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stringlengths 6
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stringlengths 11
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Q8WN98 | MKDPDPSQVYRPDMDPEAAKDKGSFRNYTSGPLLDRVFRTYKLMHTWQTVDFVRKKHAQFGGFSYKRMTVLEAVDMLDGLVDESDPDVDFPNSFHAFQTAEGIRKAHPDKDWFHLVGLLHDLGKVLVLAGEPQWAVVGDTFPVGCRPQASVVFCDSTFQDNPDLQDPVYSTELGMYQPHCGLENALMSWGHDEYMYQMMKFNKFSLPGEAFYIIRFHSFYPWHTGGDYRQLCNEQDLAMLPWVQEFNKFDLYTKGSDMPDVDELRPYYQGLIDKYCPGVLCW | Cofactor: Binds 2 iron ions per subunit.
PTM: The N-terminus is blocked.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
Sequence Mass (Da): 32653
Sequence Length: 282
Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Subcellular Location: Cytoplasm
EC: 1.13.99.1
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P38162 | MVDNRRTFTAPQSLLETNLTFPNDEPSLTTITVTRERCVDPSLIDSFLRFLRHGSDDIIRQKLNNYRKGSINGKNKCKEFLKQELYPNWQIRNNIISFCEKEAAEMKNETDQQCGNNKKTTAEPLIDARIDPYAARERAEKQEAQYKDWTKVTEWVANNRKIEQILTSTTEGILRQNCEQNNDYLKEFTQFCKDNS | Function: Regulator of the mitochondrial protein import machinery that is localized in the mitochondrial intermembrane space (IMS) and facilitates the transport of proteins from the cytosol into the mitochondrial matrix . Not essential for mitochondrial protein import but induced and required when mitochondrial import is compromised . Stimulates or stabilizes the translocation into the mitochondria of proteins such as OXA1, ATP1 and COX12 .
Sequence Mass (Da): 22966
Sequence Length: 196
Domain: The Cx14C/Cx13C motifs are involved in the recognition by the mitochondrial MIA40-ERV1 disulfide relay system and the subsequent transfer of disulfide bonds by dithiol/disulfide exchange reactions to the newly imported protein.
Subcellular Location: Mitochondrion intermembrane space
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Q9H2W2 | MATAESRALQFAEGAAFPAYRAPHAGGALLPPPSPAAALLPAPPAGPGPATFAGFLGRDPGPAPPPPASLGSPAPPKGAAAPSASQRRKRTSFSAEQLQLLELVFRRTRYPDIHLRERLAALTLLPESRIQVWFQNRRAKSRRQSGKSFQPLARPEIILNHCAPGTETKCLKPQLPLEVDVNCLPEPNGVGGGISDSSSQGQNFETCSPLSEDIGSKLDSWEEHIFSAFGNF | Function: Transcription factor that play a central role in proper axial mesendoderm morphogenesis and endoderm formation. Required for efficient differentiation of cells from the primitive streak stage to blood, by acting early in the recruitment and/or expansion of mesodermal progenitors to the hemangioblastic and hematopoietic lineages. Also involved in the morphogenesis of the heart and the gut during embryogenesis. Acts as a negative regulator of brachyury expression (By similarity).
PTM: Phosphorylated at multiple sites.
Sequence Mass (Da): 24659
Sequence Length: 232
Subcellular Location: Nucleus
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D7SSD8 | MEKRERHFVLVHGACHGAWCWYKVTTFLRSAGHKVTALDLAAAGANGKRLDELNSISDYHEPLMKFMTSLVAGEKVILVAHSLGGVSVSVAMERFPQKISVAVFVSAYMPGPDFNLSTVYQELHQRRQGASKDTQYTFDRGSNNPPTSIIFSPEDLAAKLYQLSPPEDLTLATTLMRPTKLFRGENLLKETTVTREKYGTVRRVYIVCDKDNILKEDFQRWMIKNNPSDEVKVIMGSDHMPMFSKPLDLCAYLQEIVESYS | Function: Methylesterase that catalyzes the hydrolysis of methyl jasmonate (MeJA) into jasmonate (JA) . Can also use methyl salicylate (MeSA) as substrate with a lower efficiency .
Catalytic Activity: H2O + methyl (-)-jasmonate = H(+) + jasmonate + methanol
Sequence Mass (Da): 29486
Sequence Length: 261
Pathway: Plant hormone biosynthesis.
EC: 3.1.1.-
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Q57604 | METYEKIELGIIVIILLILIESVILMTVEGWDFFTAFYTAVVTISTVGYGDYTPQTFLGKLSVIIYIFAGVGAVAYTMGNIASFFIEGHFRKYFRLRKMMDRIKKLNNHYIICGYGRLGKVIAEEFKKCNIPFVIIDSDEKLLEEALEKDPNLICIVGDATSDDILKKAKIEKAKGLISVVSSDAENVFITLSAKKLNPNIYIVAKAEKPSTLDKLIKAGADRAVCPYIVGGMEIARIAINPDIVEFIHSLVATEEDMEVRRYIVKNKELDNKLLKDSGIREKTGATILAVKKGDKTITSPPPDTVINIGDIIYAFGTKEQLEKLKRYVEGVE | Function: Potassium channel protein. Seems to conduct potassium at low membrane potentials.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37150
Sequence Length: 333
Subcellular Location: Cell membrane
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Q58752 | METSKKLVIVAVLSITLILTYAYLISIIEGVDYFTALYFSVITITTTGYGDFTPKTFLGRTLTVVYLCVGVGIVMYLFSLIAEFIVEGKFEEFVRLKKMKNKIKTLKDHYIICGYGRLGKVVGEKFIEENIPFIAIDINEDVLKEEYEKYPDKFLYIVGDAKKEEVLKKAKIDKAKGLIATLPSDADNVFLTLTARELNPNILITAKADEKEAIRKLKIAGANRVVSPYLIGGLRMAEVSVRPGILDFLSTFIKIAKDEYEEDIELRKFVIEKDSELAYKSLKDANIRGKTGATILGIRREKEFCINPYPEFILKPGDVIYAFGTEENLKYLENLVKKKKKKL | Function: Probable potassium channel protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38884
Sequence Length: 343
Subcellular Location: Cell membrane
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Q501Q9 | MSGPEVEDHISQKYDIKKRLGKGAYGIVWKAIDRKSGEIVAVKKIFDAFRNRTDAQRTFREIMFLQEFGEHPNIIKLLNVIRAQNDKDIYLVFEHMETDLHAVIKKGNLLKDIHMRYILYQLLKATKFIHSGNVIHRDQKPSNILLDGDCLVKLCDFGLARSLYQIQEDVGNPALTEYVATRWYRAPEILLASNRYTKGVDMWSVGCILGEMLLGKPLFPGTSTINQIERIMSIIEPPTHEDIVSIKSEYGASVISRMSSKHKVPMAELFPASCPREALDLLSKLLVFNPGKRLTAEEALEHPYVSRFHSPAREPALDYDVILPVDDDIQLSVAEYRNKLYEMILERKMNIRRQKRESLKESVSSSANGAKDRQDTDTSKTPAPPAGTNPAPQPTSSTVPQRAAIAAPNQPPAQKDSTQQSPKIKAPSSNPITHSTTHGSTEDWRTSHNKKAGQQGAAGTTAQEVRKEVESRSRTAPIGRARSFSHSQQARAAATNSALIRKDAPPTGTVSVAAVSARLNQRTAPIQGRDPRSAPRFGRKMFQGKTNVESAGDPKATLHSYTQAYGTISKAALQNLPQQGGAFKGK | Function: Atypical MAPK protein that regulates ciliogenesis by phosphorylating rcsd1 through its binding with dvl2.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 64989
Sequence Length: 586
Subcellular Location: Cytoplasm
EC: 2.7.11.24
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O62618 | MSVSITKKFYKLDINRTEWEIPDIYQDLQPVGSGAYGQVSKAVVRGTNMHVAIKKLARPFQSAVHAKRTYRELRLLKHMDHENVIGLLDIFHPHPANGSLENFQQVYLVTHLMDADLNNIIRMQHLSDDHVQFLVYQILRGLKYIHSAGVIHRDLKPSNIAVNEDCELRILDFGLARPTENEMTGYVATRWYRAPEIMLNWMHYDQTVDIWSVGCIMAELITRRTLFPGTDHIHQLNLIMEMLGTPPAEFLKKISSESARSYIQSLPPMKGRSFKNVFKNANPLAIDLLEKMLELDAEKRITAEEALSHPYLEKYAEPSVEQTSPPYDHSFEDMDLPVDKWKELIYKEVTNFKPPPSYAQVLKDVK | Function: Kinase involved in a signal transduction pathway. May down-regulate insect immunity gene expression after prolonged infection.
PTM: Dually phosphorylated on Thr-184 and Tyr-186, which activates the enzyme.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 42256
Sequence Length: 366
Domain: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Subcellular Location: Nucleus
EC: 2.7.11.24
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O61443 | MSRKMAKFYKLDINRTEWEIPETYQNLQPVGQGAYGQVCKAVVRGTSTKVAIKKLARPFQSAVHAKRTYRELRLLKHMDHENVIGLLDVFHPGQPADSLDQFQQVYMVTHLMDADLNNIIRTQKLSDDHVQFLVYQILRGLKYIHSAGVIHRDLKPSNIAVNEDCELRILDFGLARPAESEMTGYVATRWYRAPEIMLNWMHYNQTADIWSVGCIMAELLTGRTLFPGTDHIHQLNLIMEVLGTPADEFMSRISSESARNYIRSLPVMPRRNFRDIFRGANPLAIDLLEKMLELDADKRITAEQALAHPYMEKYHDPTDEQTAALYDQSFEENELPVEKWREMVFSEVTAFKPTAAFAELLPKEQ | Function: Kinase involved in dpp signal transduction pathway in the process of wing morphogenesis when the levels of dpp are enhanced or inhibited. May down-regulate insect immunity gene expression after prolonged infection.
PTM: Dually phosphorylated on Thr-183 and Tyr-185, which activates the enzyme.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 42098
Sequence Length: 365
Domain: The TXY motif contains the threonine and tyrosine residues whose phosphorylation activates the MAP kinases.
Subcellular Location: Nucleus
EC: 2.7.11.24
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Q75A60 | MGSLSDISFFDHLQELARRDCCVNALLWCAFTVGAVKLTTFMLSLISIALETTVLPSASYKKYGARKGAYALVTGASDGIGKEFALQLASKGFNVLLVSRTEAKLLELKQEIMAKYKVDARVLSVDFGVDNRLTYTAISELCGELPVTVLVNNVGVSHSIPVSFLETTEEELRGIITVNNTATLMVTQTVAPLVIANARRLQCRGLVLTMGSFGGLLPTPLLATYSGSKAFLQAWSAALAGELAPHNVDVQIVLSYLVTSAMSKVRRASALIPTPRAFVRSTLASLGRRVGAQERYATCTPYWSHALYHFLIENTVGVHSRLANAINYRFHADIRKRALRKAARKAAEKQE | Function: Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids.
Catalytic Activity: a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-long-chain 3-oxoacyl-CoA + H(+) + NADPH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 38228
Sequence Length: 351
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.1.330
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A1C6J8 | MDFVSKYMSCLSSWGLDLQPGLQSVGAAVLLATGGLFLASRVLTFVRVLLSLFVLPGKPLRSFGPKGSWAVVTGASDGLGKEFALQLARAGFNIVLVSRTASKLATLAEEITAKHSVQTRTLAMDFAANDDTDYEDLKTLVDGLDVSILINNVGKSHDIPVPFALTPEDEMTDIVTINCLGTLRATQLVIPGMMQRRRGLVLTMGSFGGLLPTPLLATYSGSKAFLQQWSTSLGSELEPYGITVELVQAYLITSAMSKVRRTSALIPSPRAFVSSVLSKIGRNGGSPTYSYSSSPYWSHGLMAYFLTCVLQPMGKLVVGQNRTMHEAIRKRALRKAEREKGKKST | Function: Component of the microsomal membrane bound fatty acid elongation system, which produces the 26-carbon very long-chain fatty acids (VLCFA) from palmitate. Catalyzes the reduction of the 3-ketoacyl-CoA intermediate that is formed in each cycle of fatty acid elongation. VLCFAs serve as precursors for ceramide and sphingolipids.
Catalytic Activity: a very-long-chain (3R)-3-hydroxyacyl-CoA + NADP(+) = a very-long-chain 3-oxoacyl-CoA + H(+) + NADPH
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 37244
Sequence Length: 345
Pathway: Lipid metabolism; fatty acid biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.1.1.330
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B0FHH8 | MAALHWLLLAALLGCTLAEEQAIFYNCEEASEAVCSVKEVRINPCNPNKKCIFKKGVNASISFDFEPNFASSKLVTTLYGPFDVEFDEMTNVDACQYTKCPTEPGKSQVLDYTLYIGKKLPQGTYTFKWKLWNPEETSQLCCFKTTIKIRK | Function: Binds to lipopolysaccharide from a variety of Gram-negative bacteria and to lipid A.
PTM: N-glycosylated.
Sequence Mass (Da): 17102
Sequence Length: 151
Subcellular Location: Secreted
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P81446 | MNGHLASRRAWVWYFLMLGQVFGATVKAETKFSYERLRLRVTHQTTGEEYFRFITLLRDYVSSGSFSNEIPLLRQSTIPVSDAQRFVLVELTNEGGDSITAAIDVTNLYVVAYQAGDQSYFLRDAPRGAETHLFTGTTRSSLPFNGSYPDLERYAGHRDQIPLGIDQLIQSVTALRFPGGSTRTQARSILILIQMISEAARFNPILWRARQYINSGASFLPDVYMLELETSWGQQSTQVQQSTDGVFNNPIRLAIPPGNFVTLTNVRDVIASLAIMLFVCGERPSSSDVRYWPLVIRPVIADDVTCSASEPTVRIVGRNGMCVDVRDDDFHDGNQIQLWPSKSNNDPNQLWTIKRDGTIRSNGSCLTTYGYTAGVYVMIFDCNTAVREATLWEIWGNGTIINPRSNLVLAASSGIKGTTLTVQTLDYTLGQGWLAGNDTAPREVTIYGFRDLCMESNGGSVWVETCVISQQNQRWALYGDGSIRPKQNQDQCLTCGRDSVSTVINIVSCSAGSSGQRWVFTNEGAILNLKNGLAMDVAQANPKLRRIIIYPATGKPNQMWLPVP | Function: The A chain is responsible for inhibiting protein synthesis through the catalytic inactivation of 60S ribosomal subunits by removing adenine from position 4,324 of 28S rRNA. The B chain binds to cell receptors and probably facilitates the entry into the cell of the A chain; B chains are also responsible for cell agglutination (lectin activity). Inhibits growth of the human tumor cell line Molt4.
PTM: The A chain of variant MLA' is not glycosylated.
