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TRX2

Gene
TRX2
Protein
Triplex capsid protein 2
Organism
Psittacid herpesvirus 1 (isolate Amazon parrot/-/97-0001/1997)
Length
321 amino acids
Function
Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.
Similarity
Belongs to the herpesviridae TRX2 protein family.
Mass
35.068 kDa
Sequence
MAHATSSAYEVKITLPGNLTRDEEDRLRCLTGTILMAPSLRRCLFLHDVDRNSYYVHGSEPDYATSLAAYRRRFPLLVTAVGRQELSAVSLSIGCPKGLNFRNTGPFQLLNGSNVSLIPPIGGRWRVELLSCGSVIEPAMTIPTEVGSELLGKILAGMTYEFCARNQIPADRPAEVYRVACDNKALDLTQAIRGGDSDLQDTMKTLFASVLFAMNEGVLQVMTLMPALLAGGNTNPFLNALLQMQSATRLSAQIFNPPTLPVHDPTGGARRYNVFDAFASWLTMSHRLGELFHMKPALKVVMFYSDVSAIDEGQTANAIVP

Gene
TRX2
Protein
Triplex capsid protein 2
Organism
Gallid herpesvirus 2 (strain Chicken/Md5/ATCC VR-987)
Length
319 amino acids
Function
Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.
Similarity
Belongs to the herpesviridae TRX2 protein family.
Mass
34.865 kDa
Sequence
MSTSNGTIVEIELPCKLSTCDANLLQRCEGRVLFLPFVRARVLLKDVDYKSFYIAGTEPDTLSLLSTFKTRFAAVITRALPGRMSAVVLGMGSIPNGLALQNTGPFDLCNGDTVCLMPPIFPNVCCRIRLESIDTELLFPVTVPTRLANEILAKTLSRAIEAIGRGQMPPPTSRESETIMYNGRSYTISPTLHSLDAAESTVRTLLLNMIFAINEGNMILYTMIPTLLTLGASDGYINALVGLETATRAVGQLIRIPNPPPLQDAWRRYPVYEALSAWITMTLNLGNVLSLHPLLKVCTFDGPANIKAGDLCPVIANWY

Gene
TRX2
Protein
Triplex capsid protein 2
Organism
Human herpesvirus 1 (strain 17)
Length
318 amino acids
Function
Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.
Similarity
Belongs to the herpesviridae TRX2 protein family.
Mass
34.271 kDa
Sequence
MLADGFETDIAIPSGISRPDAAALQRCEGRVVFLPTIRRQLTLADVAHESFVSGGVSPDTLGLLLAYRRRFPAVITRVLPTRIVACPLDVGLTHAGTVNLRNTSPVDLCNGDPISLVPPVFEGQATDVRLDSLDLTLRFPVPLPSPLAREIVARLVARGIRDLNPSPRNPGGLPDLNVLYYNGSRLSLLADVQQLGPVNAELRSLVLNMVYSITEGTTIILTLIPRLFALSAQDGYVNALLQMQSVTREAAQLIHPEAPALMQDGERRLPLYEALVAWLTHAGQLGDTLALAPVVRVCTFDGAAVVRSGDMAPVIRYP

Gene
TRX2
Protein
Triplex capsid protein 2
Organism
Human herpesvirus 2 (strain HG52)
Length
318 amino acids
Function
Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.
Similarity
Belongs to the herpesviridae TRX2 protein family.
Mass
34.344 kDa
Sequence
MITDCFEADIAIPSGISRPDAAALQRCEGRVVFLPTIRRQLALADVAHESFVSGGVSPDTLGLLLAYRRRFPAVITRVLPTRIVACPVDLGLTHAGTVNLRNTSPVDLCNGDPVSLVPPVFEGQATDVRLESLDLTLRFPVPLPTPLAREIVARLVARGIRDLNPDPRTPGELPDLNVLYYNGARLSLVADVQQLASVNTELRSLVLNMVYSITEGTTLILTLIPRLLALSAQDGYVNALLQMQSVTREAAQLIHPEAPMLMQDGERRLPLYEALVAWLAHAGQLGDILALAPAVRVCTFDGAAVVQSGDMAPVIRYP

