TRM1

Tripartite terminase subunit 1

859 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

95.189 kDa

MPPAPKNGSAANAWRSERNARPREVWRAIVPKNLMADDTTRRLLAVAGQLQTLLFQIELLKRCDPEVLVKRALRAKIKHNALMVLYLHSRLAGDLAAQAAHRLTVGIYCLWMWLRRACSEAAALANEIDTYATYRDKDRFFSATMNLSPGGTCRLHSLVGLSLYGRTQDVTRELGLINDAENLLKQINYCHLIVSTESAEAALVGVDEFLTATVGGGMVASPETYDHTQPCCICLDELSVTANQGDTIYKRLGYSVCDHLVKQVKVNVTPDDVLRHMPFLNSVDANTLRGAIDKLRGSSGGEVGGGRRLAGVVPTGCRAEVGRSEQEDGAPAGDDRADLEHEARASRILDSYDVFTEAPGPVYRLSELRYWLASGKAAGAKTRGSCAHATHQATVLQKLDTDLSAMFARAETFERECRSAEREIFGTSFAHFHRHVASKIASVRGVGGGGEALIDKLLAGSPATAPEAEIETLISSCYSHHMSLPLFSRLGNPEKADTDALVEILKSYRDQTRPRADKAGGRAEDGAGDCDDEGYPGAADATRRGQRDWIGRVRVDTAAVADEHEDKVKKLLDRAERDLTTRRKNYAERLSARSFSNLDRCVKNQRAELEKLLRVNVYGAALPAMYVELKNGFLARQAFMKAVTSDESQHIRRCRLAREDVEGYEQHQYVRSALMRTSLDPAALPHLASRFYELVSGPMFRRHVERFPQPPNTSLYFTVENVGLLPHLKEELASFTRTYAHAEWMVSEFREFYDFSGISGVSETQRAAYAYIREAVFAAALFESIFQCGRAKLMRADSVEVDAGGPLLTDGIYLTFEERFPLIAIWGVGEDRRLCATSVVVTEKDLYAVLYAVLHKQDK

TRM1

Tripartite terminase subunit 1

850 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

95.868 kDa

MEMNLLQKLCVVCSKCNEYAMELECLKYCDPNVLLAESTPFKRNAAAIVYLYRKIYPEVVAQNRTQSSLLTLYLEMLLKALHEDTALLDRALMAYSRQPDRAAFYRTVLRLDRCDRHHTVELQFTDNVRFSVSLATLNDIERFLCKMNYVYGILAPEAGLEVCAQLLELLRRLCGISPVARQEVYVEGTTCAQCYEELTIIPNQGRSLNKRLQGLLCNHIAVHRPSSQSDVNIQTVEQDLLDLTTRIPHLAGVLSALKSLFSSSSAYHSYIQEAEEALREYNLFTDIPERIYSLSDFTYWSRTSEVIVKRVGITIQQLNVYHQLCRALMNGISRHLYGEDVEDIFVLGEKALDGEERMFVGSVFAAPNRIIDLITSLSIQAFEDNPVFNKLHESNEMYTKIKHILEEIRRPLPDGTGGDGPEGEAIHLRGREAMSGTGTTLMTASNSSNSSTHSQRNNGGGGRARGGGKKVVGGGVNGQDGDGSENGLRVRNCDEHEALDLVDARSRIHNVTREVNVRKRAYLQKVSEVGYGKVIRCIKTQERLTSKLIDVNLVGPLCLDFISKLMNGFLYRSQYHQDQDVVDVGDQFTYDEHLYVVNNLIHKSLPVESLPLLGQQIYELCNGPLFTHCTDRYPLSHNVDMAYACDNAGVLPHVKDDLVKCAEGTVYPSEWMVVKYMGFFNFSDCQDLNVLQKEMWMHVRELVLSVALYNETFGKQLSIACLRDELHPDRDVILTYNKEWPLLLRHEGSLYKSKDLYLLLYRHLSRPDESGDVPTAPVAKPSTLTAAAAVSGVFREPDRPWLPSPYPSSSTAGVSRRVRATRKRPRRASSLLDLARDEHGIQDLVPGSLR

TRM1

Tripartite terminase subunit 1

850 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

95.811 kDa

MEMNLLQKLCVVCSKCNEYAMELECLKYCDPNVLLAESTPFKRNAAAIVYLYRKIYPEVVAQNRTQSSLLTLYLEMLLKALHEDTALLDRALMAYSRQPDRAAFYRTVLRLDRCDRHHTVELQFTDNVRFSVSLATLNDIERFLCKMNYVYGILAPEAGLEVCAQLLELLRRLCGISPVARQEVYVEGTTCAQCYEELTIIPNQGRSLNKRLQGLLCNHIAVHRPSSQSDVNIQTVEQDLLDLTTRIPHLAGVLSALKSLFSSSSAYHSYIQEAEEALREYNLFTDIPERIYSLSDFTYWSRTSEVIVKRVGITIQQLNVYHQLCRALMNGISRHLYGEDVEDIFVLGEKALDGEERMFVGSVFAAPNRIIDLITSLSIQAFEDNPVFNKLHESNEMYTKIKHILEEIRRPLPDGTGGDGPEGEVIHLRGREAMSGTGTTLMTASNSSNSSTHSQRNNGGGGRARGGGKKAVGGGANGQDGDGSENGLRVRNCDEHEALDLVDARSRIHNVTREVNVRKRAYLQKVSEVGYGKVIRCIKTQERLTSKLIDVNLVGPLCLDFISKLMNGFLYRSQYHQDQDVVDVGNQFTYDEHLYVVNNLIHKSLPVESLPLLGQQIYELCNGPLFTHCTDRYPLSHNVDMAYACDNAGVLPHVKDDLVKCAEGTVYPSEWMVVKYMGFFNFSDCQDLNVLQKEMWMHVRELVLSVALYNETFGKQLSIACLRDELHPDRDVILTYNKEWPLLLRHEGSLYKSKDLYLLLYRHLSRPDESGDVPTAPVAKPSTLTAAAAVSGAFREPDRPWLPSPYPSSSTAGVSRRVRATRKRPRRASSLLDLARDEHGIQDLVPGSLR

TRM1

Tripartite terminase subunit 1

798 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

89.101 kDa

MAMNTLQKLCVVCSKCNECAMDVECLKYCDPNIVSMDSTAFRRNGVMVIHLYRTLYPALVSQNAVQTSVLTLYMEMLLQGLYDTMREIDMALTDFGTHRDRQRYYRRVLKLDSCNRHESITITFAPELALTIDLATLNDVERLLCKINCVYGAVDASQGVAVCRRLLSLLARLCDICPVAGPEIYRETVTCFQCYEELMAVPNQGRSINRRMQGLLCDHITIKKVLVQLDMDAQAVEQDMGDIAIRAPSVKGIIRAIKSLASFSPASYAYINDAEEALRGYNLFSEIPDRIYSLSDYTYWSKTSEAIVRHVGITMRQLNVSHSLWKTLRTELSRYHYGEDLEDVFTLGEGRFGGDERIYVGSIFAAPGKVVDMITSMSIKSFENNPLFNRLHESNEIYAKIKSLIEEIRGVGDGPAAGAARSRAEAASGAGAGGEEGAGAAAGRGNTGGDEGAGTTTAMSSALECGDPLLRVHDVNKEVNVRKRAYLKKVSEMGYNKVMACIRNQEHLVTKLVNVNLVGTVCLEAVSKIMNGFLSRQRSITEAETYPDVAESLGYDEHLYVINNLVHKRLPSELLPQLGQQIYRFINGPMFTHYLDRHPLPYNVNMAYACDNAGILPHVKEDLVRCADGTVVPSDWMTVGYMGFFRFADIRELNDLQKMVWAHIRELVLSVALYNETFGKQLALWRVEDGDEIGDGIILTYNPESPLILRRGDRSYRSRDLYLLLYKHLSVDSETLADAGSRASVADLCQVERPGPIAEQRSSTQNVKKKRKRMSLLELVRDVDGAGGDDLVPPCLYK

TRM1

Tripartite terminase subunit 1

793 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

90.142 kDa

MLGMSHNRLQSQGTEHDKFATQKLFAIWGQIQSYLFQVELLKRCDPTVGVRMINRLKLNVLMIYYLEKKMVPALKEQREMNLTPLTYGLWLALRRAKLEGELLLDALCEFKDGGNLRDFFRKSMSMCGDCPYHSTVELDTYGGKVSTEIKFLHDVENVLKQLNYCHLILKADTVENFMVSLDNYLLKTLGSGSVVPPELYDPSQPCSVCFEELCVTANSGDSTHKRIVRKICDHITKQINIRVNSDDMVTHLPHATYVPDDKRTTAQTALDVIQSTMRDTTTENDSNISVSKAAAAALDAHNVFLPASGDLYAISELQFWIASSGRKLHQPRGNTVESFADNLEALVSKERLFDLRTSIVETAVFDRRMDHFERVFAQEIEHMNAADRLLLGGRAAAPDDIIEALIKACYDHHMSAPLLKRLLYPDEAAHDALKTVLERVSSHCIGNDIQCQDGDGTCGERMNETGHFRTNDSFAMSTTSLGHDEWLEMVKSASSDVARRRKMYAERLTKKSLASLDKCITEQRHELEKMLRVNVYGEVLIDSYTALFNGFRSRKRLLEAVKNCCANIIDNRNSDDAFDAHRFMQTSLLKHRIDPAMLPSLTHKFFQLVNGPMFSHDRHRFAQPSNTALYFSVENVGLLPHLKEEMARFMFHSSRKTDWTVSKFRGFYDFSTIDNVTAAHRMAWKYIKELIFATALFSSVFKCGELHICRADSLQINSNGDYVWKNGIYITYETEYPLIMILGSESSTSETQNMTAIIDTDVFSLLYSILQYMAPVTADQVRVEQITNSHAPI

TRM1

Tripartite terminase subunit 1

785 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

85.578 kDa

MAAPVSEPTVARQKLLALLGQVQTYVFQIELLRRCDPHIGRGKLPQLKLNALQVRALRRRLRPGLEAQAGAFLTPLSVTLELLLEYAWREGERLLGSLETFATAGDVAAFFTETMGLARPCPYHQRVRLDTYGGTVHMELCFLHDVENFLKQLNYCHLITPSRGATAALERVREFMVGAVGSGLIVPPELSDPSHPCAVCFEELCVTANQGATIARRLADRICNHVTQQAQVRLDANELRRYLPHAAGLSDADRARALSVLDHALARTAGGDGQPHPSPENDSVRKEADALLEAHDVFQATTPGLYAISELRFWLASGDRAGQTTMDAFASNLTALARRELQQETAAVAVELALFGRRAEHFDRAFGSHLAALDMVDALIIGGQATSPDDQIEALIRACYDHHLTTPLLRRLVSPEQCDEEALRRVLARMGAGGAADAPKGGAGPDDDGDRVAVEEGARGLGAPGGGGEDEDRRRGPGGQGPETWGDIATQAAADVRERRRLYADRLTKRSLASLGRCVREQRGELEKMLRVSVHGEVLPATFAAVANGFAARARFCALTAGAGTVIDNRSAPGVFDAHRFMRASLLRHQVDPALLPSITHRFFELVNGPLFDHSTHSFAQPPNTALYYSVENVGLLPHLKEELARFIMGAGGSGADWAVSEFQRFYCFDGISGITPTQRAAWRYIRELIIATTLFASVYRCGELELRRPDCSRPTSEGRYRYPPGVYLTYDSDCPLVAIVESAPDGCIGPRSVVVYDRDVFSILYSVLQHLAPRLPDGGHDGPP