Catalytic Activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Sequence Mass (Da): 62628
Sequence Length: 564
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Q47XX8 | MTKFTSLLLVIFTTVLLSACDKENDSSSLSRILARGYINVGTIFGPTNYYTTANGFAGFEYELAKQYADSLNVELRIVPTYSLDELFIKLNTGEVDLLASGLSITDKRLQRFRFAPSYETISQKLVFKQGNVRPRKVADLTGTLMVTSGSSYVENLEKLKQTNSELAWQESTEFDSEELLRKVLSGEIDYTIIDSNNLAINRRYYPEISIGFSINEPEPLAWMVSENSHDDILASLVEFFGTVHHDGTLLALDDKYYGHIEQFNYVETRTFIKAVAGTLPEYQPLFEKYAQELDWRLLAAISYQESHWNPTARSYTGVRGMMMLTLATAKQMGIKSRLDTEQSIQGGAKYFKRMIAMMPDRIPTPDRIWFALASYNIGFGHLNDARIITQRQGGDPDRWVEVKSRLPLLQQKKYYKNTKHGYARGEEPVQYVDNIRRYYDTLSWLDEKAKEQAIALQLAQEKSQALLLNDIVNDSVNESTSEENATESILKEEEVTAETAQ | Function: Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella.
Catalytic Activity: Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 57042
Sequence Length: 501
Domain: The N-terminal domain does not have lytic activity and probably modulates enzymatic activity. The C-terminal domain is the catalytic active domain.
Subcellular Location: Cell outer membrane
EC: 4.2.2.n1
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A8ZWR8 | MRRPLRRVTVVLLWVALAIGVAWFYDYRRSMQSLWKIRQHGKIVVLTENNANSYYIYKETPMGFEYDLAKAFAGHLGVDLEVKTPGWDALFASLQRGDGDFIAASMTHTRKREQYADFSEPYLSVRQHLILHKSDHSIVTPAGLAGRTVHVREDTTYQQRLEALQADGIDLQLVLHRNTPTEELIEQVAKRQIDITVADSAIALLNRRYYPDIRIAFPIEKEQPLAWAVRKGDRGLRTEINRFFDEIKENGTFTRIYNRYYTAVDTFDYVDVKKFHQRIYTRLPRFRPLIEKAADRHGFDWQMIAAVIYQESHFDPFAQSHTGVKGLMQLTRVTAEEMGVTDRFDFEQNITAGVAYLAKLRHRFDDIEDPRTRLLFALASYNIGYGHVRDAQQIAKNMGMDPNRWQSLKEVLPLLRNREYYADTTYGYARGNEAVRYIERILTYYDILKQKKAV | Function: Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella.
Catalytic Activity: Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 52993
Sequence Length: 454
Domain: The N-terminal domain does not have lytic activity and probably modulates enzymatic activity. The C-terminal domain is the catalytic active domain.
Subcellular Location: Cell outer membrane
EC: 4.2.2.n1
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Q8XA45 | MKKLKINYLFIGILALLLAVALWPSIPWFGKADNRIAAIQARGELRVSTIHTPLTYNEINGKPFGLDYELAKQFADYLGVKLKVTVRQNISQLFDDLDNGNADLLAAGLVYNSERVKNYQPGPTYYSVSQQLVYKVGQYRPRTLGNLTAEQLTVAPGHVVVNDLQTLKETKFPELSWKVDDKKGSAELMEDVIEGKLDYTIADSVAISLFQRVHPELAVALDITDEQPVTWFSPLDGDNTLSAALLDFFNEMNEDGTLARIEEKYLGHGDDFDYVDTRTFLRAVDAVLPQLKPLFEKYAEEIDWRLLAAIAYQESHWDAQATSPTGVRGMMMLTKNTAQSLGITDRTDAEQSISGGVRYLQDMMSKVPESVPENERIWFALAAYNMGYAHMQDARALTAKTKGNPDSWADVKQRLPLLSQKPYYSKLTYGYARGHEAYAYVENIRKYQISLVGYLQEKEKQATEAAMQLAQDYPAVSPTELGKEKFPFLSFLSQSSSNYLTHSPSLLFSRKGSEEKQN | Function: Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella.
Catalytic Activity: Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 58317
Sequence Length: 518
Domain: The N-terminal domain does not have lytic activity and probably modulates enzymatic activity. The C-terminal domain is the catalytic active domain.
Subcellular Location: Cell outer membrane
EC: 4.2.2.n1
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P82679 | MQTIPSTTETAADFDAVIXGAGFXGLYALHR | Function: Catalyzes the NADPH- and oxygen-dependent oxidation of the monocyclic monoterpene ketones 1-hydroxy-2-oxolimonene, dihydrocarvone and menthone. Is able to convert all enantiomers of these natural substrates with almost equal efficiency. Is thus involved in the conversion of the monocyclic monoterpene ketone intermediates formed in the degradation pathways of all stereoisomers of three different monocyclic monoterpenes, i.e. limonene, (dihydro)carveol and menthol, which likely make R.erythropolis able to grow on these compounds as the sole source of carbon and energy.
Catalytic Activity: 1-hydroxylimonen-2-one + NADPH + O2 = 3-isopropenyl-6-oxoheptanoate + H2O + NADP(+)
Sequence Mass (Da): 3277
Sequence Length: 31
Pathway: Terpene metabolism; monoterpene degradation.
EC: 1.14.13.105
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O51798 | MFAWYKAGSPQQKKTFWACYSGWALDSFDMQMFSFLLPALTLTWGLTKAEVGVLGTVALVVTAIGGWGAGILSDRYGRARILVLAIIWFTLFGVLAGFAQSYQQLLIARTLQGLGFGGEWAVGAALMAEVIDSRHRGKAIGFVQSGFALGWALAVVVATLLLAWLPKEMAWRVAFWSGIIPALIVLFIRRHVKDSSMFERARQSRAPRASLSSVFNRKYARTLALSSVLVIGLQAGCYAILVWLPSLLNQRQVAAGSMIVTVFIMAFGSFCGFAVTADLSDRIGRRPTLILLSVCAWIVTVSYMLLPLNTTLTAILGFLVGFSAIGMFAALGPFLSELFPTNVRTTCMGFAYNVGKSIGAGSVVGVGVLSTHIGLANAMGTFCLVAYAFAVFGIMLLPETRGIAIENIGEADAHSPAAPLAQPASARS | Function: Probable uptake of 4-methylmuconolactone.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45804
Sequence Length: 428
Subcellular Location: Cell membrane
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Q6CAP9 | MSQFVLPAVASEGIINWPFLTGFMLGQFSVGLVLLIFVRFFIFSDQTEPDINTQRRTAKVLPTGNPSTDAILEKTYYNTKTHQPESLDWFSVLVAQALYQLRDEVRGNDEVLERLNEILKSDKLPGFLDTINVVDLDIGDAFPQFGACKVNKDESGDLEAEIKVSLEDTIKLGVETKMLLNFPIPKFASVPVSLSVSLVKFSGTLTVAIRSAFNSGEANRVLVSFAPDYELQWKIESSVGSTQKLQNAEKISRLIESRIRRWFKDRCVYPEYQQFELPKLWRKTSAPPPSAGAGTGTSTGVPPSPFPQPANPSSVPKPLELPGGFPHRNMSMSSQRPNINNPKFIRSMSVNTRPTYSSSFYEMQGTAGSSSGSAVADEAYRSLQTSPRR | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The MDM12-MMM11 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 43117
Sequence Length: 389
Domain: The SMP-LTD domain is a barrel-like domain that can bind various types of glycerophospholipids in its interior and mediate their transfer between two adjacent bilayers.
Subcellular Location: Endoplasmic reticulum membrane
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Q6CA06 | MVIPAELIQKALKQQSGWGFTEGLVLGQLSVIITVIIILKFVIFAENKSPKKGNDMTAVSAKDKEAEHVAMGGQTANGVKTSGVRRNKSSTNLRNRLATGAAGASISRPGSSRVSMVRSTSGAVPVLGQNGGATPRGMAGSSVAGSTSNLAVPVPTTPTIAEGIEPENDSTLQDDSAIIDLDLDLDLSPVDEILHKTCYQLSSHAPESLDWFNVLVAQIITQLRFDAKANNNLNLLNSLDAAFNSKRPDFIDRINVTEINLGDDYPILSNCKITHKGTGPAGSGAASGNNMPNNAEYDDSRLEAQMDIDLSDTITLGIETRLNLNQPKILSPFLSLSTSLPVSLSVTIVRFTARLNISLYQQIEQTEEDEKDKRDTILSINFEPDYKLQLSVKSLVGSRSRLQNVPTLESLVDSKIQKWFRDHYVEPHQMIFILPSLWPRKKRSATAGAAGTATGADTASGSS | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 49799
Sequence Length: 463
Domain: The SMP-LTD domain is a barrel-like domain that can bind various types of glycerophospholipids in its interior and mediate their transfer between two adjacent bilayers.
Subcellular Location: Endoplasmic reticulum membrane
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Q75FA5 | MKGVENTLSQSESVNRGYNGWMGMESETSARATHSSEQMISLEEYVREMLPMHLQKLLMERIIEAEQTGAAHTSVFAAPTGVAAQYPAMGPPMLPGQTFSSRSFAEGLVVGQLSVIVVLIFFIKFFIFSDGPAKTGGGGGSSAESRSSGFTGSPLTSTTSRLLSTLIKRGGKEGTEFAEDSENERTRQINAILEKTYYDVETHSPESLDWFNVLIAQTIQKFREEALQKDNIVHSLNDFISRKSSQLPNYLDAVKITELDIGDDFPIFSNCRIKYSPPLNKKRLEAKIDIDLSDRLTLGIETRLLMNYPKYLTASLPVKLTVSMLRFQACLTVSLTTAEEFVPTMAATTDTDAGDSEGHYLVFSFSPDYRMEFDIKSLIGARSKLENIPKISSLVEYQIKKWFMDRCVEPRFQFVKLPSMWPRSKNTREEKSDMQEEDPSRAPE | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The MDM12-MMM1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The MDM10-MDM12-MMM1 subcomplex further acts in the TOM40-specific pathway after the action of the MDM12-MMM1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 49774
Sequence Length: 444
Domain: The SMP-LTD domain is a barrel-like domain that can bind various types of glycerophospholipids in its interior and mediate their transfer between two adjacent bilayers.
Subcellular Location: Endoplasmic reticulum membrane
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A1CM86 | MSSQPGDPATLPAQSSLSFTQGFLLGQLSVVLVLAAFIKFFIFGEAPPPPSRGLSHRSATHRRSNSIYSNSPQEAGSRSLREKPSTSNVLRPVPSSSTNTRSILRKTYYSAIPTNPAKHGRLRIHHSSHQPESLDWFNVLIAQTIAQYRQTAYSLKDSPTSSILNSLTAALNNPEKKPAFIDKITVTDISLGEEFPIFSNCRIIAVDDPNSDGGRLQALMDVDLSDDNLSIAIETQLLLNYPKPCSAILPVALSISVVRFSGTLCISLVPASTPPLDTPSHSPSPPTADTATSGRSKPGDKAGGNQPRSNGSTEDPAGGNPPKTSPKSNVAFSFLPDYRLDLSVRSLIGSRSRLQDVPKVAQLVEARVQAWFEERVVEPRVQVVGLPDLWPRMGRTGVRTGDDAETASNGPRSTVSADIGGSARHEELAREPEALRFRGLLGARPPFDVASRTSSFNVETGDLRSRSMTRQESSGDLSDQLHIPGSLPEAVTPG | Function: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. The mdm12-mmm1 subcomplex functions in the major beta-barrel assembly pathway that is responsible for biogenesis of all outer membrane beta-barrel proteins, and acts in a late step after the SAM complex. The mdm10-mdm12-mmm1 subcomplex further acts in the TOM40-specific pathway after the action of the mdm12-mmm1 complex. Essential for establishing and maintaining the structure of mitochondria and maintenance of mtDNA nucleoids.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 53099
Sequence Length: 494
Domain: The SMP-LTD domain is a barrel-like domain that can bind various types of glycerophospholipids in its interior and mediate their transfer between two adjacent bilayers.
Subcellular Location: Endoplasmic reticulum membrane
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P50282 | MSPWQPLLLVLLALGYSFAAPHQRQPTYVVFPRDLKTSNLTDTQLAEDYLYRYGYTRAAQMMGEKQSLRPALLMLQKQLSLPQTGELDSETLKAIRSPRCGVPDVGKFQTFDGDLKWHHHNITYWIQSYTEDLPRDVIDDSFARAFAVWSAVTPLTFTRVYGLEADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELWSLGKGAVVPTYFGNANGAPCHFPFTFEGRSYLSCTTDGRNDGKPWCGTTADYDTDRKYGFCPSENLYTEHGNGDGKPCVFPFIFEGHSYSACTTKGRSDGYRWCATTANYDQDKADGFCPTRADVTVTGGNSAGEMCVFPFVFLGKQYSTCTSEGRSDGRLWCATTSNFDADKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMYPMYHYHEDSPLHEDDIKGIHHLYGRGSKPDPRPPATTAAEPQPTAPPTMCSTAPPMAYPTGGPTVAPTGAPSPGPTGPPTAGPSEAPTESSTPDDNPCNVDVFDAIADIQGALHFFKDGRYWKFSNHGGNQLQGPFLIARTWPAFPSKLNSAFEDPQPKKIFFFLWAQMWVYTGQSVLGPRSLDKLGLGSEVTLVTGLLPRRGGKALLISRERIWKFDLKSQKVDPQSVTRLDNEFSGVPWNSHNVFQYQDKAYFCHDKYFWRVSFHNRVNQVDHVAYVTYDLLQCP | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (By similarity). Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (By similarity). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (By similarity). Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N-terminal one quarter fragments. Degrades fibronectin but not laminin or Pz-peptide (By similarity).
PTM: N- and O-glycosylated.
Catalytic Activity: Cleavage of gelatin types I and V and collagen types IV and V.
