAVVEKAVKTED

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM 11007 / NBRC 100824 / MB4)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.864 kDa
Sequence
MGEQLGGLKRTHMCGELGVKDVGKSVVVMGWVNSRRDHGGLVFIDLRDRTGIVQIVFSEQVSKEVFEKVQSVRSEYVLAVEGEVVKRLPENVNPKIPTGEIEIYAKNLKILSKSETPPFPIEDRSNVSEAVRLKYRYLDLRRPSMQRNLITRFKLTQAVREFLNDNGFIEIETPMLIKSTPEGARDYLVPSRIYPGKFYALPQSPQIFKQLLMIAGFDRYYQIARCLRDEDLRADRQPEFTQIDIEMSFVEVEDVLDINERMIKHVFKKVLDVDLDIPFRRLTYQEAMERFGTDKPDLRFGMELKDLSDILRESEFNVFKNALKNGGSIRGINVKGAASMTRKQLDELVEFAKNFGAKGLLWMQVLEGEVKSPATKFLTEGELNKILERLEAEVGDLLLIVADKDEVVFDTLGHLRVEMAKRFNLIDESKYEFVWVVDFPLLEYDEEEKRYVAKHHPFTSPKDEDIDLLEKEPLKVRAKAYDIVLNGTEIGGGSIRIHDTELQKRMFKVLGFSEEEAWKKFGFLMEAFKYGAPPHGGIAYGLDRLAMIMTGSDTIRDVIAFPKTQNAVCLMSDAPSEVSEKQLKELHIKIDL

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Carboxydothermus hydrogenoformans (strain ATCC BAA-161 / DSM 6008 / Z-2901)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.744 kDa
Sequence
MLKRSHYCGELRKEHAGQKVILNGWVQRRRDHGGLIFVDLRDRSGIVQVVFSPDVDLEAFRVAEAVRNEYVLAIEGTVRLRPEGTENPNLLTGEVEVYASKVEVLNKAKTPPFYIEDGIDVDEQVRLRYRYLDLRRPEMQRALELRHKAAKAVRDFLDRHGFWEIETPMLTKSTPEGARDFLVPSRLNPGKFYALPQSPQIFKQILMVAGMERYFQIVRCFRDEDLRADRQPEFTQIDIEMSFIDREDIMSLMEEMIAYVFKEAIGVEVKTPFKRISYQEAMLKYGTDKPDLRFGLEITDVTELVKDVEFKVFQTVAHAGGVIRGLNAKGCAGFSRKDLDDLTKFVGNFGAKGLAYLILTPEEVKSPIAKFFKEEELRALINALQGEPGDILFFVADKPEVAAQALGNLRLHLAERLGLIPENEFNFLWVIDFPLLEYDNEEKRFVAMHHPFTAPMDEDLPLMDENPLLVRAKAYDMVLNGVEIGGGSIRIHRRDIQEKMFKLIGLSEEEAKEKFGFMLEAFEYGTPPHGGIAFGFDRLVMLMAGRESIRDVIAFPKTQSATDLMVGAPNVVERRQLKELHIKVDLPVKEQQ

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shewanella baltica (strain OS195)
Length
592 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.002 kDa
Sequence
MRSHYCGDVNKSHVGQEVTLVGWVNRSRDLGGVVFLDLRDREGLIQVVYDPDLPEVFNVASTLRAEFCVQVKGLVRARPDSQVNGQMKTGEIEVLGQALTIINAADPLPLSMDNYQNNSEEQRLKYRYLDLRRPEMAQRLIFRAKVTSSVRRFLDSNGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMSSEQVMAKTEEMMRGLFLEMLNVDLGEFPRMTYNEAMRRFGSDKPDLRNPLELVDIADLLKEVEFAVFSGPANDEEGRVAALRIPGGAALSRKQIDDYTKFVGIYGAKGLAWMKINDLSLGLEGIQSPVLKFLNESIVNEIVSRTAAQTGDIILFGADQATVVAESMGALRLKAGEDFNLLQGEWRPLWVVDFPMFEKINGNFHAVHHPFTAPRGVTAAELEANPANRVSDAYDMVLNGCELGGGSVRIHNQEMQSAVFRILGITDEEAKEKFGFLLEALRYGTPPHAGLAFGLDRIIMLMTGASSIRDVMAFPKTTTAACPLTNAPGFANPQQLAELGIAVVEKAVKTED

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shewanella loihica (strain ATCC BAA-1088 / PV-4)
Length
592 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.939 kDa
Sequence
MRSHYCGDVNRSHVGEEVTLVGWVNRSRDLGGVVFLDLRDREGVIQVVYDPDLPEVFDVASTLRSEFCVQVKGLVRARPDSQINDQMRTGEIEVLGKALTILNSAPALPINMDKNQHNTEEQRLKYRYLDLRRPEMAERIIFRSKVTSAVRRFLDGNGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTSAQVMDKTEEMVRGLFKELLNVDLGEFPKMTFAEAMRRYGSDKPDLRNPLELVDVADLVKDVDFKVFQEPANDSEGRVAVLCVPGGASLSRKQLDEYGKYVNIYGAKGLAWMKVNELENGLEGIQSPVLKFLSEEVVKGILERTGAANGDLILFGADKANIVAEAMGALRLKVGEDFDLLQGDWKPLWVVDFPMFERTSDGGLHAMHHPFTAPSGITPAELEADPTAAISDAYDMVLNGCELGGGSVRIYDAEMQSAVFRILGINDEEAQEKFGFLLEALKYGTPPHAGLAFGLDRMVMLMTGASSIRDVMAFPKTTTAACPLTNAPGFANPVQLEELGVSVVEAKKEQE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shewanella putrefaciens (strain CN-32 / ATCC BAA-453)
Length
592 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.872 kDa
Sequence
MRSHYCGDVNKSHVGQEVTLVGWVNRSRDLGGVVFLDLRDREGLVQVVYDPDLPEVFAVASTLRAEFCVQVKGVVRARPDSQVNGQMKTGEIEVLGKALTIINAADPLPLSLDNYQNNSEEQRLKYRYLDLRRPEMAQRLMFRAKVTSAVRRFLDSNGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTSEQVMAKTEEMMRGLFLEMLNVDLGEFPRMTYNEAMRRFGSDKPDLRNPLELVDIADLLKEVEFAVFSAPANDEEGRVAVLRIPGGAALSRKQIDDYTKFVGIYGAKGLAWMKINDLSLGLEGIQSPVLKFLNESIVNEIISRTGAQTGDIILFGADQATVVAESMGALRLKAGEDFSLLQGEWRPLWVVDFPMFEKINGNFHAVHHPFTAPRGVTAAELEANPANRVSDAYDMVLNGCELGGGSVRIHNQEMQSAVFRILGITDDEAKEKFGFLLEALRYGTPPHAGLAFGLDRIIMLMTGASSIRDVMAFPKTTTAACPLTNAPGFANPQQLAELGIAVVEKAVKTEG

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shewanella sp. (strain W3-18-1)
Length
592 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.857 kDa
Sequence
MRSHYCGDVNKSHVGQEVTLVGWVNRSRDLGGVVFLDLRDREGLVQVVYDPDLPEVFAVASTLRAEFCVQVKGVVRARPDSQVNGQMKTGEIEVLGKALTIINAADPLPLSLDNYQNNSEEQRLKYRYLDLRRPEMAQRLMFRAKVTSAVRRFLDSNGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTSEQVMAKTEEMMRGLFLEMLNVDLGEFPRMTYNEAMRRFGSDKPDLRNPLELVDIADLLKEVEFAVFSAPANDEEGRVAALRIPGGAALSRKQIDDYTKFVGIYGAKGLAWMKINDLNLGLEGIQSPVLKFLNESIVNEIVSRTGAQTGDIILFGADQATVVAESMGALRLKAGEDFSLLQGEWRPLWVVDFPMFEKINGNFHAVHHPFTAPRGVTAAELEANPANRVSDAYDMVLNGCELGGGSVRIHNQEMQSAVFRILGITDDEAKEKFGFLLEALRYGTPPHAGLAFGLDRIIMLMTGASSIRDVMAFPKTTTAACPLTNAPGFANPQQLAELGIAVVEKAVKTEG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Anoxybacillus flavithermus (strain DSM 21510 / WK1)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.044 kDa
Sequence
MFGRTHYCGEVTDMAIGQTVRLKGWVQKRRDLGGLIFIDLRDRTGIVQIVFSPDVSKEALQVAETIRSEYVLDVEGTVVQREEGQVNPNLPTGTIEVHAMHVTILSEAKTPPFLISDKTDVSEDVRLKYRYLDLRRPVMFQTFKMRHQVTKAIRDFLDEEGFLEVETPILTKSTPEGARDYLVPSRVHPGEFYALPQSPQIFKQLLMVAGFERYYQIARCFRDEDLRADRQPEFTQVDIETSFMSQDDILAMIERMMARVMKVAKGVDISIPFPRMSYDEAIARYGSDKPDTRFGLELVDLSEQVKDCGFKVFASAVQNGGQVKAINVKGAADKYSRKDIDALTEYVARYGAKGLAWLKVEADGLKGPIAKFFTEDEQKQMMQTLEAETGDLLLFVADKKSVVADALGALRLKLGKDLQLIDESAFHFLWITDWPLFEYDEEEGRYYAAHHPFTMPVREDVPKFETDPASVRAQAYDLVLNGYELGGGSLRIFERDIQEKMFKTLGFTEEQAREQFGFLLEAFEYGTPPHGGIALGLDRLVMLLAGRSNLRDTIAFPKTASASCLLTEAPSAVSEEQLEELHLRIKDVQKVD

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Clostridium tetani (strain Massachusetts / E88)
Length
592 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.915 kDa
Sequence
MGEALKGLKRTIMCGQLREENINEQHTVMGWVQRKRNLGGLIFIDLRDRDGILQVVFGEEINKEAFEKADTVRSEYCLAVTGKIIKRQAVNENLPTGIVELQGESIKILSESETPPIYIKEDLDAAENIRLKYRYLDLRRPDMQKILKIRHKTAKAVRDFLDKEEFLEVETPMLTKSTPEGARDYLVPSRNYPGMFYALPQSPQLFKQLLMVSGFDKYFQIVKCFRDEDLRANRQPEFTQIDLEMSFVEMDDVIDLNERLIQYVFKNVVGKDIKLPIERMPYKIAMSKYGSDKPDLRFGMEIENLDDVLKETSFKVFKEVIDNGGTVSAIKAENCAGMGRKQIDKLGDFVKTFKAKGLAWIAYKEDEIKSPIAKFLTEEELKSIIDKMDAKVGDLILIVSDAKEKVVQQSLGQLRLHLAKELGLLKDNDELRFVWVTEFPLVSYNEEEDRWEAEHHPFTAPMDEDIQYLDTDPGKVRAKAYDIVLNGEELGGGSIRIHDTKLQEKMFEVLGFTEEKAWERFGFLLEAFKFGPPPHGGLAFGFDRMIMFLSGTENIKDVIAFPKNQNAFCPMTEAPNVVDEVQLDELGIKIKK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Cronobacter sakazakii (strain ATCC BAA-894)
Length
592 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.23 kDa
Sequence
MRTEYCGQLNLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADAFSLASELRNEFCIQITGTVRARDEKNVNRDMATGEVEVFATELTIINRAEPLPLDSNQVNSEEARLKYRYLDLRRPEMAQRLKTRAKITSFVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEKLIRQLWLDVKGVDLGEFPVMTFAEAERRYGSDKPDLRNPMELVDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGAQLSRKQIDDYGNFVKIYGAKGLAYIKVNERAKGLDGINSPVAKFLNAEIVEAILERTGAQDGDMIFFGADHKKVVADALGALRLKLGKDLSLTDEAKWAPLWVIDFPMFEDDGEGGLSAMHHPFTAPKDMTAEELKAAPEDAVANAYDMVINGYEVGGGSVRIHRGEMQQTVFGILGINEHEQREKFGFLLDALKFGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELGIEVVKKASPENK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Phenylobacterium zucineum (strain HLK1)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.337 kDa
Sequence
MHLYRTHTCGQLRASDTGSKVRLSGWVHRKRDHGGLIFIDLRDHYGLTQLVVSPSTPGFDLVEHVRAESVIRVDGEVVARSAETVNPNLPTGEIEVVVRQVEVLSEAAELPLPVFGEPEYPEDIRLKYRYLDLRRETLHRNIVLRSQVIQSIRRRMIDQGFLEFQTPILTASSPEGARDFLVPSRLHPTKFYALPQAPQQFKQLLMVSGFDRYFQIAPCFRDEDLRADRSLEFYQLDVEMSFVTQDDVFAAIEPVMHGVFTEFGEGKPVTPYPFPRIPYREAIAKYGSDKPDLRNPIEMQDVSEHFRGGGFGLFARILEDAKNAVWAIPGPKGGSRAFCDRMNSWAQGEGQPGLGYIFWSDDQGGWGGPIAKNLGPEKTDGLMKALGLGQGDAAFFVAGDPKVFYKFAGAARTKVGTDLKLIDEGRFEFCWIVDFPMFEWSDEEKKYDFSHNPFSMPQGELDALLNKEPGEIVAYQYDIVCNGHELCSGAIRNHRPDVMLKAFEIAGYGPEVVEEQFGGMLNAFRHGAPPHGGLAPGIDRIVMLLAGETAIREVIAFPLNQQGQDLLMNAPSEVSEKQLKELHIRLAPPIKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.739 kDa
Sequence
MRTDYCGNINASHIGQTVTLCGWVNRRRDLGGVIFIDLRDREGIVQVVYDPDLAELFDTANSLRSEFCVQIEGLVRARPQGQVNKDMGTGEIEILGKGLTILNKSAVLPLDSNQENSEEQRLKYRYLDLRRPVMSDRLKFRAKVTSAVRSYLEGDGFLDIETPMLTKATPEGARDYLVPSRTHKGKFFALPQSPQLFKQLLMMSGMDRYYQIVKCFRDEDLRADRQPEFTQIDIETTFLGAEQVMKITEGMIRNLFMKMLNVDLGEFPQMTYADAMRRFGSDKPDLRNPLELVDVADILKDVEFKVFSGPANDAKGRVAVIRVPGGASMTRKQIDEYTKFVGIYGAKGLAWMKVNDIDAGLEGLQSPILKFLGEDVAKQVLSRVEAQSGDILLFGADSATVVTEALGALRLKVGEDLDLLEGEWKPLWVIDFPMFEEFDGQFYALHHPFTAPRDMTAEQLAADPANALSNAYDMVLNGCELGGGSVRIHNQDMQAKVFNILGISEEEAEVKFGFLLDALKFGAPPHAGLAFGLDRLVMLMTGATSIRDVMAFPKTTTAACPLTDAPGIASDEQLKELSIKTDIVQEKAPSAE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / CIP 101130 / JCM 8532 / LMG 13131)
Length
592 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.608 kDa
Sequence
MVYRTHNLGELRLKNIGEVVTLSGWVDTKRNVSTNLTFIDLRDREGKTQIVFNNELLSEKVLEEVQKLKSESVIRVIGEVKERSNKNPNIPTGEIEVFAKEIEILNACDTLPFQISGVDDNLSENMRLTYRYLDIRRNKMLNNLKMRHRMIMSIRNYMDNAGFLDVDTPVLTKSTPEGARDFLVPSRTNPGTFYALPQSPQLFKQLLMIGGVEKYFQIAKCFRDEDLRADRQPEFTQLDIEMSFVEKEDVMNEIEGLAKYVFKNVTGEEANYIFQRMPYAEAMDRFGSDKPDLRFGVELKDLSDIINNSSFNAFSSTVQNGGLVKAVVAPNANEKFSRKVISEYEEYVKTYFGAKGLAYIKLTADGIASPIAKFLSEEEMKAIIEKTEAKTGDVIFIVADKKKVVHSALGALRLRIGKDLELINKDDFKFLWVVDFPMFDYDEEEQRYKAEHHPFTSIKAEDLDKFLAGQTEDIRTNTYDLVLNGSEIGGGSIRIFNPQIQSMVFDRLGLSQEEAKAKFGFFLDAFKYGAPPHGGLAFGIDRWLMVMLKEESIRDVIPFPKTNKGQCLMTEAPNTVDEKQLEELFIKSTYEK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Vibrio campbellii (strain ATCC BAA-1116 / BB120)
Length
592 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.881 kDa
Sequence
MRTHYCGHLNKSLAGQTVELCGWVNRRRDLGGLIFIDMRDREGIVQVVVDPDMADAYEVANTLRNEFCIKLTGEVRVRPESQVNKDMATGEVEILAKGLEIINRSDVLPLDFNQKNSEEQRLKYRYLDLRRPEMSDRIKLRAKASSFVRRFLDDNGFLDIETPVLTKATPEGARDYLVPSRVHKGSFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTADQVRATTEKMVREMWQELLNVDLGEFPVMPFSEAIRRFGSDKPDLRNPLELVDVADLVKDVEFKVFSGPANDEKGRVAVIRVPGGAELTRKQIDGYAEFVGIYGAKGLAWMKVNDRAAGMEGIQSPVAKFLNEDVINGILDRTQAESGDIILFGADKANIVAEALGALRLKLGKDLDITKEGTWAPLWVVDFPMFEEDDEGNLHAMHHPFTSPLGVTAEELKANPAAANSNAYDMVLNGYEVGGGSVRIHNAEMQAAVFDILGINAEEQQLKFGFLLDALKFGTPPHAGLAFGLDRLVMLLCGTENIRDVIAFPKTTAAACLLTDAPSLANPAALEELAIAVTVAKEKDAE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633)
Length
592 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.763 kDa
Sequence
MRTHYCGHLNKSLAGQTVELCGWVNRRRDLGGLIFIDMRDREGIVQVVVDPDMADAYEVANTLRNEFCIKLTGEVRVRPESQVNKDMATGEVEILAKGLEIINRSDVLPLDFNQKNSEEQRLKYRYLDLRRPEMSDRIKLRAKASSFVRRFLDDNGFLDIETPVLTKATPEGARDYLVPSRVHKGSFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTADQVREVTEKMVREMWQELLNVDLGEFPVMPFSEAIRRFGSDKPDLRNPLELVDVADLVKDVEFKVFSGPANDEKGRVAVIRVPGGAELTRKQIDGYAEFVGIYGAKGLAWMKVNDRAAGVEGIQSPVAKFLSEDVINGILDRTQAESGDIILFGADKANIVAEALGALRLKLGKDLGLTKEGTWAPLWVVDFPMFEEDDEGNLHAMHHPFTSPLGVTAEELKANPAVANSNAYDMVLNGYEVGGGSVRIHNAEMQAAVFDILGIDAEEQQLKFGFLLDALKFGTPPHAGLAFGLDRLVMLLCGTENIRDVIAFPKTTAAACLLTDAPSIANPAALEELAIAVTAAKAKDAE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Vibrio tasmaniensis (strain LGP32)
Length
592 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.981 kDa
Sequence
MRTHYCGNLNKSLAGQTVELCGWVNRRRDLGGLIFIDMRDREGVVQVVVDPDMKDIFPIANQLRNEFCIKFTGEVRVRPDSQVNKDMATGEVELYATGLEIINRSEALPLDFNQTNSEEQRLKYRYIDLRRPEMSDRIKLRARASSFVRRFLDENLFLDIETPVLTKATPEGARDYLVPSRVHKGSFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFLTSQEVRNVTEKLVHDMWKELLDVELGQFPVMPFSEAIRRFGSDKPDLRNPLELVDVADLVKDVEFKVFSGPANDEKGRVAVIRVPGGAKLTRKQIDGYAEHVNIYGAKGLAWMKVNDRAAGMEGIQSPVAKFLSEDVINGILDRTQAESGDIILFGADKAGIVAEAMGALRLKLGTDLELTDTSAWAPLWVVDFPMFEEDGEGNLHAMHHPFTSPLGVNAEELKANPAAANSDAYDMVINGYEVGGGSVRIHSAEMQTAVFGILGIEAKEQQEKFGFLLEALKYGTPPHAGLAFGLDRLAMLLCGTENIRDVIAFPKTTAAACLLTDAPSLANPASLEELAIAVKLAEKKEQA

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Vibrio vulnificus (strain CMCP6)
Length
592 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.842 kDa
Sequence
MRTHYCGHLNKSLAGQTVELCGWVNRRRDLGGLIFIDMRDREGIVQVVVDPDMADAYAVASQLRNEFCIKLTGEVRTRPESQVNKEMATGEVEILAKGLEIINRSDVLPLDFNQKNSEEQRLKYRYLDLRRPEMSDRIKLRAKASSFVRRFLDDNGFLDIETPVLTKATPEGARDYLVPSRVHKGSFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTSDQVRAVTEKMVREMWLELLNVDLGEFPVMPFSEAIRRFGSDKPDLRNPLELVDVADLVKDVDFKVFSGPANDEKGRVAVIRVPGGAELTRKQIDEYTGFVNIYGAKGLAWMKVNDRAAGMEGIQSPVAKFLSEDVINGILERTQAESGDIILFGADKANIVAEALGALRLKLGKDLGLTKEGTWAPLWVVDFPMFEEDDEGNLHAMHHPFTSPLGLTAEELKANPAPAISNAYDMVLNGYEVGGGSVRIHNAEMQAAVFDILGIDADEQKLKFGFLLDALKFGTPPHAGLAFGLDRLVMLLCGTENIRDVIAFPKTTAAACLMTDAPSVANPAALEELAIAVTVAKEKSAE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Vibrio vulnificus (strain YJ016)
Length
592 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.828 kDa
Sequence
MRTHYCGHLNKSLAGQTVELCGWVNRRRDLGGLIFIDMRDREGIVQVVVDPDMADAYAVASQLRNEFCIKLTGEVRTRPESQVNKEMATGEVEILAKGLEIINRSDVLPLDFNQKNSEEQRLKYRYLDLRRPEMSDRIKLRAKASSFVRRFLDDNGFLDIETPVLTKATPEGARDYLVPSRVHKGSFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTSDQVRAVTEKMVREMWLELLNVDLGEFPVMPFSEAIRRFGSDKPDLRNPLELVDVADLVKDVDFKVFSGPANDEKGRVAVIRVPGGAELTRKQIDEYTGFVNIYGAKGLAWMKVNDRAAGMEGIQSPVAKFLSEDVINGILERTQAESGDIILFGADKANIVAEALGALRLKLGKDLGLTKEGTWAPLWVVDFPMFEEDDEGNLHAMHHPFTSPLGLTAEELKANPAPAVSNAYDMVLNGYEVGGGSVRIHNAEMQAAVFDILGIDADEQKLKFGFLLDALKFGTPPHAGLAFGLDRLVMLLCGTENIRDVIAFPKTTAAACLMTDAPSVANPAALEELAIAVTVAKEKSAE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768)
Length
592 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.203 kDa
Sequence
MRSHYCGQLNETLVDEEVALCGWVHRRRDHGGVIFLDLRDRDGIAQVVVDPDTPEAFANADRARNEFVLRIRGRIRLRPEGTQNAHMPTGMIEVLAKDVEVLNTAATPPFQLDEHGKVGEEIRLKHRYIDLRRPEMIDKLRLRSRITHSVRAYLEGQGFLDIETPILTRATPEGARDYLVPSRTHAGEFFALPQSPQLFKQLLMVSGFDRYYQIAKCFRDEDLRADRQPEFTQIDLEASFVEESDIMSLTEDMIRRLFQDVLDVELPAFPKMPYSEAMNRYGSDKPDLRIPLELVDVDDLMQGVDFKVFSGPAKADDGRVAALKVTGGATLSRKEIDAYTDFVNIYGAKGLAWIKVNERAKGIQGLQSPIVKFMEDIIESLLDRVGAEDGDIIFFGADKARIVNEALGALRVKLGEDLDLYTQAWAPLWVVDFPMFEADDNGRLAALHHPFTAPSCTPEAFKADPANALSRAYDMVLNGTELGGGSIRIHDQTMQRAVFEVLGIGEEEADEKFGFLLDALKFGAPPHGGLAFGLDRLVMLMSGARTIREVIAFPKTQSAACLMTDAPGEVSAEQLKELNIRLRQKAQNNGDV

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46)
Length
592 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.378 kDa
Sequence
MFGRTYYCGEITEKAIGETVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPDVSKDALETAESIRSEYVLDITGKVVAREEATVNPNLKTGRIEIQAESVDVLSAAKTPPFAISDQAAEVSEDIRLKHRYLDLRRPEMFNSLKMRHNVTKAVRRFLDDNGFLDIETPVLTKSTPEGARDYLVPSRVHEGEFYALPQSPQIFKQLLMVSGFDRYYQIARCFRDEDLRADRQPEFTQIDIEMSFMSQEDIMKLSEEMMAHVMRETHGIEISLPLPRMSYEDAMNRYGSDKPDTRFGMLLTDVSEAVKDSDFKVFASAVANGGAVKAINVKGAAANYSRKDIDALGEFAANYGAKGLAWLKTEADGLKGPIAKFFAGEKQEALVQALDAADGDLLLFVADKLEVANDALGALRLKLGKELNLIDESLFNFLWVVDWPLLEYDAEEGRYYAAHHPFTMPVREDLKLIETNPQDMKAQAYDLVLNGYELGGGSIRIFEKDVQEKMFGLLGFSEEEAKEQFGFLLEAFDYGAPPHGGIALGLDRLVMLLSGRTNLRDTIAFPKTASASCLMTEAPSEVDNAQLDELHLEIKRKIRQ

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Pseudoalteromonas haloplanktis (strain TAC 125)
Length
592 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.258 kDa
Sequence
MRSIYCGQLNKTHVDQEVELCGWINKRRDLGGLIFVDLRDREGLVQVVFDSDIEELMSSANTLRQEFCVQLKGIVRARPDSQVNKDMPTGEIEILGTELNIINRSEPLPLDFNQVNSEERRLKYRYLDLRRLEMSDRIKLRAKASSFVRRFLDENGFLDIETPVLTKATPEGARDYLVPSRVHKGSFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMSSDQVRGMTEKMIREMWQTLLNVDLGDFPIMPYSEAMSLYGSDKPDLRNPMKLVDIADLVKDVEFNVFSGPANDEKGRVAVLTVPGGAKLSRKQLDDYTKFIGIYGAKGMAWMKVNDHTAGAEGVQSPVAKFLTADVITQLLERTNAQSGDIILFGADKRNTVNEAMGALRVKIGIDLEITNLDSWAPLWVVDFPMFEEDDEGTLHAVHHPFTAPKDMSASELEANPAAAISDAYDMVLNGYEVGGGSVRIHNADMQEAAFRILGINEQEQQDKFGFLLDALKYGTPPHAGLAFGLDRLAMLLCGTDNIRDVIAFPKTTQASCLLTNAPSKPNADSLAELAISVVEKAVLSAE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Macrococcus caseolyticus (strain JCSC5402)
Length
592 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.42 kDa
Sequence
MDNRTTYCGLVTESYIGQEIILKGWVQKRRDLGGLIFIDLRDREGVVQIVFNPDFSKEALTIAETIRSEYVIEVHGKVTMRDEAVINPKIKTGKVEVQVSEVTIINKSETPPFQIEAETDSSEDVRLKYRYLDLRREPLANTFKMRHQITRAVRNYLDESGFYEVETPVLTKSTPEGARDYLVPSRVQEGEFYALPQSPQIFKQLLMIGGFDKYYQIVKCFRDEDLRADRQPEFTQIDIEMSFVDQEDVMSMNEGMLKRIMKDVKGIDIATPFPRMTYEEAMRDYGIDKPDTRFDMKLVTLNDLASKMEFKVFKGAVESGGAVKAIVVKGASDKYSRKDIDALQEYAKIYGAKGLAWVKVTEDGLNGPIAKFFEESHASELLDATNAEMGDLILFVADKWSVVNASLANLRNKLGKELGLIDENKYNFLWVTDWPLFEYDEELDRYFAAHHPFTAPKKEHVEMLKTDKEKVQANAYDVVLNGYELGGGSIRIHDQEMQKKMFEALGFSDEEAQEQFGFLMDAFKYGAPPHGGIALGLDRMVMLLSGRSNLRDVIAFPKTASATCLLTDAPSKVDDKQLEELHIQLNIENSEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pseudomonas aeruginosa (strain LESB58)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.208 kDa
Sequence
MMRSHYCGQLNESLDGQEVTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPDRAETFAKADRVRSEFVVKITGKVRLRPEGARNPNMASGSIEVLGYELEVLNQAETPPFPLDEYSDVGEETRLRYRFIDLRRPEMAAKLKLRARITSSIRRYLDDNGFLDVETPILGRPTPEGARDYLVPSRTYPGHFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLDESDIIGITEKMVRQLFKEVLDVEFDEFPHMPFEEAMRRYGSDKPDLRIPLELVDVADQLKEVEFKVFSGPANDPKGRVAALRVPGAASMPRSQIDDYTKFVGIYGAKGLAYIKVNERAKGVEGLQSPIVKFIPEANLNVILDRVGAVDGDIVFFGADKAKIVCDALGALRIKVGHDLKLLTREWAPMWVVDFPMFEENDDGSLSALHHPFTSPKCTPAELEANPGAALSRAYDMVLNGTELGGGSIRIHDKSMQQAVFRVLGIDEAEQEEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMTGASSIREVIAFPKTQSAGDVMTQAPGSVDGKALRELHIRLREQPKAE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pseudomonas aeruginosa (strain UCBPP-PA14)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.208 kDa
Sequence
MMRSHYCGQLNESLDGQEVTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPDRAETFAKADRVRSEFVVKITGKVRLRPEGARNPNMASGSIEVLGYELEVLNQAETPPFPLDEYSDVGEETRLRYRFIDLRRPEMAAKLKLRARITSSIRRYLDDNGFLDVETPILGRPTPEGARDYLVPSRTYPGHFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLDESDIIGITEKMVRQLFKEVLDVEFDEFPHMPFEEAMRRYGSDKPDLRIPLELVDVADQLKEVEFKVFSGPANDPKGRVAALRVPGAASMPRSQIDDYTKFVGIYGAKGLAYIKVNERAKGVEGLQSPIVKFIPEANLNVILDRVGAVDGDIVFFGADKAKIVCDALGALRIKVGHDLKLLTREWAPMWVVDFPMFEENDDGSLSALHHPFTSPKCTPAELEANPGAALSRAYDMVLNGTELGGGSIRIHDKSMQQAVFRVLGIDEAEQEEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMTGASSIREVIAFPKTQSAGDVMTQAPGSVDGKALRELHIRLREQPKAE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Is 1.5 times more efficient at aminoacylating E.coli tRNA(Asp) over tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.208 kDa
Sequence
MMRSHYCGQLNESLDGQEVTLCGWVHRRRDHGGVIFLDVRDREGLAQVVFDPDRAETFAKADRVRSEFVVKITGKVRLRPEGARNPNMASGSIEVLGYELEVLNQAETPPFPLDEYSDVGEETRLRYRFIDLRRPEMAAKLKLRARITSSIRRYLDDNGFLDVETPILGRPTPEGARDYLVPSRTYPGHFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLDESDIIGITEKMVRQLFKEVLDVEFDEFPHMPFEEAMRRYGSDKPDLRIPLELVDVADQLKEVEFKVFSGPANDPKGRVAALRVPGAASMPRSQIDDYTKFVGIYGAKGLAYIKVNERAKGVEGLQSPIVKFIPEANLNVILDRVGAVDGDIVFFGADKAKIVCDALGALRIKVGHDLKLLTREWAPMWVVDFPMFEENDDGSLSALHHPFTSPKCTPAELEANPGAALSRAYDMVLNGTELGGGSIRIHDKSMQQAVFRVLGIDEAEQEEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMTGASSIREVIAFPKTQSAGDVMTQAPGSVDGKALRELHIRLREQPKAE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pseudomonas entomophila (strain L48)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.523 kDa
Sequence
MMRSHYCGQLNESLDGQEVTLCGWVHRRRDHGGVIFLDIRDREGMAQVVFDPDRAETFAAADRVRSEYVVQITGKVRKRPEGAVNTNMASGAIEILGYQLNVLNEAETPPFPLNEYSDVGEETRLRYRFIDLRRPEMADKLRLRSRITSSIRRFLDENGFLDVETPILTRATPEGARDYLVPSRTHAGSFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLDESEIMGLTESMIRKLFKEVLDLEFGEFPHMTFEEAMRRYGSDKPDLRNPLELVDVADQLKDVDFKVFAGPANDPKCRVTALRLPGGASMPRSKIDEYTKFVGIYGAKGLAYIKVNERAKGVEGLQSPIVKNIPEANLNNILDRVGAVDGDIVFFGADKFKVVSEALGALRIRLGHDFELLTCEWAPMWVVDFPMFEENEDGSFTALHHPFTAPKCTPEELEANPATALSRAYDMVLNGTELGGGSIRIHRKEMQQAVFRLLGIEAAEQEEKFGFLLDALKFGAPPHGGLAFGLDRLVMLMTGAQSIREVIAFPKTQSAACVMTQAPGLVDAKALRELHIRLREQTKVE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.282 kDa
Sequence
MMRSHYCGQLNESLEGQEVTLCGWVHRRRDHGGVIFLDIRDREGLAQVVFDPDRAETFAAADRVRSEYVVKITGKVRLRPAGAGNANMASGMIEVLGYELEVLNEAETPPFPLNEYSDVGEETRLRYRFIDLRRPEMAEKLRLRSRMTTSIRRYLDENGFLDVETPILTRATPEGARDYLVPSRTHAGSFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLDEKDIMGLTEGMIRNLFKEVLGLEFGEFPHMTFEEAMRRYGSDKPDLRNPLELVDVADQLKEVEFKVFSGPANDPKCRIAALRVPGGASMPRKQIDDYTKFVGIYGAKGLAYIKVNERAKGVEGLQSPIVKNIPEANLNVILDRVGAVDGDIVFFGADKAKIVSEALGALRIKLGHDLNLLTCEWAPMWVVDFPMFEENDDGSFTALHHPFTAPKCSPEELEANPATALSRAYDMVLNGTELGGGSIRIHRKEMQQAVFRLLGISEAEQEEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMTGAQSIREVIAFPKTQSAACVMTQAPGLVDAKALRELHIRLREQPKAE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pseudomonas fluorescens (strain SBW25)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.262 kDa
Sequence
MMRSHYCGQLNETLEGQEITLCGWVHRRRDHGGVIFLDIRDRDGLAQVVFDPDRAESFAAADRVRSEYVVKITGKVRLRPAGAVNKNMASGGIEVLGYELEVLNESETPPFPLNEYSDVGEETRLRYRFLDLRRPEMAEKLRLRSRMTTSIRRFLDENGFLDVETPILTRATPEGARDYLVPSRTHAGSFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLDEKEIMGLTEQMIRNLFKEVLDLEFGDFPHMTFEEAMRRYGSDKPDLRNPLELVDVADQLKDVDFKVFSGPANDPKCRIAALRVPGGASMPRKQIDDYTKFVGIYGAKGLAYIKVNERANGVDGLQSPIVKNIPLDNLNAILDRVGAVDGDIVFFGADKAKIVSEALGALRIKLGHDLNLLTCEWAPMWVVDFPMFEENDDGSFSALHHPFTAPKCSPAELEANPAGALSRAYDMVLNGTELGGGSIRIHRKEMQQAVFRLLGINEAEQEEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMTGAQSIREVIAFPKTQSAADVMTQAPGVVDAKALRELHIRLRETPKAE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pseudomonas mendocina (strain ymp)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.048 kDa
Sequence
MMRSHYCGQLNESLDGQEITLCGWVHRRRDHGGVIFLDIRDREGLAQVVFDPDRAETFAKADRVRSEYVVKITGKVRLRPAGAVNPNMASGAIEVLGYELDVLNEAETPPFPLNEYTDVGEETRLRYRFIDLRRPEMAEKLKLRSRITSSIRRYLDDNGFLDVETPILTRATPEGARDYLVPSRTHAGSFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLDEKDIMDITETMVRNLFKEVLGVEFGELPHMPLAEAMRRFGSDKPDLRIPLELVDVEDQLKDVEFKVFAGPANDPKCRVTALRVPGGASMPRKQIDDYTKFVGIYGAKGLAYIKVNERAAGVDGLQSPIVKNIPLDNINVILDRVGAVDGDIVFFGADKAKIVSEALGALRIKLGHDLNLLTCEWAPLWVVDFPMFEENDDGSLTAMHHPFTSPKCTPEDLEANPAAALSRAYDMVLNGTELGGGSIRIHDKAMQQTVFRVLGISEDEQQEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMTGASSIREVIAFPKTQSAACVMTQAPGVVDAKSLRELHIRLREQAKAE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.568 kDa
Sequence
MMRSHYCGQLNESLDGQEVTLCGWVHRRRDHGGVIFLDIRDREGMAQVVFDPDRAETFAAADRVRSEYVVQITGKVRKRPEGAVNANMASGAIEILGYQLNVLNEAETPPFPLNEYSDVGEETRLRYRFIDLRRPEMADKLRLRSRITSSIRRFLDENGFLDVETPILTRATPEGARDYLVPSRTHAGSFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLDESEIMGLTESMIRKLFKEVLDLEFGEFPHMTFEEAMRRYGSDKPDLRIPLELVDVADQLKDVDFKVFAGPANDPKCRVTALRLPGGASMPRSKIDEYTKFVGIYGAKGLAYIKVNERAKGVEGLQSPIVKNIPEANLNNILDRVGAVDGDIVFFGADKFKVVSEALGALRIRLGHDFELLTCEWAPMWVVDFPMFEENEDGSFTALHHPFTAPKCTPEELEANPATALSRAYDMVLNGTELGGGSIRIHRKEMQQAVFRLLGIEAEEQEEKFGFLLDALKFGAPPHGGLAFGLDRLVMLMTGAQSIREVIAFPKTQSAACVMTQAPGMVDAKALRELHIRLREQTKVE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pseudomonas fluorescens (strain Pf0-1)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.253 kDa
Sequence
MMRSHYCGQLNESLEGQEITLCGWVHRRRDHGGVIFLDIRDRDGLAQVVFDPDRAESFAAADRVRSEYVVKITGKVRLRPAGATNANMASGMIEVLGYELEVLNESETPPFPLNEFSDVGEETRLRYRFLDLRRPEMAEKLRLRSRMTTSIRRYLDENGFLDVETPILTRATPEGARDYLVPSRTHAGSFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLDEKDIMGLTEGMIRNLFKEVLDLEFGEFPHMTFEEAMRRYGSDKPDLRNPLELVDVADQLKEVDFKVFSGPANDPKCRIAALRVPGGASMPRKQIDDYTKFVGIYGAKGLAYIKVNERAAGVEGLQSPIVKNIPEANLNVILDRVGAVDGDIVFFGADKAKIVSEALGALRIKLGHDLKLLTCEWAPMWVVDFPMFEENDDGSFSALHHPFTAPKCSPEELEANPAGALSRAYDMVLNGTELGGGSIRIHRKEMQQAVFRLLGINEAEQEEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMTGAQSIREVIAFPKTQSAADVMTQAPGVVDAKALRELHIRLRETPKAE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pseudomonas putida (strain GB-1)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.537 kDa
Sequence
MMRSHYCGQLNESLDGQEVTLCGWVHRRRDHGGVIFLDIRDREGMAQVVFDPDRAETFAAADRVRSEYVVQITGKVRKRPDGAVNANMASGAIEILGYQLNVLNEAETPPFPLNEYSDVGEETRLRYRFIDLRRPEMADKLRLRSRITSSIRRFLDENGFLDVETPILTRATPEGARDYLVPSRTHAGSFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLDESEIMGLTESMIRKLFKEVLDLEFGEFPHMTFEEAMRRYGSDKPDLRNPLELVDVADQLKDVDFKVFAGPANDPKCRVTALRLPGGASMPRSKIDEYTKFVGIYGAKGLAYIKVNERAKGVEGLQSPIVKNIPEANLNNILDRVGAVDGDIVFFGADKFKVVSEALGALRIRLGHDFELLTCEWAPMWVVDFPMFEENEDGSFTALHHPFTAPKCTPEELEANPATALSRAYDMVLNGTELGGGSIRIHRKEMQQAVFRLLGIEAEEQEEKFGFLLDALKFGAPPHGGLAFGLDRLVMLMTGAQSIREVIAFPKTQSAACVMTQAPGLVDAKALRELHIRLREQTKVE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.568 kDa
Sequence
MMRSHYCGQLNESLDGQEVTLCGWVHRRRDHGGVIFLDIRDREGMAQVVFDPDRAETFAAADRVRSEYVVQITGKVRKRPEGAVNANMASGAIEILGYQLNVLNEAETPPFPLNEYSDVGEETRLRYRFIDLRRPEMADKLRLRSRITSSIRRFLDENGFLDVETPILTRATPEGARDYLVPSRTHAGSFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLDESEIMGLTESMIRKLFKEVLDLEFGEFPHMTFEEAMRRYGSDKPDLRIPLELVDVADQLKDVDFKVFAGPANDPKCRVTALRLPGGASMPRSKIDEYTKFVGIYGAKGLAYIKVNERAKGVEGLQSPIVKNIPEANLNNILDRVGAVDGDIVFFGADKFKVVSEALGALRIRLGHDFELLTCEWAPMWVVDFPMFEENEDGSFTALHHPFTAPKCTPEELEANPATALSRAYDMVLNGTELGGGSIRIHRKEMQQAVFRLLGIEAEEQEEKFGFLLDALKFGAPPHGGLAFGLDRLVMLMTGAQSIREVIAFPKTQSAACVMTQAPGMVDAKALRELHIRLREQTKVE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pseudomonas putida (strain W619)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.492 kDa
Sequence
MMRSHYCGQLNESLDGQEVTLCGWVHRRRDHGGVIFLDIRDREGMAQVVFDPDRAETFAAADRVRSEYVVQITGKVRKRPDGAVNANMASGAIEILGYQLNVLNEAETPPFPLNEYSDVGEETRLRYRFIDLRRPEMADKLRLRSRITSSIRRFLDENGFLDVETPILTRATPEGARDYLVPSRTHAGSFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLDESEIMGLTESMIRKLFKEVLDLEFGEFPHMTFEEAMRRYGSDKPDLRNPLELVDVADQLKDVDFKVFAGPANDPKCRVTALRLPGGASMPRSKIDEYTKFVGIYGARGLAYIKVNERAKGVEGLQSPIVKNIPEANLNVILDRVGAVDGDIVFFGADKFKVVSEALGALRIRLGHDFELLTCEWAPMWVVDFPMFEENEDGSFTALHHPFTAPKCTPEELEANPATALSRAYDMVLNGTELGGGSIRIHRKEMQQAVFRLLGIEAAEQEEKFGFLLDALKFGAPPHGGLAFGLDRLVMLMTGAQSIREVIAFPKTQSAACVMTQAPGLVDAKALRELHIRLREQTKVE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.352 kDa
Sequence
MMRSHYCGQLNESLEGQEITLCGWVHRRRDHGGVIFLDIRDREGMAQVVFDPDRADSFAAADRVRSEYVVKVVGKVRARPAGAVNANMASGAIEVLGYELEVLNESETPPFPLNEYSDVGEETRLRYRFIDLRRPEMAEKLRLRSRITTSIRRYLDENGFLDVETPILTRATPEGARDYLVPSRTHPGSFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLNEEDIIGLTEKMVRQLFKEVLNVEFGDFPHMTFEEAMRRYGSDKPDLRNPLELVDVADQLNAVEFKVFSGPANDPKGRVAALRVPGAASMARSQIDDYTKFVSIYGAKGLAYIKVNERAKGPEGLQSPIVKFIPEENLNVILDRVGAVDGDIVFFGADKFKVVSEALGALRIKIGNDLKLHTCEWAPMWVVDFPMFEENDDGSFSALHHPFTAPKCTPEELEANPATALSRAYDMVLNGTELGGGSIRIHRKEMQQAVFRLLGIAEDEQQEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMTGAQSIREVIAFPKTQSAADVMTQAPGVVDAKALRELHIRLREQPKAE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pseudomonas syringae pv. syringae (strain B728a)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.34 kDa
Sequence
MMRSHYCGQLNESLEGQEITLCGWVHRRRDHGGVIFLDIRDREGMAQVVFDPDRADSFAAADRVRSEYVVKVVGKVRARPAGAVNANMASGAIEVLGYELEVLNESETPPFPLNEYSDVGEETRLRYRFIDLRRPEMAEKLRLRSRITTSIRRYLDDNGFLDVETPILTRATPEGARDYLVPSRTHPGSFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLNEEDIIGLTEKMVRQLFKEVLDLEFGDFPHMTFEEAMRRYGSDKPDLRNPLELVDVADQLTGVEFKVFSGPANDPKGRVAALRVPGAASMARSQIDDYTKFVSIYGAKGLAYIKVNERAKGPEGLQSPIVKFIPEDNLNVILDRVGAVDGDIVFFGADKFKIVSEALGALRIKIGNDLKLHTCEWAPMWVVDFPMFEENDDGSFTALHHPFTAPKCTPEELEANPATALSRAYDMVLNGTELGGGSIRIHRKEMQQAVFRLLGIAEDEQQEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMTGAQSIREVIAFPKTQSAADVMTQAPGVVDAKALRELHIRLREQPKAE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Jannaschia sp. (strain CCS1)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.33 kDa
Sequence
MHAYRSHSCAALTAANVGETIRLSGWVHRRRDHGGVIFIDLRDHFGITQILCDPDSPVFAEVEKLRAEFCIRIDGEVKARAPELVNEKLPTGEIEVYIRDMEVLGAAGELPLQVFGDQEYPEETRLKYRYLDLRREKMQTNMMLRSDVVASIRKRMWDKQFREYQTPIITASSPEGARDFLVPSRQHPGKFYALPQAPQQFKQLLMVSGFDKYFQIAPCFRDEDPRADRSPTDFYQLDLEMSFVEQQDVFDTIEPVLRGVFEEFGDGATVDQQWPLISYADAALWYGTDKPDLRNPIKMQIVSEHFAGSGFAIFAKLLEQEGTQVRAIPAPKGGSRKFCDRMNKFAQEQGLPGMGYIFWRDQGEGMEAAGPLAKNIGPERTEAIRQQLDLGVGDAAFFLAGKPSQFEAVAGRARSVIGDELGLTEQNRFAFAWIVDFPMFEADEETGKIDFSHNPFSMPQGGLAALDGDPLSVLGYQYDLACNGYELVSGAIRNHQPEIMFKAFEVAGYGADEVRKRFGGMVNAFQYGAPPHGGCAAGIDRIVMLLADTANIREVILFPMNQRAEDLMMNAPSEPMPDQLMELGLRVLPQD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bacillus cereus (strain AH187)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.336 kDa
Sequence
MAERTHACGKVTVEAVGQTVQLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPETSKEALEVAETIRSEYVLHVEGTVVERGEGAINDNMATGRIEVQATKVNVLNAAKTTPIIIADDTDASEDVRLKYRYLDLRRPVMFNTFKMRHDVTKTIRNFLDTEEFLEVETPILTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMVGGFERYYQVARCFRDEDLRADRQPEFTQIDIEASFLTQEEILDMMERMMTKVMKDAKGVEISAPFPRMTYADAMARYGSDKPDTRFEMELTDLSEFAAGCGFKVFTSAVESGGQVKAINAKGAASKYSRKDIDALTEFVKVYGAKGLAWLKVEEDGLKGPIAKFFGEEDANVLMNTLEATAGDLLLFVADKKSVVADSLGALRLRLGKELELIDESKFNFLWVTDWPLLEYDEDADRYFAAHHPFTMPFREDVELLETAPEKARAQAYDLVLNGYELGGGSLRIYERDVQEKMFKALGFSQEEAQEQFGFLLEAFEYGTPPHGGIALGLDRLVMLLAGRTNLRDTIAFPKTASASCLLTEAPSPVAEAQLEELNLKLSLKEEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bacillus cereus (strain Q1)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.336 kDa
Sequence
MAERTHACGKVTVEAVGQTVQLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPETSKEALEVAETIRSEYVLHVEGTVVERGEGAINDNMATGRIEVQATKVNVLNAAKTTPIIIADDTDASEDVRLKYRYLDLRRPVMFNTFKMRHDVTKTIRNFLDTEEFLEVETPILTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMVGGFERYYQVARCFRDEDLRADRQPEFTQIDIEASFLTQEEILDMMERMMTKVMKDAKGVEISAPFPRMTYADAMARYGSDKPDTRFEMELTDLSEFAAGCGFKVFTSAVESGGQVKAINAKGAASKYSRKDIDALTEFVKVYGAKGLAWLKVEEDGLKGPIAKFFGEEDANVLMNTLEATAGDLLLFVADKKSVVADSLGALRLRLGKELELIDESKFNFLWVTDWPLLEYDEDADRYFAAHHPFTMPFREDVELLETAPEKARAQAYDLVLNGYELGGGSLRIYERDVQEKMFKALGFSQEEAQEQFGFLLEAFEYGTPPHGGIALGLDRLVMLLAGRTNLRDTIAFPKTASASCLLTEAPSPVAEAQLEELNLKLSLKEEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bacillus cereus (strain ATCC 14579 / DSM 31 / JCM 2152 / NBRC 15305 / NCIMB 9373 / NRRL B-3711)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.313 kDa
Sequence
MAERTHACGKVTVEAVGQTVQLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPETSKEALEVAETIRSEYVLHVEGTVVERGEGAINDNMATGRIEVQATKVNVLNAAKTTPIIIADDTDASEDVRLKYRYLDLRRPVMFNTFKMRHDVTKTIRNFLDTEEFLEVETPILTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMVGGFERYYQVARCFRDEDLRADRQPEFTQIDIEASFLTQDEILDMMERMMTKVMKDAKGVEVSAPFPRMKYADAMARYGSDKPDTCFEMELTDLSEFAADCGFKVFTSAVESGGQVKAINAKGAASKYSRKDIDALTEFVKVYGAKGLAWLKVEEDGLKGPIAKFFGEEDANVLMSTLEATAGDLLLFVADKKSVVADSLGALRLRLGKELELIDESKFNFLWVTDWPLLEYDEDADRYFAAHHPFTMPFREDVELLETAPEKARAQAYDLVLNGYELGGGSLRIYERDVQEKMFKALGFSQEEAQEQFGFLLEAFEYGTPPHGGIALGLDRLVMLLAGRTNLRDTIAFPKTASASCLLTEAPSPVAEAQLEELNLKLSLKEEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bacillus cereus (strain ZK / E33L)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.321 kDa
Sequence
MAERTHACGKVTVEAVGQTVQLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPETSKEALEVAETIRSEYVLHVEGTVVERGEGAINDNMATGRIEVQATKVNVLNAAKTTPIIIADDTDASEDVRLKYRYLDLRRPVMFNTFKMRHDVTKTIRNFLDTEEFLEVETPILTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMVGGFERYYQVARCFRDEDLRADRQPEFTQIDIEASFLTQDEILDMMERMMTKVMKDAKGVEVSAPFPRMKYADAMARYGSDKPDTRFEMELTDLSEFAAGCGFKVFTSAVESGGQVKAINAKGAASKYSRKDIDALTEFVKVYGAKGLAWLKVEEDGLKGPIAKFFGEEDANVLMNTLEATAGDLLLFVADKKSVVADSLGALRLRLGKELELIDESKFNFLWVTDWPLLEYDEDADRYFAAHHPFTMPFREDVELLETAPEKARAQAYDLVLNGYELGGGSLRIYERDVQEKMFKALGFSQEDAQEQFGFLLEAFEYGTPPHGGIALGLDRLVMLLAGRTNLRDTIAFPKTASASCLLTEAPSPVAEAQLEELNLKLSLKEEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bacillus thuringiensis subsp. konkukian (strain 97-27)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.348 kDa
Sequence
MAERTHACGKVTVEAVGQTVQLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPETSKEALEVAETIRSEYVLHVEGTVVERGEGAINDNMATGRIEVQATKVNVLNAAKTTPIIIADDTDASEDVRLKYRYLDLRRPVMFNTFKMRHDVTKTIRNFLDTEEFLEVETPILTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMVGGFERYYQVARCFRDEDLRADRQPEFTQIDIEASFLTQDEILDMMERMMTKVMKDAKGVEVSAPFPRMKYADAMARYGSDKPDTRFEMELTDLSEFAAGCGFKVFTSAVESGGQVKAINAKGAASKYSRKDIDALTEFVKVYGAKGLAWLKVEEDGLKGPIAKFFGEEDANVLMNTLEATAGDLLLFVADKKSVVADSLGALRLRLGKELELIDESKFNFLWVTDWPLLEYDEDADRYFAAHHPFTMPFREDVELLETAPEKARAQAYDLVLNGYELGGGSLRIYERDVQEKMFKALGFSQEEAQEQFGFLLEAFEYGTPPHGGIALGLDRLVMLLAGRTNLRDTIAFPKTASASCLLTEAPSPVAEAQLEELNLKLNVKEEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bacillus weihenstephanensis (strain KBAB4)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.319 kDa
Sequence
MAERTHACGKVTVEAVGQTVQLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPETSKEALEVAETIRSEYVLHVEGTVVERGEGAINDNMATGRIEVQASKVNVLNAAKTTPIIIADDTDASEDVRLKYRYLDLRRPAMFNTFKMRHDVTKTIRNFLDTEEFLEVETPILTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMVGGFERYYQVARCFRDEDLRADRQPEFTQIDIEASFLTQDEILEMMERMMTKVMKDAKGVEVSAPFPRMKYADAMARFGSDKPDTRFEMELKDLSEFAVGCGFKVFTSAVENGGQVKAINAKGAASKYSRKDIDALTEFAKVYGAKGLAWLKVEEDGLKGPIAKFFGEEEANVLMSTLEADAGDLLLFVADKKSVVADSLGALRLRLGKELELIDESKFNFLWVTDWPLLEYDEDADRYFAAHHPFTMPFREDVELLETAPEKARAQAYDLVLNGYELGGGSLRIYERDVQEKMFKALGFSQEEAQEQFGFLLEAFEYGTPPHGGIALGLDRLVMLLAGRTNLRDTIAFPKTASASCLLTEAPSPVAEAQLEELSLKLSLKEEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.654 kDa
Sequence
MHRYRTHTCGALRDSHIDQTVRLSGWCHRIRDHGGVLFIDLRDHYGLTQCVADPDSPAFKDAEKLRAEWVVRIDGKVRRRPEGTDNPDLPTGAVEVFVTEIEVLGPAGELPLPVFGEQEYPEDVRLRYRFLDLRREKLHQNIMTRGAIVDSMRRRMKEQGFFEFQTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMMSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDVEMSFVTQDDIFAAMEPVITGVFEEFAKGKRVTKGWPRIAFADSMRKYGTDKPDLRNPIEMQDVSEHFRGSGFKVFARMLEEQRNQVWAIPGPGGGSRAFCDRMNSWAQGEGQPGLGYIMWREGGEGAGPLANNIGPERTEAIRAALGLKAGDAAFFVAGDPSKFVKFAGLARTKVGEELNLIDKDQFALAWVVDFPMYEYNEDDKKVDFSHNPFSMPQGGMEALTSQDPLTIKAFQYDITCNGYEIASGGIRNHRPEAMVKAFEIAGYGEQEVVDRFGGMYRAFQYGAPPHGGMAAGVDRIVMLLCGTTNLREISLFPMNQRAEDLLMGAPSEVSPKQLRELHIRLNLPDTK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rhodopseudomonas palustris (strain TIE-1)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.684 kDa
Sequence
MHRYRTHTCGALRDSHIDQTVRLSGWCHRIRDHGGVLFIDLRDHYGLTQCVADPDSPAFKDAEKLRAEWVVRIDGKVRRRPEGTDNPDLPTGAVEVFVTEIEVLGPAGELPLPVFGEQEYPEDVRLRYRFLDLRREKLHQNIMTRGAIVDSMRRRMKEQGFFEFQTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMMSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDVEMSFVTQDDIFAAMEPVITGVFEEFAKGKRVTKGWPRIAFADSMRKYGTDKPDLRNPIEMQDVSEHFRGSGFKVFARMLEEQRNQVWAIPGPGGGSRAFCDRMNSWAQGEGQPGLGYIMWREGGEGAGPLANNIGPERTEAIRTALGLKAGDAAFFVAGDPSKFVKFAGLARTKVGEELNLIDKDQFALAWVVDFPMYEYNEDDKKVDFSHNPFSMPQGGMEALTSQDPLTIKAFQYDITCNGYEIASGGIRNHRPEAMVKAFEIAGYGEQEVVDRFGGMYRAFQYGAPPHGGMAAGVDRIVMLLCGTTNLREISLFPMNQRAEDLLMGAPSEVSPKQLRELHIRLNLPDTK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rhodobacter sphaeroides (strain ATCC 17029 / ATH 2.4.9)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.358 kDa
Sequence
MHAYRSHTCTELNAAHVGQEVRLSGWVHRVRDHGGVLFLDLRDHYGITQVIADADSPAFAELETVRAEWVIRIEGRVKARDASLVNPKLATGEIEVYATGMSVLGAADELPLPVFGETDYPEETRLTYRFLDLRREKLHQNMMLRSNVVRSLRNRMWGAGFNEFQTPIITASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLIMVAGFDRYFQIAPCFRDEDPRADRSPTDFYQLDIEMSFVEQEDVFAAVQPVIQGLFEEFGHGKRVDADWPRIAYRDAMLWYGSDKPDLRNPIKMQVVSEHFAGSGFAIFAKLLENEGTEIRAIPAPTGGSRKFCDRMNAFAQSQGLPGMGYIFWRKGDDGAMEAAGPLAKNIGPERTEAIRQQLGLGEGDAAFFLGGKPETFEAVAGRARTEIGRELGLTEENCFKFAWIVDFPMYEKDDEGKIDFSHNPFSMPQGGMEALEGDPLKVHAYQYDLACNGYELISGGIRNHKPEIMFKAFELAGYPKEEVEKRFGGMVKAFRYGAPPHGGCAAGIDRIVMLLADEANIREVIMFPMNQRAEDLLMGAPSEPTNEQLRELRLRVVPKD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rhodobacter sphaeroides (strain ATCC 17023 / 2.4.1 / NCIB 8253 / DSM 158)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.358 kDa
Sequence
MHAYRSHTCTELNAAHVGQEVRLSGWVHRVRDHGGVLFLDLRDHYGITQVIADADSPAFAELETVRAEWVIRIEGRVKARDASLVNPKLATGEIEVYATGMSVLGAADELPLPVFGETDYPEETRLTYRFLDLRREKLHQNMMLRSNVVRSLRNRMWGAGFNEFQTPIITASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLIMVAGFDRYFQIAPCFRDEDPRADRSPTDFYQLDIEMSFVEQEDVFAAVQPVIQGLFEEFGHGKRVDADWPRIAYRDAMLWYGSDKPDLRNPIKMQVVSEHFAGSGFAIFAKLLENEGTEIRAIPAPTGGSRKFCDRMNAFAQSQGLPGMGYIFWRKGDDGAMEAAGPLAKNIGPERTEAIRQQLGLGEGDAAFFLGGKPETFEAVAGRARTEIGRELGLTEENCFKFAWIVDFPMYEKDDEGKIDFSHNPFSMPQGGMEALEGDPLKVHAYQYDLACNGYELISGGIRNHKPEIMFKAFELAGYPKEEVEKRFGGMVKAFRYGAPPHGGCAAGIDRIVMLLADEANIREVIMFPMNQRAEDLLMGAPSEPTNEQLRELRLRVVPKD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rhodobacter sphaeroides (strain ATCC 17025 / ATH 2.4.3)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.275 kDa
Sequence
MHAYRSHTCAELNAGHVGQEVRLSGWVHRVRDHGGVLFIDLRDHYGITQVIADADSPAFAELETVRAEWVIRIEGRVKGRDAALVNPKLATGEIEVYATGLTVLGAADELPMPVFGEVDYPEETRLTYRFLDLRREKLHANMMLRSNVVRSLRNRMWDAGFNEFQTPIITASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLIMVAGFDRYFQIAPCFRDEDPRADRSPTDFYQLDVEMSFVEQEDVFRAVQPVIRGIFEEFGGGRRVDADWPRIAYRDAMLWYGSDKPDLRNPIKMQVVSEHFRGSGFAIFAKLLENEGTEIRAIPAPTGGSRKFCDRMNAFAQSQGLPGMGYIFWRKGDDGAMEAAGPLAKNIGPERTEAIRQQLGLGEGDAAFFLGGKPETFEAVAGRARNEIGRELGLTEENCFRFAWIVDFPMYEKDDEGKVDFSHNPFSMPQGGMAALEGDPLKVLAYQYDLACNGYELISGGIRNHKPEIMFKAFELAGYPASEVEKRFGGMVKAFRYGAPPHGGCAAGIDRIVMLLADEANIREVIMFPMNQRAEDLLMGAPSEPTNEQLRELRLRVVPKD