TRM1

Tripartite terminase subunit 1

785 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

85.608 kDa

MAAPVSEPTVARQKLLALLGQVQTYVFQIELLRRCDPHIGRGKLPQLKLNALQVRALRRRLRPGLEAQAGAFLTPLSVTLELLLEYAWREGERLLGSLETFATAGDVAAFFTETMGLARPCPYHQRVRLDTYGGTVHMELCFLHDVENFLKQLNYCHLITPSRGATAALERVREFMVGAVGSGLIVPPELSDPSHPCAVCFEELCVTANQGATIARRLADRICNHVTQQAQVRLDANELRRYLPHAAGLSDADRARALSVLDHALARTAGGDGQPHPSPENDSVRKEADALLEAHDVFQATTPGLYAISELRFWLASGDRAGQTTMDAFASNLTALARRELQQETAAVAVELALFGRRAEHFDRAFGSHLAALDMVDALIIGGQATSPDDQIEALIRACYDHHLTTPLLRRLVSPEQCDEEALRRVLARMGAGGAADAPKGGAGPDDDGDRVAVEEGTRGLGAPGGGGEDEDRRRGPGGQGPETWGDIATQAAADVRERRRLYADRLTKRSLASLGRCVREQRGELEKMLRVSVHGEVLPATFAAVANGFAARARFCALTAGAGTVIDNRSAPGVFDAHRFMRASLLRHQVDPALLPSITHRFFELVNGPLFDHSTHSFAQPPNTALYYSVENVGLLPHLKEELARFIMGAGGSGADWAVSEFQRFYCFDGISGITPTQRAAWRYIRELIIATTLFASVYRCGELELRRPDCSRPTSEGRYRYPPGVYLTYDSDCPLVAIVESAPDGCIGPRSVVVYDRDVFSILYSVLQHLAPRLPDGGHDGPP

TRM1

Tripartite terminase subunit 1

785 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

85.241 kDa

MAAAPPAAVSEPTAARQKLLALLGQVQTYVFQLELLRRCDPQIGLGKLAQLKLNALQVRVLRRHLRPGLEAQAAAFLTPLSVTLELLLEYAWREGERLLGHLETFATTGDVSAFFTETMGLARPCPYHQQIRLQTYGGDVRMELCFLHDVENFLKQLNYCHLITPPSGATAALERVREFMVAAVGSGLIVPPELSDPSHPCAVCFEELCVTANQGATIARRLADRICNHVTQQAQVRLDANELRRYLPHAAGLSDAARARALCVLDQALARTAAGGGARAGPPPADSSSVREEADALLEAHDVFQATTPGLYAISELRFWLASGDRARHSTMDAFADNLNALAQRELQQETAAVAVELALFGRRAEHFDRAFGGHLAALDMVDALIIGGQATSPDDQIEALIRACYDHHLTTPLLRRLVSPEQCDEEALRRVLARLGAGGATGGAEEEEPRAAAEEGGRRRGAGTPASEDGERGPEPGAQGPESWGDIATRAAADVRERRRLYADRLTKRSLASLGRCVREQRGELEKMLRVSVHGEVLPATFAAVANGFAARARFCALTAGAGTVIDNRAAPGVFDAHRFMRASLLRHQVDPALLPSITHRFFELVNGPLFDHSTHSFAQPPNTALYYSVENVGLLPHLKEELARFIMGAGGSGADWAVSEFQKFYCFDGVSGITPTQRAAWRYIRELIIATTLFASVYRCGELELRRPDCSRPTSEGLYRYPPGVYLTYNSDCPLVAIVESGPDGCIGPRSVVVYDRDVFSILYSVLQHLAPRLAGGGSDAPP

TRM1

Tripartite terminase subunit 1

782 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

87.393 kDa

MNTLQRLCVVCSKCNECAMELECLKYCDPAIVLVDSAPFKRNALTVVHLYRRLCPALAEQNARYQASLITLYLEMLLRCLYEDVLLVDEALGEFERHGDRQRYYRRVLRLDRCACHDTLEVTFTERIRLTVDVATLNEVERLLCKINCVYGVLEPTRGLELCRRLLSLMGRLCGISPVAAPEAYVENLTCLQCYEELAAVPNQGRSILKRLRGLLCDHLTVRKSLVQLETGIQTMEQDIVETVGSRPRLSSLLELLKGLSSSAAVSHAYISEAEDTLRRYNLFTDIPPRIYSLSDFTYWSKTSEVIVQRVNVTVQQLNMYHSLCRTLRNELGQYLYGDRVEDLFTLSEAQLGEDERLYVGSIYAAPERIVDLMTSLSLQSFENNPVFNKLHENNEIYSKIRSLLEEIRRPLDGAGTRGAAAATAAGARGAAEGTGGAAAAGGAAAAAGEAAGGPFQCGDPAARAHDVVREVHVRKKAYLQKVSELGYNRVMQCIKGQEKLIKKLVNVNLLGTVCFEVLAKVINGFIRRRAYLERVDGVVDVDRLLQYDDHLYVVNNLVHRRLPAESLPALGQEFYRFVNGPVFQHHADRYPLPYNIDMAYACDNAGMLPHLKEDLVRLAEGTVAPSEWMVAPYRRFFDLGAALDLNELQKGFWAHVREIVFSVALYNEAFGKELRLCRADEPVDEERERLVVTYNVDGPLFLYAGGGVWKSKDLYLLLYQHLNGAAAPPPPAAPSPPPAEPATTAGASRKRPAVESPGVLLDLVRDADRESSLVPDCLLYDP

TRM1

Tripartite terminase subunit 1

780 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

83.846 kDa

MAAPVSEPTVARQKLLALLGQVQTYVFQIELLRRCDPHIGRGNAPPTEAERASGAGAAASSEAGPGGPAGAFLTPLSVTLELLLEYAWREGERLLGSLETFATAGDVAVFFTETMGLARPCPYHQRVRLDTYGGTVHMELCFLHDVENFLKQLNYCHLITPSRGATALERVREFMVGAVGSGLIVPPELSDPSHPCAVCFEELCVTANQGATIAAAWRTVSVTTSPSRRRCGWTPTSVRRYLPHAAGLSDADRAGALRVGPCAGPDRGGRRAAPPVAENDSVRKEADALLEAHDVFQATTPGLYAISELRFWLASGDRAGQTTMDAFASNLTALARELQQETAAVAVELALFGRRAEHFDRAFGSHLAALDMVDALIIGGQATSPDDQIEALIRACYDHHLTTPLLRRLVSPEQCDEEALRRVLARMGAGAGGPKGGAGPDDDGDRVAVEEGARGLGAPGGGGEDEAPSPRARGTGPETWGDIATQAAADVRERRRLYADRLTKRSLASLGRCVREQRGELEKMLRVSVHGEVLPATFAAVANGFAARALLAALTAGAGTVIDNRSAPGVFDAHRFMRASLLRHQVDPALLPSITHRFFELVNGPLFDHSTHSFAQPPNTALYYSVENVGLLPHLKEELARFIMGAGGSGADWAVSEFQRFYCFDGISGITPTQRAAWRYIRELIIATTLFASVYRCGELELRRPDCSRPTSEGRYRYPPGVYLTYDSDCPLVAIVESAPDGCIGPRSVVVYDRDVFSILYSVLQHLAPRLPDGGHDGPP

TRM1

Tripartite terminase subunit 1

770 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

86.972 kDa

MELDINRTLLVLLGQVYTYIFQVELLRRCDPRVACRFLYRLAANCLTVRYLLKLFLRGFNTQLKFGNTPTVCALHWALCYVKGEGERLFELLQHFKTRFVYGETKDSNCIKDYFVSAFNLKTCQYHHELSLTTYGGYVSSEIQFLHDIENFLKQLNYCYIITSSREALNTLETVTRFMTDTIGSGLIPPVELFDPAHPCAICFEELCITANQGETLHRRLLGCICDHVTKQVRVNVDVDDIIRCLPYIPDVPDIKRQSAVEALRTLQTKTVVNPMGAKNDTFDQTYEIASTMLDSYNVFKPAPRCMYAISELKFWLTSNSTEGPQRTLDVFVDNLDVLNEHEKHAELTAVTVELALFGKTPIHFDRAFSEELGSLDAIDSILVGNRSSSPDSQIEALIKACYAHHLSSPLMRHISNPSHDNEAALRQLLERVGCEDDLTKEASDSATASECDLNDDSSITFAVHGWENLLSKAKIDAAERKRVYLEHLSKRSLTSLGRCIREQRQELEKTLRVNVYGEALLQTFVSMQNGFGARNVFLAKVSQAGCIIDNRIQEAAFDAHRFIRNTLVRHTVDAAMLPALTHKFFELVNGPLFNHDEHRFAQPPNTALFFTVENVGLFPHLKEELAKFMGGVVGSNWLLSPFRGFYCFSGVEGVTFAQRLAWKYIRELVFATTLFTSVFHCGEVRLCRVDRLGKDPRGCTSQPKGIGSSHGPLDGIYLTYEETCPLVAIIQSGETGIDQNTVVIYDSDVFSLLYTLMQRLAPDSTDPAFS

TRM1

Tripartite terminase subunit 1

766 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

84.384 kDa

MGSAQARQRLLAIFGQVQAYIFQVEMLKRCDPSALLPLVGSLKLNALTIRMLRRKLGGALIEQAQHQQTPLACALTMALEYAEVEGERVLRAVDDVNLAGPEGFFRATMRLDEPCEYHVRVHLDTYGGPIDAEVQFLHDAENFLKQLNYCHLITGFEAGLDALESVARFLTRTVGSGIVVPPELCDPTHPCSVCFEELCVTANQGEAVHRRLLECTCDHITRQMAVRVANIDIARHLPHALSVASERRAAAEAALRALEARRVQGHNGKSAGTEDPTQQVASRLLESHHVFKPASRCLYAVSELKFWLASTKHGDMGQPRAIDTFTENLETLDKQEKFFHLQAATVELALFGRTLDHFDRLFADQLLGLDVIDGMLVGSCAVSPDDHIEALIKACYTHHMSAPLLQRLTDPDTSNREALKQLLGRIGVDTDDGAGELGDALDVDLDNLGGAPPVNSTPCGEDALCRTVSEERPWDKLLERATADASQRRRMYAERLSKRSIASLGRCVREQRRELEKTLRVNVYGEVLLHTYVSSYNGFCARRGFCAAVSRAGTIIDNRSSTSAFDSHQFMKAALLRHPIDQSLMPSITHKFFELINGPVFDNAGHNFAQPPNTALYYSVENVGLLPHLKEELARFMITAAKGDWSISEFQRFYCFEGVTGVTATQRLAWKYIGELILAAAVFSSVFHCGEVRLLRADRTYPDSSGAQRCVSGIYITYEASCPLVAVLSAAPHGAIGAETVVIYDSDVFSLLYAVLQQLAPGSGAN

TRM1

Tripartite terminase subunit 1

766 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

84.384 kDa

MGSAQARQRLLAIFGQVQAYIFQVEMLKRCDPSALLPLVGSLKLNALTIRMLRRKLGGALIEQAQHQQTPLACALTMALEYAEVEGERVLRAVDDVNLAGPEGFFRATMRLDEPCEYHVRVHLDTYGGPIDAEVQFLHDAENFLKQLNYCHLITGFEAGLDALESVARFLTRTVGSGIVVPPELCDPTHPCSVCFEELCVTANQGEAVHRRLLECTCDHITRQMAVRVANIDIARHLPHALSVASERRAAAEAALRALEARRVQGHNGKSAGTEDPTQQVASRLLESHHVFKPASRCLYAVSELKFWLASTKHGDMGQPRAIDTFTENLETLDKQEKFFHLQAATVELALFGRTLDHFDRLFADQLLGLDVIDGMLVGSCAVSPDDHIEALIKACYTHHMSAPLLQRLTDPDTSNREALKQLLGRIGVDTDDGAGELGDALDVDLDNLGGAPPVNSTPCGEDALCRTVSEERPWDKLLERATADASQRRRMYAERLSKRSIASLGRCVREQRRELEKTLRVNVYGEVLLHTYVSSYNGFCARRGFCAAVSRAGTIIDNRSSTSAFDSHQFMKAALLRHPIDQSLMPSITHKFFELINGPVFDNAGHNFAQPPNTALYYSVENVGLLPHLKEELARFMITAAKGDWSISEFQRFYCFEGVTGVTATQRLAWKYIGELILAAAVFSSVFHCGEVRLLRADRTYPDSSGAQRCVSGIYITYEASCPLVAVLSAAPHGAIGAETVVIYDSDVFSLLYAVLQQLAPGSGAN