Gene
TRX2
Protein
Triplex capsid protein 2
Organism
Varicella-zoster virus (strain Dumas)
Length
316 amino acids
Function
Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.
Similarity
Belongs to the herpesviridae TRX2 protein family.
Mass
34.389 kDa
Sequence
MAMPFEIEVLLPGELSPAETSALQKCEGKIITFSTLRHRASLVDIALSSYYINGAPPDTLSLLEAYRMRFAAVITRVIPGKLLAHAIGVGTPTPGLFIQNTSPVDLCNGDYICLLPPVFGSADSIRLDSVGLEIVFPLTIPQTLMREIIAKVVARAVERTAAGAQILPHEVLRGADVICYNGRRYELETNLQHRDGSDAAIRTLVLNLMFSINEGCLLLLALIPTLLVQGAHDGYVNLLIQTANCVRETGQLINIPPMPRIQDGHRRFPIYETISSWISTSSRLGDTLGTRAILRVCVFDGPSTVHPGDRTAVIQV

Gene
TRX2
Protein
Triplex capsid protein 2
Organism
Equine herpesvirus 1 (strain Ab4p)
Length
314 amino acids
Function
Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.
Similarity
Belongs to the herpesviridae TRX2 protein family.
Mass
33.842 kDa
Sequence
MASAAFEIDILLPSDLSPADLSALQKCEGKLVFLTALRRRVMLSSVTLSSYYVNGAPPDTLSLMAAFRRRFPAIIQRVLPNKMIAAALGVAPLPPGAFIQNTGPFDLCNGDSVCALPPILDVEDKLRLGSVGEEILFPLTVPLAQARELIARLVARAVQALTPNAQAQRGAEVMFYNGRKYNVTPDLRHRDAVNGVARSLVLNMIFAMNEGSLVLLSLIPNLLTLGTQDGFVNAIIQMGSATREVGQLVHQQPVPQPQDGARRFCVYDALMSWISVASRLGDVVGGKPLVRICTFEGQATISRGEKAPVIQTLL

Gene
TRX2
Protein
Triplex capsid protein 2
Organism
Alcelaphine herpesvirus 1 (strain C500)
Length
306 amino acids
Function
Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.
Similarity
Belongs to the herpesviridae TRX2 protein family.
Mass
34.095 kDa
Sequence
MAVDSKIVVSCTSRLFTDEVCKLQEKVGCIVPLRDSHGSQNLQTVGLKPALGIDLGSDYVLMCNYLSTCTLAILEEVTTDSLVLTKISRNGTYQIKNKYHPFFQWDSNIQVCVMPPLFDQESNSVDLQSNNFTLLLPIVVPCEVAHEALQKVLTYNIYLRVTQAEPNAARMADVLAQTNYVTYLGNHYSLNLEGMESLGALAFLDNLATYLCIMVGLLPRACVRLLTTLLRHGENELLNVFRRMIPDEFNAAAANLNADTVYPDMTKIGLLITYLQTLGSIFNLSPRLQVSTYTPENLSATCWYVC

Gene
TRX2
Protein
Triplex capsid protein 2
Organism
Human cytomegalovirus (strain AD169)
Length
306 amino acids
Function
Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.
Similarity
Belongs to the herpesviridae TRX2 protein family.
Mass
34.595 kDa
Sequence
MAAMEANIFCTFDHKLSIADVGKLTKLVAAVVPIPQRLHLIKHYQLGLHQFVDHTRGYVRLRGLLRNMTLTLMRRVEGNQILLHVPTHGLLYTVLNTGPVTWEKGDALCVLPPLFHGPLARENLLTLGQWELVLPWIVPMPLALEINQRLLIMGLFSLDRSYEEVKAAVQQLQTITFRDATFTIPDPVIDQHLLIDMKTACLSMSMVANLASELTMTYVRKLALEDSSMLLVKCQELLMRLDRERSVGEPRTPARPQHVSPDDEIARLSALFVMLRQLDDLIREQVVFTVCDVSPDNKSATCIFKG