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shewanella amazonensis (strain ATCC BAA-1098 / SB2B)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.825 kDa
Sequence
MRSHYCGDVNKSHVGQEVTLVGWVNRSRDLGGVIFLDLRDREGLVQVVYDPDLPDVFDVASSLRAEFCVQVKGVVRPRPDSQVNSQMKTGEIEVLGKALTIINAADPLPLSLDNHQNNSEEARLKYRYLDLRRPEMAQRLIFRAKVTSFVRRFMDGNGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTSDQVMETTERMIRNLFLELMNVDLGDFPKMTWDEAMRRFGSDKPDLRNPLELVDVADLLKAVEFAVFSGPANDEEGRVAALRIPGGAELSRKQIDDYTKFVGIYGARGLAWMKVNNLAAGVEGIQSPVAKFLNEDIIKEIIARTKAADGDIIFFGADKANVVAESMGALRLKAGEDFKLLEGEWRPLWVVDFPMFEKADGRFYAVHHPFTAPRGVTAAELEASPGKAVSDAYDMVLNGVELGGGSVRIHNGDMQSTVFRILGIDDEEAKEKFGFLLDALRFGTPPHAGLAFGLDRLVMLMTGASSIRDVMAFPKTTTAACPLTNAPGHANPDQLVELGIAVLPKEPKQD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.327 kDa
Sequence
MLRSHAAGSLRSSDAGQQVTLAGWVARRRDHGGVIFIDLRDASGITQVVFRDPDVLKQAHRLRAEFCVAVTGLVEIRPEGNANPEIATGDIEVNASSLTVLGESAPLPFQLDEPAGEELRLKYRYLDLRRDAPASAIRLRSKVNAAAREVLDRHDFVEIETPTITRSTPEGARDFLVPARLHPGSFYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDMEMSFVDAEDVIAISEEILAALWALIGYDIPRPIPRISYADAMARYGSDKPDLRFGLELVECSEFFKDTTFRVFQAPYVGAVVMPGGASQPRRTLDGWQEWAKQRGAKGLAYVLVGEDGELGGPVAKNLSEAERAGLAGHVGAAPGDCIFFAAGPAKPSRALLGAARSEIAHRLGLIDPQAWAFVWVVDPPLFEPADDATAAGDVAVGSGAWTAVHHAFTAPKPGYEDAIETDTGNVLADAYDIVCNGNEIGGGSIRIHRRDIQERVFAVMGLDHAEAQEKFGFLLEAFTFGAPPHGGIAFGWDRINALLSRVDSIREVIAFPKTGGGVDPLTDAPAPITEQQRKESGIDVKPEPSKPH

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Actinobacillus pleuropneumoniae serotype 5b (strain L20)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.809 kDa
Sequence
MMRSHYCGALNRSHVGQTVTLSGWVHRVRNLGRFIFMQIRDREGIVQVFFDEKDEAIFKIASSLRSEACVQIQGEVIARDESQINKEMATGEIEVLVKNVVVYNNADVLPLDFNQNNTEEQRLKYRYLDLRRPEMAEKLKTRAKITSFVRRYMDDNGFLDIETPMLTKATPEGARDYLVPSRVHNGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFLTAEEVRELMENMIHGLWLDRLNVDLGKFPIMTWQEAMQRFGSDKPDLRNPLELVDVADILKDVEFKVFNEPANSADGRVTVLRVPNGASLTRKQIDEYTQFVGIYGAKGLAWAKINNVNAGMEGIQSPVAKFLNEEVFKALIERTNATSGDILFFGADKWQVVTDSMGALRLKVGRDLALTDLSAWKPLWVIDFPMFEKDDEGNLSAMHHPFTSPKNLTPEELAANPVNAVANAYDMVINGYEVGGGSVRIYDPKMQQTVFGILGINEQDQQEKFGFLLDALKFGTPPHAGLAFGLDRLTMLITGTENIRDVIAFPKTTAAACLMTEAPSFANPQALEELGIAVLKKEKAE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Actinobacillus pleuropneumoniae serotype 7 (strain AP76)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.81 kDa
Sequence
MMRSHYCGALNRSHVGQTVTLSGWVHRVRNLGRFIFMQIRDREGIVQVFFDEKDEAIFKIASSLRSEACVQIQGEVIARDESQINKEMATGEIEVLVKNVVVYNNADVLPLDFNQNNTEEQRLKYRYLDLRRPEMAEKLKTRAKITSFVRRYMDDNGFLDIETPMLTKATPEGARDYLVPSRVHNGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFLTAEEVRELMENMIHGLWLDRLNVDLGKFPIMTWQEAMQRFGSDKPDLRNPLELVDVADILKDVEFKVFNEPANSADGRVTVLRVPNGASLTRKQIDEYTQFVGIYGAKGLAWAKINDVNAGMEGIQSPVAKFLNEEVFKALIERTNATSGDILFFGADKWQVVTDSMGALRLKVGRDLALTDLSAWKPLWVIDFPMFEKDDEGNLSAMHHPFTSPKNLTPEELAANPVNAVANAYDMVINGYEVGGGSVRIYDPKMQQTVFGILGINEQDQQEKFGFLLDALKFGTPPHAGLAFGLDRLTMLITGTENIRDVIAFPKTTAAACLMTEAPSFANPQALEELGIAVLKKEKAE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Actinobacillus pleuropneumoniae serotype 3 (strain JL03)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.809 kDa
Sequence
MMRSHYCGALNRSHVGQTVTLSGWVHRVRNLGRFIFMQIRDREGIVQVFFDEKDEAIFKIASSLRSEACVQIQGEVIARDESQINKEMATGEIEVLVKNVVVYNNADVLPLDFNQNNTEEQRLKYRYLDLRRPEMAEKLKTRAKITSFVRRYMDDNGFLDIETPMLTKATPEGARDYLVPSRVHNGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFLTAEEVRELMENMIHGLWLDRLNVDLGKFPIMTWQEAMQRFGSDKPDLRNPLELVDVADILKDVEFKVFNEPANSADGRVTVLRVPNGASLTRKQIDEYTQFVGIYGAKGLAWAKINNVNAGMEGIQSPVAKFLNEEVFKALIERTNATSGDILFFGADKWQVVTDSMGALRLKVGRDLALTDLSAWKPLWVIDFPMFEKDDEGNLSAMHHPFTSPKNLTPEELAANPVNAVANAYDMVINGYEVGGGSVRIYDPKMQQTVFGILGINEQDQQEKFGFLLDALKFGTPPHAGLAFGLDRLTMLITGTENIRDVIAFPKTTAAACLMTEAPSFANPQALEELGIAVLKKEKAE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Aliivibrio fischeri (strain ATCC 700601 / ES114)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.828 kDa
Sequence
MRTHYCGNLNKSLAGQTVELCGWVNRRRDLGGLIFIDMRDREGIVQVVVDPDMKDVFEVASQLRNEFCIKFTGEVRVRPDSQVNKDMATGEVELLATGLEIINRSAALPLDFNQTNSEEQRLKYRYIDLRRPEMSDRIKLRARASSFVRRFLDENLFLDIETPVLTKATPEGARDYLVPSRVHKGSFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTSQEVRNVTERLVHDMWKELLDVELGQFPVMPFSEAMRRFGSDKPDLRNPLELVDVADLVKDVDFKVFSGPANDEKGRVAVIRVPGGASLSRKQIDEYGNFVGIYGAKGLAWMKVNDRAAGFEGVQSPVAKFLNEEVVNAILERTQAETGDIILFGADKAGIVSEAMGALRLKLGTDLELTDTSAWAPLWVVDFPMFEEDGEGNLHAMHHPFTSPLGVSAEELQANPAVANSDAYDMVINGYEVGGGSVRIHNAEMQTAVFGILGIEAKEQQEKFGFLLEALKYGTPPHAGLAFGLDRLAMLLCGTENIRDVIAFPKTTAAACLLTDAPSLANPASLEELAIAVKLAEKKDA

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Aliivibrio fischeri (strain MJ11)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.804 kDa
Sequence
MRTHYCGNLNKSLAGQTVELCGWVNRRRDLGGLIFIDMRDREGIVQVVVDPDMKDVFEVASQLRNEFCIKFTGEVRVRPDSQVNKDMATGEVELLATGLEIINRSAALPLDFNQTNSEEQRLKYRYIDLRRPEMSDRIKLRARASSFVRRFLDENLFLDIETPVLTKATPEGARDYLVPSRVHKGSFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTSQEVRNVTERLVHDMWKELLDVELGQFPVMPFSEAMRRFGSDKPDLRNPLELVDVADLVKDVDFKVFSGPANDEKGRVAVIRVSGGASLSRKQIDEYGNFVGIYGAKGLAWMKVNDRAAGFEGVQSPVAKFLNEEVINAILERTQAETGDIILFGADKAGIVSEAMGALRLKLGTDLELTDTSAWAPLWVVDFPMFEEDGEGNLHAMHHPFTSPLGVSAEELQANPAAANSDAYDMVINGYEVGGGSVRIHNAEMQTAVFGILGIEAQEQQEKFGFLLEALKYGTPPHAGLAFGLDRLAMLLCGTENIRDVIAFPKTTAAACLLTDAPSLANPASLEELAIAVKLAEKKDA

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Aliivibrio salmonicida (strain LFI1238)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.029 kDa
Sequence
MRSHYCGNLNKSLAGQTVELCGWVNRRRDLGGLIFIDMRDREGVVQVVVDPDMKDIFSTANQLRNEFCIKFTGEVRVRPDSQVNKDMSTGEVELYATGLEIINRSEALPLDFNQTNSEEQRLKYRYIDLRRPEMSDRIKLRARASSFVRRFLDENLFLDIETPVLTKATPEGARDYLVPSRVHKGSFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFLSSNQVRDITERLVHDMWKELLDVELGQFPIMKFSEAIRRFGSDKPDLRNPLELVDIADLLKDVEFQVFAGPANDEKGRVAVIRVPGGASLSRKQIDEYGKFVGIYGAKGLAWMKVNDRAAGLEGVQSPVAKFLNADVVNGILERTEAESGDIILFGADKANIVSEAMGALRIKLGDDLELTDKKAWAPLWVIDFPMFEEDGEGNLHAMHHPFTSPLGMTAEELKVNPAAANSDAYDMVINGYEVGGGSVRIHNAEMQTAVFGILGIEAKEQQEKFGFLLEALKYGTPPHAGLAFGLDRLAMLLCGTENIRDVIAFPKTTAAACLLTNAPSPANPDSLAELAIAVKFAEKKDA

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shewanella frigidimarina (strain NCIMB 400)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.699 kDa
Sequence
MRSHYCGDINQSHLGQEVTLVGWVNRSRDLGGVVFLDLRDREGLVQVVYDPDLKDVFEMASTLRSEFCVQIKGVVRARPESQINSQMKTGEIEILGKQLTIINASAPLPLSMDNYQNNSEEQRLKYRYLDLRRPEMAERLIFRAKVTSSVRRFLDGNGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMSAEQVMEKTEQMMRGLFQDLLNVDLGDFPRMTYAEAMKRYGSDKPDLRNPLELVDIADLVKDVEFAVFNGPANDVEGRVAALRIPTGASLSRKQIDDYTKFAGIYGAKGLAWMKINDLAAGMDGIQSPVLKFLTESIVNDIISRTGAQTGDIILFGADKANVVAEALGALRLKAGEDFKLLEGEWRPMWVVDFPMFEKINGGFHAVHHPFTAPRGISPAELAADPAAAISDAYDMVLNGCELGGGSVRIHNAEMQSTVFSILGIEAEEAQEKFGFLLEALRYGTPPHAGLAFGLDRIIMLMTGASSIRDVMAFPKTTTAACPLTNAPGFANPVQLTELGIAVIEKVKTEE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shewanella oneidensis (strain MR-1)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.076 kDa
Sequence
MRSHYCGDVNKSHVGQEVTLVGWVNRSRDLGGVVFLDLRDREGLVQVVYDPDLPEVFNVASTLRAEFCVQVKGVVRARPDSQVNAQMKTGEIEVLGKALTIINSSEPLPLSLDNYQNNSEEQRLKYRYLDLRRPEMAQRLMFRAKVTSAVRRFLDSNGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTSEQVMNKTEEMMRGLFLEMLNVDLGEFPRMTYNEAMRRFGSDKPDLRNPLELVDVADLLKDVEFAVFSGPANDEEGRVAALRIPGGASLSRKQIDDYTKFVGIYGAKGLAWMKLNDLTQGLEGIQSPVLKFLNENIVNEIINRTGAQTGDIILFGADQATVVAESMGALRLKAGEDFNLLEGQWRPLWVVDFPMFEKINGSFHAVHHPFTAPRGVTPQELEANPANRVSDAYDMVLNGCELGGGSVRIHNQEMQSAVFRILGITDEEAKEKFGFLLEALRYGTPPHAGLAFGLDRIIMLMTGASSIRDVMAFPKTTTAACPLTNAPGFANPQQLAELGIAVVKTAKTED

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shewanella sp. (strain ANA-3)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.992 kDa
Sequence
MRSHYCGDVNKSHVGQEVTLVGWVNRSRDLGGVVFLDLRDREGLVQVVYDPDLPEVFNVASTLRAEFCVQVKGVVRARPDSQVNAQMKTGEIEVLGKELTIINSSEPLPLSLDNYQNNSEEQRLKYRYLDLRRPEMAQRLMFRAKVTSAVRRFLDSNGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTSEQVMAKTEEMMRGLFLEMLNVDLGEFPRMTYNEAMRRFGSDKPDLRNPLELVDVADLLKEVEFAVFSGPANDEEGRVAALRIPGGASLSRKQIDDYTKFVGIYGAKGLAWMKLNDLTQGLEGIQSPVLKFLNEGIVNEIISRTGAQTGDIILFGADNATVVAESMGALRLKAGEDFNLLEGQWRPLWVVDFPMFEKINGSFHAVHHPFTAPRGVTPQELEANPANRVSDAYDMVLNGCELGGGSVRIHNQEMQSAVFRILGITDEEAKEKFGFLLEALRYGTPPHAGLAFGLDRIIMLMTGASSIRDVMAFPKTTTAACPLTNAPGFANPQQLAELGISVVKAAKTED

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shewanella sp. (strain MR-4)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.063 kDa
Sequence
MRSHYCGDVNKSHVGQEVTLVGWVNRSRDLGGVVFLDLRDREGLVQVVYDPDLPEVFNVASTLRAEFCVQVKGLVRARPNSQVNAQMKTGEIEVLGKELTIINSSEPLPLSLDNYQNNSEEQRLKYRYLDLRRPEMAQRLMFRAKVTSAVRRFLDSNGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTSEQVMAKTEEMMRGLFLEMLNVDLGEFPRMTYNEAMRRFGSDKPDLRNPLELVDVADLLKEVEFAVFSGPANDEEGRVAALRIPGGASLSRKQIDDYTKFVGIYGAKGLAWMKLNDLTQGLEGIQSPVLKFLNEDIVNEIISRTGAQTGDIILFGADNATVVAESMGALRLKAGEDFNLLEGQWRPLWVVDFPMFEKINGSFHAVHHPFTAPRGVTPQELEANPANRVSDAYDMVLNGCELGGGSVRIHNQEMQSAVFRILGITDEEAKEKFGFLLEALRYGTPPHAGLAFGLDRIIMLMTGASSIRDVMAFPKTTTAACPLTNAPGFANPQQLAELGISVVKAAKTED

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shewanella sp. (strain MR-7)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.989 kDa
Sequence
MRSHYCGDVNKSHVGQEVTLVGWVNRSRDLGGVVFLDLRDREGLVQVVYDPDLPEVFNVASTLRAEFCVQVKGVVRARPDSQVNAQMKTGEIEVLGKELTIINSSEPLPLSLDNYQNNSEEQRLKYRYLDLRRPEMAQRLMFRAKVTSAVRRFLDSNGFLDIETPILTKATPEGARDYLVPSRTYKGQFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTSEQVMAKTEEMMRGLFLEMLNVDLGEFPRMTYNEAMRRFGSDKPDLRNPLELVDVADLLKNVEFAVFSGPANDEEGRVAALRIPGGASLSRKQIDDYTKFVGIYGAKGLAWMKLNDLTQGLEGIQSPVLKFLNEGIVNEIISRTGAQTGDIILFGADNAIVVAESMGALRLKAGEDFNLLEGQWRPLWVVDFPMFEKINGSFHAVHHPFTAPRGVTPQELEANPANRVSDAYDMVLNGCELGGGSVRIHNQEMQSAVFRILGITDEEAKEKFGFLLEALRYGTPPHAGLAFGLDRIIMLMTGASSIRDVMAFPKTTTAACPLTNAPGFANPQQLAELGISVVKAAKTED

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Azotobacter vinelandii (strain DJ / ATCC BAA-1303)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.029 kDa
Sequence
MMRSHYCGQLNESLEGQEVTLCGWVHRRRDHGGVIFLDIRDREGLAQVVFDPDRAETFAKADRVRSEYVVRITGKVRPRPAGAVNPNMASGAIEVLGYELDVLNQAETPPFPLDEYSDVGEETRLRYRFIDLRRPEMAAKLKLRSSITSSIRRYLDENGFLDVETPILTRATPEGARDYLVPSRTHAGSFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLDEADIMGITENMIRKLFKEVLDVEFGELPHMTFEEAMRRYGSDKPDLRIPLELVDVADQLKAVEFKVFSGPANDPKGRVAALRVPGAASMPRSQIDDYTRFVGIYGAKGLAYIKVNERAKGVEGLQSPIVKFIPKENLDVILDRVGAVDGDIVFFGADKAKIVSEALGALRIRLGHDLKLLTCEWAPLWVVDFPMFEENDDGSLSALHHPFTAPKCTPEELAANPAVALSRAYDMVLNGTELGGGSIRIHRKEMQQAVFRILGIDEAEQQEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMTGASSIREVIAFPKTQSAACVMTQAPGAVDAKALRELHIRLREQPKAE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bacillus anthracis (strain A0248)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.294 kDa
Sequence
MAERTHACGKVTVEAVGQTVQLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPETSKEALEVAETIRSEYVLHVEGTVVERGEGAINDNMATGRIEVQATKVSVLNAAKTTPIIIADDTDASEDVRLKYRYLDLRRPVMFNTFKMRHDVTKTIRNFLDTEEFLEVETPILTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMVGGFERYYQVARCFRDEDLRADRQPEFTQIDIEASFLTQDEILDMMERMMTKVMKDAKGVEVSAPFPRMKYADAMARYGSDKPDTRFEMELTDLSEFAAGCGFKVFTSAVESGGQVKAINAKGAASKYSRKDIDALTEFVKVYGAKGLAWLKVEEDGLKGPIAKFFGEEDASVLMNTLEATAGDLLLFVADKKSVVADSLGALRLRLGKELELIDESKFNFLWVTDWPLLEYDEDADRYFAAHHPFTMPFREDVELLETAPEKARAQAYDLVLNGYELGGGSLRIYERDVQEKMFKALGFSQEEAQEQFGFLLEAFEYGTPPHGGIALGLDRLVMLLAGRTNLRDTIAFPKTASASCLLTEAPSPVAEAQLEELNLKLNVKEEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bacillus anthracis (strain CDC 684 / NRRL 3495)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.291 kDa
Sequence
MAERTHACGKVTVEAVGQTVQLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPETSKEALEVAETIRSEYVLHVEGTVVERGEGAINDNMATGRIEVQATKVSVLNAAKTTPIIIADDTDASEDVRLKYRYLDLRRPVMFNTFKMRHDVTKTIRNFLDTEEFLEVETPILTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMVGGFERYYQVARCFRDEDLRADRQPEFTQIDIEASFLTQDEILDMMERMMTKVMKDAKGVEVSAPFPRMKYADAMARYGSDKPDTRFEMELTDLSEFAAGCGFKVFTSAVESGGQVKAINAKGAASKYSRKDIDALTEFVKVYGAKGLAWLKVEEDGLKGPIAKFFGEEDASVLKNTLEATAGDLLLFVADKKSVVADSLGALRLRLGKELELIDESKFNFLWVTDWPLLEYDEDADRYFAAHHPFTMPFREDVELLETAPEKARAQAYDLVLNGYELGGGSLRIYERDVQEKMFKALGFSQEEAQEQFGFLLEAFEYGTPPHGGIALGLDRLVMLLAGRTNLRDTIAFPKTASASCLLTEAPSPVAEAQLEELNLKLNVKEEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bacillus thuringiensis (strain Al Hakam)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.348 kDa
Sequence
MAERTHACGKVTVEAVGQTVQLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPETSKEALEVAETIRSEYVLHVEGTVVERGEGAINDNMATGRIEVQATKVNVLNAAKTTPIIIADDTDASEDVRLKYRYLDLRRPVMFNTFKMRHDVTKTIRNFLDTEEFLEVETPILTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMVGGFERYYQVARCFRDEDLRADRQPEFTQIDIEASFLTQDEILDMMERMMTKVMKDAKGVEVSAPFPRMKYADAMARYGSDKPDTRFEMELTDLSEFAAGCGFKVFTSAVESGGQVKAINAKGAASKYSRKDIDALTEFVKVYGAKGLAWLKVEEDGLKGPIAKFFGEEDANVLMNTLEATAGDLLLFVADKKSVVADSLGALRLRLGKELELIDESKFNFLWVTDWPLLEYDEDADRYFAAHHPFTMPFREDVELLETAPEKARAQAYDLVLNGYELGGGSLRIYERDVQEKMFKALGFSQEEAQEQFGFLLEAFEYGTPPHGGIALGLDRLVMLLAGRTNLRDTIAFPKTASASCLLTEAPSPVAEAQLEELNLKLNVKEEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bacillus anthracis
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.294 kDa
Sequence
MAERTHACGKVTVEAVGQTVQLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPETSKEALEVAETIRSEYVLHVEGTVVERGEGAINDNMATGRIEVQATKVSVLNAAKTTPIIIADDTDASEDVRLKYRYLDLRRPVMFNTFKMRHDVTKTIRNFLDTEEFLEVETPILTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMVGGFERYYQVARCFRDEDLRADRQPEFTQIDIEASFLTQDEILDMMERMMTKVMKDAKGVEVSAPFPRMKYADAMARYGSDKPDTRFEMELTDLSEFAAGCGFKVFTSAVESGGQVKAINAKGAASKYSRKDIDALTEFVKVYGAKGLAWLKVEEDGLKGPIAKFFGEEDASVLMNTLEATAGDLLLFVADKKSVVADSLGALRLRLGKELELIDESKFNFLWVTDWPLLEYDEDADRYFAAHHPFTMPFREDVELLETAPEKARAQAYDLVLNGYELGGGSLRIYERDVQEKMFKALGFSQEEAQEQFGFLLEAFEYGTPPHGGIALGLDRLVMLLAGRTNLRDTIAFPKTASASCLLTEAPSPVAEAQLEELNLKLNVKEEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bacillus cereus (strain AH820)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.348 kDa
Sequence
MAERTHACGKVTVEAVGQTVQLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPETSKEALEVAETIRSEYVLHVEGTVVERGEGAINDNMATGRIEVQATKVNVLNAAKTTPIIIADDTDASEDVRLKYRYLDLRRPVMFNTFKMRHDVTKTIRNFLDTEEFLEVETPILTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMVGGFERYYQVARCFRDEDLRADRQPEFTQIDIEASFLTQDEILDMMERMMTKVMKDAKGVEVSAPFPRMKYADAMARYGSDKPDTRFEMELTDLSEFAAGCGFKVFTSAVESGGQVKAINAKGAASKYSRKDIDALTEFVKVYGAKGLAWLKVEEDGLKGPIAKFFGEEDANVLMNTLEATAGDLLLFVADKKSVVADSLGALRLRLGKELELIDESKFNFLWVTDWPLLEYDEDADRYFAAHHPFTMPFREDVELLETAPEKARAQAYDLVLNGYELGGGSLRIYERDVQEKMFKALGFSQEEAQEQFGFLLEAFEYGTPPHGGIALGLDRLVMLLAGRTNLRDTIAFPKTASASCLLTEAPSPVAEAQLEELNLKLNVKEEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bacillus cereus (strain ATCC 10987 / NRS 248)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.339 kDa
Sequence
MAERTHACGKVTVEAVGQTVQLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPETSKEALEVAETIRSEYVLHVEGTVVERGEGAINDNMATGRIEVQATKVNVLNAAKTTPIIIADDTDASEDVRLKYRYLDLRRPVMFNTFKMRHDVTKTIRNFLDTEEFLEVETPILTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMVGGFERYYQVARCFRDEDLRADRQPEFTQIDIEASFLTQEEILDMMERMMTKVMKDAKGVEISAPFPRMTYADAMARYGSDKPDTRFEMELTDLSEFAAGCGFKVFTSAVESGGQVKAINAKGAASKYSRKDIDALTEFVKVYGAKGLAWLKVEEDGLKGPIAKFFGEEDANVLMTTLEATAGDLLLFVADKKSVVADSLGALRLRLGKELELIDESKYNFLWVTDWPLLEYDEDADRYFAAHHPFTMPFREDVELLETAPEKARAQAYDLVLNGYELGGGSLRIYERDVQEKMFKALGFSQEEAQEQFGFLLEAFEYGTPPHGGIALGLDRLVMLLAGRTNLRDTIAFPKTASASCLLTEAPSPVAEAQLEELNLKLSLKEEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bacillus cereus (strain G9842)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.322 kDa
Sequence
MAERTHACGKVTVEAVGQTVQLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPETSKEALEVAETIRSEYVLHVEGTVVERGEGAINDNMATGRIEVQATKVNVLNAAKTTPIIIADDTDASEDVRLKYRYLDLRRPVMFNTFKMRHDVTKTIRNFLDTEEFLEVETPILTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMVGGFERYYQVARCFRDEDLRADRQPEFTQIDIEASFLTQDEILDMMERMMTKVMKDAKGVEVSAPFPRMKYADAMARYGSDKPDTRFEMELTDLSEFAAGCGFKVFTSAVESGGQVKAINAKGAASKYSRKDIDALTEFVKVYGAKGLAWLKVEEDGLKGPIAKFFGEEDANVLMTTLEATAGDLLLFVADKKSVVADSLGALRLRLGKELELIDESKFNFLWVTDWPLLEYDEDADRYFAAHHPFTMPFREDVELLETAPEKARAQAYDLVLNGYELGGGSLRIYERDVQEKMFKALGFSQEEAQEQFGFLLEAFEYGTPPHGGIALGLDRLVMLLAGRTNLRDTIAFPKTASASCLLTEAPSPVAEAQLEELNLKLSLKEEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bacillus cereus (strain 03BB102)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.348 kDa
Sequence
MAERTHACGKVTVEAVGQTVQLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPETSKEALEVAETIRSEYVLHVEGTVVERGEGAINDNMATGRIEVQATKVNVLNAAKTTPIIIADDTDASEDVRLKYRYLDLRRPVMFNTFKMRHDVTKTIRNFLDTEEFLEVETPILTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMVGGFERYYQVARCFRDEDLRADRQPEFTQIDIEASFLTQDEILDMMERMMTKVMKDAKGVEVSAPFPRMKYADAMARYGSDKPDTRFEMELTDLSEFAAGCGFKVFTSAVESGGQVKAINAKGAASKYSRKDIDALTEFVKVYGAKGLAWLKVEEDGLKGPIAKFFGEEDANVLMNTLEATAGDLLLFVADKKSVVADSLGALRLRLGKELELIDESKFNFLWVTDWPLLEYDEDADRYFAAHHPFTMPFREDVELLETAPEKARAQAYDLVLNGYELGGGSLRIYERDVQEKMFKALGFSQEEAQEQFGFLLEAFEYGTPPHGGIALGLDRLVMLLAGRTNLRDTIAFPKTASASCLLTEAPSPVAEAQLEELNLKLNVKEEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bacillus cereus (strain B4264)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.308 kDa
Sequence
MAERTHACGKVTVEAVGQTVQLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFNPETSKEALEVAETIRSEYVLHVEGTVVERGEGAINDNMATGRIEVQATKVNVLNAAKTTPIIIADDTDASEDVRLKYRYLDLRRPVMFNTFKMRHDVTKTIRNFLDTEEFLEVETPILTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMVGGFERYYQVARCFRDEDLRADRQPEFTQIDIEASFLTQDEILDMMERMMTKVMKDAKGVEVSAPFPRMKYADAMARYGSDKPDTRFEMELTDLSEFAAGCGFKVFTSAVESGGQVKAINAKGAASKYSRKDIDALTEFVKVYGAKGLAWLKVEEDGLKGPIAKFFGEEDANVLMSTLEATAGDLLLFVADKKSVVADSLGALRLRLGKELELIDESKFNFLWVTDWPLLEYDEDADRYFAAHHPFTMPFREDVELLETAPEKARAQAYDLVLNGYELGGGSLRIYERDVQEKMFKALGFSQEEAQEQFGFLLEAFEYGTPPHGGIALGLDRLVMLLAGRTNLRDTIAFPKTASASCLLTEAPSPVAEAQLEELNLKLSLKEEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.283 kDa
Sequence
MMRSHYCGQLNESLEGQEITLCGWVHRRRDHGGVIFLDIRDREGMAQVVFDPDRADSFAAADRVRSEYVVKVVGKVRARPAGAVNANMASGAIEVLGYELEVLNESETPPFPLNEYSDVGEETRLRYRFIDLRRPEMAEKLRLRSRITTSIRRYLDDSGFLDVETPILTRATPEGARDYLVPSRTHPGSFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDIETSFLNEEDIIGLTEKMVRQLFKEVLDLEFGDFPHMTFEEAMRRYGSDKPDLRNPLELVDVADQLTGVEFKVFSGPANDPKGRVAALRVPGAASMARSQIDDYTKFVSIYGAKGLAYIKVNERAKGPEGLQSPIVKFIPEDNLNVILDRVGAVDGDIVFFGADKFKIVSEALGALRIKIGNDLKLHTCEWAPMWVVDFPMFEENDDGSFTALHHPFTAPKCTPEELEANPATALSRAYDMVLNGTELGGGSIRIHRKEMQQAVFRLLGIAEDEQQEKFGFLLDALKYGAPPHGGLAFGLDRLVMLMAGAQSIREVIAFPKTQSAADVMTQAPGVVDAKALRELHIRLREQPKAE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Edwardsiella ictaluri (strain 93-146)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.506 kDa
Sequence
MRTNYCGQLNLSHVGQEVTLCGWVHRRRDLGGLIFIDLRDREGVVQVFFDPDHQDAFRQASELRNEFCVQVTGTVRARPESQRNSEMPTGEIEVFGHGLTLINRAEPLPLDFNQTNSEENRLKYRYLDLRRPEMAARLKTRAKITAFVRRFMDNHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMSAGQVREIMEALARALWMEIKGVDLGDFPVMTFAEAMRRFGSDKPDLRNPLELVDVADLVKSVDFKVFSGPANDARGRVIALRVPGGATLTRKNIDEYGQFVGIYGAKGLAWMKVNDRAAGMDGVQSPIAKFLNAEVLEGILARSGAQSGDIIFFGADSAKVATDAMGALRLKVGRDLQLTDESRWAPLWVVDFPMFEEDGEGGLAAMHHPFTSPRDISPEALKANPVGAIANAYDMVMNGYEVGGGSVRIHSGAMQSAVFDILGINEQEQREKFGFLLDALKFGTPPHAGLAFGLDRLVMLLTGTENIRDVIAFPKTTAAACPLTDAPSRANPAALQELSIAVCAKQGSDA

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.769 kDa
Sequence
MRSHYCGHLNKSLVGQTVELCGWVNRRRDLGGLIFIDMRDREGIVQVVVDPDMADVFAVANQLRSEFCIKLTGEVRARPESQVNKEMATGEVELLARSLEIINRSDVLPLDFNQKNSEEQRLKYRYLDLRRPEMSDRIKLRAKASSFVRRFLDTHGFLDIETPVLTKATPEGARDYLVPSRVHKGSFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTAEQVRAVTEKMIREMWLELLNVDLGDFPIMPYSEAMRRFGSDKPDLRNPMELVDVADLLKDVDFKVFSGPANDPKGRVAALCIPGGAALTRKQIDEYTAFVAIYGAKGLAWLKVNDLAAGMEGIQSPVAKFLTEEIIQAIIERTQAQTGDIILFGADSAKVVAEALGALRLKAGKELGITNESAWAPLWVVDFPMFESDDEGNVAAMHHPFTSPLNLSPEQLKANPEEALSNAYDMVLNGYEVGGGSVRIHNAEMQSAVFDILGITPEEQRLKFGFLLDALKFGTPPHAGLAFGLDRLVMLLCGTENIRDVIAFPKTTAAACLMTDAPSLANPAALEELAIAVKLATKDKA

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.769 kDa
Sequence
MRSHYCGHLNKSLVGQTVELCGWVNRRRDLGGLIFIDMRDREGIVQVVVDPDMADVFAVANQLRSEFCIKLTGEVRARPESQVNKEMATGEVELLARSLEIINRSDVLPLDFNQKNSEEQRLKYRYLDLRRPEMSDRIKLRAKASSFVRRFLDTHGFLDIETPVLTKATPEGARDYLVPSRVHKGSFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTAEQVRAVTEKMIREMWLELLNVDLGDFPIMPYSEAMRRFGSDKPDLRNPMELVDVADLLKDVDFKVFSGPANDPKGRVAALCIPGGAALTRKQIDEYTAFVAIYGAKGLAWLKVNDLAAGMEGIQSPVAKFLTEEIIQAIIERTQAQTGDIILFGADSAKVVAEALGALRLKAGKELGITNESAWAPLWVVDFPMFESDDEGNVAAMHHPFTSPLNLSPEQLKANPEEALSNAYDMVLNGYEVGGGSVRIHNAEMQSAVFDILGITPEEQRLKFGFLLDALKFGTPPHAGLAFGLDRLVMLLCGTENIRDVIAFPKTTAAACLMTDAPSLANPAALEELAIAVKLATKDKA

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Vibrio cholerae serotype O1 (strain M66-2)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.769 kDa
Sequence
MRSHYCGHLNKSLVGQTVELCGWVNRRRDLGGLIFIDMRDREGIVQVVVDPDMADVFAVANQLRSEFCIKLTGEVRARPESQVNKEMATGEVELLARSLEIINRSDVLPLDFNQKNSEEQRLKYRYLDLRRPEMSDRIKLRAKASSFVRRFLDTHGFLDIETPVLTKATPEGARDYLVPSRVHKGSFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTAEQVRAVTEKMIREMWLELLNVDLGDFPIMPYSEAMRRFGSDKPDLRNPMELVDVADLLKDVDFKVFSGPANDPKGRVAALCIPGGAALTRKQIDEYTAFVAIYGAKGLAWLKVNDLAAGMEGIQSPVAKFLTEEIIQAIIERTQAQTGDIILFGADSAKVVAEALGALRLKAGKELGITNESAWAPLWVVDFPMFESDDEGNVAAMHHPFTSPLNLSPEQLKANPEEALSNAYDMVLNGYEVGGGSVRIHNAEMQSAVFDILGITPEEQRLKFGFLLDALKFGTPPHAGLAFGLDRLVMLLCGTENIRDVIAFPKTTAAACLMTDAPSLANPAALEELAIAVKLATKDKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Mycobacterium avium (strain 104)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.3 kDa
Sequence
MLRSHAAGSLRSSDAGQQVTLAGWVARRRDHGGVIFIDLRDASGITQVVFRDPDVLKQAHRLRAEFCVAVAGLVEIRPEGNANPEIATGDIEVNASSLTVLGESAPLPFQLDEPAGEELRLKYRYLDLRRDAPAAAIRLRSKVNAAAREVLDRHDFVEIETPTITRSTPEGARDFLVPARLHPGSFYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDMEMSFVDAEDVIAISEEILAALWALIGYEIPRPIPRISYADAMARYGSDKPDLRFGLELVECSEFFKDTTFRVFQAPYVGAVVMPGGASQPRRTLDGWQEWAKQRGAKGLAYVLVGEDGELGGPVAKNLSEAERAGLAGHVGAAPGDCIFFAAGPAKPSRALLGAARSEIAHRLGLIDPQAWAFVWVVDPPLFEPADDATAAGDVAVGSGAWTAVHHAFTAPKPGYEDAIETDTGNVLADAYDIVCNGNEIGGGSIRIHRRDIQERVFAVMGLDNAEAREKFGFLLEAFTFGAPPHGGIAFGWDRINALLSRVDSIREVIAFPKTGGGVDPLTDAPAPITEQQRKESGIDVKPEPSKPH

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Lactobacillus fermentum (strain NBRC 3956 / LMG 18251)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.935 kDa
Sequence
MKRTNYAGRTSEEQIGQEVVVKGWVAKRRNLGGLIFIDLWDREGIVQLVFNEEEDQAAFEVANQARNQYILEARGLVRARAEVNPDIATGKIEIEVKEAKILAKSQTPPFEVQDDVDASEDLRLKYRYVDLRRPKMMNYLKLRSKVTSIVHNYFDNNDFLDVETPELTRSTPEGARDYIVPSRVYPGHFYALPQSPQLFKQLLMAAGVDKYYQIAKCFRDEDLRGDRQPEFTQIDTEMSFAEPEEIQAMAEGLIKRVMKEAVGVDVPTPFPRMEWQEAMDKYGSDKPDTRFDMLIQDVSDLVKDSSFKVFSATVADGNFVRAIVVPGGADKYSRKDITKKEDYIKRYGAKGLAWVKVTEEGYNGPVAKFLNDDANALNERLSAKVGDLVLFVAGSFHVVCDSLGYLRESIAKELDLIDENKFNYLWVINWPMFEYDEGFGKWIAAHHPFTMLNEDDLKYLEEGEDPHQAHAQSYDIVLNGNEIGGGSIRIHDPEVQEKVFKALGYTKEAAQARFGFLIKALENGMPPEGGMAFGLDRWVMLLAHADSIRDVIAFPKNSKAVEPLTAAPGTVDDEQLEVLHLNVEEAPKEAE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Paracoccus denitrificans (strain Pd 1222)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.11 kDa
Sequence
MSAYRSHTCGELTAAAAGSEIRLSGWVHRVRDHGGVLFIDLRDHYGITQVIADSDSLAFAALEKLRAETVIRIDGRVKLRDPSLVNPKLPTGEIEVYATAMEVLGAADDLPLPVFGDQDYPEETRLTYRFLDLRRESLHNNIMLRSRVVKWLRDAMWDQGFTEFQTPIITASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLIMVAGFDKYFQIAPCFRDEDPRADRSPTDFYQLDLEMSFVEQEDVFRAIQPVIQGLFEEFGGGRRVDTDWPRIPYAEAMLKYGSDKPDLRNPIEMQVVSDHFRGSGFAIFAKLLEQDGTEVRAIPAPGGGSRKFADRMNAFAQGQGLPGMGYIFWRKAEDGTTEAAGPIAKALGPEKTEAIRTQLGLGEGDAAFFLGGKPETFEAVAGRARNEIGRELGLIDENQFKFAWIVDFPMYEKGEDGRIDFSHNPFSMPQGGLDALEGDPLAVMGYQYDLACNGYELVSGAIRNHRPEIMFRAFELAGYGRDEVEKRFGGMVKAFRYGAPPHGGCAAGIDRIVMLLADEVNIREVIMFPMNQRAEDLMMGAPSEPTNEQLRELRLRVLPRE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Oceanobacillus iheyensis (strain DSM 14371 / CIP 107618 / JCM 11309 / KCTC 3954 / HTE831)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.933 kDa
Sequence
MSERLMAGRLNEKNIGEKVLLKGWVQKRRDLGGLIFIDLRDKSGLIQVVFNPDHSKKALETAENIRSEYVIEINGTVVARDEATINPSMKTGKIEVNASSVQILNKAKTPPFTIQDETDVSEDVRLKYRYLDLRRNSLQETFRLRHQTTQSIRNYLNDKDFLEMETPILTKSTPEGARDYLVPSRVHPGEFYALPQSPQLFKQLIMMGGFERYYQIARCFRDEDLRADRQPEFTQIDIETSFLTSDEIMDMTEHMMKKVMKEVKDIDISLPLPRMPYQEAMDRYGSDKPDTRFDLELIHVSDIVASSGFKVFSQAVDNGGKVALLNIKGKADNYSRKDIDKLTEYVKVYDAKGLAWLKADESELKGPIAKFLSEEEVAGIRDRANVEQGDLLLFVADKTNVVYDSLGALRLYLGKELGLIDESKFHFLWVTDWPLLEYDEGLGRYFAAHHPFTSAIEEDLDKLETDPASVRANAYDLVLNGFELGGGSIRIHQKEQQDQMFKVLGFSEEEARSQFGFLLDALEYGAPPHGGIALGLDRIIMLLAGRSNLRDTILFPKTASASDLMTAAPSGVSDDQLQELSIQLQSGEKNQ

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rhodobacter sphaeroides (strain KD131 / KCTC 12085)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.372 kDa
Sequence
MHAYRSHTCTELNAAHVGQEVRLSGWVHRVRDHGGVLFLDLRDHYGITQVIADADSPAFAELETVRAEWVIRIEGRVKARDASLVNPKLATGEIEVYATGMSVLGAADELPLPVFGETDYPEETRLTYRFLDLRREKLHQNMMLRSNVVRSLRNRMWGAGFNEFQTPIITASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLIMVAGFDRYFQIAPCFRDEDPRADRSPTDFYQLDIEMSFVEQEDVFAAVQPVIQGLFEEFGHGKRVEADWPRIAYRDAMLWYGSDKPDLRNPIKMQVVSEHFAGSGFAIFAKLLENEGTEIRAIPAPTGGSRKFCDRMNAFAQSQGLPGMGYIFWRKGDDGAMEAAGPLAKNIGPERTEAIRQQLGLGEGDAAFFLGGKPETFEAVAGRARTEIGRELGLTEENCFKFAWIVDFPMYEKDDEGKIDFSHNPFSMPQGGMEALEGDPLKVHAYQYDLACNGYELISGGIRNHKPEIMFKAFELAGYPKEEVEKRFGGMVKAFRYGAPPHGGCAAGIDRIVMLLADEANIREVIMFPMNQRAEDLLMGAPSEPTNEQLRELRLRVVPKD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Roseobacter denitrificans (strain ATCC 33942 / OCh 114)
Length
591 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.357 kDa
Sequence
MHMYRSHTCADLSAQDVGKTVRLSGWVHRVRDHGGVLFIDLRDHYGITQVLCDPDSPVFEQMEQVRAEWCIRVDGVVKARDASLINPKISTGEIELFVKDLEVLGASEELPLQVFGDQEYPEETRLKYRYLDLRRANMQANMKLRSDVVASLRQQMWKADFREFQTPIITASSPEGARDFLVPSRLHPGRFYALPQAPQQFKQLLMVSGFDKYFQIAPCFRDEDPRADRSPTDFYQLDIEMSFVTQQDVFDVIQPVLTQVFEQFGNGKAVDQEWPQISYKDAALWYGSDKPDLRNPIKMQSVSEHFAGSGFAIFANLLEQEGTEIRAIPAPGGGSRKFCDRMNAFAQKEGLPGMGYIFWRDQGAGMEAAGPLAKNIGPERTEAIRQQLGLGVGDAAFFLGGKPKAFETVAGKARNHIGMELGLTDQNRFAFAWIVDFPIYEKDSETGRIDFEHNPFSMPQGGLEALQGDPLSVVGYQYDLSCNGYELVSGAIRNHKPEIMFKAFEIAGYGEDEVRKRFGGMVNAFQYGAPPHGGCAAGIDRIVMLLAEEANIREVILFPMNQRAEDLMMSAPSEPESEQLMELGLRVIPKD

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / NCDO 523)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.71 kDa
Sequence
MKRTNYAGLIDETYLNQTVTLTGWVQKRRDFGDLIFVDLRDREGIVQLTFNATNADALAVAEKVRSEYVLKITGHVIERAENQINTKIKSGTIEVDVTEAEILSTSKTPPFYIEDDVNANEELKLQYRYLDLRRPEMQKNLRIRSKIMSSAMHFMDTHDFINIETPVLAKSTPEGARDYLVPSRVFPGSFYALPQSPQLFKQLLMGAGFDRYFQIARAFRDEDLRGDRQPEFTQMDVETSFMTADEIRELVNAWVKAMMHDVVDFDLDTAEIPTLTWQESMDRFGTDKPDLRIAYEIKDLSETVKNSEFGVFANAIKGGGVVKALAVPGGADHYSRKDIDKLTKYIERFGAKGLAWMKVAPEGLTGPIAKFFDDEAQAALIASADAQVGDLLLFGAGRADVVSATLDYLRRETAKALDLIDQTNPWAFAWIVDWPLFEYSEDFDRWIAAHHPFTMPNEEDLHYLNDGEDPHKAHAQSYDLVLNGYELGSGSIRIHRMDIQEKMLKALGFTPEKAHEAFGFLLEGMEYGFPPMGGIALGLDRLAMLLAGQENIREVIAFPKNSRATEPMTEAPTRVEGKQLNELGLFVPEAE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.375 kDa
Sequence
MEKRTSYCGELNETHIGQSVILHGWVQKRRDLGGLIFIDLRDREGIVQVVFNPEFSKEALEIADSVRNEFVVTIKGKVHARGEKAINDKLATGKVEVLAEEITILNTSKTPPFYIEDGVNVSDELRLKYRYLDLRRPEMNNIFKMRHTVTRTFRNKLDALGFFDIETPYLTKSTPEGARDYLVPSRVYPGNFYALPQSPQILKQLLMTAGFDKYYQIVRCFRDEDLRGDRQPEFTQIDLETSFLTKEEIQAITEDMLVDVVKEAKNITIEKPFPRMTYKEAMDRFGSDKPDIRFGLELQNVSEVVKDVDFKVFQSAIENGGEVKAINAKAAATNFSRKDLDALGVFVANYGAKGLAWLKIEAGELKGPIAKFFPEDKAAELQAALQAEDGDLLLFAADKADIVAASLGALRNKLGKDLDLINEDELAFLWVTDWPLFEYDEEAGRYVSAHHPFTLPKEEDIPFLETDSSKVMAEAYDIVLNGYEIGGGSLRIYKKEVQESMFRALGFTDESAKEQFGFLMEALEYGTPPHGGIALGLDRIVMILAGRNNLRDTIAFPKTGSAVDPLTNAPGEVSAAQLAELKLETVKKETN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Listeria monocytogenes serotype 4b (strain CLIP80459)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.329 kDa
Sequence
MEKRTSYCGELNEAHIGQSVVLHGWVQKRRDLGGLIFIDLRDREGIVQVVFNPEFSKEALEIADSVRNEFVVTIKGTVHARGEKAINEKLATGKVEVLAEEITILNSSKTPPFYIEDGVNVSDELRLKYRYLDLRRPEMNNIFKMRHTVTRTFRNKLDALGFFDIETPYLTKSTPEGARDYLVPSRVYPGNFYALPQSPQILKQLLMTAGFDKYYQIVRCFRDEDLRGDRQPEFTQIDLETSFLTKEEIQAITEDMLVDVVKEAKNITIDKPFPRMTYKEAMDRFGSDKPDIRFGLELQNVSDVVKDVDFKVFQSAIENGGEVKAINAKAAAANFSRKDLDALGVFVANYGAKGLAWLKVEAGELKGPIAKFFPEEKATELKASLQAEDGDLLLFAADKADIVAASLGALRNKLGKELNLINEEELAFLWVTDWPLFEYDEEAGRYVSAHHPFTLPKEEDIPLLETDSSKVMAEAYDIVLNGYEIGGGSLRIYKKEVQESMFRALGFTDESAKEQFGFLMDALEYGTPPHGGIALGLDRIVMILAGRNNLRDTIAFPKTGSAVDPLTNAPGEVSEAQLAELKLETVKKETN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Listeria monocytogenes serotype 4b (strain F2365)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.3 kDa
Sequence
MEKRTSYCGELNEAHIGQSVVLHGWVQKRRDLGGLIFIDLRDREGIVQVVFNPEFSKEALEIADSVRNEFVVTIKGTVHARGEKAINDKLATGKVEVLAEEITILNTSKTPPFYIEDGVNVSDELRLKYRYLDLRRPEMNNIFKMRHTVTRTFRNKLDALGFFDIETPYLTKSTPEGARDYLVPSRVYPGNFYALPQSPQILKQLLMTAGFDKYYQIVRCFRDEDLRGDRQPEFTQIDLETSFLTKEEIQAITEDMLVDVVKEAKNITIDKPFPRMTYKEAMDRFGSDKPDIRFGLELVNVSDVVKDVDFKVFQSAIENGGEVKAINAKAAAANFSRKDLDALGVFVANYGAKGLAWLKVEAGELKGPIAKFFPEEKATELKASLQAEDGDLLLFAADKADIVAASLGALRNKLGKELNLINEEELAFLWVTDWPLFEYDEEAGRYVSAHHPFTLPKEEDIPLLETDSSKVMAEAYDIVLNGYEIGGGSLRIYKKEVQESMFRALGFTDESAKEQFGFLMDALEYGTPPHGGIALGLDRIVMILAGRNNLRDTIAFPKTGSAVDPLTNAPGEVSEAQLAELKLETVKKETN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Listeria monocytogenes serotype 4a (strain HCC23)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.242 kDa
Sequence
MEKRTSYCGELNEAHIGQSVVLHGWVQKRRDLGGLIFIDLRDREGIVQVVFNPEFSKEALEIADSVRNEFVVTIKGTVHARGEKAINEKLATGKVEVLAEEITILNTSKTPPFYIEDGVNVSDELRLKYRYLDLRRPEMNNIFKMRHTVTRTFRNKLDALGFFDIETPYLTKSTPEGARDYLVPSRVYPGNFYALPQSPQILKQLLMTAGFDKYYQIVRCFRDEDLRGDRQPEFTQIDLETSFLTKEEIQAITEDMLVDVVKEAKNITIDKPFPRMTYKEAMDRFGSDKPDIRFGLELQNVSDVVKDVDFKVFQSAIENGGEVKAINAKSAAANFSRKDLDALGVFVANYGAKGLAWLKVEASELKGPIAKFFPEDKAADLKAALQAEDGDLLLFAADKADIVAASLGALRNKLGKDLNLINEEELAFLWVTDWPLFEYDEEAGRYVSAHHPFTLPKEEDIPLLETDSSKVMAEAYDIVLNGYEIGGGSLRIYKKEVQESMFRALGFTDESAKEQFGFLMDALEYGTPPHGGIALGLDRIVMILAGRNNLRDTIAFPKTGSAVDPLTNAPGEVSAAQLAELKLETVKKETN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.383 kDa
Sequence
MEKRTSYCGELNEAHIGQSVVLHGWVQKRRDLGGLIFIDLRDREGIVQVVFNPEFSKEALEIADSVRNEFVVTIKGTVHARGEKAINEKLATGKVEVLAEEITILNTSKTPPFYIEDGVNVSDELRLKYRYLDLRRPEMNNIFKMRHTVTRTFRNKLDALGFFDIETPYLTKSTPEGARDYLVPSRVYPGNFYALPQSPQILKQLLMTAGFDKYYQIVRCFRDEDLRGDRQPEFTQIDLETSFLTKEEIQAITEDMLVDVVKEAKNITIEKPFPRMTYKEAMDRFGSDKPDIRFGLELQNVSDVVKDVDFKVFQSAIENGGEVKAINAKAAAANFSRKDLDALGVFVANYGAKGLAWLKVEAGELKGPIAKFFPEDKAAELKVALQAEDGDLLLFAADKADIVAASLGALRNKLGKDLNLINEEELAFLWVTDWPLFEYDEEAERYVSAHHPFTLPKEEDIPLLETDSSKVMAEAYDIVLNGYEIGGGSLRIYKKEVQESMFRALGFTDESAKEQFGFLMDALEYGTPPHGGIALGLDRIVMILAGRNNLRDTIAFPKTGSAVDPLTNAPGEVSEAQLAELKLETVKKETN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / SLCC5334)
Length
591 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.586 kDa
Sequence
MEKRTNYCGELNETHIDQHVVLHGWVQKRRDLGGLIFIDLRDREGIVQVVFNPEFSKEALEIADSVRNEFVVTIKGKVHARGEKAINEKLATGKVEILAEEITILNTSKTPPFYIEDGVNVSDELRLKYRYLDLRRPEMNNIFKMRHTVTRTFRNKLDALGFFDIETPYLTKSTPEGARDYLVPSRVYPGNFYALPQSPQILKQLLMTAGFDKYYQIVRCFRDEDLRGDRQPEFTQIDLETSFLTKEKIQAITEDMLIDVVKEAKGITIEKPFPRMTYKEAMDRFGSDKPDIRFGLELQNVSEVVKDVDFKVFQSAIENGGEVKAINAKAAAANFSRKDLDALGIFVSNYGAKGLAWLKVEAGELKGPIAKFFPEEKALELKAALKAEDGDLLLFAADKADIVAASLGALRNKLGKDLNLINEDELAFLWVTDWPLFEYDEEAGRYVSAHHPFTLPKEEDIPLLETDSSKVMAEAYDIVLNGYEIGGGSLRIYKKEVQESMFRALGFTDESAKEQFGFLMDALEYGTPPHGGIALGLDRIVMILAGRNNLRDTIAFPKTGSAVDPLTNAPGEVSDAQLDELKLQITKKELN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.396 kDa
Sequence
MHAFRTHTCAELTKDAVGQTVRLSGWVHRVRDHGGVLFIDLRDHYGMTQVLCDPDSPVFSQVEKVRSEWCIRIDGTVKARDESLINPKIPTGEIEVFIRDMEVLGTAEELPLPVFGDQEYPEETRLKYRFLDLRRESLHDNIMLRSKVVQSIRKRMWDIDFTEFQTPIITASSPEGARDFLVPSRLHPGKFYALPQAPQQFKQLIMVGGFDKYFQIAPCFRDEDPRADRSPTDFYQLDLEMSFVSQQDVFDTIQPVIAGIFEEFGGGRRVDTDWPLISYRDSALWYGTDKPDLRNPIKMQIVSDHFAGSGFAIFAKLLEQEGTEIRAIPAPGGGSRKFCDRMNKFAQEQGLPGMGYIFWRDQGQGMEAAGPLAKNIGPERTEAIRQQLGLQVGDAAFFLGGKPASFEAVAGRARTVIGEELGLIDQDRFAFAWIVDFPMYEKDDEGRIDFSHNPFSMPQGGMAALEGDPLEVLGYQYDLACNGYELVSGAIRNHKLDIMYKAFEIAGYGADEVEKRFGGMVNAFKYGPPPHGGCAAGIDRIVMLLADTANIREVIMFPMNQRAEDLMMNAPSEPTGEQLRDLSLRVIPQE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Ehrlichia canis (strain Jake)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.29 kDa
Sequence
MNIYRTHLCNELREEHINQEVILSGWVYRKRDHGKIIFVDLRDHYGITQLVFNEADNEIFQLISYLKLESVITIKGTVVARDSSTINTTVSTGLIEVVVNHVTIESEANLLPMNIASTQEYPEDIRFKYRFLDLRRDKVKHNIILRSKVIAELRKSMENMGFIEIQTPILTSSSPEGARDYLVPSRIHHGKFYALPQAPQLFKQILMVSGFDKYFQIAPCFRDEDARADRSPGEFYQLDMEMSFVTQEDVFNVIEPVLLNIFSKFSSKTIHKEFPRISYHNAMLYYGSDKPDLRNPLIIQDVTEIFRDSQFNIFNSNIKKGMVVRAIPAPKTANNPRSFFDNKIEFAKTLGAQGLGYITFNDDSSAKGPIAKFLDEERLNKIKSICNLQTGDSVFFVSETEDKAAEFAGEIRTILGTELNLIEPDTFRFCWVVDFPYFKYDKKEKSIGFFHNPFSMPQGGLEALNNQDPLSILAYQYDIVCNGIEISSGAIRNHKLDIMYKAFSIAGYTQEMVDKKFNSLTRAFKFGAPPHGGIAPGIDRMVMLLADATNIREVICFPLNQSGEDLLMGAPSEIDTEHLKLLSLNITKKS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Ehrlichia chaffeensis (strain ATCC CRL-10679 / Arkansas)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.421 kDa
Sequence
MNIYRTHLCDQLRKEHINQEVTLSGWIYRKRDHGKIIFVDLRDHYGITQLVFNEADNQNFQLITHLRLESVITVKGIVVARDSSTINTAVSTGFIEVVVKHVIIEGEADPLPLNITSTQDYPEEIRLKYRFLDLRRDKVKNNIILRSKIISELRKSMEAMGFIEIQTPILTSSSPEGARDYLVPSRIHHGKFYALPQAPQLFKQILMVSGFDKYFQIAPCFRDEDARSDRSPGEFYQLDIEMSFVSQEDVFNVIEPVLLNVFSKFSNKTIDKEFPRISYHDAMLHYGSDKPDLRNPLIIQDVTEIFRDSQFNIFNSNIKQGMVVRAIPAPNTATNPRSFFDNKIEFAKTLGAQGLGYITFNDDFSAKGPIAKFLDEERLNRIKSICNLQPGDSVFFVSETEDKATELAGEVRTLLGKELNLIEKDTFRFCWIIDFPYFKYDKKEKSINFFHNPFSMPQGGLEALNNQNPLDILAYQYDIVCNGIEISSGAIRNHKLDIMYKAFSIAGYTKEMVDQKFNSLTRAFKFGAPPHGGIAPGIDRMVMLLADATNIREVICFPLNQSGEDLLMSAPSEIDKEHLKLLSLSITKKS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Ehrlichia ruminantium (strain Gardel)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.223 kDa
Sequence
MNVYRTHLCNELREEHIDQTVTLSGWVYRKRDHGKIIFVDLRDHYGITQLVFNDSDTTIFQLITTLRLESVITIKGIVKARDSSTINETLDTGSIEVIVSSINIETASDILPINIASMQDYSEDIRLTYRFLDLRRDKVKNNIILRSKVITEIRKSMENMGFIEIQTPILTSSSPEGARDYLVPSRIHHGKFYALPQAPQLFKQLLMVSGFDKYFQIAPCFRDEDARADRSPGEFYQLDIEMSFVTQEDIFNIIEPLMINIFSKFSSKTINKEFPKISYHDAMLYYGSDKPDLRNPLVIQDVTEIFRDSEFKIFNSNIKQGMVVRAIPAPNTAHNPRSFFDSKIEFAKTLGAQGLGYITFIDDSLAKGPIAKFLDKDRLDNIKLICNIKAGDSVFFVSEIADKAALFAGEVRTLLGKELNLIEENTFKFCWVIDFPYFKYDHKEKSINFFHNPFSMPQGGLEALENQDPLNILAYQYDIVCNGIEISSGAIRNHKLNIMYKAFSIAGYTKEMVDEKFKALTRAFKFGAPPHGGIAPGIDRIVMLLADVPNIREVICFPLNQSGEDLLMGSPSEIDNDHLKLLSLNIIKKT

