ids
stringlengths 6
10
| seqs
stringlengths 16
1.02k
| texts
stringlengths 117
4.4k
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A0A7R9QQE9 | MPKVHEEVLMRKLKKRLKHKEKQRVKNRELRKQTDDHLDDEADDVDEDTGDHRKRTIGDRVETNNKKFKSSEEPTVGSNEEIDGDDDENGEECPPLVTADSIPFTTSLTVTRFDELKDKVSDLTLNAIKDMEFSQMTEIQSKTIPHLLEGKDLVGAAKTGSGKTLAFLIPAIELMYKLRFMPRNGTGILIISPTRELSMQTFGVLKELMKYHKQTYGLIMGGTNRQSEALKLTRGVNIVVATPGRLLDHLQNTKQFLFKNLQSLIIDEADRILDIGFEEEMKAIVRLLPQRRQTMLFSATLTKKTDDLIATQLCE | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 315
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 35841
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A0A8B8DC57 | MAVIGRRLLLSLCGLTALVVMLDHIVNMSVVETSKLITSHREWRDYGDGSRYSVQLSAVTTSSSSAKPSTTIPTAVTQKPVKKTSYPLTLTSPYLINNPSMCKSDSKLNFVFIVHTSTDHFNRRNAIRQTWGNIRALRNLSFRVVFFLGLTKNKKIQTMLENESTVYGDIIQGQFMDSYHNLTHKGVLTYRWISEFCSNTELVVKVDDDMFVNIFNLVDHYLPIYRNASRKIMCHLRPQGTSPIMREKSKWQVHVDQFKNITHYPVPYCNGYFVLISSDIIRQLYRASYLTPFFWVDDVYLYGLLPQKIGNVTFTSITVNLTLHQETGMKCYTGNTTCKYLASYAEKQGYMESMWFAALRMFKNIAEKIVVKELL | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 375
Sequence Mass (Da): 43145
Location Topology: Single-pass type II membrane protein
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A0A0S7KEP6 | LEGVPFMSCSLATTVSSSEPHVVNQIVCFAVKSADSGIQNSADGSREMLATTPSTNSLADAEAAESPPMPATLPTASPCKDVVFFEPKEYSPGLQLYWASFSRSLPDMAEALAHGAEVNWVNTEEDKRTPLIMAVHGGSLVTCEFLLQNAVNVNQLDAQGRGPLHHATMLGHTGQVCLFLKRGANQNAADIDEKTPLSIAVEAANADIVTLLRLAKMNEEMREAEGPYNPSGQYNSNSPTEMQYRKCMQEFISLQLDDESD | Function: GTPase-activating protein for the ADP ribosylation factor family.
Subcellular Location: Endosome membrane
Sequence Length: 261
Domain: PH domain binds phospholipids including phosphatidic acid, phosphatidylinositol 3-phosphate, phosphatidylinositol 3,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3). May mediate protein binding to PIP2 or PIP3 containing membranes.
Sequence Mass (Da): 28180
Location Topology: Peripheral membrane protein
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A0A0S7L4Z2 | MNSSHVRLCRLLVVNGRAVTAAATAPRCDYSPYRTVSHFVRSMATSGNQFSATRPQKQKLRWQKIKESKDKRGDVHGPSNVYVQVVGAGSRDNTASLYVFSEYNRYLFNCGEGTQRLMQEHKLKAARLDNIFLTRLSWDNVGGLSGMILTLKDTGVPECVVSGPPQLKNYLHAIKSFSGPLEEMKLFVRPYTEEMHKDETMTVYQVPIFANSGIDRGRNSPQAGRSSSRSPKRDGPQRKTREEESGDRSAAGRDSSLVIAFVCKLHPKKGNFLVTKAKDLGLPVGTSEIGPLIRALKNGETVMHDGKEVQSVCLAVIRLHLQSAA | Catalytic Activity: Endonucleolytic cleavage of RNA, removing extra 3' nucleotides from tRNA precursor, generating 3' termini of tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'-phosphoryl group is left at the trailer molecule.
EC: 3.1.26.11
Subcellular Location: Mitochondrion matrix
Sequence Length: 325
Sequence Mass (Da): 35963
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A0A8D8E405 | ELGHNVTVVNLYKHGFVRGVQLVKLEGIVEELAAEEEDYVEFGQMSPFEVHVAFFDLELHVCQRAVKSAGFQRMLDYPKDFRFDLVIHDHLAGPCLLTLLSTFGYPPLIYASAYNRQSTLTTSLGTVVYPGFVPNQVYDVQHPMTFYHRIINHLLYFWEYFFKAFIYYPKLDSLIQQELNQTESVTSLEKRSLLAILNSNQILDPPEPISPNIVQVGGLHIKSQKSLPSNLLRILDHSNKVVLFSLGSNVRSDQLDSQILNKIIAAMTALPTTTFIWKLESNLPQKLPPNVITSPWFPQSDLLAHPKLSLFITHGGLLSVQEAVWHGVPMLGMPIYGDQFGNVNQLVHKGVAKRLSLVDATSDQLVEAILEITTNAR | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
EC: 2.4.1.17
Subcellular Location: Membrane
Sequence Length: 377
Sequence Mass (Da): 42492
Location Topology: Single-pass membrane protein
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A0A254UCB1 | MATNSGAPDLGKDGSGSIAITVEFTGGLEILFANERKHHVTLPSLLDDGSRPTISYLLGHLVKNYMKDQRQELFILEGNVRPGILVLINDADWELEGEENYELQQNDNIVFVSTLHGG | PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) via the hesA/moeB/thiF part of UBA4, then thiocarboxylated (-COSH) via the rhodanese domain of UBA4.