Gene
TRX2
Protein
Triplex capsid protein 2
Organism
Human cytomegalovirus (strain Merlin)
Length
306 amino acids
Function
Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.
Similarity
Belongs to the herpesviridae TRX2 protein family.
Mass
34.595 kDa
Sequence
MAAMEANIFCTFDHKLSIADVGKLTKLVAAVVPIPQRLHLIKHYQLGLHQFVDHTRGYVRLRGLLRNMTLTLMRRVEGNQILLHVPTHGLLYTVLNTGPVTWEKGDALCVLPPLFHGPLARENLLTLGQWELVLPWIVPMPLALEINQRLLIMGLFSLDRSYEEVKAAVQQLQTITFRDATFTIPDPVIDQHLLIDMKTACLSMSMVANLASELTMTYVRKLALEDSSMLLVKCQELLMRLDRERSVGEPRTPARPQHVSPDDEIARLSALFVMLRQLDDLIREQVVFTVCDVSPDNKSATCIFKG

Gene
TRX2
Protein
Triplex capsid protein 2
Organism
Human herpesvirus 8 type P (isolate GK18)
Length
305 amino acids
Function
Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.
Similarity
Belongs to the herpesviridae TRX2 protein family.
Mass
34.373 kDa
Sequence
MALDKSIVVNFTSRLFADELAALQSKIGSVLPLGDCHRLQNIQALGLGCVCSRETSPDYIQIMQYLSKCTLAVLEEVRPDSLRLTRMDPSDNLQIKNVYAPFFQWDSNTQLAVLPPFFSRKDSTIVLESNGFDLVFPMVVPQQLGHAILQQLLVYHIYSKISAGAPDDVNMAELDLYTTNVSFMGRTYRLDVDNTDPRTALRVLDDLSMYLCILSALVPRGCLRLLTALVRHDRHPLTEVFEGVVPDEVTRIDLDQLSVPDDITRMRVMFSYLQSLSSIFNLGPRLHVYAYSAETLAASCWYSPR

Gene
TRX2
Protein
Triplex capsid protein 2
Organism
Saimiriine herpesvirus 2 (strain 11)
Length
304 amino acids
Function
Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.
Similarity
Belongs to the herpesviridae TRX2 protein family.
Mass
34.357 kDa
Sequence
MLTDKTIIVSLTSRLFADEITKLQKKIGSILPLQDPHKLQSLDTLGLNAVCSRDVFPDYVHMFSYLSKCTLAILEEVNPDNLILTRLDPSETYQIKNVYEPMFQWDGFSNLTVIPPVFGRQQATVTLESNGFDLVFPSVVPSDLAQAIIGKLLLYNLYSRLVESDPEINIEEVNMYTTNVTHMGRHYVLDINHNNPNEALKSLDDLAVYTCILSALIPRACLRVLTILMRHDQHELLDVFRGIVPREVYEIDANALSIGDDITRMTTFITYLQSLSSIFNLGAKLHLSSYASETQTATCWISYC

Gene
TRX2
Protein
Triplex capsid protein 2
Organism
Epstein-Barr virus (strain B95-8)
Length
301 amino acids
Function
Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.
Similarity
Belongs to the herpesviridae TRX2 protein family.
Mass
33.624 kDa
Sequence
MDLKVVVSLSSRLYTDEIAKMQQRIGCILPLASTHGTQNVQGLGLGQVYSLETVPDYVSMYNYLSDCTLAVLDEVSVDSLILTKIVPGQTYAIKNKYQPFFQWHGTGSLSVMPPVFGREHATVKLESNDVDIVFPMVLPTPIAEEVLQKILLFNVYSRVVMQAPGNADMLDVHMHLGSVSYLGHHYELALPEVPGPLGLALLDNLSLYFCIMVTLLPRASMRLVRGLIRHEHHDLLNLFQEMVPDEIARIDLDDLSVADDLSRMRVMMTYLQSLASLFNLGPRLATAAYSQETLTATCWLR

Gene
TRX2
Protein
Triplex capsid protein 2
Organism
Equine herpesvirus 2 (strain 86/87)
Length
300 amino acids
Function
Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.
Similarity
Belongs to the herpesviridae TRX2 protein family.
Mass
33.418 kDa
Sequence
MQVDSRIVVTLTSRLYADEISKLQERVGSVVPLKDSHRLQNLNSVGMYSVYMRNVAPDFVAMFSYLSEATLAILDEVTPDTLVFSRLDHSQNYELKNVYYPSFAWHSHTLLTVVPPVFGREAATVALESNGFEIVFPVVMPHALAQAVLQKLMLYNIYARLSDANVGDVNMDHVRFHATTLHHMGRAYTLHIDQANPGGMLGLLDNLAIYLAIISALLPNSLARLLPAIMRHEQHELLNIFAGVAPPDDGGDFNIEDDMQKMESFMAYMQSVSSIFNLGPKLRLGQYSSETQSGTAWLAS