Sequence Mass (Da): 78611
Sequence Length: 708
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellular Location: Secreted
EC: 3.4.24.35
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G5EGM1 | MFTGLHDILIILFLLVTLKIAQNVDHTKFLQKYGYLTSGDNQLSSESLSDALKNMQRMAGLEETGELDERTIQMMERPRCGHPDVEDHQKSRGKRYAPPQFKWKEKIITYGCKAVGTSTRISLDDLRRTMHQAASQWSELADVEIVESSVKNPMMVISAGRENHYPCTVRFDTKTLAHAFFPTNGQIHINDRVQFAMTNYTERMGANSLYSVVAHEMGHALGFSHSPDIDSVMFAYDTPRKWKFTSMDKYNMRSYYGAKASKKENEEEERKTENEDKRRKTEKDRGRTREHESDDIRPNECRVENPIVVQYRGEYLIFKSQWVWRVSSDWKRLIIKAVPINQLFPGLPNPIDAAVTVGHNLWVFVGEMIYVIYGNHMVHAPLRLSDIGINEKYVDLAYEWHYFNPPAVYIWKGSRYWKLDEKMYHRRVDERYPKDTDLNWARVPKGVHSAFTYEKEIHLLRGNQVFRMNSSRSVFDIADGYPQPLQSFFGFCPRNEKLVLNSSSSHFSLIYATITILILIF | Function: Metalloprotease which, together with cadherin cdh-3 and hemicentin him-4, plays a role in anchor cell (AC) invasion during postembryonic vulval development probably by promoting the degradation of the basement membrane separating the gonad from the vulva epithelium.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 60700
Sequence Length: 521
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellular Location: Cell membrane
EC: 3.4.24.-
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Q9A710 | MIGFLIMLVSLLFVLSVVVTVHELGHYWAARACGVAIERFSIGFGAPLISWRDKRGVEWCVASIPLGGYVRFAGDENAASVPDQNDLDAMRNEIRRREGDDAVNRYFHFKPVWQRAFIAVAGPMANFILAILVFAVILVSFGAQKTSTTVGEVVAGTPAAAAGFKPGDVILKADNRQIRSFQDIQGYVALRANMPIDFAVERDGRTVHLTATPRLVERQNEISGRVKVGELGLRSAPGGRFERSSLLSAIPDATVEVWDMIKTIAFYLGRLLMGQLPADQISGIIGIGHTAGAVTNGVVEQAPNGKALAIGLIYSQFWLIASLSVSIGFMNLLPIPVLDGGHLVMYAYEAVAKRPLRAEFQAAGFRAGLALILGFMLFAAWNDLNRYDVFKFIGGLFT | Function: Involved in the regulated intramembrane proteolysis (RIP) of the short isoform of PodJ protein (PodJS), during the swarmer-to-stalked transition. The cleavage occurs near or within the single transmembrane of PodJS thereby releasing the N-terminal segment into the cytoplasm for subsequent degradation. It contributes to preserve asymmetry in the next cell cycle through sequential degradation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43231
Sequence Length: 398
Subcellular Location: Cell inner membrane
EC: 3.4.24.-
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O44836 | MTKWSPNGNPLSTIYLILSLFTLAHTAPTTQHSRTTTQLRLEDEDGGGGVDEDSIHFVKGQMEKYGYLKGIDHSSPQEFRQALMFFQEVLEVEQTGNVDEMTVEAASKPRCTQTDVRQEQTKRTKRFTLSKRAKWAHASGQSVTLKWYISDYTSDIDRLETRKVVEKAFKLWSSQSYIKNEKKVTLTFQEASSKDEADINILWAEGNHGDEHDFDGANGKIEGNKKENVLAHTFFPGYARPLNGDIHFDDAEDWEIDVDQVGHGSNKRFFPYVLAHEIGHALGLDHSQKADALMHPYYKNVPINEIQLDIDDKCGVIWNYGGASDFCLYVWLMSQIVEAHNSSAQNNHGVGSITSSRTNKKSFKSEGFFLFQLKFPHSTLTHTDDVVMREKDKRSYRGDSKIPKCSSNNSSQRTLAEKKLTLGLHLSEADAKRYTEMVCNFLAGLHMWRTNPNHHASESLEKEYKGVSQEMGTFSGKSIAVRRLIRHAEHQKERSEKGPLDPDYFDDDFFENFFMEYSK | Function: Metalloprotease involved in molting, a process during larval stages in which a new cuticle is formed and the old cuticle is shed . Plays a role in thermotolerance probably by preventing the accumulation of oxidized lipoproteins and cholesterol .
Sequence Mass (Da): 59254
Sequence Length: 519
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellular Location: Secreted
EC: 3.4.24.-
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G5EBU3 | MRLIYVIAILLVSTCQAGFFSSLVSRFTGGGNSSPSSSSSSSSFSNSRKPSLSDEKARSYLQTFGYVPPSNSLQSRNGMAGDIQSAEQVFKSAIRKFQEFAGIAKTGFLDAATKAKMALSRCGVTDAPLALTSGSSQFKWSKTRLTYSIESWSSDLSKDDVRRAISEAYGLWSKVTPLEFSEVPAGSTSDIKIRFGVRNHNDPWPFDGEGGVLAHATMPESGMFHFDDDENWTYKDARKIHNNEATDLLAVAIHEGGHTLGLEHSRDENAIMAPFYQKTTDSSGNYVYPNLKSDDISAIQAIYGAGSGRSSSGSDFGGSSGGGSRTTARPTTTTRSWFGRFFGDDDDDVRSRTTTRRTTLWPTTQSPFSGDDWGSGSGSSGRGGSSSGSSGGGCPSHIDAYTPSSSFSYAFSGSQVYTISGTKVTKVQSIHDLFPSAPTPVNAALWNPISGSMLLFSSNRVYSYYFSNIRQIFQMDSGFPKTLPSDLGFSVSGALRWINGHQILMSSGDEFAVYDEFWNQVTLKNRISSYFPNLPRGVKGVESPAGSVITAFTSNQVFEYNSRTKSIGRQSGFSSYIAC | Function: Metalloproteinase.
Sequence Mass (Da): 62540
Sequence Length: 579
Domain: The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme.
Subcellular Location: Secreted
EC: 3.4.24.-
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A0QP27 | MFAWWGRTVYQFRYIVIGVMVALCLGGGVYGISLGNHVTQSGFYDEGSQSVAASLIGDEVYGRDRTSHVVAILTPPDDKKVTDKAWQKKVTEELDQVVKDHEDQIVGWVGWLKAPDTTDPTVSAMKTQDLRHTFISIPLQGDDDDEILKNYQVVEPELQQVNGGDIRLAGLNPLASELTGTIGEDQKRAEVAAIPLVAVVLFFVFGTVIAAALPAIIGGLAIAGALGIMRLVAEFTPVHFFAQPVVTLIGLGIAIDYGLFIVSRFREEIAEGYDTEAAVRRTVMTSGRTVVFSAVIIVASSVPLLLFPQGFLKSITYAIIASVMLAAILSITVLAAALAILGPRVDALGVTTLLKIPFLANWQFSRRIIDWFAEKTQKTKTREEVERGFWGRLVNVVMKRPIAFAAPILVVMVLLIIPLGQLSLGGISEKYLPPDNAVRQSQEQFDKLFPGFRTEPLTLVMKREDGEPITDAQIADMRAKALTVSGFTDPDNDPEKMWKERPANDSGSKDPSVRVIQNGLENRNDAAKKIDELRALQPPHGIEVFVGGTPALEQDSIHSLFDKLPLMALILIVTTTVLMFLAFGSVVLPIKAALMSALTLGSTMGILTWMFVDGHGSGLMNYTPQPLMAPMIGLIIAVIWGLSTDYEVFLVSRMVEARERGMSTAEAIRIGTATTGRLITGAALILAVVAGAFVFSDLVMMKYLAFGLLIALLLDATIIRMFLVPAVMKLLGDDCWWAPRWMKRVQEKLGLGETELPDERKRPTVRESETDQRALVGVGAPPPPPRPHDPTHPAPEPVRPMPPMRSNAPSAAGTARISTPPQPPQPPQAPAQQAGDEPATTRFAMARNAVRNAVNSAVHGGAGSAAAPTERAPRPGGPAQPPAPPQREEREIESWLGALRGPAPAKNVPQPPAQPQRPSTDTTRAMPPQGRPPAGPADRGNENAPTTAFSAQRPPNGGAPADATTAIPTPPQREQEPSTEKLNTREDAPEDPETKRRGGGMSAQDLLRREGRL | Function: Transports trehalose monomycolate (TMM) to the cell wall . Flips TMM across the inner membrane. Membrane potential is not required for this function . Transports probably phosphatidylethanolamine (PE) as well. Binds specifically both TMM and PE, but not trehalose dimycolate (TDM). Binds also diacylglycerol (DAG) and other phospholipids, including phosphatidylglycerol (PG), phosphatidylinositol (PI), and cardiolipin (CDL) . Contributes to membrane potential, cell wall composition, antibiotic susceptibility and fitness .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 109399
Sequence Length: 1013
Subcellular Location: Cell inner membrane
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P9WJV5 | MFAWWGRTVYRYRFIVIGVMVALCLGGGVFGLSLGKHVTQSGFYDDGSQSVQASVLGDQVYGRDRSGHIVAIFQAPAGKTVDDPAWSKKVVDELNRFQQDHPDQVLGWAGYLRASQATGMATADKKYTFVSIPLKGDDDDTILNNYKAIAPDLQRLDGGTVKLAGLQPVAEALTGTIATDQRRMEVLALPLVAVVLFFVFGGVIAAGLPVMVGGLCIAGALGIMRFLAIFGPVHYFAQPVVSLIGLGIAIDYGLFIVSRFREEIAEGYDTETAVRRTVITAGRTVTFSAVLIVASAIGLLLFPQGFLKSLTYATIASVMLSAILSITVLPACLGILGKHVDALGVRTLFRVPFLANWKISAAYLNWLADRLQRTKTREEVEAGFWGKLVNRVMKRPVLFAAPIVIIMILLIIPVGKLSLGGISEKYLPPTNSVRQAQEEFDKLFPGYRTNPLTLVIQTSNHQPVTDAQIADIRSKAMAIGGFIEPDNDPANMWQERAYAVGASKDPSVRVLQNGLINPADASKKLTELRAITPPKGITVLVGGTPALELDSIHGLFAKMPLMVVILLTTTIVLMFLAFGSVVLPIKATLMSALTLGSTMGILTWIFVDGHFSKWLNFTPTPLTAPVIGLIIALVFGLSTDYEVFLVSRMVEARERGMSTQEAIRIGTAATGRIITAAALIVAVVAGAFVFSDLVMMKYLAFGLMAALLLDATVVRMFLVPSVMKLLGDDCWWAPRWARRLQTRIGLGEIHLPDERKRPVSNGRPARPPVTAGLVAARAAGDPRPPHDPTHPLAESPRPARSSPASSPELTPALEATAAPAAPSGASTTRMQIGSSTEPPTTRLAAAGRSVQSPASTPPPTPTPPSAPSAGQTRAMPLAANRSTDAAGDPAEPTAALPIIRSDGDDSEAATEQLNARGTSDKTRQRRRGGGALSAQDLLRREGRL | Function: Transports trehalose monomycolate (TMM) to the cell wall. Flips TMM across the inner membrane . Membrane potential is not required for this function. Transports probably phosphatidylethanolamine (PE) as well. Binds specifically both TMM and PE, but not trehalose dimycolate (TDM). Binds also diacylglycerol (DAG) and other phospholipids, including phosphatidylglycerol (PG), phosphatidylinositol (PI), and cardiolipin (CDL). Contributes to membrane potential, cell wall composition, antibiotic susceptibility and fitness (By similarity). Could also be part of a heme-iron acquisition system .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 100904
Sequence Length: 944
Subcellular Location: Cell inner membrane
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P9WJV1 | MIVQRTAAPTGSVPPDRHAARPFIPRMIRTFAVPIILGWLVTIAVLNVTVPQLETVGQIQAVSMSPDAAPSMISMKHIGKVFEEGDSDSAAMIVLEGQRPLGDAAHAFYDQMIGRLQADTTHVQSLQDFWGDPLTATGAQSSDGKAAYVQVKLAGNQGESLANESVEAVKTIVERLAPPPGVKVYVTGSAALVADQQQAGDRSLQVIEAVTFTVIIVMLLLVYRSIITSAIMLTMVVLGLLATRGGVAFLGFHRIIGLSTFATNLLVVLAIAAATDYAIFLIGRYQEARGLGQDRESAYYTMFGGTAHVVLGSGLTIAGATFCLSFTRLPYFQTLGVPLAIGMVIVVAAALTLGPAIIAVTSRFGKLLEPKRMARVRGWRKVGAAIVRWPGPILVGAVALALVGLLTLPGYRTNYNDRNYLPADLPANEGYAAAERHFSQARMNPEVLMVESDHDMRNSADFLVINKIAKAIFAVEGISRVQAITRPDGKPIEHTSIPFLISMQGTSQKLTEKYNQDLTARMLEQVNDIQSNIDQMERMHSLTQQMADVTHEMVIQMTGMVVDVEELRNHIADFDDFFRPIRSYFYWEKHCYDIPVCWSLRSVFDTLDGIDVMTEDINNLLPLMQRLDTLMPQLTAMMPEMIQTMKSMKAQMLSMHSTQEGLQDQMAAMQEDSAAMGEAFDASRNDDSFYLPPEVFDNPDFQRGLEQFLSPDGHAVRFIISHEGDPMSQAGIARIAKIKTAAKEAIKGTPLEGSAIYLGGTAAMFKDLSDGNTYDLMIAGISALCLIFIIMLITTRSVVAAAVIVGTVVLSLGASFGLSVLIWQHILGIELHWLVLAMAVIILLAVGADYNLLLVARLKEEIHAGINTGIIRAMGGSGSVVTAAGLVFAFTMMSFAVSELTVMAQVGTTIGMGLLFDTLIVRSFMTPSIAALLGKWFWWPQVVRQRPIPQPWPSPASARTFALV | Function: Part of an export system, which is required for biosynthesis and secretion of siderophores.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 104785
Sequence Length: 964
Subcellular Location: Cell inner membrane
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P41218 | MVNEYKKILLLKGFELMDDYHFTSIKSLLAYDLGLTTKMQEEYNRIKITDLMEKKFQGVACLDKLIELAKDMPSLKNLVNNLRKEKSKVAKKIKTQEKAPVKKINQEEVGLAAPAPTARNKLTSEARGRIPVAQKRKTPNKEKTEAKRNKVSQEQSKPPGPSGASTSAAVDHPPLPQTSSSTPSNTSFTPNQETQAQRQVDARRNVPQNDPVTVVVLKATAPFKYESPENGKSTMFHATVASKTQYFHVKVFDINLKEKFVRKKVITISDYSECKGVMEIKEASSVSDFNQNFEVPNRIIEIANKTPKISQLYKQASGTMVYGLFMLQKKSVHKKNTIYEIQDNTGSMDVVGSGKWHNIKCEKGDKLRLFCLQLRTVDRKLKLVCGSHSFIKVIKAKKNKEGPMNVN | Function: May act as a transcriptional activator/repressor in the myeloid lineage. Plays a role in the granulocyte/monocyte cell-specific response to interferon. Stimulates the DNA binding of the transcriptional repressor protein YY1.
Sequence Mass (Da): 45836
Sequence Length: 407
Domain: Its N-terminal half (200 amino acids) is sufficient for maximum enhancement of YY1 DNA binding and a portion of this sequence is responsible for binding YY1.