TRM1

Tripartite terminase subunit 1

766 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

84.41 kDa

MGSAQARQRLLAIFGQVQAYIFQVEMLKRCDPLALLPLVGSLKLNALTIRMLRRKLGGALIEQAQHQQTPLACALTMALEYAEVEGERVLRAVDDVNLAGPEGFFRATMRLDEPCEYHVRVHLDTYGGPIDAEVQFLHDAENFLKQLNYCHLITGFEAGLDALESVARFLTRTVGSGIVVPPELCDPTHPCSVCFEELCVTANQGEAVHRRLLECTCDHITRQMAVRVANIDIARHLPHALSVASERRAAAEAALRALEARRVQGHNGKSAGTEDPTQQVASRLLESHHVFKPASRCLYAVSELKFWLASTKHGDMGQPRAIDTFTENLETLDKQEKFFHLQAATVELALFGRTLDHFDRLFADQLLGLDVIDGMLVGSCAVSPDDHIEALIKACYTHHMSAPLLQRLTDPDTSNREALKQLLGRIGVDTDDGAGELGDALDVDLDNLGGAPPVNSTPCGEDALCRTVSEERPWDKLLERATADASQRRRMYAERLSKRSIASLGRCVREQRRELEKTLRVNVYGEVLLHTYVSSYNGFCARRGFCAAVSRAGTIIDNRSSTSAFDSHQFMKAALLRHPIDQSLMPSITHKFFELINGPVFDNAGHNFAQPPNTALYYSVENVGLLPHLKEELARFMITAAKGDWSISEFQRFYCFEGVTGVTATQRLAWKYIGELILAAAVFSSVFHCGEVRLLRADRTYPDSSGAQRCVSGIYITYEASCPLVAVLSAAPHGAIGAETVVIYDSDVFSLLYAVLQQLAPGSGAN

TRM1

Tripartite terminase subunit 1

728 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

79.676 kDa

MARELAAVYAQVFDLAAEVSLLGYCDPSSIDKRCVMANSNKVFKLCESLLPCLRLQNDTECSPLSLELQHLLQNTREALGVLTDLLSGDPSRSEYFEALHPSRPLEGPCKRHARVRVPFYGGAEKTVSLSLLNDVEVFFKRLNSVFYCLPAEGALEALGETVAFLGRLRGVSPIPPADAYVSSVPCASCFAEAAMLPNQGESVLSMLAAVNCNHVCRQVPSDPVIGVFENELRHLGADARAAGRAGGGRESERRGREDADDEEDDEEEPRDGQGDAGDGAALRVLTESSLSVLAGHTIFEEEDGRLAEISNLVYWSSAADRGGVGGTARATSSSHMAKLFAHEARMHRSRAWLGRGAPSHFFDAHRPSPLESLFCGGVFNSIDDTIAALQKDCSATFLKKSNYQTLIQQQNELYVRLNEVLNGAGRDEGGAKGAEAIADAEPLKPDGGASCDPRDVLSDARVRRDLYLKKLTRDGLRRLTDCIETHGRVLSDTLSLRVWGSALYASAARLVNHFLFRRQFVGLGWADLTAGGEAAFENSKYIKNALHGQRLNREHLDSIVVHFYRLITGPLSLQNSHFPVPDNVALAYCLDAAGAMPHQKLVITEMIWPGIESKDWIDCNFNSFYSIETGDLNLTQKKTLNYIREAVLSISLYNRVWEKSLSLLSATELRGSCLAESASGELGEGVYLTYEGTAPLVLVFDSKGYVFKDLYTLLYTHLQLSGRRQASV

TRM1

Tripartite terminase subunit 1

726 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

82.878 kDa

MNSLQSLCVLCARLNECALDLECLKFCDPVIVLSDMANFKKNGIVILHLYQTFFEGIKEQNLLCASALTVYMQVLLKAMYEQVLLLDAALESFMVDQDRKKYFEKVLCLRRCAETLSINISLNNGVEFIVQLSTLNDIEQLISKINSVYALLLPQEGLQICGKIIDLLTIMCGACMVAKPESYLETKTCMKCYEELTLTPNQGKSLRRRLHGKFCNHLTEQKAFFNIEKNIETIEKDLGEAILNYGTVQSVATEIKKIFKQQRSAESLHVSDAEKTLKKYNIFSKVPDVIYSLSEFTYWSKISETIVRNVAITLQQLNSCHTLYKQLQNDVSLYLYGEVSEDFLALSENLLTHDERLYVGSIYVSPSRLIDLVTGLSIKNLEESPIFKRLAEEDEVQHKIKSLLHDIRDPQTTETPGRLNTINCMLQTHNLQQEVLARKKAYFQKVSESGYNRVMACIREQESLINKVVSVNVYGNFIFEALSKIMNGFVLRKMYLDGSFRVDSCTYDEHLYIKNNLMPKKLPLELLPDLSEIMYTLLTGPLSDFHKSAYPLPANISMAYGCDHAEMLPHMKEDLARCIEGTIHPSVWMVCEYNEFFNFSGVTDVNDMQKKMWNFIRELTLSVALYNDVFGKRLKIVRIDEEGDLSGNVVLTFNHESPLLFHTGGGMTKFKDVYSLLYCDLQAQLSRETVDVPEGVSYSVRTPNLLDLVRENEQDGSIIPGCLFDE

TRM1

Tripartite terminase subunit 1

726 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

83.037 kDa

MNSLQSLCVLCARLNECALDLECLKFCDPVIVLSDMANFKKNGIVILHLYQTFFEGIKEQNLLCASALTVYMQVLLKAMYEQVLLLDAALESFMVDQDRKKYFEKVLCLKRCAEHLSINISLNNGVEFIVQLSTLNDIEQLISKINSVYALLLPQEGLQICGKIIDLLTIMCGACMVAKPESYLETKTCMKCYEELTLTPNQGKSLRKRLHGKFCNHLTEQKAFFNIEKNIETIEKDLGEAILNYGTIQSVVTEIKKIFKQQRSAESLHVSDAEKTLKKYNIFSKVPDVIYSLSEFTYWSKISETIVRNVAITLQQLNSCHTLYKQLQNDVSLYLYGEVSEDFLALSENLLTHDERLYVGSIYVSPSRLIDLVTGLSIKNLEESPIFKRLAEEDEVQHKIKSLLHDIRDPQTTETPGRLNTINCMLQTHNLQQEVLARKKAYFQKVSESGYNRVMACIREQESLINKVVSVNVYGNFIFEALSKIMNGFVLRKMYLDGSIRVDSCTYDEHLYIKNNLMPKKLPLELLPDLSEIMYTLLTGPLSDFHKSAYPLPANISMAYGCDHAEMLPHMKEDLARCIEGTIHPSVWMVCEYNEFFNFSGVTDVNDMQKKMWNFIRELTLSVALYNDVFGKRLKIVRIDEEEDLNGNVVLTFNHESPLLFHTGGGMTKFKDVYSLLYCDLQAQLSRETVDVPEGVSYSVRTPNLLDLVRENEQDESIIPGCLFDE

TRM1

Tripartite terminase subunit 1

724 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

78.882 kDa

MAERRLVAVLGQVQTYVFQLEMLKRCDPAVVRELAPRVKLNALMCRYLARRLPLEAQTTPLTCALRLALAYARAEGDRVLGALAAAGDDAEAYFERTMGGACRFHARVALDTYGGRVETELQFLHDAENLLKQLNYCHLITPHAVDLSAVDEFLARTIGGGLVVPPELYDPAQPCAVCFEELCVTANQGEATHRRLLGCVCDHLTRQLAVRVDPEDVAKNLPHVHGLDEARRGRALAALAAVDAAEAREAEAASTAAAGAEAGDAGETARRRADALLDAHDVFRPASRRLYAVSELQFWLASTNQAVRALDLFTHNLDDLERRERRAEVRAAAVELALFGRRPEHFDRARAARELDIIDGLLVGGCAASPDERLEALIRACYDHHMSTPMLRMLDPDRANRDALERLLEGGDDADADGGAAGGADAGDGGVGDEDGPGAPPPADAVAWADLPAAALRDAERRRRLYADRLSRRSAASLAQCVREQRRELEKTLRVNVYGDALLHTYVAVAAGFRARRAFCEAAARAGTVVDERETGCFDAHSFMKATVQRHPVDAALLPAVTRKFFELVNGPLFAHDTHAFAQPPNTALYFAVENVGLLPHLKEELARFMVARDWCVSEFRGFYRFQTAGVTATQRQAWRYIRELVLAVAVFRSVFHCGDVEVLRADRFAGRDGLYLTYEASCPLVAVFGAGPGGIGPGTTAVLASDVFGLLHTTLQLRGAPSR

TRM1

Tripartite terminase subunit 1

721 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

83.167 kDa

MNSLQSLCVLCSRLSECALELECLRFCDPVTLIPDMTNFRKNGVVIIHLFKTLFAELCHQNFNCASPVTIYLQILLKAMYNQVLLLDASIHQFLLDNDKQKYFENIFQLNECKQHLKLDLALNNYLTFSVDISTINDIEKLLCKMNCIFGLISPLDGINACSQIIEFLTILCGVCVVMKPEVFSETTTCLKCYEELSLVPNQGKSIRKRLAGKFCNHLTETHMVSNLEKNVDIIEKDLDFSTKQYGLVKEYMAKITNIFQQQLYSKPPHLQEAENTLINFDLFSKIPDTIYSLSEFTYWSKISESVIQKASITLNQLNLCHSLYADLQNEISKFLYGETIQDVFNFNEENVTNDDKLYIGSRFISPCRLVDIITNVSIKNLEEDPVFTKLAEEDEIQTKIKTLLNELENSAHETVPKKYVTHSMTQDHNLQQEIHIRKKAYYQKISESGYSKVMLCIKEQEALINKLMNINILGNHIFESLSKMMNAFANRQLQSLENFSADPFTYDDHLYIKNNLLSKKLPQELLPNLSQEMYRLLTGPLSNYHTASFPLSSNISMAYACDVADFLPHMKEDLAKCVEGTIYPENWMLCTYNKFFNFDGLHNINDMQRQMWNFIRELVLSVALYNDVFGKQLSIVKFGEETETVEKILLTFDSGSPLLFKRGTTTTKFNDLYSLLYFDLKTQCDPVQISQTKQVSHIPAPNLLDLCRQNENSIPECFYNF

TRM1

Tripartite terminase subunit 1

695 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

78.386 kDa

MAKELAAVYADVSALAMDLCLLSYADPATLDTKSLALTTGKFQSLHGTLLPLLRRQNAHECSGLSLELEHLLENVADALTTLGVCTSRKLSPEEHFSLLHLDITCNKHRSVRFNFYGNWALELKLSLINDVEIFFKRLSSVFYCIGSGSALEGLGEVLRFVGKLRGISPVPGPDLYVSNLPCLECLQEVCLTPNQGTSLQAMLPDTACSHICTPACGEPVRGLFENELKQLGLQTPESIPTTPCQSRVRQDDEIRQSSLMAVGDHHIFGEVTRSVLEISNLIYWSSGHSDATCDGDRDCSHLASLFTHEADMHKRRVDLAGCLGERGTPKHFFDCFRPDSLETLFCGGLFSSVEDTIESLQKDCSSAFYQQVNYTTALQKQNEFYVRLSKLLAAGQLNLGKCSTESCPSEARRQLVGGDKPEEVLRDAKHRQELYLQKVARDGFKKLSDCIRHQGHILSQTLGLRLWGSVIYNEASALQNHFLHRAQFISLPWQDLTVDCPTRFENSKYIKNSLYCQRLGREHVEILTLEFYKLITGPLSKRHTLFPSPPNVTLAQCFEAAGMLPHQKMMVSEMIWPSIEPKDWIEPNFNQFYSFENQDINHLQKRAWEYIRELVLSVSLYNRTWERELKILLTPQGSPGFKEPKPAGLTTGLYLTFETSAPLVLVDKKYGWIFKDLYALLYHHLQLSNHNDSQV