Gene
TRX2
Protein
Triplex capsid protein 2
Organism
Human herpesvirus 6A (strain Uganda-1102)
Length
296 amino acids
Function
Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.
Similarity
Belongs to the herpesviridae TRX2 protein family.
Mass
33.464 kDa
Sequence
METVYCTFDHKLSLSDISTLCKLMNIVIPIPAHHHLIGSGNLGLYPIVSSNKDYVHVRNVLRTMVVTILQKVEGNQLVLRKPVTGHQYAIKNTGPFPWEKGDTLTLIPPLSTHSEEKLLKLGDWELTVPLVVPTAIAAEINIRLLCIGLIAVHREYNEMQTIIDELCSIQYRDVLIKLPDIVNDKQSMYSMKTACISLSMITAMAPDIVRTYIDRLTLEDHSMLLIKCQELLSKRTTLNTQRCGQLHATEIKDELKKVKSVLTMIDQINSLTNEKTYFVVCDVSADNRMATCIYKN

Gene
TRX2
Protein
Triplex capsid protein 2
Organism
Human herpesvirus 6B (strain Z29)
Length
296 amino acids
Function
Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.
Similarity
Belongs to the herpesviridae TRX2 protein family.
Mass
33.474 kDa
Sequence
METVYCTFDHKLSLSDISTLCKLMNIVIPIPAHHHLIGSGNLGLYPIVSSNKDYVHIRNVLRTMVVTILQKVEGNQLVLRKPMTGQQYAIKNTGPFPWEKGDTLTLIPPLSTHSEEKLLKLGDWELTVPLVVPTAIAAEINIRLLCIGLIAVHREYNEMQTIIDELCSIQYRDVLIKLPDIVNDKQSMYSMKTACISLSMITAMAPDIVRTYIDRLTLEDHSMLLIKCQELLSKRTTLSTQRCGQLHATDIKDELKKIKSVLTMIDQINSLTNEKTYFVVCDVSADNRMATCIYKN

Gene
TRX2
Protein
Triplex capsid protein 2
Organism
Human herpesvirus 7 (strain JI)
Length
293 amino acids
Function
Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.
Similarity
Belongs to the herpesviridae TRX2 protein family.
Mass
33.338 kDa
Sequence
MDSIYCTFDQKLTLSDIGTLCKLTNAVIPIPSHRHLIGNTNLGLYTVLSTTTDYIQIRDILKTMVLTILQKVEGNQLILIRPKIGHQYEIKNTGPFPLEKGDQLSLLPPFLKPSQQLLVLPNWELILPLLIPTDVATEINVRMLCISLLSIHRKYEEVQIIIDELRTLQYRDVTIKLPDVINDCKSTFSMKTACISFSMIATMAPDIVQTYIERLSLEDQSMLLIKCQELLAKKNFSQEPSSFKATEIKTELQKIKTVFTMINQINSLTQEKTFFIVADVSADNRLATCIFKE

Gene
TRX2
Protein
Triplex capsid protein 2
Organism
Human herpesvirus 7 (strain MUK)
Length
293 amino acids
Function
Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.
Similarity
Belongs to the herpesviridae TRX2 protein family.
Mass
33.338 kDa
Sequence
MDSIYCTFDQKLTLSDIGTLCKLTNAVIPIPSHRHLIGNTNLGLYTVLSTTTDYIQIRDILKTMVLTILQKVEGNQLILIRPKIGHQYEIKNTGPFPLEKGDQLSLLPPFLKPSQQLLVLPNWELILPLLIPTDVATEINVRMLCISLLSIHRKYEEVQIIIDELRTLQYRDVTIKLPDVINDCKSTFSMKTACISFSMIATMAPDIVQTYIERLSLEDQSMLLIKCQELLAKKNFSQEPSSFKATEIKTELQKIKTVFTMINQINSLTQEKTFFIVADVSADNRLATCIFKE