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Ehrlichia ruminantium (strain Welgevonden)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.25 kDa
Sequence
MNVYRTHLCNELREEHIDQTVTLSGWVYRKRDHGKIIFVDLRDHYGITQLVFNDSDTTIFQLITTLRLESVITIKGIVKARDSSTINETLDTGSIEVIVSSINIETASEILPINIASMQDYSEDIRLTYRFLDLRRDKVKNNIILRSKVITEIRKSMENMGFIEIQTPILTSSSPEGARDYLVPSRIHHGKFYALPQAPQLFKQLLMVSGFDKYFQIAPCFRDEDARADRSPGEFYQLDIEMSFVTQEDIFNIIEPVMINIFSKFSNKTINKEFPKISYHDAMLYYGSDKPDLRNPLVIQDVTEIFRDSEFKIFNSNIKQGMVVRAIPAPNTAHNPRSFFDSKIEFAKTLGAQGLGYITFIDDSLAKGPIAKFLDKDRLDNIKLICNIKAGDSVFFVSEIADKAALFAGEVRTLLGKELNLIEENTFKFCWVIDFPYFKYDHKEKSINFFHNPFSMPQGGLEALENQDPLNILAYQYDIVCNGIEISSGAIRNHKLNIMYKAFSIAGYTKEMVDEKFKALTRAFKFGAPPHGGIAPGIDRIVMLLADVPNIREVICFPLNQSGEDLLMGSPSEIDNDHLKLLSLNIIKKT

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli O139:H28 (strain E24377A / ETEC)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.869 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli O127:H6 (strain E2348/69 / EPEC)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.869 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLLFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILERTGAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli O45:K1 (strain S88 / ExPEC)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.869 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILERTGAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli (strain 55989 / EAEC)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.869 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli O157:H7
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.814 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLRSVEFAVFAGPANDPKGRVAALCVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPAALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli O157:H7 (strain EC4115 / EHEC)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.867 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLRSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPAALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli O7:K1 (strain IAI39 / ExPEC)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.842 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVASAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli O81 (strain ED1a)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.869 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILERTGAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli O8 (strain IAI1)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.869 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli (strain K12 / MC4100 / BW2952)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.913 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEDILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli (strain K12 / DH10B)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.913 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEDILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli O9:H4 (strain HS)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.913 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEDILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli O1:K1 / APEC
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.869 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILERTGAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli O6:K15:H31 (strain 536 / UPEC)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.869 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILERTGAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.869 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILERTGAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli (strain ATCC 8739 / DSM 1576 / Crooks)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.869 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli (strain K12)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp). Also mischarges tRNA(Asp) with D-aspartate, although it is a poor substrate (PubMed:10918062).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.913 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEDILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.869 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Treponema denticola (strain ATCC 35405 / CIP 103919 / DSM 14222)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.578 kDa
Sequence
MEKMQRTVTCGGLNKDFAGKTVVLNGWIHRKRDHGGITFLNLRDRYGLTQVVVDDDASEDLKALAVSLKQEFCIAVEGLVRPRPDSMINKEMATGEIEVKALKIEVLSKSEVLPFQIDEKTNANEDLRLKYRYLDLRSKAMQEHIMLRSKFTFAVREFLTSKDFLEIETPTFIKSTPEGARDYLVPSRLYPGKFYALPQSPQIYKQILMVSGFDKYFQIARCYRDEDARGDRQPEFTQIDLEMSFASREDVLSLTEGMMQYAFKKSINVDLPKTFERISYDEAIDIYGTDKPDLRFEMKMQDAAFMAEIGNFAVFKDAVSLGGAVKALVVKGQAEAYSRKKIEELEAAAKIYKAKGLAWIKVTEGGAKLEGGVSKFFEGKEAEICSKLGAEKGDLILFVADKYKIACTALGAVRSKLGKDLGLLNPAEFKFAWIVDFPLFEWNEEENKWDPAHHMFSAPQEKYIATMEENPEPVKGDLYDLVLNGYEVASGSIRIHNPELQKRIFKIVGFDESEAEKKFGFLTEAFKYGAPPHGGIAPGLDRIVMIMAGETSIKEVIAFPKNSFAVSPMDDSPSEVDQKQLDELHLVIKE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shigella sonnei (strain Ss046)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.897 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTVLAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rhodopseudomonas palustris (strain HaA2)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.7 kDa
Sequence
MHRYRTHTCGALRDSDIDQTVRVSGWCHRIRDHGGLLFIDLRDHYGLTQCVADPDSPAFKDAEKLRAEWVVRIDGRVRRRPEGTDNDDLPTGKVEIFITEIEVLGPAGELPLPVFGEQDYPEDVRLRYRFLDLRREKLHQNIMTRGAIVDAMRKRMKEQGFFEFQTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMMSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDVEMSFVTQDDVFAAMEPVITGVFEDFAKGKPVTKSWPRIPYFESLRKYGTDKPDLRNPLEMQDVSEHFRGSGFKVFARMLEEERNQVWAIPGPGGGSRAFCDRMNSWAQGEGQPGLGYIMWREGNEGAGPLANNIGPERTEAIRVALGLKAGDAAFFVAGDPAKFVKFAGLARTKVGEELNLIDKDQFALAWVVDFPMYEYNEDDKKVDFSHNPFSMPQGGMDALTSQDPLTIKAFQYDITCNGYEIASGGIRNHRPEAMVKAFEIAGYGEQEVIDRFGGMYRAFQYGAPPHGGMAAGVDRIVMLLCGTNNLREISLFPMNQRAEDLLMGAPSQVAPKQLRELHIRLNLPES

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rhodopseudomonas palustris (strain BisA53)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.73 kDa
Sequence
MHRYRSHTCGALRESHIDQTVRVSGWCHRIRDHGGLLFIDLRDHYGLTQCVADPDSPAFKDAEKLRAEWVVKIDGKVRRRPEGTDNADLPTGQVEIFITEIEVLGPAGELPLPVFGEQEYPEDIRLKYRFLDLRREKLHQNIMTRGAIVDSMRKRMKEQGFFEFQTPILTASSPEGARDFLVPSRIHPGRFYALPQAPQQYKQLLMMSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDVEMSFITQEDVFAAMEPVITGVFEEFAKGKRVNSVWPRIPFAEAMQKYGSDKPDLRNPIEMQDVSEHFRGSGFKVFARMLEEPRNQVWAIPGKGGGSRAFCDRMNSWAQGEGQPGLGYIMWREGNEGAGPLANNIGPERTEAIRIALGLGAGDAAFFVAGDPAKFVRFAGLARTRVGEELNLVDKEQFALAWVVDFPMYEYNEDDKKVDFSHNPFSMPQGGMEALVTQDPLNIKAFQYDITCNGFEIASGGIRNHRPEAMVKAFEIAGYGEQEVVDRFGGMYRAFQYGAPPHGGMAAGVDRIVMLLCGTNNLREISLFPMNQRAEDLLMGAPSEVTPKQLRELHIRLNLQEE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rhodopseudomonas palustris (strain BisB18)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.795 kDa
Sequence
MHRYRSHTCGALRESDIDQTVRVSGWCHRIRDHGGLLFIDLRDHYGLTQCVADPDSPAFKDAEKLRAEWVVRIDGKVRRRPEGTDNNDLPTGQVEIFITEIEVLGPAGELPLPVFGEQEYPEDIRLKYRFLDLRREKLHQNIMTRGAIVDSMRKRMKEQGFFEFQTPILTASSPEGARDFLVPSRIHPGRFYALPQAPQQYKQLLMMSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDVEMSFITQDDVFAAMEPVITGVFEDFAKGKPVTKSWPRIAYADSLKKYGTDKPDLRNPIEMQNVSEHFRGSGFKVFARMLEEERNQVWAIPGPGGGSRAFCDRMNSWAQGEGQPGLGYIMWREGGEGAGPLANNIGPERTAAIREQLGLKAGDAAFFVAGDPSKFVRFAGLARTRLGEELNLVDKERFELAWIVDFPMYEYNEDDKKVDFSHNPFSMPQGGMDALLNQDPLTIKAFQYDITCNGFEIASGGIRNHRPEAMVKAFEIAGYGEQEVVDRFGGMYRAFQYGAPPHGGMAAGVDRIVMLLCGTNNLREISLFPMNQRAEDLLMGAPSDVTPKQLRELHIRLNLPEN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Rhodopseudomonas palustris (strain BisB5)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.581 kDa
Sequence
MHRYRTHTCGALRDSDIDQTVRLSGWCHRIRDHGGLLFIDLRDHYGLTQCVADPDSPAFKDAEKLRAEWVVRIDGRVRRRPEGTDNDDLPTGKIELFITEIEVLGPAGELPLPVFGEQEYPEDVRLRYRFLDLRREKLHQNIMTRGAIVDAMRARMKQQGFFEFQTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMMSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDVEMSFVTQDDVFAAMEPVITGVFEDFAKGKRVTKGWPRIPYADSMRKYGTDKPDLRNPIEMQDVSEHFRGSGFKVFARMLEEERNQVWAIPGPGGGSRAFCDRMNSWAQGEGQPGLGYIMWREGGEGAGPLANNIGPERTEAIRAALGLKAGDAAFFVAGDPSKFVKFAGLARTKVGEELNLIDKDQFALAWVVDFPMYEYNEDDKKVDFSHNPFSMPQGGMDALLGQDPLTIKAFQYDITCNGFEIASGGIRNHRPEAMVKAFEIAGYGEQEVVDRFGGMYRAFQYGAPPHGGMAAGVDRIVMLLCGTNNLREISLFPMNQRAEDLLMGAPSQVTPKQLRELHIRLNLPEN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Salmonella agona (strain SL483)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.767 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDAKNVNADMATGEIEVLASSLTIINRADSLPLDANHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDEHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELVDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGAQLSRKQIDDYGNFVKIYGAKGLAYIKVNERAKGLDGINSPVAKFLTADIVDAILERTGAQDGDMIFFGADNKKVVADALGALRLKLGKDLSLTDEDKWAPLWVIDFPMFEDDGEGGLTAMHHPFTAPRDMTASELKTAPEEAVANAYDMVINGYEVGGGSVRIHNGEMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANQAALTELGIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.738 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDAKNVNADMATGEIEVLASSLTIINRADSLPLDANHINTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKDVDLGDFPVMTFAEAERRYGSDKPDLRNPMELVDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGAQLSRKQIDDYGNFVKIYGAKGLAYIKVNDRAKGLDGITSPVAKFLSTEIVEAILARTGAQNGDMIFFGADNKKVVADALGALRLKLGKDLSLTDEDKWAPLWVIDFPMFEDDGEGGLTAMHHPFTAPRDMTASELKAAPENAVANAYDMVINGYEVGGGSVRIHNGEMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANQAALTELGIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Salmonella choleraesuis (strain SC-B67)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.781 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDAKNVNADMATGEIEVLASSLTIINRADSLPLDANHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVEISFMTALQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELVDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGAQLSRKQIDDYGNFVKIYGAKGLAYIKVNERAKGLDGINSPVAKFLTADIVDAILERTGAQDGDMIFFGADNKKVVADALGALRLKLGKDLSLTDEDKWAPLWVIDFPMFEDDGEGGLTAMHHPFTAPRDMTASELKTAPEEAVANAYDMVINGYEVGGGSVRIHNGEMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANQAALTELGIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Salmonella dublin (strain CT_02021853)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.753 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDAKNVNADMATGEIEVLASSLTIINRADSLPLDANHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELVDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGAQLSRKQIDDYGNFVKIYGAKGLAYIKVNERAKGLDGINSPVAKFLTADIVDAILERTGAQDGDMIFFGADNKKVVADALGALRLKLGKDLSLTDEDKWAPLWVIDFPMFEDDGEGGLTAMHHPFTAPRDMTASELKTAPEEAVANAYDMVINGYEVGGGSVRIHNGEMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANQAALTELGIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Salmonella enteritidis PT4 (strain P125109)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.753 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDAKNVNADMATGEIEVLASSLTIINRADSLPLDANHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELVDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGAQLSRKQIDDYGNFVKIYGAKGLAYIKVNERAKGLDGINSPVAKFLTADIVDAILERTGAQDGDMIFFGADNKKVVADALGALRLKLGKDLSLTDEDKWAPLWVIDFPMFEDDGEGGLTAMHHPFTAPRDMTASELKTAPEEAVANAYDMVINGYEVGGGSVRIHNGEMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANQAALTELGIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Salmonella gallinarum (strain 287/91 / NCTC 13346)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.753 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDAKNVNADMATGEIEVLASSLTIINRADSLPLDANHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELVDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGAQLSRKQIDDYGNFVKIYGAKGLAYIKVNERAKGLDGINSPVAKFLTADIVDAILERTGAQDGDMIFFGADNKKVVADALGALRLKLGKDLSLTDEDKWAPLWVIDFPMFEDDGEGGLTAMHHPFTAPRDMTASELKTAPEEAVANAYDMVINGYEVGGGSVRIHNGEMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANQAALTELGIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Salmonella heidelberg (strain SL476)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.753 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDAKNVNADMATGEIEVLASSLTIINRADSLPLDANHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELVDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGAQLSRKQIDDYGNFVKIYGAKGLAYIKVNERAKGLDGINSPVAKFLTADIVDAILERTGAQDGDMIFFGADNKKVVADALGALRLKLGKDLSLTDEDKWAPLWVIDFPMFEDDGEGGLTAMHHPFTAPRDMTASELKTAPEEAVANAYDMVINGYEVGGGSVRIHNGEMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANQAALTELGIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Salmonella newport (strain SL254)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.767 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDAKNVNADMATGEIEVLASSLTIINRADSLPLDANHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELVDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGAQLSRKQIDDYGNFVKIYGAKGLAYIKVNERAKGLDGINSPVAKFLTADIVEAILERTGAQDGDMIFFGADNKKVVADALGALRLKLGKDLSLTDEDKWAPLWVIDFPMFEDDGEGGLTAMHHPFTAPRDMTASELKTAPEEAVANAYDMVINGYEVGGGSVRIHNGEMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANQAALTELGIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Salmonella paratyphi A (strain ATCC 9150 / SARB42)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.736 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDAKNVNADMATGEIEVLASSLTIINRADSLPLDANHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELVDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGAQLSRKQIDDYGNFVKIYGAKGLAYIKVNERAKGLDGINSPVAKFLTADIVEAILERTGAQDGDMIFFGADNKKVVADALGALRLKLGKDLSLTDEDKWAPLWVIDFPMFEDDGEGGLTAMHHPFTAPRDMTASELKTAPEEAVANAYDMVINGYEVGGGSVRIHNGEMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANQAALTELGIPVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.767 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDAKNVNADMATGEIEVLASSLTIINRADSLPLDANHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELVDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGAQLSRKQIDDYGNFVKIYGAKGLAYIKVNERAKGLDGINSPVAKFLTADIVEAILERTGAQDGDMIFFGADNKKVVADALGALRLKLGKDLSLTDEDKWAPLWVIDFPMFEDDGEGGLTAMHHPFTAPRDMTASELKTAPEEAVANAYDMVINGYEVGGGSVRIHNGEMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANQAALTELGIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Salmonella paratyphi C (strain RKS4594)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.769 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDAKNVNADMATGEIEVLASSLTIINRADSLPLDANHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTALQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELVDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGAQLSRKQIDDYGNFVKIYGAKGLAYIKVNERAKGLDGINSPVAKFLTADIVDAILERTGAQDGDMIFFGADNKKVVADALGALRLKLGKDLSLTDEDKWAPLWVIDFPMFEDDGEGGLTAMHHPFTAPRDMTASELKTAPEEAVANAYDMVINGYEVGGGSVRIHNGEMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANQAALTELGIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Salmonella paratyphi A (strain AKU_12601)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.736 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDAKNVNADMATGEIEVLASSLTIINRADSLPLDANHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELVDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGAQLSRKQIDDYGNFVKIYGAKGLAYIKVNERAKGLDGINSPVAKFLTADIVEAILERTGAQDGDMIFFGADNKKVVADALGALRLKLGKDLSLTDEDKWAPLWVIDFPMFEDDGEGGLTAMHHPFTAPRDMTASELKTAPEEAVANAYDMVINGYEVGGGSVRIHNGEMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANQAALTELGIPVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Salmonella schwarzengrund (strain CVM19633)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.767 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDAKNVNADMATGEIEVLASSLTIINRADSLPLDANHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELVDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGAQLSRKQIDDYGNFVKIYGAKGLAYIKVNERAKGLDGINSPVAKFLTADIVEAILERTGAQDGDMIFFGADNKKVVADALGALRLKLGKDLSLTDEDKWAPLWVIDFPMFEDDGEGGLTAMHHPFTAPRDMTASELKTAPEEAVANAYDMVINGYEVGGGSVRIHNGEMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANQAALTELGIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Salmonella typhi
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.795 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDAKNVNADMATGEIEVLASSLTIINRADSLPLDANHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELVDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGAQLSRKQIDDYGNFVKIYGAKGLAYIKVNERAKGLDGINSPVAKFLTADIVEAILERTGAQDGDMIFFGADNKKVVADALGALRLKLGKDLSLTDEDKWAPLWVIDFPMFEDDGEGGLTAMHHPFTAPRDMTASELKTAPEEAVANAYDMVINGYEVGGGSVRIHNGEMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHVGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANQAALTELGIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.666 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDAKNVNADMATGEIEVLASSLTIINRADSLPLDANHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELVDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGAQLSRKQIDDYGNFVKIYGAKGLAYIKVNERAKGLDGINSPVAKFLTADIVEAILERTGAQDGDMIFFGADNNKVVADALGALRLKLGKDLSLTDEDKWAPLWVIDFPMFEDDGEGGLTAMHHPFTAPRDMTASELKTAPEGAVANAYDMVINGYEVGGGSVRIHNGEMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANLAALTELGIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Mycobacterium gilvum (strain PYR-GCK)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
63.882 kDa
Sequence
MLRTRTAGSLRPADAGQTVTLAGWVARRRDHGGVIFIDLRDASGVSQVVFRDGAVLEQAHRLRSEFCVAVTGVVEIRPEGNANADIPTGEVEVNATSLTVLGESAALPFQLDETAGEEARLKYRYLDLRREVPGNAIRLRSKVNAAARGVLAGHDFVEIETPTLTRSTPEGARDFLVPARLQPGSFYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDMEMSFVDADDVMALSEEVLRAVWATIGYDLPLPLPRISYADAMRRFGSDKPDLRFGLELVECTEYFADTPFRVFQAPYVGAVVMPGGASQPRRTLDGWQEFAKQRGHKGLAYVLVGKDGELTGPVAKNLTDAERAGLTAHVGANPGDCVFFAAGTAKSARALLGATRIEVAKRLDLIDPDAWAFTWVVDWPMFESAAEATASGDVAVGSGAWTAMHHAFTAPTPESEATFDTDPGSALSNAYDIVCNGNEIGGGSLRIHRRDVQERVFAMMGISQEEAEDKFGFLLEAFTFGAPPHGGIAFGWDRIVALLAGLDSIREVIAFPKSGGGVDPLTEAPAPITAQQRKESGIDAKPGKDGA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Mycobacterium sp. (strain JLS)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.239 kDa
Sequence
MLRSHAAGSLRPADAGQNVTLAGWVARRRDHGGVIFIDLRDASGVSQVVFREGAVLEAAHRLRAEFCVAVEGVVEVRPEGNENPEIPTGGIEVNATSLTVLGESAPLPFQLDDEAGEEARLKYRYLDLRREGPGKALRLRSKVNAAAREVLARHDFVEIETPTMTRSTPEGARDFLVPARLQPGSFYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDMEMSFVDADDVIAVSEEILKALWALIGHDLPTPLPRITYAEAMRRFGTDKPDLRFGLELVECKEFFADTTFRVFQAPYVGAVVMPGGASQPRRTLDGWQEWAKQRGAKGLAYVLVGDDGTLGGPVAKNLTDAERDGLAAHVGANPGDCIFFAAGPPKSSRALLGAARIEIAKRLDMIDPDAWAFTWVVDWPLFEMAEDATAAGDVAVGSGAWTAVHHAFTAPQPQSEATFDTDPAGALADAYDIVCNGNEIGGGSIRIHRRDVQERVFAMMGIEHDEAQEKFGFLLDAFTFGAPPHGGIAFGWDRITALLARMDSIREVIAFPKSGGGADPLTGAPAPITPQQRRESGIDAKPKKDGE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Mycobacterium sp. (strain KMS)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.22 kDa
Sequence
MLRSHAAGSLRPADAGQNVTLAGWVARRRDHGGVIFIDLRDASGVSQVVFREGAVLEAAHRLRAEFCVAVEGVVEVRPEGNENPEIPTGGIEVNATSLTVLGESAPLPFQLDDEAGEEARLKYRYLDLRREGPGKALRLRSKVNAAAREVLARHDFVEIETPTMTRSTPEGARDFLVPARLQPGSFYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDMEMSFVDADDVIAVSEEILKALWALIGHDLPTPLPRITYAEAMHRFGTDKPDLRFGLELVECKEFFADTTFRVFQAPYVGAVVMPGGASQPRRTLDGWQEWAKQRGAKGLAYVLVGDDGTLGGPVAKNLTDAERDGLAAHVGANPGDCIFFAAGPPKSSRALLGAARIEIAKRLDMIDPDAWAFTWVVDWPLFEMAEDATAAGDVAVGSGAWTAVHHAFTAPQPQSEATFDTDPAGALADAYDIVCNGNEIGGGSIRIHRRDVQERVFAMMGIEHDEAQEKFGFLLDAFTFGAPPHGGIAFGWDRITALLARMDSIREVIAFPKSGGGADPLTGAPAPITPQQRRESGIDAKPKKDGE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shigella boydii serotype 18 (strain CDC 3083-94 / BS512)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.869 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shigella boydii serotype 4 (strain Sb227)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.869 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shigella dysenteriae serotype 1 (strain Sd197)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.885 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDLKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shigella flexneri serotype 5b (strain 8401)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.785 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLSAEIIEAILDRTAAQDGDMIFFGADNKKIVADGMGALLLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Shigella flexneri
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.812 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILDRTAAQDGDMIFFGADNKKIVADGMGALLLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / NBRC 14845 / NCIMB 13405 / ORS 571)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.324 kDa
Sequence
MHRYRTHTCGALTEAQVGDTVRVSGWCHRIRDHGGVLFVDLRDHYGLTQVVFDPDSAAFAAAEKVRAEWVIRVDGRVRLRPEGTENSELATGKVEIYATDLEVLGPAAELPLPVFGDQDYPEDIRLRYRFLDLRRERIHGNIMKRGQIIDSLRQRMKGQGFFEFQTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLIMMSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVTQDDVFAAVEPVIRGVFEEFGGGKPVTQNWPRIPYAEALRKYGSDKPDLRNPLVMQNVSEHFRGSNFKVFARLLEDPKNEVWAIPGPTGGSRAFCDRMNSWAQGEGQPGLGYIMWREGGEGAGPLANNIGPERTAAIREQLGLKDGDAAFFVAGNPEKFYKFAGLARTKVGEELKLIDTERFELAWIVDFPFYEWSDEEKKIDFSHNPFSMPQGGLEALNGQDPLTIKAFQYDIACNGYEIASGGIRNHRPEAMVKAFELAGYDEATVIERFGGMYRAFQYGAPPHGGMAAGIDRIVMLLCGVSNLREISLFPMNQQALDLLMGAPNEATPKQMKELHIRPALPAK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Marinomonas sp. (strain MWYL1)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.837 kDa
Sequence
MRSHYCGELNASNISQEITLCGWVHRRRDHGGVIFLDVRDREGITQVVFDPDRAESFALADSVRNEFVVKLKGLVRARPEGTVNPNMNTGEIEVLGTELEILNAAKTPPFQLDEHQSVGEDVRLKNRFIDLRRPEIQQKMRFRSKVTSVLRRYLDGNGFLDIETPILTRATPEGARDYLVPSRTQQGSFFALPQSPQLFKQLLMVSGFDRYYQIAKCFRDEDLRADRQPEFTQVDIETSFMSEQEIMAMTEEMIVGLFKELMDIDLGTFPRMPYSEAMETYGSDKPDLRIPLTIVTVSDLMAGVDFKVFSGPATDPKGRVAALKVPGGNALTRKQIDDYTKFVSIYGAKGLAYIKVNDKSNLEEGLQSPIVKFLPVEVRAALLERLEAEDGDLIFFGADSAKIVNEALGALRCKLGDDLNLYTCKWAPLWVVDFPMFEETSDGGITAIHHPFTAPSCSPENLKASPLTALSQAYDMVLNGTELGGGSIRIHQSSMQETVFELLNITKEEQEEKFGFLLDALKFGAPPHGGLAFGLDRLVMLMTGSSSIRDVIAFPKTQSATCLLTQAPGEVSEKQLKELNIRIRKPVVES

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Clostridium kluyveri (strain NBRC 12016)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.182 kDa
Sequence
MGEELKTLKRTCMCGGLTEANIGDKITVMGWVQRKRNLGGLVFVDLRDRTGILQIVFGEAINKEAFEKSDSVKSEYCIAAVGTIVKRESPNMEIPTGMVELKGEYIKIFSESETPPIYIKENLDAAENIRLKYRYLDLRRPDMQRIFMLRHKTAKVIRDFLDEQGFLEIETPILGKSTPEGARDYLVPSRNYKGKYYALPQSPQLFKQLLMVSGYDRYFQIAKCFRDEDLRANRQPEFTQVDMEISFVDQEEVMDLNERLIQRVFKQILDVDVKLPIERMTYKTAMDKYGSDKPDLRFGMEINDISEVVKGVDFKVFQNALENGGSVRAIKVTGSAALGRKQLDKLVEFVKTYGASGLIWMAYKKEGIKCSISKFLTEEDTQNILNKMEAAEGDLILIVADKNKVVFESLGALRIHMAKQTGILEGNNDFKFVWITEFPLLSYNEEENRYQAEHHPFVMPMDEDIQYLESNPEKVRAKAYDIVLNGEELGGGSIRIHDTKLQEKMFGAIGISKDTAWNKFGYFLEALKFGPPPHGGLAYGFDRMIMFLAGTDNIKDVIAFPKNQNAFCPLTEAPNSVDKSQLKDLGIEVK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.182 kDa
Sequence
MGEELKTLKRTCMCGGLTEANIGDKITVMGWVQRKRNLGGLVFVDLRDRTGILQIVFGEAINKEAFEKSDSVKSEYCIAAVGTIVKRESPNMEIPTGMVELKGEYIKIFSESETPPIYIKENLDAAENIRLKYRYLDLRRPDMQRIFMLRHKTAKVIRDFLDEQGFLEIETPILGKSTPEGARDYLVPSRNYKGKYYALPQSPQLFKQLLMVSGYDRYFQIAKCFRDEDLRANRQPEFTQVDMEISFVDQEEVMDLNERLIQRVFKQILDVDVKLPIERMTYKTAMDKYGSDKPDLRFGMEINDISEVVKGVDFKVFQNALENGGSVRAIKVTGSAALGRKQLDKLVEFVKTYGASGLIWMAYKKEGIKCSISKFLTEEDTQNILNKMEAAEGDLILIVADKNKVVFESLGALRIHMAKQTGILEGNNDFKFVWITEFPLLSYNEEENRYQAEHHPFVMPMDEDIQYLESNPEKVRAKAYDIVLNGEELGGGSIRIHDTKLQEKMFGAIGISKDTAWNKFGYFLEALKFGPPPHGGLAYGFDRMIMFLAGTDNIKDVIAFPKNQNAFCPLTEAPNSVDKSQLKDLGIEVK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Coxiella burnetii (strain Dugway 5J108-111)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.737 kDa
Sequence
MRTHYADKVDSSLIDQTITLCGWVHRRRDHGGLIFIDLRDREGLVQVVCNPTESTVFKVAESLRNEYVIKVTGKVHKRPEGTVNPHIPSGEVEIAASDITLLNKSKPLPFNIDEYQEVSEEVRLKFRYLDLRRPEVAQRLKMRSYIIREIRRFLDERGFLDIETPMLTKSTPEGARDYLVPSRTHPGQFFALPQSPQIFKEILMVAGFDRYYQIVRCFRDEDLRADRQPEFTQLDLEMSFVEEKDIQQLMETMIRHLFSTFLNVPLPDPFPRITYDEAIKTYGTDRPDLRNPLTLVDVTDLMKSVEFKVFKEPANNPHGRIAVLRLPKGAELSRKAIDDYTQFVGIYGAKGLAYIKVENIDNGTGGLHSPILKFLPENVIAEILKRTQAQSGDILFFGADKAKIVNESLGALRDRLCADLNLYEGQWKPVWVVDFPMFDREDVGDWQALHHPFTALQETDPEKVIANPGDVLSRAYDIVLNGSEIGGGSIRINDIGMQYAVLKVLGISKEMAEAQFGHLLMALQFGSPPLGGIAFGLDRLVAIMTGASSIRDVIAFPKTQTAQCPLTNAPAQVETLQLETLGLKVSKHRK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Coxiella burnetii (strain RSA 331 / Henzerling II)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.789 kDa
Sequence
MRTHYADKVDSSLIDQTITLCGWVHRRRDHGGLIFIDLRDREGLVQVVCNPTESTVFKVAESLRNEYVIKVTGKVHKRPEGTVNPHIPSGEVEIAASDITLLNKSKPLPFNIDEYQEVSEEVRLKFRYLDLRRPEVAQRLKMRSYIIREIRRFLDERGFLDIETPMLTKSTPEGARDYLVPSRTHPGQFFALPQSPQIFKEILMVAGFDRYYQIVRCFRDEDLRADRQPEFTQLDLEMSFVEEKDIQQLMETMIRHLFSTFLNVPLPDPFPRITYDEAIKTYGTDRPDLRNPLTLVDVTDLMKSVEFKVFKEPANNPHGRIAVLRLPKGAELSRKAIDDYTQFVGIYGAKGLAYIKVENIDNGTGGLHSPILKFLPENVIAEILKRTQAQSGDILFFGADKAKIVNESLGALRDRLCADLNLYEGQWKPVWVVDFPMFDREDVGDWQALHHPFTALQETDPEKVIANPGDVLSRAYDMVLNGSEIGGGSIRINDIGMQYAVFKVLGISKEMAEAQFGHLLMALQFGSPPLGGIAFGLDRLVAIMTGASSIRDVIAFPKTQTAQCPLTNAPAQVETLQLETLGLKVSKHRK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.755 kDa
Sequence
MRTHYADKVDSSLIDQTITLCGWVHRRRDHGGLIFIDLRDREGLVQVVCNPTESTVFKVAESLRNEYVIKVTGKVHKRPEGTVNPHIPSGEVEIAASDITLLNKSKPLPFNIDEYQEVSEEVRLKFRYLDLRRPEVAQRLKMRSYIIREIRRFLDERGFLDIETPMLTKSTPEGARDYLVPSRTHPGQFFALPQSPQIFKEILMVAGFDRYYQIVRCFRDEDLRADRQPEFTQLDLEMSFVEEKDIQQLMETMIRHLFSTFLNVPLPDPFPRITYDEAIKTYGTDRPDLRNPLTLVDVTDLMKSVEFKVFKEPANNPHGRIAVLRLPKGAELSRKAIDDYTQFVGIYGAKGLAYIKVENIDNGTGGLHSPILKFLPENVIAEILKRTQAQSGDILFFGADKAKIVNESLGALRDRLCADLNLYEGQWKPVWVVDFPMFDREDVGDWQALHHPFTALQETDPEKVIANPGDVLSRAYDMVLNGSEIGGGSIRINDIGMQYAVLKVLGISKEMAEAQFGHLLMALQFGSPPLGGIAFGLDRLVAIMTGASSIRDVIAFPKTQTAQCPLTNAPAQVETLQLETLGLKVSKHRK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli (strain SE11)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.869 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli (strain SMS-3-5 / SECEC)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.869 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia coli (strain UTI89 / UPEC)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.869 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILERTGAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Enterobacter sp. (strain 638)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.738 kDa
Sequence
MRTEYCGQLRQSHVGQQVTLCGWVNRRRDLGSLIFIDLRDREGIVQVFFDPDRAEALKLASELRNEFCIQVTGTVRARDEKNINADMATGEIEVLASDLTIINRSESLPLDSNHVNTEEARLKFRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVRELMEALVRSLWLDVKGVDLGDFPIMTFAEAERRYGSDKPDLRNPMELVDVADLLKAVEFAVFSGPANDAKGRVAALRVPGGASLSRKQIDDYGNFVKIYGAKGLAYIKVTERAKGIEGITSPVAKFLNAEIVESILERTGAQDGDMIFFGADNKKVVADALGALRLKLGKDLSLTDEAKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSAKDMNADELKAAPETAIANAYDMVINGYEVGGGSVRIHSGEMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPASLAELGIDVVKKEEKN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Escherichia fergusonii (strain ATCC 35469 / DSM 13698 / CDC 0568-73)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.885 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEAILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALSELSIQVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Exiguobacterium sp. (strain ATCC BAA-1283 / AT1b)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.264 kDa
Sequence
MIGRTHMNGRVTESLIGQEVQLKGWVQKRRDLGGLIFIDLRDRTGIVQVVVRPENEAVHQLAETIRSEYVLDVKGTVLERENKNPNMPTGNIEVIASEINILNAAKMTPIPIGDEAENVSEDLRLKYRYLDLRRPALQETFRLRSKTSNTIRNFLTEQEFLEVETPILTKSTPEGARDYLVPSRVHGGEFYALPQSPQLFKQLLMVAGFDRYFQIARCFRDEDLRADRQPEFTQVDIETSFMDIEDLMAMMESMMGQVMESTLGRTDTPAKFERMTHAEAMRRFGSDKPDTRFGLELIDVADAVKGAGFKVFDAALESNGQVKAINVKGEADNFSRKDIDKLQEFTAVYGAKGLAWLKVTAEGLNGPIAKFFDETYAQKLIEATNAEAGDLLLFVASKPTVVADSLGALRVKLGHELGLIDESKFNFLWVTDFPLVTFEEEDGRFYANHHPFTMPNREDLHLLETDPASVRAVAYDLVLNGYELGGGSQRIYERDIQERMFKLLGFTQEEAVEQFGFLLEAFEYGTPPHAGIALGLDRLVMILAGRSNLRDTIAFPKTASASCLLTQAPSPVADAQLEELSIRTAIKEKK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Geobacillus kaustophilus (strain HTA426)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.013 kDa
Sequence
MERTYYCGEVPETAVGERVVLKGWVQKRRDLGGLIFIDLRDRTGIVQVVASPDVSAEALAAAERVRSEYVLSVEGTVVARAPETVNPNIATGSIEIQAERIEIINEAKTPPFSISDDTDAAEDVRLKYRYLDLRRPVMFQTLALRHKITKTVRDFLDSERFLEIETPMLTKSTPEGARDYLVPSRVHPGEFYALPQSPQIFKQLLMVGGVERYYQIARCFRDEDLRADRQPEFTQIDIEMSFIEQKDIMDLTERMMAAVVKAAKGIDIPRPFPRITYDEAMSRYGSDKPDIRFGLELVDVSEIVRNSAFQVFARAVKEGGQVKAINAKGAAPRYSRKDIDALGEFAGRYGAKGLAWLKAEGEELKGPIAKFFTDEEQAALRRALAVEDGDLLLFVADEKAIVAAALGALRLKLGKELGLIDEAKLAFLWVTDWPLLEYDEEEGRYYAAHHPFTMPVRDDIPLLETNPSAVRAQAYDLVLNGYELGGGSLRIFERDVQEKMFRALGFSEEEARRQFGFLLEAFEYGTPPHGGIALGLDRLVMLLAGRTNLRDTIAFPKTASASCLLTEAPGPVSDKQLEELHLAVVLPENE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bradyrhizobium diazoefficiens (strain JCM 10833 / IAM 13628 / NBRC 14792 / USDA 110)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.69 kDa
Sequence
MHRYRSHTCGALRESNIGETIRLSGWVHRVRDHGGVLFIDLRDHYGLTQCVVDPDSPAFSLAEKLRSEFVIKMDGKVRRRPEGTDNDDLPTGKIEIYVSEIEVLGPAGDLPLPVFGDQEYPEDIRLKYRFLDLRREKLHQNIMTRVEIIKSMRRRMEGQGFFEFNTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMMSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDVEMSFVTQEDVFAAMEPVITGVFEEFAKGKPVSKNWRRIPFAEALRKYGSDKPDLRNPIEMQEVSEHFRGSGFKVFARMLEDPKNQVWAIPAPGGGSRAFCDRMNSWAQGEGQPGLGYIMWREGGEGAGPLANNIGPERTAAIRAQIGVKEGDAAFFVAGDPDKFWKFSGLARNKVGEELNLTDKERFELAWIVDFPMYEYNEDDKKVDFSHNPFSMPQGGLEALKGQDPLTIKAFQYDITCNGYEIASGGIRNHVPEAMVKAFEIAGYGEQEVVDRFGGMYRAFQYGAPPHGGMAAGVDRIVMLLCGTTNLREISLFPMNQQAMDLLMGAPSEATTKQLRELHVRVNLPQK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.606 kDa
Sequence
MHRYRTHTCGALRDSNIGETVRLSGWCHRIRDHGGVLFVDLRDHYGITQCVVDPDSKAFGLAEKLRSEWVVRMEGKVRRRPEGTDNAELPTGQVELYVADIEVLGPAAELPLPVFGEQEYPEDIRLKYRFLDLRREKLHQNIMTRGAIIDSMRRRMKEQGFFEFQTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMMSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDVEMSFVEQEDVFAAMEPVITGVFEDFAKGKPVTKGWPRIPFAEALRKYGTDKPDLRNPIEMQDVSEHFRGSGFKVFARMLEDTKNQVWAIPAPGGGSRAFCDRMNSWAQGEGQPGLGYIMWREGGEGAGPLANNIGPERTAAIRTQLGTKEGDAAFFVAGDPEKFWKFAGLARTKVGEELNLIDKDRFALAWIVDFPMYEYNEDDKKVDFSHNPFSMPQGGLEALQTKDPLTIKAFQYDIACNGYEIASGGIRNHKPEAMVKAFEIAGYGEQEVVDRFGGMYRAFQYGAPPHGGMAAGVDRIVMLLCGTTNLREISLFPMNQQAMDLLMGAPSEATTKQLRELHIRTNLPNK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bradyrhizobium sp. (strain ORS 278)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.536 kDa
Sequence
MHRYRTHTCGALRDSNIGETVRLSGWCHRIRDHGGVLFVDLRDHYGITQCVVDPDSKAFGLAEKLRSEWVVRMEGKVRHRPEGTENPELPTGQVELYVADIEVLGPAAELPLPVFGEQDYPEDIRLKYRFLDLRRDRLHQNIMTRGAIIDSMRRRMKEQGFFEFQTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMMSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDVEMSFVEQEDVFAAMEPVITGVFEDFAKGKPVTKGWPRIPFAEALRKYGTDKPDLRNPLEMQDVSEHFRGSGFKVFARMLEDPKNQVWAIPAPGGGSRAFCDRMNSWAQGEGQPGLGYIMWREGGEGAGPLANNIGPERTAAIRSQLGTKEGDAAFFVAGDPDKFWKFAGLARTKVGEELNLIDKDRFALAWIVDFPMYEYNEDDKKVDFSHNPFSMPQGGLEALTTKDPLTIKAFQYDIACNGYEIASGGIRNHKPEAMVKAFEIAGYGEQEVVDRFGGMYRAFQYGAPPHGGMAAGVDRIVMLLCGTTNLREISLFPMNQQAMDLLMGAPSEATTKQLRELHIKPNLPNK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Haemophilus parasuis serovar 5 (strain SH0165)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.54 kDa
Sequence
MMRSHYCGVLNRTHVGEQVTLSGWVHRVRNLGRFIFMQIRDREGIVQVFFDEKDEALFKQASALRAEACVQIKGEVIARDTSQINKEMATGEIEVLVKELVVYNNSEVLPLDFNQNNTEEQRLKYRYLDLRRPEMAERLKTRAKITSFVRRYMDDNGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIAKCFRDEDLRADRQPEFTQIDVETTFMTAPEVRAMMEKMIRGLWLDRLNVDLGEFPQMTFAEAMRRYGSDKPDLRNPLELVDVADILKDVEFKVFSGPANDPEGRVAVIRVPNGAEITRKQIDEYTQFVGNYGAKGLAWAKVNDVNAGLEGLQSPIAKFLTDDVVKALLARVNAQNGDIIFFGADSEKVVTDAMGALRLKVGRDLGLTDLTAWKPLWVVDFPMFEKDDEGNWSAMHHPFTAPKDLSPEELVQNPKGAVANAYDMVINGYEVGGGSVRIFDPKMQQTVFGILGINEEEQKEKFGFLLDALKFGTPPHAGLAFGLDRLTMLITGTENIRDVIAFPKTTAAACLMTDAPSFGNPKALAELAIQTTVEKES

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Lactococcus lactis subsp. lactis (strain IL1403)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.545 kDa
Sequence
MKRTNYAGNITEEYLNQTVTVKGWVAKRRNLGGLIFIDLRDREGIVQIVVNPETAAADVAEAADKARNEFVLEVTGKVVERASKNDKIKTGGIEIEATAIEILSTSKTTPFEIKDDVEVLDDTRLKYRYLDLRRPEMLKNITMRHATTRSIREYLDGAGFIDVETPFLNKSTPEGARDYLVPSRVNKGEFYALPQSPQLMKQLLMTAGLDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLSEEEIQDLTEELIAKVMKDVKGIDVTLPFPRMKYDDAMNFYGSDKPDTRFELLLTDLSALAKTIDFKVFQEAEVVKAIVVKDAADKYSRKSIDKLTEQAKQNGAKGLAWVKFEKGEFAGGVSKFLAESTDSFVNELKLTDNDLVLFVADSLDVANSALGALRLTIGKQQGLIDFRQFNFLWVIDWPMFEWSDEEERYMSAHHPFTLPTKETQAFLSADGHSKDSDLKKVRAHAYDIVLNGYELGGGSLRINTRQLQEEMLSALGFKLEDANEQFGFLLEALDYGFPPHGGLALGLDRFVMLLAGKDNIREVIAFPKNNKASDPMTQAPSIVAEKQLEELSIKLANKDQ

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Lactococcus lactis subsp. cremoris (strain MG1363)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.529 kDa
Sequence
MKRTNYAGNITEEYLNQTITVKGWVAKRRNLGGLIFIDLRDREGIVQIVVNPETAATEVAEAADKARNEFVLEVTGKVVERASKNDKIKTGGIEIEATAIEILSTSKTTPFEIKDDVEVLDDTRLKYRYLDLRRPEMLKNITMRHATTRSIREYLDGAGFIDVETPFLNKSTPEGARDYLVPSRVNKGEFYALPQSPQLMKQLLMTAGLDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLGEEEIQELTEELIAKVMKDVKGIDVTLPFPRMNYDDAMNFYGSDKPDTRFELLLTDLSALAKTVDFKVFQEAEVVKAIVVKGAADKYSRKSIDKLTEQAKQNGAKGLAWVKFEKGEFAGGVSKFLAESTDSFVNELKLTDNDLVLFVADSLDVANSALGALRLTIGKQQGLIDFRKFNFLWVIDWPMFEWSDEEERYMSAHHPFTLPTKETQAFLSADGHRKDSDLKKVRAHAYDIVLNGYELGGGSLRINSRDLQEEMLSALGFKLEDANEQFGFLLEALDYGFPPHGGLALGLDRFVMLLAGKDNIREVIAFPKNNKASDPMTQAPSIVADKQLEELSIKLANKDQ

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Lactococcus lactis subsp. cremoris (strain SK11)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.543 kDa
Sequence
MKRTNYAGNITEEYLNQTITVKGWVAKRRNLGGLIFIDLRDREGIVQIVVNPETAATEVAEAADKARNEFVLEVTGKVVERASKNDKIKTGGIEIEATAIEILSTSKTTPFEIKDDVEVLDDTRLKYRYLDLRRPEMLKNITMRHATTRSIREYLDGAGFIDVETPFLNKSTPEGARDYLVPSRVNKGEFYALPQSPQLMKQLLMTAGLDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLGEEEIQELTEELIAKVMKDVKGIDVTLPFPRMNYDDAMNFYGSDKPDTRFELLLTDLSALAKTVDFKVFQEAEVVKAIVVKGAADKYSRKSIDKLTEQAKQNGAKGLAWVKFEKGEFAGGISKFLAESTDSFVNELKLTDNDLVLFVADSLDVANSALGALRLTIGKQQGLIDFRKFNFLWVIDWPMFEWSDEEERYMSAHHPFTLPTKETQAFLSADGHRKDSDLKKVRAHAYDIVLNGYELGGGSLRINSRDLQEEMLSALGFKLEDANEQFGFLLEALDYGFPPHGGLALGLDRFVMLLAGKDNIREVIAFPKNNKASDPMTQAPSIVADKQLEELSIKLANKDQ

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Lactobacillus salivarius (strain UCC118)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.562 kDa
Sequence
MRRTTYAGLVDEKYLDQEVCLKGWVQKRRNLGNLIFVDLRDIEGIVQLVFSQEFNPEALKVAEQLRSEYVIEVKGKVVARGEKAINPNMRTGKVEVEVSDIEILNKAKTTPFDIADDINASDDLRLQYRYLDLRRPEMQKALMIRNRITQTVHSYLDENHFLDIETPYLTRSTPEGARDYLVPSRVYPGHFYALPQSPQLFKQLLMGAGYDRYYQIARCFRDEDLRGDRQPEFTQIDIETSFMSAEEIQEMTEGLLKRVMKETLDVDIKTPIQRITWNEAMDRFGSDKPDIRFGMELKDMSGAVRNAGFKVFDMTLENGGQVKAITVPGGADKYSRKQIEEKQEYIKRFGAKGLAWVKVTDDGLTGPIAKFFTERAEDIKEAAEAKSGDLILFVASNRKVVADSLGYLRVAIAKEMDMINKDEFAFIWVVDWPLFEYSEEFDRYIAAHHPFTMPNEEDLDLLETDPHKCHAQSYDIVLNGYELGGGSIRIHRRDIQEAMFKALGFTKEKAEEQFGWFMDALDFGFPPHGGLALGLDRFAMLLAGKDNIREVIAFPKNSKASEPLTHAPSTVAPKQLDELYLKTDVPEEDE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Lactobacillus sakei subsp. sakei (strain 23K)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.144 kDa
Sequence
MKTRTTYSGLVDETFVGQTVTLHGWVQKRRSLGNLIFVDLRDREGLVQLVFNQDNADILALANTLRNEYVIEVTGMVQARDEAAINPDMKTGKVEVIVSELTILNEAKNLPFEIKDGITTSEETKLKYRYLDLRRPEMQQAIIRRSQITQAAHKYLDNNGFLNIETPDLTRSTPEGARDYLVPSRVYPGSFYALPQSPQVFKQLLMDAGFDRYYQMARCFRDEDLRGDRQPEFTQIDVETSFMSAEEIQEQAEGIIKQVMQDVMHIDVPTPFKRMKWQEAMDRYGSDKPDIRFDLEIQDLTEMMKTSSFKVFSDTANSGNLVRAIVVPEGAAKYSRKMLDEQTEYIKRYGARGMAWVKVVDGELTGPAAKFLKEQEAELLSALSAKDGDLVLFVADKFQVVCDSLGYLRKHFAHDMGLVDESQFAYLWVVDWPLFEYDEGFGRWIAAHHPFTRPNDSDVDLLETDPHKAHAQSYDIILNGYELGGGSLRIYQRDIQERMFKALGISPETYEEQFGHLLSAMDYGFPPHGGFAIGLDRFAMLLAGRDNIRDVIAFPKNSHASEPMTNAPSRVAPAQLDELGLEVEPEVEKD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.735 kDa
Sequence
MHRYRSHTCGALRDSHIDQTVRLSGWCHRIRDHGGVLFIDLRDHYGLTQCVADPDSPAFAQAEKLRSEWVVRIDGKARLRPAGTENPELPTGQIEIYINEIEVLGPADELPLPVFGEQEYPEDIRLKYRFLDLRREKLHQNIMTRGAIVDSMRKRMKEQGFFEFQTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMMSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVEQDDVFAAVEPVVTGVFEEFAKGKPVTKNWPRIPFAESLRKYGTDKPDLRNPLLMQDVSQHFRGSGFKVFARMLEDSKNQVWAIPGPGGGSRAFCDRMNSWAQGEGQPGLGYIMWREGGEGAGPLANNIGPERTEAIRQQLGLKAGDAAFFVAGDPAKFWKFAGLARTKLGEELNVIDKDRFELAWIVDFPMYEYNEDEKKVDFSHNPFSMPQGGLDALNNQDPLTIKAFQYDITCNGYEIASGGIRNHRPEAMVKAFEIAGYGENDVVERFGGMYRAFQYGAPPHGGMAAGVDRVVMLLCGTTNLREISLFPMNQRAEDLLMGAPSDVTPKQLRELHIRLNLPQD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.704 kDa
Sequence
MHRYRSHTCGALRDSHIDQTVRLSGWCHRIRDHGGVLFIDLRDHYGLTQCVADPDSPAFALAEKLRSEWVVRIDGKARRRPAGTENPELPTGDVEIYVTEIEVLGPAAELPLPVFGEQEYPEDIRLKYRFLDLRRENLHQNIMTRGAIVDSMRKRMKEQGFFEFQTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMMSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVEQDDVFAAVEPVITGVFEEFAKGKPVTRNWPRIPFAESLRKYGTDKPDLRNPLLMQDVSEHFRGSGFKVFARMLEDSKNQVWAIPGPGGGSRAFCDRMNSWAQGEGQPGLGYIMWREGGEGAGPLANNIGPERTEAIRVQLGLKAGDAAFFVAGDPAKFWKFAGLARTRLGEELNLIDKDRFELAWIVDFPMYEYNEEDKKVDFSHNPFSMPQGGLDALNTQDPLTIKAFQYDITCNGYEIASGGIRNHRPEAMVKAFEIAGYGENDVVERFGGMYRAFQYGAPPHGGMAAGVDRIVMLLCGTNNLREISLFPMNQRAEDLLMGAPSEVAPKQLRELHIRLNLPQN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Nocardioides sp. (strain ATCC BAA-499 / JS614)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.541 kDa
Sequence
MIRTQDAGALRAENVGQTVTLAGWVANRRDHGGVAFIDLREASGVVQVVIRDEQVAHHLRAEYCLAVTGEVTRRKEGNENPNLATGEVEVVANEVEVLSAAAPLPFPISDHVDVGEEARLKHRYLDLRRSGPNNALRLRSKVNKAARDVLDRHDFVEIETPTLTRSTPEGARDFLVPARLQPGSWYALPQSPQLFKQLLMVAGMERYYQIARCYRDEDFRADRQPEFTQLDIEMSFVEQDDVLAVAEEVLVALWKLVGHDVPVPLPRMTYAESMERYGTDKPDLRMGQELVDCTAYFADTPFRVFQADYVGAVVMPGGASQPRKQLDAWQEWAKQRGAKGLAYVLVQDDGELTGPVSKNITDGESAGLAEHTGAKPGDCIFFAAGAPKPSRALLGAARLEIGRRCDLIDEDAWSFLWVVDAPLFEPTADATASGDVALGYSAWTAVHHAFTSPQDVDGFDADPGSALAWAYDIVCNGNEIGGGSIRIHREDVQKRVFAIMGIDEAEAQEKFGFLLEAFKYGAPPHGGIAFGWDRIVALLAGTESIRDVIAFPKSGGGFDPLTAAPAPITPEQRKEAGVDARPQQDLPPQS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Oligotropha carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.845 kDa
Sequence
MHRYRSHTCGALRESDIDSNVRLSGWCHRIRDHGGLLFIDLRDHYGITQCVVDPDSKAFRLAETLRSEWVVKFDGRVRRRPDGTDNPELPTGAVEVFINEIEVLGEAAELPMPVFGDQEYPEEIRLKYRFLDLRRDRLHQNIMTRGKIIDSMRARMKEVGFFEFQTPILTASSPEGARDFLVPSRIHPGKFYALPQAPQQYKQLLMMSGFDRYFQIAPCFRDEDPRADRLPGEFYQLDLEMSFVTQEDVFAAMEPVITGVFEDFADGKPVTKNWPRIPFAEALRKYGTDKPDLRNPLIMQDVSEHFRGSGFKVFARMLEQEGNEVWAIPGPAGGSRAFCDRMNSWAQGEGQPGLGYIMWREGGEGAGPLANNIGPERTAAIRDQLGLKEGDAAFFVAGDPQKFWKFAGLARTKLGEELNLIDKDRFELAWIVDFPMYEYNEDEKKVDFSHNPFSMPQGGLEALQTQDPLTIKAFQYDIACNGYEIASGGIRNHKPAAMVKAFEIAGYGEETVIERFGGMYRAFQYGAPPHGGMAAGVDRIVMLLCGTNNLREISLFPMNQRAEDLLMGAPSDVTTQQLRELHIRLNLPQN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Citrobacter koseri (strain ATCC BAA-895 / CDC 4225-83 / SGSC4696)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.662 kDa
Sequence
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNVNADMATGEIEVLASDLTIINRADSLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWQEVKGVDLGDFPIMTFAEAERRYGSDKPDLRNPMELVDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLSRKQIDDYGNFIKIYGAKGLAYIKVTERAKGLEGINSPVAKFLNAEIVEAILDRTAAQDGDMIFFGADNKKVVADALGALRLKVGKDLNLTDEAKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDLTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHSGDMQQTVFGILGINEQEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPAALAELGIDVVKKAENN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Photorhabdus luminescens subsp. laumondii (strain DSM 15139 / CIP 105565 / TT01)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.229 kDa
Sequence
MRTDYCGQLNLTHEGQKVTLCGWVNRRRDLGGLIFIDMRDREGIVQVFFDPDQQAAFSQAAELRNEFCIQITGTVRARPDSQINKDMATGEIEVFAESLNIINRSEPLPLDSNQTNSEEQRLKYRYIDLRRPEMANRLKTRAKITSFVRRFMDNQGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAEQVREMMEKMIRELWFEIDGVDLGHFPVMTFAEVMRRFGSDKPDLRNPLELVDVADLVKDVEFSVFAEPANDSKGRVAVIRVPGGAELSRKQIDEYGKFVGIYGAKGLAWIKVNARAAGLEGVQSPIAKFLNAEVIEGLLSRTDAQDGDILFFGAGSVKVVTDALGALRLKLGRDLNLTKLDSWRPLWVIDFPMFEDDGEGGLTAMHHPFTSPCNMSAAELAQDPVSAIANAYDMVINGYEVGGGSVRIHRNEMQQAVFRILGINEQEQQEKFGFLLDALKFGTPPHAGLAFGLDRLVMLLTGTDNIRDVIAFPKTTAAACLMTEAPSYANPASLEELSISVVAKKESE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Francisella tularensis subsp. holarctica (strain FTNF002-00 / FTA)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.805 kDa
Sequence
MRTHYSSDINEKLQGQKVTVCGWVHRRRDHGGVIFLDIRDRTGLVQLVFNPDNDNFKVADSLRSEFVIKAEGVVNLRPEGQENKNISSGKVEIIGDSIEVINKSKTIPFQLDDFQSTGEDVKLKYRYIDLRRPEMQHKLITRSKAIRYVRNFLDNNGFLDIETPFLTKATPEGARDYLVPSRNFNGKFYALPQSPQLFKQLLMVSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIEASFIDEAFIMSTMERMIAGLFKETIGVEFATPFQVMTFADAIDKYGSDKPDLRIPLEFVNIKEDMQNEEFKVFSGPANDPQSRVIALRISGGNDKLTRKMIDEYTKFVGIYGAKGLAYIKINSLSQGKEGLQSPIVKNISEETLFKVIEKTSAKEDDLLFFGAGKTKIVNDSMGALRAKIGEDLDLFNKDWAPLWVVDFPMFEKDDNRLYAMHHPFTAPKVSSVEDLVNTNPEELSSRAYDMVINGYEVGGGSIRIHKQDIQAKVFNLLGISDDEAREKFGFMLDALSYGTPIHGGIAFGVDRLIMLLTGTTNIRDVIAFPKTQTASCLMTEAPSTVSLEQLNELGIAVKKEER