Subcellular Location: Nucleus
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A0A0H3AJF5 | MFVYGSIINPCPTEHVMSVLAISITTVALAEIGDKTQLLSLLLASRYRKPIPIIAAIFLATLANHALAAWLGVVVADYLSPDILKWVLVVSFLTMAGWILIPDKLDGEESISTRGPFVASFIAFFMAEIGDKTQIATSILGAQYADALSWVIVGTTLGMLLANVPVVLIGKLSADKMPLGLIRKVTAGLFLLMALATAFF | Function: Involved in manganese homeostasis. May function as a manganese exporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21380
Sequence Length: 200
Subcellular Location: Cell inner membrane
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C0SP78 | MASEREQISRKVALIALIANLILMAGKVFFGLVGDSEAVFADGIHSAADVVASIAVLAVIGISNKPPDQDHPFGHGKAEVISEAIVGIILVIVSVYILIEAILSFVKGPSVPQYSALFAALISYVAKEILYRYSIKQGKKWNSKAIIAIAYDHKGDIVASLAAFIGVLLAIIGNSRGWSYLLYADAIASAIVAYLIFKISMELIRPSVDVLMEKSVDPELIEEYKAVIFQCDQVKRIDRIRAREHGHYKLLDVRLSLDHDLTIKQGHDIAREIRNEIKRQFSDVEEVLIHVNPYFEE | Function: Primary efflux pump for manganese. May prevent manganese intoxication.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32854
Sequence Length: 297
Subcellular Location: Cell membrane
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P46348 | MERYDELKKGESGALVSIAAYLVLSAIKLIIGYLFHSEALTADGLNNTTDIIASVAVLIGLRISQKPPDEDHPYGHFRAETIASLIASFIMMVVGLQVLFSAGESIFSAKQETPDMIAAWTAAGGAVLMLIVYRYNKRLAKKVKSQALLAAAADNKSDAFVSIGTFIGIVAAQFHLAWIDTVTAFVIGLLICKTAWDIFKESSHSLTDGFDIKDISAYKQTIEKISGVSRLKDIKARYLGSTVHVDVVVEVSADLNITESHDIANEIERRMKEEHAIDYSHVHMEPLEQK | Function: Secondary manganese efflux system. May prevent manganese intoxication.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31785
Sequence Length: 290
Subcellular Location: Cell membrane
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P54745 | MVLFYRAHWRDYKNDQVRIMMNLTTLTHRDALCLNARFTSREEAIHALTQRLAALGKISSTEQFLEEVYRRESLGPTALGEGLAVPHGKTAAVKEAAFAVATLSEPLQWEGVDGPEAVDLVVLLAIPPNEAGTTHMQLLTALTTRLADDEIRARIQSATTPDELLSALDDKGGTQPSASFSNAPTIVCVTACPAGIAHTYMAAEYLEKAGRKLGVNVYVEKQGANGIEGRLTADQLNSATACIFAAEVAIKESERFNGIPALSVPVAEPIRHAEALIQQALTLKRSDETRTVQQDTQPVKSVKTELKQALLSGISFAVPLIVAGGTVLAVAVLLSQIFGLQDLFNEENSWLWMYRKLGGGLLGILMVPVLAAYTAYSLADKPALAPGFAAGLAANMIGSGFLGAVVGGLIAGYLMRWVKNHLRLSSKFNGFLTFYLYPVLGTLGAGSLMLFVVGEPVAWINNSLTAWLNGLSGSNALLLGAILGFMCSFDLGGPVNKAAYAFCLGAMANGVYGPYAIFASVKMVSAFTVTASTMLAPRLFKEFEIETGKSTWLLGLAGITEGAIPMAIEDPLRVIGSFVLGSMVTGAIVGAMNIGLSTPGAGIFSLFLLHDNGAGGVMAAIGWFGAALVGAAISTAILLMWRRHAVKHGNYLTDGVMP | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane . This system is involved in mannosyl-D-glycerate transport . Also involved in thermoinduction of ompC .
Catalytic Activity: (2R)-2-O-(alpha-D-mannosyl)-glycerate(out) + N(pros)-phospho-L-histidyl-[protein] = (2R)-2-O-(6-phospho-alpha-D-mannosyl)-glycerate(in) + L-histidyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69668
Sequence Length: 658
Domain: The PTS EIIA type-2 domain is phosphorylated by phospho-HPr on a histidyl residue. Then, it transfers the phosphoryl group to the PTS EIIB type-2 domain.
Subcellular Location: Cell inner membrane
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P54746 | MKAVSRVHITPHMHWDREWYFTTEESRILLVNNMEEILCRLEQDNEYKYYVLDGQTAILEDYFAVKPENKDRVKKQVEAGKLIIGPWYTQTDTTIVSAESIVRNLMYGMRDCLAFGEPMKIGYLPDSFGMSGQLPHIYNGFGITRTMFWRGCSERHGTDKTEFLWQSSDGSEVTAQVLPLGYAIGKYLPADENGLRKRLDSYFDVLEKASVTKEILLPNGHDQMPLQQNIFEVMDKLREIYPQRKFVMSRFEEVFEKIEAQRDNLATLKGEFIDGKYMRVHRTIGSTRMDIKIAHARIENKIVNLLEPLATLAWTLGFEYHHGLLEKMWKEILKNHAHDSIGCCCSDKVHREIVARFELAEDMADNLIRFYMRKIADNMPQSDADKLVLFNLMPWPREEVINTTVRLRASQFNLRDDRGQPVPYFIRHAREIDPGLIDRQIVHYGNYDPFMEFDIQINQIVPSMGYRTLYIEANQPGNVIAAKSDAEGILENAFWQIALNEDGSLQLVDKDSGVRYDRVLQIEESSDDGDEYDYSPAKEEWVITAANAKPQCDIIHEAWQSRAVIRYDMAVPLNLSERSARQSTGRVGVVLVVTLSHNSRRIDVDINLDNQADDHRLRVLVPTPFNTDSVLADTQFGSLTRPVNDSAMNNWQQEGWKEAPVPVWNMLNYVALQEGRNGMAVFSEGLREFEVIGEEKKTFAITLLRGVGLLGKEDLLLRPGRPSGIKMPVPDSQLRGLLSCRLSLLSYTGTPTAAGVAQQARAWLTPVQCYNKIPWDVMKLNKAGFNVPESYSLLKMPPVGCLISALKKAEDRQEVILRLFNPAESATCDATVAFSREVISCSETMMDEHITTEENQGSNLSGPFLPGQSRTFSYRLA | Cofactor: Binds 1 divalent metal cation per subunit.
Function: May hydrolyze 6-phospho-mannosyl-D-glycerate to mannose-6-phosphate and glycerate.
Catalytic Activity: (2R)-2-O-(6-phospho-alpha-D-mannosyl)-glycerate + H2O = (R)-glycerate + alpha-D-mannose 6-phosphate
Sequence Mass (Da): 100015
Sequence Length: 877
EC: 3.2.1.-
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Q9KER1 | MKKTAHIISHSHWDREWYMPFEGHRYYLIQLMDDLLELFATDPNFRSFHMDGQTIMLEDYLNIRPEKEAEVRKYIQDGRLVIGPWYILQDAFLTSAEANVRNLLYGIKDTETFGQKREQIGYFPDTFGIYGQAPQLLAQAGIRAAVFGRGVTPTGFNNQVQHDDYSSPFSELIWEAPDGSQVIGILLANWYSNGNEIPTDEDEAQTFWVKKLRDAERFASTSQLLFMNGCDHQPVQKDVTQAIKVAETLFPDVAFKHSNFHDYLTQIKEELPKELQKITGELRNQKTDGWSTLVNTASARIYLKQANDRCQTLLTNVLEPMCLLVENKSLHRDFSEYYWKLLMENHPHDSICGCSIDAVHREMKTRFEKVEAGATTFIAEQGKEIAAQINTLHDSEEAIPLVVLKTNGTSGKRVVRHKVAMKKIYFDEMDFRHIPDRLKEIVMPTYRLEFPNKGSVPIEVQDAGVRFGYDLPRDGFRRPYYARELEVTFSYDSDLYLGYECGFLVPVEEKQTEARKELIGDPSMNTLENEAMKVMIHRNGSYSILDKTTGFEYRHLGIYEDVGDIGNEYMFKASSDGVRYTTEACEASIRIIENNSLCATVEICQTLSVPAAADERLKEEQERLVWHPDRKAGRSKERTDITLRTELTLEQGAKGLKVNVNIDNTAKDHRMRALFPVERARGNHYADSIYEIVERPNTPDPKWQNPAFDHHMQRLVSLDNGEYGLTIATKGLHEYEIVSDSIAVTLLRSVGELGDWGLFETPEAQCFGQNEAQFVLLPHKGDVLSANVYVAAYDDPVEPTVIQTEQSMGPLPHATNLFQWSGEGLVLTACKPTMDGRGMILRWFNPKREGEALIVQSTHFLQIYRSTILEEQIEKLGTENVQIEVRPQEIVTLRFE | Cofactor: Binds 1 divalent metal cation per subunit.
Function: May hydrolyze 6-phospho-mannosyl-D-glycerate to mannose-6-phosphate and glycerate.
Catalytic Activity: (2R)-2-O-(6-phospho-alpha-D-mannosyl)-glycerate + H2O = (R)-glycerate + alpha-D-mannose 6-phosphate
Sequence Mass (Da): 102540
Sequence Length: 896
EC: 3.2.1.-
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Q49W87 | MAIQILVNLILSVFWLFVTGSYNFNNFILGYLFALLLVYIMRGVLPGRFYLITVYKIIKLFLVFLIELIKANIDVIRIVVKPNIDNEPAFFTYNTDLKKDWQIVLLSNLITLTPGTIVLGISDDRTKIYIHSIDFSTKEEEVESIKSSLEKVVREVGENE | Function: Mnh complex is a Na(+)/H(+) antiporter involved in Na(+) excretion.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18439
Sequence Length: 160
Subcellular Location: Cell membrane
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B2UPK4 | MARILVGLSGGVDSSVAAALLVEQGHDVVGAYMKNWVNDEGIPGECPWEQDIQDALAVAKTTGIEFRVIDLVDEYRARIVNYLIEGYRAGYTPNPDVLCNREMKFGVFLDYALEQGFDYVATGHYARRMDTPQGAFILRGRDPNKDQSYFLSLMRPDQIARAVFPLGDLLKPEVRVLAEKYGLPTARKKDSQGICFIGQVKMSDFLRHYLPDKPGNIVDTEGRTLGTHNGLHLFTMGQRKGHGVASPREGVAYVVVGKDVRRNRLILGYEDASTRGLYASRAVVGGISNTLAPLPARVMAQPRYRAKAEWASCEYLEEGKVRLGFDTPLRALAVGQVCAFYDGGKLLGGGFFESIEP | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 39372
Sequence Length: 357
Subcellular Location: Cytoplasm
EC: 2.8.1.13
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Q5WHN4 | MKKREDTRVVVGMSGGVDSSVTALLLKEQGYDVIGIFMKNWDDSNDSGFCSATEDYEDVERVAQQLGIPYYAVNFEKQYWDKVFTYFLEEYKAGRTPNPDVMCNKEIKFKAFLNHAISLGADYVATGHYAQLQELDGEYRLIKGADANKDQTYFLNALSQKQLSKVMFPLGHLQKAEVRKIAAEAELATATKKDSTGICFIGERDFKEFLQTFLPAQPGRMETMDGIDKGQHDGLMYYTLGQRQGLGIGGAGEPWFVIDKDLERNVLIVGQGYHHPGLYSDGLWATDMNWIAKEERTSPFTCKAKFRYRQEDQGVTVFPKEDGRAFIQFDQPQRAITPGQAVVLYEGDRCIGGGVIDKIHRENA | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 41035
Sequence Length: 364
Subcellular Location: Cytoplasm
EC: 2.8.1.13
|
A7HCV7 | MRVLVALSGGVDSSTAAALLVAEGHDVIGVSMRVADYSDARRGRSCCAPDDLEDARAAARRLDIPFYVANVEARFRERVIEPFVRDYVEGRTPNPCVACNSDVKFDWLLARARALGAKLATGHYARVERRGGRFALCRAGDPAKDQTYFLYGLGQEALRDVLFPVGDLAKRDVRAVAAQAGLPNAEKAESQEICFVTQGDAGDFVALRAPGSVRAGEIVSTAGEVLGRHDGVHRFTVGQRRGLGLAGPAPRYVVRLEPGTARVVVGSAGEASRDRFAVTEVRWIAGAPPPRPVAARVKVRHRHEGEEGTVTPDGGGGQVRLARPVRGVAPGQAAVFYDGDEVLGGGRIV | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 37156
Sequence Length: 349
Subcellular Location: Cytoplasm
EC: 2.8.1.13
|
O67274 | MRVAVGMSGGVDSSVTALLLKEQGHDVIRVTLRFHTVEACEVNETHNVCCSPKDVQDASRVAKRLGIPHLVFSWEEIFKSKVIDYFVEEYKRGRTPNPCALCNREVKTGFFARYLKQVADIDKLATGHYAKIEEDKKYGLVIKRPKDRKRDQTYFLSLVRREDLELLTFPLGAYTKEEVREIAKRYGLEVAQKRDSQEVCFLMGKSPGEYLEGILGKQRGLIKHVSGKVLGEHEGVYRYTIGQRRGLGISYGKPVYVIDIDAKTNTLIVGEEEYLYNDKLLVKEINFHVPLEKWENVSAQIRYRHKPVPVERIEKTEEGFLVKFKEDVRGITPGQVVAFYDGDVLLGGGIIEESVK | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 40574
Sequence Length: 356
Subcellular Location: Cytoplasm
EC: 2.8.1.13
|
Q2NIM9 | MTKVVVGLSGGVDSAVAAFLLKKQGYLVEAVFMRNWDSNLNFDIQGNPTLNDICPQELDYKDALKVSEQLGIKLHRVDFIEEYWQKVFMSFIKAFENNLTPNPDILCNNEIKFRAFIEYVTTKLAPRYIAMGHYANIIYETFSEQKLFPQLACAVDQNKDQTYFLSQLATKQLQNILFPLGNLTKQEVRQIALENNLINATKKDSTGICFIGERNFFQFLSNYLPAQKGDIKTLDGTFLAHHKGVMYYTIGQRKNLGLGDFSSQKPWFVVGKHLQTNTLYVEQGNTHPYLYSDKALISDIVWRGKKTNLHLQAKMRYRQPNQDVILTWIDQNTLEIYYPQTIKAVTPGQICAFYNNNICCGAGVIKEVYFQGTKRLYT | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 43380
Sequence Length: 378
Subcellular Location: Cytoplasm
EC: 2.8.1.13
|
Q4JUL5 | MRVVAAMSGGVDSAVAASRALEAGHEVIGVHLALSQSPEAVRAGSRGCCSLEDSADARRVADKLGIPFYVWDFSDRFKADVIDDFVDSYAIGETPNPCLRCNEKIKFEALLDRSIALGFDAVVTGHYARLHDGVMRRGVDANKDQSYVLGVLTDEQLAHCMFPVGDTIKPEIREEAKDHGFGVASKPDSHDICFIPDGQTQAFLGKKIGLRPGLMKDQDGSTVAEHDGVYGFTIGQRKGLGLPREGLDGKPRYVTDIDAATGTVTIGQRDDLRVGGITADRLKRLDPAVHGREFECEVQVRAHGGVVPATARLVDDPERTTPAGRVKKEDESPWRLELDLHEPLQGVARGQAAVVYQPDADGDILLGSGTIRATAPWSDAGAAGTAGERATPAEA | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 42232
Sequence Length: 395
Subcellular Location: Cytoplasm
EC: 2.8.1.13
|