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Function: Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by the MOCS3 homolog UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates.
Subcellular Location: Cytoplasm
Sequence Length: 118
Sequence Mass (Da): 12980
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A0A7R9MG71 | MFEKAKVLSDDKVQLAMQTYEMVDKHIRRLDTELTKFDNDLKDTHITTQITDTTPHATDEVKKKGRRGDKTKNTGFNPKHVIKNESEGKGRKKQDIKMTDTIALANTSVASVLPALMANADIGLDMAVDPNEPTYCLCHQVSYGEMIGCDNPDCPIEWFHFGCVGLTIKPKGKWFCPKCVTERKKK | Function: Component of an histone acetyltransferase complex.
Subcellular Location: Nucleus
Sequence Length: 186
Domain: The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence Mass (Da): 20975
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A0A843BY60 | MKMKKATHRTQKGLIEVELNLENNKISALKITGDFFIYPEEALEIIEQELLNFEIEEEQLKNKIDEIYKQQQISTPGISIDDWVTVILKAVNL | Pathway: Protein modification; protein lipoylation via exogenous pathway; protein N(6)-(lipoyl)lysine from lipoate: step 1/2.
EC: 6.3.1.20
Catalytic Activity: (R)-lipoate + ATP + L-lysyl-[lipoyl-carrier protein] = (R)-N(6)-lipoyl-L-lysyl-[lipoyl-carrier protein] + AMP + diphosphate + H(+)
Sequence Length: 93
Sequence Mass (Da): 10817
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A0A1I7S624 | MSKPTNSNVCQGVDAVVYVMTMMTKGATERRKALRNVVFNKTNLPSNYTVLHRYVVGRYPVEREYQKRIIEEITEFDDIIMYNIEENYRKNYIKWHTMHAWHMRHCPQVKYFTKMDDDVIIYLKRLFQWVDIRFGEITKGNNKYIVCKVMSAADVLRDSNHKSFLSFEQFNEPTYPEYCDGPVVFTTNETIADLVQAYGNMTYLSIDDVYYTGVVRQKAEIEMVNFEGFDGRGRRCSALKLPYFTSRHGKETVEKMIRTLETMKKVKC | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 268
Sequence Mass (Da): 31665
Location Topology: Single-pass type II membrane protein
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A0A125YZL9 | MLVGKRGADATASLGVGEPQLKRRQVETGNCVVDCGAYRLLASCYGDKGMRKQMEDEHVIVPSLLPFQPALSPAYDFALFAVFDGHGGRQSAAFVKEAFPSELAAQLLLLQQEKENGSSSSVSEEKADATASAASAGGLTDREMKQVIYGACRKVDARIATEIPSCRDGCTAVVALFHGQQVYVACLGDSAAYLARRKDRTLHCIPLTEVHRHWVIEEKERIARMGGTIENGRVNGSLEVTRSFGDISLKRYGVSCVPTVKKFTLDPALDEFVLMGCDGFWNCWTASEALNLASEAWEKEIRSSKVHSRPVDPQNVSKQLVEHVLIDKKSQDNITVLLLKISRK | Function: Enzyme with a broad specificity.
Subcellular Location: Membrane
Sequence Length: 344
Sequence Mass (Da): 37632
Location Topology: Peripheral membrane protein
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A0A932SS56 | MIPVLKRALTAIVGVPLVICLFTVAPGWLGRHGVWLVVGVVMLVAGIGAWELTTLFLRAGRPVHRGLATVLAVLVTASFVDPTTPIRIMTVALAFTLAVPLLQPSRASFEPSAYTLLAIAYLGWPLGHALRLYALPGGPWLLVYVLLVTWAGETAAYVFGSLLGRTPLAPQISPRKTLEGAVAQIGLSAIVAIVLSPWVVPGWSLSTALGAGLVLGVVGQVGDLVESVIKRTMGAKDAGTLFPGHGGMLDRIDSLLFNVPAFFYYAAVVGVRA | Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 3/3.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
EC: 2.7.7.41
Subcellular Location: Membrane
Sequence Length: 273
Sequence Mass (Da): 28663
Location Topology: Multi-pass membrane protein
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A0A804I8I1 | MERTTRFFLFVYSCFVLAAAAAAQNGSRNSTAAFHVGVILDLGTLVGKMGSTSISMAVEDFYAMHGNYTSRIVFHAKDSKSDVIQAASAALDLIENSEVEVIIGPQKSSQAAFVAELGDRSQVPIISFSATSPTLTSSLIPYFVRTTLNDSSQVNSISSIIKAYGWREVVLIYEDTDYGRGVIPILVNALQGIDTRVPYHSVIPVSATDDQIMEELYKLMTMQTRVFIVHVSSFMGSRLFLNAKEAGMMTGGFVWIMSDGLANIIDSLDPSVIESMQGTLGVKLYVPKTRKLDDFTTRWKRRFQQDHPNDQQAELSIFALWAYDTVWAVAMAAEKIGIKVASFRKPRIVPNSTVLETLGASMNGPKLLKAILESRFKGLSGEFYLIDRQLRSSIFQIINVVGKGERGIGFWTPEYGISKQLNNTKGYSTLITDLNTVIWPGDYNAVPKGWEMPVSGKKLRIGVPVTQGFPHLMNVETDPVTNSTMGNGYCIDVFETVIKKLRYSIPYEYIPFKTIQGELGGSYNDLTYQVYLQKYDAVVGDVTIRHNRSLYVDFTLPFTESGVSMIVPVADGTKKNAWVFLKPLTLDLWLGSLAFVIYTGFVIWVMEHRINTDFRGPFSQQLGTIFFFSFSTLVFSHREKIENILSKFVVIVWVFVVLVLTSSYTASLTSMLTVQQLQPTVTDVHELLKHGDYVGYHKGSFVEGLLKQLNFDESKLRAYETTGEYFEALSKGSQNGGVSAIVHEIPYIKLFLAEHCTGFTMIGPIYKTAGFGFVFPKGSPLVPDVSRAILNLTDGDSILQIERKWFGDQNACLKQGSIISSDNLSFRNFWGLFMITGVVSTCALFIFLLMFLHKNWHELKGIDSNKPIWQRIGSWARYYNNKDMNSYTFRADGPYNTSPATNSKYGDVADPEATTCENSPNQQGFLMTDSDATHYPPVEESSSGEITRIAA | Function: Glutamate-gated receptor that probably acts as non-selective cation channel.