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Francisella tularensis subsp. holarctica (strain LVS)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.805 kDa
Sequence
MRTHYSSDINEKLQGQKVTVCGWVHRRRDHGGVIFLDIRDRTGLVQLVFNPDNDNFKVADSLRSEFVIKAEGVVNLRPEGQENKNISSGKVEIIGDSIEVINKSKTIPFQLDDFQSTGEDVKLKYRYIDLRRPEMQHKLITRSKAIRYVRNFLDNNGFLDIETPFLTKATPEGARDYLVPSRNFNGKFYALPQSPQLFKQLLMVSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIEASFIDEAFIMSTMERMIAGLFKETIGVEFATPFQVMTFADAIDKYGSDKPDLRIPLEFVNIKEDMQNEEFKVFSGPANDPQSRVIALRISGGNDKLTRKMIDEYTKFVGIYGAKGLAYIKINSLSQGKEGLQSPIVKNISEETLFKVIEKTSAKEDDLLFFGAGKTKIVNDSMGALRAKIGEDLDLFNKDWAPLWVVDFPMFEKDDNRLYAMHHPFTAPKVSSVEDLVNTNPEELSSRAYDMVINGYEVGGGSIRIHKQDIQAKVFNLLGISDDEAREKFGFMLDALSYGTPIHGGIAFGVDRLIMLLTGTTNIRDVIAFPKTQTASCLMTEAPSTVSLEQLNELGIAVKKEER

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Francisella tularensis subsp. holarctica (strain OSU18)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.805 kDa
Sequence
MRTHYSSDINEKLQGQKVTVCGWVHRRRDHGGVIFLDIRDRTGLVQLVFNPDNDNFKVADSLRSEFVIKAEGVVNLRPEGQENKNISSGKVEIIGDSIEVINKSKTIPFQLDDFQSTGEDVKLKYRYIDLRRPEMQHKLITRSKAIRYVRNFLDNNGFLDIETPFLTKATPEGARDYLVPSRNFNGKFYALPQSPQLFKQLLMVSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIEASFIDEAFIMSTMERMIAGLFKETIGVEFATPFQVMTFADAIDKYGSDKPDLRIPLEFVNIKEDMQNEEFKVFSGPANDPQSRVIALRISGGNDKLTRKMIDEYTKFVGIYGAKGLAYIKINSLSQGKEGLQSPIVKNISEETLFKVIEKTSAKEDDLLFFGAGKTKIVNDSMGALRAKIGEDLDLFNKDWAPLWVVDFPMFEKDDNRLYAMHHPFTAPKVSSVEDLVNTNPEELSSRAYDMVINGYEVGGGSIRIHKQDIQAKVFNLLGISDDEAREKFGFMLDALSYGTPIHGGIAFGVDRLIMLLTGTTNIRDVIAFPKTQTASCLMTEAPSTVSLEQLNELGIAVKKEER

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.727 kDa
Sequence
MRTHYSSDINEKLQGQKVTVCGWVHRRRDHGGVIFLDIRDRTGLVQLVFNPDNDNFKVADSLRSEFVIKAEGVVNLRPEGQENKNISSGKVEIIGDSIEVINKSKTIPFQLDDFQSTGEDVKLKYRYIDLRRPEMQHKLITRSKAIRYVRNFLDNNGFLDIETPFLTKATPEGARDYLVPSRNFNGKFYALPQSPQLFKQLLMVSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIEASFIDEAFIMSTMERMIAGLFKETIGVEFATPFQVMTFADAIDKYGSDKPDLRIPLEFVNIKEDMQNEEFKVFSGPANDPQSRVIALRIPGGNDKLTRKMIDEYTKFVGIYGAKGLAYIKINSLSQGKEGLQSPIVKNISEETLFKVIDKTSAKEGDLLFFGAGKAKIVNDSMGALRAKIGEDLDLFNKDWAPLWVVDFPMFEKDDNRLYAMHHPFTAPKVSSVEDLVNTNPEELSSRAYDMVINGYEVGGGSIRIHKQDIQAKVFNLLGISDDEAREKFGFMLDALSYGTPIHGGIAFGIDRLIMLLTGTTNIRDVIAFPKTQTASCLMTEAPSTVSLEQLNELGIAVKKEER

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Francisella tularensis subsp. tularensis (strain WY96-3418)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.727 kDa
Sequence
MRTHYSSDINEKLQGQKVTVCGWVHRRRDHGGVIFLDIRDRTGLVQLVFNPDNDNFKVADSLRSEFVIKAEGVVNLRPEGQENKNISSGKVEIIGDSIEVINKSKTIPFQLDDFQSTGEDVKLKYRYIDLRRPEMQHKLITRSKAIRYVRNFLDNNGFLDIETPFLTKATPEGARDYLVPSRNFNGKFYALPQSPQLFKQLLMVSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIEASFIDEAFIMSTMERMIAGLFKETIGVEFATPFQVMTFADAIDKYGSDKPDLRIPLEFVNIKEDMQNEEFKVFSGPANDPQSRVIALRIPGGNDKLTRKMIDEYTKFVGIYGAKGLAYIKINSLSQGKEGLQSPIVKNISEETLFKVIEKTSAKEGDLLFFGAGKAKIVNDSMGALRAKIGEDLDLFNKDWAPLWVVDFPMFEKDDNRLYAMHHPFTAPKVSSVEDLVNTNPEELSSRAYDMVINGYEVGGGSIRIHKQDIQAKVFNLLGISDDEAREKFGFMLDALSYGTPIHGGIAFGVDRLIMLLTGTTNIRDVIAFPKTQTASCLMTEAPSTVSLEQLNELGIAVKKEER

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Hahella chejuensis (strain KCTC 2396)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.738 kDa
Sequence
MRSHYCGEVNESLVDQEVTLCGWVHRRRDHGGVIFLDLRDRDGIAQVVYDPDTNEVFQLAEQIRDEFVVKVTGRVRLRPEGKANTDMSTGMVEVLGKQLEILSTAKTPPFQLDEFVQVGEDVRLRYRYMDLRRPEMLNKLRFRSKVTSYIRNFLDGNGFMDVETPILTRATPEGARDYLVPSRTHEGSFFALPQSPQLFKQLLMMSGVDRYYQIAKCFRDEDLRADRQPEFTQVDIETSFLNENEIMSITERLVRDMFRDLLEVELPEFPRMPFSEAMNRYGSDKPDLRIPLELVDVGDLLTNVSFNVFSGPANDPKSRVAALRLPKGGELLSRKQIDDYTKFVGIYGAKGLPYIKVNEKAKGLDGLQSPIVKHIADAIDPLLERVGAEDGDIIFFGTDKTRVVNEALGALRVKLGHDLNLLEKQWAPLWVVDFPMFEEDGEGGWTAIHHPFTAPSCAVEMLESDPENALSRAYDMVLNGTELGGGSVRIHDSDMQETVLRILGIGQDEAREKFGFLLDALKFGCPPHGGLAFGLDRLVMLMTGAQSIREVIAFPKTQSAMCMMTQAPGKVDPKQLRELNIRLRKTEQPE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Halothermothrix orenii (strain H 168 / OCM 544 / DSM 9562)
Length
590 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.815 kDa
Sequence
MAESINGLKRTHYAGKISTQQIGKKVTVMGWVQKRRDHGGVIFIDLRDRSGIVQVVFNPDNNERAFKKATELRSEYVIAVEGEVEKRPEGNINPDIPTGEIEIRGNRLRILDESETPPFEIDDDINVGEDLRLKYRYLDLRRPRMKKNLELRHRVMKTTRDYLDDNGFWEVETPILTRSTPEGARDYLVPSRIHPGHFYALPQSPQLFKQLLMVGGVERYFQIARCFRDEDLRANRQPEFTQIDIEMSFIDKEDVFSLVNGLMKRLFALVDIEIPEKIPVMPYQEAIDRFGSDKPDLRFGMELKDVSDVVKDSEFRVFSGVVKDGGQVKGINFKGGAISPRSKIDGYTDYVKIFGAKGLAWIALKENGLKSPIAKFLSEKELEGIKEKMGAQTGDLLLFVADKPSIVADALGNLRLKIAREEGLIPDGVYKFVWVVDFPLMEYDEDEGRYVAKHHPFTAPLDEDIPLLDSNPEKIRSKAYDFVLNGEELGGGSIRINNKDLQMKVFNALNISEEKASDKFGFLLEAFNYGAPPHGGIAFGLDRLLMVLSGSESMRDVIAFPKTQKASSPLTEAPSTVAEKQLRELHIKID

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Mannheimia succiniciproducens (strain MBEL55E)
Length
590 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.646 kDa
Sequence
MMRSHYCGGLNRENIGQEVTLSGWVHRRRDLGGLIFIDMRDREGIVQVCFDPKYQQALTRAASLRNEFCIQIKGEVIARPDNQINKNMATGEVEVLAKELSVYNAADVLPLDFNQNNTEEQRLKYRYLDLRRPEMAQRLKTRAKITSFVRRFMDDNGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFLTAPEVREIMEKMIHGLWLNTINVDLGKFPVMTWTEAMQRFGSDKPDLRNPLEITDVADIVKDVDFKVFSGPANDPNGRVAVIRVPNGASVTRKQIDEYTQFVGIYGAKGLAWLKVNDVNAGLEGVQSPIAKFLTEEKIKAIFDRTSAQTGDILFFGADKWQTATDALGALRLKLGRDLALTQLDQWAPLWVIDFPMFERDEEGNLAAMHHPFTSPKDFSPEQLEADPTGAVANAYDMVINGYEVGGGSVRIFDPKMQQTVFRILGIDEQQQREKFGFLLDALKFGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPQALEELSISVVKTDKE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Bacillus cytotoxicus (strain DSM 22905 / CIP 110041 / 391-98 / NVH 391-98)
Length
589 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.065 kDa
Sequence
MAERTHACGRVTVEAIGQTVQLKGWVQKRRDLGGLIFIDLRDRTGIVQVVFSPETSKEALEVAETIRGEYVLHVEGTVVARGAGAINENMATGQIEVQATKVTVLNAAKTTPIIIADDTDASEDVRLKYRYLDLRRPVMYNTFKMRHDVTKTIRNFLDTEEFLEVETPILTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMVGGFERYYQVARCFRDEDLRADRQPEFTQIDIEASFLTQEEILDMMERMMTKVMKDVKGVEISVPFPRMTYADAMARYGSDKPDTRFEMELTDLSEFAAGCGFKVFTGAVENGGQVKAINAKGAASKYSRKDIDALTEFVKVYGAKGLAWLKVEEDGLKGPIAKFFNEEEANVIMTTLEASAGDLLLFVADKKSVVADSLGALRLRLGKELELIDENKFNFLWVTDWPLLEYDEEANRYFAAHHPFTMPFREDVELLETAPEKARAQAYDLVLNGYELGGGSLRIYERDVQEKMFKALGFTQEEAREQFGFLLEAFEYGTPPHGGIALGLDRLVMLLAGRTNLRDTIAFPKTASASCLLTDAPSPVAGAQLEELHLKLNVKE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl)
Length
589 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.653 kDa
Sequence
MYRSHTCGELRPAHAGQEVTLAGWVHRRRDHGDLIFIDLRDRYGITQVVFNSAHPTAHEVAETVRSEYVLQVRGKVRIRPPEAVNPDLATGEIELEASEAQVLNPARTPPIYIAKEGGEDESVRLKYRYLDLRRERMQRNLILRHRVVKFIRDFLDAEGFLEIETPILIKSTPEGARDYLVPSRLHPGKFYALPQSPQQLKQLLMVAGYDKYFQIARCFRDEDQRADRQPEFTQLDMEMSFVDQDDVLDLIERMFTALCRTVVPHKHLPTPFRRLSYAEAMERYGSDKPDLRYGLELVNLSDLLIETPFQVFRNVLNSGGQVKGIRAPGCAHFSRKQIDELTDVVRAGGAKGLAWAVLPTDGGEVRSSFAKNLAPGEFAAIVERMQAEAGDLLLIVADQPAVVAASLDKLRRNLAERLQLADPNTLCFAWIVDFPLVEWNEDEQRWDAVHHPFTAPKDEDMHLLATDPGKVRAKAYDLILNGYEAGGGSIRIHRRDVQQQIFSLLGISEELAQAQFGHMLEAFEYGAPPHGGIAPGIDRLVMILADEPTIREVMAFPKTQQAVDLMTNAPSPVDERQLKELHIRIVMPE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Mycobacterium leprae (strain Br4923)
Length
589 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.631 kDa
Sequence
MLRSHGAGVLRKSDAGQQVTLAGWVSRRRDHGGVIFIDLRDSSGITQAVFREPDVLAQAHRLRAEFCIAVSGVVEIRPEGNANAEIPTGDIEVNATSLTVLGESAPLPFQLDEPAGEELRLKYRYLDLRRDGPGSAIRLRSKVNATARAVLARHDFVEIETPTITRSTPEGARDFLVPARLRPGTFYALPQSPQLFKQLLMVAGMERYYQIAHCYRDEDFRADRQPEFTQLDMEMSFVDAEDVIAISEEILTELWMLIGYHIPAPIPRISYADAMRRFGSDKPDLRFGLELVECTEFFCDTTFRVFQAPYVGAVVMPGGAAQPRRTLDEWQDWAKQRGHRGLAYVLVTDDGTLGGPVAKNFSDAERSRLASHVGAEPGDCIFFSAGPAKSSRALLGAARGEIANRLGLIDPEAWAFVWVVDPPLFERADEATKVGEMAVGSGAWTAVHHAFTSPKPEFEDSIESDPGSVLADAYDIVCNGHEIGSGSVRINRRDIQERVFAVMGLEKAEAEEKFGFLLEAFTFGAPPHGGIAFGWDRTNALLAGMESIREVIAFPKTGGGVDPLTDAPASITAQQRKESGIDTKPKEVE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Mycobacterium leprae (strain TN)
Length
589 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.631 kDa
Sequence
MLRSHGAGVLRKSDAGQQVTLAGWVSRRRDHGGVIFIDLRDSSGITQAVFREPDVLAQAHRLRAEFCIAVSGVVEIRPEGNANAEIPTGDIEVNATSLTVLGESAPLPFQLDEPAGEELRLKYRYLDLRRDGPGSAIRLRSKVNATARAVLARHDFVEIETPTITRSTPEGARDFLVPARLRPGTFYALPQSPQLFKQLLMVAGMERYYQIAHCYRDEDFRADRQPEFTQLDMEMSFVDAEDVIAISEEILTELWMLIGYHIPAPIPRISYADAMRRFGSDKPDLRFGLELVECTEFFCDTTFRVFQAPYVGAVVMPGGAAQPRRTLDEWQDWAKQRGHRGLAYVLVTDDGTLGGPVAKNFSDAERSRLASHVGAEPGDCIFFSAGPAKSSRALLGAARGEIANRLGLIDPEAWAFVWVVDPPLFERADEATKVGEMAVGSGAWTAVHHAFTSPKPEFEDSIESDPGSVLADAYDIVCNGHEIGSGSVRINRRDIQERVFAVMGLEKAEAEEKFGFLLEAFTFGAPPHGGIAFGWDRTNALLAGMESIREVIAFPKTGGGVDPLTDAPASITAQQRKESGIDTKPKEVE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / 130Z)
Length
589 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.297 kDa
Sequence
MMRSHYCGALNRGNIGQEVTLSGWVHRRRDLGGLIFIDMRDREGIVQVCFDPKYQEALTAAADLRNEFCIQIKGEVTARPGNQINKNMATGEVEVLAKALSVYNASDVLPLDFNQNNTEEQRLKYRYLDLRRPEMAQRLKTRAKITSFVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFLTAPEVRAIMENMIRGLWLNILGADLGKFPIMTWNEAMTRFGSDKPDLRNPLEIADVADIVKDVDFKVFADPANDANGRVSVIRVPNGASITRKQIDEYTQFVGIYGAKGLAWLKVNDVNAGLEGVQSPIAKFLSEEKIKAIFDRTSAQTGDILFFGADKWQIATDAMGALRLKLGRDLGLTRLDEWQPLWVIDFPMFECDEEGNLAAMHHPFTSPKDFSPEQLEADPTAAVANAYDMVINGYEVGGGSVRIFDPKMQQTVFRILGIDEQQQREKFGFLLDALKFGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANQQALEELAITVVTKEE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Arcobacter butzleri (strain RM4018)
Length
589 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.053 kDa
Sequence
MRTHYCTDVTEKLIGQTVTVAGWVNSRRDHGGIIFIDLRDKSGLVQLVADPQDCKDALAIAETVRDEFVLIATGKVRARGEGLENPNLITGKIEIILENLVIENRSRPMPFDINDEKVNDEIKLRNRFLELRSKKSFDIFQLRSKATIQARNTLDELGFLDVETPILTKSTPEGARDYLVPSRVHAGEFYALPQSPQLFKQLLMVAGFDKYFQIAKCFRDEDLRADRQPEFTQIDVEMSFCNQEDVIKVAEKLIYDIFTKCGKNVPSTFRRMKYSEAMEKYGSDKPDLRFDMPLVDVIDIFANSTNEIFAEIAKDKKNNRIKALKCKNGDNIFSKRQMKSFEDYVRKFGAKGLGYFQMKEDGLKGPLTKFFSEADLEEIIKVTELEVGDVVFFGAGAKKVVWDYMGRFRLFLANEMNIVPKDAYEFLWVIDFPMFEVEDGRTKALHHPFTMPNVEKYDLDNIEDLEEIESIAYDIVLNGTELGGGSIRIHKEEIQSKVFKLMGISQEEAKEKFGFLLDALSYGAPSHGGFALGLDRMIMLLAGTDSIRDVIAFPKTQKAQCLLTQAPSAVDEEQLKELSIRIRKTVVDS

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Enterococcus faecalis (strain ATCC 700802 / V583)
Length
589 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.675 kDa
Sequence
MEKRTTYCGNVSAEFIEKEVVLKGWVQKRRDLGGVIFIDLRDREGIVQVVFNPEKSKEAWEIADKCRSEYVIEVKGQVVYRDKEAINPKMKTGEFEVMATDITILNTAKTTPFTIEDDNNVNDELRMKYRYLDLRRPSMTNNIKLRHQVTKTIRHYLDNHDFLDIETPYLGKSTPEGARDYLVPSRVHAGHFYALPQSPQLFKQLLMGAGFDRYYQIVRCFRDEDLRGDRQPEFTQIDIETTFLTPEEIQTYTENMLAEVMKETKGIEISVPFPRMSYDEAMARYGSDKPDTRFAMELIDVAEVVKDVDFKVFQAALENGGHVKALNAKGAADKYSRKDMDNLGKYVSQFGAKGLAWLKVEEDGLKGPIAKFLTEVSDELIAATNAEVGDILMFGADKPEIVAAALGAVRTRLGKELGLIDESKFNFLWIVDWPLFEYDEEAGRYVSAHHPFTQPKAEDVDRLATDPASVYAEAYDVVLNGYELGGGSLRIHTRELQEKMFETLGFTKEEAQDQFGFLLDALDYGFPPHGGIALGLDRLAMLLAGEENIREVIAFPKNGKAIDPMNNAPSLVSPLQLFELNIDVTAIDE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Haemophilus ducreyi (strain 35000HP / ATCC 700724)
Length
589 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.71 kDa
Sequence
MMRSHYCGTLNRSHVGQAVTLSGWVHRIRNLGRFIFMQIRDREGIVQVFFDEKDDTLFKVASQLRAEACVQIQGQVIARDEAQINPEMATGEIEVLVQNVLVYNNAEVLPLDFNQNNTEEQRLKYRYLDLRRHKMAENLKTRAKITSFVRRYMDEHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFLTAEEVRALMENMIHSLWLDRLNVDLGKFPIMSWQEAMQHFGSDKPDLRNPLELVDIADIVKNVEFNVFNEPANAIDGRVTVLRVPNGATLTRKQIDEYTQFVAIYGAKGLAWAKINDINAGMDGIQSPVAKFLNAEIFNALIERTAAQNGDILFFGADKWQVVTDAMGALRLKIGRDLALTDQTAWKPLWVIDFPMFERDGEGNLSAMHHPFTAPKDLSPDQLAADPIKAVANAYDMVINGYEVGGGSVRIFDPKMQQTVFNILGINEQDQQEKFGFLLDALKFGTPPHAGLAFGLDRLTMLITGTENIRDVIAFPKTTAAACLMTEAPSYANPQVLQELAIQTTVETE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Hamiltonella defensa subsp. Acyrthosiphon pisum (strain 5AT)
Length
589 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.75 kDa
Sequence
MRTHCCGELSLSVLNQTVCLCGWVDRRRDLGGLIFIDMRDFSGIVQVFFDPEQQALFEQASSLRNEFCIQITGKVKARPHHQINQKMLTGAVEVFSENLTIINCSEPLPLDRNQNNTEEQRLRYRYLDLRRPEMLARLKTRSKITSFVRQFLDKEGFLDVETPTLTKATPEGARDYLVPSRVQKGKFYALPQSPQLFKQLLMVSGVDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMTAQQVRTVTEKLIRQLWLQIKNIHLGAFPVMTFEEAIRRFGSDKPDLRNPLELVDLDDVLKNVDFKVFSEPANDAHSRVVGIRVPNGADISRKQIDEYTAFVHIYAARGLAWLKIKQADAGLEGIQSPIAKFLSPEILERILKRTQAKDGDLLFFGADKKKIVTDAMGALRLKLGLDRQLTQLDRWAPLWVIDFPMFSNDTETGLTAMHHPFTSPKNTNLSEFAANPETALANAYDMVINGYEVGGGSVRIHHSDLQQQVFSLIGIEANQQKQQFGFLLEALKYGAPPHAGIAFGLDRLVMLLTGTNNIRDVIAFPKTTAAACLMTDAPSFASDSSLQELFIDVVKKEKK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Idiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR)
Length
589 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.148 kDa
Sequence
MRTHYCGQINAELAGQEVTLCGWVNKRRDLGGLIFIDLRDREGLLQVVFDPDQKALFETANSLRQEFCVRLSGKVNRRPESQVNKNMATGEVELLATDLEIFSRSEPLPIDFNQQVSEEARLRYRYLDLRRPQMNEKLQFRAKVTSAVRRFFDDNGFLDIETPMLTRATPEGARDYLVPSRTHKGRFFALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDIETSFMSAEQVMEITEQMARDLFKQLLDVDLGEFPSMTWHEAMRRFGSDKPDLRNPLELVDVADVLKDVEFKVFSGPANDEEGRVAAIRLPGQAENVSRKMIDEYTQFVGIYGAKGLAWIKVNDRSAGREGLQSPVLKFLPDEVIEPLLERMQAETGDVLFFGSDKSHVVAEALGALRLKLGKDFELVSNEWKPLWVVDFPMFEVADDGSLAALHHPFTAPVNVTPEELKANPAAAISNAYDMVLNGVELGGGSVRIHENAMQQAVFEVLGIEKDEAQEKFGFLLEALKYGTPPHAGLAFGLDRLVMLMVGASSIRDVIAFPKTTTAACVLTDAPGAANPAALQELGVKSIVKEDE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chloroflexus aurantiacus (strain ATCC 29364 / DSM 637 / Y-400-fl)
Length
589 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.668 kDa
Sequence
MYRSHTCGELRPAHAGQEVTLAGWVHRRRDHGDLIFIDLRDRYGITQVVFNSAHPTAHEVAETVRSEYVLQVRGKVRIRPPEAVNPDLATGEIELEASEAQVLNPARTPPIYIAKEGGEDESVRLKYRYLDLRRERMQRNLILRHRVVKFIRDFLDAEGFLEIETPILIKSTPEGARDYLVPSRLHPGKFYALPQSPQQLKQLLMVAGYDKYFQIARCFRDEDQRADRQPEFTQLDMEMSFVDQDDVLDLIERMFTALCRTVVPHKHLPTPFRRLSYAEAMERYGSDKPDLRYGLELVNLSDLLIETPFQVFRNVLNSGGQVKGIRAPGCAHFSRKQIDELTDVVRAGGAKGLAWAVLPTDGGEVRSSFAKNLAPGEFAAIVERMQAEAGDLLLIVADQPAVVAASLDKLRRNLAERLQLADPNTLCFAWIVDFPLVEWNEDEQRWDAVHHPFTAPKDEDMHLLATDPGKVRAKAYDLILNGYEAGGGSIRIHRRDVQQQIFSLLGISEEQAQAQFGHMLEAFEYGAPPHGGIAPGIDRLVMILADEPTIREVMAFPKTQQAVDLMTNAPSPVDERQLKELHIRIVMPE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Bacillus clausii (strain KSM-K16)
Length
589 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.682 kDa
Sequence
MKRTHHCGQLDKTLAGQQVQLKGWVQRRRDLGQVIFLDLRDRSGIVQVVCSPEVSEEALKAADRVRNEYLVAVSGIVVERNEQAVNDKLATGAIEVHVRELEILNVSKSLPFQIEADTDAAEDVRLKYRYLDLRRPDMQEAFAMRHKIMKSVRDFLDADGYLEIETPMLTKSTPEGARDYLVPSRVHHGQFYALPQSPQIFKQLLMVSGFEKYFQIVRCFRDEDLRADRQPEFTQIDIETSFLDTEDILAMTEAMMEKLLKETHGLELKRPFSRMTYEEAMNRYGSDKPDTRFGMELIELSDVLKDTEFKVFKGALEAGGIIKGLTLKGGADKLSRKDIDALADFVKPYGAKGLAWLKVDDEGIKGPIAKFFNEAQTAALLAAMDAEAGDLLFFGADKKQVVFHALGALRLKFGKEFQLIDENAFHFLWVTDFPLVEYDEQAKRFVALHHPFTRPKAEDLDLMETHPEQVRAEAYDLVLNGFELGGGSQRIYERELQEKMFKLLGFSSEAAKEEFGFLLEAFDYGTPPHGGIALGLDRIVMLLARKSNLREVIAFPKTASASDLLTEAPNKVSVEQLIDLNLSIISKRS

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Baumannia cicadellinicola subsp. Homalodisca coagulata
Length
589 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.501 kDa
Sequence
MRTIYCGQLNKSHLGQEVILCGWVYRYRNLGRLIFIELSDREGRVQVVFDLTHPSIFSNAAKLRNDFCIQLHGIVRTRLDKQINYNITTGEIEVLATNLTILNSSQPLPLDINFHNNEEQRLKFRYLDLRNPEMAQRLKLRAKITSLVRHFMEKKGFLDIETPMLTKTTPEGARDYLVPSRVHKGQFYALPQSPQLFKQLLMISGFDRYYQIVKCFRDEDLRADRQPEFTQIDVEASFINAEQICKIMEDLVRHLWREIQEVELENFQYMSYTAAMYRFGSDKPDLRNPIEIVDVVDLVKNTTCTILADIAKDIKNRVVALRVPNGAKLSLNDIKKYEKYIQTYGIKFIIWMKVYQGKDGVKTTQSSITKYLLPEDIMSIIERTGACDGDILFFAAGNNNIINNVMGALRIKLGCDLKLNRENSWAPLWIVDFPMFEKDDEGNLHAVHHPFTAPKNIDIPTLLQYPLKAKANAYDMVINGYEVGSGSVRIHCAELQQTIFSILGMTRNEQSSKFGFFIDALKYGAPPHAGFAFGLDRLVMLLTSTENIRDVIAFPKTTTAIDLMTEAPSIGNTIALKELSIEILDKNKI

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Xylella fastidiosa (strain M23)
Length
589 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.041 kDa
Sequence
MRTHFCGLINETLIGHTVTLAGWTDVARNLGGVCFIDLRDHEGIVQITVDSRAIDQNNSELFRVASGLSYEDVLQVEGVVHARHAVNDKIKTGKVEVIATKIKILNKAAPLPFHAHENPGEDIRLKYRYLDLRRPEMQRMQRTRIKLVQALRRHLDMHGFQDIETPILTKATPEGARDFLVPARMHPGEFYALPQSPQLFKQILMVAGFDRYYQIARCFRDEALRADRQLEFTQLDMEFAFVSERDVQDFVEEMIRRVFKEVAGIELDTTFPRMTWKEAMRRFGSDKPDMRINLELIDVAALVADSTFTPFTNAVAHPNGRVAALRIPRGAVLSRKQIDEYAAYTAKYGATGLAYAKLAPTGEITSPIAKFFSEDAFAALLSHIGAEKGDIVFFGAGNYNKVSDFMGALRLKAGKDFALITADWRPLWVTDFPMFEWDEEAQRYVALHHPFTAPAAINDIDELRTHARTALSRGYDMVLNGNEIGGGSIRIHRPEMQRAVFELLGITEDEARAKFGFLLDALNYGAPPHGGIAFGIDRIAALIAGTESIRDVIPFPKTTGAQCLMTDAPSPISEEQLSEIHVITKKLTP

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Xylella fastidiosa (strain 9a5c)
Length
589 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.809 kDa
Sequence
MRTHFCGLIDETLIGHTVTLAGWTDVARNLGGVCFIDLRDHEGIVQVTVDSRAIDQNNSELFKVASGLSYEDVLQVEGVVCARHAVNDKIKTGKVEVIATKIKILNKAAPLPFHAHENPGEDIRLKYRYLDLRRPEMQRMQRTRIKLVQALRRHLDMHGFQDIETPILTKATPEGARDFLVPARMHPGEFYALPQSPQLFKQILMVAGFDRYYQIARCFRDEALRADRQLEFTQLDMEFAFVSERDVQDFVEEMIRRVFKEVAGIELDTTFPRMTWTEAMRRFGSDKPDLRINLELIDVAALVADSTFTPFTDAVAHPNGRVAALRIPSGAVLSRKQIDEYAAYTAKYGATGLAYAKLAPIGEITSPIAKFFSEDAFAALLSHIGAEKGDIVFFGAGNYNKVSDFMGALRLKAGKDFALITADWRPLWVTDFPMFEWDEEAQRYVALHHPFTAPAAIDDIDELRAHARTALSRGYDMVLNGNEIGGGSIRIHRPEMQRAVFELLGITEDEARAKFGFLLDALNYGAPPHGGIAFGIDRIAALIAGTESIRDVIPFPKTTGAQCLMTDAPSSISEEQLSEIHVITKKPTP

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Xylella fastidiosa (strain M12)
Length
589 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.927 kDa
Sequence
MRTHFCGLINETLIGHTVTLAGWTDVARNLGGVCFIDLRDHEGIVQITVDSRAIDQNNSELFKVASGLSYEDVLQVEGVVCARHAVNDKIKTGKVEVIATKIKILNKAAPLPFHAHENPGEDIRLKYRYLDLRRPEMQRMQRTRIKLVQALRRHLDMHGFQDIETPILTKATPEGARDFLVPARMHPGEFYALPQSPQLFKQILMVAGFDRYYQIARCFRDEALRADRQLEFTQLDMEFAFVSERDVQDFVEEMIRRVFKEVAGIELDTTFPRMTWKEAMRRFGSDKPDLRINLELIDVAALVADSTFTPFTDAVAHPNGRVAALRIPSGTVLSRKQIDEYAAYTAKYGATGLAYAKLAPTGEITSPIAKFFSEDAFASLLSHIGAEKGDIVFFGAGNYNKVSDFMSALRLKAGKDFALITADWRPLWVTDFPMFEWDEEAQRYVALHHPFTAPAAIDDIDELRAHARTALSRGYDMVLNGNEIGGGSIRIHRPEMQRAVFELLGITEDEARAKFGFLLDALNYGAPPHGGIAFGIDRIAALIAGTESIRDVIPFPKTTGAQCLMTDAPSPISEEQLSEIHVITKKTTP

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Xylella fastidiosa (strain Temecula1 / ATCC 700964)
Length
589 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.041 kDa
Sequence
MRTHFCGLINETLIGHTVTLAGWTDVARNLGGVCFIDLRDHEGIVQITVDSRAIDQNNSELFRVASGLSYEDVLQVEGVVHARHAVNDKIKTGKVEVIATKIKILNKAAPLPFHAHENPGEDIRLKYRYLDLRRPEMQRMQRTRIKLVQALRRHLDMHGFQDIETPILTKATPEGARDFLVPARMHPGEFYALPQSPQLFKQILMVAGFDRYYQIARCFRDEALRADRQLEFTQLDMEFAFVSERDVQDFVEEMIRRVFKEVAGIELDTTFPRMTWKEAMRRFGSDKPDMRINLELIDVAALVADSTFTPFTNAVAHPNGRVAALRIPRGAVLSRKQIDEYAAYTAKYGATGLAYAKLAPTGEITSPIAKFFSEDAFAALLSHIGAEKGDIVFFGAGNYNKVSDFMGALRLKAGKDFALITADWRPLWVTDFPMFEWDEEAQRYVALHHPFTAPAAINDIDELRTHARTALSRGYDMVLNGNEIGGGSIRIHRPEMQRAVFELLGITEDEARAKFGFLLDALNYGAPPHGGIAFGIDRIAALIAGTESIRDVIPFPKTTGAQCLMTDAPSPISEEQLSEIHVITKKLTP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Francisella philomiragia subsp. philomiragia (strain ATCC 25017)
Length
589 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.683 kDa
Sequence
MRTHYSSDVNEKLQNQKVTICGWVHRRRDHGGVIFLDIRDRTGLVQLVFNPESKAFKVADSLRGEYVIKATGTVNLRPEGQENKNLASGKVEIIGEDLEIVNKSKTIPFQLDDFQSTGEDVKLKYRYIDLRRPEMQNKLITRSKAIRYVRNFLDNNGFLDIETPFLTKATPEGARDYLVPSRNFNGKFYALPQSPQLFKQLLMVSGFDRYYQVVKCFRDEDLRADRQPEFTQIDIEASFIDEAFIMSTMEKMIAGLFDATIGVKFDTPFQVMTYAEAMDKYGSDKPDLRIPLEFVNIKEDMKNEEFKVFSGPANDPEARVVAMRVPGGNDKLSRKKIDEYTKFVGIYGARGLAYIKINSLSEGKEGLQSPIVKNISEETLFKVIEKTGAQVGDVLFFGAAKAKIVNDSMGALRAKIGEDFEIFTKDWAPLWVVDFPMFEKDDNRLYAVHHPFTAPKVDTVEELTKDPENLLSRAYDMVINGYEVGGGSIRIHRQDMQAKVFNLLGISDEEAREKFGFMLDALSYGTPIHGGIAFGVDRLIMLLTNTTNIRDVIAFPKTQTASCLMTEAPSNVSLEQLNELGIAVKKEDK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Roseiflexus castenholzii (strain DSM 13941 / HLO8)
Length
589 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.946 kDa
Sequence
MYRSHTCGELRVEHAGQEVLLAGWVHRRRDHGPLIFIDLRDRYGLTQVVFDSAAAPTAHAVATDARIEYVLQVRGRVVQRPEEAYNPDLATGMIEVHATEATILNPAKNPPLYINKEGGEDETIRLKYRYLDLRRERMQRNIILRHRIVKFIRDFLDREGFVEIETPILIKSTPEGARDYLVPSRLHPGKFYALPQSPQQLKQLLMVAGFDRYFQIARCFRDEDQRADRQPEFTQLDMEMSFVDQDDVLDIIERLFTALCREITPHKRLLTPFPRLTFAEAMERFGSDKPDLRYGLELVNLGETVATSSFGVLRAALDNGGQVKGLRVPGAGHYSRKQIDEVVDLARQAGAKGLLWAIVPEMGGEVRSSFGKQVSPDEMTAIIRRMEGAPGDLLLIVADTPKIVAQTLDRLRREFGARLNLADPNTLAWAWVLDFPLVEWNDEEQRWDAVHHPFTAPKDEDLHLMDSDPGKVRAKAYDLILNGYEAGGGSIRIHQRDVQQRLFDLLGIDRETAMRQFGHMLEAFEYGAPPHGGIAPGIDRICMILADEVTIREVMAFPKTQQAVDLMTNAPSPVDERQLRELHIALRLD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Roseiflexus sp. (strain RS-1)
Length
589 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.909 kDa
Sequence
MYRSHTCGELRAEHIGQEVLLAGWVHRRRDHGPLIFIDLRDRYGITQIVFDSADSPVAHAVASDARVEYVLQVRGRVVQRPEEAYNPDIATGMIEVHATEATVLNPAKTPPLYINKEGGEEETLRLKYRYLDLRRERMQRNIMLRHRIVKFIRDFLDREGFVEIETPILIKSTPEGARDYLVPSRLHPGKFYALPQSPQQLKQLLMVAGFDRYFQIARCFRDEDQRADRQPEFTQLDMEMSFVDQGDVLDIIERLFTALCREIVPHKRLVTPFPRLTYAEAMERFGSDKPDLRYGLELVDVSDVVAASSFGVFRAALDTGGQVKGLRIPGAGSYSRKQIDEVVELAKQAGARGLLWAVVPGEGGEVRSSFGRQVSPDEMAAIIRRMEGAPGDLLLIVADPPKIVAQTLDRLRREFGARLNLADPNVLAWAWVIDFPLVEWNEEEQRWDAVHHPFTAPKDEDLHLMDTDPGRVRAKAYDLILNGYEAGGGSIRIHRRDVQQRLFDLLGIDRETAMRQFGHMLEAFEYGAPPHGGIAPGIDRICMILADEVTIREVMAFPKTQQAVDLMTNAPSPVDERQLRELHIALRLD

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Leuconostoc citreum (strain KM20)
Length
589 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.595 kDa
Sequence
MKRTTYAGLVDEKYLNQTVTLSGWVQKRRDFGDLIFVDLRDREGIVQLTFNATHAEALAVAENMRNEYVISVTGQVVRREASQINNKIHSGQIEIDVIEAEILATSKTPPFYIEDNVNANEELKLQYRYLDLRRPEMQKNLRIRSKIMSSAMHFMDQNDFINIETPILAKSTPEGARDYLVPSRIFPGSFYALPQSPQLFKQLLMGSGFDRYFQIARAFRDEDLRGDRQPEFTQMDVETSFMSADEIRELVNAWVKAMMSDVVNFDLDTTKIPTLTWQESMDRFGTDKPDLRIAYELKDVSETVKSSEFGVFAKAVEAGGVVKAIAVPGGAENYSRKDIDKMAQYIERFGAKGLAWLKVTDEGISGPIAKFFPNHAALLQVTGAKPGDLLLFGAGRNDIVAATLDYLRRQTAKDLNLIDMTNPWAFAWIVDWPLFEYSEDFDRWIAAHHPFTMPNEEDLHYLDDGEDPHQAHAQSYDLVLNGYELGSGSIRIHRMDIQEKMLKALGFTPEAAHEAFGFLLEGMTFGFPPMGGIALGLDRLAMLLAGQENIREVIAFPKNSRATEPMTQAPTRVDHKQVNDLGLFVSDVE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Lysinibacillus sphaericus (strain C3-41)
Length
589 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.582 kDa
Sequence
MATRTHASNELSETLQGEKVVLKGWVQRRRDLGGLIFIDLRDRTGITQVVFSPDVAEAHALADKVRSEYVIEIEGTVILRTEDQINPNVPNGKIEVEATRLVVINTAKTTPFQIEDRTDVSEDLRLKYRYLDLRRPVMFDTFKMRSDVTRTIRNFLQNEGFLEVETPILTKSTPEGARDYLVPSRVHEGEFYALPQSPQLFKQLLMVAGFEKYFQIARCFRDEDLRADRQPEFTQVDIETSFLTQEEVLEMNERLIQAVMKEVKGIDIPAPFQRMKYQEAMDRYGSDKPDVRFGLELVALNDVFEGCGFKVFADTVAQGKQVKSINIKGAADKYSRKDMDELTKFVGIYGAKGLAWLKVTEEGLNGPIAKFFDEALAAALIERMGAEVGDILVFVADKASVVAASLGALRTKLGQDLDLIDESQFAFLWITDWPLFEYSEEDGRYYAAHHPFTRPFDEDIPLMDTDPSAVRAQAYDIVLNGYELGGGSLRIYERDLQEKMFELLGFSEEEAQAQFGFLLEAFEYGVPPHAGLAFGLDRFVMLLAGRHNLRDTIAFPKTASASCLMTEAPSEVSPEQLSELSLAIKPFRK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Staphylococcus aureus (strain Mu3 / ATCC 700698)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.599 kDa
Sequence
MSKRTTYCGLVTEAFLGQEITLKGWVNNRRDLGGLIFVDLRDREGIVQVVFNPAFSEEALKIAETVRSEYVVEVQGTVTKRDPETVNPKIKTGQVEVQVTNIKVINKSETPPFSINEENVNVDENIRLKYRYLDLRRQELAQTFKMRHQITRSIRQYLDDEGFFDIETPVLTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMISGFDKYYQIVKCFRDEDLRADRQPEFTQVDIEMSFVDQEDVMQMGEEMLKKVVKEVKGVEINGAFPRMTYKEAMRRYGSDKPDTRFEMELIDVSQLGRDMDFKVFKDTVENDGEIKAIVAKGAAEQYTRKDMDALTEFVNIYGAKGLAWVKVVEDGLTGPIGRFFETENVETLLTLTGAEAGDLVMFVADKPNVVAQSLGALRVKLAKELGLIDETKLNFLWVTDWPLLEYDEDAKRYVAAHHPFTSPKEADIAKLGTAPEEAEANAYDIVLNGYELGGGSIRIHDGELQEKMFEVLGFTKEQAQEQFGFLLDAFKYGAPPHGGIALGLDRLVMLLTNRTNLRDTIAFPKTASATCLLTNAPGEVSDKQLEELSLRIRH

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Staphylococcus aureus (strain JH1)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.599 kDa
Sequence
MSKRTTYCGLVTEAFLGQEITLKGWVNNRRDLGGLIFVDLRDREGIVQVVFNPAFSEEALKIAETVRSEYVVEVQGTVTKRDPETVNPKIKTGQVEVQVTNIKVINKSETPPFSINEENVNVDENIRLKYRYLDLRRQELAQTFKMRHQITRSIRQYLDDEGFFDIETPVLTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMISGFDKYYQIVKCFRDEDLRADRQPEFTQVDIEMSFVDQEDVMQMGEEMLKKVVKEVKGVEINGAFPRMTYKEAMRRYGSDKPDTRFEMELIDVSQLGRDMDFKVFKDTVENDGEIKAIVAKGAAEQYTRKDMDALTEFVNIYGAKGLAWVKVVEDGLTGPIGRFFETENVETLLTLTGAEAGDLVMFVADKPNVVAQSLGALRVKLAKELGLIDETKLNFLWVTDWPLLEYDEDAKRYVAAHHPFTSPKEADIAKLGTAPEEAEANAYDIVLNGYELGGGSIRIHDGELQEKMFEVLGFTKEQAQEQFGFLLDAFKYGAPPHGGIALGLDRLVMLLTNRTNLRDTIAFPKTASATCLLTNAPGEVSDKQLEELSLRIRH

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Staphylococcus aureus (strain USA300)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.599 kDa
Sequence
MSKRTTYCGLVTEAFLGQEITLKGWVNNRRDLGGLIFVDLRDREGIVQVVFNPAFSEEALKIAETVRSEYVVEVQGTVTKRDPETVNPKIKTGQVEVQVTNIKVINKSETPPFSINEENVNVDENIRLKYRYLDLRRQELAQTFKMRHQITRSIRQYLDDEGFFDIETPVLTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMISGFDKYYQIVKCFRDEDLRADRQPEFTQVDIEMSFVDQEDVMQMGEEMLKKVVKEVKGVEINGAFPRMTYKEAMRRYGSDKPDTRFEMELIDVSQLGRDMDFKVFKDTVENDGEIKAIVAKGAAEQYTRKDMDALTEFVNIYGAKGLAWVKVVEDGLTGPIGRFFETENVETLLTLTGAEAGDLVMFVADKPNVVAQSLGALRVKLAKELGLIDETKLNFLWVTDWPLLEYDEDAKRYVAAHHPFTSPKEADIAKLGTAPEEAEANAYDIVLNGYELGGGSIRIHDGELQEKMFEVLGFTKEQAQEQFGFLLDAFKYGAPPHGGIALGLDRLVMLLTNRTNLRDTIAFPKTASATCLLTNAPGEVSDKQLEELSLRIRH

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Staphylococcus aureus (strain NCTC 8325)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.629 kDa
Sequence
MSKRTTYCGLVTEAFLGQEITLKGWVNNRRDLGGLIFVDLRDREGIVQVVFNPAFSEEALKIAETVRSEYVVEVQGTVTKRDPETVNPKIKTGQVEVQVTNIKVINKSETPPFSINEENVNVDENIRLKYRYLDLRRQELAQTFKMRHQITRSIRQYLDDEGFFDIETPVLTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMISGFDKYYQIVKCFRDEDLRADRQPEFTQVDIEMSFVDQEDVMQMGEEMLKKVVKEVKGVEINGAFPRMTYKEAMRRYGSDKPDTRFEMELIDVSQLGRDMDFKVFKDTVENDGEIKAIVAKGAAEQYTRKDMDALTEFVNIYGAKGLAWVKVVEDGLTGPIGRFFETENVETLLTLTGAEAGDLVMFVADKPNVVAQSLGALRVKLAKELGLIDETKLNFLWVTDWPLLEYDEDAKRYVAAHHPFTSPKEADIAKLGTAPEEAEANAYDIVLNGYELGGGSIRIHDGELQEKMFEVLGFTKEQAQEQFGFLLDAFKYGAPPHGGIALGLDRLVMLLTNRTNLRDTIAFPKTASATCLLTNAPSEVSDKQLEELSLRIRH

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Staphylococcus aureus (strain JH9)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.599 kDa
Sequence
MSKRTTYCGLVTEAFLGQEITLKGWVNNRRDLGGLIFVDLRDREGIVQVVFNPAFSEEALKIAETVRSEYVVEVQGTVTKRDPETVNPKIKTGQVEVQVTNIKVINKSETPPFSINEENVNVDENIRLKYRYLDLRRQELAQTFKMRHQITRSIRQYLDDEGFFDIETPVLTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMISGFDKYYQIVKCFRDEDLRADRQPEFTQVDIEMSFVDQEDVMQMGEEMLKKVVKEVKGVEINGAFPRMTYKEAMRRYGSDKPDTRFEMELIDVSQLGRDMDFKVFKDTVENDGEIKAIVAKGAAEQYTRKDMDALTEFVNIYGAKGLAWVKVVEDGLTGPIGRFFETENVETLLTLTGAEAGDLVMFVADKPNVVAQSLGALRVKLAKELGLIDETKLNFLWVTDWPLLEYDEDAKRYVAAHHPFTSPKEADIAKLGTAPEEAEANAYDIVLNGYELGGGSIRIHDGELQEKMFEVLGFTKEQAQEQFGFLLDAFKYGAPPHGGIALGLDRLVMLLTNRTNLRDTIAFPKTASATCLLTNAPGEVSDKQLEELSLRIRH

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Staphylococcus aureus (strain bovine RF122 / ET3-1)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.599 kDa
Sequence
MSKRTTYCGLVTEAFLGQEITLKGWVNNRRDLGGLIFVDLRDREGIVQVVFNPAFSEEALKIAETVRSEYVVEVQGTVTKRDPETVNPKIKTGQVEVQVTNIKVINKSETPPFSINEENVNVDENIRLKYRYLDLRRQELAQTFKMRHQITRSIRQYLDDEGFFDIETPVLTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMISGFDKYYQIVKCFRDEDLRADRQPEFTQVDIEMSFVDQEDVMQMGEEMLKKVVKEVKGVEINGAFPRMTYKEAMRRYGSDKPDTRFEMELIDVSQLGRDMDFKVFKDTVENDGEIKAIVAKGAAEQYTRKDMDALTEFVNIYGAKGLAWVKVVEDGLTGPIGRFFETENVETLLTLTGAEAGDLVMFVADKPNVVAQSLGALRVKLAKELGLIDETKLNFLWVTDWPLLEYDEDAKRYVAAHHPFTSPKEADIAKLGTAPEEAEANAYDIVLNGYELGGGSIRIHDGELQEKMFEVLGFTKEQAQEQFGFLLDAFKYGAPPHGGIALGLDRLVMLLTNRTNLRDTIAFPKTASATCLLTNAPGEVSDKQLEELSLRIRH

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Staphylococcus aureus (strain COL)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.599 kDa
Sequence
MSKRTTYCGLVTEAFLGQEITLKGWVNNRRDLGGLIFVDLRDREGIVQVVFNPAFSEEALKIAETVRSEYVVEVQGTVTKRDPETVNPKIKTGQVEVQVTNIKVINKSETPPFSINEENVNVDENIRLKYRYLDLRRQELAQTFKMRHQITRSIRQYLDDEGFFDIETPVLTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMISGFDKYYQIVKCFRDEDLRADRQPEFTQVDIEMSFVDQEDVMQMGEEMLKKVVKEVKGVEINGAFPRMTYKEAMRRYGSDKPDTRFEMELIDVSQLGRDMDFKVFKDTVENDGEIKAIVAKGAAEQYTRKDMDALTEFVNIYGAKGLAWVKVVEDGLTGPIGRFFETENVETLLTLTGAEAGDLVMFVADKPNVVAQSLGALRVKLAKELGLIDETKLNFLWVTDWPLLEYDEDAKRYVAAHHPFTSPKEADIAKLGTAPEEAEANAYDIVLNGYELGGGSIRIHDGELQEKMFEVLGFTKEQAQEQFGFLLDAFKYGAPPHGGIALGLDRLVMLLTNRTNLRDTIAFPKTASATCLLTNAPGEVSDKQLEELSLRIRH

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Staphylococcus aureus (strain Newman)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.599 kDa
Sequence
MSKRTTYCGLVTEAFLGQEITLKGWVNNRRDLGGLIFVDLRDREGIVQVVFNPAFSEEALKIAETVRSEYVVEVQGTVTKRDPETVNPKIKTGQVEVQVTNIKVINKSETPPFSINEENVNVDENIRLKYRYLDLRRQELAQTFKMRHQITRSIRQYLDDEGFFDIETPVLTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMISGFDKYYQIVKCFRDEDLRADRQPEFTQVDIEMSFVDQEDVMQMGEEMLKKVVKEVKGVEINGAFPRMTYKEAMRRYGSDKPDTRFEMELIDVSQLGRDMDFKVFKDTVENDGEIKAIVAKGAAEQYTRKDMDALTEFVNIYGAKGLAWVKVVEDGLTGPIGRFFETENVETLLTLTGAEAGDLVMFVADKPNVVAQSLGALRVKLAKELGLIDETKLNFLWVTDWPLLEYDEDAKRYVAAHHPFTSPKEADIAKLGTAPEEAEANAYDIVLNGYELGGGSIRIHDGELQEKMFEVLGFTKEQAQEQFGFLLDAFKYGAPPHGGIALGLDRLVMLLTNRTNLRDTIAFPKTASATCLLTNAPGEVSDKQLEELSLRIRH

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Staphylococcus aureus (strain Mu50 / ATCC 700699)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.599 kDa
Sequence
MSKRTTYCGLVTEAFLGQEITLKGWVNNRRDLGGLIFVDLRDREGIVQVVFNPAFSEEALKIAETVRSEYVVEVQGTVTKRDPETVNPKIKTGQVEVQVTNIKVINKSETPPFSINEENVNVDENIRLKYRYLDLRRQELAQTFKMRHQITRSIRQYLDDEGFFDIETPVLTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMISGFDKYYQIVKCFRDEDLRADRQPEFTQVDIEMSFVDQEDVMQMGEEMLKKVVKEVKGVEINGAFPRMTYKEAMRRYGSDKPDTRFEMELIDVSQLGRDMDFKVFKDTVENDGEIKAIVAKGAAEQYTRKDMDALTEFVNIYGAKGLAWVKVVEDGLTGPIGRFFETENVETLLTLTGAEAGDLVMFVADKPNVVAQSLGALRVKLAKELGLIDETKLNFLWVTDWPLLEYDEDAKRYVAAHHPFTSPKEADIAKLGTAPEEAEANAYDIVLNGYELGGGSIRIHDGELQEKMFEVLGFTKEQAQEQFGFLLDAFKYGAPPHGGIALGLDRLVMLLTNRTNLRDTIAFPKTASATCLLTNAPGEVSDKQLEELSLRIRH

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Staphylococcus aureus (strain N315)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.599 kDa
Sequence
MSKRTTYCGLVTEAFLGQEITLKGWVNNRRDLGGLIFVDLRDREGIVQVVFNPAFSEEALKIAETVRSEYVVEVQGTVTKRDPETVNPKIKTGQVEVQVTNIKVINKSETPPFSINEENVNVDENIRLKYRYLDLRRQELAQTFKMRHQITRSIRQYLDDEGFFDIETPVLTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMISGFDKYYQIVKCFRDEDLRADRQPEFTQVDIEMSFVDQEDVMQMGEEMLKKVVKEVKGVEINGAFPRMTYKEAMRRYGSDKPDTRFEMELIDVSQLGRDMDFKVFKDTVENDGEIKAIVAKGAAEQYTRKDMDALTEFVNIYGAKGLAWVKVVEDGLTGPIGRFFETENVETLLTLTGAEAGDLVMFVADKPNVVAQSLGALRVKLAKELGLIDETKLNFLWVTDWPLLEYDEDAKRYVAAHHPFTSPKEADIAKLGTAPEEAEANAYDIVLNGYELGGGSIRIHDGELQEKMFEVLGFTKEQAQEQFGFLLDAFKYGAPPHGGIALGLDRLVMLLTNRTNLRDTIAFPKTASATCLLTNAPGEVSDKQLEELSLRIRH

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Staphylococcus aureus (strain MRSA252)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.569 kDa
Sequence
MSKRTTYCGLVTEAFLGQEITLKGWVNNRRDLGGLIFVDLRDREGIVQVVFNPAFSEEALKIAETVRSEYVVEVQGTVTKRDPETVNPKIKTGQVEVQVTNIKVINKSETPPFSINEENVNVDENIRLKYRYLDLRRQELAQTFKMRHQITRSIRQYLDDEGFFDIETPVLTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMISGFDKYYQIVKCFRDEDLRADRQPEFTQVDIEMSFVDQEDVMQMGEEMLKKVVKEVKGVEINGAFPRMTYKEAMRRYGSDKPDTRFEMELIDVSQLGRDMDFKVFKDTVENDGEIKAIVAKGAAEQYTRKDMDALTEFVNIYGAKGLAWVKVVEDGLTGPIGRFFEAENVETLLTLTGAEAGDLVMFVADKPNVVAQSLGALRVKLAKELGLIDETKLNFLWVTDWPLLEYDEDAKRYVAAHHPFTSPKEADIAKLGTAPEEAEANAYDIVLNGYELGGGSIRIHDGELQEKMFEVLGFTKEQAQEQFGFLLDAFKYGAPPHGGIALGLDRLVMLLTNRTNLRDTIAFPKTASATCLLTNAPGEVSDKQLEELSLRIRH