A9KE87 | MPNFEQNQVIAVGLSGGVDSSVAALVLKEKGYEVIGLFMQNWETDSKDPFCTAEQDLSDAKAIADHIGIPLYVVNFSKAYWNHVFQHCLDEFAQGRTPNPDVWCNREIKFKSLLDHAKKLGATHLATGHYACIQNENNEYRLLKSNDSHKDQSYFLHLLNQYQLANSVFPIGGYQKSEVRAIAKKRGFINHAKKDSTGICFIGERKFKDFLNEFLLAQPGNIETPEGKIIGKHDGIMFYTVGQRKGLHIGGRPDAGEAPWYVVDKDVKRNVLIVVQGYEHPLLYSQELTCTNLHWIRDTEPSFPLTCKAKTRCRQADQTCVVTRLDNDHCHVQFEHPQRAITRGQSVVFYLGNECLGGGIIN | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 40870
Sequence Length: 362
Subcellular Location: Cytoplasm
EC: 2.8.1.13
|
B1X0U7 | MKKVVVGLSGGVDSSVAAASLHHQGYDVIGLTLWLMKGKGQCCSEGMVDAAFICEQLGVPHHIVDTRELFEANIINYLVSGYESGVTPLPCSQCNRAVKFGPMLAYAKEELNCDRIATGHYARIRYDEQTRRYQLLRAIDRNKDQSYFLYDLSQDILKGTIFPLGEQTKEETRRIAAEFDLKTASKPESQDLCLIEAHGSMASFLDQYIKPKEGEIVDLDGKVLGTHQGIHHYTIGQRKGLGIAAPEPLYVVKLDAVMNRVIVGNRAAGGRSDCTVGRLNWVSIAEPSSPITVEVQVRYRSKAVPVSIIPIENNRVTLQFNEPQFGITPGQAAVFYDGEIVLGGGIILQDNDSVK | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 39043
Sequence Length: 355
Subcellular Location: Cytoplasm
EC: 2.8.1.13
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Q1D6N0 | MRVVVAMSGGVDSSAAAALLKEQGHEVIGITLRVWSYEGKATCGSCCSPDDIDDARAVAQTLGIPFYVANAEEIFQDRVINPFVQSYLGGRTPIPCVACNRDVKFNFLLKRARALGARLATGHYARVEEVDGRFVLRRAVDAAKDQSYFLFTLGQDELRDILFPVGGMTKAEVRAVAERHGLVTSQKPESMEICFVPDGDYAGFVEKVAGPQPAGDIVDTEGNVLGTHQGIHRYTVGQRKGLNLGGGEIRYVHRLEPETQRVVVGPAEGTGRDNFGLLQPHWVDGPPPASQPVEVRIRHRHSGAQGRVHVSPHGLVSVKLDAPARAVTPGQAAVVYDQDRVLGGGWIV | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 37577
Sequence Length: 348
Subcellular Location: Cytoplasm
EC: 2.8.1.13
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B2A5K1 | MMMSNRVLVAMSGGVDSSVAALMLKEQGYEVIGAHMRIWYREEDEELYEQNVKGCCSLAAVHDAKRVADKIGIPFYVLNFKEPFYDWVVKNFIDEYLQGRTPNPCIACNRFIKWEEFLKRAMALECDYIATGHYSKIVYDNLKNRYLLYRGKDKTKDQSYMLSQLTQEQLARTLFPLGDYYKEDVRNIAEQNELGVADKPDSQEICFVPNNDYGEFLQSVVPEHINPGPILDAQGNKLGEHKGIAFYTIGQRRGLGISLGRPVYVIDIDADNNALIVGDKEELYSDGLIAEEINLIPYEQIENSIDIECKIRYNSRNVSSTLQPYGNDQLLVKFNQPVEAVTPGQGVTFYQDDLVIGGGTILKATTKK | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 41737
Sequence Length: 368
Subcellular Location: Cytoplasm
EC: 2.8.1.13
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Q9JTJ9 | MNTTANPSNIIVGLSGGVDSSVTAALLKQQGYQVRGVFMQNWEDDDNDEYCSIKQDSFDAIAVADIVGIDIDIVNFAAQYKDKVFAYFLQEYSAGRTPNPDVLCNAEIKFKCFLDYAVGQGADTIATGHYARKEVRNGVHYLLKGLDQNKDQSYFLYRLKPFQLERAIFPLGGLEKPEVRRLAAEFNLPTAAKKDSTGICFIGERPFREFLQKYLPTDNGKMVTPEGKTVGEHVGLMFYTLGQRKGLGIGGGGEPWFVAAKDLTKNELMVVQGHDHPLLYTRSLVMNDLSFTLPERPKEGHYTCKTRYRMADAPCELRYLDDETVELVFDEPQWAVTPGQSAVLYDGDICLGGGIIQSTDKPVIITR | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 40900
Sequence Length: 367
Subcellular Location: Cytoplasm
EC: 2.8.1.13
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Q2GDU3 | MKLMQELAEIIPGKAYNDVKVMVAMSGGVDSSTVAAYLHRVGYKVIGVTLQLHNNFTSTQTNRKTCCAGSDIFDAKRVAAQFGFLHYVVNMEETFRKEVIENFAESYLKGETPVPCVKCNQTVKFRDLMKIAKSLSVDALATGHYVRRLTTTNGVELHKGIDPSKDQSYFLFNTTREQLEFLRFPLGNLKKSETRDLARKLSVDISEKPESQDICFVNGKSYADVIKKFRPDAQRPGKILSTDGEVLGTHNGTIHYTIGQRHGLQLSAPIPLYVVKIDAQNNIIIVGTRDKLQQRSLYVKEVNWLDRKELTAGLECEVKLRSGADTVKGYLYPNGELLKVSLAEEPKCAIAPGQACVMYHGSKVLGGGWIV | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 41283
Sequence Length: 371
Subcellular Location: Cytoplasm
EC: 2.8.1.13
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Q8DRS4 | MTDNSKTRVVVGMSGGVDSSVTALLLKEQGYDVIGVFMKNWDDTDEFGVCTATEDYKDVAAVADQIGIPYYSVNFEKEYWDRVFEYFLAEYRAGRTPNPDVMCNKEIKFKAFLDYAMTLGADYVATGHYAQVSRDADGTVHMLRGADNNKDQTYFLSQLSQEQLQKVMFPLGHLQKPRVREIAEKAGLVTAKKKDSTGICFIGEKNFKEFLSSYLPAQKGRMMTIDGRDMGEHNGLMYYTIGQRGGMGIGGQKGGDNAPWFVVGKDLSQNILYVGQGFYHDALMSTSLTASQVHFTQNMPDKFTLNCTAKFRYRQPDSKVDVKVNGDKAEVIFDEPQRAITPGQAVVFYDGDECLGGGLIDNAYQEEKICQYI | Function: Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34.
Catalytic Activity: AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-cysteinyl-[protein]
Sequence Mass (Da): 41689
Sequence Length: 373
Subcellular Location: Cytoplasm
EC: 2.8.1.13
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Q5ZVA8 | MSSPFVPIITADIDWRDDLPYSLQFDDIYYSAEGGINQSLYVFVEGNNLINRWQQLPTNESNVFTIAETGFGTGMNFLLTWKLWEKFAPQNARLHYISCDKHPLKKNDLIKCLQKWPELSVQAEKLIAHYPVLTPGYHHLTFSNNQITLTLMLGDVLECYEQLLFCGDINLEHQLRESYVNAWYLDGFSPSKNQSMWSDNLFTVIAMLSKESTTVATYSASSIVKTALTNAGFVIEKRKGFGPKRHMICAHYEKAYSSSKKNRHTPWHINYPVTKDERTALIVGGGLAGCFIANSLAKRGWEVTILEEKEKVGCGGSANQQAVLFPKLSTYKSPFTQFMLYSFLYANDVYKELLKYYDLGELKGSLLLAHNEKEKANQQSLIHWLELYPELGQLVDEKQSSELSGISLPCGGLFIPSSGWINSPELCDILIDNKRISLITGNRVQSINYNQKNWVVNGIEASVLILANGQQVNYFHETNHLPVKAIRGQMTTIQSTQESTKLKIPLCAEGHVLPALNNSHKVGASYDIGTSEPELNALDDQLNLARLKRIAPDIMWSQNVLDHWAGIRAASPDYLPIVGPLPNALEFKEIYSELKSNSKRWIAEAAPCYPNLYVCAAFGSRGLTTIPLATEWLAGLINKEISILPRKLIQAISPARFLRKKIIQGP | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
Catalytic Activity: 5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 74904
Sequence Length: 666
Subcellular Location: Cytoplasm
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B1Y222 | MRRSNPITPARLGRSAEGLPFSEDFGAPYHPSAGALAQAEQVFLRGTDLPARWAGQARHVILETGFGLGHNFLATWAAWRRDPRRCERLVYLAIDKHPPAPADLADVHRDSPLADLAAQLIAAWPLATPDLHLLDFEGGRVQLMLALGDIHDVLPGLQAEAHSLYLDGFVPARNPAMWSADVFKRIARLAAPGAMAASGHADSAVRDGLVRQGFEVRATGADATVARYAPRFQPEPPRGWRWPHAAAREALVIGGGLAGCAVAQALALQGWRSTVIDRQAGPAQETSGNAGGLMHGIFNAPDSPHARWFRAAAMHTARNAAAGLAAGELAGTLAGFLRLDERLNTTQAEAQLSAVGLPRAWLAWLDVAGARAAAGLELPCGAWHYGAAGWLDPAGYSRWMLQSAGDSARWIGGTGVAALRGPRDGAADHHGGWQAIDRHGRVIASAPVLVLANALDAARLLPAHCPPPGLSAVRGQVTRIPAGTPGLRPPRLTVAGQGYALRLDNGDVLVGATTQDEPVGIDGAALRLADQQRNLQRAAGLGVLDATAAEFGTTLLPGRAGWRAVTADRLPLVGPPIDLAQLAQARGGRVRLDAHRHQPRCVDDRSGLYLCTGLGSRGITSAALAGRLLAAWVSGAPAPVDADLRNALDPARLSK | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
Catalytic Activity: 5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 68778
Sequence Length: 655
Subcellular Location: Cytoplasm
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Q8F0E4 | MLTWKNNLTPVSEQFDDIYFSPENGLEETKHVFIKGNDLYNRWRNWNIQNAFCILELGFGTGLNFLTTWKEYLEYKDRFRLHFISIEKFPLNREEISKALSIFSELVEIKKEFLSSYQDLIPGMNYFQFLGGKIHFSLFLGDVSSALCEISGKVDAIFLDGFAPSKNPEMWDKSVLENLKYVSKKGTTLSTFTVARMVRDSLSFSGFKLEKRPGFGRKREMLIGSYSDSFLESNPKEKPWCKRAYPELQIKTVAIVGAGIAGTTLAYSLSRRGIQVFLIDPSGIAKETSGIPMAISHPHLTKIPGPISLFTLRAFRYALSFLSSFADQNFFEKTGLFHSVTQEMDSERLQKGIENHKLSEEIVFWKPIASKFQNGDFLENEPGVFFRNGFWTRPESIAKKCAEQPGVEFIKGTASRIEQDGTSWKLLIQESGHEIVANSIIFCNSHSIGKLIASLFEGEEPFPIRKVRGQLISLKETEKSSRISNILCAEHYLTPSILGEHILGSTFDEFDLNPLPQKKDTDRLLEFVQNKYPSLNFDSSCVLIEKVGLRAQTPDRLPILGPVFDPREFRKIYKEIDLPKNRNKKFPNLKTIQGLYVFGGLGSRGILSSFLGSEIMASLILGEPVPVESSVLEHLHPARFLYRKVRK | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
Catalytic Activity: 5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 73587
Sequence Length: 647
Subcellular Location: Cytoplasm
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A0LA84 | MSKQQAPNTTGIGTADLQWHSDETPYSPRFDDIYYAPTHGAEESTHVFLEGINAPACWQQRPHYTLAETGFGTGLNFLLTLDLWLATAPAHGRLHYIAVEAYPMDQAALARAHAPFAWLAPHSAALVQAWPPAVAGFHQRSLAQGRVTLTLLFGPAASMLAQLSATVDGWYLDGFAPSRNPEMWSDTLFAQLSRLSRLGTRLASFTVAGTVKRGLRAQGFTLHKAPGFGQKRECLRGVLENPLPHKPNIPPWYAPPQRSEPVSSVAIIGAGIAGAACAYACRRAGLQVTLFERHAQPGAEASGNPSGLFSPRLTAGVSLDGRFHAAAYFHALDLYAQLAQHTPEIYHPGRGLLQMAESEADVQRLQQALFHSAWPPQHAQWWDAATASQQLGTPLPRGGLWHAQAGALNPSVLCAALLADVTAHYQTEIVRLAPQPEGWTLHTAQRHYGTFDAVVIAAGATAPLLYPEAEIPNTAVQGQLSILPAANPLNQHALVFGGYLTPPYQDEQGQLCQVLGSTYRPWDDLSDCSWSECQPEAHQLVWQQLNETLPQLGQQWLGPARQGRAALRAAMKDHFPLFGPLINPSAYRTNYATLYQGKRVSLAKPAVYIDGLYLIGGLGSRGLLTAPLFGACMAALLSGGPLPLEADLWCAVHPARLLVRSLKKPPL | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
Catalytic Activity: 5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 72207
Sequence Length: 667
Subcellular Location: Cytoplasm
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Q0ALP0 | MTPDGLYCDPAELDWSQPSGPRARAYGDVYFSAEDGLEEARAVFLRGCGLPEAWTGRRHYVVGELGFGTGLNALALWQLWRQTRPTDGWLDFVTVEKHPLDRDAAARAFAAWPELSDLASRLLTQWPSRLRGPQRLVFPEDGFAITIFQDEVEAALSQMTRPVDAWFLDGFAPDRNAAMWSQAVFNRLGELSVPGTRVGTFTVAGFVRRGLAEAGFDVAKRPGFGRKRERLEAVWPGEAVDGSLANVDGPVAVLGAGIAGASLVHALRRRGIETVLIDAHGVASGASGAPAGLLTPRLEKADRPHVRATLAAFDFARRLYDGRPGFHAEPVRRLPKDEREAERFAILADWMPDHLDWTGEALVMPGAGRFEPARLVADLVADAQCHRARIGRVEPLGSGIGLYDDAGECRFEVAHLVIAAGAGARRFYPDLQPSAGQLAVFDGAPPDMPTAWGNYACAAPGGVLVGATHDRGDQVGPEDVAEAGFRASVAERMPGLALGPVQGRWQGVRAATPDRLPVAGRLSERVSILAGLGSRGFAHAPLLAEDLASELMGGVPALAQTGREAMAPGRFAERRSRRAGQGAAG | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
Catalytic Activity: 5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 62598
Sequence Length: 585
Subcellular Location: Cytoplasm
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A6W0S5 | MLTSYQLESPALSWGEDGAPHSNQFDDVYFDKESGLEETRHVFLKNNQLSGRWASLQKNAFVIAETGFGTGLNFLCAWQAFLTEAASDKQLHFISVEKYPMTKSMLTDALKMWPSISHLSQQLIDAYPEVCHGLHRIELEQGRIQLTLWFGEAEDGFAALDADVDAWFLDGFAPSKNPEMWSDNLFKHIHRLSHQGTTFSTFTAAGIVRRGLKNVGFDVRKVKGFGQKREMTVGELNSSTAPLSARMSQGQAWFNLRQDKTSEITKVLVVGAGLAGANTAYALAKQGIKVEVWEQGNCIAGGASGNPQGMLYPKLASQDTPVNRFYLSAYLHATRLYSSLDRHKQFWDACGLIQIPKNDKEAVRFQKLLDEKLYPEAILQASKDREGCLFLPLSGWVVLTQLCETLLSHENIHVCLNTKLESLSPIELDDKTFGWQARSKYQQAPLNDRQACFSHVVLCTANDTKALGVTPKTPDYPIRGQVSFMDIEKAKAACQTIGESADKIDFDKILCEFGYVSPSINGLLHFGSTYDLKDLDDRVREEGHKRNLAILESLLLLPKETFNSEDCGGRVSFRCAVPDYTPIVGPVQSEDVYQQAYSTLTKNAKWQSNEIAEPIKQLYINIGHGSRGLISTPLSGSYIASLITGTPSPLEQKVSHKLHPSRFIIRDLKRSQIL | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
Catalytic Activity: 5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 75186
Sequence Length: 674
Subcellular Location: Cytoplasm