TRM1

Tripartite terminase subunit 1

692 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

80.149 kDa

MNKLQLLGVVFAKVNECSLELSCVRYCDPNLLLTKRKEFLHNAFVCKYLCDSLLSELQHFSCTNGLTACKHLAIILENLCEHFYVINKALCSFEIHKDHQQYYRTLFDVDQCSLHDPIKISFVNKQDLEITLTDFNEIERFLCKLNLIFPLIDARSGMRIISQIYDRLRKFTGISPLARLEFYKSACGGCYLCYEELQMTPNNGSSVQKRLNGVLCEHVTYTKDLVFQENEYLEVLREDLKRDNLLREDMRTELDDMKKILSNKKERGFYVPEAEQLLHRYDVFTDDIPNYIYTLSDLTYWSKTSEKIIKTMNMTMQQLNVYNNNMIKLKRSISRALNDIEVRDCFDVFEKVVDKRHCMFLGSMFTSSAKIISLLATQCLTAFEEKAVFERLNECDALCSTVNTILERLKSASGDGKEGITKQDFQADELIKGYNVSDEVSVRKKTYLNKVADKGYSKIVASLSTEERSIKKLIDINFLGTLCIDMMVKLEKMFYKRSQIGQMVENGVHLLALCNYDNHLYIRNNLSRQSISTENVNGVIQHILSFLCGPIFTHRHDIFPMPPNIDMAYACDNANVLPHRKEELMQCVNDITSVHGWSISSYNTFFKIDSVDLNTAHAHVWGYVKEFIVAVTLYNELYGQRLRAFRVDENTIRECGLYLTYNSDIPLVLKTDKNVIYGSDIYSILYAHMHHA

TRM1

Tripartite terminase subunit 1

685 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

74.764 kDa

MSGLLAAAYSQVYALAVELSVCTRLDPRSLDVAAVVRNAGLLAELEAILLPRLRRQNDRACSALSLELVHLLENSREASAALLAPGRKGTRVPPLRTPSVAYSVEFYGGHKVDVSLCLINDIEILMKRINSVFYCMSHTMGLESLERALDLLGRFRGVSPIPDPRLYITSVPCWRCVGELMVLPNHGNPSTAEGTHVSCNHLAVPVNPEPVSGLFENEVRQAGLGHLLEAEEKARPGGPEEGAVPGPGRPEAEGATRALDTYNVFSTVPPEVAELSELLYWNSGGHAIGATGQGEGGGHSRLSALFARERRLALVRGACEEALAGARLTHLFDAVAPGATERLFCGGVYSSSGDAVEALKADCAAAFTAHPQYRAILQKRNELYTRLNRAMQRLGRGEEEASRESPEVPRPAGAREPGPSGALSDALKRKEQYLRQVATEGLAKLQSCLAQQSETLTETLCLRVWGDVVYWELARMRNHFLYRRAFVSGPWEDRRAGEGAAFENSKYIKTHLFTQTLSSEHLHALTHSLYTFITGPLAEESGLFPPPSNVALARCCDAAGTLPHQKAFLTSLIWPGIEPSDWIETSFNSFYSVPGGSLASSQQILCRALREAVLTVSLYNKTWGRSLILRRADAVSPGQALPPDGLYLTYDSDRPLILLYKGRGWVFKDLYALLYLHLQMRDDSA

TRM1

Tripartite terminase subunit 1

680 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

77.179 kDa

MGQYLAALYSQIYGLCLDVSLVEFCKPTSLCLTKIADACNKVHKIHEYVSASLLQQNSLEACALSLELSHLLENLKTRLFFIYHALLDNPTYFSKLHSSVGLCDLHKKLNVQFYNECGIEVNLTLINDIERFLSRLNCVFYCLSSSSALLALKEALTFLGQLRGISPVPRTDIYITSSSCLECVLETSVVPNQGETLNELLLNHNCHHLVERVPPEPIKGLFESELQNLGLKVHIATDTIEQSVGKHEAVLQESLAYLKAHTIFNNTPKQVLELSNLLYWNSGQNQPSDSGVKCSELSKIWSRENELQKYRPKLNNGEPPGHFFDLHSPQGTELLFCGGIFSSTHDTITALKQDCSNTFMKQTRLTGVAKRQNELFMRLSNILYGEEVPTKPKQTESALKTCDQSDASKNQVLQEAELRKEAYLNKLSKEGFRKLQACLSTHEEMLNSQLSLKIWGSVVYKQSATLLNHFLFRQSWVTQASLPPSVNGSPEQFENSKFIKSSLYVKSLSREYLSTLRLHFFALITGPLTTQEGLFPSPPNVQLAHCLEAAHFMPHQKMLLNEMIKPTMEPQDWICSNFNEFYTIHETDLNGVQYECWKYLRELVLSVALYNITWEKNLCIYRTDHSCPTACSSGIKEGLYVTYESHAPLILVYSNKKWIFKDLYALLYAHMQLANNGAHR

TRM1

Tripartite terminase subunit 1

679 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

77.597 kDa

MAQHLAAVYSQIYGLTLDVSILTFVDPAHINWKTVTKNTEKINKIYLQIMPLLHNQNNIESTSLSVELQHLLHNLKIVLETFSAHLSDYNMYFENIHSLSAPCSRHKSIVFQFYNNCCVSVKMCIINDIEIFSKRLSSVFYCIRSCDALRGINHVIDFLGHLRGVSPIPLPDTYLSNIPCIYCLNEHMMLPNQGESLPSLMMCVNCKHVCKQLNPEPIQGMFENELLQRHIIVESNKQKEQNQTCSIDNQIRDASLSKLNQHTIFENISAPVLELSNLIYWSSGAHKKCANVENTSEMAKLLSYEAKMQNYRKYICKNSTHFFDKYKPYPIESIFCGGIFSSVDDTVKSLKSDCSLAFMKRANYQQLIKKQNELFVRLNKILQGEDTVSHAASAVPLSDKATIVNPDQVLHDAHARKDAYLQKVTKDGLKSLYTCLETQGAVLSNTLSMRVWGGAVYDEIVKLKNHFLFRDQFISLDWIHCETDSVTGFENSKYIKNLIYSQKLSSEHISSLTLQFYKLITGPLSQNVSFFPLPSNIALAHCLDAAGALPHHKLLLTEMIWPSIEPKDWVSQTYNKFYTITSTDLNSIQKEAWFFIRELVLSVSLYNEVLEKNLLVFSALNFEKNCVNLSPNQFCSGIYLTYEDSSPLIFVYENQGWVFKDLYALLYHHLQLSGKNHGT

TRM1

Tripartite terminase subunit 1

664 amino acids

Component of the molecular motor that translocates viral genomic DNA in empty capsid during DNA packaging. Forms a tripartite terminase complex together with TRM2 and TRM3 in the host cytoplasm. Once the complex reaches the host nucleus, it interacts with the capsid portal vertex. This portal forms a ring in which genomic DNA is translocated into the capsid. TRM1 carries an endonuclease activity that plays an important role for the cleavage of concatemeric viral DNA into unit length genomes.

Belongs to the herpesviridae TRM1 protein family.

72.368 kDa

MADAFDPSDTRPDELAAVARQKLLVVLGQLQTYIFQVELLKRCDPQVARHQIGKLKLNALQVRAVSRHFMEGMSSQAATLITPLTLALELSLEYARREGEKLLEALNDLGERSSPVAYFEGTMGLARGCPHHQAVKLATYGGEIDKELCFLHDVENFLKQMNYCHLITPASAAAEALVSVKAFLARTVGSELIVPPEISDPSHPCHVCFEELCVTANQGATASRRLAGKICDHVTQQARVRLDADEMRRNLPHVVGLSEARRARALHALEVSSKMTEANSGGPAEAPGPAAAQEREASALLDAHHVFKSAPPGLYAVSELRFWLSSGDRTSGSTVDAFADNLSALAERERRYETGAVAVELAAFGRRGEHFDRTFGDRVASLDMVDALFVGGQSAAPDDQIEALVRACYNHHLSAPVLRQLAGSEHGDAEALRSALEGLHAAEDPPGDGNAEKEARRAPSLGGGPEDDWAALAARAAADVGARRRLYADRLTKRSLASLGRCVREQRGELEKMLRVSTYGEVLPTVFAAVCNGFAARTRFCELTARAGTVIDNRGNPDTFDTHRFMRASLMRHRVDPALLPGITHQFFELVNGPLFDHATHGFAQPPNTALYFSVENVGLLPHLKEELARFMMGKADSDWAISEFQKFYHFDGTSGITPTQRIA

TRM1

tRNA (guanine(26)-N(2))-dimethyltransferase, mitochondrial

570 amino acids

Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups. Required for the modification of both mitochondrial and cytoplasmic tRNAs.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

64.052 kDa

MEGFFRIPLKRANLHGMLKAAISKIKANFTAYGAPRINIEDFNIVKEGKAEILFPKKETVFYNPIQQFNRDLSVTCIKAWDNLYGEECGQKRNNKKSKKKRCAETNDDSSKRQKMGNGSPKEAVGNSNRNEPYINILEALSATGLRAIRYAHEIPHVREVIANDLLPEAVESIKRNVEYNSVENIVKPNLDDANVLMYRNKATNNKFHVIDLDPYGTVTPFVDAAIQSIEEGGLMLVTCTDLSVLAGNGYPEKCFALYGGANMVSHESTHESALRLVLNLLKQTAAKYKKTVEPLLSLSIDFYVRVFVKVKTSPIEVKNVMSSTMTTYHCSRCGSYHNQPLGRISQREGRNNKTFTKYSVAQGPPVDTKCKFCEGTYHLAGPMYAGPLHNKEFIEEVLRINKEEHRDQDDTYGTRKRIEGMLSLAKNELSDSPFYFSPNHIASVIKLQVPPLKKVVAGLGSLGFECSLTHAQPSSLKTNAPWDAIWYVMQKCDDEKKDLSKMNPNTTGYKILSAMPGWLSGTVKSEYDSKLSFAPNEQSGNIEKLRKLKIVRYQENPTKNWGPKARPNTS

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

548 amino acids

Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

60.297 kDa

MYEANMLRLSQRISNAVNHFSTAMMSGASASLTEGSAIIPFSNPNEVFYNPVQQFNRDLSVTAIRAWSETRSKKIVAKSHHRHQLLDQNSELSQENLTKCDTTHDFEKNCSEKTDSTSADNIAGFTILEALSATGLRSIRYAKELPNVKRILANDLLENAVKTIEKNVNYNNVSDIVIPNKGDANAVMHMNKFHYDVIDLDPYGSAAPFLDAAVQSVSKDGLLCITCTDSAVLAGNAYPEKCFSNYGGSSLRSNFCHEQAVRHLLYAIAASAAKYGRAIKPLLSLSIDFYFRVFVQIKAKPVLVKNLQSQSLLIYHCSGCGSFAEQPLGKTSPGRLPGTTKFSNASGPPVSANCEHCGYVHHVGGPLWGGPLHDAEFLKKMRAIAEDLDPEVYGTKRRILGMLALADEELPDVPFYFVLSQICSVLRSQSPPQNIFVSALLNAGYRVSGSHAKSNAIKTNAPWSFVWDVLRSWIKDHPVKLENISKTSAGAAILEKTPTAEVDFTFRPDSEFASKKEGYTRYQMNPTENWGPKSKPGKRTIAEVDSKS