Subcellular Location: Membrane
Sequence Length: 951
Sequence Mass (Da): 106006
Location Topology: Multi-pass membrane protein
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A0A7R9ML47 | MHLMESMDTNSDSLILNIFHSNESPNKKAKLRQKVQKKAIHKKNTDNSAEDNADTDGRTSPDRSWMDRTSSRPDRRPPGGDRRADKRADNRFSYAKLNSRLFDSASQDVPPIHIVDTKSRVEPVFSSHNYSELSLHPYLVKCLSDRLSISETTSVQQNSIPALMSGSDALIKSMTGSGKTLAFAVPVVQDLQSLAPPIGRSDGVHALVIVPTRELALQCYECFSVLCQSFKRLVTGYLCGGEKKKSEKARIRKGINILVTTPGRLLDHMQSTGNLRLNRVKWFVVDEADRLLEAGFEESVKKVMDHLYSVCTVRPQTVLLSATLTPGVERLAGMSLNEPQ | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 340
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 37822
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A0A1I7SDG7 | MVKKEKKPNASKSANSASLSYPAIFLIVVGSIALGFYAKDLKELLVKSFSNSELYSPSNQPLSDAKENIIYRGPQRILTSKPEELNEIEQRLKLEIDEFNFDPVGPGAFNKPTILPENLKKKSEERYSENNFDVVVSDLVSINRALTDVRNHACQKRFTDQLSIANLPNTSLIIVFHNEAFSTLIRTLHSIIQRTPLQLIHEIILVDDQSDRDWLKEPLQRYLDEFPFKNIKLIRLPERSGLIKARLVASDAASGQVLLFLDAHIEVTKNWLQPLLTRVHEEPNVLVAPLIDVIDLDTFEYRTTIDGLVGGFNWRLTYNWGNLDEIEAKRRAGNHAEPFKTPVIAGGLFAVRREYFYQIGTYDEDMKVWGGENVEISMRVWRCGGQLEIHPCSRVGHVFRKVTPYTFPGGIEEMITHNELRTALVWLDEYLPFYTNTHPFSQKVSPGSVEKRLALREKLQCKSFRWYITNIYRTSPFPLDFHFLARIRSVQDDFLVDSRQQKQGKLFIAAFENFGNHQLWVFDKQGVLYNDHACIAIVGGNVEVIPFEHKLEGCARFEYEKQAQRFIEKSSGLCLGRNGALAILDQCDRPLTTEWKVEELATPSE | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 605
Sequence Mass (Da): 69363
Location Topology: Single-pass type II membrane protein
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A0A8D8GDM5 | IDVVISYDMPRHINTYIHRIGRTGRAGNRGTSITMLIDEERKKIPINPGRGRQAAAGTDRNPLQRRGGILRAVLGGAERPARSPGPREANDPEDPQRNVDRQHDQGEPAEQAQGSRRH | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 118
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 13101
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A0A7R9QXC5 | MRKLNQLFLILVISLILLLFVSIFYNLYYIQTYQTNAVLKTRDDGLSSLATIYVITPTYDRLVQKAELIRLSHTLILAKNIHWILVEDSLQKTPLVTRFLKNIQNYGHLSYTHLNALTPPQFKLKTTDPNWLKPRGVLQRNAGIEW | Pathway: Protein modification; protein glycosylation.