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A1TZU2 | MITDLRPPAMEPAELIWQDGVPESARFGDVYFSRDDGLAETRYVFIERNGLPGRFAELDRNSHFVIAETGFGTGLNFLATWAEWLAQRPDDQDHAILHFISVERYPLALADLEKALESWPGLQPLARELIDNYPPLIKGTHRLVLGGGAIRLTLCFGDVLDAWNELEFVADAWFLDGFAPSLNPDMWLEKAIHQIRAHSQPGTTLATFTSVGRVRRALADEGFEMAKVPGFGRKREMLTGRLPTSEDVSAPTVGTDPIVIIGAGIAGAALARNLAERGVPVVLADQASGPGAGASGNDQGALYVKLGVEYNDQTELAATALSFSQRFYQRWQGEFWHPSGLLQLAATDQEQDRQRRFLERNTYPENMLAAVTAAEASRIAGMPVQCEGLWFPSSGWIQPARACQTLIDHPHIRTVFDFNVDTLRYVDNHWVIKASDGRSLRATKVVVAAGHESGSLAPVPDGQSLRLKPIRGQVTRLPADDCQLPDVVVCGTKYLNPAYDGSAITGATFDLRDDNPEPTPEGHQENLDQLRELLPSVNISKHIQAEHLEGRVAFRCATHDYQPVAGPCPDNNEISRTGVYLLTGLGSKGLVWAPLLAEYLADRICQQPACLNTRLARRVETGRLYRNQLTV | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
Catalytic Activity: 5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 69469
Sequence Length: 631
Subcellular Location: Cytoplasm
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Q1H1H9 | MSIPPFSQASLEWHEGQPYSAHFGDVYFSRESGLEETRHVFLRHNQLAERWQTMQQDAFTIVETGFGTGLNFLCAWQMWEHTAPSHVRLHFVSIEKFPLSHADLARALALWPELRQYSTALLAQYHQIVPGWQRLVFCQGRVQLTLLVGDVLALLPQLSSHADAWFLDGFAPSRNPEMWQEALFDNMAAFSHKHTTFATFTSAGIVKRGLQAAGFEVHKVAGHGRKRDMLCGRFTLNERPAMRAGRAVVIGGGIAGTASSHMLAERGWQVNLVEQEPALAQHASGNPVGVLYPKLARKDVPLGRLSLAGYLHSLRLLQQLGLDATAHARCGMLQLAFDQRELERCQTIAAQGFPPELLHWVDQEQAGNIAGIALQYGALYFPEAGWVRPRAYCEALAGHANITRTLATRVTGLSQHGNAWQVWTGEQLLDEADIVVIANAAQAASFVQSRHLPLEQVRGQISRLHHVDGAPVLHALLCTDGYISPLIDGAYCLGATFVPGDTTTSVRDEEHAQNLDMLKHMAPSLYDTLMPQAPTGRAAVRCTSVDYLPLVGPVLDAALLEARPPRYTADPASSLPWLPGLYVNTGHGSKGLTTAPIAAEMLACAIHHEPAPVDSELLAVLDPNRFVLRKLGLKRLVRGLACHPLRR | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
Catalytic Activity: 5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 71144
Sequence Length: 647
Subcellular Location: Cytoplasm
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A2SH83 | MKTAPITPGRLAFSPDGVPLAPEFGDVYHPAAGALQQAHHVFLGGNRLPARWGGRGRFVILETGFGLGNNFLATWDAWQRDPQRCERLVFVSIEKHPLTREDLARAHAASPLPELARALVSAWPLSTPNLHPIAFEGGRVQLLLGFGDVALLLPQLVVSVDAFFLDGFAPARNPEMWEPRRLQRLGRLAAPGATAATWSAARVVRDGLSAAGFTVETTAGTGGKRDITVARFTPRHIAVPPPGGWHAHDAASREALVIGAGLAGCAAAWALSQQGWQCQLLDRAAEPADVTSGNPAGLFHGSFHRDDGPHARTLRAAALATERLAGAWIAQGRVSGQLAGCLRLESRWSDDAARAAMAAQQIAPGYIDWMDRAVASTLSGLALPSGAWFYPGGGWLAPRDYARELLARSGSLFRGGIDVATIERHSGLWRVLDEQRQVIAEAPVLVLANGLGANGLLASGRGEVPWPLTAVRGQISSLATDGHPATLPCPRLPVAGGGYVLPQTGGRLLFGATSQPDDIDPALRDADHRFNLQQLAGLSGCDVEAWSSLPWQGRVGWRAVTSDRLPLIGAVPDLEALDRTSRADQPRFVPRQRDARGGLYVFTGLGSRGITWAALGGQLLASWISGAPCPLEADLRDALDPARYALPRWRSDS | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
Catalytic Activity: 5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 69568
Sequence Length: 653
Subcellular Location: Cytoplasm
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Q2Y7P9 | MLDWQNGQLYSTRFGDVYFSRDSGLEEKQYVFLQGNRLADRFESLQPDTAFSIGETGFGTGLSFLCTWRLFIQIAPLRTSLDFFSVEKYPLDEKELSAALALWPELGPYADELMLRWQRRVPGWNRWSFAGGRVRLTLAIEDVTRALPETHGIDAWFLDGFSPARNPEMWTLQIFHWIARASRAGATFATYTSAGVVRRGLEQAGFQVKKISGFGHKREMLQGDLPGPPPVRLAPTTAIVIGGGIAGCAAASALASRGLIVELLESHTLGAGASGNPIGILHARLSAGMNALHRFVLASYGHALALLDEKIPVDGVMRSECGELQLSFSAEEARRIGKLATLDWPAHVFRPVDAAEASALAGIELSYGGLWFPGSGWLAPPQLCVALLGSQAITLYTGRTVKSLTPTSHGWRVQAEDQRKQAWSLEAEIVVVCTGYQVKSLPALANLPLTPVRGQLTLIPATTASQNLRTIVCGSGYFSPAVAGRHMVGATHRFNDTSINLNVSEHAENLSRLREISPVLRRLSDEVSQDIRQLEQLDGRTSIRGSVPGAMPLVGELLPGLYTSLGHGTRGLITAGISAELVAATACGQLLPLPLSVVNALSPVRRASPAIPVSIKG | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
Catalytic Activity: 5-aminomethyl-2-thiouridine(34) in tRNA + S-adenosyl-L-methionine = 5-methylaminomethyl-2-thiouridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 66614
Sequence Length: 617
Subcellular Location: Cytoplasm
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Q8R6K8 | MEFDTIAAISTFPGEAGIGIVRISGDEALEIISKIFRPFRKKDIKSVKSHTIHYGHIVDPETGEVYDEVLVTVMRKPNTYTREDVVEINCHGGIVVSSKILELVLKHGARLAEPGEFTKRAFLNGRIDLSQAEAVIDIITSKTMLANRYAQKQLAGVLGQKMKDLKNKIMELLSHLLALIDFPEEDVEELEREEIKRRAKDILNDIEYLIASSESGRIIREGLKTAIIGKPNVGKSSLLNALLKQNRAIVTDIPGTTRDVIEEYMNIKGIPIKLIDTAGIRHTDELVEKIGVEKSKEVLAEADLILFVLDASRDLTKEDYEIFDILSGKNIIFVLNKVDLPKKIDEEELKKLVGNGIIVEVSTVERTGLDKLESEIYNLVFKGKVSATEEEIITNARHREVLINAKKHMESVIEAIEKGYSEDLITIDVNGALNEIGKITGETATEDVINQIFERFCVGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 51369
Sequence Length: 460
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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A4XN51 | MEFDTIAAISTPIGTGGIGIIRISGQNSIEVAGKIIKSKRFNSIYDIPVRYAALVEVYDNDEFIDQAILIKFKAPHSYTGEDVVEIQSHGGMVVLRRILEVVIKNGARHAMPGEFTKRAFLNGRLDLSQAEAIIDIINSKTELLQKNAAKQLKGVLSKKIDEIAEILLNLISSIEASIDFSEHEVDEISPQEIEKSIDTALEMIYRLLKTYETGRAIKSGIYTVIVGRPNVGKSSLLNRLLKEERSIVTDIPGTTRDVIEEVLDIEGIPIILVDTAGVRQTEDIVERIGVERTLKSVERADLVIFMIESDGITKEDIEIFSSIKNKKYIILVNKTDKGINISQDEIKKLFGKEGIFISIAKDENLELVEKAIKEAILEQNIEGFDEVLITNLRHKELLLKAKGFLTSAKQNLYSFPLDILSIDLKNALDSIYQITGKNVTEDMVDRIFSMFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 50811
Sequence Length: 455
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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A0RNG2 | MNIVALASAYGVGSISIVRLSGDGAYDLAINLCKKPLTPRYAHLRKLYCENMVFLDEAIVIYYKAPFSFTGEDVVEFQTHGGVVVANLIIDELLRLGARVANPGEFSKRAFLNGKMDLVKAESIQSLINARSEGAAKILARTMNGELSVFVNSLRDELIKILAYTETCIDYADDDLPSDILHSSKDLLLNSYKKLEHIINISNSKKGLIDGYKVAIIGRPNVGKSSILNSLLHYERAITSETAGTTRDTIEEQIKFGSHLVRIIDTAGIRDEFDSSIEAAGIEYSKRAAREADIIFCVFDSSQKASLEDRQILEFISNLNKKTIYVLNKSDLEFKFDISLNAVLVSAKLDSTPLSKELESYLNSQDTNDIMLSSNRQIEASRLASEAIKNALELLNESELELFAYELNIALKHIGSITKPMENSELLDKMFSSFCLGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 48565
Sequence Length: 438
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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A7I145 | MSETIVAVATAHGIGGISIVRLSGENALSLSDILINKNRKKNKTQNSVSSSQNRIQNFKKINLKPRYATLCELYDNDGNFMDESVVIYYKSPNSFTGEDIVEFQIHGGFTLENLIMDELITNGARIAMPGEFSKRAFLNDKMDLSKAEAIQSIILSRSKSAAKILARNLHGELKNFVIDLRKEIVKTMAFVETCIDYADDDLPNDILDKIQNLLSENITKIDEITQISASRRGLLEGFKVAIIGKPNVGKSSILNSLLKFSRAIVSDEAGTTRDRIEENLQIGSHLIRIIDTAGIRKSENSVENIGISYSIKAANEADIILAVFDASREFDKEDEKIFEILQNQKDKKIIKILNKIDLALKFKAGNSDNFLKISAKNDTKIITKVLNDYLNSQNFDGIMLSSNRQIMAFSNAGKALKRAQNLLNENSLELFAFELNIAIKEIASIYKPFERDEILESMFSNFCLGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 52097
Sequence Length: 466
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q9PNX9 | MSDTIAAIATAHGVGSISIVRLSGERALEFALKLSHKTKLTPRHATFTKLFNQNNEIIDEAIMIYFKAPYSFTGEDIVEFQTHGGFSVSEVLLEELVSLGARLALAGEFSKRACLNGKMTPLKALNIQDLILSKSALAAKIIARNMQGNLGELLEKIRTDLVKTLAFVETSIDYADDDLPSDLLEQISTMCEENSKILKEIYTLSQSKKGLIEGFKIAIVGKPNVGKSSLLNALLSYERAIVSDIAGTTRDTIEENFKLGTHLLRIIDTAGIRESKDVIEQIGVALSKKSLEDADIILAVFDASRVQDKEDEKIFDLLANTDKKIFWILNKSDLENVFKNTQNKNFIKLSAQKDITLLKEELQNYLNSFDSEGIMVSSLDLINACKISSEAIFRAKGLLEESSLEFFAFELNLAINELARFTKDFQRDEILDEMFGNFCLGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 49145
Sequence Length: 442
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q3AG56 | MMEDTIAAISTPLGEGGIGIVRVSGPGAIEAVKNVFIPRQSKDLSKVPSFTLHYGKIVDPADGKIVDEVLVSVMRAPKSYTGEDVVEINCHGGIVAVEKVLELILKQGIRLAEPGEFTKRAFLNGRIDLSQAEAVIDIIRAKTEASLKLAGRQLSGELREKINAVRQKIINILAFIEVSIDYPEYEFDEVTPETALKNIDEIINDVRRLLSSYERGRILREGITAVIAGKPNVGKSSLLNALLRKKRAIVTDIPGTTRDVIEDYLNLKGIPVKIVDTAGIRETEDLVEKLGVEKTREYLNQADVTLFVVDVSIGIDEDDEKILSLINKDKSLLVINKIDLLQGKVNFEQYAVKTGIKNFVPFSARNFEGLEILENKLYEILIPEQEGEGESALISNLRHKNYLEKALNSLLSAKESIASGEPVDLVAIDLNEALRELGAITGDALGDEIINEIFSQFCVGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 50656
Sequence Length: 461
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q05FY9 | MNTIFSRITPLGNGTLCVIRISGKNVKFLIQKIVKKNIKEKIATFSKLFLDKECVDYAMIIFFKKPNTFTGEDIIEFHIHNNETIVKKIINYLLLNKARFAKAGEFLERRYLNGKISLIECELINNKILYDNENMFQLTKNSEKKIFLCIIKNLKFKINSLIICIEIANFNFSFFFFNDFLFIKYTFKKLLKLLKILIDKITVINYLKKNFTIMILGRRNVGKSTLFNKICAQYDSIVTNIPGTTKNIISKKIKILSKKIKMMDTAGLKIRTKNLIEKIGIIKNINKIYQGNLILYMIDKFNIKNIFFNIPIDFIDKIKLNELIILVNKSDILGKEEGVFKIKNILIILISSKNGTFIKNLKCFINKIVDNKDFSKNNYSDVKILFNKFSFFYKEFSCNYDLVLSKLIDFQKNIFKLTGNFTNKKIINSCFRNFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 51218
Sequence Length: 438
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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B0T6E0 | MNDTIYAPATGAGAAAVAVVRISGARSADIVRGLAGDLPKPRRAVLRQLTRDGVALDDALVLWFQGPASYTGEDAAEFHVHGGRAVVEAVLEALAAEGLRLAEPGEFTRRAFENGKLDLTQAEGVADLIDAETEAQRRQALGQLGGALSQRYEAWRGLLVQALAMLEAAVDFPDEELPEDVAARARPGLEALEAEIGAALVDASRGRRVRDGYRIALVGAPNAGKSTLLNALVERDAAIVTSTPGTTRDIIEVPLTLGGYKTLLADTAGLRKTEDTIEAEGVRRARAWAAGADLRLWVIDAAMFHVKQDDELAVIQRGDWAVINKIDLVDAGRLAELRATFSEQGLKVVELAARKPGGAEPARAALSTHVIDALSGAEFPAATRIRHAESLTEARTYLQRALSDVGLEVELVAEDVRLAARALSRITGRIDPEDVLDRVFSSFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 47622
Sequence Length: 447
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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P0CAX2 | MTDTIFALATAAGRSAVAVVRVSGPRSSEIAAALCGRLPSPRLASVRTLKHNGVALDAALVLRFEKPASYTGEDSVEFHVHGGRAVVEALLAALSELGARLAEAGEFTRRAFENGKLDLAQAEGVADLIDAETEAQRRQALGQVGGALSQRYDRWRDLLVQALAMLEAAVDFPDEDLPEEVAERARPGLRQLSAELNAALADVSRGRRVRDGFRIALIGAPNAGKSTLLNGLAERDAAIVTDVAGTTRDVIEVPLVLGGYKVLVADTAGIRETADVIEAEGVRRAKAWAEAADLRLWVVDGFHVKQADARPEAIRVGDWLILNKTDIADADASAHVAERWAGEGLTVLHIAGTSAEGPEALRAALASHVADALSGAEFPAATRLRHAERLSEARSYLERALSDVGLEVELAAEDVRLAARALERISGRIDPEDVLGRVFSTFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 47394
Sequence Length: 446