TRM1

tRNA (guanine(26)-N(2))-dimethyltransferase

432 amino acids

Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

48.235 kDa

MESKDGARETISEESTVITKNEWTFFNPAQKFNRDISIEVVKECFKDRASIRVLDAMSATGLRGIRYLKEIGNSIVYLNDISQSSVDTIRSNVLLNGIEDAEYFGSDLQGIKESGNARANVVKSDCNVLMTSLPCFFDVIDIDPFGSCSEYIDSALRAIRHKGILCLTATDKGVLCSNERKCLIKYSTSIMKGMGMNEVPLRTIVSLVSRQASKFDCSVEPVMSLSIDFYVRIFLRIVRRNPRSVVERNSHVLMCVCHNLAEIRSGQREIDSRCSNCSRRMRLCGPFWNGPLHDVKVIQGVLGGMNGGNKRLLGILRYLEQEIPTMFYYEIPRLCSLLGISTIKQSRLMHALANMGYQVSYTHSELNAIKTNAPIASINKVLILSGAGDQERMEELGVEFNGNEGVKALESIEFFKGLLKSGMGPLPLPRKH

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

407 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

43.643 kDa

MPVPSPMRLAVTHEGRSIIYIPSPEYAVASGRLEPAWLEVFYNPAMEFNRDVSVVAASALRRTGLLTRSGVAFDAHAGVGVRGVRYAVEAGYVKVIMNDINPKASMLAALNARANGLEPGSYMIFNKESNSLMFHLSRERPTPVSLIDIDPYGSPAPFVDAALALSGKGTVVAMTATDLAVLEGGKARAAVRRYMLRSVSKTPVSKETGLRVLLGYVARVAAAHDKAVKPLLAYYADHYYRVYVAVERGARRSDSMLEENLGRLVYCPETGVALALSYAEDPASACGGSYVVAADPAWIGSLGDQAFLEAMLNIAVEAVWLGTRPRVEKLLNTLHGEAPLSPRSIYVSLTSVASKARVNTPKKSKVVELLRSMGYRAVATHFSGEGVRTDAPWGEVLEAVVKLGSSG

trm1

tRNA (guanine(26)-N(2)/guanine(27)-N(2))-dimethyltransferase

392 amino acids

Dimethylates the guanine residues at position 26 and 27 of one or more tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

45.479 kDa

MEIVQEGIAKIIVPEIPKTVSSDMPVFYNPRMRVNRDLAVLGLEYLCKKLGRPVKVADPLSASGIRAIRFLLETSCVEKAYANDISSKAIEIMKENFKLNNIPEDRYEIHGMEANFFLRKEWGFGFDYVDLDPFGTPVPFIESVALSMKRGGILSLTATDTAPLSGTYPKTCMRRYMARPLRNEFKHEVGIRILIKKVIELAAQYDIAMIPIFAYSHLHYFKLFFVKERGVEKVDKLIEQFGYIQYCFNCMNREVVTDLYKFKEKCPHCGSKFHIGGPLWIGKLWDEEFTNFLYEEAQKREEIEKETKRILKLIKEESQLQTVGFYVLSKLAEKVKLPAQPPIRIAVKFFNGVRTHFVGDGFRTNLSFEEVMKKMEELKEKQKEFLEKKKQG

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

390 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

44.038 kDa

MDTHIIEEGLVKIEVPDFEKVSAKAPVFYNPVMEMNRDISVAVINQYRKEVDHDISICDAFGGTGIRGARYSKEIHGVEKVVVGDVNPLAVEISKKNMQLNNISNVEVQKNDANILLQSNKGLFDVVDIDPFGTPAMFTQSTAANIRPGGLICISATDTSALCGTYHDPCLRKYGAKPLKTEYCHENGIRILIAFISRNLAVNQKYLHVLFSHSTEHYMRVYAIVKRGGKKTNKALDNIGFIAHCPNCLHRETTYGFAPKIPHTCPECGGEYDVAGPLWLGKIWDKEFIYNTMELVKNLNLNKKDDLMSLFEKCYMEADGPVTFYDIHKICKKLKISSPKINDVMDEIRNRGYFISRTHFKLTGMRTDMPLDELKQLILDIKEDKLGPEK

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

388 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

42.51 kDa

MICRTIVEGTTKISVPIPPPDVNFPPSAAPVFYNPEMELNRDINVAATAAFVKRLLSRKDLKREEVRYVDAFSASGIRGLRIAGEVGIHSTMNDWNPEAFELIKENIKINGLEEKAQATRKNANVLLHEQKFHIVDVDPFGTPAPYLDAAATAAQGMLSVTATDTAPLCGAHLNSGIRKYAAVPLNTEYHSEMGLRVLLGACARECAKHEKGMLPLLSHVTRHYVRSYLEVLPGTKHADRALKSMGFSIYCPKCGFRGPVYGLAVHIEKECPACGALTKIAGPLWLGPFREPKFCNEVLSELEAHPLNTKEKAKKIITFCRDELDIPMFYDQHVICKELGASATGIETLIEALKAGGFEASRTHFSGTSFRTDAPIAEIKKIIQALSG

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

388 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

42.848 kDa

MIYKTIVEGTTKVSVPVPPPDATFPPSAAPVFYNPEMELNRDINVAATAAFVERLLAKKELLREEVRYVDAFSASGIRGLRIAGEVGIHATMNDWSPEAFELIKENSKINGLEENTLATRKSANVLLHEQKYHIVDIDPFGTPAPFLDAASASVRGMLSVTATDTAPLCGAHLKAGIRKYASVPLNTEYHSEMGLRVLLGACARELAKHEKGMLPLLSHVTRHYVRTYLEVLPGTKQTDRTLKSMGFSIHCPKCGFRGPVYGLAVHIEKECPVCGSFTQIAGPLWLGPFREQAFCDEVISELEMHPLNTKDKAKKIITFCRDELDIPMFYDQHVICKELGASATGIEILIEALKAHGFEASRTHFSGTSFRTDAPITEIKEIIRALSW

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

388 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

42.784 kDa

MICRTIVEGTTKISVPVPPPDANFPPSAAPVFYNPEMELNRDINVAATAAFVERLLSKKDILREEIRYVDAFSASGIRGLRIAGEVGIHSTMNDWSHEAFELIKENIKINGLEEKAQATRRNANVLLHEQRFHIVDVDPFGTPSPYLDAAASSAYSMLSVTATDTAPLCGAHLNSGIRKYASVPLNTEYHSEMGLRVLLGACARELAKHEKGMLPLLSHVTRHYVRTYLEVLPGSRKADKTLKSMGFVAHCPRCGFRKPVYGLAVHIEKECPECGGLTKIAGPLWLGPYREPEFCNEVISELEAHPLNTKEKVRKIITFCRDELDIPMFYDQHVICKELGASATGIESLIEALRAGGFEASRTHFTGTSFKTDAPIAEIKKIILALSG

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

388 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

44.101 kDa

MDEYKIKTVEEGLTKIQFPEFDKISSDAPVFYNPHMELNRDISILALQTFQKQEDRNINICDLFGGSGIRGVRYKNEIDGVGHVFINDISETANEYERHNVELNNLKDIEIFQHDASMFLRMHRGEFDVIDIDPFGTPSPFLDSAGYCSRRNSLLCVTATDTSALCGTYKEPCIRKYNAKPYKSEYCHETGIRILAGFVALTLAKYSKSIEVKLSHSTEHYMRLYIEVKKGSKKSDECLKNIGYLSHCKHCLYREENKGLATSTPDICPECGEKLIQAGPLWLGEIQNEEFISKMIVESENKKLNTKEDVLKLLESCRIEAKSPATFYDVHKICKILKISAPKLDLVFGNLEKEGFEAVKTHFNPLGIKTNAPLKKIKEIIKTLSSSN

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

386 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

42.463 kDa

MLSTKVTEGSTTVSVPVPPEGVPFPPSEAPVFYNPHMELNRDISVAATSACAKRILLKKDMELKDITYLDAMSASGIRGLRIANEVGITSILNDWSDDAYGLILENIGLTGVSDIAEATCKNANVLMHERRFNIVDLDPFGSPTPYLDAATRSAVHFLEVTATDTAPLCGAHFNSGMRKYAAVPLNNEFHSEMGVRILLGKIARELAKHDKGMTPLLSHATRHYVRTYLQVKKGAKLADKAFKDLGFLSHCEHCGHREIFHGMAISISDHCSSCGNDVYIAGPLWLGQLHEPQYCDEVLLELEDRSLGTKEQAKKLILACRDELDIPFFYDQHVICKMIGVSAPAMDMFIAALRETGANVSRTHFTGISFKTDAKIDTIKDVLRSL

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

385 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

42.328 kDa

MNITEGVVELTVPAARDGADAGVGDDVFYNPTQELNRDITVAALRAYQEREPRAETYLDAMTASGVRGVRAAASGYDVTCTDIDPDAVALAQSNLEKNDLDGQTLPSDANAVLHQSGPESPLGPEAIFDVVDLDPFGTPIPFADAAFANARNLVCVTATDTAPLCGAHQQSGIRTYSTLPRNTEYHPEMGLRVLLSALIRTAARYDTAAIPILSHVTRHYVRTYLELDTRATRADELLSDLGYVYHCEDCLTRQHEFGHIAHPPSMCHHCEGNRVITAGPLYLGSIREQGFTRRVRNHITTEMGEIKQADSILKMVENELETPTHYDQHRLCKKWTRSAIGMDEFIEQLHTAGFDATRTHYSGTAFKTNATIAEIRSATTDPDEQ

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

383 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

43.035 kDa

MELEIITEGRTPLKVPKTRGQPSARDPVFYNPAMQLSRDLTVSSLVQYGPKIVCDPLAGVGARGIRIAVELSPEVVVLNDLNPRAVELIEENVRLNDVEDVCRIENRDANALMHEDELAGRFDYVDIDPFGPPVPFLDAAVRTVRNRGVVGISATDVSALAGRYPRSARRKYWVEVERVEFYQEVAIRALISYIVRTCAKYDLAFEPHIAFFQRHHVRVIGEIRRGARRADRALKRLGYLLHCRECGYTSEREFDRECPRCGSGSVVRLGPLWLPDFADRERAERAASDARELGLEEAAELLETVAKETGTNPWAYDIHRWASRLGLSRVPSLTSVLEGLREEGFNAVRPHYSKRAVVKTDASPEEFEAVLTEVAGDSGCLHR

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

382 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

42.812 kDa

MKLTEVIEGKARLVIPDPSEFSREGKFDPAWSPVFYNPRMVFNRDVSVLAVSVISPPSVLDAMSATGVRGIRYVKESGVKGEVLFNDKNPVSVELISKNLELNGITGKVLRSDANSLMHQVKVGYTDLDPFGSPAPYLFSAISSLRRKGVLGVTATDLSALEGKSRTSSKRKYGVQGSRLSYSKEAGLRVLLGKIVKEASVQEKGIRPLMGFYHDYYYRLFVKMEDGAKRADRSLESLGTLYECDRCGYSFMSSDECERKCPVCGGELKYYGPAWIGEFNDLEFLKEMKNRLTEFSYLSNSVKISELLEYLERENRFGPYYRVDVLASRLKVNMPPMNSLLGCLGDAVRTHFDPRGFKSFREFSEILECVKGSSATYETSGR

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

382 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

43.464 kDa

MSLVEIIEGKARILIPNYKDYMKDGKFDPSWAPVFYNPKMILNRDLSVLAANVVKPKSLIDGLSATGVRGIRYGLEINGVEEIILNDIDSDAVELIKKNVKINDLESRAKIYNNNINSLLHEIKVDYVDIDPFGSPAPFLLSSFSAAKSKQYVAITATDLAALMCSSKTSARRKYGLICNKMSFSRELGLRGLISKAITEAAVVEKAVTPVFSFYNDYYYRVIFKVERGAKKVDRQLSKLVYYYECPKCGYRIESEYLQQMKCTNCNLVMQTYGPAYKESLVDYEFLNNMISELDKFSYFQTFSKLKSILLTIKDESKYSENYYRIDFLASLARVNVPRRDNVINCLVDASRTHLDPLGVKTSKNLDEIKECIKKLSSRNTS