Catalytic Activity: 3-O-(beta-D-galactosyl-(1->3)-beta-D-galactosyl-(1->4)-beta-D-xylosyl)-L-seryl-[protein] + UDP-alpha-D-glucuronate = 3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP
EC: 2.4.1.135
Subcellular Location: Golgi apparatus membrane
Sequence Length: 146
Sequence Mass (Da): 17040
Location Topology: Single-pass type II membrane protein
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A0A1I7RZF3 | MTRPSSLRRLAMIWLLLFLSLPFIICFEEEDDDSNIKAFLNMNGTIRRVPHYVEVHGIEGVNYNLDEHGMPYIYCDALNTTCKGSEADCTKPKKCYQERRSHRLGCMAVFVYNTTEMSSSANKTIPQESAMLKGCWSQDESELRECEEHDECVASTRKTGAQGRAAKFCCCRTHNCNQNLTFYSDVLPKTRIHNDPKLMFFDNVHWLSRLLLSTDFFAVSAILLLIILFLFGLCFAVWIYRKQKRRKTTIKLEPYAPEDIHSEGTVEITTEGTALLGHKANDLRQSTLQNMTSTVLISSGHFSELYRAEVADASVVLKVYHNGDSDCWLNEQEVYSIKAVRKHENMATFLASFKHNAQYWFVIRYYPLGSIFDFLESNVANVQEATKILSTMLNGLSFLHEEFFFEGELKPTVVHRDFKSKNVLLKADLTAVIGDFSLSIKCENGRMSTDENQSQVGTRRYMSPEVLEGATEFTGFAFQQIDVYAAALVIWEVASRTVVPEHPDEPLPVYFLPYELEIGKTPTLGTMRDLVVMKKCRPQSRCTLYENPITSRILKTMQDMWDNEPDGRITSSCARDRMVHLHDVALGRCPIDGHMIEAGPTPCGSVHSLDGTTRTESSLGVPSGTGTTIPLEQLIRMADTPSTSTSSVTGYNPVYNP | Catalytic Activity: ATP + L-threonyl-[receptor-protein] = ADP + H(+) + O-phospho-L-threonyl-[receptor-protein]
EC: 2.7.11.30
Subcellular Location: Membrane
Sequence Length: 657
Sequence Mass (Da): 74255
Location Topology: Single-pass type I membrane protein
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A0A7R9LJZ4 | MNGYYRQDSPYRHESPYTRTSPYRVTPYNGHPRAHIRDVWNHNLIDEFKTINRLVADYPYVSLDTEFPGVLQTRPTGPNGGVYYDQKEFDYQTVRCNVDELQVIQVGLTLMDGYGRTPYDRVGVSTWQFNFRFNLNVDKHSADSIHLLMSSELNFQRLATEGIVSQDFAEQLMASGLVLNDKCEWISFHGAYDFGYLIKILTDAPLPPMLRAFHELLRIYFPVIFDVKLILNAFNGHTGGLQEEAQNLGLRRFGRPHQAGSDSLLTGQLFFRVLDAYPYQSQDIDRFVGNIFKFSDAGSDSLLTGQLFFRVLDAYPYQSQDIDRFVGNIFKFSDVFIYN | Catalytic Activity: Exonucleolytic cleavage of poly(A) to 5'-AMP.
EC: 3.1.13.4
Subcellular Location: Nucleus
Sequence Length: 339
Sequence Mass (Da): 39125
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A0A7R9R2R7 | MGINVCVEYLRPLVTQYGLRSVLLFPVMEGDKQVEHALDATRNPVLRLIPRLNTEFPELLIVCDVCLCTFAPEGHCCVFTAHQKMDNSASVEKIATIATRYAEVGAHVVAPSDMMDTRISHIRNALNVAGFDTVSILSYSAKFQSCFYGPFRDAAGIHRYSGHTLET | Pathway: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4.
Function: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen.
EC: 4.2.1.24
Catalytic Activity: 2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen
Sequence Length: 167
Sequence Mass (Da): 18508
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A0A804LA91 | MEKAALLLLFLAWFASEFRALGDDWIPASATFYGGGDASGTMGGACGYQNLYTDGYGIKNTALSTALFNNGAACGACFQIVCDSRKSTWCKKGTHITVTATNYCPPNYDLPSDNGGWCNPPRQHFDMSQPAWETIAVYRGGIVPVYYRRVKCQRSGGIRFTINGKNYFELVLIANVGGSGVVSGAWIKGSDTQWMAMSRNWGMNWQSNAYLTGQSLSFRVQTSDGKVKTAYDVAPATWKFGDTYASSIRF | Function: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found.
Subcellular Location: Secreted
Sequence Length: 250
Sequence Mass (Da): 27328
Location Topology: Peripheral membrane protein
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A0A7C4JJQ0 | MNVHILPTTLKRIFSLAHTYFRESIQLVTGPREFVGHKLRSEIYSYTHKVVAVGDVVCLTLLEYVGVPRLCIADGKTLRDIHGDIDKLLKNFAVILKCRNPPGSISEECLQVISKALGEPIPKLILVDGEEDLLTLAVILVGEDVDFVIYGVPREGVGMIDVKRFTIIAINLFSQFELSKIPQ | Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
Function: Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
EC: 2.7.1.237
Catalytic Activity: 3'-dephospho-CoA + GTP = CoA + GDP + H(+)
Sequence Length: 183
Sequence Mass (Da): 20399
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A0A1I7SMU5 | MSEISLKRARNDSRGNQAVETKKRQNVAGDIMKRLGYEEGGGLGQNGEGRLETVEDAIQVGRLEFGHQLNKKKVASWDQSEENKSIEERPEYLEASEDDREFFSTSFDINWIVKGKPLKTLLDEEDFCDNQVIRDLLKAKSIFDYMDIRDIQNARQRANPYETIMGAIFQNRAAMKMANLDRVFDWKLSREDNPDIRRQHNPLCGSDCDFNLQRNKDVFYFADICAGPGGFSEYMMWRKAFYNSKGIGFTLRGKDDFKLYNFKASSQAFFETYYGTNGDGDIYNPDNIKSLEDYVRRRTDGRMCDTVMSDGGFSVEGKEEIQEILSKRIYLCQFLVGLSLCRIRNSTKSGGNFICKMFDVFTTFSAGLLYIMYLAFEKVSIHKPNTSRPGNSERYIFCENLSEFGATVLKNYLIYINGELDKTSEGEDILEIIPLDVLKHDVKFVNYLKTSNEKWASRQILYLQKYETYALNKSVYDEDQPELREKCLQYWEIPNKSRPVIENQPPTMALRVMVPEHAEYSFDFATSLTTSAMSSFESLESRMLCLLPENNPPMLLVSNGKGESFLLDSEHSNIKQHELLLPPKTLLLVQKTSIYTITDKGALLPTSDWSSVMYVIDAGWLAGDAVYECNLSERRRCINKFCESINKCPESYRQNFEYRLEKVWSIKRKGKGKPVMNCQMNSYYLIPSPTLSLEDGTNQLSDLKIGFLETNNRCEKMAVLQLPVPRSLLAENDDKNRYLSVKAVRLYQTKDEQQNPYGFFDTYNKKCVWDWIWKPDSRGENGIYQILHEEVDNFLTVPTFNKLVQKIK | Function: S-adenosyl-L-methionine-dependent methyltransferase that mediates RNA cap1 2'-O-ribose methylation to the 5'-cap structure of RNAs. Methylates the ribose of the first nucleotide of a m(7)GpppG-capped mRNA to produce m(7)GpppNmp (cap1).