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q4AAC5 | MLSDTICAIASGQINQAISIIRISGPNAFKIMEKIFLGKVGRSMEITFGWIHDDNQKIDQVLVLWFAGNKNFVGEDTVEINAHGGVLNTNLILELILKTKLARLANPGEFSLRAFLNGKIDLVKAQAINDLIHAEVKVQHQAALNQFLGKSSNFIKNLIEKIEEIIGIIEVNIDYPEYDDVEILTSDVLLPRINQLLADFDQLIKIANNSRLIYQGIKTCLVGAPNSGKSSLLNILINENKAIISEIPGTTRDVVEGNFVLDGLLFKLFDTAGIRKTTEKIEQIGIEKSYESIKKADLILHIIDASEKNRQNLDLKAKTRPDQIYLKIYNKSDLLENQEEFKDEILISAKYQKIENLLEKIKSIFAFLGKNKEFVANSFQISQIELGKLAILDAKTSLESGFGPEIAIVDLRIAWKELKTIFGRVDDENLLDSIFSKFCLGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 49516
Sequence Length: 442
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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A2SMI8 | MLLPRHHDPIVAIATAPGRGAVGIVRVSGRGLGALIEAVCGRALQPRHAHYGPFLDAQGEAIDQGLALHFPAPHSYTGEEVLELQAHGGPVLLQLLLARCLEAAAQPDARSGLPRLRGLRVAEPGEFTERAFLNDKLDLAQAEAVADLIDASTEAAARSAGRALAGAFSQQVDTLRDRLIELRMLVEATLDFPEEEIDFLEKADARGRLARIAEALDAVLARAKQGALLREGLRVVLAGQPNVGKSSLLNALAGAELAIVTPIAGTTRDKVAETIQIEGVPLHVVDTAGLRAEDDARDEVERIGMQRSWGAIGEADAVIFLHDLTRAGDPGYDAAERDIEQRLPAGVHVLDVHNKADAAAAGAAALAPQALRLSARTGEGLDTLRRRLLQLAGWQAGSEGVFIARTRHLQALQATAEHLVRARQLADRADAALDLLAEELRLAHDALGAITGRYTPDELLGDIFSRFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 50101
Sequence Length: 471
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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B1M0E0 | MNETDTLFAPASGFGRAAVAVIRISGPAAGGVLATLGGRLPTPRRLSLRSLRDPRDGTELDRALVAWFPGPDTYSGEDMAELHLHGGAAVRMRVLATLARLPGCRAAEPGAFTRRAVLNGRMDLAEAEAVADLIDAETEGQRRQALRQLDGALSRQVAAWRAEAIDCLAAAEAALDFADEGDVDDAGLDAALFDRAARLRDAVAATLRDGHRGERLREGFTVVLAGAPNSGKSTLLNALSRRDVAIVSDSPGTTRDAIEVRLDLGGLPVLLVDTAGLRETAEPIEAQGIVRTRARIDTADLVVALVPPGGAVPDLGPGCRPILIVRTKADLFAGSQPAGDSADVTVSAHTGAGMDDLLDAIQAAAEDGLGTGDALITRARHRAALEACVAHLDRVSGSAGGLPELAAEDLRLAVRALGEVAGHVGVEDVLDRLFSGFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 45736
Sequence Length: 441
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q7NAD9 | MINKIMKKYETIYALATAPYNSAIHVIRLSGPDAFEIINKICDKQITKEGYRIQNARIVDNDQIIDDVLLMKFVAPKSFTGEDSIEINCHGGLFVINKIMALLNKHGAHLARRGEFSKRSYINKKIDLNQATAIHDLIFAKNNLSHSASIKALSGEFSKDIKNIQQEIFRLIGLVEIAIDYPEYEDEKKELTEEFKNLTNIRQKLQRIVNKSLKLKQISEGIKIAIVGEPNAGKSSLLNALLNEQKAIVTNIPGTTRDTVEGQIVLNDELIINLIDTAGIRKSSDQIEQIGINKSFKTIDKSDLVIYLIDLNKYQNYDKTNIYKYLINKKKQFVLVGNKVDEVDPTLNTGEIQIKISAKNNDISDLIKYLEETSLAIFNDENKQDSIFQEEWQINLLQTALYNINLILNDPNQYHDLVIQHLNEANNSLLKVLSEYEDYNLIDEIFKNFCLGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 51666
Sequence Length: 453
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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P47254 | MKSEINIFALATAPFNSALHIIRFSGPDVYEILNKITNKKITRKGMQIQRTWIVDENNKRIDDVLLFKFVSPNSYTGEDLIEISCHGNMLIVNEICALLLKKGGVYAKPGEFTQRSFLNGKMSLQQASAVNKLILSPNLLVKDIVLNNLAGEMDQQLEQIAQQVNQLVMQMEVNIDYPEYLDEQVELSTLNNKVKLIIEKLKRIIENSKQLKKLHDPFKIAIIGETNVGKSSLLNALLNQDKAIVSNIKGSTRDVVEGDFNLNGYLIKILDTAGIRKHKSGLEKAGIKKSFESIKQANLVIYLLDATHPKKDLELISFFKKNKKDFFVFYNKKDLITNKFENSISAKQKDIKELVDLLTKYINEFYKKIDQKIYLIENWQQILIEKIKEQLEQFLKQQKKYLFFDVLVTHLREAQQDILKLLGKDVGFDLVNEIFNNFCLGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 50806
Sequence Length: 442
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q98RJ5 | MFDNIVAISSGAKVNQAISIIRLSGPDVFEIMKKIFTGKVGKDKSITYGYIKNDQEIIDEVLVMWFKGPNNFVGEDTVEINAHGGIVVSTLILETIVANGARLAEPGEFSKRAFLNGKLDLVKAEAINDLIHSKTVQQAKINIKKFDRKTSMFINDLINKLVFIIGTCEVNIDYPEYDDIEELTLEVLLPKLKDLEKEISKAVELSERSRIYFNEIPIAIVGRPNVGKSSLLNALLEEDKSIVTNIEGTTRDVVEARFVLNGINFLLKDTAGIRHSENVIEKIGIEKSFKQIQDSEIIIHLVLENQDEDDFERKIKELSEGKKYIRVINKKDLISKDKIKKDQIYISALKGEISELEKAILFEYQNIDLDDFRMIQNTRQLALIKSSLFSIQEAIKGLEQGYTPDVVIVDITKAWEDLVNIVGRADNEKLLDSMFSNFCLGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 49933
Sequence Length: 442
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q4A647 | MNYQSYSDTICAISSGNNINQPISIIRISGKNAQSIVSKIFSGKVGENKTITYGFIKENSEIVDEVLVSWFLGEPQGDITVYNNYVGEPLIEINAHGGMIVTNKILELLISNGARLAEPGEFTRRAFLNGKLDLSKADAIHNLIMSKTRLQARNEASKLKGSASKVIKDLLKELSLLIGSIEVGIDYPEYIDDYEEDLKANSKEDINLTRINKLIARLEKIVKSSETALNYFEGIKLAIVGKPNVGKSSLLNTMLKEDKAIVTNVAGTTRDIVEGIYYLDNFIFKIIDTAGIRKTRQEIEKIGIERSYKAILDADIVLHLFDNLNSEDEFDLDIKKIVQENNKNYIKVVNKSDLKSDIKWSDDFIKISAKNNDIKNLEDHLLKIYSGFDFNSEDIFATARQIKLFKESLEYAYAAREEIKNQLTYITAIVDLNNLFDTLQLIIGNSNREDLLDEMFKNFCLGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 52215
Sequence Length: 463
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q1CVG4 | MTSSSMTIAALATAPAAGAVGILRLSGPEALDVGRLLAPGVPAQPTPRHAYLASFVDAEGRSLDEGLFLYFRGPQSFTGEDVVELQAHGSPRLLRLLLTRALEDARVRHAAPGEFTRRAFLNGRLDLTRAEAVADLVAADSEAAVRAAAAGLSGALASRVQALEEPLRALHADMEGVLSFPDEAEGADEDVGERVTALRAQAETLLAEVGRGRLVRRGARVALFGPVNAGKSTLFNRLVGEARALVDDEPGTTRDALEARVEWDGLAVTLFDTAGLRETPGRVEALGIARTRALLTGVDLAVLVLPPGVTQAEVEAWTRDVGGTPVLVVDGKCDVAEVSSSPRQRVSGLTGEGVDALRDDMLGRLWGGGTPSAVALVSERHADALRRASEALGRAESASRVSTLEVVSGEVGLALEALGEVSGTVVSEALLDAIFQRFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 46134
Sequence Length: 442
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q67J33 | MGEETIAAIATGAGEGGIGIVRISGADALQVAERIFRPRRGRPLGCRRSHTVTYGWVVTPGGDRIDEALALVMRGPHSYTGEDVVELQCHGGQLAVRRVLEQALQAGARLAEPGEFTRRAFLNGRLDLSQAEAVVDLIRAKTDRAMAAAVAHLRGSLRQAIGRIRERLMEMMAHLEADIDFPELELEVQTREEVAAGCAWCLGEVERLLGGARTGRILREGLRAVLAGRPNVGKSSLLNRLVRENRAIVTPIPGTTRDVIAEWVELGGVPVQLFDTAGLRPTDDPVERIGVARTHEALAQAHLVLVVVDAAAGLGPEDREWISQLPQGAARVGVANKIDLNPAFELSALREALGGAPVVGVSAETGEGFDALEAEVARVAGAFDASEELLVNARQAEAIRRARNHLRDAQATLESGLGDELVAIDLRAAWMALGEVTGETAGEELLDQIFSRFCIGK | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 48885
Sequence Length: 457
Subcellular Location: Cytoplasm
EC: 3.6.-.-
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Q8Y652 | MLFLEGLMQYSFLQKALITSVTVGIVSGVIGSFIILRGMSLMGDAISHAVLPGVAISYMMGMNFFIGAATFGIAAALGIGFVNQKSRIKNDTAIGIVFSAFFALGIILISFAKSSTDLYHILFGNVLAVRSSDMWMTIIIAIIVISLVALFYKEFLVSSFDPVMAEAYGLNVKFLHYFLMLLLTLVTVSALQTVGIILVVAMLITPAATAYLLTNKLSKMIVLASTFGAVSAIIGLYFSYIFNLASGAAMVLVATIIFFIAFLFAPKQGLLFSKKREVIE | Function: This protein is probably a component of a manganese permease, a binding protein-dependent, ATP-driven transport system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30174
Sequence Length: 280
Subcellular Location: Cell membrane
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O34500 | MSFEAWIIATGVLVGVSCGLIGTFLVLRSMAMLADAISHTVLLGIVGAFLVTGSLDGIYMFIGAAATGLLTAFLVQLLHSKGVQSDAAIGVVFTSLFAIGVILLSVYGANVHLDIEHSLMGEIAFVPWNTVTVFGVDIGPKAFWMLASVLVLNVVLISVCYKEFKIASFDPQMALALGIPVLLIHYVQMGMLSLTTVASFDSVGAVLVVAMLIVPPAAAHLLTDRLLYMLILSALIGGLSAVMGYFFATWLNVSISGAMAAMTGVCYASAFLFSPANGVITKKLRTLNMQKERAG | Function: Probably part of the ABC transporter complex MntABCD involved in manganese import. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31058
Sequence Length: 295
Subcellular Location: Cell membrane
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Q9RPF3 | MKYSLPTTATAPFCPSAVSHSVAVPADASPLRKLALFVGPGLLVSVGYMDPGNWATAIEAGSRFGYALLFVVVLASFSGMLLQSLCSRLGIATGRDLAQLSRERYRPGVARGQWLLAELSIVATDLAEVLGAALAFHLLLGVSITTGVVLTAFDTLIVLALQGANFRRLEAIVLGLIATIGACFFVELVLIGPYWPDVAAGLRPSWDTLSSQEPLYLAIGILGATVMPHNLYLHSSVVQTRVSGDDAASKRSAIRFSRLDTIGSLSLALLVNAAILILAAAAFHGSGHTEVVEIQDAYHLLDPLVGGALASFLFGFALLAAGQSSTFTGTIAGQVVMEGFLRAKIPCWQRRLITRGLALVPALIGVLWLGEAAVGKLLVLSQVVLSLQLPFALWPLIRFSSDRGLMGEFVNPRWVSALAWSLFGLISAANLTLLYFWFG | Function: H(+)-stimulated, divalent metal cation uptake system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46603
Sequence Length: 439
Subcellular Location: Cell inner membrane
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Q9RPF2 | MSAKDTPAPQAAEPGRAQPVEVPGGGHWWRRLLAFAGPGYLVAVGYMDPGNWATDVAGGAQLGYLLLSVILLSSLMAMLLQALSARLGIASGLDLAQACRERYSPSTCRLLWLACETAIIACDLAEVIGTAIALKLLFGLPLAWGALLCVGDALLVLVLIGRGQRPLEAFVVALLTLIFACFAVQLLLSRPELGEVLQGFLPSPRVLSDPAALYLAIGIVGATVMPHNLYLHSSLVQSRAYPRSLAGKRKALRWAVADSSLALTLALLVNAAILIVAASVFHRNGHTEVVDIEQAHALLSPLLGLELASLLFAVALLASGLNSTVTTTLAGQIVMEGFLRLRLAPWARRLLTRGVAVLPVLLVTLLYGEDGTARLLIFSQVILSMQLPLAVIPLLQFVSDRRLMGPLAIGAGTRWLAWAVALAIVGLNLQLLADFAFG | Function: H(+)-stimulated, divalent metal cation uptake system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46380
Sequence Length: 438
Subcellular Location: Cell inner membrane
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A0KG66 | MQPALTTAIPARKFKLTLLGPAFIAAIGYIDPGNFATNIQAGSTFGYQLLWVVVWANLMAMLVQTLSAKLGIVTGKNLAEHIRDRLPKPAVWAYWVQAEIIAMATDLAEFIGAAVGFKLLLGVTLLEGAGITAVVTWGILMLQSRGQKPLEFVVGGLLLFVAAAYIVELVFSRPHLPSLLEGALFPGLPNSDAVYLAAGVLGATVMPHVIYLHSALTQHTQDQGSVPQRLHTTRVDVAIAMTIAGFVNLAMMAMAAAAFHSSGNQQVAELESAYQTLTPLLGQAAATLFGLSLVASGISSTVVGTLAGQVVMQGFVRFTIPLWLRRAITMAPAFVVIAMGLNTTEILVLSQVVLSFGIALALIPLLILTGDRALMGEYRNHPVTQAVGRLIVALVIGLNAYLLVAMI | Function: H(+)-stimulated, divalent metal cation uptake system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43101
Sequence Length: 407
Subcellular Location: Cell inner membrane
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Q8UEM1 | MFFMRMICNCINSISMKAQKMDKPVFGWRRNGDDLSLSDVHSSIRIKPDASTFRRAMAFFGPGYLVAVGYMDPGNWATSLAGGSKFGYTLLAVALVSNIMAIVLQSLCARLAIASGRDLAQACRDAYPKPVAMVLWLLAEIAIIATDIAEVIGTAIGLNLIFGIPLELGVLITALDVFLILYLQKLGFRWVEALVITLLGVIAVCFAIQLALADPDWGQVILGFAPTTEIVTNPDMLYLALGILGATVMPHNLYLHSGIVQTREIGPTIAEKREALKFATLDSTIALMFALLINASILILAAATFNKTGQTNVAELGEAHSLLAPLLGLAIAPTLFGVALLCCGINSTVTATLAGQIVMEGFLKMRLAPWLRRLITRAIAIVPAAGVTIFYGDSGTGQLLILTQVVLSLQLSFAVFPLVMFTSDKAKMGELRSPLWLSAIAWLIAVVIAALNVKLLMDFMG | Function: H(+)-stimulated, divalent metal cation uptake system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49460