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

381 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

41.113 kDa

MDIEEGGLTVSVPEARDGASEGTGGGVFFNPTQELNRDVTVAVLRAYRDREPRASSYLDAMAASGIRGVRAAAEGYDTTCADVDPDAVELAAENLAANDLDGETVHRDVNALLYENVFDVVDLDPYGTPIPFADAALANARNLVCVTATDTAPLCGAHLNSGIRKYGAVPRNTDYHPEMGLRTLISALVRTAARYDKAARPIVSHVSRHYARTYLELESGAQVADDCIDELGYIDNCEDCLWRDPTHGLIADPVDTCPVCGSDRVLTAGPLWLGPVADPDFARAVRERVTDDMGEAKRARKLLGTVARELDTPTHYDQHRLYKAWGEPAIGMDEFVDRLRGAGYEASRAHYRGTAVKSTASIPEMRDAILGNEGDADGDAD

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

381 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

43.319 kDa

MSMELFEVHEGKAKVLVPKAKTIYDSPVFYNPRMAPNRDVVVLLLNVLKPKIVLDALSATGIRGIRFALETPAEEIWMNDINELAYELMKKNVLLNFKGTLKENAKRAIFEGEKTIVINNDDANRLMAEKHRYFHFIDLDPFGSPMEFLDTALRSVKRKGILGVTATDGAPLCGAHPKACLRKYLAVPLRGELCHEVGTRILVGVIARYAAKYDLGMEVLLAYYKDHYFRAFVKLKDGAKKGDETLENLGYVYFDEKTGRFEVEKSFLSTRPNAYGPLWLGPLKNEKVVGEMLELLVSGFEVANYREVLKLLHMLHEELDIPLFYDTHALGKRLKIEPKKLGEIIKELKSMGYEATRTHFSPTGIKTNAPYEVFVEVMRKN

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

381 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

43.271 kDa

MVNLELIEVQEGKAKILIPKAESIYDSPVFYNPRMALNRDIVVVLLNILNPKIVLDALSATGIRGIRFALETPAEEVWLNDISEDAYELMKRNVMLNFDGELRESKGRAILKGEKTIVINHDDANRLMAERHRYFHFIDLDPFGSPMEFLDTALRSAKRRGILGVTATDGAPLCGAHPRACLRKYLAVPLRGELCHEVGTRILVGVIARYAAKYDLGIDVILAYYKDHYFRAFVKLKDGARKGDETLEKLGYIYFDDKTGKFELEQGFLPTRPNAYGPVWLGPLKDEKIVSKMVKEAESLSLARKKQALKLLKMIDQELDIPLFYDTHAIGRRLKIETKKVEEIISALREQGYEATRTHFSPTGIKTSAPYEVFIETIKRI

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

380 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

41.679 kDa

MITVNEGSVTIRVPDFSKVSARAPVFYNPAMEFNRDVSVVALQVFQRLLGGEISVADTFSGSGIRAIRYLVEVEGVSEAFANDINPLAVECIKNNSVINSVSPEVSREDASIFLRSNHGRFDVIDIDPFGTPAPFMDSAAASARNNSLLAVTATDTSSLCGTYIKPCLRKYSSRPLKTEYCHETGLRILAGFTAMNLARYRKAASVLLSHSSQHYMRLYIRVRRGARRADESIRNIGFMLHCFRCLHHEHVNGFAPLKRECPHCGAEMDVAGPLWVGDIQDSKFIGEMIGEVENKELNTAGDVLKLLKGCLDEAGMPPGFYDIHEVCSKLGRSAPPLRDVMDGLEAAGFRVSRTHIRPTGIRTDAGIGEIEEVLAGLMPE

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

379 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

42.751 kDa

MECREITEGSTTFTAPVQDETTQFPPGSAPVFYNTKMEFNRDMTVLLTKIVQPEDYLDAMAATGVRGLRIANEAKIPVTINDRDEQAVKIIKYNAEKLGGDISVTCDDANRLMCTSRFDSIDLDPFGTPVPFLDAASRAAKHYLFVTATDTAPLCGAHFKAGCRRYFATPRNTEYHAEVGLRMMMGTMARELVKYDRGMKPILSYAKSHYFRSHVRVLGKVTAADETLAQIGFVMQCPKCLYREEQKGSLYPKMHICPHCGVETVPVGPLWMGPLQEKEILAEMQTALAELQFGTKRQMEKMLTFLLAEPETCTYYDYHIISRNMKVSPPNMEELIASLNEAGYYTTRTHFCDTGIKTTAPLPLIEEKIRLWNAKNLQM

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

379 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

42.792 kDa

MELVEVLEGKAKILTPKAESIYDAPVFYNPRMALNRDIAVVLLNVLKPRIVLDALSATGIRGIRFALETPAEEIWMNDISEDAYNLMKKNVLLNFKGELEESNGRAVLKSEKTLVVNHDDANRLMAEKHRYFHFIDLDPFGSPMEFLDTALRSVKRKGILGITATDGAPLCGAHPKACMRKYLAVPLRGELCHEVGTRILVGVVARYAAKYDLGIEVILAYYKDHYFRAFIKLKDGARKGDESLENLGYIYFDESTGKFEVERSFLPSKPNAYGPVWLGPLKSQEIVEEMLEISQQLSLARKKQAVKLLKILKDELDVPLFYDTHGLGRRLKIEARKIEEIINELRSLGYRASRTHFSPTGVKTDAPYEVFVNVLSSAK

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

378 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

43.071 kDa

MELVEIREGLARVLVPKAERIYDAPVFYNPVMALNRDISVLAVKALSPRRVLDALSATGIRGLRYSLETSAEEVWMNDINEDAFRLILKNLELNFGSKPVLANGRAELGLPEKRLVVNLGDANKLMSENFRYFDFIDLDPFGSPVEFLDSALRSVRRRGFLGLTATDTGVLCGAYRRACRRKYLAEPIRGELCHEAGLRILIGTIVRYAAKYDLGVEVLLAYYRDHYFRVFLRLRSGAKKADESVELLGYLWQDETGKFKYERDFLPGKRGAYGPMWLGPLKNQAFLEELVRLTKTSEESISHRKTFQFLSLLVEELDVPFHYDTHALARKNGLEVVKISRVIETLHSLGFEATRTHFSPTSIKTNAPFDVVLRSMRK

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

378 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

42.874 kDa

MKLKEVTEGKVRIFVPDPTGYMVEGKFDPSWAPVFYNPKMTFNRDLSVIVVSILKPKIIVDALSATGIRGIRYYVESWKSEQLILNDKNPNATSLIQINAKNNGIENAKIYNKDANALLYEVKSDYIDIDPFGSPAPFILSSLNAATRNGIVAFTATDLSPLEGSSPTSCRRKYDAINHKLSSSKELGLRVLIGKIIREAAILEKTVYPLFSFYADYYYRLFVRVENGARKADDNINKHLKYFGECPRCGFQTFVEENCKTKCPVCGEIFSIIGPLYIGPLYSMEFLKRIMDLYSNFNYLTSFNRIQKLLNVIEKEARFKNVFYNISKLASKLKISAIPPIESILECLGDASRTHFAPTGIRTDKEYEEITKCIKSLR

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

378 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

42.874 kDa

MKLKEVTEGKVRIFVPDPKEYMIEGKFDPSWAPVFYNPKMTFNRDLSVIVVSLLKPKIILDALSATGIRGIRYYVESWKSEQLILNDKNSTAASLIQINVKNNGIENAKIFNKDANALLYEIKSEYIDIDPFGSPVPFILSSINATIRNGIAAFTATDLSPLEGSSRTSCRRKYDAINYKLSSSKELGLRILIGKIIREAATLEKTVHPLFSFYADYYYRLFVIVESGARKADENINKNLKYFGECPRCGFQTFVDENCKTKCPICGENFIIIGPLYIGPLHNMEFLKRMIDTYSDFNYLSSFNRIQKLLNVIEKEAKYKSVFYNISKLASKLKVSAIPPIDSILECLGDASKTHFAPTGIRTDKGYEEIIRCVKSLR

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

378 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

42.918 kDa

MKLKEVTEGKVRIFVPDPKEYMIEGKFDPSWAPVFYNPKMTFNRDLSVIVVSLLKPKIILDALSATGIRGIRYYVESWKSEQLILNDKNSTAASLIQINVKNNGIENAKIYNKDANALLYEIKSEYIDIDPFGSPVPFILSSINATIRNGIVAFTATDLSPLEGSSRTSCRRKYDAINYKLSSSKELGLRILIGKIIREAATLEKTVHPLFSFYADYYYRLFVIVESGARKADENINKNLKYFGECPRCGFQTFVDENCKTKCPICGENFIIIGPLYIGPLHNMEFLKRMIDTYSDFNYLSSFNRIQKLLNVIEKEAKYKSVFYNISKLASKLKVSAIPPIDSILECLGDASKTHFAPTGIRTDKGYEEIIRCVKSLR

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

378 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

42.904 kDa

MKLKEVTEGKVRIFVPDPKEYMIEGKFDPSWAPVFYNPKMTFNRDLSVIVVSLLKPKIILDALSATGIRGIRYYVESWKSEQLILNDKNSTAASLIQINVKNNGIENAKIYNKDANALLYEIKSEYIDIDPFGSPVPFILSSVNATIRNGIVAFTATDLSPLEGSSRTSCRRKYDAINYKLSSSKELGLRILIGKIIREAATLEKTVHPLFSFYADYYYRLFVIVESGARKADENINKNLKYFGECPRCGFQTFVDENCKTKCPICGENFIIIGPLYIGPLHNMEFLKRMIDTYSDFNYLSSFNRIQKLLNVIEKEAKYKSVFYNISKLASKLKVSAIPPIDSILECLGDASKTHFAPTGIRTDKGYEEIIRCVKSLR

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

378 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

42.918 kDa

MKLKEVTEGKVRIFVPDPKEYMIEGKFDPSWAPVFYNPKMTFNRDLSVIVVSLLKPKIILDALSATGIRGIRYYVESWKSEQLILNDKNSTAASLIQINVKNNGIENAKIYNKDANALLYEIKSEYIDIDPFGSPVPFILSSINATIRNGIVAFTATDLSPLEGSSRTSCRRKYDAINYKLSSSKELGLRILIGKIIREAATLEKTVHPLFSFYADYYYRLFVIVESGARKADENINKNLKYFGECPRCGFQTFVDENCKTKCPICGENFIIIGPLYIGPLHNMEFLKRMIDTYSDFNYLSSFNRIQKLLNVIEKEAKYKSVFYNISKLASKLKVSAIPPIDSILECLGDASKTHFAPTGIRTDKGYEEIIRCVKSLR

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

378 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

42.876 kDa

MKLKEVTEGKVRIFVPDPKEYMIEGKFDPSWAPVFYNPKMTFNRDLSVIVVSLLKPKIILDALSATGIRGIRYYVESWKSEQLILNDKNSTAASLIQINVKNNGIENAKIYNKDANALLYEIKSEYIDIDPFGSPVPFILSSVNATIRNGIVAFTATDLSPLEGSSRTSCRRKYDAINYKLSSSKELGLRILIGKIIREAATLEKTVHPLFSFYADYYYRLFAIVESGARKADENINKNLKYFGECPRCGFQTFVDENCKTKCPICGENFIIIGPLYIGPLHNMEFLKRMIDTYSDFNYLSSFNRIQKLLNVIEKEAKYKSVFYNISKLASKLKVSAIPPIDSILECLGDASKTHFAPTGIRTDKGYEEIIRCVKSLR

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

378 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

42.876 kDa

MKLKEVTEGKVRIFVPDPKEYMIEGKFDPSWAPVFYNPKMTFNRDLSVIVVSLLKPKIILDALSATGIRGIRYYVESWKSEQLILNDKNSTAASLIQINVKNNGIENAKIYNKDANALLYEIKSEYIDIDPFGSPVPFILSSVNATIRNGIVAFTATDLSPLEGSSRTSCRRKYDAINYKLSSSKELGLRILIGKIIREAATLEKTVHPLFSFYADYYYRLFAIVESGARKADENINKNLKYFGECPRCGFQTFVDENCKTKCPICGENFIIIGPLYIGPLHNMEFLKRMIDTYSDFNYLSSFNRIQKLLNVIEKEAKYKSVFYNISKLASKLKVSAIPPIDSILECLGDASKTHFAPTGIRTDKGYEEIIRCVKSLR