Catalytic Activity: a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.57
Subcellular Location: Nucleus
Sequence Length: 808
Sequence Mass (Da): 93381
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A0A6B1UAF7 | MGPDRARAKGRLLHLGQTVLILLVCTAVAALFDRVGIRQENITMVYLTGVLVIVVETGVFFWGIVASLVCVFAFNFLFTQPRLTFRIADPSYIVTLILFLLVSLIAASLTSQLQRHAQLARKKEDQTQRLYEISRSFLNLSGLKEVVCHGIASIYAGVQRRCVVYLIEEGEGLSQPYYLPGHYLDGVEVGDDTLARWCLKEGAPCGCGTENFAISQWRYAPFKSGSRLLGVVEVYCGNTPLGEGETLFIDTVISQLALAVEREQLYALQQRNQVEIEKEKLRNNLLRAVSHDLRTPLTGIGGSAEFLRHSYDRLDRETAMKLLGDISGDVAWLESMVENLLNMTRIQDGKLALQVKNEVVDDVVAEATARLARLPHTRPVTVSLPDELLLAPMDGKLMVQVLVNLLGNAVAHTPDSAAIRLAVRGEGERVVFEVIDDGGGVAPELLPHLFDSFVTSPGDSRRGIGLGLSICQSIVQAHGGGIEAENNDIGGATFRFWLPLEKSKEGKTCLQSAVF | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 515
Sequence Mass (Da): 56487
Location Topology: Multi-pass membrane protein
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A0A7C4JKJ4 | MISLQHKKKAIIVVGILVLGLATQMFLSLREAIVQSQQLPPGVDEKEFNDRLKLLSEASGFGAKVIGGLYGKTYYVTRLDDERAFGTLRYALENPEPLWIRFNVSGTITPTSVITVKSFKTIDGRGAEVIISGFGLKIASAKDVIIANIRFDTGYEDALAIEASSNVWIHRCDFTNWGDGAIDIKYSSTNITISWNRFWNHNKVMLIGHSPDNVADKAMKITIHHNYFFATVQRHPRVRFATVDVFNNYYYNWESYAIGSSQEGLVLAEANIFEAGNRKEAIVYTFEADPLPGCIKLVGNLLLNGTTIKENCPEKIFSRSSYYTDEVEPATEKLKLKIMWSAGTSISTYPRIMIRNPLVALDDKQPPYVPLPAQTNILRQVDPYNVVFKADIPPYKHPSESVIACEWNFGDGSRRVVNGSCLSPIEYRYKSPGLYLVSLTLYLANGLTLTTSGVIAVDTSLPSNVTLELSQRYPSLLVVPPKTITYPITRTTIRIVTQSETVLVNHTITVKEIEKEITTLAYTETYTKAITSEKIITFTTSTAIKEINWLATTSIAVTLLVLGFAMGWVVKRR | Pathway: Glycan metabolism; pectin degradation; 2-dehydro-3-deoxy-D-gluconate from pectin: step 2/5.
EC: 4.2.2.2
Catalytic Activity: Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends.
Sequence Length: 573
Sequence Mass (Da): 64001
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A0A8D7ZYY2 | MNVNIRETGSHVEFEPSSYYAAFSCELEASAYPMWSIISHLKDPSHAPLAKKIMLFCVNYLQDWLDAVNFYIHPKFDKEELYRASFHFPLHRYLAAFICQGVKTMGMSLSDILPSADLLPMLMMHPLRVQVSRGTFLARCGTTGTVRFLGKFWALFKITVIHYNYVEPKVPQRKCLVDRRQSPACVFRLLDRGLHVGTKVVRHDLGRDEATELGPTLVEEASSGQGHGFSGHHRLGVEEGDRRLGGVHAAITLAEPDELVADGVRDGLGGGEQWDVRPVQLEFGSLVVAMFGLVATDPDALVRVHQVAHGKVHLGHPNLQVEMAA | Pathway: Protein modification; protein ubiquitination.
Function: Ubiquitin ligase protein which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation.