Gene
TRX2
Protein
Triplex capsid protein 2
Organism
Elephantid herpesvirus 1 (isolate Asian elephant/Berlin/Kiba/1998)
Length
292 amino acids
Function
Structural component of the T=16 icosahedral capsid. The capsid is composed of pentamers and hexamers of major capsid protein/MCP, which are linked together by heterotrimers called triplexes. These triplexes are formed by a single molecule of triplex protein 1/TRX1 and two copies of triplex protein 2/TRX2. Additionally, TRX1 is required for efficient transport of TRX2 to the nucleus, which is the site of capsid assembly.
Similarity
Belongs to the herpesviridae TRX2 protein family.
Mass
32.632 kDa
Sequence
MNEVKCVFETKLSPGDVAKLNKIVGAVVPVARCTPLISPRDVGLHKHVSHRTDYGKLHMALNMMYPTVFRKLEGNQMVMTPMQHGNIYTIRNTGPFSWEVGDRLAIIPPVFSVEHTTIMQTPSWDLMLPIIVPVQVAKEINIRNLVLTLMSLNRPGRDVELSQEVRRIHFRDVTIDIPATLDTRQLNSVRNVCLALALITNVAPSLLQQYVPRLALAETDMLLVKCYDLLKKLDLPGDGNGGEPPNIPNEIQRMSGLLNLITYVSSIVTENSLFIVNDITPDNKMATCTFTL

Gene
TRX2
Protein
Thioredoxin H2
Organism
Arabidopsis thaliana
Length
133 amino acids
Function
Thiol-disulfide oxidoreductase probably involved in the redox regulation of a number of cytosolic enzymes. Possesses insulin disulfide bonds reducing activity.
Similarity
Belongs to the thioredoxin family. Plant H-type subfamily.
Mass
14.676 kDa
Sequence
MGGALSTVFGSGEDATAAGTESEPSRVLKFSSSARWQLHFNEIKESNKLLVVDFSASWCGPCRMIEPAIHAMADKFNDVDFVKLDVDELPDVAKEFNVTAMPTFVLVKRGKEIERIIGAKKDELEKKVSKLRA

Gene
trx2
Protein
Thioredoxin-2, mitochondrial
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843)
Length
133 amino acids
Function
Disulfide reductase which serves multiple functions in mitochondria, protecting mitochondrial components against thiol-oxidative damage as a thiol-disulfide oxidoreductase, and supporting urea cycle and respiration in mitochondria in a manner independent of active site thiols.
Similarity
Belongs to the thioredoxin family.
Mass
15.079 kDa
Sequence
MRGFIANSLKPHMRSFALRRSFTSSRILRKVNAVESFGDYNTRISADKVTVVDFYADWCGPCKYLKPFLEKLSEQNQKASFIAVNADKFSDIAQKNGVYALPTMVLFRKGQELDRIVGADVKTLSSLLAKYQE

Gene
trx2
Protein
Thioredoxin 2
Organism
Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
Length
109 amino acids
Function
Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.
Similarity
Belongs to the thioredoxin family.
Mass
11.859 kDa
Sequence
MSGKYFEATDQNFQAEILNSDKVALVDFWAAWCGPCMMLGPVIEELAGDYEGKAIIAKLNVDENPNTAGQYGIRSIPTMLIIKGGKVVDQMVGALPKNMIAKKLDEHIG

Gene
TRX2
Protein
Thioredoxin-2
Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Length
104 amino acids
Function
Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and redox homeostasis. Thioredoxin-dependent enzymes include phosphoadenosine-phosphosulfate reductase MET16, alkyl-hydroperoxide reductase DOT5, thioredoxin peroxidases TSA1 and TSA2, alkyl hydroperoxide reductase AHP1, and peroxiredoxin HYR1. Thioredoxin is also involved in protection against reducing stress. As part of the LMA1 complex, it is involved in the facilitation of vesicle fusion such as homotypic vacuole and ER-derived COPII vesicle fusion with the Golgi. This activity does not require the redox mechanism. Through its capacity to inactivate the stress response transcription factor YAP1 and its regulator the hydroperoxide stress sensor HYR1, it is involved in feedback regulation of stress response gene expression upon oxidative stress.
Similarity
Belongs to the thioredoxin family.
Mass
11.204 kDa
Sequence
MVTQLKSASEYDSALASGDKLVVVDFFATWCGPCKMIAPMIEKFAEQYSDAAFYKLDVDEVSDVAQKAEVSSMPTLIFYKGGKEVTRVVGANPAAIKQAIASNV