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

377 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

42.632 kDa

MELKEVREGLARILVPKAERIYDAPVFYNPLMALNRDISVLALKALGSRRVLDALSATGIRGIRYALETPAGEIWLNDINPNAFRLIVDNVKLNFSGELEIEGKMAVLEGEKTLVVTNADANRLMNEQFRYFDFVDLDPFGSPMEFLDSALRAVKRRGVLAITATDTGVLCGAYRNACLRKYLAEPIRGELCHEAGLRILIGTLVRYAAKYDLGVEVLLAYYRDHYFRAFLQLRNGAKTADKSMKQLGYLYQDESGKFEFENTFLPSKATAHGPLWLGPLKNQEFVEELHRLSAEHPLGSKKTQKFLGLLKDELEVPFFYDTHAVARRHGLEVRKLAGVIEILYEKGYKATRTHFSPTALKTDAPFEEVLEALRELQ

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

376 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

42.04 kDa

MELVAVKEGLARILVPKAERIYDAPVFYNPVMSLNRDISVLAVKVLGPKRVLDALSATGIRGIRYALETPAEEVWLNDISEEAYGLMKKNASLNIDGELYEEGDRSYLWGEKLVVINKGDANRLMAENFRYFDFLDLDPFGSPVEFLDTALRSVRRNGVLAVTATDTGVLCGAYRNACLRKYLAEPIRGPLCHEAGLRILIGTVVRYAAKYDLGVEVLLAYHRDHYFRAFLKLKSGAKKADKSLSQLGFLWADKSGRFEYRRGFLPDKPGASGPLWLGPLKDESFVEELLESARDHPLAHKKTLSFLQLISEELDVPFHYDTHTLARACSLTPPKLDVIIQRLRELGHSATKTHFSPTSVKTDAPFGVVAEVMKNV

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

375 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

42.201 kDa

MKYITEGNTKLKIPEDATISKKDKIFYNPIMEVNRDISVSIVQSFLNKYDRDEFFICDPLGGSGARGLRYANELKINSGTGAPHITIGDINPNAISLAQENAKLNNLNNVNIVHKDANVLLSENFRKFNVVDIDPFGAPSPYLDSAIRSIITKNGILCMTATDTAVLYGSYRKTCIRNYDATPLKGNKELAIRLLVGHAIRMASKYDIGLKPIFSHFTAHYVRTFLMTERGAKKADEAVDKLGYVKNIEEEYIIKSRKEGNSDGFCGLYYLDNLTDENITKDAIKIAEERNYSKESVKVMKTVYEESLINNVGCYDVHKICKNIKKKVPPVDILMSGLNEMGFNACRTHHNPHSIKSDAKLIDIVEFIYKYDGNK

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

374 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

40.934 kDa

MDVIEATEGTTTFLVPVQDSTGQFPPGTAPVFFNRRMELNRDATVLLLSVLQPSDYLDAMGATGVRGLRVAHEVGIPVTINDRDPEAIPLIRENVARLGLPVTVTCRDACSLLFEQAFDAVDIDPFGTPAPFTDAGIRGTRRFLLLTATDTAPLCGAHLKAGIRRYFARPGNTGYHGEVGLRILLGFVARETVKYDRGIEPLFCFAREHFVRLNLRLTRGPKAADRTIERLGFILQCPTCAYREELPGMFPPAATCPFCGKPLRPIGPLFLGAISSDEILGQMQARLPSCGLGTQKELEKLLTTCREELPTSSHYDYHRVAQQLVVSPPKIETLLEALRSAGFDASRTHYSGTGVKTNAPLPVLYDAIRGKNEP

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

374 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

42.588 kDa

MILKEGEVVFEVPDKLTVTKKDEVFYNPRMKTCRDISIAVIQAFLNLYHKRDKFYIADALAGSGIRGLRYAKELEFNGELKVFLNDINPKAYEKIINNAKLNEIENIDVFNEDANTFLSKHFRFFNVVDIDPFGSPAPYVEQAIRALVTRNGLLCLTATDTAALCGRSKKSCLRKYLAYPLFGRDCHEFALRVLVGYVMRMATKYELALKPVFCHATDHYVRVYLVTDRGAKRADKVFEMLGYVKDVNGIKIIKKFEEGYEKGFAGPLYIGNLYDKALVEEALKIAEKREFSERVLKILNAIKGESAINQVGCYDTHQIGKMLKISVPPMQDIINKLKEMGFNAVVTHYNPKGIKTDATLKNVIEAIYQCTKIR

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

374 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

43.333 kDa

MNLIEIREGKASLLIPNPKDYEKEGRYDPSWSPVFYNPKMRLNRDISVLALSVIKPKSVVDALSASGVRGIRYYTEIGGIEKLILNDKNPIATELIKKNAEKNYVNARITTKDANSLLYEIKADFVDIDPFGSPAPFILSAINATINKGYVAFTATDLSALECSSKFSARRKYDLICERLSFSKELGIRGLIAKVIREGAIIEKAAYPIFSFYFDYYYRVFFRIENGAKKVDKLLEKQGYYYECSKCGYREVDYYAERKICPRCGIEMRRYGPAWTGELWNREFLLSMKENLKNFTYFDTFMQVNKLLNILVEESKYVSPYFRLDFIASLIKRNIPKREKMLECLKEASITHFDYRGIKTNKEIDEIVNCIKIN

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

373 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

41.842 kDa

MKIISEGETKLMVPEESTLSKKDTVFYNPVMETNRNISVSVVQSFLDNFKRDEFLMCDPLGGSGARGIRYANELEFNGDLKVSIGDINPSAVKMIKENLKLNELENVEVFHEDANVLLSKNFKVFNVVDLDPFGSPVPYLDSGIRASLTKGGLLCMTATDTAVLCGAYRKTCIRKYNAIPLKGDKELAVRLMIGYAVKMASKYDIGLKPIFSHVTDHYARTFMVTERGAGKADSAIENLGYIRQDSEQKSFKAFEEGYEKGYAGSFYLGEISDKDIVQNSLETAKNRNYSKRAVDILELISKESEIEQVGCFDIHELCSFIKKLVPPVNDIMDNLKENGFKVSRVHYNPYGLKTDAELSDLVVLISEYHSKKY

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

373 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

41.928 kDa

MKIISEGETKLMVPEESTLSKKDTVFYNPMMETNRDISVSVVQSFLDNFNRDEFLMCDPLGGSGARGIRYANELKFNGDLKVSIGDINPSAVKMIKENLKLNELENVEVFHEDANVLLSKNFKIFNVVDLDPFGSPVPYLDSGIRASLTKGGLLCMTATDTAVLCGAYRKTCIRKYNAIPLKGDKELAVRLMIGYAVKMASKYDIGLKPIFSHVTDHYARTFMVTERGAGKADSAIENLGYIRQDSEQKSFKSFEEGYEKGYTGPFYLGEISDNDIVQNSLETAKNRNYSKRAVDILELISKESKIEQVGCFDIHELCSFIKKLVPPVNDIMKNLKENGFKVSRVHYNPYGLKTDAELSDLVVLISEYHSKKY

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

373 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

41.936 kDa

MKIISEGETKLMVPEESTLSKKDTVFYNPVMETNRDISVSVVQSFLDNFKRDEFLMCDPLGGSGARGIRYANELKFNGELKVSIGDINPSAVKMIKENLKLNELENVEVFHEDANVLLSKNFKIFNVVDLDPFGSPVPYLDSGIRASLTKGGLLCMTATDTAVLCGAYRKTCIRKYNAIPLKGDKELAVRLMIGYAVKMASKYDIGLKPIFSHVTDHYARTFMVTERGAGKADSAIENLGYIRQDSEQKSFKTFEEGYEKGYAGPFYLGEISDKNIVQNSLETAKNRNYSKRAIDILELISKESKIEQVGCFDIHELCSFIKKLVPPVNDIMENLKENGFKVSRVHYNPYGLKTDAELSDLVVLISEYHSKKY

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

373 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

41.82 kDa

MKIISEGETKLMVPEESTLSKKDTVFYNPVMETNRDISVSVVQSFLDDFKRDEFLMCDPLGGSGARGIRYAKELKFNGDLKVSIGDINPSAVKMIKENLKLNELENVEVFHEDANVLLSKNFKVFNVVDLDPFGSPVPYLDSGIRASLTKGGLLCMTATDTAVLCGAYRKTCIRKYNAVPLKGDKELAVRLMIGYAVKMASKYDIGLKPIFSHVTDHYARTFMVTERGAGKADSAIENLGYIRQDSEQKSFKTFEEGSEKGYAGPFYLGEISDKNIVQNALNTAKTRNYSKRAVNILEMISRESEINQVGCFDIHELCSFIKKLVPPVNDIMENLKENGFKVTRVHYNPYGLKTDAELSDLVVLISEYHSKKY

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

373 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

41.82 kDa

MKIISEGETKLMVPEESTLSKKDTVFYNPVMETNRDISVSVVQSFLDDFKRDEFLMCDPLGGSGARGIRYAKELKFNGDLKVSIGDINPSAVKMIKENLKLNELENVEVFHEDANVLLSKNFKVFNVVDLDPFGSPVPYLDSGIRASLTKGGLLCMTATDTAVLCGAYRKTCIRKYNAVPLKGDKELAVRLMIGYAVKMASKYDIGLKPIFSHVTDHYARTFMVTERGAGKADSAIENLGYIRQDSEQKSFKTFEEGSEKGYAGPFYLGEISDKNIVQNALNTAKTRNYSKRAVNILEMISRESEINQVGCFDIHELCSFIKKLVPPVNDIMENLKENGFKVTRVHYNPYGLKTDAELSDLVVLISEYHSKKY

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

371 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

39.82 kDa

MDVSEGGVTVSVPTASGGGEGAADDVFFNATQELNRDLTVATLAAFREREPRAASYLDAMTASGIRGVRAANAGWDVTMADVDADAVELATSNLARNGLDGEVVARDANSLLHDHDRVLDVVDIDPFGSPMPFADAAFANARNLVCVTATDTAPLCGAHFESGVRKYSATPRNTNYHAEMGLRILLGALARTAARYDVGVTPILSHVSDHYVRTYLELDHRATDANAAVEQVGHVYHCQQCLSRDHEYGLVAAPRAECPRCGGHQVLTAGPLWLGPAHEEAFAASVREQLTREMGEASQAFHLLQTIEGELHEPTHYDQHRLYSQWGEPAVGMAEFLDQLRDAGLRASRTHFGGTTFKTDGGLAEVEAAVL

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

371 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

39.82 kDa

MDVSEGGVTVSVPTASGGGEGAADDVFFNATQELNRDLTVATLAAFREREPRAASYLDAMTASGIRGVRAANAGWDVTMADVDADAVELATSNLARNGLDGEVVARDANSLLHDHDRVLDVVDIDPFGSPMPFADAAFANARNLVCVTATDTAPLCGAHFESGVRKYSATPRNTNYHAEMGLRILLGALARTAARYDVGVTPILSHVSDHYVRTYLELDHRATDANAAVEQVGHVYHCQQCLSRDHEYGLVAAPRAECPRCGGHQVLTAGPLWLGPAHEEAFAASVREQLTREMGEASQAFHLLQTIEGELHEPTHYDQHRLYSQWGEPAVGMAEFLDQLRDAGLRASRTHFGGTTFKTDGGLAEVEAAVL