EC: 2.3.2.27
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Length: 325
Sequence Mass (Da): 36179
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A0A1A9AYZ6 | MRDQVQQQVIDALQQLNLRYEQCWQNNMQTLPQSVSLCDISSPCVVSQDSERVYWQPQPRCQDINLQAVEQALDIQIREDIHAYFSAQFAADMAVNWQNHALILLQVWNEEDWSRLQENLIGHLVAQRQRKCTPTLFVALTDDDNQIVSVCNLTGAVVLERLGSSEHTVLADNLVAFLGGLQPRIAEL | Function: Interacts with the SecY protein in vivo. May bind preferentially to an uncomplexed state of SecY, thus functioning either as a chelating agent for excess SecY in the cell or as a regulatory factor that negatively controls the translocase function.
Subcellular Location: Cell inner membrane
Sequence Length: 188
Sequence Mass (Da): 21442
Location Topology: Peripheral membrane protein
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A0A804JNG0 | MAFPSLFSFVTLLIMFGVAHGGDGGWIDAHATFYGGGDASGTMGGACGYGNLYDQGYGTESAALSTALFNNGQSCGACFEIKCAGGQWCLKGSIVITATNFCPPNNALPNDDGGWCNPPRHHFDLSQPVFEKIAQYKAGIVPIQYKRVPCVKKGGIRFTINGHSYFNLVLITNVGGAGDVVAVSVKGSRTGWQPMSRNWGQNWQSSSNLDGQSLSFSVTTSDGLSVTSMDVAPPNWSFGQTYLGGQF | Function: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found.
Subcellular Location: Secreted
Sequence Length: 247
Sequence Mass (Da): 26125
Location Topology: Peripheral membrane protein
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A0A447QME1 | MTILKPLLARNRSWALQQRQRNPHYFRKHVAGQQPHALWIGCSDSRVPAEVLTGAHPGELFVHRNIANMVLQDDDSLMSVLQYALDYLHVSAIVLCGHYGCGGVQAAVNLPDLPLSQENSALARRLKHLRQSLASELPQYQQSEEEEAQRLNRVIDAHVVTQFAHLVDCPPVQQVWRQGRPLDVFGCVYDLHEGHLKELIHQDSAEVRDELKHSA | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 215
Sequence Mass (Da): 24334
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A0A804JP01 | MRSLSLPSCGGCDGEDDPSSLWSVASILQYQKAGDLLIALAYFSIPLELFYFVTCSDIFPFRWVILQFGAFIVLCSLSHLAAAFTYAPHSFLLFLTLTVLKFLTALVSLATAISLVALIPQLLRLFVREGLLRQKARELDRDLGLMRRQEEAAWRVPMLTAEIRRSLDRNTILDTTLVQLSAALSLRECAIWMPTSPSSMSLTHQLHSGPRPPASVSTDDADVIEIMSRNGVVILDPKSNLVRAAMASEAVGRVAATRVPLLKVSHFNDESMEASHAILILVLPDGEVREWTSHELETVEVVADQVAVALSHAAILEDSLLIREKLLEQNMVLNRARHDALLAREARESFKCFMTREIIGPIRSIGAIFSLLQVEKLSPQQLGMVTTGLTLSSLIGEAANISGFEEGELELILQQFHVRAILEEAVTMSRLLCACRGVHFKFEVSGQVHRAVVGDTKRILQALWCMLGNVLGFGDCRAIFLQVLVESSMQDDISISKYGVMQQGLEEGTVVLKFEVRRIGIKRKDNNIAHSKHGPDIGDPGISFAICEKLARLMHGSFSALPEAAYEESFQLLIRLPCPRSRDELLMTRHTDIESCPFKGMRVLLMDIDRSSIVITKLLLEKLGCHLTTVHSWRHGVHMMGSQFHLLLIDDKILENNRHEVASRIKQLSSKSWPLFVALTPNADRKTKERCLQDGMHGVLCKPVILKQMIDELQRITQQLQIPHPLLMTQQN | Cofactor: Binds 1 copper ion per dimer.
Function: May act early in the ethylene signal transduction pathway, possibly as an ethylene receptor, or as a regulator of the pathway.