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Staphylococcus aureus (strain MSSA476)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.599 kDa
Sequence
MSKRTTYCGLVTEAFLGQEITLKGWVNNRRDLGGLIFVDLRDREGIVQVVFNPAFSEEALKIAETVRSEYVVEVQGTVTKRDPETVNPKIKTGQVEVQVTNIKVINKSETPPFSINEENVNVDENIRLKYRYLDLRRQELAQTFKMRHQITRSIRQYLDDEGFFDIETPVLTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMISGFDKYYQIVKCFRDEDLRADRQPEFTQVDIEMSFVDQEDVMQMGEEMLKKVVKEVKGVEINGAFPRMTYKEAMRRYGSDKPDTRFEMELIDVSQLGRDMDFKVFKDTVENDGEIKAIVAKGAAEQYTRKDMDALTEFVNIYGAKGLAWVKVVEDGLTGPIGRFFETENVETLLTLTGAEAGDLVMFVADKPNVVAQSLGALRVKLAKELGLIDETKLNFLWVTDWPLLEYDEDAKRYVAAHHPFTSPKEADIAKLGTAPEEAEANAYDIVLNGYELGGGSIRIHDGELQEKMFEVLGFTKEQAQEQFGFLLDAFKYGAPPHGGIALGLDRLVMLLTNRTNLRDTIAFPKTASATCLLTNAPGEVSDKQLEELSLRIRH

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Staphylococcus aureus (strain USA300 / TCH1516)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.599 kDa
Sequence
MSKRTTYCGLVTEAFLGQEITLKGWVNNRRDLGGLIFVDLRDREGIVQVVFNPAFSEEALKIAETVRSEYVVEVQGTVTKRDPETVNPKIKTGQVEVQVTNIKVINKSETPPFSINEENVNVDENIRLKYRYLDLRRQELAQTFKMRHQITRSIRQYLDDEGFFDIETPVLTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMISGFDKYYQIVKCFRDEDLRADRQPEFTQVDIEMSFVDQEDVMQMGEEMLKKVVKEVKGVEINGAFPRMTYKEAMRRYGSDKPDTRFEMELIDVSQLGRDMDFKVFKDTVENDGEIKAIVAKGAAEQYTRKDMDALTEFVNIYGAKGLAWVKVVEDGLTGPIGRFFETENVETLLTLTGAEAGDLVMFVADKPNVVAQSLGALRVKLAKELGLIDETKLNFLWVTDWPLLEYDEDAKRYVAAHHPFTSPKEADIAKLGTAPEEAEANAYDIVLNGYELGGGSIRIHDGELQEKMFEVLGFTKEQAQEQFGFLLDAFKYGAPPHGGIALGLDRLVMLLTNRTNLRDTIAFPKTASATCLLTNAPGEVSDKQLEELSLRIRH

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Staphylococcus aureus (strain MW2)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.599 kDa
Sequence
MSKRTTYCGLVTEAFLGQEITLKGWVNNRRDLGGLIFVDLRDREGIVQVVFNPAFSEEALKIAETVRSEYVVEVQGTVTKRDPETVNPKIKTGQVEVQVTNIKVINKSETPPFSINEENVNVDENIRLKYRYLDLRRQELAQTFKMRHQITRSIRQYLDDEGFFDIETPVLTKSTPEGARDYLVPSRVHDGEFYALPQSPQLFKQLLMISGFDKYYQIVKCFRDEDLRADRQPEFTQVDIEMSFVDQEDVMQMGEEMLKKVVKEVKGVEINGAFPRMTYKEAMRRYGSDKPDTRFEMELIDVSQLGRDMDFKVFKDTVENDGEIKAIVAKGAAEQYTRKDMDALTEFVNIYGAKGLAWVKVVEDGLTGPIGRFFETENVETLLTLTGAEAGDLVMFVADKPNVVAQSLGALRVKLAKELGLIDETKLNFLWVTDWPLLEYDEDAKRYVAAHHPFTSPKEADIAKLGTAPEEAEANAYDIVLNGYELGGGSIRIHDGELQEKMFEVLGFTKEQAQEQFGFLLDAFKYGAPPHGGIALGLDRLVMLLTNRTNLRDTIAFPKTASATCLLTNAPGEVSDKQLEELSLRIRH

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Staphylococcus carnosus (strain TM300)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.846 kDa
Sequence
MSKRTTYCGLVTEDLLGQRVTLKGWVHNRRDLGGLIFVDLRDREGYVQIVFNPDFSKEALEIAESIRSEYVIEVEGTVTKRDPETVNPKIKTGNVEVQVDHINIINKAQTPPFSINDENQQVDENIRLKYRYLDLRRQELAQTIKMRHQITRSVREFLDRDGFFDIETPVLTKSTPEGARDYLVPSRVHEGQFYALPQSPQLFKQLLMISGFDKYYQIVKCFRDEDLRADRQPEFTQVDVEMSFVDQEDVMEMGEALLKKVVKDVKGIDLTEQFPRMTYAEAMSRYGSDKPDTRFEMELKDVSELGRTMDFKVFKDTVEKGGEVKALAAKGAADKYTRKDMDALTEFVNIYGAKGLAWVKVVEDGFSGPIARFFEDKDVEKVKELTGAETGDLVMFVADKPSVVAQSLGALRVKLAHELGLIDNNKLNFLWVTDWPLLEYDEDEKRYVAAHHPFTSPKDEDLDKLDSAPEKAQAKAYDIVLNGYELGGGSIRIHNADIQSKMFEVLGFTKEQAQEQFGFLLDAFKYGAPPHGGIALGLDRFVMLLAGRNNLRDTIAFPKTASAVSLMTQAPSEVSDKQLEELSLRIRH

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.883 kDa
Sequence
MNKRTTYCGLVTEEFLNEKVTLKGWVHNRRDLGGLIFVDLRDREGIVQIVFNPDFSEEALQVAETVRSEYVVEVEGVVTKRDAETINPKIKTGQVEVQVSNIEIINKSETPPFSINEENVNVDENIRLKYRYLDLRRQELAQTFKMRHQTTRSIRQYLDNNGFFDIETPVLTKSTPEGARDYLVPSRVHEGEFYALPQSPQLFKQLLMISGFDKYYQIVKCFRDEDLRADRQPEFTQVDIEMSFVDQEDIIAMGEDMLRKVVKDVKGIDVSGPFPRMTYAEAMDRFGSDKPDTRFGMELINVSQLGKEMNFKVFKDTVDNNGEIKAIVAKDAANKYTRKDMDALTEFVNIYGAKGLAWVKVVDDGLSGPIARFFEDVNVETLKQLTEAKPGDLVMFVADKPNVVAQSLGALRIKLAKELGLIDESKLNFLWVTDWPLLEYDEDAKRYVAAHHPFTSPKREDIEKLDTEPENVQANAYDIVLNGYELGGGSIRIHDGELQQKMFEVLGFTNEQAQEQFGFLLDAFKYGAPPHGGIALGLDRLVMLLTNRTNLRDTIAFPKTASATCLLTDAPGEVSDKQLQELSLRIRH

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Staphylococcus epidermidis (strain ATCC 12228)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.883 kDa
Sequence
MNKRTTYCGLVTEEFLNEKVTLKGWVHNRRDLGGLIFVDLRDREGIVQIVFNPDFSEEALQVAETVRSEYVVEVEGVVTKRDAETINPKIKTGQVEVQVSNIEIINKSETPPFSINEENVNVDENIRLKYRYLDLRRQELAQTFKMRHQTTRSIRQYLDNNGFFDIETPVLTKSTPEGARDYLVPSRVHEGEFYALPQSPQLFKQLLMISGFDKYYQIVKCFRDEDLRADRQPEFTQVDIEMSFVDQEDIIAMGEDMLRKVVKDVKGIDVSGPFPRMTYAEAMDRFGSDKPDTRFGMELINVSQLGKEMNFKVFKDTVDNNGEIKAIVAKDAANKYTRKDMDALTEFVNIYGAKGLAWVKVVDDGLSGPIARFFEDVNVETLKQLTEAKPGDLVMFVADKPNVVAQSLGALRIKLAKELGLIDESKLNFLWVTDWPLLEYDEDAKRYVAAHHPFTSPKREDIEKLDTEPENVQANAYDIVLNGYELGGGSIRIHDGELQQKMFEVLGFTNEQAQEQFGFLLDAFKYGAPPHGGIALGLDRLVMLLTNRTNLRDTIAFPKTASATCLLTDAPGEVSDKQLQELSLRIRH

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Staphylococcus haemolyticus (strain JCSC1435)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.728 kDa
Sequence
MSKRTTYCGLVTEELLNQKVTLKGWVHNRRDLGGLIFVDLRDREGIVQIVFNPDFSEEALSVAETVRSEYVVEVEGTVTKRDPDTVNSKIKTGQVEVQVSNISIINKSETPPFSINEENQNVDENIRLKYRYLDLRRPELAQTFKMRHQTTRAIREYLDNNGFFDIETPVLTKSTPEGARDYLVPSRVHEGEFYALPQSPQLFKQLLMISGFDKYYQIVKCFRDEDLRADRQPEFTQVDIEMSFVDQEDVIQMGEEMLRKVVKDVKGIDVSGPFPRMTYEEAMRRYGSDKPDTRFEMELKDVSQLGREMDFKVFKDTVENNGEVKAIVAKGAADNYTRKDMDALTEFVNIYGAKGLAWVKVVDDGLSGPIARFFEDSNVATLKDLTQAESGDLVMFVADKPNVVAQSLGALRIKIAKELGLIDENKLNFLWVTDWPLLEYDEDAKRYVAAHHPFTSPKQEDISKLDSEPQNAQANAYDIVLNGYELGGGSIRIADGELQEKMFEVLGFTKEQAREQFGFLLDAFKYGAPPHGGIALGLDRLVMLLTNRTNLRDTIAFPKTASATCLLTDAPGEVSDKQLEELSLRIRH

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chloroflexus aggregans (strain MD-66 / DSM 9485)
Length
588 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.411 kDa
Sequence
MYRSHTCGELRPAHAGQEVTLAGWVHRRRDHGDLIFIDLRDRYGITQVVFNSANAAAHAVAETVRSEYVLQVRGKVRIRPAEAVNPDIATGEIEVDAFEAQVLNPARTPPIYIAKEAGEDESVRLKYRYLDLRRERMQRNLILRHRVVKFIRDFLDAEGFIEIETPILIKSTPEGARDYLVPSRLHPGKFYALPQSPQQLKQLLMVAGYDKYFQIARCFRDEDQRADRQPEFTQLDMEMSFVDQEDVINLIERLFTELCRTVTPHKRLLTPFRRLTYAEAMERYGSDKPDLRYDLELVNLSDVLAETPFQVFRSVLAVGGQVKGIRVPGCGHFSRKQIDELTEVARSGGAKGLAWAVVPTDGGDVRSSFAKNLAPGEFDALAQRMGAQPGDLLLIVADRPVVVAASLDKLRRKLADLLQLADPDTLCFAWVVDFPLVEWNEEEQRWDAVHHPFTSPKDEDLHLLATDPGKVRAKAYDLILNGYEAGGGSIRIHRRDVQQQVFSLLGIGEEKAQAQFGHMLEAFEYGAPPHGGIAPGIDRLVMILADEPTIREVMAFPKTQQAVDLMTNAPSPVDERQLKELHIRIVED

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Aeromonas salmonicida (strain A449)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.386 kDa
Sequence
MRSIYCGQVNEAHAGQTITLCGWVHRRRDLGGLIFIDMRDREGIVQVFFDPDKPDAFALASELRGEFCIQVSGVVRTRPDSQRNSDMATGAIEVFAHELTIINRAEPLPLDFNQVNSEEQRLKFRYLDLRRPEMAKYLKTRAKASAFVRRFMDEHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVRELMEEMIRNLWQHVLAVDLGDFPVMTFDEAMRRFGSDKPDLRLPMELVDVADLLTAVEFAVFAGPANDPKGRVAALKVPGGAELSRKQIDEYTKFVGIYGAKGLAWMKVNEAANGIEGVQSPVAKFLSDEIVREILARTGAADGDIIFFGADSKKVVADAIGALRLKVGRDLGLMENSWKPLWVIDFPMFEEDSEGGLAAMHHPFTAPSNLGPSELKANPLSAYANAYDMVINGYEVGGGSVRIHNSEMQATVFDILGITPAEQRLKFGFLLDALKYGTPPHAGLAFGLDRLSMLLTGTDNIRDVIAFPKTTAAACLMTDAPSFANQAQMSELAIATTVKGDE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Exiguobacterium sibiricum (strain DSM 17290 / JCM 13490 / 255-15)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.844 kDa
Sequence
MIGRTHMNGTVTEETIGQAVQLKGWVQKRRDLGGLIFLDLRDRTGIVQVVFQPENEQAHRLAESIRSEYVLDIKGTVVQRENPNPNIPTGQVEVVADEVIILNASKMTPFPISEEAEQTSEDLRLKYRYLDLRRPSLQETFRLRSKASNIMRNFLDEQDFLEVETPILTKSTPEGARDYLVPSRVHPGEFYALPQSPQLFKQLLMVSGFERYFQIARCFRDEDLRADRQPEFTQVDIETSFMDVEDLYAMMESMMTRVMKETLGKDITTPFPRMPYAEAMSRFGSDKPDTRFGLELIDVAEAVTGAGFKVFDMALESGGEVKALNVKGAADQFSRKDIDKLQEFTAIYGAKGLAWVKVTADGLNGPIAKFFDEAATARLVEATTAEAGDLLVFVAAKASIVADSLGALRQKLGKELGLIDETVFNFLWVTDFPLVTFEEADSRFYANHHPFTMPRREDLDKLETDPGSVLAVAYDLVLNGYELGGGSQRIYERDIQERMFKLLGFTEEEANEQFGFLMEAFEYGTPPHAGIALGLDRLIMLLAGRTNLRDTIAFPKTASASDLLTAAPSPVSDAQLNELSIRTAVKQS

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Haemophilus influenzae (strain 86-028NP)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.714 kDa
Sequence
MMRTHYCGALNRNNIGQDVTLSGWVHRRRDLGGLIFIDMRDRDGIVQVCFDPKYQDALTAAAGLRNEFCIQIKGEVIARPENQINKNMATGEVEVLAKELRIYNASDVLPLDFNQNNTEEQRLKYRYLDLRRPEMAQRLKTRAKITSFVRRFMDDNGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFLTAPEVREIMERMVHDLWLDTIGVDLGKFPVMTWQEAMRRFGSDKPDLRNPLEMVDVADIVKDVEFKVFNEPANNPNGRVAVIRVPNGAEITRKQIDEYTQFVGIYGAKGLAWAKVNDINAGLEGVQSPIAKFLNEEVWKALAERVNAQTGDILFFGADKWQTTTDAMGALRLKLGCDLGLTRLDEWQPLWVIDFPMFERDEEGNLAAMHHPFTSPKDFSPEQLEADPTSAVANAYDMVINGYEVGGGSVRIFDPKMQQTVFRILGIDEEQQREKFGFLLDALKFGTPPHAGLAFGLDRLTMLLTGTENIRDVIAFPKTTAAACLMTEAPSFVNPQALEELAISVVKAE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Haemophilus influenzae (strain PittEE)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.708 kDa
Sequence
MMRTHYCGALNRNNIGQDVTLSGWVHRRRDLGGLIFIDMRDRDGIVQVCFDPKYQDALTAAAGLRNEFCIQIKGEVIARPENQINKNMATGEVEVLAKELRVYNASDVLPLDFNQNNTEEQRLKYRYLDLRRPEMAQRLKTRAKITSFVRRFMDDNGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFLTAPEVREIMERMVHGLWLDTIGVDLGKFPVMTWQEAMRRFGSDKPDLRNPLEIVDVADIVKDVEFKVFNEPANNPNGRVAVIRVPNGAEITRKQIDEYTQFVGIYGAKGLAWAKVNDINAGLEGVQSPIAKFLNEEVWKALAERVNAQTGDILFFGADKWQTTTDAMGALRLKLGRDLGLTRLDEWKPLWVIDFPMFERDEEGNLAAMHHPFTSPKDFSPEQLEADPTSAVANAYDMVINGYEVGGGSVRIFDPKMQQTVFRILGIDEEQQREKFGFLLDALKFGTPPHAGLAFGLDRLTMLLTGTENIRDVIAFPKTTAAACLMTEAPSFANPQALEELAIQVTKSE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Haemophilus influenzae (strain PittGG)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.746 kDa
Sequence
MMRTHYCGALNRNNIGQDVTLSGWVHRRRDLGGLIFIDMRDRDGIVQVYFDPKYQDALTAAASLRNEFCIQIKGEVIARPENQINKNMATGEVEVLAKELRIYNASDVLPLDFNQNNTEEQRLKYRYLDLRRPEMAQRLKTRAKITSFVRRFMDDNGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFLTAPEVREIMERMVHGLWLDTIGVDLGKFPVMTWQEAMCRFGSDKPDLRNPLEMVDVADIVKDVEFKVFNEPANNPNGRVAVIRVPNGAEITRKQIDEYTQFVGIYGAKGLAWAKVNDINVGLEGVQSPIAKFLNEEVWKALAERVNAQTGDILFFGADKWQTTTDAMGALRLKLGRDLGLTRLDEWQPLWVIDFPMFERDEEGNLAAMHHPFTSPKDFSPEQLEADPTSAVANAYDMVINGYEVGGGSVRIFDPKMQQTVFRILGIDEEQQREKFGFLLDALKFGTPPHAGLAFGLDRLTMLLTGTENIRDVIAFPKTTAAACLMTEAPSFANPQALEELAISVVKAE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.639 kDa
Sequence
MMRTHYCGALNRNNIGQDVTLSGWVHRRRDLGGLIFIDMRDRDGIVQVCFDPKYQDALTAAAGLRNEFCIQIKGEVIARPDNQINKNMATGEVEVLAKELRIYNASDVLPLDFNQNNTEEQRLKYRYLDLRRPEMAQRLKTRAKITSFVRRFMDDNGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFLTAPEVREIMERMVHGLWLDTIGVDLGKFPVMTWQEAMRRFGSDKPDLRNPLEMVDVADIVKDVEFKVFNEPANNPNGRVAVIRVPNGAEITRKQIDEYTQFVGIYGAKGLAWAKVNDINAGLEGVQSPIAKFLNEDVWKGLAERVNAQTGDILFFGADKWQTTTDAMGALRLKLGRDLGLTRLDEWQPLWVIDFPMFERDEEGNLAAMHHPFTSPKDFSPEQLEADPTSAVANAYDMVINGYEVGGGSVRIFDPKMQQTVFRILGIDEEQQREKFGFLLDALKFGTPPHAGLAFGLDRLTMLLTGTENIRDVIAFPKTTAAACLMTEAPSFANPQALEELAISVVKAE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Tolumonas auensis (strain DSM 9187 / TA4)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.052 kDa
Sequence
MRSIYCGQVTSSHVEQTVTLCGWVHRRRDLGGLIFIDMRDREGIVQVFFDPDKPEAFALASELRNEFCIRVTGVVRARPDSQINKDMATGEVEIFAHGLEIINRAEPLPLDFNQTNTEEQRLKYRYLDLRRPEMAASLKTRARITSFVRRYMDEHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFLNAEQVRELMENLIRGLWQNIIGVDLGQFPIMTFDEAMRRYGSDKPDLRNPMEMVDIADLLKDVSFAVFAGPANDPKGRVAALRVPDGAQLSRKQIDEYTQFVSIYGAKGLAWMKVNQADSGLAGVQSPVAKFLNDEIVREILSRTSAQDGDIIFFGADSKKVVCDAIGALRLKLARDLDLVENCWKPLWVVDFPMFEEDGEGGVTAMHHPFTAPKDFTPAQLEADPLAAYANAYDMVINGYEVGGGSVRIHRGDMQQTVFRAIGISEAEQKEKFGFLLDALKFGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTDAPSFANQQQLSELAIQTTVKAAE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Xanthomonas axonopodis pv. citri (strain 306)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.032 kDa
Sequence
MRTHFCGLVDETLIGQTVTLAGWTDVARNLGGVCFIDLRDHEGIVQVTVEPVAGDDASAELFKVAASLGYEDVLQVEGVVRARHAVNDKLRSGKVEVIATRISILNKAAPLPFHAHENPGEETRLKYRYLDLRRPEMQRMQRTRIKLVQALRRHLDARDFQDIETPILTKATPEGARDFLVPARMHPGEFYALPQSPQLFKQILMVAGFDRYYQIARCFRDEALRADRQLEFTQLDMEFAFVRERDVQDFVEDMIRAIFKEVVDVDLAAQFPRMTWAEAMRRFGSDKPDLRIALELVDVAELVKASQFPVFTAAANDADGRVAALRIPGGASLSRKQIDEYAAHAAKYGAKGLAYIKLSETGEVSSPIAKFFSEESFAALLKHVGAGNGDIVFFGAGGYTKVSDFMGALRLKAGKEFDLIADGWAPLWVTDFPMFEWDEEAQRYVALHHPFTAPAVDDIADLRANARTAVSRGYDMVLNGNEIGGGSIRIHRPDMQSAVFELLGIGAEEARAKFGFLLDALNYGAPPHGGIAFGIDRIAALMAGTESIRDVIPFPKTTGAQDLMTDAPSPIAADQLAEVHVQVRPKQV

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Xanthomonas campestris pv. vesicatoria (strain 85-10)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.993 kDa
Sequence
MRTHFCGLVDETLIGQTVTLAGWTDVARNLGGVCFIDLRDHEGIVQVTVEPVAGDDASAELFKVAASLGYEDVLQVEGVVRARHAVNDKLRSGKVEVIATRISILNKAAPLPFHAHENPGEETRLKYRYLDLRRPEMQRMQRTRIKLVQALRRHLDARDFQDIETPILTKATPEGARDFLVPARMHPGEFYALPQSPQLFKQILMVAGFDRYYQIARCFRDEALRADRQLEFTQLDMEFAFVRERDVQDFVEDMIRAIFKEVVDVDLAAQFPRMTWAEAMRRYGSDKPDLRIALELVDVAELVKASQFPVFTAAADDADGRVAALLIPGGASLSRKQIDEYAAHAAKYGAKGLAYIKLSETGEVSSPIAKFFSEESFAALLKHVGASNGDIVFFGAGGYTKVSDFMGALRLKAGKDFNLVADGWAPLWVTDFPMFEWDDEAQRYVALHHPFTAPAVDDIADLRANARTAVSRGYDMVLNGNEIGGGSIRIHRPDMQSAVFELLGIGAEEARAKFGFLLDALNYGAPPHGGIAFGIDRIAALMAGTESIRDVIPFPKTTGAQDLMTDAPSPIAADQLAEVHVQVRPKQV

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Xanthomonas campestris pv. campestris (strain 8004)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.876 kDa
Sequence
MRTHFCGLVDETLIGQTVTLAGWTDVARNLGGVCFIDLRDHEGIVQVTVEPAEGDANSAEVFKVAASLGYEDVLQVEGVVRARHAVNDKIRTGKVEVIATRITILNKAAPLPFHAHENPGEDTRLKYRYLDLRRPEMQRMQRTRIKLVQALRRHLDARDFQDIETPILTKATPEGARDFLVPARMHPGEFYALPQSPQLFKQILMVAGFDRYYQIARCFRDEALRADRQLEFTQLDMEFAFVRERDVQDFVEDMIRAIFKEVVDVELAAQFPRMTWAEAMRRYGSDKPDLRIALELVDVAELVKTSEFPVFAAAANDADGRVAALRIPGGATLSRKQIDDYAAHAAKYGAKGLAYSKLSETGEVSSPIAKFFGEEAFAALLAHVGAANGDIVFFGAGSYNKVSDFMGALRLKAGKDFGLVAAGWAPLWVTDFPMFEWDEEAQRYVALHHPFTAPAVDDIADLRANARTAVSRGYDMVLNGNEIGGGSIRIHRPDMQSAVFELLGIGAEEARAKFGFLLDALNYGAPPHGGIAFGIDRIAALMAGTESIRDVIPFPKTTGAQDLMTDAPSPIAAEQLAEVHVQVRPKQA

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Xanthomonas campestris pv. campestris (strain B100)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.888 kDa
Sequence
MRTHFCGLVDETLIGQTVTLAGWTDVARNLGGVCFIDLRDHEGIVQVTVEPAEGDANSAEVFKVAASLGYEDVLQVEGVVRARHAVNDKIRTGKVEVIATRITILNKAAPLPFHAHENPGEDTRLKYRYLDLRRPEMQRMQRTRIKLVQALRRHLDARDFQDIETPILTKATPEGARDFLVPARMHPGEFYALPQSPQLFKQILMVAGFDRYYQIARCFRDEALRADRQLEFTQLDMEFAFVRERDVQDFVEDMIRAIFKEVVDVELAAQFPRMTWAEAMRRYGSDKPDLRIALELVDVAELVKTSEFPVFAAAANDADGRVAALRIPGGATLSRKQIDDYAAHAAKYGAKGLAYIKLSESGEVSSPIAKFFGEEAFAALLAHVGAANGDIVFFGAGSYNKVSDFMGALRLKAGKDFGLVAAGWAPLWVTDFPMFEWDEEAQRYVALHHPFTAPAVDDIADLRANARTAVSRGYDMVLNGNEIGGGSIRIHRPDMQSAVFELLGIGAEEARAKFGFLLDALNYGAPPHGGIAFGIDRIAALMAGTESIRDVIPFPKTTGAQDLMTDAPSPIAAEQLAEVHVQVRPKQA

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Histophilus somni (strain 2336)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.538 kDa
Sequence
MMRSHYCGALNRSHIGQQVILSGWVHKRRDLGGLIFIDMRDREGIVQVCFDPKYQEALTEASALRNEFCIKIEGEVIARPDNQINKNMATGEVEVVAKALSVYNVSDVLPLDFNQNNTEEQRLKYRYLDLRRPEMAQHLKTRAKITAFVRRYMDENGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPEVREIMEKMVHGLWLNTIGVDLGKFPTMTWQEAMERFGSDKPDLRNPLEIVDVADIVKDIDFNVFSDPANSSNGRVAVIRVPNGINITRKQIDEYTQFVGIYGAKGLAWVKINDINAGLEGVQSPIAKFLTTEKIKAIFDRTSAQSDDILFFGADKWQTATDAMGALRLKLGRDLGLTHLDEWKPLWVIDFPMFERDEEGNLAAMHHPFTSPKDFTPEQLEANPTSAVANAYDMVINGYEVGGGSVRIFDPKMQQTVFHILGIDEDQQREKFGFLLDALKFGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTDAPSLANEKALEELAIKVTRSE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.014 kDa
Sequence
MSKRTTYCGLVTESLLDQEVTLKGWVHNRRDLGGLIFVDLRDREGYVQIVFNPDFSEEALKTAETVRSEYVVEVKGLVKKRDPQTVNPKIATGQVEVQVSEINIINKSETPPFAINEENQNVDENIRLKYRYLDLRRQELAQTFKMRHQTTRSIRQYLDKEGFFDIETPVLTKSTPEGARDYLVPSRVHDGEFYALPQSPQIFKQLLMISGFDKYYQIVKCFRDEDLRADRQPEFTQVDIEMSFVDQEDVMDMGEEMLQNVVKDVKDVEIPRPFPRMTYNEAMERYGSDKPDTRFEMELINVSELGEEMDFKVFKDAVNNDGQVKAIVAKGAADQYTRKDIDALTEFVNIYGAKGLAWVKVVDDGLSGPIARFFETTHIEKLQSLTNAESGDLVLFVADKPNVVAQSLGALRLKLARELDLIDESKLNFLWVTDWPLLEYDEDLKRYTAAHHPFTAPKQEDIEKLDSEPENAQANAYDVVLNGYELGGGSIRIHNGELQAKMFEVLGFTEEQAQEQFGFLLDAFKYGAPPHGGIALGLDRLVMLLTGRTNLRDTIAFPKTASATCLLTDAPSEVSENQLEELSLRIRH

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Nitrosospira multiformis (strain ATCC 25196 / NCIMB 11849 / C 71)
Length
588 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.318 kDa
Sequence
MRTNYCGLIDVQYLDQTVILYGWVHRRRDHGGVIFVDLRDREGLVQVVCDPDNPTAFQVAEKIRNEFVVRITGRVRHRPPGTVNPNLISGEIEVLVSSIDILNASLTPPFLMDDESLSEATRLEHRYLDLRRPQMQENLRLRYKVAMAVRLFLDQHGFIDVETPMLTKSTPEGARDYLVPSRVNTGHFFALPQSPQLFKQLLMVSGFDRYYQITKCFRDEDLRADRQPEFTQIDIETSFLNESQIMQMMERMICTVFKSVRNIDLPTPFPRLTHGEAMSKYGSDKPDMRVSLVLTELTDVMQEVEFKVFREAALRTGGRVAALRVPGGGALSRKEIDDYTGFVAIYGAKGLAYIKVNALEKGMDGLQSPILKFLPENVIQIVLERTGAKDGDLIFFGADKAQVVNEALGALRAKVGHDRGLAESGWKPLWVVDFPMFERDEEENRWKALHHPFTSPAEGHEDLLETDPEKALSKAYDMVLNGSEIGGGSVRIHRQEVQSKVFRALNIGADEANEKFGFLLEALQYGAPPHGGIAFGLDRIVAMMAGAESIREVIAFPKTQRAQCLLTHAPSTVGEKQLRELHIKLRHA

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.876 kDa
Sequence
MRTHFCGLVDETLIGQTVTLAGWTDVARNLGGVCFIDLRDHEGIVQVTVEPAEGDANSAEVFKVAASLGYEDVLQVEGVVRARHAVNDKIRTGKVEVIATRITILNKAAPLPFHAHENPGEDTRLKYRYLDLRRPEMQRMQRTRIKLVQALRRHLDARDFQDIETPILTKATPEGARDFLVPARMHPGEFYALPQSPQLFKQILMVAGFDRYYQIARCFRDEALRADRQLEFTQLDMEFAFVRERDVQDFVEDMIRAIFKEVVDVELAAQFPRMTWAEAMRRYGSDKPDLRIALELVDVAELVKTSEFPVFAAAANDADGRVAALRIPGGATLSRKQIDDYAAHAAKYGAKGLAYSKLSETGEVSSPIAKFFGEEAFAALLAHVGAANGDIVFFGAGSYNKVSDFMGALRLKAGKDFGLVAAGWAPLWVTDFPMFEWDEEAQRYVALHHPFTAPAVDDIADLRANARTAVSRGYDMVLNGNEIGGGSIRIHRPDMQSAVFELLGIGAEEARAKFGFLLDALNYGAPPHGGIAFGIDRIAALMAGTESIRDVIPFPKTTGAQDLMTDAPSPIAAEQLAEVHVQVRPKQA

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Xanthomonas oryzae pv. oryzae (strain MAFF 311018)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.071 kDa
Sequence
MRTHFCGLVDETLIGQTVTLAGWTDVARNLGGVCFIDLRDHEGIVQVTVEPVAGDDASAELFKVAASLGYEDVLQVEGVVRARHAVNDKLRTGKVEVIATRISILNKAAPLPFHAHENPGEETRLKYRYLDLRRPEMQRMQRTRIKLVQALRRHLDARDFQDIETPILTKATPEGARDFLVPARMHPGEFYALPQSPQLFKQILMVAGFDRYYQIARCFRDEALRADRQLEFTQLDMEFAFVRERDVQDFVEDMMRAIFKEVVDVDLAAQFPRMTWAEAMRRYGSDKPDLRIALELVDVAELVKSSEFPVFTAAANDADGRVAALRIPGGATLSRKQIDDYAAHAAKYGAKGLAYIKLSETGEVSSPIAKFFSEEAFAALLKHVGAGNGDIVFFGAGGYTKVSDFMGALRLKAGKEFDLVAEGWAPLWVTDFPMFEWDEEAQRYVALHHPFTAPAVDDIADLRANARTAVSRGYDMVLNGNEIGGGSIRIHRPDMQSAVFELLGIGAEEARAKFGFLLDALNYGAPPHGGIAFGIDRIAALMAGTESIRDVIPFPKTTGAQDLMTDAPSPIAADQLAEVHVQVRSKQV

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Xanthomonas oryzae pv. oryzae (strain PXO99A)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.052 kDa
Sequence
MRTHFCGLVDETLIGQTVTLAGWTDVARNLGGVCFIDLRDHEGIVQVTVEPVAGDDASAELFKVAASLGYEDVLQVEGVVRARHAVNDKLRTGKVEVIATRISILNKAAPLPFHAHENPGEETRLKYRYLDLRRPEMQRMQRTRIKLVQALRRHLDARDFQDIETPILTKATPEGARDFLVPARMHPGEFYALPQSPQLFKQILMVAGFDRYYQIARCFRDEALRADRQLEFTQLDMEFAFVRERDVQDFVEDMMRAIFKEVVDVDLAAQFPRMTWAEAMRRYGSDKPDLRIALELVDVAELVKSSEFPVFTAAANDADGRVAALRIPGGATLSRKQIDDYAAHAAKYGAKGLAYIKLSETGEVNSPIAKFFGEEAFAALLKHVGAGNGDIVFFGAGGYTKVSDFMGALRLKAGKEFDLVAEGWAPLWVTDFPMFEWDDEAQRYVALHHPFTAPAVDDIADLRANARTAVSRGYDMVLNGNEIGGGSIRIHRPDMQSAVFELLGIGAEEARAKFGFLLDALNYGAPPHGGIAFGIDRIAALMAGTESIRDVIPFPKTTGAQDLMTDAPSPIAADQLAEVHVQIRAKQV

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Xanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.071 kDa
Sequence
MRTHFCGLVDETLIGQTVTLAGWTDVARNLGGVCFIDLRDHEGIVQVTVEPVAGDDASAELFKVAASLGYEDVLQVEGVVRARHAVNDKLRTGKVEVIATRISILNKAAPLPFHAHENPGEETRLKYRYLDLRRPEMQRMQRTRIKLVQALRRHLDARDFQDIETPILTKATPEGARDFLVPARMHPGEFYALPQSPQLFKQILMVAGFDRYYQIARCFRDEALRADRQLEFTQLDMEFAFVRERDVQDFVEDMMRAIFKEVVDVDLAAQFPRMTWAEAMRRYGSDKPDLRIALELVDVAELVKSSEFPVFTAAANDADGRVAALRIPGGATLSRKQIDDYAAHAAKYGAKGLAYIKLSETGEVSSPIAKFFSEEAFAALLKHVGAGNGDIVFFGAGGYTKVSDFMGALRLKAGKEFDLVAEGWAPLWVTDFPMFEWDEEAQRYVALHHPFTAPAVDDIADLRANARTAVSRGYDMVLNGNEIGGGSIRIHRPDMQSAVFELLGIGAEEARAKFGFLLDALNYGAPPHGGIAFGIDRIAALMAGTESIRDVIPFPKTTGAQDLMTDAPSPIAADQLAEVHVQVRSKQV

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Pasteurella multocida (strain Pm70)
Length
588 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.433 kDa
Sequence
MMRTHYCGALNRDNIGQEVTLSGWVHRRRDLGGLIFIDMRDREGIVQVCFDPVYQEALTTAASLRNEFCIQIKGEVIARPDNQINKNMATGEVEVLAKSLSIYNSAEPLPLDFNQNNTEEQRLKYRYLDLRRPEMAQRLKTRAKITSFVRRFMDEHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFLTAPEVREIMEKMVHGLWRETLGVDLGKFPVMTFAEAMRRFGSDKPDLRNPLEMVDVADLLKEVEFKVFNGPANDPNGRIAVIRVPNGTDITRKQIDEYTQFVGIYGAKGLAWLKVNDLAAGMDGVQSPIAKFLSEAVLKALLERVQAQNGDILFFGADNYKVTTDAMGALRLKLGRDLGLTKLEEWQPLWVIDFPMFERDDEGDLAAMHHPFTSPKDFSPEQLEADPTSAVANAYDMVINGYEVGGGSVRIFDPKMQQTVFRILGINEAEQREKFGFLLDALKFGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPQALNELSVQVIKSE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2)
Length
587 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.33 kDa
Sequence
MRSHYCGDLRASHDGETVELCGWVSRRRDHGGVIFLDLRDRNGLVQVVFDPDTVDAFALADKVRSEYVVRLSGRVRMRDESVRNNKMATGDIEVLGKELTILNEAETPPFELDAHSAAGEEVRLKYRYMDLRRPDVLKNFQFRSRLTHVVRAFLEGEGFMDVETPILTRATPEGARDYLVPSRTHPGSFFALPQSPQLFKQLLMVAGFDRYYQIAKCFRDEDLRADRQPEFTQIDLEASFVEEEDIMGITERMVRSVFKELLSVDLPDFPRMPFSEAMQRFGSDKPDLRIALELIDIADLLAGVDFKVFSGPANDPKGRVAAMRVPGGCSLSRKDIDGYTKFVSIYGAKGLAYIKVNDLAAGAEGLQSPILKFLTEDAIKGILERTGAETGDLIFFGADKAKIVNEALGALRVKVGHDLNLVEGEWAPLWVVDFPMFEEDEGQYHALHHPFTMPSCSAEELKSNPGEALSRAYDMVLNGTELGGGSIRIHSPAMQRTVFEALGISDEEAEEKFGFLLDGLKYGAPPHGGLAFGLDRMVMLMTGCESIRDVIAFPKTQTAACTMTNAPSPVDNKQLREVGVQVRKEEG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC 11488 / FDC 602W)
Length
587 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.057 kDa
Sequence
MYVLRTHLCTQLGEGNIGEEVILCGWCNTYRDHGGVIFIDLRDKSGIIQLVSDPDDSPKAHENARVVRDEFVLIAKGKVRARGTGLENPKLATGKIEVILEELIIENRSLTPPITIGDESVGEDLRLKYRFLDLRNPKAYDTFRLRSKAAIAARNSLDGMGFLEVETPILTKATPEGARDYLVPSRVHPGEFFALPQSPQLFKQLLMISGFDRYFQIAKCFRDEDLRADRQPEFTQIDVEMSFCDQEDVMGVAEKLLGDIFSACGHTIPEHFPHLTYDRAMEEYGSDKPDLRFEMPLVEVIDLFGDSNNEIFAKIAQDSKKNRFKALKVKGGDLFFTRKTLGVLEEFVKKFGAAGLAYIQVKEEGLKGPLVKFMSERSLSLLLERLNPEVGDIIFFGAGEKKSVWDYMGRLRLEVAKQMGLIDPNQLCFLWVVNFPMFEKDEGKVKALHHPFTMPKNLDCEDVEEISSIAYDVVLNGVELGGGSIRIHQEAIQKRVFDLLGIAPEEAQEKFDFLLEALKFGAPPHGGFAIGFDRLIMLLTQSPSIRDVIAFPKTQKATCPLTSAPSPVSSEQLKELHIRIKEKTQTH

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680)
Length
587 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.725 kDa
Sequence
MHRYRSHTCGELRASDVGSDVRLSGWLHNRRDLGGILFIDLRDHYGITQLVARPGTPAYEALDKVSKESTVRVDGKVVSRGTENVNPDLPTGEIEVEVSEVELLGAAAPLPFTINAEDGVNEERRLEYRFLDLRRERMHRNILLRTAVISAIRHKMTALGFNEMATPILSATSPEGARDFVVPSRLHPGKFYALPQAPQQFKQLLMISGFDRYFQIAPCFRDEDARADRSPGEFYQLDVEMSFVEQEDVFQPIEKLMTELFEEFGGGRHVTSPFPRIPFREAMLKYGSDKPDLRAQLELVDITDIFEGSEFKAFAGKHVRALPVPDVSGQTRKFFDGLGDYAVEQGAKGLAWVRVGEDGSLTGPIAKFLTEENVAELTKRLSLAPGHAVFFGAGEFDEVSKIMGAVRVEAAKRSGNFEENVFRFCWIVDFPMYEKDEDTGKIDFSHNPFSMPQGGLEALETQDPLDILGWQYDIVCNGVELSSGAIRNHEPEIMLKAFEIAGYDRDTVEEQFAGMLRAFRFGAPPHGGIAPGVDRIVMLLADEPNIRETIAFPLNGNAQDLMMGAPTELDETRLRELHLSVRKPQPK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Length
587 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.002 kDa
Sequence
MHRYRSHTCGELRSSDVGTDVRLSGWLHNRRDLGGILFIDLRDHYGITQLVARPGTEAYEALDKLTKESTVRVDGKVVSRGADNINPDLPTGEVEVEVGEVELLGAAQPLPFTINTEDGVNEERRLEYRFLDLRRERMHRNIMLRTSVISSIRSKMVALGFNEMATPILTATSPEGARDFVVPSRLHAGRFYALPQAPQQFKQLLMISGFDRYFQIAPCFRDEDARADRSPGEFYQLDVEMSFVEQEDVFRPIEQLMTELFEEFGNGRHVTSPFPRIPFREAMLKYGSDKPDLRAQLELVDITDVFEGSEFKAFAGKHVRALPVPDVSGQPRRFFDQLGDYAVSQGAKGLAWVRVGEDGKLSGPIAKFLTEENVAELTKRLSLAPGHAVFFGAGEFDEVSKIMGAVRVEAAKRAGHFEENVFRFCWIVDFPMYEKDEETGKIDFSHNPFSMPQGGMDALENQDPLDILAWQYDIVCNGVELSSGAIRNHEPEIMLKAFEIAGYDAETVEREFAGMLRAFRFGAPPHGGIAPGVDRIVMLLADEPNIRETIAFPLNGNAQDLMMGAPTELDESRLRELHLTVRKPQPK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466)
Length
587 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.255 kDa
Sequence
MKRSMYAGRVREEHIGQEITLKGWVGRRRDLGGLIFIDLRDREGIMQLVINPEKVSAEVMATAESLRSEFVIEVTGQVAAREQANDKLPTGAVELNVTALIVLNTAKTTPFEIKDGIEANDDTRLRYRYLDLRRPEMLENLKLRAKVTHSIRNYLDELEFIDVETPFLSKSTPEGARDYLVPSRVNKGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLTEQEIQDITEGLIARVMKETKDIEVTLPFPRMKYDDAMALYGSDKPDTRFDMLLQDLTEVVKGVDFKVFSEALAVKAIVVKGAADNYSRKDIDKMTEVAKQYGAKGLAWVKVVDGELNGPVAKFLTGIQEELTTALALEDKDLVLFVADTLEVANATLGALRGRIAKELGLIDNDKFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPQEETAHELEGDLAKVRAIAYDIVLNGYELGGGSLRINQKDLQERMFKALGFSAEEANDQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGEENIREVIAFPKNNKATDPMTQAPSTVALKQLEELSLQVEEDETSKTN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus pneumoniae serotype 19F (strain G54)
Length
587 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.224 kDa
Sequence
MKRSMYAGRVREEHIGQEITLKGWVGRRRDLGGLIFIDLRDREGIMQLVINPEKVSAEVMATAESLRSEFVIEVTGQVAAREQANDKLPTGAVELNVTALIVLNTAKTTPFEIKDGIEANDDTRLRYRYLDLRRPEMLENLKLRAKVTHSIRNYLDELEFIDVETPFLSKSTPEGARDYLVPSRVNKGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLTEQEIQDITEGLIARVMKETKGIEVTLPFPRMKYDDAMALYGSDKPDTRFDMLLQDLTEVVKGVDFKVFSEALAVKAIVVKGAADNYSRKDIDKMTEVAKQYGAKGLAWVKVVDGELNGPVAKFLTGIQEELTTALALEDKDLVLFVADTLEVANATLGALRGRIAKELGLIDNDKFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPQEETAHELEGDLAKVRAIAYDIVLNGYELGGGSLRINQKDLQERMFKALGFSAEEANDQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGEENIREVIAFPKNNKATDPMTQAPSTVALKQLEELSLQVEEDETNKTN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus pneumoniae (strain 70585)
Length
587 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.176 kDa
Sequence
MKRSMYAGRVREEHIGQEITLKGWVGRRRDLGGLIFIDLRDREGIMQLVINPEKVSAEVMATAESLRSEFVIEVTGQVAAREQANDKLPTGAVELNVTALIVLNTAKTTPFEIKDGIEANDDTRLRYRYLDLRRPEMLENLKLRAKVTHSIRNYLDELEFIDVETPFLSKSTPEGARDYLVPSRVNKGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLTEQEIQDITEGLIARVMKETKGIEVTLPFPRVKYDDAMALYGSDKPDTRFDMLLQDLTEVVKGVDFKVFSEAPAVKAIVVKGAADNYSRKDIDKMTEVAKQYGAKGLAWVKVVDGELNGPVAKFLTGIQEELTTALALEDKDLVLFVADTLEVANATLGALRGRIAKELGLIDNDKFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPQEETAHELEGDLAKVRAIAYDIVLNGYELGGGSLRINQKDLQERMFKALGFSAEEANDQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGEENIREVIAFPKNNKATDPMTQAPSTVALKQLEELSLQVEEDETNKTN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482)
Length
587 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.563 kDa
Sequence
MFRTHTCGELRISDVNKQITLSGWVQRSRKMGGMTFIDLRDRYGITQLVFNEEINAELCDRANKLGREFVIQITGTVNERFSKNANIPTGDIEIIVSELNVLNTAMTPPFTIEDNTDGGDDIRMKYRYLDLRRNAVRSNLELRHKMTIEVRKYLDSLGFIEVETPVLIGSTPEGARDFVVPSRMNPGQFYALPQSPQTLKQLLMVSGFDRYFQIAKCFRDEDLRADRQPEFTQIDCEMSFVEQEDIISTFEGMAKHLFKTLRGVELTEPFQRMPWADAMKYYGSDKPDLRFGMKFVELMDIMKGHGFSVFDNAAYVGGICAEGAATYTRKQLDALTEFVKKPQIGAKGMVYARVEADGTVKSSVDKFYTQEVLQQMKEAFGAKPGDLILILSGDDVMKTRKQLCELRLEMGSQLGLRDKNKFVCLWVIDFPMFEWSEEEGRLMAMHHPFTHPKEEDIPLLDTDPAAVRADAYDMVVNGVEVGGGSIRIHDAQLQARMFEILGFTPEKAQAQFGFLMNAFKYGAPPHGGLAYGLDRWVSLFAGLDSIRDCIAFPKNNSGRDVMLDAPSEIDQTQLDELNLIVDIKENK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Bacteroides vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / NBRC 14291 / NCTC 11154)
Length
587 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.451 kDa
Sequence
MFRSHTCGELRLSDAGKSVTLAGWVQRARKMGGMTFVDLRDRYGITQLVFNEAVNAELCERANHLGREFVIQITGEVNERSNKNMNIPTGEIEIIVSVLNVLNSAVTPPFTIEDNSDGGDDIRMKFRYLDLRRNCVRKNLELRHKMTMEVRRYLDSKGFLEVETPMLVGSTPEGARDFVVPSRMNPGQFYALPQSPQTLKQLLMVSGFDRYFQIVKCFRDEDLRADRQPEFTQIDCEMSFVEQEDIISTFEGMAKHLFKELRGVELSEPFLRMTWADAIKYYGSDKPDLRFGMKFVELMDIMKGHGFSVFDDAAYIGGICAEGAASYTRKQLDQLTEFVKKPQIGAKGMVYARVEADGNVKSSVDKFYSQEVLQQMKEAFSAKPGDLILILSGPDAMKTRKQLCELRLEVGRQLGLRDKNKFACLWVVDFPMFEWSEEEGRLMAMHHPFTHPKEEDIPLLDTDPAAVRADAYDMVVNGVEVGGGSIRIHDSQLQAKMFEILGFTPERAQEQFGFLMNAFKYGAPPHGGLAYGLDRWVSLFAGLDSIRDCIAFPKNNSGRDVMLDAPAALDQSQLDELNLVVDIKEDK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
Length
587 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.056 kDa
Sequence
MYRTNTCGELRLSHLQQTVTLCGWVQRVRRMGGMTFVDLRDRYGTTQLVFNRDSAPAELCDRAEDLGREWVIRATGTVMERSSKNPNIPTGDIEIAVGEMDVLNRSEVPPFTIEDETDGGDDLRMKYRYLDLRRHCVRSNMELRHRMALEVRKYLDGEGFLEVETPMLIKSTPEGARDFVVPSRMNPGQFYALPQSPQTFKQLLMVSGFDRYFQIVKCFRDEDLRADRQPEFTQIDCEMSFVEQEDVLSTFEGMAKHLFRTIRHVEISEAFPRMTWHDAMKYYGSDKPDTRFDMRFVELMDVLKGHDFSVFDSAAYIGGICAKGAGSYTRKQLDALTDFVKRPQVGAKGMVYARVESDGSVKSSVDKFYTQETLQELRRTMEAEPGDLILILSGDDLMKTRKQLCELRLEVGSQLGLRDKNKFSCLWVVDFPLFEWDEETKRFYAMHHPFTSPKPEDIPLLDTDPGAVRANAYDMVINGVEVGGGSIRIHDSALQQKMFELLGFTPEKAQEQFGFLMNAFKYGAPPHGGLAYGLDRWVSLFAGLDSIRDCIAFPKNNAGRDVMIDAPSVIDEAQLQELFLELIPNEN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Length
587 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.998 kDa
Sequence
MYRTNTCGELRLSHLQQTVTLCGWVQRVRRMGGMTFVDLRDRYGTTQLVFNRDSAPAELCDRAEDLGREWVIRATGTVMERSSKNPNIPTGDIEIAVGEMDVLNRSEVPPFTIEDETDGGDDLRMKYRYLDLRRHCVRSNMELRHRMALEVRKYLDGEGFLEVETPMLIKSTPEGARDFVVPSRMNPGQFYALPQSPQTFKQLLMVSGFDRYFQIVKCFRDEDLRADRQPEFTQIDCEMSFVEQEDVLSTFEGMAKHLFRTIRHVEISEAFPRMTWHDAMKYYGSDKPDTRFDMRFVELMDVLKGHGFSVFDSAAYIGGICAKGAGSYTRKQLDALTDFVKRPQVGAKGMVYARVESDGSVKSSVDKFYTQETLQELRRTMEAEPGDLILILSGDDLMKTRKQLCELRLEVGSQLGLRDKNKFSCLWVVDFPLFEWDEETKRFYAMHHPFTSPKPEDIPLLDTDPGAVRANAYDMVINGVEVGGGSIRIHDSALQQKMFELLGFTPEKAQEQFGFLMNAFKYGAPPHGGLAYGLDRWVSLFAGLDSIRDCIAFPKNNAGRDVMIDAPSVIDEAQLQELFLELIPNEN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus pneumoniae (strain Hungary19A-6)
Length
587 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.155 kDa
Sequence
MKRSMYAGRVREEHIGQEITLKGWVGRRRDLGGLIFIDLRDREGIMQLVINPEKVSAEVMATAESLRSEFVIEVTGQVAAREQANDKLPTGAVELNVTALIVLNTAKTTPFEIKDGIEANDDTRLRYRYLDLRRPEMLENLKLRAKVTHSIRNYLDELEFIDVETPFLSKSTPEGARDYLVPSRVNKGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLTEQEIQDITEGLIARVMKETKGIEVTLPFPRMKYDDAMALYGSDKPDTRFDMLLQDLTEVVKGVDFKVFSEAPAVKAIVVKGAADNYSRKDIDKMTEVAKQYGAKGLAWVKVVDGELNGPVAKFLTSIQAELTTALSLEDKDLVLFVADTLEVANATLGALRGRIAKELGLIDNDKFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPQEETAHELEGDLAKVRAIAYDIVLNGYELGGGSLRINQKDLQERMFKALGFSAEEANDQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGEENIREVIAFPKNNKASDPMTQAPSTVALKQLEELSLQVEEDETSKTN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1)
Length
587 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.238 kDa
Sequence
MKRSMYAGRVREEHIGQEITLKGWVGRRRDLGGLIFIDLRDREGIMQLVINPEKVSAEVMATAESLRSEFVIEVTGQVAAREQANDKLPTGAVELNVTALIVLNTAKTTPFEIKDGIEANDDTRLRYRYLDLRRPEMLENLKLRAKVTHSIRNYLDELEFIDVETPFLSKSTPEGARDYLVPSRVNKGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLTEQEIQDITEGLIARVMKETKGIEVTLPFPRMKYDDAMALYGSDKPDTRFDMLLQDLTEVVKGVDFKVFSEAPAVKAIVVKGAADNYSRKDIDKMTEVAKQYGAKGLAWVKVVDGELNGPVAKFLTGIQEELTTALALEDKDLVLFVADTLEVANATLGALRGRIAKELGLIDNDKFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPQEETAHELEGDLAKVRAIAYDIVLNGYELGGGSLRINQKDLQERMFKALGFSTEEANDQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGEENIREVIAFPKNNKATDPMTQAPSTVALKQLEELSLQVEEDETNKTN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Length
587 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.297 kDa
Sequence
MKRSMYAGRVREEHIGQEITLKGWVGRRRDLGGLIFIDLRDREGIMQLVINPEKVSAEVMATAESLRSEFVIEVTGQVAAREQANDKLPTGAVELNVTALIVLNTAKTTPFEIKDGIEANDDTRLRYRYLDLRRPEMLENLKLRAKVTHSIRNYLDELEFIDVETPFLSKSTPEGARDYLVPSRVNKGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLTEQEIQDITESLIARVMKETKGIEVTLPFPRMKYDDAMALYGSDKPDTRFDMLLQDLTEVVRGVDFKVFSEAPAVKAIVVTGAADNYSRKDIDKMTEVAKQYGAKGLAWVKVVDGELNGPVAKFLTGIQEELTTALVLEDKDLVLFVADTLEVANATLGALRGRIAKELGLIDNDKFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPQEETAHELEGDLAKVRAIAYDIVLNGYELGGGSLRINQKDLQERMFKALGFSTEEANDQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGEENIREVIAFPKNNKATDPMTQAPSTVALKQLEELSLQVEEDETNKTN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus pneumoniae (strain CGSP14)
Length
587 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.238 kDa
Sequence
MKRSMYAGRVREEHIGQEITLKGWVGRRRDLGGLIFIDLRDREGIMQLVINPEKVSAEVMATAESLRSEFVIEVTGQVAAREQANDKLPTGAVELNVTALIVLNTAKTTPFEIKDGIEANDDTRLRYRYLDLRRPEMLENLKLRAKVTHSIRNYLDELEFIDVETPFLSKSTPEGARDYLVPSRVNKGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLTEQEIQDITEGLIARVMKETKGIEVTLPFPRMKYDDAMALYGSDKPDTRFDMLLQDLTEVVKGVDFKVFSEAPAVKAIVVKGAADNYSRKDIDKMTEVAKQYGAKGLAWVKVVDGELNGPVAKFLTGIQEELTTALALEDKDLVLFVADTLEVANATLGALRGRIAKELGLIDNDKFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPQEETAHELEGDLAKVRAIAYDIVLNGYELGGGSLRINQKDLQERMFKALGFSTEEANDQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGEENIREVIAFPKNNKATDPMTQAPSTVALKQLEELSLQVEEDETNKTN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus pneumoniae (strain ATCC BAA-255 / R6)
Length
587 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.255 kDa
Sequence
MKRSMYAGRVREEHIGQEITLKGWVGRRRDLGGLIFIDLRDREGIMQLVINPEKVSAEVMATAESLRSEFVIEVTGQVAAREQANDKLPTGAVELNVTALIVLNTAKTTPFEIKDGIEANDDTRLRYRYLDLRRPEMLENLKLRAKVTHSIRNYLDELEFIDVETPFLSKSTPEGARDYLVPSRVNKGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLTEQEIQDITEGLIARVMKETKDIEVTLPFPRMKYDDAMALYGSDKPDTRFDMLLQDLTEVVKGVDFKVFSEALAVKAIVVKGAADNYSRKDIDKMTEVAKQYGAKGLAWVKVVDGELNGPVAKFLTGIQEELTTALALEDKDLVLFVADTLEVANATLGALRGRIAKELGLIDNDKFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPQEETAHELEGDLAKVRAIAYDIVLNGYELGGGSLRINQKDLQERMFKALGFSAEEANDQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGEENIREVIAFPKNNKATDPMTQAPSTVALKQLEELSLQVEEDETSKTN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus pneumoniae (strain JJA)
Length
587 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.238 kDa
Sequence
MKRSMYAGRVREEHIGQEITLKGWVGRRRDLGGLIFIDLRDREGIMQLVINPEKVSAEVMATAESLRSEFVIEVTGQVAAREQANDKLPTGAVELNVTALIVLNTAKTTPFEIKDGIEANDDTRLRYRYLDLRRPEMLENLKLRAKVTHSIRNYLDELEFIDVETPFLSKSTPEGARDYLVPSRVNKGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLTEQEIQDITEGLIARVMKETKGIEVTLPFPRMKYDDAMALYGSDKPDTRFDMLLQDLTEVVKGVDFKVFSEAPAVKAIVVKGAADNYSRKDIDKMTEVAKQYGAKGLAWVKVVDGELNGPVAKFLTGIQEELTTALALEDKDLVLFVADTLEVANATLGALRGRIAKELGLIDNDKFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPQEETAHELEGDLAKVRAIAYDIVLNGYELGGGSLRINQKDLQERMFKALGFSTEEANDQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGEENIREVIAFPKNNKATDPMTQAPSTVALKQLEELSLQVEEDETNKTN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus pneumoniae (strain P1031)
Length
587 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.194 kDa
Sequence
MKRSMYAGRVREEHIGQEITLKGWVGRRRNLGGLIFIDLRDREGIMQLVINPEKVSAEVMATAESLRSEFVIEVTGQVAAREQANDKLPTGAVELNVTALIVLNTAKTTPFEIKDGIEANDDTRLRYRYLDLRRPEMLENLKLRAKVTHSIRNYLDELEFIDVETPFLSKSTPEGARDYLVPSRVNKGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLTEKEIQDITEGLIARVMKETKGIEVTLPFPRMKYDDAMALYGSDKPDTRFDMLLQDLTEVVKGVDFKVFSEAPAVKAIVVKGAADNYSRKDIDKMTEVAKQYGAKGLAWVKVVDGELNGPVAKFLTGIQEELTTALALEDKDLVLFVADTLEVVNATLGALRGRIAKELGLIDNDKFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPQEGTAHELEGDLAKVRAIAYDIVLNGYELGGGSLRINQKDLQERMFKALGFSTEEANDQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGEENIREVIAFPKNNKATDPMTQAPSTVALKQLEELSLQVEEDETNKTN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus pneumoniae (strain Taiwan19F-14)
Length
587 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.149 kDa
Sequence
MKRSMYAGRVREEHIGQEITLKGWVGRRRDLGGLIFIDLRDREGIMQLVINPEKVSAEVMATAESLRSEFVIEVTGQVAAREQANDKLPTGAVELNVTALIVLNTAKTTPFEIKDGIEANDDTRLRYRYLDLRRPEMLENLKLRAKVTHSIRNYLDELEFIDVETPFLSKSTPEGARDYLVPSRVNKGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLTEQEIQDITEGLIARVMKETKGIEVTLPFPRVKYDDAMALYGSDKPDTRFDMLLQDLTEVVKGVDFKVFSEAPAVKAIVVKGAADNYSRKDIDKMTEVAKQYGAKGLAWVKVVDGELNGPVAKFLTGIQEELTTALALEDKDLVLFVADTLEVANATLGALRGRIAKELGLIDNDKFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPQEETAHELEGDLAKVRAIAYDIVLNGYELGGGSLRINQKDLQERMFKALGFSAEEANDQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGEENIREVIAFPKNNKATDPMTQAPSTVALKQLEELSLQVEEDETSKTN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen)
Length
586 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.867 kDa
Sequence
MKRTHNATELDIHLVGREVMLNGWVDTRRDHGGLIFVDLRDRSGIIQLVFSPEVKEEAFHLAEQIRSEYVIAVRGKLSLRPEATENPNLKTGKVEVYVEDIEVLSPAKTPPFYIENDIDVDENLRLKYRYLDLRRPEMRDNLLLRHRVVKCMRDFLDSRGFIEIETPILTKSTPEGARDYLVPSRVHPGEFYALPQSPQIFKQILMVAGMEKYFQIARCFRDEDLRADRQPEFTQLDMEMSFVDEEDIIVLVEEMMAEIFFKAAGKVIRTPFPRLAYDDAMINYGSDKPDLRFGLEIVELSEMLQNTQFKVFASALQSGGVVRALNAKGCGSFTRREIDALGAMAVENGAKGMAWILVQENELRSPITKFLSEEEIEQILMTTGAEAGDLILFGADQAEIVARVMGILRLELGRKKGLIAEEELNFVWVTDFPLLEYDEEEKRYQAKHHPFTSPRLEDIEIMDSEPGRVKARAYDLVLNGTELGGGSIRIHRREWQEKMFSVLGMSQEEARDKFGFMLEAFEYGTPPHGGIAFGVDRLLMLLAGRNSVRDVMAFPKTQSASCPMTEAPSTVSARQLRELALRIREK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Borrelia afzelii (strain PKo)
Length
586 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.229 kDa
Sequence
MFKVIKCNELNEKLINKKVEINAWVKKIRHHGKFTFLDIRDRYEKAQVLITEEHLLKIVEKIKLEYCIKIQGLLIKRPSNMINANMTTGYFEILAKNIEIISKCNELPFMIEDDNNASENSKLKYRYLDLRRDSLKNKIILRCQATHLIRNFLVKRKFLELETPTFVKSTPEGARDFVIPSRIHKGSFYALPQSPQLYKQLIMIAGFDKYFQIARCYRDEDSRGDRQPEFTQLDLEMSFVKKENIFKLIENMLFSIFKNCLNIKLSKKFKKITYKTAMNKYGSDKPDTRFELTLQDISRNLKNSEFNVFKDILNNKGSIKTLIVKDKADTFSRAKINNLEEIAKLYKTQGLYFTKIENNKFSGGIAKFLKTEEQQLIKAYSLENNDIIFFIANNKWEIACKAMGQIRIKIANDLGLIDENKFEFLWVYDFPLFEYDENTKTYIPAHHMFSIPKKRYISNLEKNPNKAIGEIYDLVLNGVELGSGSIRIHNKELQQRIFNIIGFQKEKSEDRFGFFLKALEYGAPNHGGIAIGIDRLIMLMTKSTSIKDVILFPKNSFAASPLDNSPSKISNEQLKELGINIAPDDT