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

371 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

40.568 kDa

MDVVEVTEGRTRFFVSRQDPHLQFPPGSGQVFYNSRMEMNRDATVLLLSVLRPESYLDAMGASGVRGLRVAHEVGIPVTINDWNAKAVDLARQNVEALGLVAEVTHGDANVLMSGRTFDAVDLDPFGTPAPFVDSAARSAGNYLFVTATDTAPLCGAHLKAGMRRYFSRPRNTEYHAEVGLRTLMGFVVREVIKYDRGVEPLFCYAHEHFHRLHLRLRYGAAAADRALARIGYVMQCPNCLYRSEQTGMLPEPEECPLCSAALVPVGPLWTGGINDDATLAAMQEALPSVTAGTGARIGRLLATCRQELDTSSHYDYHVIAKRLRVSPGRIETVIERLVALGYRASRAHYSGTALKTDAPLPVLEKVVSGG

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

371 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

40.413 kDa

MDLIEVTEGRTTFRIPVQDPNSPFPPSSAPVFFNPKMAMNRDATVLLLSVLNPEEYLDTMGASGVRGLRVAGECRIPVVINDRDPAAADLIRANLAGAGLEGRVTVEDANVLLSRERFDAVDLDPFGSPAPFTDAACRSAKRYLFVTATDTAPLCGAHLKAGIRRYATKPLNTEYHAEVGLRILLGYVARTMVKYDRGLSPLFCFASAHFLRLHLQAEKGADAADRTVARLGFLYHCPSCPERTEEPGVLPHDHVCPRCGTTMLPIGPLWLGSLSDMALLDQMKERLPDLSLSTERRLGKLLDVLKVELPTSSHYDYHRIAKWIGGSPPAIDVVIARLIQTGYRASRAHYSGTALKTDAPLDAIAAALSAQ

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

370 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

40.669 kDa

MDLTWVTEGRTTIAVPCQNPDVPFPPGTAPVFYNSRMALNRDSTVLVVRQTHPHSYLDAMAASGIRGCRVGYETGVPVTFNDRDQLAIDLITHNVQSLGIKADITCRDANSLMSDEKFGFVDLDPFGTPAPFIDAAIRSSGKYLGVTATDTAPLCGAHLKAGIRRYMARPLNTEYHTEVGLRILLGNVARHAAVYDKGITPLFCYAHEHFVRLHLQLKSSASAADKSIARLGYIHQCPKCPYRLEEQKFFPGIHTCPLCGASLTPTGPLWTGSTHDPNILAGMIEDAETFIAGDPSGLLKLLALCRDEPDISFSYDYHKLGKFYRLSPGPIDVLLNRLRDKGYRAGRVHYSGYGIKTDAPLEEIRDCISS

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

367 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

40.356 kDa

MRVSEGRVTVTVPEQPEAGKGADVFFNPVQELNRDITVAALRAYRERTPRVSTYLDATAASGIRGVRAAANDWETTLCDIDDDATALCEQNLERNDLAASVRRSDANVLMHSEAFDVVDVDPFGTPIPFADAAVQGTKHLLCVTATDTAPLCGAHFESGVRSYGAVPRNTEFHAEMGMRVLLSAMVRTAARYDIAARPILSHATKHYARTYLEFDHGAKVANDCIDELGYVHHCQHCLWRDHDYGLIADPPEDCPVCEKHLQTAGPIWLGRTCDPEFVSAVSEQVSEEMGTADEAKELLATLGAEIDTPTHYDQHRLCKRWGRGAEAMDEFIEKLRDAGYAASRTHYGGTTFKTDADVVEIREATAD

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

366 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

39.71 kDa

MEVSEGSVTVEVPEERHGASEGSGEGVFYNPVQELNRDITAAVLRTVSDDCDEYLDAMAASGIRSVRAAAAGYDVTACDIDDDAVALTRRNLDRNGVDGTVHHRNVNAHMHESAHDVVDLDPFGTPMAFADAAVRSAGEYLCVTATDTAPLCGAHFESGVRSYDAVPRNTEFHAEMGLRVLLSALVRTAARHDIAAEPVLSHVTSHYVRTYLRVDSGARAADALLEHLGYIDHCQRCLWRDHERGRVPDPTTTCPHCGQSTWTAGPVWLGPAHDAAFVDDVAGAIPDSFGTADKARDLLSTVATELHQPTHYDQHKLYKRWNEPNIAMDDFLAALRAAGHEASRTHYGGTTFKTDADVADIRNAVE

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

363 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

40.108 kDa

MRHLVLRREGGVKFYAPDPEKYGGIYSAPVFYNPAMEKNRTLSTLLLKAYGKGGLVVCEPLSGTGVRGIRYAVESGVVGKLILNDISKEAVELIKKNLEINGVDAEVYNEDANVLLHKLKDSCDVVDIDPFGSPAPFIHGAFRALKEEGLICATATDTAVLVGRYPRKCLRRYGSVIVKTPFYIEVGLRNLLGYIARVAAAEDYKITPLMSYWEGHYFRVCAYAARGARDADDNFHHIAYIKYERGVRKILHAQSEGSSGPLWVGPLGDPLIINKMSEIGPYQDFLKILAEEYSISAPWFYRLPEFAAGGKSPTLKEAVGVLRAAGIYAVRTHMAPDGFKADGEYGEVLMAFKRYISSAHSLQ

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

358 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

40.121 kDa

MDDYVIRREGKAVFYAPNPKKYDIYSAPVFYNPAMEKNRTLSVLLLKVAGAQMGGGLTVCEPLSGTGIRGIRYVIESGVVGKLILNDLSKEAVHVIQKNLSINGVEADVYNEDANVLLHKLRGQCDVVDVDPFGSPAPFLSAAFRALKNEGIVCATATDTAVLVGRYPRKCLRRYGSVIRKSPFYLEMGLRNLVGYVARIAASEDFAIRPLLSYWEGHYFRTCVYAVKSAKDADDMLQRDVGYVEYRRYRKVTRRQSEYTSGPVWIGELGDPSIAFFMAREGQYSDFLKLLEEEYSVSLPWFYKLPEFAVDGKSPTLEEAMAALRRAGVYAARTHMASDGFKAEATYGEVERVLRRVT

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

356 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

39.542 kDa

MSRIVLRREGTVEFYAPDPRAYGSIYSAPVFYNPAMEKNRTLSVLFLKAYGATGLTVCEPLSGTGVRGIRYAVETGAVGRLILNDISREAVELIKKNLEVNGVDAEVYNEDANVLLHRLRDKCDVVDIDPFGSPAPFLQAGFRALREEGVICVTATDTAVLVGRYPKKCLRRYGAVMFKTPFYIEAGLRNLTGYVARVAASEDYGFEPLFAYWEGHYFRLCARAVRGARDADSNFNFIGYVEYKKPSRKVVRRPGERSLGPLWVGPMGDPILVNKMAEYGPYGDFLQLLSEEYSVAAPWFFKVPEFALGGVSRGIEEALNALKKGGIYAVRTHMAPDGFKTEVSAGEVERVLRIVI

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

352 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

39.968 kDa

MKLILNKEGAVEFYIPDPQTYRSIYSAPVFYNPSMEKNRTLSVLLLKTYGSGLTVCEPLSGTGIRGIRYAIESNAVGRLILNDISKEAVELIKKNLELNGVEGEVYNEDANVLLHKLRNTCDVVDIDPFGSPAPFLHAAFRALRDEGLICVTATDTAVLVGRYPRKCFRRYNSVIRRTPFYIELGLRNLVGYVARVAASEDFSIQPVFSYWENHYFRTCALATRGAREADDSLNNLGYIWYLKKRRKIVQTLDEHSSGPLWIGPLGDPLVVHKMSQYGVYSVFLQTLEMEYSIQAPWYFRLPEFAVDGKSPTLEKTLELLRRGGIYATRTHMSYDGFKAEANYDEIARILSI

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

351 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

39.045 kDa

MNLVLRREGAVQFYAPDPQRYGSIYSAPVFYNPAMEKNRTLSVLLLRTLGGGLTVCEPLSGTGVRGIRYAVESKAVARLVLNDISRDAAELIKKNLELNGVDGEVYNDDANVLLHRLKNVCDVVDIDPFGSPAPYIHAAFRALRDEGLLCATATDTAVLVGRYPRKCLRRYWSTVRKTPFYIELGLRNLVGFIARVAASEDFSIRPLMSYWEGHYFRTCVAVARGARDADDALQNVGYVVYRRGMRQTTQLPDESSSGPLWLGPLGDPLIMHQMAQHGVYSDFLGVLEQEYSIEAPWHYRLPEFAVEGVSPTLAEALDLLRRSGIYATATHMAKDGFKADAGYGEVKRALF

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

349 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

38.808 kDa

MEVEEGRARVKVEGVFYNPRMRFCRDLDMLVFATMDSKEYFDALSASGIRGIRAALEAGKKAVFNDVSPKAVKVIEENLRENGVSGEVINGDAAAVMRQRAFEHIDIDPFGSPAPFMDSACFSAKRYLSVTATDTAALCGSATNSGLKKYGAFAVKTDVYHEVGLRMLIGFVVREATKYEKALFPLISWVREHYYRVHFKIKKSTAMSAKVYEKMGYLAYCSTCLRKKVLGMGEGAERCECGGKFSLIGPIWLGELKQRDFAEKVAEKAEGKLRAFLEKILAEIDAPTAYSLPALAKIHSLTLPPTDVVVEELKKLGYEASRTHYCGFCVKTDADRDVVVKILRSRKII

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

344 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

37.999 kDa

MIVREGSAEILVPEVYHGPGKRGTGFYNADQKINRDITIEFIKKMGIRNVLDGFGGTGIRGIRISKETDSAVTISEVSPDSYRLIRDNVERNGSQASVINDSFECVLQHGAYEYVDVDPYGSPVPYLDAALMGVKRNGFLGVTATDQSALTGSVPHKTRIRYDALIKNDTFRHEMGIRLLIGYMAKRAASLGRFIDPLISIWHGHYYRVFVRVRKGFEGAGRMMQNLGYVNKHNLLSGIYQDMDEGPVWKGNLQDNAVAEAVLASAGHKAFNPEENRLLFCDLTDIARARHTSLPDIESVIDALSSSGHAASRTMFSPTGIKTDASCDLVESLMMDTLHRRSPA

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

342 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

38.304 kDa

MRITEGSAVIEVPEAYSGPGRRSPGFYNADQVLNRDLTIDLINEFGVEKVLDGFGGSGVRGIRISLETKAKVVIAEISPSSCEIIKQNIAINNAEADLIHDNFQCVSSHIAFDYIDVDPYGSPVPYLDAAIMNVRKGGYLGITATDQSTLTGSTLNKTRRRYGAYIVNDIYRHEMGIRTLIGYIARRAAAFDRYIEPQLSIWNHHYYRVFVKVGKGVNGADKMIENIGYLNKHTTIDNSFKDVNEGPVWLSNLNNAELLEKIRDPRVSKKIEMIKHDNRLLFVDLTDIARKTSLSLPPLAKVMDEIMKHGYEAHRTSFSPTGIKTDCPYAEVSEILKAYAKR

TRM1

Thioredoxin M-type, chloroplastic

167 amino acids

Participates in various redox reactions through the reversible oxidation of the active center dithiol to a disulfide. The M form is known to activate NADP-malate dehydrogenase (By similarity).

Belongs to the thioredoxin family. Plant M-type subfamily.

18.073 kDa

MAMETCFRAWALHAPAGSKDRLLVGNLVLPSKRALAPLSVGRVATRRPRHVCQSKNAVDEVVVADEKNWDGLVMACETPVLVEFWAPWCGPCRMIAPVIDELAKDYAGKITCCKVNTDDSPNVASTYGIRSIPTVLIFKGGEKKESVIGAVPKSTLTTLIDKYIGSS

trm1

tRNA (guanine(26)-N(2))-dimethyltransferase

73 amino acids

Dimethylates a single guanine residue at position 26 of a number of tRNAs using S-adenosyl-L-methionine as donor of the methyl groups.

Belongs to the class I-like SAM-binding methyltransferase superfamily. Trm1 family.

8.094 kDa

single

MSMELFEVHEGKAKVLVPKAKTIYDSPVFYNPRMAPNRDVVVLLLNVLKPKIVLDALSATGIRGIRFALETPA