Sequence Length: 461
Subcellular Location: Cell inner membrane
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P96593 | MMNKDITAQSPRSKAVQDALDGKIRGFRGLLPFLGPAFIAAIAYIDPGNFATNISAGSKYGYMLLWVILFSNIMALLIQSLSAKLGIATGKNLPEVAREEFPKPVSIGLWIQGELVIIATDLAEFIGAALGLYLLFGIPMLEASIIAAIGSFAILELQRRGYRSLEAGIAGMLFVVVIAFALQTFFAKPDAVSVMKGLFVPAFHGTDSVLLAAGILGATVMPHAIYLHSALTQRRVVGKTDAERKKIFRFEFIDILIAMLIAGAINASMLIVAAALFFKNGLFVEDLDVAFQQFGHLVSPMSAALFGIGLLVAGLSSSSVGTLSGDVIMQGFINYRIPLYVRRFITIIPPILIIASGVNPTTALVLSQVVLSFGIAFALIPLIMFTSNKRIMGSLINAKWITVVSWLIAVLIVALNVFLIVDTFR | Function: H(+)-stimulated, divalent metal cation uptake system. Involved in manganese uptake. Can probably also transport cadmium, cobalt, copper and zinc, but not iron. May be the predominant transporter of manganese during logarithmic phase growth.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45686
Sequence Length: 425
Subcellular Location: Cell membrane
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Q0B8F7 | MIPVTSKSSSGFALPDLSTDRAHRAVPAEGAARAALEGRRTGIAALLPFVGPAVIASIGYMDPGNFATNIQAGAAYGYRLLWVVLAANAIAMLFQAMSAKLGIVTGRNLAELCREHFPAPIVWGMWIASEIAAMATDLAEFLGGALAFALLCHLPLFAGMIATALATCAILALEKRGFRPLEAAIAALVGVIGACYLGELMIAPQDWHAAAFHLVVPQIPDRAALTIAVGIIGATIMPHTLYLHSGLTQDRIAPRDDTERRRLMRFSNREVVVALGLAGFVNLAMVMMAASAFHASAPGMADIGDAYHTLIPVLGPAAGVLFLVALLTSGVSSSVVGTMAGQVVMQGFMRRRLSVWMRRAVTIAPAFAVVACGCDVTRAMVASQVVLSFVLPMPMIALLILSARNDVMGRYAMRMPLRIVAGTATVVIVGLNAYLVWAAFN | Function: H(+)-stimulated, divalent metal cation uptake system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46420
Sequence Length: 441
Subcellular Location: Cell inner membrane
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Q8R7S2 | METREIASQRRKNLYLGIELKKFLKYLGPAFIVSVAYVDPGNFATNISGGSLFDYHLIWVILWSNVIAIFLQIQSAKLGIATGYNLPEMCSIIFPRKWNWFLWITAELAAMATDLAEFLGGTMGLYLLFHIPMTYAAFLTGVVTFAIVYMEKYGQKVVEGIIFGLVAVISLAYAFELFIARPDWSKVLYHTFIPSIPNKDAMLIAVGILGATVMPHVIYLHSQLVQYRNKDGSLQAKKEHLKMEKIDILVAMNTAFIINAAMLIVSAAVFYKNGIVIESIEEAHKTLEPLLGVFSSWAFGIALLASGFSSSAVGTMAGQTIMKGFVGLNIPLNVRRLVTMVPAITIIALGIDPLKSLIVSQVVLSFELPMAIIPLLLITSNKKFMKEFADTPLERIMGVLVASFVMILNGLLLYLTLKGEV | Function: H(+)-stimulated, divalent metal cation uptake system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46518
Sequence Length: 421
Subcellular Location: Cell membrane
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Q9RTP8 | MDSRSPSLPDDRPDPPEQHLDARAGATLRGTAGPRGVRRILPFLGPAVIASIAYMDPGNFATNIEGGARYGYSLLWVILAANLMAMVIQNLSANLGIASGRNLPELIRERWPRPLVWFYWIQAELVAMATDLAEFLGAALAIQLLTGLPMFWGAVVTGVVTFWLLNLQKRGTRPLELAVGAFVLMIGVAYLVQVVLARPDLAAVGAGFVPRLQGPGSAYLAVGIIGATVMPHVIYLHSALTQGRIQTDTTEEKRRLVRLNRVDVIAAMGLAGLINMSMLAVAAATFHGKNVENAGDLTTAYQTLTPLLGPAASVLFAVALLASGLSSSAVGTMAGDVIMQGFMGFHIPLWLRRLITMLPAFIVILLGMDPSSVLILSQVILCFGVPFALVPLLLFTARRDVMGALVTRRSFTVIGWVIAVIIIALNGYLLWELLGG | Function: H(+)-stimulated, divalent metal cation uptake system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46652
Sequence Length: 436
Subcellular Location: Cell membrane
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A7H1P4 | MDFYSLIFLSCALGMDAFAVSLCKSFSVKKLHLKHYLIVGIYFGGFQALMPTIGYFIGITFASFIASIDHWIAFILLSLIGLKMIKESLENENCNSNAKQFGFKTMLALAIATSIDALAVGVSFAFLNVNLLLAIFLIGIITFILCIIALKIGNKFGIYLKNKAELLGGLVLIILGVKILIEHLFFD | Function: Probably functions as a manganese efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20558
Sequence Length: 187
Subcellular Location: Cell inner membrane
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Q3A931 | MSLWEIFLLAVALGTDSFSLCVGLGMGKIKRKEIIALSLTVLVYHIVMPILGWFAGDLTGRFLGKVATYIGGAILIYLGYKMIRHGISQEEELPHVTYNLVGLLLIGLSVSMDALSVGFTLGTVKVNLWFVALITGIVAGVMTLSGLLLGRRVSKVLGERAQIVGGLILLLIAGKLIFRG | Function: Probably functions as a manganese efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19299
Sequence Length: 180
Subcellular Location: Cell membrane
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Q1R175 | MNPASLILLAFAMSTDAFAASIGRGAELRKVRLLSALRIGAVFGVVEAIMPLLGWALGHVAMRFVSGVDHWIAFVMLALLGGHMIWAGVKKEDCAAIKAAETQPENRSIWLIAFTALATSIDAMAVGITLALTDINIIAASVAIGLATALMVTLGTLLGRAIGTIVGKWAEILGGLILIGIGIAVLYEHLAGLASA | Function: Probably functions as a manganese efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20269
Sequence Length: 196
Subcellular Location: Cell inner membrane
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Q898D6 | MDFYSLFLIAIALSLDAFGVALCIGLNNNVDLKYKSSCAIYFGFFQFLFAIIGGYAGFLFNKYIATMPQIVGGVVICIVGIIMIKEGIENEDSCKILKPGMNIILGISVSIDAMVVGFTALNKIQSGLLILRDTLFIGIVTLFVSILAFITSKYLKKIDVIGKYADYIGGIILIFFGLKMIFF | Function: Probably functions as a manganese efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20052
Sequence Length: 183
Subcellular Location: Cell membrane
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Q47ZC7 | MIEVIILAIALSMDAFAVSIGLGATKQQSKVAPLGIIVALYFGLFQGIMPIIGYLGGKGVLSWAESYTPWIAFLLLFLIGVKMIFDSFSEGIEEDISKITHRVLLILAIATSIDAMAAGFSLTLLPVNPLIACLIIASVTFIFSWLGVLVGTKGGTWLENKAEFVGGITLIVMAIKIIITS | Function: Probably functions as a manganese efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19278
Sequence Length: 181
Subcellular Location: Cell inner membrane
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Q8NQG6 | MPFLQISLLSIGVAADAFACSVVRGTAIQVNLFKRALVLAGIFGVFQAAMPLIGWFIGRFFAGITFIAEIDHWIAFALLGIVGTKMIWDAFQPEDDETIVDDGRVQFRPAIILGLATSIDALAVGMGLAFVEVSILKVALSMGSITFALSLAGAWIGHHGGGKFGKWATILGGIILIGIGANIVYEHLSA | Function: Probably functions as a manganese efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20062
Sequence Length: 190
Subcellular Location: Cell membrane
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Q171H3 | MNYLKLTFDKLEVGEINDLVAHESCGAISLFVGTTRDNFDGKTVVLLEYEAYEAMALKTMNQICEELRARWPDIKHIGIHHRLGTVPVKEASVVIAVSSPHRKSSLEAVHFAIDELKKSVPVWKKEQYADGEGCSEWKENKECSWSKSHRDNHIL | Function: Catalytic subunit of the molybdopterin synthase complex, a complex that catalyzes the conversion of precursor Z into molybdopterin. Acts by mediating the incorporation of 2 sulfur atoms from thiocarboxylated MOCS2A into precursor Z to generate a dithiolene group.
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cyclic pyranopterin phosphate + H2O = 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + 4 H(+) + molybdopterin
Sequence Mass (Da): 17623
Sequence Length: 155
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.8.1.12
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Q8TD46 | MLCPWRTANLGLLLILTIFLVAEAEGAAQPNNSLMLQTSKENHALASSSLCMDEKQITQNYSKVLAEVNTSWPVKMATNAVLCCPPIALRNLIIITWEIILRGQPSCTKAYKKETNETKETNCTDERITWVSRPDQNSDLQIRTVAITHDGYYRCIMVTPDGNFHRGYHLQVLVTPEVTLFQNRNRTAVCKAVAGKPAAHISWIPEGDCATKQEYWSNGTVTVKSTCHWEVHNVSTVTCHVSHLTGNKSLYIELLPVPGAKKSAKLYIPYIILTIIILTIVGFIWLLKVNGCRKYKLNKTESTPVVEEDEMQPYASYTEKNNPLYDTTNKVKASEALQSEVDTDLHTL | Function: Inhibitory receptor for the CD200/OX2 cell surface glycoprotein. Limits inflammation by inhibiting the expression of pro-inflammatory molecules including TNF-alpha, interferons, and inducible nitric oxide synthase (iNOS) in response to selected stimuli. Also binds to HHV-8 K14 viral CD200 homolog with identical affinity and kinetics as the host CD200.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 39041
Sequence Length: 348
Subcellular Location: Cell membrane
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Q9ES58 | MLCFWRTSHVAVLLIWGVFAAESSCPDKNQTMQNNSSTMTEVNTTVFVQMGKKALLCCPSISLTKVILITWTITLRGQPSCIISYKADTRETHESNCSDRSITWASTPDLAPDLQISAVALQHEGRYSCDIAVPDGNFQNIYDLQVLVPPEVTHFPGENRTAVCEAIAGKPAAQISWTPDGDCVAKNESHSNGTVTVRSTCHWEQSHVSVVFCVVSHLTTGNQSLSIELGRGGDQLLGSYIQYIIPSIIILIIIGCICLLKISGCRKCKLPKSGATPDIEEDEMQPYASYTEKSNPLYDTVTTTEAHPASQGKVNGTDCLTLSAMGI | Function: Inhibitory receptor for the CD200/OX2 cell surface glycoprotein. Limits inflammation by inhibiting the expression of pro-inflammatory molecules including TNF-alpha, interferons, and inducible nitric oxide synthase (iNOS) in response to selected stimuli (By similarity).
PTM: Phosphorylated on tyrosine residues.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 35534
Sequence Length: 327
Subcellular Location: Cell membrane
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Q6Q8B3 | MSAPRLLISIIIMVSASSSSCMGGKQMTQNYSTIFAEGNISQPVLMDINAVLCCPPIALRNLIIITWEIILRGQPSCTKAYKKETNETKETNCTVERITWVSRPDQNSDLQIRPVDTTHDGYYRGIVVTPDGNFHRGYHLQVLVTPEVNLFQSRNITAVCKAVTGKPAAQISWIPEGSILATKQEYWGNGTVTVKSTCPWEGHKSTVTCHVSHLTGNKSLSVKLNSGLRTSGSPALSLLIILYVKLSLFVVILVTTGFVFFQRINHVRKVL | Function: May be a receptor for the CD200/OX2 cell surface glycoprotein.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 29920
Sequence Length: 271
Subcellular Location: Membrane
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Q8ZYE5 | MLFDKYGRSLQKLRYVVNDECNYNCVFCHFEGQSRRQGRYLTAEDYGFVTSVFKSLGVADFKITGGEPLLRGDIDLIVANIAKTGAYVTLTTNGYLLRKWVRKLQAAGLKRANVSIHTTDPEKYSKITGVPPSAFREVLRGLTEARDVGISLKLNAVVLRGINTDRDSVKNLVKLAASLGAALQFIELMPSGWGASVFNELYEPIETLVNIIFELGGRPAGVRKELHNRPLYNIAGVTVELIKNFSNPTFCSGCTTMRLTSDGKLKTCIYADSSVDLMPYIKSRDVEGLLYAVRTALARREPRFKLYSSS | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Function: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Catalytic Activity: AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-methionine
Sequence Mass (Da): 34472
Sequence Length: 310
Pathway: Cofactor biosynthesis; molybdopterin biosynthesis.
EC: 4.1.99.22
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