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Borreliella bavariensis (strain ATCC BAA-2496 / DSM 23469 / PBi)
Length
586 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.267 kDa
Sequence
MFKVIKCNELNEKLINKKVEINAWVKKIRHHGKFIFLNIRDRYEKAQVLITEEHLLKIAEKIKLEYCIKIQGLLSKRPPNMINENMKTGSFEILAKNIEIISKCNELPFMIEDDNNASENSKLKYRYLDLRRDSLKNKIILRCQATHLIRNFLVKKKFLELETPTFVKSTPEGARDFVIPSRIHKGSFYALPQSPQLYKQLIMIAGFDKYFQIARCYRDEDSRGDRQPEFTQLDLEMSFVKKENIFKLIENMLFLIFKNCLNIKLPKKFKKITYKTAMNKYGSDKPDTRFELTLQDISRNLKNSEFNVFKETLKNKGSIKILIVKDEADKFSRAKINNLEEIAKLYKTQGLYFAKIENNKFSGGIAKFLKTEEQQLIKTYSLENNDIIFFTANKKWETACKAMGQIRIKIANDLGLIDENKFEFLWVYDFPLFEYDENTKTYTPAHHMFSLPKKRYIASLEKIPNKTIGEIYDLVLNGVELGSGSIRIHNKELQQRIFNIIGFQKEKSEDRFGFFLKALEYGAPNHGGIAIGIDRLIMLMTKSTSIKDVILFPKNSFATSPLDDSPSKISNEQLKELGINIVTDDA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Borrelia burgdorferi (strain ATCC 35210 / B31 / CIP 102532 / DSM 4680)
Length
586 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.344 kDa
Sequence
MFKVIKCNELNEKLIDKKVEINAWVKKIRHHGKFIFLNIRDRYEKAQVLVNEEKLLKIAEKIKLEYCIKIQGLLIKRPPNMINANMKTGHFEILAKNIEIISKCNELPFMIEDDNNASENSKLEYRYLDLRRDSLKNKIILRCQATHLIRNFLIKRKFLELETPTFVKSTPEGARDFVIPSRIHKGSFYALPQSPQLYKQLIMIAGFDKYFQIARCYRDEDSRGDRQPEFTQLDLEMSFVKKENIFKLIENMLFLIFKNCININLPKKFKKITYKKAMNKYGSDKPDTRFELELQDISRNLKNSEFNIFKDTLKNKGSIKILIVKDKADKFSRAKINNLEEIAKLYKTQGLYFTKIENNKFSGGIAKFLKTEEQELIKTYSLENNDIIFFTANNNWETACKAMGQIRIKIANDLGLIDENKFEFLWVYDFPLFEYDENTKTYSPAHHMFSLPKKQYIANLEKNPKKTIGEIYDLVLNGVELGSGSIRIHNKELQQRIFKIIGFQKEKSEDRFGFFLKALEYGAPNHGGIAIGIDRLIMLMTKSTSIKDVILFPKNSFAASPLDNSPSKISNEQLKELGINIVDGDN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Borrelia burgdorferi (strain ZS7)
Length
586 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.344 kDa
Sequence
MFKVIKCNELNEKLIDKKVEINAWVKKIRHHGKFIFLNIRDRYEKAQVLVNEEKLLKIAEKIKLEYCIKIQGLLIKRPPNMINANMKTGHFEILAKNIEIISKCNELPFMIEDDNNASENSKLEYRYLDLRRDSLKNKIILRCQATHLIRNFLIKRKFLELETPTFVKSTPEGARDFVIPSRIHKGSFYALPQSPQLYKQLIMIAGFDKYFQIARCYRDEDSRGDRQPEFTQLDLEMSFVKKENIFKLIENMLFLIFKNCININLPKKFKKITYKKAMNKYGSDKPDTRFELELQDISRNLKNSEFNIFKDTLKNKGSIKILIVKDKADKFSRAKINNLEEIAKLYKTQGLYFTKIENNKFSGGIAKFLKTEEQELIKTYSLENNDIIFFTANNNWETACKAMGQIRIKIANDLGLIDENKFEFLWVYDFPLFEYDENTKTYSPAHHMFSLPKKQYIANLEKNPKKTIGEIYDLVLNGVELGSGSIRIHNKELQQRIFKIIGFQKEKSEDRFGFFLKALEYGAPNHGGIAIGIDRLIMLMTKSTSIKDVILFPKNSFAASPLDNSPSKISNEQLKELGINIVDGDN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Brachyspira hyodysenteriae (strain ATCC 49526 / WA1)
Length
586 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.939 kDa
Sequence
MRFKSAYNGILTKDDIGKEVKLAGWVLRRRDHGGVIFVDLRDRTGFVQIVFNPEISKEAHNDAQDLRSEYVISVEGKIRARSPEMINPKIPTGEIEVMVEKMELLNTSETPPFLLEDDIDTGEDIRLKYRYLDLRRPTVFNNLYKRFQITNAFRKHLSDNGFIDVETPILNKSTPEGARDFLVPSRLNAGDFYALPQSPQIFKQILMIGGFDRYYQIAKCFRDEDLRADRQPEFTQVDIETSFLNTDEFLSIMENVTANIVKDVYGIDLPTPFPRLNYYDAMEMYGSDKPDTRFELKLINVEDAVRGCDFAVFKNALDNKFIIRCLNAKGGEKLSRKDIDDFTKYVGIFGAKGLAWMRVTDKGLESNIVKFFSEENQKKILEVTKAEKGDLLFFVADTPKVTFDALGNLRLRVAEKLNLIDKDKLNFLWVVEFPLFEYDHKEKRISATHHPFTAPVPEDVAILESEPLKVRSDTYDLVLNGNEIGGGGQRIYDSKVQAIIFKLLGIDEEKAKLRFGFLLDALKYGAPPMCGMAYGIDRVVMLLQKQDSIREVIAFPKTQKGQCLMSGCPSTVDADQLEELHLSIEE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A)
Length
586 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.076 kDa
Sequence
MRTKYCGNIRISHVNKKVKLCGWVHKVRNLGQFIFVDMRDYTGLVQVIFELKNYTIFKKALNLRNEFCIQVFGTVQKREKKNQNIKIRTGEIEILANVLNILNTSKSLPLNFTQENNDDSRLKYRYLDLRSFDILENLKIRNKITYLIRNFMTKKNFLDIETPILTKSTPEGARDYLVPSRNHYGKFYALPQSPQLFKQILMISGIDRYYQIVKCFRDEDLRSDRQPEFTQIDIEVSFMSAKKIRNLVENLIKKLWLEIRNINLKKFPQISFHEAMKKYGSDKPDLRNPIEIIDVSNIFKDKKFISFFNLNPQKNNRIALLCISKGAHLSRKKIDDYTKYVQRFDAKKLFYIKIKECKLGCLGIHSSIKNILDEIILKEIIEKSQSKNGDILFLIADQEHIVNKSLGMLRLKIGIDLNITKKNRWEPLWIVNFPMFDKDIQGNLSSVHHPFTAVKNMDREILKNSPDLAISDSYDLIINGYEIGGGSVRIHDVNMQKQVFDIIGIKKSMQNEKFGFLIEALKYGAPPHAGIALGLDRIVMLLTNSKNIRDVIAFPKTTSATCLMTNSPSTVDNLLLQELAIKHLKK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS)
Length
586 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.121 kDa
Sequence
MRTKYCGNIRISHVNKKVKLCGWVHKVRNLGQFIFVDMRDYTGLVQVIFELKNYKIFKKALNLRNEFCIQVFGTVQKREKKNQNIKIRTGEIEILANVLNILNTSKSLPLNFTQENNDDSRLKYRYLDLRSFDILENLKIRNKITYLIRNFMTKKNFLDIETPILTKSTPEGARDYLVPSRNHYGKFYALPQSPQLFKQILMISGIDRYYQIVKCFRDEDLRSDRQPEFTQIDIEVSFMSAKKIRNLVENLIKKLWLEIRNINLKKFPQISFHEAMKKYGSDKPDLRNPIEIIDVSNIFKDKKFISFFNLNPQKNNRIALLCISKGAHLSRKKIDDYTKYVQRFDAKKLFYMKIKECKLGCLGIHSSIKNILDEIILKEIIEKSQSKNGDILFLIADQEHIVNKSLGMLRLKIGIDLNITKKNRWEPLWIVNFPMFDKDIQGNLSSVHHPFTAVKNMDREILKNSPDLAISDSYDLIINGYEIGGGSVRIHDVNMQKQVFDIIGIKKSMQNEKFGFLIEALKYGAPPHAGIALGLDRIVMLLTNSKNIRDVIAFPKTTSATCLMTNSPSTVDNLLLQELAIKHLKK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Buchnera aphidicola subsp. Acyrthosiphon pisum (strain Tuc7)
Length
586 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.076 kDa
Sequence
MRTKYCGNIRISHVNKKVKLCGWVHKVRNLGQFIFVDMRDYTGLVQVIFELKNYTIFKKALNLRNEFCIQVFGTVQKREKKNQNIKIRTGEIEILANVLNILNTSKSLPLNFTQENNDDSRLKYRYLDLRSFDILENLKIRNKITYLIRNFMTKKNFLDIETPILTKSTPEGARDYLVPSRNHYGKFYALPQSPQLFKQILMISGIDRYYQIVKCFRDEDLRSDRQPEFTQIDIEVSFMSAKKIRNLVENLIKKLWLEIRNINLKKFPQISFHEAMKKYGSDKPDLRNPIEIIDVSNIFKDKKFISFFNLNPQKNNRIALLCISKGAHLSRKKIDDYTKYVQRFDAKKLFYIKIKECKLGCLGIHSSIKNILDEIILKEIIEKSQSKNGDILFLIADQEHIVNKSLGMLRLKIGIDLNITKKNRWEPLWIVNFPMFDKDIQGNLSSVHHPFTAVKNMDREILKNSPDLAISDSYDLIINGYEIGGGSVRIHDVNMQKQVFDIIGIKKSMQNEKFGFLIEALKYGAPPHAGIALGLDRIVMLLTNSKNIRDVIAFPKTTSATCLMTNSPSTVDNLLLQELAIKHLKK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Onion yellows phytoplasma (strain OY-M)
Length
586 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.521 kDa
Sequence
MKTKYSHYNNQLQLAHQGKTVFLKGFIFRKRNLGKTLFFDLRDVSGIVQLLVKENNPQYDKIALIKLETVVQIKGQVIERINKNPDLPTGDIEILVSHIEILSEAQTLPLNVFQSQESLEETRLKYRYLDLRNPEVKHFLIQRHHITQSIRQTLLKNDFLELETLILSKSTPEGARDYLVPSRIYPGNFYALPQSPQLFKQLYMIAGFERYFQVARCFRDEDLRSDRQPEFSQIDIETSFLNQDEIMSLTEEIIVDLFANIWKKPLSQPFLRLTYQQAFELYGSDKPDLRNPLKITDFTTFFDTTTCPQNMFSGNIKGFKVSKTAVLTRRKLDEYQLFFSKHFNLKLFSFVKKNDKIIGGISQFIKDDSFLKNEEICFVVSGTKDIMHKALGIFRTKLALDLSLVDTTQEALLWIVDFPLFETTQEDLPQPDLTLENSNTSNRLYSLHHPFTAPCDIAILKSNPQKALAKTYDLVWNGYEVGGGSLRINNPQTQELIFSLLGFSQEEVQTRFGFLVEALKYGTPPHGGLALGLDRLVMLFTKTNNIKDVIAFPKTQSAKDLMLEAPSAVDQEQLNTLKLKFKCNCN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Campylobacter concisus (strain 13826)
Length
585 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.863 kDa
Sequence
MRSHYCTDLSKADIGKEVILCGWANTYRDHGGVVFIDLRDVSGLIQLVCDPADSKEAHDVAAKVRDEYVLKAKGKVRARGEGLTNPKLKTGEIEVIVSELIIENPSEPLPFMIGDESVNEDIRLKYRFLDLRSERLQNIFKMRSRAAIAARNSLDKMGFIEFETPVLTRATPEGARDYLVPSRVYPGQFYALPQSPQLFKQLLMCSGFDKYFQIAKCFRDEDLRADRQPEFTQIDIEMSFVEQEDIINMAETMLKDIFKACGHDIKTPFRRMSYKEATETYGSDKPDLRYDLKMIDVIDIFERSSNEIFSSIAKDKKKNRIKALKVPNGDNIFSKREMNRFEEFVRKFGAQGLGYFQMKEDGLKGPLCKFFEQSDLDEIVSRCELKVGDVVFFGAGKKKIVLDYMGRFRIFLAEQMGIIDQDRLEFLWVLDFPMFEQNDDGSYSAMHHPFTMPKNIDEPDLEDILSIAHDVVLNGFELGGGSIRIHKNDIQQKVFKLLGIDEAEQREKFGFLLDALTFGAPPHGGIAIGFDRLNMLVNKASSIRDVIAFPKTQRAQCPLTKAPSYASNEQLRELGLRIREKEQKA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF)
Length
585 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.253 kDa
Sequence
MKRTHYCGELTRELVGKKVVLKGWADNRRDHGKLIFIDMRDNSGLVQVVCDFESNPEALEVADSVRSEYVLEITGTVRERSPENVNPDLKTGEIEVDCEDINVLNTSKTPPFFINENVDVDENIRLKYRYLDLRRPSMQNNIYLRHKITKLVRDFLDENGFIEVETPMLTKSTPEGARDFLVPSRLHEGSFYALPQSPQLFKQLLMASGVEKYFQIARCFRDEDLRADRQPEFSQIDIEMSFFEQEEFMKLMENMVSKLFKEVLGIELTKPFPRITYQEAMDRYGSDSPDLRYGLELHDVSDLVKDAEFKVFRETVASEGQVKGIAVPQGQEFSRKEIDDLTEFVKEFGAKGLAWMVLEEEEIKSPIAKFFSDEELDGIIDRMGANTGDLLLFVADEPEIVADSLSKLREHLANKLDLIPSNEYQLTWVIDFPLMEYDKDEGRYKALHHPFTSPYEDDLEKYENEPEKIRAKAYDLVLNGVEIGGGSMRIHQKELQEKMFEFLGIPLEEAKQKFGFLFEAFEYGTPPHGGIAFGLDRLVMLFTGSQSIRDVIAFPKTANASCLMTEAPAKVDENQLKELHLKTTK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Borrelia duttonii (strain Ly)
Length
585 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.003 kDa
Sequence
MFKIIKCNQINNKLINKKIEINGWVKKIRNHGKVTFINIRDRYDEAQILVSDEKLLKITSQIKMEYCIKIQGKLNLRPLELVNREMKTGELEIIAENIDIISKCNELPFMIENNNNASDNSKLEYRYLDLRREEQKQKIILRSKVIHIIRNHLTKQDFLELETPTFVKSTPEGARDFLVPSRIHKGHFYALPQSPQIYKQLAMIAGLDKYFQIARCYRDEDSRGDRQPEFTQLDLEMSFIKKENIFKLIENLIFTIFKNSLNITLPKKFKKITYKDAMNIYGSDKPDTRYELLIQDMSKALKQSPFDVFKDTLQNKGTIKALIIKNQAHNFSRSKINSLEEHAKLYKARTLYFTKIENNEFTGGIAKFINPIKKTLIETYSLKNNDLIFFIADLWETACKAIGQIRIKIATELNLINKNIFEFLWIYDFPLFEYDEDTQSYKAAHHMFSMPQAKYINTLESNPSEVLGEVYDLVLNGTELGSGSIRVHTKELQQRIFNIVGFNDKIAEERFGFFLKALEYGAPIHGGIAIGIDRLLMLMTNSNSIKDVILFPKNSFAASPLDKSPSKISNEQLKELNLTIENNKN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Borrelia hermsii (strain HS1 / DAH)
Length
585 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.27 kDa
Sequence
MFKTIRCNQINDKLVNQRIEINAWVKKIRHHGKVTFINLRDRYDEAQVLVSDENLLKITSQIKMEYCIKVQGTLELRPLELANKEMKTGAFEILAENIDIISRCNELPFMIEDNNNANDNAKLEYRYLDLRREEQKQKIILRSKVTHIIRNYLTKKDFLELETPTFVKSTPEGARDFLVPSRIHKGHFYALPQSPQIYKQLTMVAGLDKYFQIARCYRDEDSRGDRQPEFTQLDLEMSFIKKENIFKLMENLMFTIFKNTLNIALPKKFKKMTYKHAMNTYGSDKPDTRYELLIQDMSKHFKKSSFNVFQDMLQNKGTIKALIIKNQAHNFSRSKINNLEEHAKIYKARGLYFAKIENNEFSGGIAKFLNEIKQTLIEAYSLANNDIIFFIADSWETACKAMGQVRIKIATELNLINKNIFEFLWIYDFPLFEYDEDTKSYQAAHHMFSLPKQKYIHTLESNPSKVLGEVYDLVLNGMELGSGSIRVHTRELQQRIFNIVGFKNEIAEERFGFFLKALEYGAPIHGGIAIGIDRLLMLMTHSSSIKDVILFPKNSFAASPLDKSPSRISNEQLRELNLTIENYKN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Borrelia turicatae (strain 91E135)
Length
585 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
68.356 kDa
Sequence
MFKTIKCNQINDKLINQKIEINAWVKKIRHHGKVTFINLRDRYDEAQVLVNDEKLLKITSQIKMEYCIKVQGKLELRPSNLVNKEMRTGAFEILAENINIISRCNELPFMIEDNNNANENAKLEYRYLDLRREEQKQKIILRSKVTHTIRNYLTKKDFLELETPTFVKSTPEGARDFLVPSRIHKGHFYALPQSPQIYKQLTMIAGLDKYFQIARCYRDEDSRGDRQPEFTQLDIEMSFIKKENIFKLMENLIFTIFKNTLNISLPKKFKRMTYKHAMNTYGSDKPDTRYELLIQDMGKYFKQSSFNVFKDILQNKGTIKALIIKNQAHNFSRSKINNLEEHAKIYKTSGLYFAKIENNEFVGGIAKFLNKIKQTLFQTYSLKNNDIIFFIADSWETACKAMGQIRIKIANELNLTNKNTFEFLWIYDFPLFEYDEDTKNYKAAHHMFSLPQQKYIDTLESNPSKVLGEVYDLVLNGMELGSGSIRVHTRELQQRIFNIVGFKDTIAEERFGFFLKALEYGAPIHGGIAIGIDRLLMIMTHSSSIKDVILFPKNSFAASPLDKAPSKVPNEQLRELNLTIEDYKN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Haemophilus somnus (strain 129Pt)
Length
585 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.122 kDa
Sequence
MRSHYCGALNRSHIGQQVILSGWVHKRRDLGGLIFIDMRDREGIVQVCFDPKYQEALTEASALRNEFCIKIEGEVIARPDNQINKNMATGEVEVVAKALSVYNVSDVLPLDFNQNNTEEQRLKYRYLDLRRPEMAQHLKTRAKITAFVRRYMDENGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPEVREIMEKMVHGLWLNTIGVDLGKFPTMTWQEAMERFGSDKPDLRNPLEIVDVADIVKDIDFNVFSDPANSSNGRVAVIRVPNGINITRKQIDEYTQFVGIYGAKGLAWVKINDINAGLEGVQSPIAKFLTTEKIKAIFDRTSAQSGDILFFGADKWQTATDAMGALRLKLGRDLGLTHLDEWKPLWVIDFPMFERDEEGNLAAMHHPFTSPKDFTPEQLEANPTSAVANAYDMVINGYEVGGGSVRIFDPKMQQTVFHILGIDEDQQREKFGFLLDALKFGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTDAPSLANEKALEELAIKTIM

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / JCM 11019 / NCTC 9343)
Length
585 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.229 kDa
Sequence
MFRTHTCGELRISDVNKQVKLSGWVQRSRKMGGMTFVDLRDRYGITQLVFNEEIDAELCERANKLGREFVIQIVGTVNERFSKNSHIPTGDIEIIVSELNILNSAITPPFTIEDNTDGGDDIRMKYRYLDLRRSAVRSNLELRHKMTIEVRSYLDKLGFLEVETPVLIGSTPEGARDFVVPSRMNPGQFYALPQSPQTLKQLLMVSGFDRYFQIAKCFRDEDLRADRQPEFTQIDCEMSFVEQEDVITTFEGMAKHLFKVIRNIELTEPFPRMPWSEAMRLYGSDKPDIRFGMQFVELMDILKGHGFSVFDNATYIGGICAEGAAGYTRKQLDALTEFVKKPQIGAKGMVYARIEADGTVKSSVDKFYTQEVLQQLKEAFGAKPGDLILILSGDDAMKTRKQLCELRLEMGNQLGLRDKNTFACLWVVDFPLFEWSEEEGRLMAMHHPFTSPKPEDIHLLDTNPAAVRANAYDMVINGVEVGGGSIRIHDSQLQNKMFELLGFTPERAQEQFGFLMNAFKFGAPPHGGLAYGLDRWVSLFAGLDSIRDCIAFPKNNSGRDVMLDAPAALDPSQLEELNLIVDIKE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Bacteroides fragilis (strain YCH46)
Length
585 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.169 kDa
Sequence
MFRTHTCGELRISDVNKQVKLSGWVQRSRKMGGMTFVDLRDRYGITQLVFNEEIDAELCERANKLGREFVIQIVGTVNERFSKNSHIPTGDIEIIVSELNILNSAITPPFTIEDNTDGGDDIRMKYRYLDLRRSAVRSNLELRHKMTIEVRSYLDKLGFLEVETPVLIGSTPEGARDFVVPSRMNPGQFYALPQSPQTLKQLLMVSGFDRYFQIAKCFRDEDLRADRQPEFTQIDCEMSFVEQEDVITTFEGMAKHLFKVIRNIELTGPFPRMPWSEAMRLYGSDKPDIRFGMQFVELMDILKGHGFSVFDNATYIGGICAEGAAGYTRKQLDALTEFVKKPQIGAKGMVYARIEADGTVKSSVDKFYIQEVLQQLKEAFGAKPGDLILILSGDDAMKTRKQLCELRLEMGNQLGLRDKNTFACLWVVDFPLFEWSEEEGRLMAMHHPFTSPKPEDIHLLDTNPAAVRANAYDMVINGVEVGGGSIRIHDSQLQNKMFELLGFTPERAQEQFGFLMNAFKFGAPPHGGLAYGLDRWVSLFAGLDSIRDCIAFPKNNSGRDVMLDAPAALDPSQLEELNLIVDIKE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152)
Length
585 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.428 kDa
Sequence
MYRTRTCGDLRLADEGLVVTLAGWVQKTRKMGGMTFVDIRDRYGITQLVFNQEVDAALCEKANKLGREFVIQVTGTVRERSSKNAHIPTGDIELIVSELNVLNTALTPPFTIEEETDGGDDLRMKYRYLDLRRACVRKNLELRHRMAFEVRRYLDEQGFLEVETPVLVNSTPEGARDFVVPSRMNPGQFYALPQSPQTLKQLLMVSGFDRYFQIVKCFRDEDLRADRQPEFTQIDCEMSFVEQEDVLNMFEGMAKHLFKVIRGVEFKESFMRMTWQDAMKQYGSDKPDLRFGMKFVELMDIMKGHGFSVFDNAAYIGGICAEGAASYTRKQLDALTEFVKRPQVGAKGLVYARVEADGNVKSSVDKFYSQEVLQEMKNAFGAKPGDLILILSGDDAMKTRKQLCELRLEMGNQLGLRDKDKFVCLWVIDFPLFEWNEDDQRFYAMHHPFTSPNPDDIPLLDTDPGAVRANAYDMVINGVEVGGGSIRIHDSQLQDKMFKLLGFTEERAQEQFGFLMNAFKYGAPPHGGLAYGLDRFVSLFAGLDSIRDCIAFPKNNSGRDVMLDAPGVLDPAQLDELNLIVDIKK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO)
Length
585 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.725 kDa
Sequence
MLRTHTCGELTIKDVGKKVILAGWIDRIRDLGGVKFLMLRDRYGQTQIILSQNCQINLRRESVVQIEGVVQKRPEETINKDLLTGEIEVFAEKVNVFSSPEKDLPFYPGETKLPAEEIRLKYRYIDLRRKEVSDRIITRHKVTQCIRNYLSKNGFIEVETPFLTKSTPEGARDFLVPSRLKPGTFYALPQSPQLFKQLLMIGGIDRYFQVVRCFRDEDLRADRQPEFTQIDIEMSFNTMDDVLEITEGMIKHLFKEVLQVDLPGKLDRLTYNECMNKYGSDKPDRRIGMEFFDLSKHFKTCEYHAINAELSSGGVVKGFVVRDFANKMSRKLADELNEIAKSLGGGGILWFSFDSPESIKGAGAKYLQKNYNSVAKELSINYNDVCVLSAGKIDIVNTVLGEVRKILGERYFSDLRKGFDIFWVTDFPMFEYSEEENRFVAQHHPFTMPNLDDLKKYKNSDLSKIRAQSYDIVINGFEVGSGSIRIHDAELQREIFKLMRLTEEEVKLKFGFLLEAFQYGAPPHGGIALGLDRLTAIICGVPTIREVIAFPKTSSGICPLTGAPDVVNQKQLDELKIILGGDHCE

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Helicobacter acinonychis (strain Sheeba)
Length
584 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.518 kDa
Sequence
MRSHFCTEVSEKDIDKIVKVAGWCNTYRDHGGVVFIDLRDKSGLVQLVCDPSSKAYEKALEVRSEFVLVAKGKARLRGPGLENPKLKTGKIEIVLEELVIENKSATPPIEIGNKNVNEDLRLKYRYLDLRSLNAYEIFKLRSEVALIARNTLAQKGFLEIETPILSKTTPEGARDYLVPSRVHEGEFFALPQSPQLFKQLLMVGGMDRYFQIARCFRDEDLRADRQPEFTQIDAEMSFCDENDVMGVVEDLLREIFKAIGHTIPTPFKRMPYKEAMENYGSDKPDLRFELPLVEVGDCFMDSSNSIFSNIAKDSKNKRIKALNVKGADATFSRSVLKELEEFVHQFGAQGLAYLQIKEYEIKGPLVKFLSEKGLKNILERTNAQVGDIVFFGAGDKKIVLDYMGRLRLKVAEMLDLIDKNAWNFLWVVNFPMFEKTENGYHAAHHPFTMPKNIECEDIEEIEAYAYDVVLNGVELGGGSIRIHKEEMQKKVFERINIHEDEAQKKFGFLLEALKFGAPPHGGFAIGFDRLIMLMTQSNSIRDVIAFPKTQKASCLLTNAPSPISEEQLRELHIRLRKLSLKDMI

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Uncultured termite group 1 bacterium phylotype Rs-D17
Length
584 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.139 kDa
Sequence
MKRSGYCGDIRESSIGKEIAVCGWVHSRRDHGGVIFIDLRDREGILQIVFQPENKEIFEAAEKLRSEYVIAVKGWVRNRPFGTLNTNMSTGNVELVAVELKILNTSPGLPFEISDYIDTSEELRLKYRYLDLRRPNLQKNFVMRHKISKEIRNFLNEEGFLEIETPFLTKSTPEGARDFLVPSRLHHGNFFALPQSPQLFKQILMSAGFDKYYQIVRCFRDEDLRADRQPEFTQVDVEMSFVDEEDVMVVIERMLARVFKMTLNLDIKMPFERMPYSEAMLRFGSDKPDTRFEVEIKDFSRELKNSGFSVFSSVISKGGIVRGLCIPKGASFSRSEIAGLTKFVGEYGAKGLVWMKITDTGADSNIVKYFKEYEIRVFISKLNAKSGDLIVFLADEEKTVAQGLGALRLKVGRESGLIDKNKFNFLWVVDFPLMEWDKEEQRWQALHHPFTLPKDADSLTKENAGRAKAKAYDVVLNGIELGGGSIRIHKSGIQKKIFNILDISDESAEKKFGFLLKALTYGAPPHGGAALGFDRLCALISGEDSIREVIAFPKTQKAVDPLSNAPAAVSDNHLKELGLQQIEN

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Campylobacter fetus subsp. fetus (strain 82-40)
Length
584 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.354 kDa
Sequence
MRSHYCTDLSSNDIGKKVQLCGWVNSYRDHGGVIFIDLRDRTGIIQLVCDPKDSKSAHEIGSKVRDEYVLKATGTIRARGEGLINPKLKTGEIEVIVDELYIENESAALPFVIGDPNVGEDIRLKYRFLDLRNTESFDKFKLRSKASIACRNALDRLGFLEVETPILTRATPEGARDYLVPSRVYPGSFYALPQSPQLFKQLLMCAGFDKYFQIARCFRDEDLRADRQPEFTQIDVEMSFCTQEDVIKVGEEILKDIFYACGHDIITPFRRMEYKDAMETYGNDKPDLRFDLPMVDVIDIFAKSNNEIFSTPAQNIKKNRAKAIKVPGGDNIFSKRQMQRFEEFVRKFGAKGLAFIQVKEDGLKGPLVKFFEQEQIDELIKRCELKVGDVVFFGIGDKKTVLDYMGRFRAFLANELGIIDENKLEFLWVVNFPMFEQNDDGSYSAMHHPFTMPNNPDEEDLEDITSIAYDVVLNGVELGGGSIRIHKNDIQQKVFKLLKIDEAEQREKFGFLLDALSFGAPPHGGFAIGLDRLIMLVTKSASIRDVIAFPKTQRASCPMTKAPSNVSNEQLRELGLRLKGKETK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Campylobacter hominis (strain ATCC BAA-381 / LMG 19568 / NCTC 13146 / CH001A)
Length
584 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.704 kDa
Sequence
MRSNYCTELDSGDIGKIVDVCGWVNSYRDHGGVIFIDLRDRSGLIQLVCDPKHSQEAYTIANSVRDEFVLRAHGKIRARGKDLINPKLKTGEIEVVVENLIVENPSKPLPFVIGDKNVSEETRLKYRFLDLRTNENFNKFFTRSKAAIAARNALDRLGFVEVETPILTRATPEGARDYLVPSRVYNGQFYALPQSPQLFKQLLMCSCFDKYFQIARCFRDEDLRADRQPEFTQIDIEMSFCDQKDVMKVGEAVLKDIFKSCGKDIKTPFRVMQYKDAMENYGSDKPDLRFGMKFIDVADIFEKSSNEIFANIAKDKKKNRVKAIKVEGGDLKFSKRQMQRFEEYVRKFGAQGLAFIQVKEEGLKGPLVKFFEKSEIDELVKRCELKVGDVVFFGAGKKKIVLDYMGRFRIFLANELELINPDALEFLWVVDFPMFEQNEDGTYSAMHHPFTMPNNVDEPDIEEITSIAYDVVLNGIELGGGSIRIHKEDIQEKVFKLLKIEPAEQREKFGFLLDALSFGAPPHGGIAIGFDRLMMLVTRSSSIRDVIAFPKTQRAQCLLTKAPSGISNEQLRELGLKINKKEQK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chlamydia abortus (strain DSM 27085 / S26/3)
Length
584 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.482 kDa
Sequence
MKYRTHRCNELSLSNVGERVRLSGWVHRYRNHGGVVFIDLRDRFGITQIVCREDEKPELHQLVDSVRSEWVLSIEGTVCRRLEGMENANLATGEIEVDIEKVDILSKAKNLPFSISDDHIHVNEELRLEYRYLDMRRGQILDRLVHRHKVMMACRQYMDKQGFTEVVTPILGKSTPEGARDYLVPSRIYPGSFYALPQSPQLFKQILMVGGLDRYFQIATCFRDEDLRADRQPEFAQIDIEMSFGTPNDLFPIIEQLVVEMFAVQGIKIDLPLPRMTYQEAKDLYGTDKPDLRFGLQLHDCREHAKEFSFSIFLDQLAQGGTIKGFCVPGGADMSRKQLDVYTEFVKRYGAMGLVWIKKQESGIASNVAKFASEAVFQAMFADFGAQNNDILLLIAAPEDVANQSLDHLRRLIAKERNFYNEAQYNFVWITDFPLFAKEDGKICSEHHPFTSPLDEDIPLLDKDPLSVRSSSYDLVLNGYEIASGSQRIHNADLQNKIFSILELSPESIKEKFDFFIDALSFGTPPHLGIALGLDRIMMVLTGAEGIREVIAFPKTQKAADLMMDAPAEIMTSQLKELSIKVTS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chlamydophila caviae (strain GPIC)
Length
584 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.513 kDa
Sequence
MKYRTHRCNELSLSNVGERVRVSGWVHRYRNHGGVVFIDLRDRFGITQIVCREDEKPELHQLVDSVRSEWVLSVEGTVCRRLEGMENANLATGDIEVEIEKVDILSKAKNLPFSISDDHIHVNEELRLEYRYLDMRRGQILDRLIYRHKVMLACRQYMDKQGFTEVVTPVLGKSTPEGARDYLVPSRIYPGSFYALPQSPQLFKQILMVGGLDRYFQIATCFRDEDLRADRQPEFAQIDIEMSFATPDDLFPIIEQLVVEMFSVQGIKIDLPLPRMTYQEAKDLYGTDKPDLRFGLQLRDCREHAKQFSFSIFLDQLAQGGTIKGFCVPGGADMSRKQLDVYTEFVKRYGAMGLVWIKKQENGLASNVAKFASEEVFDAMFADFSAKDNDILLLIAAPESIANQSLDHLRRLIGKERNLYNESQYNFVWITDFPLFAKEEGKICSEHHPFTSPLDEDISLLDTDPLSVRSSSYDLVLNGYEIASGSQRIHNADLQNKIFSILELSPESIKEKFGFFIDALSFGTPPHLGIALGLDRIMMVLTGAEGIREVIAFPKTQKAADLMMNAPAEIMTSQLKELNIKVTS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chlamydia pneumoniae
Length
584 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.345 kDa
Sequence
MKYRTHRCNELTSNHIGENVQLAGWVHRYRNHGGVVFIDLRDRFGITQIVCREDEQPELHQRLDAVRSEWVLSVRGKVCPRLAGMENPNLATGHIEVEVASFEVLSKSQNLPFSIADDHINVNEELRLEYRYLDMRRGDIIEKLLCRHQVMLACRNFMDAQGFTEIVTPVLGKSTPEGARDYLVPSRIYPGKFYALPQSPQLFKQLLMVGGLDRYFQIATCFRDEDLRADRQPEFAQIDIEMSFGDTQDLLPIIEQLVATLFATQGIEIPLPLAKMTYQEAKDSYGTDKPDLRFDLKLKDCRDYAKRSSFSIFLDQLAHGGTIKGFCVPGGATMSRKQLDGYTEFVKRYGAMGLVWIKNQEGKVASNIAKFMDEEVFHELFAYFDAKDQDILLLIAAPESVANQSLDHLRRLIAKERELYSDNQYNFVWITDFPLFSLEDGKIVAEHHPFTAPLEEDIPLLETDPLAVRSSSYDLVLNGYEIASGSQRIHNPDLQSQIFTILKISPESIQEKFGFFIKALSFGTPPHLGIALGLDRLVMVLTAAESIREVIAFPKTQKASDLMMNAPSEIMSSQLKELSIKVAF

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Length
584 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.824 kDa
Sequence
MRTKYCGNIRIIDLHKSVILCGWVHKIRNFSQFIFIDMRDWTGIVQLVFEKKNNKVFTKAVNLKNESCIQVIGIVKKRNANNNNLDTGEIEILVNKIKVFNISKNLPLDYSNNSNDDIRLKYRYLDLRRSELLENLKIRNKITHLIRIFMENKNFLDIETPFLTKSTPEGARDYLVPSRNYPGNFYALPQSPQLFKQILMISGIDKYYQIVKCFRDEDLRSDRQPEFTQIDIEASFVSSTKIRNLVETLIKKIWLKVINYNLNKFPKISFYDSMKRYGSDKPDLRNPMEIVDISDIVIEEKVASFFQINLKKKNRIALLCFGQGNKISQKKIDEYSNYVKKFGAKKLFYIKINKIENRFQDIQSSIKNILDKNTLENILRKTNAKNGNILFLLADEEKIVNKSLGMLRIKLGNDFIFFKKNTWKPVWIVDFPMFKQNSDGKFSSNHHPFTALKKNNQNKLEKNPNLAISDSYDLVINGYEIGGGSVRIHDAKIQKKVFNIIGIEKQFQREKFGFLIEALKYGPPPHAGIALGLDRIVMLLTNTNNIRDVIAFPKTTSANCLMTDSPSKLKKSILNELGINILKK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Sulfurovum sp. (strain NBC37-1)
Length
584 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.37 kDa
Sequence
MRTHYCADVNEQHIGETVTVAGWVASRRDHGGVIFIDLRDKDEVFQLVCDPADNADAHKIAEEVRDQFVLIATGKVRARGEGLENPNLKTGKVEMVVDSLTIENRSKPMPFELNDEKVNEEIKLKYRYLELRTQKAYDTFKLRSKATIATRNALDELGFLEVETPILTKSTPEGARDYLVPSRVHGGEFYALPQSPQLFKQLLMVGGFDRYFQIAKCFRDEDLRADRQPEFTQIDVEMSFCDQEDVITVAEKLISDVFIKCGFDVPTKFNRMTHSEAMEKYGSDKPDMRYDLAMVDVIDIFERCDNEIFSGIAKMPKKNRIKALRVPKGDEIFSKRQMKGFEDYVRKFGAQGLGYFQMKEDGLKGPLTKFFTEDDIQAIIDRCGLEVGDAVFFGAGEKKLVWDYMGRFRIYLAETMDIIPEDTFEFLWVMDFPMFEVEDGKVKALHHPFTQPKSLDFNDIEEIESIAYDVVLNGTELGGGSIRIHKEDVQEEVFKLLGISEEEAQSKFGFLLDALKFGAPPHGGFALGLDRMIMIMTGASSIRDVIAFPKTQKAQCLLTQAPSEVDNEQLKELSIRVRQAAPTA

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Elusimicrobium minutum (strain Pei191)
Length
583 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.652 kDa
Sequence
MMRTNYCGDINKNYVNSVQVLCGWVNSYRDHGGVLFLDLRDRTGKVQVVVEPTNKDFELASTARTEYVLKVTGLVRLRQTEHINPNNPTGEIEVVAQEVEILNTSIQLPFEPDNSRQINEETRLKYRYIDLRNPVMLHNLTTRHKVAQAARRYFSDNGFIEIETPILTRSTPEGARDYLVPSRVHEGKFYALPQSPQMFKQTLMASGVDRYFQIARAFRDEDLRSDRQPEHTQIDIEMSFVTLADVFAAGEGMIAEVFKAAGEDAPAAPFEQMEYADVMAKYGSDKPDIRYEIDITDIGGIFTNSNFKVVSDALANGGVVRAIKAKYGAKHINRSTCDKLTDLAKASGAKGLVWLKYSDDKFEGPSAKFFTEEELASLQHTLSVEKDDMVFIGADKEKVVSPVMGAIRKELIKLLCLKPNKKWAFLWVKHFPLLEFVPEENRWDAAHNPFTAPLEKDIPLLDTDPGKVKSYQFDLVLNGVELASGSIRNHRRDLQEKILNLMKHSPEQAALRFGMLLNALEAGAPPHGGFGMGLDRLAALLCKEESIREVIAFPKTATAYCPLTESPNVVEDIQLKELHIKIK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Campylobacter jejuni subsp. jejuni serotype O:6 (strain 81116 / NCTC 11828)
Length
583 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.08 kDa
Sequence
MRSHYNTDLGISHVGQSVKLCGWVNSYRDHGGVIFIDLRDRSGIIQLVCDPNDSKEAHEIASNARNEFVLIAEGTIRPRGEGLVNPKLKTGEIEVVVSKLTIENESAVPPFAIADESVNEELRLKYRFLDLRNPKLYENFALRSKACIAARNSLANMGFLEVETPILTKATPEGARDYLVPSRVHQGEFYALPQSPQLFKQLLMCSGFDRYFQIAKCFRDEDLRADRQPEFTQIDVEMSFCEQKDVINVAETFLKDIFKACGKEIQTPFRQMQYKDAMENYGSDKPDLRFDLKFIDVIDIFAKSNNEIFANIAKDTKKNRIKAIRVPKGDTIFSKRQMQRFEEFVRKFGAQGLAFIQVKEDGLKGPLCKFFSEEDLNELSKRCELEVGDVVFFGAGAKKTVLDYMGRFRIFLANELNLIDPNALEFLWVVDFPMFEQNDDGSYSAMHHPFTMPKNIDETDLEEISSIAYDVVLNGVELGGGSIRIHKNDIQQKVFKLLNIDEEQQKEKFGFLLDALSFGAPPHGGIAIGLDRLIMLVTGANSIREVIAFPKTQRAQCLMTDAPSPASNEAMRELGIKLRENIK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Campylobacter jejuni subsp. doylei (strain ATCC BAA-1458 / RM4099 / 269.97)
Length
583 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.161 kDa
Sequence
MRSHYNIDLGISHVGQSVKLCGWVNSYRDHGGVIFIDLRDRSGIIQLVCDPNDSKEAHEIASNARNEFVLIAEGTIRPRGEGLVNPKLKTGEIEVVVSKLTIENESIVPPFAIADESVNEELRLKYRFLDLRNPKLYENFALRSKACIAARNSLANMGFLEVETPILTKATPEGARDYLVPSRVHQGEFYALPQSPQLFKQLLMCSGFDRYFQIAKCFRDEDLRADRQPEFTQIDVEMSFCEKKDVINVAETFLKDIFKACGKEIQTPFRQMQYKDAMENYGSDKPDLRFDLKFIDVIDIFAKSNNEIFANIAKDTKKNRIKAIRVPKGDTIFSKRQMQRFEEFVRKFGAEGLAFIQVKEDGLKGPLCKFFSEEDLNELSKRCKLEVGDVVFFGAGAKKTVLDYMGRFRIFLANELNLIDPNALEFLWVVDFPMFEQNDDGSYSAMHHPFTMPKNIDENDLEEISSIAYDVVLNGVELGGGSIRIHKNDIQQKVFKLLNIDEEQQKEKFGFLLDALSFGAPPHGGIAIGLDRLIMLVTGANSIREVIAFPKTQRAQCLMTEAPSPASNEAMRELGIKLRENIK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Length
583 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.167 kDa
Sequence
MRSHYNTDLGISHVGQSVKLCGWVNSYRDHGGVIFIDLRDRSGIIQLVCDPNDSKEAHEIASNARNEFVLITEGTIRPRGEGLVNPKLKTGEIEVVVSKLTIENESAVPPFAIADESVNEELRLKYRFLDLRNPKLYENFALRSKACIAARNSLANMGFLEVETPILTKATPEGARDYLVPSRVHQGEFYALPQSPQLFKQLLMCSGFDRYFQIAKCFRDEDLRADRQPEFTQIDVEMSFCEQKDVIKVAETFLKDIFKACGKEIQTPFRQMQYKDAMENYGSDKPDLRFDLKFIDVIDIFTKSNNEIFANIAKDTKKNRIKAIRVPKGDTIFSKRQMQRFEEFVRKFGAQGLAFIQVKKDGLKGPLCKFFSEEDLNELSKRCELEVGDVVFFGAGAKKTVLDYMGRFRIFLANELKLIDPNALEFLWVVDFPMFEQNDDGSYSAMHHPFTMPKNIDETDLEEISSIAYDVVLNGVELGGGSIRIHKNDIQQKVFKLLNIDEEQQKEKFGFLLDALSFGAPPHGGIAIGLDRLIMLVTGANSIREVIAFPKTQRAQCLMTDAPSPASNEAMRELGIKLRENIK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Campylobacter jejuni subsp. jejuni serotype O:23/36 (strain 81-176)
Length
583 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.08 kDa
Sequence
MRSHYNTDLGISHVGQSVKLCGWVNSYRDHGGVIFIDLRDRSGIIQLVCDPNDSKEAHEIASNARNEFVLIAEGAIRPRGEGLVNPKLKTGEIEVVVSKLTIENESAVPPFTIADESVNEELRLKYRFLDLRNPKLYENFALRSKACIAARNSLANMGFLEVETPILTKATPEGARDYLVPSRVHQGEFYALPQSPQLFKQLLMCSGFDRYFQIAKCFRDEDLRADRQPEFTQIDVEMSFCEQKDVINVAETFLKDIFKACGKEIQTPFRQMQYKDAMENYGSDKPDLRFDLKFIDVIDIFAKSNNEIFANIAKDTKKNRIKAIRVPKGDTIFSKRQMQRFEEFVRKFGAQGLAFIQVKEDGLKGPLCKFFSEEDLNELSKRCELEVGDVVFFGAGAKKTVLDYMGRFRIFLANELNLIDPNALEFLWVVDFPMFEQNDDGSYSAMHHPFTMPKNIDETDLEEISSIAYDVVLNGVELGGGSIRIHKNDIQQKVFKLLNIDEEQQKEKFGFLLDALSFGAPPHGGIAIGLDRLIMLVTGANSIREVIAFPKTQRAQCLMTDAPSPASNEAMRELGIKLRENIK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Campylobacter jejuni (strain RM1221)
Length
583 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.148 kDa
Sequence
MRSHYNTDLGISHVGQSVKLCGWVNSYRDHGGVIFIDLRDRSGIIQLVCDPNDSKEAHEIASNARNEFVLIAEGTIRPRGEGLINPKLKTGEIEVVVSKLTIENESAVPPFAIADESVNEELRLKYRFLDLRNPKLYENFALRSKACIAARNSLANMGFLEVETPILTKATPEGARDYLVPSRVHQGEFYALPQSPQLFKQLLMCSGFDRYFQIAKCFRDEDLRADRQPEFTQIDIEMSFCEQKDVINVAETFLKDIFKACGKEIQTPFRQMQYKDAMENYGSDKPDLRFNLKFIDVIDIFAKSNNEIFANIAKDTKKNRIKAIRVPKGDTIFSKRQMQRFEEFVRKFGAQGLAFIQVKEDGLKGPLCKFFSEEDLNELSKRCELEVGDVVFFGAGAKKTVLDYMGRFRIFLANELKLIDPNALEFLWVVDFPMFEQNDDGSYSAMHHPFTMPKNIDETDLEEISSIAYDVVLNGVELGGGSIRIHKNDIQQKVFKLLNIDEEQQKEKFGFLLDALSFGAPPHGGIAIGLDRLIMLVTGANNIREVIAFPKTQRAQCLMTDAPSPASNEAMRELGIKLRENIK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / UW101)
Length
583 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.138 kDa
Sequence
MYRSHNCGELNASNINTEVTLAGWVQKSRDKGFMNWVDLRDRYGITQLIFDESRTDKTVFELAKTLGREFVIQVKGTVIEREAKNKNIPTGEIEILVSELTILNTALTPPFTIEDETDGGEDIRMKYRYLDIRRNPVKNSLLFRHKVAMEVRKYLSDLDFCEVETPYLIKSTPEGARDFVVPSRMNEGQFYALPQSPQTFKQLLMVGGMDKYFQIVKCFRDEDLRADRQPEFTQIDCEMAFVEQEDILNVFEGLTRHLLKEIKGIEVDKFPRITYDYAMKTYGNDKPDIRFGMKFGELNEFAQHKEFPVFNAAELVVGIAVPGAGNYTRKEIDGLIDWVKRPQVGASGMVYVKCNEDGTYKSSVDKFYDNDDLAKWAKATEANPGDMIFVLSGPANKTRAQLSALRMELATRLGLRNPEEFAPLWVVDFPLLELDEESGRYHAMHHPFTSPKPEDMALLETEPGKVRANAYDMVLNGNEIGGGSIRIHDKATQQLMFKYLGFTEEEAKAQFGFLMDAFQFGAPPHGGLAFGLDRLVAILGGQETIRDFIAFPKNNSGRDVMIDAPAAIDDAQLKELHIKIDSI