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 732
Sequence Mass (Da): 81704
Location Topology: Multi-pass membrane protein
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A0A8B8CJB9 | MRSREIRIEPCYEGWGRFQFLTGTTYRRLHRTLASSRGFGTLDPFPLPIAAETRTTAMDGASMKKIRNCRISYKTLVLSLGVLLVVGLVYTKFFHYRNSGKRWRPVNLIPVEKCVGSKCILANDTSTGMKYALYFQPRKTKVNEFVYRFLNQPTGACDPASPPVLMIIVPSSPSHTEERNAIRSTWGSVSRGKRWPLQSIKGKAKLVFLLGITENITILQNLQDEVTEYNDIVQSDYLDTYQNLSLKILSGIRWTYLKCPDVKFILKADDDTFVHLPLLIATLEGYYRKVDRNGAIFGNINTDAKVRRRGMWKVSEIDYPFPHFPPYAYGNTYVISANIASRIFSASEYMPYIPIEDAFITGILAKVIGASHIFVSGFTFWLDYKPNYCDFVNDIRISATKVNFKYMYFLWEKLQSEDIDC | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 421
Sequence Mass (Da): 48295
Location Topology: Single-pass type II membrane protein
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A0A1D2KNF9 | MIEDERPNPDAILKQVTQQNRQKTGKLRVFFGYAAGVGKTYAMLRDAHEQLLQGKKIMAGYIEPHVRPETLALLEGIPTIPVKQMSYKKMTLSEFDLDEALRLKPDIVLVDELAHTNVIGSRNKKRYQDIDELLHAGIDVYTTVNVQHIESLNDVVESITHVQVVETVPDTFLDQAYLRLIDIEPEELLERLRAGKIYRPLQAKKAMQHFFALENLKLLREIAVRRAADHIGMTNPIEEVSVRVKLLTYLDEEHIQGTEKCLRWTARLAAAFRSEWTLLVIENEEDEHDDLMREQRFKVMKLAQSLGADIVTLSGHDTLDTLTHYAKMTGVTDIIIAKQRNHSHVHRLFKQELEDDLIQRLPQVDLHIIPYHDKREGQKRNRLNHINFIQRHFSAADFIKMLFYILVATLLSKIVLLMHSGDQNVIIVYLFFILIISRVTHGYFYGALASVISVLLFNWLFVDPLYSLTVYKPGYPVTMVIMLLVALFTSNMMIRVKSQAKEAVRKEHRMTILYELNQQLLASQSLAGMMAIANTKVMETMGRSVIFYSGLPEGKSDRKLSVYRGDPTAAALTTPEEEAVAHWVYLNQKFAGSGTDTLNGAAGYYFPVVSQGRSLAVIGLRVNPERPLHRENLNFLKLLTSQLSLALERHRLMIEQQQTVIENEKEKMRGNLLRAISHDLRTPLTGILGASSAIIENHEKFSAELTLNLVKDIKEDSEWLIRMVENLLSVTRIDEGTMKVKKTPEAIEEIVGAAVRRIRKRFKETDLTVRVPEELLLVPMDGTLIEQVLINLIENAIKHAESTAISVIVKQRKQRVIFEVSDNGKGLPTQRLETLFRPFNNEQHSEIPVDATRGMGIGLSICQTIVAAHGGTIEACNKTQGGAVFRFTLPIKEGD | Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
EC: 2.7.13.3
Subcellular Location: Membrane
Sequence Length: 895
Sequence Mass (Da): 101665
Location Topology: Multi-pass membrane protein
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A0A172MLI5 | MLSSKSMSIALLWSVMLFGTLSLIQAALQPEQNLEEITNKVYFDVEINGKPAGRITMGLFGKAVPKTVENFRALCTGEKGTGKSGKLLTYKGSSFHRIIPSFMIQGGDFTHGDGRGGESIYGEKFADENFKLTHTGPGILSMANSGRDTNGSQFFITTVETSCWARLCLSSNWFSPPILECRLDGKHVVFGKVIAGMDVVYKVEAEGTQDGKPKTKVVIANSGELPL | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
EC: 5.2.1.8
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Length: 227
Sequence Mass (Da): 24593
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A0A804JP03 | MKLVMSFFLTLSNTCLIQTLCEGCLENTFNLGRVSSRITFSGKHNIICRWFQILHLVITRVAPDVGCGVASFGAVLLSHNVSTMSIAPKYVHENQIQFALEHGVSALVAGFATHWLPYPSQAFDLIHRSRCRTNSTRDGMQFCNSWKQLLSSSYLSCLKIIVTGKVSKYWCPVLTPSTSIFLP | EC: 2.1.1.-
Subcellular Location: Membrane
Sequence Length: 183
Sequence Mass (Da): 20421
Location Topology: Single-pass type II membrane protein
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A0A8E4J9Z1 | GEFGNWLVPLMLGAPDMAFPRMNNMSFWLLPPSLTLLTMSMIVENGAGTGWTVYPPLSSNIGHNGSSVDLTIFSLHLAGVSSILGAINFITTVINMRSKGMSMDQMPLFVWSVAITALLLLLSLPVLAGAITMLLTDRNLNTSFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHIVSQESGKKETFGTLGMIYAMLSIGLLGFIVWAHHMFTV | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 220
Sequence Mass (Da): 23951
Location Topology: Multi-pass membrane protein
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A0A804KTJ8 | MEMVASLPAPSTVEEVFRDYLGRHRGLVRALTAEVDDLYALCHPERENLCLYGHPDGSWEVNVPPEEVPPEMPEPTLGINFARNGPKRWDWLSRVAMHSDSWLLSVAFFFAARFSGDERKRLFNLINDLPTIFEAFCSHQLTKKNTRVDRGSKPMRSSKRLKTVNNGSDEDANEISATSCGSCGTKHRSNFWIQCDVCERSFHGKCVKMTRAKAEKTKRYRCPSCSSK | Function: Histone-binding component that specifically recognizes H3 tails trimethylated on 'Lys-4' (H3K4me3), which mark transcription start sites of virtually all active genes.
Subcellular Location: Nucleus
Sequence Length: 228
Domain: The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence Mass (Da): 25933
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A0A655CGA7 | MGSALQGRVMLVDDVITAGTAIRESMEIIQAHGATLAGVLISLDRQERGRGEISAIQEVERDYGCKVISIITLKDLIAYLEEKPDMAEHLAAVRAYREEFGV | Pathway: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2.
Function: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP).
EC: 2.4.2.10
Catalytic Activity: diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate
Sequence Length: 102
Sequence Mass (Da): 11174
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A0A8B8CPH9 | MLIRLINTAIRTYALRGAMPYYAVRRGRNVGIYGDWDSCKAQVHGYAGARYKKFNTQKEAQAFVDGHDDTSSNNSSSNYTRSSSHTSSSCTSKFEQSSEQYSFSSKSRVDSSHFTHTKQKKHTSGHRSSPYSCNSRQYSSSSFSFTATQTGSSPKDTEEDHVYTDGCCLNNGQNHSVAGVGVYWGPNHPSNVSERLPGKPTNNRAEIHAARIAVKQAKEKGMKSVTVVTDSQFLINGMTSWIHNWKRNGWVLSDKTEVKNKEDWKAIDSEMQGIEVKFKHVYGHRGVEGNEAADRLANEGAIKTGPGNSSSWFK | Function: Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
EC: 3.1.26.4
Catalytic Activity: Endonucleolytic cleavage to 5'-phosphomonoester.