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Flavobacterium psychrophilum (strain JIP02/86 / ATCC 49511)
Length
583 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.453 kDa
Sequence
MYRSHNCGELNATHINKEVTLAGWVQKSRDKGFMNWVDLRDRYGITQLMFDESRSDKTVFELAKTLGREFVIQVKGTVIEREAKNKNISTGEIEILVTQMTILNSSLTPPFTIEDETDGGEDIRMKYRYLDIRRNPVKNSLLFRHKVAMEVRKYLSDLDFCEVETPYLIKSTPEGARDFVVPSRMNEGQFYALPQSPQTFKQLLMVGGMDKYFQIVKCFRDEDLRADRQPEFTQIDCEMAFVEQEDILNIFEGLTRHLLKELKGIEVEKFPRMTYNHAMKTYGNDKPDIRFGMEFGELNEYAKHKDFPVFNAAELVVAIAVPGVGEYSRKEIDALIEWVKRPQVGASGMVYVKCNEDGTYKSSVDKFYDQGDLSHWAKTTGAKAGDMIFVLSGPADKTRAQLSALRMELATRLGLRNPAEFAPLWVVDFPLLEFDEESGRYHAMHHPFTSPKPEDMHLLETDPKSVRANAYDMVLNGNEIGGGSIRIHDKNTQALMFKYLGFTEEEAKNQFGFLMDAFQFGAPPHGGLAFGLDRLVAILGGQETIRDFIAFPKNNSGRDVMIDAPSIIDDSQLKELHIQLDLK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Borrelia recurrentis (strain A1)
Length
583 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.833 kDa
Sequence
MFKIIKCNQINNKLINKKIEINGWVKKIRNHGKVTFINIRDRYDEAQILVSDEKLLKITSQIKMEYCIKIQGKLNLRPLELVNREMKTGELEIIAENIDIISKCNELPFMIENNNNASDNSKLEYRYLDLRREEQKQKIILRSKVIHIIRNHLTKQDFLELETPTFVKSTPEGARDFLVPSRIHKGHFYALPQSPQIYKQLAMIAGLDKYFQIARCYRDEDSRGDRQPEFTQLDLEMSFIKKENIFKLIENLIFTIFKNSLNITLPKKFKKITYKDAMNIYGSDKPDTRYELLIQDMSKALKQSPFDVFKDTLQNKGTIKALIIKNQAHNFSRSKINSLEEHAKLYKARTLYFTKIENNEFTGGIAKFINPIKKTLIETYSLKNNDIIFFIADLWETACKAIGQIRIKIATELNLINKNIFEFLWIYDFPLFEYDEDTQSYKAAHHMFSMPQAKYINTLESNPSKVLGEVYDIVLNGTELGSGSIRVHTKELQQRIFNIVGFNDKIAEERFDFFLKALEYGAPIHGGIAIGIDRLLMLMTNSNSIKDVILFPKNSFAASPLDKSPSKISDEQLKELNLTIENK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC SS700)
Length
583 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.127 kDa
Sequence
MKRSMYAGRVRSEHIGTSITLKGWVGRRRDLGGLIFIDLRDREGIMQLVINPEEVSASVMATAESLRSEFVIEVSGVVTAREQANDNLPTGEVELKVQELSVLNTSKTTPFEIKDGIEANDDTRMRYRYLDLRRPEMLENFKLRAKVTHSIRNYLDNLEFIDVETPMLTKSTPEGARDYLVPSRVNQGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLSDQEIQDIVEGMIAKVMKDTKGLEVSLPFPRMAYDDAMNNYGSDKPDTRFDMLLQDLTEVVKEVDFKVFSEASVVKAIVVKNKADKYSRKNIDKLTEIAKQYGAKGLAWLKYADNTISGPVAKFLTAIEDRLTEALQLENNDLILFVADSLEVANETLGALRTRIAKELELIDYSKFNFLWIVDWPMFEWSEEEGRYMSAHHPFTLPTAETAHELEGDLAKVRAVAYDIVLNGYELGGGSLRINQKDTQERMFKALGFSAESAQEQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGKDNIREVIAFPKNNKASDPMTQAPSLVSEQQLEELSLTVESYEN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus agalactiae serotype III (strain NEM316)
Length
583 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.082 kDa
Sequence
MKRSMYAGRVRSEHIGTSITLKGWVGRRRDLGGLIFIDLRDREGIMQLVINPEEVAASVMATAESLRSEFVIEVSGVVTAREQANDNLPTGEVELKVQELSVLNTSKTTPFEIKDGIEANDDTRMRYRYLDLRRPEMLENFKLRAKVTHSIRNYLDNLEFIDVETPMLTKSTPEGARDYLVPSRVNQGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLSDQEIQDIVEGMIAKVMKDTKGLEVSLPFPRMAYDDAMNNYGSDKPDTRFDMLLQDLTEIVKEVDFKVFSEASVVKAIVVKDKADKYSRKNIDKLTEIAKQYGAKGLAWLKYVDNTISGPVAKFLTAIEGRLTEALQLENNDLILFVADSLEVANETLGALRTRIAKELELIDYSKFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPTAETAHELEGDLAKVRAVAYDIVLNGYELGGGSLRINQKDTQERMFKALGFSAESAQEQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGKDNIREVIAFPKNNKASDPMTQAPSLVSEQQLEELSLTVESYEN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)
Length
583 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.084 kDa
Sequence
MKRSMYAGRVRSEHIGTSITLKGWVGRRRDLGGLIFIDLRDREGIMQLVINPEEVSASVMATAESLRSEFVIEVSGVVTAREQANDNLPTGEVELKVQELSILNTSKTTPFEIKDGIEANDDTRMRYRYLDLRRPEMLENFKLRAKVTHSIRNYLDNLEFIDVETPMLTKSTPEGARDYLVPSRVNQGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLSDQEIQDIVEGMIAKVMKDTKGLEVSLPFPRMAYDDAMNNYGSDKPDTRFDMLLQDLTEIVKEVDFKVFSEASVVKAIVVKDKADKYSRKNIDKLTEIAKQYGAKGLAWLKYADNTISGPVAKFLTAIEGRLTEALQLENNDLILFVADSLEVANETLGALRTRIAKELELIDYSKFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPTAETAHELEGDLAKVRAVAYDIVLNGYELGGGSLRINQKDTQERMFKALGFSAESAQEQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGKDNIREVIAFPKNNKASDPMTQAPSLVSEQQLEELSLTVESYEN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Stenotrophomonas maltophilia (strain R551-3)
Length
583 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.569 kDa
Sequence
MRTHFCGLVDETLIGQTVTLAGWTDVARNQGGVCFIDLRDHEGIVQVTVEVDNAEVFAVAASLGYEDVLQVEGVVRARHAVNDKMRTGKVEVIATAITVLNKAAPLPFHAHENPGEETRLKYRYLDLRRPEMQRMQRTRIKLVQALRRHLDEKGFQDIETPILTKATPEGARDFLVPARMHPGEFYALPQSPQLFKQILMVAGFDRYYQIARCFRDEALRADRQLEFTQLDMEFAFVRERDVQDFVEDMIRGIFKEVVNVELDASFPRMTWAEAMRRYGSDKPDLRIALELVDVAELVKNSEFPVFTGPANDADGRVAALRIPGGASLSRKQIDEYAAHAAKYGAKGLAYIKIADNGEVSSPIQKFFSEESFAALVAHVGAGNGDIVFFGAGGYNKVSDFMGALRLKAGKDFGLVADGWAPLWVTDFPMFEWDEEEQRYVALHHPFTAPAVDDIADLRANARTAVSRGYDMVLNGNEIGGGSIRIHRPDMQSAVFELLGIGAEEARAKFGFLLDALNYGAPPHGGIAFGIDRIAALMAGTESIRDVIPFPKTTGAQDLMTDAPSPIVDAQLAEVHIQVRPKTN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Stenotrophomonas maltophilia (strain K279a)
Length
583 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.554 kDa
Sequence
MRTHFCGLVDETLIGQTVTLAGWTDVARNQGGVCFIDLRDHEGIVQVTVEVDNAEVFAVAASLGYEDVLQVEGVVRARHAVNDKMRTGKVEVIATAITVLNKAAPLPFHAHENPGEETRLKYRYLDLRRPEMQRMQRTRIKLVQALRRHLDEKGFQDIETPILTKATPEGARDFLVPARMHPGEFYALPQSPQLFKQILMVAGFDRYYQIARCFRDEALRADRQLEFTQLDMEFAFVRERDVQDFVEDMIRAIFKEVVDVQLDASFPRMTWAEAMRRYGSDKPDLRIALELVDVAELVKDSEFPVFTGPANDAEGRVAALRIPGGASLSRKQIDEYAAHAAKYGAKGLAYIKIADNGEISSPIQKFFSEASFAALVAHVGAGNGDIVFFGAGGYNKVSDFMGALRLKAGKDFGLVADGWAPLWVTDFPMFEWDEEEQRYVALHHPFTAPAVDDIADLRANARTAVSRGYDMVLNGNEIGGGSIRIHRPDMQSAVFELLGIGAEEARAKFGFLLDALNYGAPPHGGIAFGIDRIAALMAGTESIRDVIPFPKTTGAQDLMTDAPSPIVDAQLAEVHIQVRPKTN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Azobacteroides pseudotrichonymphae genomovar. CFP2
Length
583 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.026 kDa
Sequence
MYRTNTCGELRIVNENQEVILCGWVQKSRRMSGIVFVDLRDRYGITQLIFNKKVNLALYNKALELGREWVIQIEGKVVKRFNKNSDIPTGDIEIIVSRLRTLNPSEVPPFTIEENTDGGDDLRMKYRYLDLRRTLIRSNLELRHQMVFAIRNYLNSHEFMEVETPVLINSTPEGARDFIVPSRMNMGEFYSLPQSPQLFKQLLMIAGFDRYFQVVKCFRDEDLRTDRQPEFTQVDCEMSFVEQEDILSIFEGLTKHLFKTIKGLDISGFSRLSYADAIRFYGSDKPDIRFGMQLVEIKDITIGRGFDVFDESEYVGAICAEGCAFYTRKQLDELTDFVKHPQIGAAGLIYVRYSFDGSLKSSVDKFYSTVDLQKWIDRVGAKQGDLVLILYGEKRETQKQLSRLRLEMGSRLGLRDKKQFGCLWVIDFPLFEYDNVLNRFFAKHHPFTSPKQEDVCLLETNPEFVRANAFDMVINGIEIGGGSIRIHNYELQKKIFALLGFSESYTQSQFGFFVDAFKYGAPPHGGIALGLDRFVATFAGLDSIRDCIAFPKNNSGRDTMVGAPSIISRERLSELNLIVEGWQ

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Ruthia magnifica subsp. Calyptogena magnifica
Length
583 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.713 kDa
Sequence
MRTHFCGELNKDNIGQTVEIYGWVNRRRDHGGVIFLDMRDKHGIAQVVINPDNADFSLAETVRNEFVLKITGTIIARGEGLTNPKLSTGKIEIKAQNIEILNTSKPVPFQIDATDTSEEVRLRYRYLDLRSDTMQNRLRLRSRVTRYMREFMDEHDFLDIETPFLTKATPEGARDYLVPSRTHSGKFFALPQSPQLFKQLLMMSGFERYYQIVKCFRDEDLRADRQPEFTQLDVETSFMSENEIMTMMEKMTRGLFKLVINVDLGDNFPTITYADSMAKYGLDRPDMRISMQIVSIDKIMQGVDFKVFSGPANYDDSRVAALKVPNGASISRKNIDKYTKYVSIYGAKGLAYIKLNKNGPASPILKFLGDEVIAKVIEMTDAKTGDIIFFGADKSKIVNEALGNLREQLAKDLDLFDTQWAPIWVVDFPMFEVGDDGSLNTTHHPFTAPSVDAKTLEKTATTALSKAYDLVINGSEVGGGSIRIHQIDMQKTVLKLLGISDQEIQDKFGFFLNALEYGCPPHGGMAFGLDRLMMIMTGANSIRDVVAFPKTQTAACLLTDTPTSISRKLLRELSVKINLPEKD

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus suis (strain 98HAH33)
Length
583 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.696 kDa
Sequence
MKRSMYAGRVRKEHVGQEITLKGWVGRRRGLGGLIFIDLRDREGIMQLVINPESVEAEVMAKAESLRSEFVIEVTGTVVEREQANDNIPTGAVELQVTSLTVLNTAKTTPFEIKDGIEASDDTRLRYRYLDLRRPEMLNNFKLRAAVTHSIRNYLDDLEFIDVETPMLTKSTPEGARDYLVPSRVSKGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLNEVEIQDIVEGLIAKVLKDTKGIDVTLPFPRMAYDHAMNFYGSDKPDTRFEMLLQDLTELVKEVDFKVFSEAPVVKAIVVKGAADSYSRKDIDKLTDYAKQFGAKGLAWVKVDKGELAGPVAKFLTGITEKLTASLQLEDKDLVLFVADELEVANNTLGALRNRLAKEQGLIDESKFNFLWIVDWPMFEWSEEEGRYMSAHHPFTLPTEETAHHLDGDLAQVRAVAYDIVLNGYELGGGSLRINQKDMQEQMFKALGFSAEDAHEQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGEDNIREVIAFPKNNKASDPMTQAPSTVASAQLEELALDITLENE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus suis (strain 05ZYH33)
Length
583 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.696 kDa
Sequence
MKRSMYAGRVRKEHVGQEITLKGWVGRRRGLGGLIFIDLRDREGIMQLVINPESVEAEVMAKAESLRSEFVIEVTGTVVEREQANDNIPTGAVELQVTSLTVLNTAKTTPFEIKDGIEASDDTRLRYRYLDLRRPEMLNNFKLRAAVTHSIRNYLDDLEFIDVETPMLTKSTPEGARDYLVPSRVSKGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLNEVEIQDIVEGLIAKVLKDTKGIDVTLPFPRMAYDHAMNFYGSDKPDTRFEMLLQDLTELVKEVDFKVFSEAPVVKAIVVKGAADSYSRKDIDKLTDYAKQFGAKGLAWVKVDKGELAGPVAKFLTGITEKLTASLQLEDKDLVLFVADELEVANNTLGALRNRLAKEQGLIDESKFNFLWIVDWPMFEWSEEEGRYMSAHHPFTLPTEETAHHLDGDLAQVRAVAYDIVLNGYELGGGSLRINQKDMQEQMFKALGFSAEDAHEQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGEDNIREVIAFPKNNKASDPMTQAPSTVASAQLEELALDITLENE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus thermophilus (strain CNRZ 1066)
Length
583 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.952 kDa
Sequence
MERSMYAGRVRSEHIGTTITLKGWVSRRRNLGGLIFIDLRDREGLMQLVVNPENADAAVVETAESLRSEFVIEVTGTVEAREQANDNLPTGAVELKVEDLKVLNTAKTTPFEIKDGVEASDDTRMRYRYLDLRRPEMLENFKLRAKVTHTIRNYLDDLEFIDVETPMLTKSTPEGARDYLVPSRVSQGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLNEQEIQDITEGLIAKVMKETKGVEVTLPFPRMSYDDAMNNYGSDKPDTRFDMLLQDLTELVKDIDFKVFAEAPAVKAIVVKGNADKYSRKSIDKLTDFAKQFGAKGLAWVKMTDGVLAGPVAKFLTSIEEKLTDTLQIEENDLVLFVADTLEIANNTLGALRNQIAKELDMIDNTKFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPTEDSAAELEGDLSKVRAVAYDIVLNGYELGGGSLRINQKDLQERMLKALGFSEESAYEQFGFLLEAMDYGFPPHGGLALGLDRFVMLLAGKDNIREVIAFPKNNKASDPMTQAPSLVADKQLEELALHVELENE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311)
Length
583 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.937 kDa
Sequence
MERSMYAGRVRSEHIGTTITLKGWVSRRRNLGGLIFIDLRDREGLMQLVVNPENADAAVVETAESLRSEFVIEVTGTVEAREQANDNLPTGAVELKVKDLKVLNTAKTTPFEIKDGVEASDDTRMRYRYLDLRRPEMLENFKLRAKVTHTIRNYLDDLEFIDVETPMLTKSTPEGARDYLVPSRVSQGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLNEQEIQDITEGLIAKVMKETKGVEVTLPFPRMSYDDAMNNYGSDKPDTRFDMLLQDLTELVKDVDFKVFAEAPAVKAIVVKGNADKYSRKSIDKLTDFAKQFGAKGLAWVKMTDGVLAGPVAKFLTSIEEKLTDTLQIEENDLVLFVADTLEIANNTLGALRNQIAKELDMIDNTKFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPTEDSAAELEGDLSKVRAVAYDIVLNGYELGGGSLRINQKDLQERMLKALGFSEESAYEQFGFLLEAMDYGFPPHGGLALGLDRFVMLLAGKDNIREVIAFPKNNKASDPMTQAPSLVADKQLEELALHVELENE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus thermophilus (strain ATCC BAA-491 / LMD-9)
Length
583 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.938 kDa
Sequence
MERSMYAGRVRSEHIGTTITLKGWVSRRRNLGGLIFIDLRDREGLMQLVVNPENTDAAVVETAESLRSEFVIEVTGTVEAREQANDNLPTGAVELKVEDLKVLNTAKTTPFEIKDGVEASDDTRMRYRYLDLRRPEMLENFKLRAKVTHTIRNYLDDLEFIDVETPMLTKSTPEGARDYLVPSRVSQGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLNEQEIQDITEGLIAKVMKETKGVEVTLPFPRMSYDDAMNNYGSDKPDTRFDMLLQDLTELVKDVDFKVFAEAPAVKAIVVKGNADKYSRKSIDKLTDFAKQFGAKGLAWVKMTDGVLAGPVAKFLTSIEEKLTDALQIEENDLVLFVADTLEIANNTLGALRNQIAKELDMIDNTKFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPTEDSAAELEGDLSKVRAVAYDIVLNGYELGGGSLRINQKDLQERMLKALGFSEESAYEQFGFLLEAMDYGFPPHGGLALGLDRFVMLLAGKDNIREVIAFPKNNKASDPMTQAPSLVADKQLEELALHVELENE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Amoebophilus asiaticus (strain 5a2)
Length
582 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.419 kDa
Sequence
MLRTHTCGELRLQHIGISVTLCGWVQKIRNKGSLVWIDLRDRYGITQLILEEHITAPEILSQVQHIGREYVIQATGSVIERSAKNPSMPTGDIEIEVKSLTILNTAKTPPFLIEEQTDGGEELRMQYRYLDLRRPPLQKNLLLRQLVAQHARAYLEQHHFVDVETPLLIKSTPGGARDFVVPSRIHPQQFYALPQSPQIFKQLLMVAGLDRYYQIAKCFRDEDFRADRQPEFTQIDCELSFVTQADILHIFENFTKYIFEATIQVRLDKFPCITYAEAMQKYGTDKPDIRFGMRLIELTELVKNSEFPLFKQAKLIAGICVKGCADYTRKQLDDLTEYIKKLNLVTSGLVYVKYLADGSFNSPVSKFYDVEQLTLWAKQMHAVPGDLLLILAGEIEATQIALGSLRLKLRDELHLVSKDKFAPLWVVDFPLLEWNEESQRYVSRHHPFTSPKQEDIELLSTKPETVRANAYDLVINGMEIGGGSIRIHDRALQEQIFNVLGFSEEEARQQFGFLTDAFEYGAPPHGGIAFGFDRLCAIIGREDSIRPFIAFPKNNAGRDVMMKAPSTITEQQISELGIILSK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus equi subsp. equi (strain 4047)
Length
582 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.131 kDa
Sequence
MKRSMYAGHVRKEHIGRTIVLKGWVSRRRDLGGLIFIDLRDREGVMQLVINPEDVSGDVMATAERLRSEYVIEVEGSVEARQQANDKLATGAVELKVSGLTILNTAKTTPFEIKDGVEVSDDTRLRYRYLDLRRPEMLESFKLRAKTTHVIRNYLDNLGFIDVETPMLTKSTPEGARDYLVPSRISQGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLSEQEIQDIVEGMIAKVMKDTKGIEVKLPFPRMAYDDAMNHYGSDKPDTRFDMLLQDLTDLVKEIDFKVFSEAQAVKAIVVKGHADRYSRKDIDKLTEFAKQFGAKGLAWLKVVDGAFTGPIAKFLTGVKSKLTESLQLEHNDLVLFVADTLEVANNTLGALRTRIAKELDMIDMSQFNFLWVVDWPMFEWSEEEERYMSAHHPFTLPTAESAHELEGDLAKVRAVAYDIVLNGYELGGGSLRINQKDMQERMFRALGFTAEEANEQFGFLLEAMEYGFPPHGGLAIGLDRLVMLLAGKDNIREVIAFPKNNKASDPMTQAPSLVSEKQLEELQLQIEHHD

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus equi subsp. zooepidemicus (strain MGCS10565)
Length
582 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.206 kDa
Sequence
MKRSMYAGHVREEHIGRTIVLKGWVSRRRDLGGLIFIDLRDREGVMQLVINPEDVSGDVMATAERLRSEYVIEVEGSVEARQQANDKLATGAVELKVSGLTILNTAKTTPFEIKDGVEVSDDMRLRYRYLDLRRPEMLESFKLRAKTTHVIRNYLDNLGFIDVETPMLTKSTPEGARDYLVPSRISQGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLSEQEIQDIVEGMIAKVMKDTKGIEVKLPFPRMAYDDAMNHYGSDKPDTRFDMLLQDLTDLVKEVDFKVFSEAQAVKAIVVKGHADDYSRKDIDKLTEFAKQFGAKGLAWLKVVDGAFTGPIAKFLTGVESKLTESLQLEHNDLVLFVADTLEVANNTLGTLRTRIAKELDMIDMSQFHFLWVVDWPMFEWSEEEERYMSAHHPFTLPTQESAHELEGDLAKVRAVAYDIVLNGYELGGGSLRINQKDMQERMFKALGFTKEEASDQFGFLLEAMEYGFPPHGGLAIGLDRLVMLLAGKDNIREVIAFPKNNKASDPMTQAPSLVSEKQLEELQLQIEHHD

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus pyogenes serotype M1
Length
582 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.028 kDa
Sequence
MKRSMYAGRVREEHIGTTITLKGWVSRRRDLGGLIFIDLRDREGVMQLVINPEEVSSDVMATAERLRSEYVIEVEGFVEARQQANDKLATGMVELKVSALTILNTAKTTPFEIKDDVEVSDDTRLRYRYLDLRRPEMLENFKLRAKVTHSIRNYLDDLEFIDVETPMLTKSTPEGARDYLVPSRVSQGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLSEQEIQDIVEGMIAKVMKETKEIDVTLPFPRMSYDVAMNSYGSDKPDTRFEMLLQDLTVTVKGNDFKVFSEAPAVKAIVVKGNADRYSRKDIDKLTEFAKQFGAKGLAWVKVTDGQLAGPVAKFLTAIETELSSQLKLAENDLVLFVADTLEVANNTLGALRNRIAKDLDMIDQSQFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPTPESAHELEGDLAKVRAIAYDIVLNGYELGGGSLRINQKEMQERMFKALGFTADEANDQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGKDNIREVIAFPKNNKASDPMTQAPSLVSENQLEELSLQIESHD

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus pyogenes serotype M3 (strain ATCC BAA-595 / MGAS315)
Length
582 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.993 kDa
Sequence
MKRSMYAGRVREEHIGTTITLKGWVSRRRDLGGLIFIDLRDREGVMQLVINPEEVSSDVMATAERLRSEYVIEVEGFVEARQQANDKLATGMVELKVSALTILNTAKTTPFEIKDDVEVSDDTRLRYRYLDLRRPEMLENFKLRAKVTHSIRNYLDDLEFIDVETPMLTKSTPEGARDYLVPSRVSQGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLSEQEIQDIVEGMIAKVMKETKEIDVTLPLPRMSYDVAMNSYGSDKPDTRFEMLLQDLTVTVKGIDFKVFSEAPAVKAIVVKGNADRYSRKDIDKLTEFAKQFGAKGLAWVKVTDGQLAGPVAKFLTAIETELSSQLKLAENDLVLFVADTLEVANNTLGALRNRIAKDLDMIDQSQFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPTPESAHELEGDLAKVRAIAYDIVLNGYELGGGSLRINQKEMQERMFKALGFTADEANDQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGKDNIREVIAFPKNNKASDPMTQAPSLVSENQLEELSLQIESHD

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394)
Length
582 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.128 kDa
Sequence
MKRSMYAGRVREEHIGTTITLKGWVSRRRDLGGLIFIDLRDREGVMQLVINPEEVSSDVMATAERLRSEYVIEVEGFVEARQQANDKLATGMVELKVSALTILNTAKTTPFEIKDDVEVSDDTRLRYRYLDLRRPEMLENFKLRAKVTHSIRNYLDDLEFIDVETPMLTKSTPEGARDYLVPSRVSQGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLSEQEIQDIVEGMIAKVMKETKEIDVTLPFPRMSYDVAMNSYGSDKPDTRFEMLLQDLTVTVKGIDFKVFSEAPAVKAIVVKGNADRYSRKDIDKLTEFAKQFGAKGLAWVKVTDGQLAGPVAKFLTAIETELSSQLKLAENDLVLFVADTLEVANNTLGALRNRIARDLDMIDQSQFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPTPESAHELEGDLAKVRAIAYDIVLNGYELGGGSLRINQKEMQERMFKALGFTADEANDQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAEEDNIREVIAFPKNNKASDPMTQAPSLVSENQLEELSLQIESHD

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus pyogenes serotype M18 (strain MGAS8232)
Length
582 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.027 kDa
Sequence
MKRSMYAGRVREEHIGTTITLKGWVSRRRDLGGLIFIDLRDREGVMQLVINPEEVSSDVMATAERLRSEYVIEVEGFVEARQQANDKLATGMVELKVSALTILNTAKTTPFEIKDDVEVSDDTRLRYRYLDLRRPEMLENFKLRAKVTHSIRNYLDDLEFIDVETPMLTKSTPEGARDYLVPSRVSQGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLSEQEIQDIVEGMIAKVMKETKEIDVTLPFPRMSYDVAMNSYGSDKPDTRFEMLLQDLTVTVKGIDFKVFSEAPAVKAIVVKGNADRYSRKDIDKLTEFAKQFGAKGLAWVKVTDGQLAGPVAKFLTAIETELSSQLKLAENDLVLFVADTLEVANNTLGALRNRIAKDLDMIDQSQFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPTPESAHELEGDLAKVRAIAYDIVLNGYELGGGSLRINQKEMQERMFKALGFTADEANDQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGKDNIREVIAFPKNNKASDPMTQAPSLVSENQLEELSLQIESHD

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus pyogenes serotype M5 (strain Manfredo)
Length
582 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.121 kDa
Sequence
MKRSMYAGRVREEHIGTTITLKGWVSRRRDLGGLIFIDLRDREGVMQLVINPEEVSSDVMATAERLRSEYVIEVEGFVEARQQANDKLATGMVELKVSALTILNTAKTTPFEIKDDAEVSDDTRLRYRYLDLRRPEMLENFKLRAKVTHSIRNYLDDLEFIDVETPMLTKSTPEGARDYLVPSRVSQGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLSEQEIQDIVEGMIAKVMKETKEIDVTLPFPRMSYDVAMNSYGSDKPDTRFEMLLQDLTVTVKGIDFKVFSEAPAVKAIVVKGNADRYSRKDIDKLTEFAKQFGAKGLAWVKVTDGQFSGPVAKFLTAIETELSSQLKLAENDLVLFVADTLEVANNTLGALRNRIAKDLDMIDQSQFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPTPESAHELEGDLAKVRAIAYDIVLNGYELGGGSLRINQKEMQERMFKALGFTADEANDQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAEKDNIREVIAFPKNNKASDPMTQAPSLVSENQLEELSLQIESHD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chlamydia muridarum (strain MoPn / Nigg)
Length
582 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.386 kDa
Sequence
MKYRTHKCNELSLNHVGEHVRLSGWVHRYRNHGGVVFIDLRDRFGITQIVCRQEENPELHRLMDQVRSEWVLCVEGLVCARLGGMENPNLVTGSIEVEVSHLEVLSRAQNLPFSISDEHINVNEELRLTYRYLDMRRGDIVDRLMCRHKVMLACRQYLDEQGFTEVVTPVLGKSTPEGARDYLVPSRIYPGNFYALPQSPQLFKQILMVGGLDRYFQIATCFRDEDLRADRQPEFSQIDMEMSFGGPEDLFPIVEELVTRLFAVKGIELSIPFQRMTYQEAKEFYGTDKPDLRFGLRLKNCCEYAKKFSFSIFLDQLAQGGTVKGFCVPGGADISRKQLDVYTDFVKRYGAMGLVWIKNQDGGISSNVAKFASEEVFHEMFEAFEAKDQDILLLIAAPEAIANQSLDHLRRLIAKERQLYDAEQYNFVWITDFPLFAKEEGELCSEHHPFTAPLEEDIPLLDKDPLSVRSSSYDLVLNGYEIASGSQRIHNPDLQNKIFSLLRLSQESVKEKFGFFIDALSFGTPPHLGIALGLDRIMMVLTGAETIREVIAFPKTQKAGDLMMSAPSEILPIQLKELGLKL

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chlamydia trachomatis serovar L2 (strain 434/Bu / ATCC VR-902B)
Length
582 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.272 kDa
Sequence
MKYRTHKCNELSLDHVGEHVRLSGWVHRYRNHGGVVFIDLRDRFGITQIVCRQEENPELHQLMDQVRSEWVLCVEGLVCARLEGMENPNLVTGSIEVEVSSLEVLSRAQNLPFSISDEHINVNEELRLTYRYLDMRRGDILDRLMCRHKVMLACRQYLDEQGFTEVVTPILGKSTPEGARDYLVPSRIYPGNFYALPQSPQLFKQILMVGGLDRYFQIATCFRDEDLRADRQPEFTQIDMEMSFGGPEDLFPVVEELVTRLFAVKGIELKAPFLRMTYQEAKDSYGTDKPDLRFGLRLKNCCEYARKFTFSIFLDQLAHGGTVKGFCVPGGADMSRKQLDIYTDFVKRYGSMGLVWIKKQDGGVSSNVAKFASEDVFQEMFEAFEAKDQDILLLIAAPEAVANQALDHLRRLIAKERQLYDSTQYNFVWITDFPLFAKEEGELCPEHHPFTAPLDEDISLLDSDPFAVRSSSYDLVLNGYEIASGSQRIHNPDLQNKIFALLKLSQESVKEKFGFFIDALSFGTPPHLGIALGLDRIMMVLTGAETIREVIAFPKTQKAGDLMMSAPSEILPIQLKELGLKL

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13)
Length
582 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.227 kDa
Sequence
MKYRTHKCNELSLDHVGEHVRLSGWVHRYRNHGGVVFIDLRDCFGITQIVCRQEENPELHQLMDQVRSEWVLCVEGLVCARLEGMENPNLVTGSIEVEVSSLEVLSRAQNLPFSISDEHINVNEELRLTYRYLDMRRGDILDRLMCRHKVMLACRQYLDEQGFTEVVTPILGKSTPEGARDYLVPSRIYPGNFYALPQSPQLFKQILMVGGLDRYFQIATCFRDEDLRADRQPEFTQIDMEMSFGGPEDLFPVVEELVARLFAVKGIELKAPFLRMTYQEAKDSYGTDKPDLRFGLRLKNCCEYARKFTFSIFLDQLAYGGTVKGFCVPGGADMSRKQLDIYTDFVKRYGAMGLVWIKKQDGGVSSNVAKFASEDVFQEMFEAFEAKDQDILLLIAAPEAVANQALDHLRRLIARERQLYDSTQYNFVWITDFPLFAKEEGELCPEHHPFTAPLDEDISLLDSDPFAVRSSSYDLVLNGYEIASGSQRIHNPDLQNKIFALLKLSQESVKEKFGFFIDALSFGTPPHLGIALGLDRIMMVLTGAETIREVIAFPKTQKAGDLMMSAPSEILPIQLKELGLKL

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chlamydia trachomatis serovar L2b (strain UCH-1/proctitis)
Length
582 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.272 kDa
Sequence
MKYRTHKCNELSLDHVGEHVRLSGWVHRYRNHGGVVFIDLRDRFGITQIVCRQEENPELHQLMDQVRSEWVLCVEGLVCARLEGMENPNLVTGSIEVEVSSLEVLSRAQNLPFSISDEHINVNEELRLTYRYLDMRRGDILDRLMCRHKVMLACRQYLDEQGFTEVVTPILGKSTPEGARDYLVPSRIYPGNFYALPQSPQLFKQILMVGGLDRYFQIATCFRDEDLRADRQPEFTQIDMEMSFGGPEDLFPVVEELVTRLFAVKGIELKAPFLRMTYQEAKDSYGTDKPDLRFGLRLKNCCEYARKFTFSIFLDQLAHGGTVKGFCVPGGADMSRKQLDIYTDFVKRYGSMGLVWIKKQDGGVSSNVAKFASEDVFQEMFEAFEAKDQDILLLIAAPEAVANQALDHLRRLIAKERQLYDSTQYNFVWITDFPLFAKEEGELCPEHHPFTAPLDEDISLLDSDPFAVRSSSYDLVLNGYEIASGSQRIHNPDLQNKIFALLKLSQESVKEKFGFFIDALSFGTPPHLGIALGLDRIMMVLTGAETIREVIAFPKTQKAGDLMMSAPSEILPIQLKELGLKL

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Chlamydia trachomatis (strain D/UW-3/Cx)
Length
582 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.227 kDa
Sequence
MKYRTHKCNELSLDHVGEHVRLSGWVHRYRNHGGVVFIDLRDCFGITQIVCRQEENPELHQLMDQVRSEWVLCVEGLVCARLEGMENPNLVTGSIEVEVSSLEVLSRAQNLPFSISDEHINVNEELRLTYRYLDMRRGDILDRLMCRHKVMLACRQYLDEQGFTEVVTPILGKSTPEGARDYLVPSRIYPGNFYALPQSPQLFKQILMVGGLDRYFQIATCFRDEDLRADRQPEFTQIDMEMSFGGPEDLFPVVEELVARLFAVKGIELKAPFLRMTYQEAKDSYGTDKPDLRFGLRLKNCCEYARKFTFSIFLDQLAYGGTVKGFCVPGGADMSRKQLDIYTDFVKRYGAMGLVWIKKQDGGVSSNVAKFASEDVFQEMFEAFEAKDQDILLLIAAPEAVANQALDHLRRLIARERQLYDSTQYNFVWITDFPLFAKEEGELCPEHHPFTAPLDEDISLLDSDPFAVRSSSYDLVLNGYEIASGSQRIHNPDLQNKIFALLKLSQESVKEKFGFFIDALSFGTPPHLGIALGLDRIMMVLTGAETIREVIAFPKTQKAGDLMMSAPSEILPIQLKELGLKL

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus pyogenes serotype M28 (strain MGAS6180)
Length
582 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.967 kDa
Sequence
MKRSMYAGRVREEHIGTTITLKGWVSRRRDLGGLIFIDLRDREGVMQLVINPEEVSSDVMATAERLRSEYVIEVEGFVEARQQANDKLATGMVELKVSALTILNTAKTTPFEIKDDVEVSDDTRLRYRYLDLRRPEMLENFKLRAKVTHSIRNYLDDLEFIDVETPMLTKSTPEGARDYLVPSRVSQGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLSEQEIQDIVEGMIAKVMKETKEIDVTLPFPRMSYDVAMNSYGSDKPDTRFEMLLQDLTVTVNGIDFKVFSEAPAVKAIVVKGNADRYSRKDIDKLTEFAKQFGAKGLAWVKVTDGQLAGPVAKFLIAIETELSSQLKLAENDLVLFVADTLEVANNTLGALRNRIAKDLDMIDQSQFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPTPESAHELEGDLAKVRAIAYDIVLNGYELGGGSLRINQKEMQERMFKALGFTADEANDQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGKGNIREVIAFPKNNKASDPMTQAPSLVSENQLEELSLQIESHD

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus pyogenes serotype M3 (strain SSI-1)
Length
582 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.993 kDa
Sequence
MKRSMYAGRVREEHIGTTITLKGWVSRRRDLGGLIFIDLRDREGVMQLVINPEEVSSDVMATAERLRSEYVIEVEGFVEARQQANDKLATGMVELKVSALTILNTAKTTPFEIKDDVEVSDDTRLRYRYLDLRRPEMLENFKLRAKVTHSIRNYLDDLEFIDVETPMLTKSTPEGARDYLVPSRVSQGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLSEQEIQDIVEGMIAKVMKETKEIDVTLPLPRMSYDVAMNSYGSDKPDTRFEMLLQDLTVTVKGIDFKVFSEAPAVKAIVVKGNADRYSRKDIDKLTEFAKQFGAKGLAWVKVTDGQLAGPVAKFLTAIETELSSQLKLAENDLVLFVADTLEVANNTLGALRNRIAKDLDMIDQSQFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPTPESAHELEGDLAKVRAIAYDIVLNGYELGGGSLRINQKEMQERMFKALGFTADEANDQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGKDNIREVIAFPKNNKASDPMTQAPSLVSENQLEELSLQIESHD

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus pyogenes serotype M49 (strain NZ131)
Length
582 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.027 kDa
Sequence
MKRSMYAGRVREEHIGTTITLKGWVSRRRDLGGLIFIDLRDREGVMQLVINPEEVSSDVMATAERLRSEYVIEVEGFVEARQQANDKLATGMVELKVSALTILNTAKTTPFEIKDDVEVSDDTRLRYRYLDLRRPEMLENFKLRAKVTHSIRNYLDDLEFIDVETPMLTKSTPEGARDYLVPSRVSQGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLSEQEIQDIVEGMIAKVMKETKEIDVTLPFPRMSYDVAMNSYGSDKPDTRFEMLLQDLTVTVKGIDFKVFSEAPAVKAIVVKGNADRYSRKDIDKLTEFAKQFGAKGLAWVKVTDGQLAGPVAKFLTAIETELSSQLKLAENDLVLFVADTLEVANNTLGALRNRIAKDLDMIDQSQFNFLWVVDWPMFEWSEEEGRYMSAHHPFTLPTPESAHELEGDLAKVRAIAYDIVLNGYELGGGSLRINQKEMQERMFKALGFTADEANDQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGKDNIREVIAFPKNNKASDPMTQAPSLVSENQLEELSLQIESHD

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus equi subsp. zooepidemicus (strain H70)
Length
582 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.137 kDa
Sequence
MKRSMYAGHVRKEHIGRTIVLKGWVSRRRDLGGLIFIDLRDREGVMQLVINPEDVSGDVMATAERLRSEYVIEVEGSVEARQQANDKLATGAVELKVSGLTILNTAKTTPFEIKDGVEVSDDTRLRYRYLDLRRPEMLESFKLRAKTTHVIRNYLDNLGFIDVETPMLTKSTPEGARDYLVPSRISQGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLSEQEIQDIVEGMIAKVMKDTKGIEVKLPFPRMAYDDAMNHYGSDKPDTRFDMFLQDLTDLVKEIDFKVFSEAQAVKAIVVKGHADRYSRKDIDKLTEFAKQFGAKGLAWLKVADGAFTGPIAKFLTGVESKLTESLQLEHNDLVLFVADTLEVANNTLGALRTRIAKELDMIDMSQFNFLWVVDWPMFEWSEEEERYMSAHHPFTLPTAESAHELEGDLAKVRAVAYDIVLNGYELGGGSLRINQKDMQERMFRALGFTAEEANEQFGFLLEAMEYGFPPHGGLAIGLDRLVMLLAGKDNIREVIAFPKNNKASDPMTQAPSLVSEKQLEELQLQIEHHD

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Streptococcus uberis (strain ATCC BAA-854 / 0140J)
Length
582 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.146 kDa
Sequence
MKRSMYAGHVRSEHIGQELTLKGWVGRRRDLGGLIFIDLRDREGIMQLVINPEDVAKDVMEIAESLRSEYVIEVTGIVEERQQANNQIATGAVELKVEQITVLNTSKTTPFEIKDGVEVSDETRLRYRYLDLRRPEMLENFKLRAKVTHSIRNYLDDLNFIDVETPMLTKSTPEGARDYLVPSRISEGHFYALPQSPQITKQLLMNAGFDRYYQIVKCFRDEDLRGDRQPEFTQVDLETSFLSEQEIQDIVEGMIAKVMKETKGIDVSLPFPRMSYDLAMNQYGSDKPDTRFDMLLQDVSELVKGIDFKVFSQAPVVKAIVVKGNADRYSRKDIDKMTEFAKQFGAKGLAWIKVDDGKLTGPVSKFLTEIESLLTDALQLVDNDLVLFVADELDIANATLGALRNRIAKELQLIDESAFNFLWVIDWPMFEWSEEEGRYMSAHHPFTLPTEASAHELEGDLANVRAIAYDIVLNGYELGGGSLRINQRDLQERMFKALGFTEEEAKEQFGFLLEAMDYGFPPHGGLAIGLDRFVMLLAGKDNIREVIAFPKNNKASDPMTQAPSLVSEKQLEELSLQIESHD

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Helicobacter hepaticus (strain ATCC 51449 / 3B1)
Length
581 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.326 kDa
Sequence
MLRTHLCAELGEEHIGTEVQVCGWCNTYRDHGGVVFIDLRDKSGIVQLVCDPSTQAHAIASSVRDEYVLVAKGKVRARGAGLENPKLKTGMIEIVLNSLIIENKSPTPPIAIGDESVNEELRLKYRYLDLRSPKAYNIFKIRSDAAIATRNSLQKMGFLEVETPILTKATPEGARDYLVPSRVHQGEFYALPQSPQLFKQLLMMSGFDKYFQIAKCFRDEDLRADRQPEFTQIDIEMSFCEQEDIISVAENLLKDIFSACGTEIEIPFMRLPYAQAMESYGSDKPDLRFCMPLVEVGDLFVDSSNAIFKNIAQDSKNNRIKALCVKGGDTFFSRKTLGEAEDFVRKFGAKGLAYIQIKENELKGPLVKFISESALNELVSRVKAEVGDIIFFGAGAKKIVWDYMGRLRLKVAEDMKLINENEYKFLWVVDFPMFEKDEGKTKALHHPFTMPNDLDKEDIEEITSVAYDVVLNGIELGGGSIRIHKDSIQKRVFELLGISTQEAEDKFGFLLEALSFGAPPHGGIAIGFDRLIMLLSKSQSIRDVIAFPKTQRATCPLTLAPSKVNDEQLKELHIRVKNELK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Thermosipho melanesiensis (strain DSM 12029 / CIP 104789 / BI429)
Length
581 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.257 kDa
Sequence
MYRTHNCGELRKKDVEKEVILSGWVDRIRDLGGIKFIILRDRYGKTQLVVNPNSPAYEISQELGREWVIQVYGKVLERPDETKTEMVTGEIEVEVNKIKVLSKSDVPPFYPGENVSEDLRLKYRYIDLRDERMQKNLIIRHKMAQAAREFLNKHDFLEVETPYLTKSTPEGARDFLVPSRLQKGKFYALPQSPQLFKQILMVSGFDRYYQFARCFRDEDLRADRQPEFTQIDIEMSFVKMDEILDLMESFARFVFGKVGIKLPEKFDRLSYEEAMELYGSDKPDRRYGMQLQDFTNYFVNTEFKVIKNVLERSGSVKGFITTIPISRKIASQFEEFVKQYGLGGLLWFKLDDEIVSPTAKFLKESYKKIVKEYNLDKGSVVLLAAHENREILNTALGALRLKVGKEYFNELEKVFDALWIVDFPFLEWNEEESRFEARHHPFTMPKNLEQKLEDIKAYAYDMILNGMEIGGGSIRIHDSEVQKRVFEIIGLTEEEANEKFGFFISALKYGVPPHGGIAFGFDRMVSIAANVASIRDVIAFPKTSSGICQLTGAPSTVEEKQLKELSIQIFKGGIENERNES

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Thermosipho africanus (strain TCF52B)
Length
581 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.506 kDa
Sequence
MYRTHTCGELNIKDVGKKVVLSGWVDRIRDLGGIKFIILRDRYGVTQVVVNPESPAYEISQKIGREWVIQIEGTVSERPESTKTETQTGEIEVIVEKINVLSKAELPPFYPGDKVSEDLRLKYRYLDLRDKNMNKNLIIRHKMAQAAREFLNKHGFLEIETPYLTKSTPEGARDFLVPSRLQKGKFYALPQSPQLFKQLLMVSGFDKYYQFARCFRDEDLRADRQPEFTQIDIEMSFVEMEDVINLMENFVRYVYSSVGIKLPEKFDRITYDEAMEIYGSDKPDRRFGMELKDLTNYFKDTDFKIIKNVINNGGSIKGFITQIPISRKIASELESYVKEFGLGGLLWFKLENGEISSPTNKFLGGSYENISKDYNLKDGDVVLLAAHTNREQLNTALGALRLRIAKEHFKNLEEGFDALWVVDFPFLEWNEEEKRYVARHHPFTMPKNIDSKPEDIKAYAYDMILNGNEIGGGSIRIHNSEIQRKVFEIIGLTNKEAEEKFGFLLEALKYGAPPHGGIAFGFDRMVSIALRTSSIRDVIAFPKTTSGTCQLTGAPSSVDKSQLEELSIKLFDIKEGGDENE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039)
Length
580 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.03 kDa
Sequence
MRRTHYAGSLRETHVGEEVVLEGWVNRRRDLGGLIFLDLRDREGLVQLVAHPASPAYATAERVRPEWVVRAKGLVRLRPEPNPRLATGRVEVELSALEVLAEAKTPPFPVDAGWRGEEEKEASEELRLKYRYLDLRRRRMQENLRLRHRVIKAIWDFLDREGFVQVETPFLTKSTPEGARDFLVPYRHEPGLFYALPQSPQLFKQMLMVAGLDRYFQIARCFRDEDLRADRQPDFTQLDLEMSFVEVEDVLELNERLMAHVFREALGVELPLPFPRLSYEEAMERYGSDKPDLRFGLELKEVGPLFRQSGFRVFQEAESVKALALPKALSRKEVAELEEVAKRHKAQGLAWARVEEGGFSGGVAKFLEPVREALLQATEARPGDTLLFVAGPRKVAATALGAVRLRAADLLGLKREGFRFLWVVDFPLLEWDEEEEAWTYMHHPFTSPHPEDLPLLEKDPGRVRALAYDLVLNGVEVGGGSIRIHDPRLQARVFRLLGIGEEEQREKFGFFLEALEYGAPPHGGIAWGLDRLLALMTGSPSIREVIAFPKNKEGKDPLTGAPSPVPEEQLRELGLMVVRP

Gene
aspS
Protein
Aspartate--tRNA(Asp) ligase
Organism
Thermus thermophilus
Length
580 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.03 kDa
Sequence
MRRTHYAGSLRETHVGEEVVLEGWVNRRRDLGGLIFLDLRDREGLVQLVAHPASPAYATAERVRPEWVVRAKGLVRLRPEPNPRLATGRVEVELSALEVLAEAKTPPFPVDAGWRGEEEKEASEELRLKYRYLDLRRRRMQENLRLRHRVIKAIWDFLDREGFVQVETPFLTKSTPEGARDFLVPYRHEPGLFYALPQSPQLFKQMLMVAGLDRYFQIARCFRDEDLRADRQPDFTQLDLEMSFVEVEDVLELNERLMAHVFREALGVELPLPFPRLSYEEAMERYGSDKPDLRFGLELKEVGPLFRQSGFRVFQEAESVKALALPKALSRKEVAELEEVAKRHKAQGLAWARVEEGGFSGGVAKFLEPVREALLQATEARPGDTLLFVAGPRKVAATALGAVRLRAADLLGLKREGFRFLWVVDFPLLEWDEEEEAWTYMHHPFTSPHPEDLPLLEKDPGRVRALAYDLVLNGVEVGGGSIRIHDPRLQARVFRLLGIGEEEQREKFGFFLEALEYGAPPHGGIAWGLDRLLALMTGSPSIREVIAFPKNKEGKDPLTGAPSPVPEEQLRELGLMVVRP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251)
Length
580 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.842 kDa
Sequence
MRSHYCTELSEANIGQEVVLAGWANSYRDHGGIIFIDLRDKSGLIQLTCDPEDSASSHKIASSIRDEFVLVAKGKVRLRGEGLTNPRLKTGAIEIVVSELTIENRSAAVPFVIGDKNVGEETRLKYRYLELRDPSMYETFRLRSKAAIAARNILDENGFLEVETPILTKSTPEGARDYLVPSRVHSGEFYALPQSPQLFKQLLMVGGFDRYFQIAKCFRDEDLRADRQPEFTQIDVEMSFCNQEDVMLIAEKLLVSMFGACGVEIKPPFNRIAYRDAMEWYGSDKPDLRYDLKMVDVIDIFERCDNEIFTNIAKQPHKNRIKALRVPGADLVFSKREMKTFEDFVRQFGAQGLGYFQMKEDGLKGPLIKFFSDADIALLVDRLGMKVGDVVFFGAGDKKTVWDYMGRLRIFIAEHERMNLADKDAFEFVWVVDFPMFEVEDGRVKALHHPFTQPKDTDKDDIEEIDSIAYDIVLNGTELGGGSIRIHKEEMQEEIFKLLGIGEEEAKEKFGFLLDALKFGAPPHGGFAIGFDRLMMLISKKSSIRDVIAFPKTQKASCILTKAPSEVDATQLRDLHIKLR

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Mycoplasma penetrans (strain HF-2)
Length
580 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.119 kDa
Sequence
MKTNNVVYCGNVDNKLVGKEVVIKGWIKKNRKLGSLIFIDIYDITGIVQVVVEEENKFFNNCLQTPKESVVEVIGIVRKRSNVNKELKTGEFEIDLKEFKLYSKAETPPFLIQDDTDGLEDLRLKYRYLDLRRPVMQNNIINRGKIINLFRSFLVKNNFNEIETPYLSKQTPEGARDYLVPTRSKKFFALPQSPQIYKQLLMVSGMDRYFQIARCFRDEDLRADRQPEFTQIDIETSFLSDLEIQSIVQEMFIYVFKEFFNIKLKTPFTRMSYSDAIEYYGSDKPDIRFENKIMNLTNYFKDTNFKIFKSIYESKNRISAVFVEDNIVKQDIKKLEKLAQDNKAKGLAYLYIENGKMSSGSIANVIESEIIEKICKDNKLSNGTLFFVADKYEITQQALGAIRKEFVNISKKIKMNEEFAFLWVVDWPLFEYSEEEKRYVSAHHPFTMPTAETLDTFDKDPANAKAIAYDLVLNGFEIGGGSLRIYNSELQTRMFKFLGLNDSQVKEKFGFIINAFKYGVPPHGGIAFGIERILMIMLNTNSIRDVIAFPKNSSGVDLLFETPSDVSNESLKELGIKLEK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Helicobacter pylori (strain J99 / ATCC 700824)
Length
579 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.617 kDa
Sequence
MRSHFCTEISEKDVGKTIKVAGWCNTYRDHGGVVFIDLRDKSGLVQLVCDPSSKAYEKALEVRSEFVLVAKGKARLRGAGLENPKLKTGKIEIVLEELVIENKSATPPIEIGNKSVNEDLRLKYRYLDLRSLNAYEIFKLRSEVALITRNALAQKGFLEIETPILSKTTPEGARDYLVPSRVHEGEFFALPQSPQLFKQLLMVGGMDRYFQIARCFRDEDLRADRQPEFTQIDAEMSFCDEDDVMGVVEDLLQEIFKAIGHTISKPFKRMPYKEAMENYGSDKPDLRFELPLIEVGDCFMDSSNSIFSNIAQDPKDKRIKALNVKGADAVFSRSVLKELEEFVRQFGAKGLAYLQIKEDGIKGPLVKFLSEKGLKNILERTDAQVGDIVFFGAGDKKIVLDYMGRLRLKVAETLDLIDKDALNFLWVVHFPMFEKTENGYHAAHHPFTMPKNIECEDIEEIEAHAYDVVLNGVELGGGSIRIHKEEMQKKVFEKININEEEAQKKFGFLLEALKFGAPPHGGFAIGFDRLIMLMTKSNSIRDVIAFPKTQKASCLLTDAPSPINEEQLRELHIRLRKPI

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Thermobifida fusca (strain YX)
Length
579 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.739 kDa
Sequence
MIRTHEAGTLRADHAEQNVVLAGWVARRRDHGGVVFLDLRDASGIVQVVVREDELAHDLRSEYCIKVTGTVRIRPEGNENPDIATGEIEVVASHIEVLSESAPLPFPLDGNQEISEEARLRYRYLDMRRPETAEALRVRSRATYIAHEVMNDNGFVYVETPYLTRSTPEGARDFLVPVRLQPGHWYALPQSPQLFKQLLMVGGMERYYQLTRCFRDEDFRADRQPEFTQIDIEMSFVDEEDLFDIGEKLFTRLLREVRGVELPRPFRRMKFAEAMDRFGTDKPDLRFGQELVELTDFFANTPFRVFQAPYVGAVVMPGGASQTRRELDAWQEWARSRGAKGLAYVLVHEDGTLGGPVAKNLSEEERAGLAERVGAKPGDAIFFSAGERTASQELLGAARLEIGKRCGLIDESAWEVLWITDMPMFEKDDEGGWTSVHHPFTAPAQEVADTFHNDPGSATARAFDLVMNGYELASGSIRIHRAEMQQRVFDTIGLSKDEAETKFGFLLEAFQFGPPPHGGLAVGWDRLVMLLAGQSTIRDVIAFPKTASGADPLTGAPTPITAEQRREAGVDAVPEQATS

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
Length
579 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.495 kDa
Sequence
MLRTHTCGELRATDEGKKVKLCGWVDRIRDLGGVRFIDLRDRYGETQIVCDVNSEAYSVVDELTRESVVLVEGTVRKRPEGTENPNIETGEIEVVAERIEILSLADPLPFYPGETPKEEMRLKYRYIDLRSERMKRNIILRYRISKIIRDYFDELGFLEIETPFLTRSTPEGARDFLVPSRLRPGKFYALPQSPQLFKQILMISGFDRYFQIVRCFRDEDLRADRQPEFTQVDVEMSFVDVEDVLNVSEGMVSRVFKESSGIDLKVPFDRIPYDDAMEKYGTDKPDRRYGMELRDFGYAFETTEFKVIRNVLNEGGSVKGFIVPGFASEMSRKKGEELMARMKELGLGGLIWFKLDGGITSPHLKHLEKEFRKIAETENMNEGDVCLIAAHTDRNLLNEALGTLRLEIGKEHFSHLAKGFDVLWVVDFPYFEWSEEEERFVARHHPFTMPVLETLGDDYTKVRAKAYDLVINGYEVGGGSIRIHRRDIQEKIFELLGLSEEEAQKKFGFFLEAFRYGVPPHGGIAFGLDRLVSIIAGESSIREVIAFPKTGNGVCLLTGAPAEVDERQLRELRIRIEEG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NS-E)
Length
579 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.885 kDa
Sequence
MLRTHTCGELRVEDEGKKVKLCGWVDRIRDLGGVRFIDLRDRYGETQIVCDVNSKAYETVDELTRESVVLVEGTVRRRPEGTENPNIATGEIEVVAERIEILSKAEPLPFYPNETPKEEMRLRYRYIDLRSKRMRDNIILRYNITRVIRRYFDELGFLEIETPFLTKSTPEGARDFLVPSRLRPGKFYALPQSPQLFKQLLMISGFDRYFQIVRCFRDEDLRADRQPEFTQVDVEMSFVDVEDVLSVSEGMIARVFREAIGMDLKTPFDRITYSEAMEKYGTDKPDRRYGMELRDLGYAFEGTTFRVIRSVLEEGGSVKGFVVPEFASEMTRKKGDELMERAKELGLGGLIWFKVEEKIVSPHLKHLEREFKTIVEKENLKEGDVCLIAAHKDRNLLNEALGTLRLEIGKEYFSHLAKGFDILWVVDFPYFEWSEEEERFVARHHPFTMPVEETLGDDHTKVKAKAYDIVINGYEVGGGSIRIHKREIQEKIFKLLGMREEEAREKFGFFLEAFKYGVPPHGGIAFGLDRLVAIIAGENSIREVIPFPKTGNGVCLLTGAPSSVDEKQLRELRIRVEEG

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Thermotoga sp. (strain RQ2)
Length
579 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.537 kDa
Sequence
MLRTHTCGELRAADEGKKVKLCGWVDRIRDLGGVRFIDLRDRYGETQIVCDVNSKAYSVVDELTRESVVLVEGTVRKRPEGTENPNIETGEIEVVAERIEILSLADPLPFYPGETPKEEMRLKYRYIDLRSERMKRNIILRYRISKIIRDYFDELGFLEIETPFLTKSTPEGARDFLVPSRLRPGKFYALPQSPQLFKQILMISGFDRYFQIVRCFRDEDLRADRQPEFTQVDVEMSFVDVEDVLNVSEGMVSRVFRESSGIDLKVPFDRIPYDEAMEKYGTDKPDRRYGMELRDFGYAFETTEFKVIRNVLDEGGSVKGFIVPGFASEMSRKKGEELMERMKELGLGGLIWFKLDGGITSPHLKHLEKEFRKIAETENMNEGDVCLIAAHTDRNLLNEALGTLRLEIGKEHFSHLAKGFDVLWVVDFPYFEWSEEEERFVARHHPFTMPVLETLGDDYTKVRAKAYDLVINGYEVGGGSIRIHRRDIQEKIFELLGLSEEEAQKKFGFFLEAFRYGVPPHGGIAFGLDRLVSIIAGESSIREVIAFPKTGNGVCLLTGAPAEVDERQLRELRIRIEEG

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Ureaplasma parvum serovar 3 (strain ATCC 700970)
Length
578 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
67.007 kDa
Sequence
MKVYCGYIGEEHLEKNVILNGWVKKVRKMGNLVFVDLKDRFGIVQIFATKSDGVFNELTQLSREDVINVEGLVLLRKNPNNDLKTGRFEIHVKKILIYSKAKTPPLIIEDETDANEEIRFRYRYLDLRRDVNLKIFELRSKVYQAFRNYLYSQDFIETETPILAKPTPEGARDFYVPTRTRKFYALPQSPQTFKQLLMVAGFQKYFQITKCFRDEDLRSDRQPEFTQVDIELSFADEIEIQTLIENLLKYVFKQTINVDLTTPFMRMSYEQAINDYGSDKPDLRFDLKIKTLNTYFENSKTLFFQKALLNNQSIRAILVPNINLNKKQVQTLEKFAKDKGAKGLSWISIKDEKIIDGSLLSIQEDHIIYKTIFKDFNLSTGSILLVADTFDIASQALGLVRINLASILNLKKPNIFKFVWIIDWPLYEYDNEAQRFVAAHHPFTMPTLETLNTFDVNKKDARGRSYDIVLNGYELGGGSVRIIDQQIQRRMFKSINMSDEEANLKFGFLLTAFEYGVPPHCGIALGLDRLMMILVNSEYIRDVVAFPKNNNGVDMMLDAPSNMNDEDLKELGLKIKND

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Deinococcus geothermalis (strain DSM 11300)
Length
577 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.195 kDa
Sequence
MQRTCYIGELNASLVGQTVILQGWANRRRDLGGLIFIELRDRSGSIQVEVEPDSPAFHEADTVRAEYVLEVEGRFQPRPEEQRKGGLADYEVIALRVTVLSAAKTPPFELDKGESVAEDIRLKYRYLDLRRPEMQRHLMLRSRAVAAATAFLDAEGFVQVETPMLTRSTPEGARDFLVPSRLNPGEFYALPQSPQLFKQLLMIAGFDRYYQFARCFRDEDLRADRQPDFTQLDMEMSFVTQEDVLDVQERLLAHVFRTVLDYELPLPFPRLSYQEAMDRYGSDKPDLRFDRAFADVTDLFRGGEFGAFADAETVKVLAAPALTRKQLDELERVAKQNGAKGLAWARREGDGLTGGISRFLGEQAAALLERTGVEPGGTLLFSAGEWKKAVTALGAVRLALRDLFDLAAGGPRFQVAWVLDFPQLEFDEEAGSWTYMHHPFTAPRPEDIPLFGTERQGEIRAQAYDLVLNGFEVGGGSIRIHDPAVQTQMFQAIGLSEAEAREKFGFFLDALSYGTPPHGGIAWGFDRLVMVMAGASSIREVIAFPKNNRGVDLMAGAPSPVSPAQLAEVGVAVTTES

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Helicobacter pylori (strain P12)
Length
577 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.384 kDa
Sequence
MRSHFCTEISEKDVGKTIKVAGWCNTYRDHGGVVFIDLRDKSGLVQLVCDPSSKAYEKALEVRSEFVLVAKGRVRLRGAGLENPKLKTGKIEIVLEELVIENKSATPPIEIGNKSVNEDLRLKYRYLDLRSLNAYEIFKLRSEVALITRNTLAQKGFLEIETPILSKTTPEGARDYLVPSRVHEGEFFALPQSPQLFKQLLMVGGMDRYFQIARCFRDEDLRADRQPEFTQIDAEMSFCDENDVMGVVEDLLQEIFKAIGHTISKPFKRMPYKEAMENYGSDKPDLRFELPLIEVGDCFIDSSNAIFSNIAKDPKNQRIKALNVKGADALFSRSVLKELEEFVRQFGAKGLAYLQIKEDGIKGPLVKFLSEKGLKNILEKTGAKIGDIVFFGAGDKKIVLDYMGRLRLKVAETLDLIDKDALNFLWVVNFPMFEKTENGYHAAHHPFTMPKNIECEDIEEVEAHAYDVVLNGVELGGGSIRIHKEEMQKKVFEKINIHEEEAQKKFGFLLEALKFGAPPHGGFAIGFDRLIMLMTKSNSIRDVIAFPKTQKASCLLTNAPSPINEEQLRELHIRLRK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Helicobacter pylori (strain G27)
Length
577 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.338 kDa
Sequence
MRSHFCTEISEKDVGKTIKVAGWCNTYRDHGGVVFIDLRDKSGLVQLVCDPSSKAYEKALEVRSEFVLVAKGKARLRGPGLENPKLKTGKIEIVLEELVIENKSATPPIEIGNKSVNEDLRLKYRYLDLRSPNSYEIFKLRSEVALITRNTLAQKGFLEIETPILSKTTPEGARDYLVPSRVHEGEFFALPQSPQLFKQLLMVGGMDRYFQIARCFRDEDLRADRQPEFTQIDAEMSFCDENDVMGVVEDLLQAIFKAIGHTISKPFKRMPYKEAMENYGSDKPDLRFKLPLIEVGDCFMDSSNAIFSNIAKDPKNKRIKALNVKGADALFSRSVLKELEEFVRQFGAKGLAYLQIKEDGIKGPLVKFLSEKGLKNILEKTGAKTGDIVFFGAGDKKIVLDYMGRLRLKVAETLDLIDKDALNFLWVVNFPMFEKTENGYHAAHHPFTMPKNIECEDIEEIEAHAYDVVLNGVELGGGSIRIHKEEMQKKVFEKINIHEEEAQKKFGFLLEALKFGAPPHGGFAIGFDRLIMLMTKSHSIRDVIAFPKTQKASCLLTNAPSPINEEQLRELHIRLRK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Helicobacter pylori (strain HPAG1)
Length
577 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.406 kDa
Sequence
MRSHFCTEISEKDVGKTIKVAGWCNTYRDHGGVVFIDLRDKSGLVQLVCDPSSKAYEKALEVRSEFVLVAKGRVRLRGPGLENPKLKTGKIEIVLEELVIENKSATPPIEIGNKNVNEDLRLKYRYLDLRSLNAYEIFKLRSEVALITRNTLAQKGFLEIETPILSKTTPEGARDYLVPSRVHEGEFFALPQSPQLFKQLLMVGGMDRYFQIARCFRDEDLRADRQPEFTQIDAEMSFCDENDVMGVVEDLLQAIFKAVGHTISKPFKRMPYKEAMENYGSDKPDLRFELPLIEVGDCFRDSSNAIFSNIAKDPKNKRIKALNVKGADAVFSRSVLKELEEFVRQFGAQGLAYLQIKEDGIKGPLVKFLSEKGLKNILEKTGAQTGDIVFFGAGDKKIVLDYMGRLRLKVAETLDLIDKDALNFLWVVNFPMFEKTENGYHAAHHPFTMPKNIECEDIEEVEAHAYDVVLNGVELGGGSIRIHKEEMQKKVFEKINIHEEEAQKKFGFLLEALKFGAPPHGGFAIGFDRLIMLMTKSHSIRDVIAFPKTQKASCLLTDAPSPINEEQLRELHIRLRK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Helicobacter pylori (strain Shi470)
Length
577 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.201 kDa
Sequence
MRSHFCAEISEKDVGKTIKVAGWCNTYRDHGGVVFIDLRDKSGLVQLVCDPSSKAYEKALEVRSEFVLVAKGKARLRGPGLENPKLKTGKIEIVLEELVIENKSATPPIEIGNKNVNEDLRLKYRYLDLRSLNAYEIFKLRSEVALIARNALAQKGFLEIETPILSKTTPEGARDYLVPSRVHEGEFFALPQSPQLFKQLLMVGGMDRYFQIARCFRDEDLRADRQPEFTQIDAEMSFCSENDVMGVVEDLLQEIFKAIGHNISKPFKRMPYKEAMENYGSDKPDLRFELPLIEVGDCFMDSSNAIFSNIAQDPKNKRIKALNVKGADAIFSRSVLKELEEFVCQFGAQGLAYLQIKEDGVKGPLVKFLSEKGLKNILEKTGAKTGDIVFFGAGDKKIVLDYMGRLRLKVAETLDLIDKDALNFLWVVNFPMFEKTENGYHAAHHPFTMPKNIECKDLEEIEAHAYDVVLNGVELGGGSIRIHKEEMQKKVFEKINIHEEEAQKKFGFLLEALKFGAPPHGGFAIGFDRLIMLMTKSSSIRDVIAFPKTQKASCLLTDAPSPINEEQLRELHIRLRK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Helicobacter pylori (strain ATCC 700392 / 26695)
Length
577 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Is 1.7 times more efficient at aminoacylating tRNA(Asp) over tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.602 kDa
Sequence
MRSHFCTEISEKDVGKIVKVAGWCNTYRDHGGVVFIDLRDKSGLVQLVCDPSSKAYEKALEVRSEFVLVAKGKVRLRGAGLENPKLKTGKIEIVLEELIIENKSATPPIEIGNKHVNEDLRLKYRYLDLRSPNSYEIFKLRSEVALITRNTLAQKGFLEIETPILSKTTPEGARDYLVPSRVHEGEFFALPQSPQLFKQLLMVGGMDRYFQIARCFRDEDLRADRQPEFTQIDAEMSFCDENDVMGVVEDLLQEIFKAVGHTISKPFKRMPYKEAMENYGSDKPDLRFELPLIEVGDCFRDSSNAIFSNTAKDPKNKRIKALNVKGADALFSRSVLKELEEFVRQFGAKGLAYLQIKEDEIKGPLVKFLSEKGLKNILERTDAQVGDIVFFGAGDKKIVLDYMGRLRLKVAETLDLIDKDALNFLWVVNFPMFEKTENGYHAAHHPFTMPKNIECEDIEEVEAHAYDVVLNGVELGGGSIRIHKEEMQKKVFEKINIHEEEAQKKFGFLLEALKFGAPPHGGFAIGFDRLIMLMTKSHSIRDVIAFPKTQKASCLLTNAPSPINEEQLRELHIRLRK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Deinococcus deserti (strain VCD115 / DSM 17065 / LMG 22923)
Length
577 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.113 kDa
Sequence
MKRTALIGQLSTTHLDQAVTLQGWVNRRRDLGGLIFLELRDRSGLVQVQVEPDSPAFAQADQLRAEYVAEVEGIYRARPENQRKGGAADYEVIASRVKVLNTAKTPPFELDKGESVAEDIRLKYRYLDLRRPEMQRHLLLRSRAMAAVTAFLDSSGFVQVETPMLTKSTPEGARDFLVPSRLNPGEFYALPQSPQLFKQLLMIAGYDRYYQFARCFRDEDLRADRQPDFTQLDMEMSFVEQDDVLELQEGLMAHVFKATLDVDLPRPFPRLSYFDAMDRYGSDKPDLRFESALVDVTDLFQGGEFKAFAAAQSVKVLAAAELTRKQIDELERVAKQNGAGGLAWLKRDGDSFTGGISKFVGSVAPQLIKRSGVQDGGTLLFAAGDWKKAVTALGAVRLAVRDLFDLTSSGPRFHVSWVTDFPQLEFDEDSGTWTYMHHPFTAPHPDDAELFGTLRQGEIRAQAYDLVLNGFEVGGGSVRIHDPAVQTKMFEAIGFTEAQAREKFGFFMDALEYGTPPHGGIAWGFDRLVMVMSGASSIREVIAFPKNNRGADLMAEAPSLVDDAQLAELGVGVLSPS

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Mesoplasma florum (strain ATCC 33453 / NBRC 100688 / NCTC 11704 / L1)
Length
577 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.445 kDa
Sequence
MKRTHNCNQLNISNVNQEVTLKGWIKKIRKMGQITFIDLRDFYGITQIVVGENKQELINNLKPEYVISITGKVIERKSKNADIPTGEIEIEVKNIELINKSELTPFVIENDVEVSEETRMSYRYLDLRRQKIQNNMLLRAKVNSIIRKEFEADNFVEVETPYFGKSTPEGARDFLVPSRLNKNTFYALPQSPQLYKQLLMVSGFDKYYQIVRCFRDEDLRNDRQPEFTQLDMEMSFASATEVQDQIEKVIKKIFLEVKGIDFKEKLIKMPFREAIDLYGSDKPDIRFDLKINTLNEIFDKTQIKLFESFKENKLSIRGICVEELLSKKQLEILTETAKQKSFNNLAFAKFENGTWSGSIASSLSDGEKQALIKQFNIKDKATILLNVGKYEKISDMLGAVRNKVAEILNLADPNDYKLLWIIDFPLYEWSDEESRYVAAHNPFTMPNIKSIDDFETNKEDAIADSYDLVLNGFELGSGGVRITDSGIQQRMFEAVGLDDETIEKNFGWFINAYKYGAPNHAGFAFGIDRVIMLLTHSESIRDVIAFPKNSKGIDMMNDAPSYVEDNQLSELSIKTIK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Fervidobacterium nodosum (strain ATCC 35602 / DSM 5306 / Rt17-B1)
Length
576 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
65.799 kDa
Sequence
MYRTHTCGELRGTDEGKNVILSGWIERIRDLGGVKFIVLRDRYGKTQVVVNPDSPVYPIVNNISREYVIQVEGIVRKRPAEAITPEPTGEIEIVASELKILSKSELPPFYPGDDVSEEMRLKYRYLDIRNPKMMNNLILRHKLAFATREYLSNNNFLEVETPYLTKSTPEGARDFLVPSRLKKGNFYALPQSPQLFKQILMISGIDRYFQIVRCFRDEDLRADRQPEFTQIDIEMSFVHMEDVINLAENLIRYIYKAIGIELPEKFDRITYEEAMEKYGSDKPDRRYGMEMVDLTEFFKNSDFKIIKEVLERGGSVKGFKANIPMSRKIADEYSEFVKGFGLGGVLWFKLENGQITSTTAKYLENEYKAIAEKYNMNEGEVFIIAAHDNRERMNEALGALRLKVGKQYVKVSGFDALWVVDFPFLEWSEEEGRFVARHHPFTMPYIEDLEGGVELSKVRAHAYDMVINGFEVGGGSIRIHRRDIQEKVFDIIGLTKEEAKEKFGFFLDALQYGVPPHGGIAFGLDRLAAIAAGVDNIREVIAFPKTSSGTCLLTNAPSAVTQFQLDELGIALKQSQ

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Aster yellows witches'-broom phytoplasma (strain AYWB)
Length
576 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.679 kDa
Sequence
MKTKYSYYNNQLTLIHQGKIVFLKGFIFRKRNLGKTLFFDLRDVSGIVQLLVKENNPQYDKIALIKLETVVQIKGQVIERINKNPDLPTGDIEILVSHIEILSEAQTLPLNVFQSQESLEETRLKYRYLDLRNPEVKHFLIQRHHITQSIRQTLLKNDFLELETPILSKSTPEGARDYLVPSRIYPGNFYALPQSPQLFKQLYMIAGFERYFQVARCFRDEDLRSDRQPEFSQIDIETSFLNQDEIMSLTEEIIVDLFANIWKKPLLQPFLRLTYQQAFELYGSDKPDLRNPLKITDFTTFFDTNTYSQNIFAGKIKGFKVSKTAFLTRRKLDEYQLFFSKHFNLKLFSFVKKNDKIIGGISQFIQDDSFLKNEEICFVVSGKKDIIHKALGIFRTKLALDLSLVDTTQEALLWIVDFPLFETIQEDLSPPNRLYSLHHPFTAPRDATILKSNPQKALANAYDLVWNGYEVGGGSLRINNHQTQELIFSLLGFLQEEVQNRFGFLIEALKYGTPPHGGIALGLDRLVMLFTKTNNIKDVIAFPKTQSAKDLMLEAPSAVNQEQLNTLKLQLKCNFN

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Blochmannia floridanus
Length
576 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.208 kDa
Sequence
MRTAYCGQLNLSHVGLEVTLCGWVNKYRNFGKLIFVDLRDREGCIQVYFNSDAQKKTYVRAADLKQEFCIQLTGIVRSRPVSQINKNMSTGFIEIEAKFFLVLNVSNPLPLDIHQDNIEENRLKYRYLDLRRPIMFHNIQTRSRVMALTHRFMELEGLLNIDTPVLAKSTPEGARDYLVPSRLHINKYYALPQSPQMFKQLLMIAGIDRYYQITKCFRDEDLRSDRQPEFTQIDVEISFITAKKIRELMEFFICKLWKEILNVELEVFSQFSYAEVISRFGSDSPDLRNPIEMKDVSSIFQSLGNKLFICNAGCVDTIDTQVIVMNVPSGFKLTRNEIDKYSDYAKKSGIQQFLWMKIQMNDCKEITAIDGPIINLLNKNFLQLLMAQVKIENNDILFFGFNNDKNLSTTRMLSALRSKLGYDLNLVKQDSWKPLWIVDFPMFKKNTSGKLVSMHHMFTAPKDNDLICLKRNPELAVSEAYDIVINGCEVGSGSVRIHSYKLQQAMFDILGITRENQQKKFGCLMNALKYGAPPHAGIALGLDRLVMLLTKSNNIRDVIAFPKTTGAMDLMIDAPD

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp)
Length
576 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.845 kDa
Sequence
MRTNFCGTLNVSHVGKTIKLCGWVNKFRNLKEILFIDIRDQTGIIQVLFSKKSELLFKKAADLRNEFCIQVLGIVQERITKNKNYTMSTGEIEIFALELKIFNKSQPLPIDLKSCNIEETRLKFRYLDLRHPNMIRNIIIRNDITIIIRNFMKKNKFLDIETPILTKSTPEGARDYIVPSRIHKNKYYALPQSPQLFKQLLMISGIDRYYQIAKCFRDEDLRSDRQPEFTQIDIEVSFLNAKKVRKIIERMITSVWNKIINVHLKKFQKLSFYDAIKMYGTDKPDLRNPIQLIDVTNIIHVKNNINAITLPNKKTQQNIVIAMCIPRGMSLNINYINSYHHLVQKYTKNKLFNVEVLNHCPIKEQKKTSFHKKPSSDLTFQLISKTSAKHGDMIFYLSEKSPLVYEIMGKLRIELGKDLNLIDYNSWKPLWITNFPLFKKNELNQYISTHHPFTAPKYMKIDTSITNYEEIVADSYDLVINGYEIGSGSVRIHDLELQKTVFNILGINTVLQKNNFNFFLNALKYGTPPHAGIALGLDRITMLLTNSHNLRDVIAFPKTTTGSCLTTGAPSKIIHF

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Mycoplasma capricolum subsp. capricolum (strain California kid / ATCC 27343 / NCTC 10154)
Length
575 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.695 kDa
Sequence
MKRTHTCGELTLQNVDQKVILQGWVKKIRKLGAMVFIDLKDRYGITQLVIEQENINLINNLKNEYVIEISGIVVKRKSVNKELITGEIEVIVKDLLVINKSELTPFVLENDVNVNEDTRLTYRYLDLRRQVMQNNLIIRAKINHIIRNYLTDLNFLEVETPYFAKSTPEGARHFLVPSRLNKNKFYALPQSPQLFKQLLMISGIDRYYQIVRCFRDEDLRIDRQPEFTQLDLEMSFATSEDVMQISESLIKKILKEVKNFEIKEPLLRLSYKDAIDLYGSDKPDLRYELKIHTLNDIFKNSDIKMFLDSQNKYIRAVCIDQLLTKKQLEELNQQAKQFHFNSIAFIKVENNAWSGSLASQLTEVQKKQLIEEFNIQNKATIILNIGKYEEISQLMGAIRISLAKMFNLETKDDFKLLWVVDFPLFEFSEQENRYVAAHHPFTSPKEESLADFDTNKKDALACAYDLVMNGFEIGGGSQRITNSEIQQRMFDAVELNQKQVEANFGWFMNAYKYGAPYHAGIAWGLDRISMILTDSNSIRDVIAFPKNSLGIDMMSNAPDLVSDKQLDELNIKTVE

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Blochmannia pennsylvanicus (strain BPEN)
Length
574 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.034 kDa
Sequence
MRTAYCGQLNLSHVGLEVTLCGWINKYRNFGGLIFIDLRDREGCIQVCFDVYQNKEVCISAAKLKQEFCIQLIGMVRARPKNQINSNISTGAVEVVAKKFSILNISDPLPLDISKNNIEENRLKYRYLDLRRSIMFDRIKTRSRIMSIVHRFMELEGFLNIETPMLTKVTPEGSRDYIVPSRLHAGKNYALPQSPQIFKQLLMVSGFDRYYQITKCFRDEDLRADRQPEFTQIDIETSFMTTQKIRELMEIFIRIIWREILNVELGVFSQFTYSEVMQRFGSDAPDLRNPIEMFDVSYLFNSTQNRLSFIRANNIGVQAIAMKVPNGRQLTQKQIDEYIYYSKQCGLKELLWVKVQFSDNDITKKEIQGSVTNFIDNLTLDIILNKTNIKSNDILFVGFNDNKNQFITKMLSALRLKLGNDLCLIKKDSWAPLWIIDFPMFKKNCHGEYTSMHHMFTSPKNCDVQMLKKDPLLVISEAYDMVINGCEIGSGSARIHSFDMQQAVFNILGITQNDQKKKFGYFMDALKYGAPPHAGLAFGLDRIAMLLTGSKNIREVIAFPKTTASVDIMANAPD

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Mycoplasma mycoides subsp. mycoides SC (strain PG1)
Length
574 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
66.67 kDa
Sequence
MKRTHTCGELTINNIDQEVILQGWVKKIRKLGAMVFIDLKDRYGITQLVVDQQHIDLINNVKNEYVIEIKGNVVKRKSINKELVTGDIEVIVKELFIINKSELTPFVLENDVNVNEDTRLTYRYLDLRRPVMQNNLIIRAKINHIIRNFLTDSNFLEVETPYFAKSTPEGARDFLVPSRLNKNKFYALPQSPQLFKQLLMISGIDRYYQIVRCFRDEDLRIDRQPEFTQLDLEMSFATSEDVMQISESLIKKILKEVKNFEIKEPLLRLSYKDAIDLYGSDKPDLRYDLKIHTLNDIFKNTNIKFLNNPDLFIRAICIDQLLSKKQLEDLNQQAKQFHFNSIAFIKFENNNWSGSLASQLTENEKELLIKEFDIKNKATIVLNIGKYEQISQLMGAIRISLAKMFNLETKDDFKLLWVVDFPLFEFSEQENRYVAAHHPFTSPKEECLTDFDTNKKDALTCAYDLVMNGFEIGGGSQRITNPEIQQRMFDAVELTTQQVETNFGWFMNAYKYGAPYHAGIAWGLDRISMIVTDSNSIRDVIAFPKNSLGIDMMSNAPDLVSEKQLEELNIKIVK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Mycoplasma pneumoniae (strain ATCC 29342 / M129)
Length
557 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.114 kDa
Sequence
MNLDNAKCFKQRVFIGNLTSEHLNKTVTIAGWVKRIKKLGELNFVIVGDKTNTIQVTCKNKEQVKYLTREDLVIVKGKLKRLDSVRFEITNPTITLFAKSKTPPLIIEDKTDALEEVRLRYRYLDLRRPVMQKRLALRHKVTLAVRNWLDQMGFIEVETPTLTKSTPEGARDFLVPARIREHSFYALPQSPQIYKQLLMVGGTEKYFQIAHVYRDEDSRKDRQPEHTQIDLEVAFYTKEMVMDLIQRLFVDVFRQVLNIKLKKPFPVLKFAEAFNRFGSDKPDLRYGFELEDCTDLFQDSPNQFTNLINAGGIVGGIQLPNLYLDEVSFKALRKLAKDNGVSLEFYSDKASSLKQPLDLPLAGTILLVAHKSKTQAWTALGAIRNELKYHLNLVKPNQYSFCWIVDFPLYEFDEKEQKWVSAHNMFSNPQPQWLVNFENHKAEALSEQYDLVLNGFELGSGSIRIHDPEVQTRLMQSLGVDPQQFGFVMEAYQYGAPVHAGMGLGLDRLMMIINNVDNIREVMAFPKNAQGIEMHTNAPDQVDIKDITTIWSKHPVK

Gene
aspS
Protein
Aspartate--tRNA ligase
Organism
Mycoplasma genitalium (strain ATCC 33530 / G-37 / NCTC 10195)
Length
550 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.
Mass
64.237 kDa
Sequence
MCFNQRILIGSISTEQLNKTIVIIGWIKRIKKLGEINFIIVGDKSGTIQVTCKDKEQIQQLTREDIVIVKAKLQRLDSVRFELINPTIKLFSKSKTPPLIIEDETDALEEVRLKYRYLDLRRRLMQKRLLLRHQFILAIRNWFNQQGFIEIETPTLSKSTPEGAQDFLVPARIRKDCFYALVQSPQIYKQLLMIAGVEKYFQIARVYRDEDSRKDRQPEHTQIDFEISFCNQKMIMNLVEKLFFSVFLDVFQIKIKKTFPVFKFSELFERFGSDKPDLRYGFEIKDFTSLFQDHQNQFTKLIEAKGIIGGIELTNIELSTDKIKALRKIAKDHDVSLEVHNKNNSTLKTSIKCDEKNTLLLVANKSKKKAWTALGAIRNELKYHLDIVKPNQYSFCWVVDFPLYDFDEKTNQWISNHNIFSKPKQEWIDNFESNKNEALSEQFDLVLNGFEIGSGSIRINDPIVQKRLMNSLNIDPNKFAFLLEAYQYGAPVHGGMGLGIDRLMMILNQTDNIREVIAFPKNNHGIEVHTNAPDKIDKEEVKWWIKELVK

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 / C2A)
Length
444 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
50.744 kDa
Sequence
MSLANLRTHYTAEVKPESVDNGQKITLAGWIHEVRDLGGICFVVLRDREGKAQVTLVKKKIDKELFDAARRLIRESVISVTGSVKFEEKAPNGYELLPEEIKVLNVAGSPLPMDTTGKVEAELDTRLDSRFIDLRRAETTAVFKIRHEALQAIREYFVKNKFIETATPKVVATATEGGTALFPITYFDREAFLNQSPQLFKQILMGGGFDRVFEIGPIFRAEEHDTRRHLNEATSIDVEVSFADHFDVMEILENLVAHIYTRVIENCKASLEILGVELKVPKTPFLKLTYDEVIEIVNSRCEEKMHWGDDLGTLGEHTVGNYVYETTGESHYFIIDWPTEIKPFYAMPYEDRPEFSKSFDMMHRTMELSSGAQRIHISELLKSRIESQGLNPDGFEFYLKAFEYGMPPHAGWGMGCERFVMTMLGTENIRDTVLFPRDRRRLSP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methanosarcina barkeri (strain Fusaro / DSM 804)
Length
444 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
50.796 kDa
Sequence
MSLAKLRTHYTADVKPEKVDNGQKITLAGWVHEVRDLGGICFVVLRDREGKAQVTLVKKKIDKELFDAARRLVRESVISVTGSVKFEEKAPNGYELLPEEITVLNVANSPLPMDTTGKVEAELDTRLDSRFIDLRRAETTAVFKIRHQALQATREYFVQNGFIETATPKVVATATEGGTALFPITYFDREAFLNQSPQLFKQILMSGGFDRVFEIGPIFRAEEHDTRRHLNEATSIDVEVSFADHFDVMEILENLVAYVYAQVIEKCKPSLETLGIELKVPKTPFLKLTYNEVIEIINARSEEKMHWGDDLGTFGEHIVGNYVYETTGESHYFIIDWPTEIKPFYAMPYEDRPEYSKSFDMMHRTMELSSGAQRIHIPDLLKSRIESQGLNPEGFEFYLKAFEYGMPPHAGWGMGCERFIMTMLGTENIRDTVLFPRDRRRLSP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88)
Length
444 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
50.808 kDa
Sequence
MSLANLRTHYTADVRPDKVENGQKVTLAGWVHEVRDLGGICFVVLRDREGKAQVTLVKKKIDKDLFDAARRLVRESVISVTGSVKFEEKAPNGYELLPDEINVLNVSGSPLPMDTTGKVEAELDTRLDSRFIDLRRAETTAVFKIRHESLRAIREYFVKYNFIETATPKVVATATEGGTALFPITYFDREAFLNQSPQLFKQILMSGGFDRVFEIGPIFRAEEHDTRRHLNEATSIDVEVSFADHFDVMELLENLVAYVYTRVIENCKSSLEVLGVDLKVPKTPFLKLTYDEVIEIINSRCEEKMHWGDDLGTLGEHTVGDHVYETTGESHYFIIDWPTEIKPFYAMPYEDRPEFSKSFDMMHRTMELSSGAQRIHIPSLLKNRIESQGLNPDGFEFYLKAFEFGMPPHAGWGMGCERFVMTMLGTENIRDTVLFPRDRRRLSP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methanococcoides burtonii (strain DSM 6242 / NBRC 107633 / OCM 468 / ACE-M)
Length
443 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
50.241 kDa
Sequence
MSLETPRTHYTSQIDIEQIGDDKVTVCGWVHEVRDLGGICFVVVRDREGRAQITLVKKKIDKEIFDAARKLVRESIVAVTGTAKAEGKAPNGYEIIPESIVVLNEAESPLPMDTTGKVDAELDTRLDSRFMDLRRERTTAIFKIRHEVLRAVRDFLSKDGYIETCSPKVVATATEGGTSLFPITYFDREAFLNQSPQLFKQILMSGGLDKVFEIGPIFRAEEHDTRRHLNEATSIDIEASFLDHFDVMEVLEDMVAYVYEQVIENEAASLKALDIELSVPKTPFMKVPYSQAIDIVNAESEETVEWGGDLGTVAEHTIGEHVFKETGESHYFITDWPTEIKPFYAMPYEDNPLISKSFDMMHRTMELSSGAQRIHIHDMLKARIESQGLDSDGFDFYLRAFKYGMPPHSGWGIGCERLVMTMLSVENIRDTVLFPRDRKRLSP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Length
442 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn) (By similarity).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
50.853 kDa
Sequence
MLKDRFIADIIASKESLVGGRVRVCGWAYRIRDLGRLKFILVRDRSGVIQATVKRGESPEDALRAAEDLKLESVVCVEGELRQAPTREGVEVKVERLEVLSTPVEPLPLEVEGSEKASLPTRLKYRWLDIRNPMVSAIFELEAMVAKVFRDYYWSQGFVEIFTPKIVAAGTESGAEVFPVVYFDKTAFLAQSPQFYKQFAVIAGLERVFEIGPVFRAEPHHTSRHLNEYHSLDIEVGFIESYNDVMNYVEGFMRAIVRMLEEDGRRVLELYGVELPRIPASGIPKIPLRKAYEILEEKYGKKVEYGEDLDSEGERLMGAYAGEELDSDFVFIVEYPWKVRPFYTMRKDDEPSWTYSFDLLYRGLEIVTGGQREHRYHRLLENLRDKGLDAESFQFYLDFFKHGAPPHGGAGMGLERIVMQTLKLENIREARMLPRDTERITP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3)
Length
439 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
49.924 kDa
Sequence
MTDIFEKCKRTHYSNEIGPELAGETVKVTGWVHEIRDLGGIVFVLIRDKNGITQLTAPSKKLSEEMMADVRAARKETIITLTGTVQESAKAPNGVEIIPSNIDVINVSQLPLPLDTTEKVEAEMDTRLDSRFMDLRKHDVSAIFKIKSQMLHTARNYFYDNDFTEITTPKLVASATEGGTELFPITYFEKEAFLGQSPQLYKQMMMATGLDNVFEIGQIFRAEEHDTLRHLNEALSIDAEMSFKSQTDAMNTLEELIKRILSDISTNCQKELSDLDHELDIPTEPFPIVTYEEVIDIVNSRDVEMNYGEDLNRAAEKVLGETMGSYYFITEWPTAIKPFYVMPNSDDAEKSTAFDLMYRDLELSSGAQRIHDYDLLYSQIEAKDLNPDSFEKYLQAFKYGMPPHSGWGMGADRLTMVITGAKNIRETVLFPRDRRRLTP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3)
Length
438 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
50.064 kDa
Sequence
MYALGDWRRTHYSSEVNSEMDGQEIIIMGWNHSIRKLGKLVFIILRDREGTIQIVAPKQKVSEETFATAKSLGKEDVMAIKGKVVANEKAPAGFEVIPIEIKILNKADTPLPLDPSEKVSADIDTRLDKRFLDLRRPKIQSLFKLRSEVLKSIRNTFHDNGFIDVDTPKLVASATEGGTELFPISYFDKEAFLGQSPQLYKQMMMAAGFDRVFEIGPIFRAEEHNTRRHLNEAISIDCEMSFADEKDAMEILEKVINNAFTDIYNNNQKELQTLGIDLKVQETPFPRIEYTEAVDMVNAKGVEMEWGEDFSRPAEAALGEMMDGFYFITDWPTEIRPFYTLPNEDNPKLCKAFDLMYKDLEISSGAQRNHKYDLLVEGIKRMGLNPEGFGTYLEAFKYGMPPHSGWGVGIERLMMIMACQQNIRECVLFPRDRQRLTP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Length
438 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
50.35 kDa
Sequence
MVNKMKWRRTHYSADIKPEMDGQEVIIMGWVHSIRALGKIIFVILRDREGTVQIVAPKQKVGDELFSQIKKLGAEDVIAVKGKVIANEKAPNGFEILPLELEVINTAKRPLPLDPAEKVPAELDTRLENRFLDLRRPKVQAIFKIRSEMLKSVRNTLYNEGFIEVNTPKLVASCTEGGTELFPISYFEREAFLGQSPQLYKQMLMATGLDRVFEIAPIFRAEEHNTRRHLNEATSIDIEMAFADDKDAMDILEKVVYNAFVDVYENRKKEIETLGIEFELPPEKFDRITYDEAIDIANAKGVEISWGEDLSREAEKAIGEEMEGLYFITDWPSEIRPFYTMPDEKNPNICKAFDLMYKDLEISSGAQRIHLYDLLVENIKKKGLNPDGFTYYLEAFKYGMPPHAGWGLGADRFTMVLTQQENIRECVLFPRDRQRLTP

Gene
aspS
Protein
Aspartate--tRNA(Asp) ligase
Organism
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
Length
438 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp). Is specific for tRNA(Asp) since it aspartylates tRNA(Asn) 3 orders of magnitude less efficiently than tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
50.91 kDa
Sequence
MYRTHYSSEITEELNGQKVKVAGWVWEVKDLGGIKFLWIRDRDGIVQITAPKKKVDPELFKLIPKLRSEDVVAVEGVVNFTPKAKLGFEILPEKIVVLNRAETPLPLDPTGKVKAELDTRLDNRFMDLRRPEVMAIFKIRSSVFKAVRDFFHENGFIEIHTPKIIATATEGGTELFPMKYFEEDAFLAQSPQLYKQIMMASGLDRVYEIAPIFRAEEHNTTRHLNEAWSIDSEMAFIEDEEEVMSFLERLVAHAINYVREHNAKELDILNFELEEPKLPFPRVSYDKALEILGDLGKEIPWGEDIDTEGERLLGKYMMENENAPLYFLYQYPSEAKPFYIMKYDNKPEICRAFDLEYRGVEISSGGQREHRHDILVEQIKEKGLNPESFEFYLKAFRYGMPPHGGFGLGAERLIKQMLDLPNIREVILFPRDRRRLTP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methanococcus maripaludis (strain C5 / ATCC BAA-1333)
Length
438 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
50.157 kDa
Sequence
MYLIADWRRTHYSEEVIPEMDGQEVILMGWVHSIRALGKLAFVILRDREGTIQAVVPKQKVDEETFAIAKKLGKEDIIAIRGKVVANEKAPKGFEVIPIEIRVLNKADAPLPLDPSEKVAAEIDTRLDKRFLDIRRPKIQAIFKIRSEMLRSIRKTFADGGFVEVNTPKLVASATEGGTELFPISYFEKEAFLGQSPQLYKQMMMAGGFDKVFEIAQIFRAEEHNTRRHLNEAISIDTEMSFVNEKDAMAMLEKVVYNCYADIEYNRPQEIELLELNWEIPEKTFDKITYTEAIDIANAKGVEIEWGEDLSRAAERAVGDEMGGLYFITEWPTQTRPFYTLPHKHDNKVCKAFDLMYKELEISSGAQRVHKYDLLVENISNMGMNPDSFETYLEAFKFGMPPHAGWGLGADRFAMVLTAQDNIRECVLFPRDRQRLTP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methanococcus maripaludis (strain C6 / ATCC BAA-1332)
Length
438 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
50.249 kDa
Sequence
MYLIADWRRTHYSEEVIPEMDGQEVILMGWVHSIRALGKLAFVILRDREGTIQAVVPKQKVDEETFEIAKKLGKEDIIAIRGKVVANEKAPKGFEVIPIEIRVLNKADAPLPLDPSEKVPAEIDTRLDKRFLDIRRPKIQAIFKIRSEMLRSIRKTFADEGFIEVNTPKLVASATEGGTELFPISYFEKEAFLGQSPQLYKQMMMAGGFDKVFEIAQIFRAEEHNTRRHLNEAVSIDTEMSFVNEKDAMAMLEKVVYNCYADIEYNRPQEIELLELNWEVPEKTFDKVTYTEAIDIAISKGVEIEWGEDLSRAAERAVGDEMGGLYFITEWPTQTRPFYTLPHEKDAKVCKAFDLMYKELEISSGAQRVHKYDLLVENISNMGMNPDSFETYLEAFKFGMPPHAGWGLGADRFAMVLTAQDNIRECVLFPRDRQRLTP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methanococcus maripaludis (strain C7 / ATCC BAA-1331)
Length
438 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
50.292 kDa
Sequence
MYLIADWRRTHYSEEVIPEMDGQEVILMGWVHSIRALGKLAFVILRDREGTIQAVVPKQKVDEETFEIAKKLGKEDIIAIRGKVVANEKAPKGFEVIPIEIRVLNKADAPLPLDPSEKVPAEIDTRLDKRFLDIRRPKIQAIFKIRSEMLRSIRKTFADEGFVEVNTPKLVASATEGGTELFPISYFEKEAFLGQSPQLYKQMMMAGGFDKVFEIAQIFRAEEHNTRRHLNEAVSIDTEMSFVNEKDAMAMLEKVVYNCYADIEYNRPQEIELLELNWEIPEKTFDKLTYTEAIDIAISKGVEIEWGEDLSRAAERAVGDEMGGLYFITEWPTQTRPFYTLPHENDNKVCKAFDLMYKELEISSGAQRVHKYDLLVENISNMGMNPDSFETYLEAFKFGMPPHAGWGLGADRFAMVLTAQDNIRECVLFPRDRQRLTP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methanococcus maripaludis (strain S2 / LL)
Length
438 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
50.132 kDa
Sequence
MYLIADWRRTHYSKDVIPEMDGQEVTLMGWVHSIRALGKLAFVILRDRAGTIQAVVPKQKVDEETFEIAKKLGKEDIVAIKGKVVANEKAPKGFEVIPIEIRVLNKADAPLPLDPSEKVSAEIDTRLDKRFLDIRRPKIQAIFKIRSEMLKSIRKTFADEGFIEVNTPKLVASATEGGTELFPISYFEKEAFLGQSPQLYKQMMMAGGFDKVFEIAQIFRAEEHNTRRHLNEAISIDSEMSFVNEKDAMAMLEKVVYNCYSDIEYNRPNEIELLELNWEIPEKTFDKVTYTEAIDIAIAKGVEIEWGEDLSRAAERAVGDEMGGLYFITEWPTQTRPFYTLPHKHDNKVCKAFDLMYKELEISSGAQRVHKYDLLVQNISNMGLNPDSFETYLEAFKYGMPPHAGWGLGADRFAMVLTAQDNIRECVLFPRDRQRLTP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB)
Length
438 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
50.44 kDa
Sequence
MYIIADWRRTHYSEQVIPEMDGQEVILMGWVHSIRALGKLAFIILRDREGLIQMVVPKQKVDEETFELAKKLGKEDVITIRGKVVANEKAPKGFEVIPMEIRILNKADAPLPLDPSEKVPAEIDTRLDRRFLDIRRPKIQAIFKIRSEMLKSIRKTFSEEGFIEVNTPKLVASATEGGTELFPISYFEKEAFLGQSPQLYKQMMMAGGFDKVFEIAQIFRAEEHNTRRHLNEAISIDTEMSFVNEKDAMAMLEKVVHNCYTDIEYNRPSEIETLELNFEIPEKTFPKVTYSEAVDVAVSKGVEIEWGEDLSRAAEKAIGDEMGGLYFITEWPTQTRPFYTLPDENDNKICKAFDLMYKELEISSGAQRIHKYDSLVQNIAKRGMNPDSFETYLEAFRYGMPPHAGWGLGADRFTMILTNQENIRECVLFPRDRQRLTP

Gene
aspS
Protein
Aspartate--tRNA(Asp) ligase
Organism
Pyrococcus abyssi (strain GE5 / Orsay)
Length
438 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
50.975 kDa
Sequence
MLRTHYSSEITEELNGKKVKVAGWVQEVKDLGGIKFIWIRDREGIVQVTAPKKKVPQEIFKLIPKLNSEDVIVVEGIVNFTPKAKLGFEIIPEKLEVISKAKTPLPLDPTGKVKAELDTRLDNRFMDLRNPRVMSIFKIRSSVFRATREFFYKEGFIEIHTPKIIATATEGGTELFPLKYFENDAFLAQSPQLYKQMMMSTGLDKVFEIGPIFRAEEHNTTRHLNEAWSIDAEMAFIESEEEVMDLLERLILYVINYVRENNEKELKILEFELNEPKKPFPRITYDEALEILSDLGKEIPWGEDIDTEGEKLLGKYMLENEGAELYFIYRYPSEAKPFYIMKYEDKPEVCKAFDLEYRGVEISSGGQREHRHDILVEQIREKGLNPESFEFYLRAFEYGMPPHGGFGLGAERLIMRMLDIGNIREVILFPRDRRRLVP

Gene
aspS
Protein
Aspartate--tRNA(Asp) ligase
Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Length
438 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
51.017 kDa
Sequence
MLRTHYSNEITEELNGKRVKVAGWVQEVKDLGGIKFVWIRDREGIVQITAPKKKVSEEIFKLIPKLNSEDVVVVEGIVNFTPKAKLGFEIIPEKFEILNRTQTPLPLDPTGKVKAELDTRLDNRFIDLRNPKVMAIFKIRSNVFRAIREFFYNEGFIEIHTPKIIATATEGGTELFPIKYFENDAFLAQSPQLYKQIMMATGLDKVFETAPIFRAEEHNTTRHLNEAWSIDAEIAFIENEEEVMDVLENLVVYAINYVREHNERELKILEFELEEPKQPFPRVTYDKALEILSDLGKEIPWGEDIDTEGEKLLGKYMSENEGVELYFIYKYPSEAKPFYIMKYDEKPEICRAFDLEYRGIEISSGGQREHRYEVLLEQIKEKGLNPESFEFYLKAFKYGMPPHGGFGLGAERLIMRMLNIGNIREVILFPRDRKRLIP

Gene
aspS
Protein
Aspartate--tRNA(Asp) ligase
Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Length
438 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
50.869 kDa
Sequence
MLRTHYSNEITEELNGKRVKVAGWVQEVKDLGGIKFIWIRDREGIVQVTAPKKKVSQEIFKLIPKLNSEDVIVVEGIVNFTPKAKLGFEVIPEKLEVISRAKTPLPLDPTGKVKAELDTRLDNRFMDLRNPKVMAIFKIRSSVFRAVREFFYSEGFIEIHTPKIIATATEGGTELFPLKYFERDAFLAQSPQLYKQMMMATGLDKVFEIAPIFRAEEHNTTRHLNEAWSIDAEMAFIENEGEVMDLLERLISYVINYVREHNEKELKTLEFELNEPKRPFPRITYDKALEILSDLGKEIPWGEDIDTEGEKLLGKYMAENEGADLYFIYRYPSEAKPFYIMKYDEKPEVCRAFDLEYRGVEISSGGQREHRHDVLLEQIKEKGLNPKSFEFYLKAFEYGMPPHGGFGLGAERLIMRMLDIGNIREVILFPRDRRRLVP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Length
437 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
49.838 kDa
Sequence
MLLGDLRRTHYSKDIEPEMDGDEVTVMGWVHEIRDLGGIIFVLLRDRDGLIQITAPSKKIEKDLFKSIRKLKKESVVAFGGTVQESGKAPGGFEIIPSFLKVLNISKQPLPLDPTEKVKAEIDTRLDARFLDLRKPSVSAIFKIKSRMLHSVRVFLEEQGFLEINTPKLVASATEGGTELFPITYFEREAFLGQSPQLYKQIMMSTGLDRVYEIAPIFRAEEHDTLRHLNEVISIDIEASFVDHEDVMKILENLVVRVIEDVNEHCTDALETLGRTLEVPETPFERLEYDEAVEMVNSKGVPMKHGEDLPRAAEKALGEIMDGYYFITSWPTAIKPFYVMPDEDDPERSHAFDLMYRDLEISSGAMRVHQHDLLVEKIKRQGLNPDSFESYLSAFEYGMPPHAGWGLGAERFNMTLTGLKNIRETVLFPRDRRRLTP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
Length
436 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). This indicates that it is not able to differentiate between base C36 in the tRNA(Asp) anticodon (GUC) from base U36 in the tRNA(Asn) (anticodon GUU). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
49.038 kDa
Sequence
MLERTYIEDVTPDDDGEDTTIAGHVHELRDLGGILFVIVRDATGRLQVVAKEDDTPDLFETAEGLSSEDVVQVTGTLEASDQAPGGVELAPTELTVVSEATDVPSIEISKDVDADLSTRLDERHLDVRKPSTKAVFSLRSKAMGAMTDWFYDNRFEEVDTPELSTAGAEGGADLFPVVYYDKEAYLSQSPQLYKQILVASGVDRLFEVGHAFRAEDFGTSRHVSEIAMFDVELGYVEDHHDVMDVQEESLRHTIRHVVEHAQRELDELGSDLSVPEADFPRITFEEAREILADEYDHVPEDDNDLDTKGERLLGEYFEEQGHPAVFVVGYPDEKFYYRQDVDGDDVASRKFDLLYRGQELSSGGQREHDIERLTAKMREQGVEPENFEFYLDAFRYGVPPHGGYGLGIDRLIQQLAGLDNIKEAILFPRDPDRLEP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Haloquadratum walsbyi (strain DSM 16790 / HBSQ001)
Length
434 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
48.681 kDa
Sequence
MQDRTLTAEVTPGDEITVAGWVHEIRDLGGIAFLILRDRSGKIQIKFEKDEMNDEIVQTGLDVPRESVISITGVADDEPRAPTDVEIVPTAIEVLSSADTELPLDPSGKVNADLSTRLDNRTLDLRKKEVKAVFQIRSEVLRAARDAFRELGCTEINTPKIVATGTEGGTELFPITYFGEEAFMNQSPQLFKQLMIGSGLERVFEIGPIFRAEEHNTPRHLNEATSIDFESAFINHAEAMDACEYVVTAAYQGVAENCITELETLGLRDGFSVPDESFPRISYQEAIERINATGELDEQLVWGDDLPTDGERALGADVGSHYFITDWPSEIKPFYIKDHDDDKTLSTGFDMMHPQMELVSGGQREHRYEHLVSGFEQQGLDPEQFDYYTKMFRYGMPPHAGWGLGGERLVMTMLGLENIREAVLFPRDRQRLSP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)
Length
434 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
48.797 kDa
Sequence
MENRTYTADATPGDTVTVAGWVHEIRDLGGIAFLILRDTTGKIQVKFEKDEMDDDLVETGLNVQRESVISVTGAVEEEPRAPTGVEVTPESVDVISEADPELPLDPSGKVDAELPTRLDNRTLDLRKDEVKAIFEIRAEVLRSVREAFRELNCTEINTPKIVATGTEGGTELFPITYFGQEAFMNQSPQLFKQLMVGSGLERVFEIGPIFRAEEHNTPRHLNEATSIDFESAFYDHTEAMDACEHVVQSAYEGVAENCQDQLEALGLEDEFAAPEGDFPRLTYEEALDKINATGELDEPLVWGDDLSTEAEHVLGQEVGEHYFITDWPSEIKPFYIKDHDDDEEVSTGFDMMHPSMELVSGGQREHRFDHLVEGFEQQGLDPEAFEYYTKMFKYGMPPHAGWGLGGERLIMTMLGLENIREAVLFPRDRQRLSP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Haloferax volcanii
Length
433 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
48.691 kDa
Sequence
MRNRTYTADAEPGDTVTVAGWVHEVRDLGGIAFLILRDTSGKIQVKFEKDEMDDDLVETGLGVHRESVISVTGEVDEEPRAPTGVEVTPESLDVIAEAEAQLPLDPSGKVDAELSTRLDNRTLDLRKDEVKAIFEIRAEVQRAVRDKFRDLRATEINTPKIVATGTEGGTELFPITYFGQEAFMNQSPQLFKQLMVGSGLERVFEVGPIFRAEEHNTPRHLNEATSIDFESAFIDHTEAMDVCEAVVTAAYEAVEENCQDELEALGLEEEFERRPRVPAAHLRGGHRAHQRTGELDEQLVWGDDLPTEGEKALGEDVGEHYFITDWPSEIKPFYIKDHDDDETLSTGFDMMHPNMELVSGGQREHRFDHLVAGFEQQGLDPDAFEYYTKMFKYGMPPHAGFGLGGERLIMTMLGLENIREAVLFPRDRQRLSP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / NBRC 14720 / NCIMB 2260 / Gabara)
Length
433 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
48.479 kDa
Sequence
MENRTYTADAEPGETVTVAGWVHEVRDLGGIAFLILRDTTGQIQVKFEKDEMDDELVETGLNVARESVITVSGDVEEEPRAPTGVEVTPETVEVLSEADTELPLDPTGKVDAELSTRLDNRTLDLRSEEGQAIFEIRAEVLRAVREAFRDANATEINTSKIVATGTEGGTELFPITYFGEEAFMNQSPQLFKQLVAGSNIERVFEIGPIFRAEEHNTPRHLNEATSIDFEGAFCDHTDAMDVCEQVVTAAYEAVAENCTDQLEALGITEEFEVPETPFPRLSYEEAIERINATGELDEQLVWGDDLPTEGEKALGDDVGGHYFITDWPAEIKPFYIMDHEDGELSTGFDMMHPRMELVSGGQREHRREELIAGFEQQGLEPEAFEYYTKMFKYGMPPHAGWGLGGERLLMTMLDLDNIREAVLFPRDRQRLSP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Length
431 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
49.791 kDa
Sequence
MLKDAYTADVTPERDGEEVRLAGWVHEVRDLGGIKFVLLRDRTGIVQLTLPKQKVPKETFEKVPKLTKESVIRVEGTVQANEKAPGGVEVIPQRIEVLSESDTHLPLDPTGKVDADLDTRLDARVLDLRREEPQAIFKIRNVVTTAIREFLEERGFIEVHTPKIIASATEGGTELFPVVYFERDAYLAQSPQLYKQMLMAAGFERVYEIGPIFRAEEHNTRRHLNEAISVDIEMSFIESEEDVMRVLEELLAHVFRKVREECEKELEALDRELPELETPFERITYEETLDLLSEHGIEVEWGEDLPTEAERKLGEIFEEPFFITEWPRETRPFYTMAKDDEVTTAFDLMYQGLELASGAQREHRYDVLVRQIEEQGLSPEDFRHYLEAFKYGMPPHGGWGLGLERTLMTITGAENIREVTLFPRDRKRLHP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)
Length
430 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
49.499 kDa
Sequence
MRVYTADVKPEMEGQKVTLYGWVHEVRDLGGLVFILLRDREGIVQITLPRKFVSKQVFKLAKKIRRESVIAVTGEVRREEKAPGGVEIIPESIEVLNEADAPLPLEVTEKVPAELDTRLDHRFMDLRRPRVQAIFRIRHQVMQSVREFLSEEGFIEVHTPKIVSTATEGGTELFPISYFEKEAFLNQSPQLYKQVLMAAGFEKVFEIGPIFRAEEHNTTRHLNEAISIDIEMSFTDHNGVMDVLERLVQRVYEDVAEKCERYLGWLEVSLEIPELPFPRITYDEAREIAARKGEEIPWGEDLSTNALKLVGEEMGGLYFITDWPTESKPFYAMPYEDRPEISKSFDLMHGWLELSSGAQRIHLYDMLVESIKAKGMEPESFGFYLEAFRYGMPPHAGWGLGAERLIMSMLGLKNVREAVLFPRDRHRLVP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1)
Length
430 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
48.144 kDa
Sequence
MRVPINTITPDTPSAEVIGWAHEIRDLGGLAFLLIRDRTGIIQVTVPKKKVAPEIAETIRAISRESVVRVTGTVKPEGKAPGGRELIPDAIEIVSLSATPLPLDVAEKVPAELDTRLDNRFLDARRPRVSAIFKIRNAVQHATRNFFFENGFIEINTSKIVAAATEGGTELFPIAYFEKEAFLNQSPQLYKQMMMAAGFEKVYEIGPIFRAEEHNTTKHLNEATSIDIEVSFTDHLGVMQTLEDLIRDIYQFVDKTCSDAIADLGLDDFAVPEKGFPRLPYSEAIEIASATCEEDIAYGDDIGTAAERAIGEEMGRLYFIVDWPSSIRPYYAMPYENDPEICKAFDMMHPRMELSSGAQRVHQHDLLVEQIAKKGLNPENFEFYLNPFRFGMPPHAGWGLGAERLVTTMLGLPNVREAVLFPRDRHRVVP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z)
Length
429 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
48.293 kDa
Sequence
MRIPIKDVTPEIGHARIAGWVHEERDLGGLTFLLVRDRTGILQVTIPKKKVTPEVLAAVKEATRESVIECEGVVKATEKAPGGRELVPDMLRVVSRAETPLPLDVSEKVPAELDTRLDNRYLDLRKPRINAIFQIRNACLRAISEYLWDNGFTQVQTPKIVAAATEGGTELFPLAYFDKEAFLNQSPQLYKQMLMSAGFDRVFEIGAIFRAEEHNTVRHLNEATSIDIEMSFANEEDAMHVLENVVASAYQYVADHCGDALATLGITDFKVPTVPFPRITYKEAIEISTAGGEPLVFGDDLSTAAERIVGEKMGTMYFITEWPTSTRPFYTMPFEDRPEVCRAFDMMHPRMELTSGAQRCHIHSLLVEQIKAKGLNPDAFEFYLNPFRYGMPPHAGWGLGAERLVMTMLDLQNIREAVLFPRDRHRVSP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1)
Length
429 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
48.279 kDa
Sequence
MRLPIRAVTPETESAEIVGWVHEVRDLGGLSFFLIRDRTGIIQVTIPKKKVPAEILDTARSVSRESVVRVRGTVKAIEKAPGGREIVPEELEIISTAESPLPLDVAEKVSAEMDTRLDSRFLDARKPRVRAIFFIRSAVTCAATAFLASRGCINIATPKIVAAATEGGTELFPIAYFEKEAFMNQSPQLYKQMMMAAGFEAVFEIGPIFRAEEHNTVRHLNEATSLDVEVSFADHNDVMELLEDLIVHVYDHVAKDCSEHLAELEIDLKVPSKPFPRIPYAEAIEIANKTIEEKLAFGDDLSPAAERAIGDTVGQHYFIVDWPTDIRPYYAMPYPDRPEFCKAFDLMHPRMELSSGAQRIHDHDLLVERISAKGLSPESFEFYLKPFRYGMPPHAGWGLGIERLVMTMLDLPNIREAVLFPRDRHRLMP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Length
429 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
49.074 kDa
Sequence
MYRSHFIADVTPEYDGKEVIWAGWVHLLRDLGGKKFIILRDKTGLGQVVVDKNSSAFGISQELTQESVIQVRGIVKADKRAPRGIELHAEEITLLSKAKAPLPLDVSGKVKADIDTRLRERVLDLRRQEMQAVIKIQSLALKAFRETLYKEGFIEIFTPKIIASATEGGAQLFPVIYFGKEAFLAQSPQLYKELMAGVVERVFEVAPAWRAEESDTPFHLAEFISMDVEMAFADYNDVMQLLEKILHNIVKTIKEEGKEELKILNYEPPEVKIPIKRLKYTEAIEILRSKGYNIKFGDDIGTPELRILNEELKEDLYFIVDWPSDARPFYTKSKSENPELSESFDLIYKFLEIVSGSTRNHKREVLEEALKKKGLKPESFEFFLKWFDYGMPPHAGFGMGLARLMVMLTGIQSVKEIVPFPRDKKRLTP

Gene
aspS
Protein
Aspartate--tRNA(Asp/Asn) ligase
Organism
Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Length
429 amino acids
Function
Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
48.769 kDa
Sequence
MFRTHLVSELNPKLDGSEVKVAGWVHNVRNLGGKIFILLRDKSGIGQIVVEKGNNAYDKVINIGLESTIVVNGVVKADARAPNGVEVHAKDIEILSYARSPLPLDVTGKVKADIDTRLRERLLDLRRLEMQAVLKIQSVAVKSFRETLYKHGFVEVFTPKIIASATEGGAQLFPVLYFGKEAFLAQSPQLYKELLAGAIERVFEIAPAWRAEESDTPYHLSEFISMDVEMAFADYNDIMALIEQIIYNMINDVKRECENELKILNYTPPNVRIPIKKVSYSDAIELLKSKGVNIKFGDDIGTPELRVLYNELKEDLYFVTDWPWLSRPFYTKQKKDNPQLSESFDLIFRWLEIVSGSSRNHVKEVLENSLKVRGLNPESFEFFLKWFDYGMPPHAGFGMGLARVMLMLTGLQSVKEVVPFPRDKKRLTP

Gene
aspS
Protein
Aspartate--tRNA(Asp) ligase
Organism
Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1)
Length
428 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
49.308 kDa
Sequence
MPRVYIGSLRELNHNDNVEIYGWLQDLKLLKNVSFLIMRDRTGTVQVTFKNTPDIVNLLKELPRESVLKISGKINKKSVSKSGLEVSGESVEVLNRSERPLPLPVIDPVQADLETRLNNRFIDLRKRDVSSIFNAESSILWGIREFLHSQGFIEVHTPKIVAAATEGGADLFPVKYFENDAYLNQSPQLYKEILMSSGFEKVFEVGPAFRAEEHNTTRHLNEFTSIDIEMSFADHNDAMRILENAVKSGIENMINENGKDLQENGINISIPEIPFPRITYKECIKLLEKEGLEFQFGNDFSPEELRIIGRNFKDFYFITEWPSSLRPFYTMPNRDDPTITNSFDLQYREVEVTSGAQRVHDPDLLLKRFNEKKLNIDSFKFYIQAFKYGMPPHAGWGLGLERLTMIVLGLNNIRETTLFPRDRTRIIP

Gene
aspS
Protein
Aspartate--tRNA(Asp) ligase
Organism
Pyrobaculum aerophilum (strain ATCC 51768 / IM2 / DSM 7523 / JCM 9630 / NBRC 100827)
Length
428 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
49.083 kDa
Sequence
MYPKKTHWTAEITPNLHGTEVVVAGWVWELRDIGRVKFVVVRDREGFVQVTLKAGKTPDHLFKVFAELSREDVVVIKGIVEASKIAKSGVEIFPSEIWILNKAKPLPIDIWSETPDLATRLKWRSVDLKRPRNLVVFTVASAMLRSIREVLYGEGFVEVFTPKIIVTSTEGGAELFPVMYFERVAYLSQSPQLYKEQLTASLERVFEIGPAYRAEKHNTDYHLNEFISVDAEAAFMDYNDIMDILEKIMRRLASTVSEYAPKLEEVGIKALMELSNIPRVDYDEAVDRLRQLGYAVNWGDDFTVEMQKALMKYYGPVYFIVNFPASLRPFYTKRKDGEKSESYDLIINGIEVASGATRIHKRDELEEEMKKRGLDPRLFESHLSVFDYGMPPHAGFGLGFNRLVTALLGLDNVRHATLYPRDRYRVEP

Gene
aspS
Protein
Aspartate--tRNA(Asp) ligase
Organism
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
Length
428 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
48.976 kDa
Sequence
MPRTYIDTLRDHEDGAKVVVYGWMQEARIMKNISFLMIRDNTGTIQATFKNDEATLDIIKRINRESIVRVDGSVNKKSISKAGIEISGTSISIVNEAEAPLPLPVVDPVQADLETRLNSRFMDLRKRNISAIFRIESALLWGIRQYLHSQKFIEVHTPKIVAAATEGGSDLFPVRYFEKDAYLNQSPQLYKEVLMSAGFDRVFEVGPAFRAEEHNTTRHLNEFTSIDIEMSFADHNDAMAMLENAIRSGIENAVRENAEDFESLGISISVPETPFPRITYEQCIDLLQKDGIDFTFGDDFSPDQLRTIGSRFSGFYFITEWPSSVRPFYTMPKSEDPRLTNSFDLQYREIEVTSGAQRVHDPKMLIQRFNEKKLDVKSFQFYVDAFKYGMPPHAGWGLGLERLTMILLGLNNIRETTLFPRDRTRIVP

Gene
aspS
Protein
Aspartate--tRNA(Asp) ligase
Organism
Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828)
Length
423 amino acids
Function
Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp).
Similarity
Belongs to the class-II aminoacyl-tRNA synthetase family. Type 2 subfamily.
Mass
48.589 kDa
Sequence
MRNYIKDAADLDEVELSGWAEDIRRIKSIVFIILRDVTGRIQVTVKSENVKNFDEVYKINRESVLKVHGTVDHQSRSKSGIEIIADSVEILNAAEAPLPLGVVDKVQADLDTRLNNRYIDLRKDENLIIFKAQSTLLWGIREYLNRLGFIEVHTPKIVAAATEGGADLFPVKYFERDAYLNQSPQLYKEILMAAGFEKVFEVGPAFRAEKENTLRHLNEFTSIDIEMSFADHNDVMDVLENTVKNAINTLKNNLGDELNKHGFNIDSINGRIPRITYREAIDYLNSSGFQMNFGDDFSPEAARVLGERYKSFYFITEWPVSLRPFYTMKKDDETTKSFDLQLRELEICSGAQRIHRYDDLVNNIKNKGLNPESFTFYLSAFRYGMPPHAGWAIGLERLTMNLLGIKNVRETTLFPRDRTRLLP