Sequence Length: 314
Sequence Mass (Da): 34903
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A0A254UD93 | MVSFLGQARLAVPILSAFACMLAASSAIPPPPRGALSPERLQWIREVIGNQTENDSVSDLAKRSTVLSTSQDGVDSAGFYYSVYNDNGADVGYTEYPTTGQFELGWSAEAEFLAGKGFKGGNPRSLTWDGYFTAEGDWTLAIYGWTTNPVTEWYIVETHGTGTPGNGDILGQVDSDGGVYDVYNLPYRNVPEIYGVTNFDQYWSVRRTHRTTGTVDVSAHFQGWKNLGLNPGSPVFQMVTLEGFSGQGYLDFTVSA | Pathway: Glycan degradation; xylan degradation.
Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans.
EC: 3.2.1.8
Subcellular Location: Secreted
Sequence Length: 256
Sequence Mass (Da): 27865
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A0A8B8ACY8 | MTGEDPGVMDYVHLRGVEIIHQIQHTFRHHVDLMQILTRVGDPRYAFLIYFPLAYCFHRPTGTRVLWIACLSEWLNGVLKWILHGERPYWWVNEMKQHEHIVNVPSLQQYSLTCETGPGSPSGHAMVTSAVLYSIGSSFIRHGLKKSRTFERVLVWVSFSVVLLAVNISRLFIATHFPHQVVAGSLTGILLAEAVKHEHTSHLSLRHYVAWSLIMVCGIVITYTGISYLGLDPLWSLSLAKKWCANPDWVHPDTTPFFAFVRDISSLIGFGVGVFLRDMPHHPMKLSIVQKLIYLGMALVLTLSIENIKTFPSSSLFYVIGFLKFTTMMIGIVFVIPKLLNKYNLKKQ | Pathway: Carbohydrate biosynthesis; gluconeogenesis.
EC: 3.1.3.9
Subcellular Location: Endoplasmic reticulum membrane
Sequence Length: 348
Sequence Mass (Da): 39613
Location Topology: Multi-pass membrane protein
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A0A6U9R208 | MSPSVLLSGMLWKRGGSTSKCLRRYEWKEKHVQLLDDGTIYYWSKDEDECLKKRLIATAGGVQKLPKRKEIKFGRYGQHCIMISGQNYVFYFSCASEEERQRWMEAMESTTMLYEGQEMGPTMRALHSLFRLADKDFSGTINSEEAKAIAHRLSSGIPDAELEKTFKKFLKRLKTKELDFHDFVDFWREMSLNEFVKNQFMLAGATNINDCISELQVVEYFRSCGNVDWDMEKMTSTLKEYRRSGSAMKKITADEGCDIFMFSEALYSLTNSVLKSEMYNNVYQDMDQPLTDYWINSSHNTYLTGDQLKSESTIDMYRIALEQGFRCVELDCWDGPDGDPIVYHGYTMTSKLKFEDIITCVKSYSFKKSKYPVILSLENHCSYDQQIRMAEILTNILGDTLVGRLPPERKTVPSPNELFGKIILKGKSTVISLEVEEDEEPEDDERFFESSGTPGESSRASQGVAKGMSKVPQELAQLIMMESVSRHKVKGMWADGVTKIDDMPTVGCCSFSEPTTIKLAGVHAELWREFNRECFSRNYPGGLRFNSSNFNPMLPWSLGCQLVALNIQTHDRPMQLNHGRFLENGECGYVLKPDHLRKPGGVPSMPVDLGPVIGPNGGGSGTLTLTIHCGHLIPKAKHSIGGDRVDPYVKVQVYGPSGVHEKSRTKTVNQNGYSPMWESKFKFNVEDTAVSMLLLSCWDDIPAQPDALVGVFAAPISTLLKGIRFVPIVADDGTQLTVPGGMLPGLICEFEWEAT | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+)
EC: 3.1.4.11
Subcellular Location: Cell membrane
Sequence Length: 755
Sequence Mass (Da): 85161
Location Topology: Peripheral membrane protein
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A0A356UFB4 | MELISGVVLAGGKSSRMGFNKAFLRLGQQHLIERIVATLKEVFTENILVADAPELYWNLGLPVVTDIFPGCGPLSGIHAGLVYTNTPYIFVVACDMPFVTAQFILFLLRQAGGGYEVIVPQINEQAEPLCAVYHKGCLPVVENRLKAGQYKVSGFFQAVKVKYIAQEEFSYIDEEDKIFINLNTRNDLKRAWHILDREDRSWRKISALRFKDLKKDLKF | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
EC: 2.7.7.77
Subcellular Location: Cytoplasm
Sequence Length: 219
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Sequence Mass (Da): 24815
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G8HUL8 | PAGGGDPILYQHLFWFFGHPEVYILILPGFGMISHIISQESGKKETFGSLGMIYAMLAIGLLGFVVWAHHMFTVGMDVDTRAYFTSATMIIAVPTGIKIFSWLATLHGAQMSYSPSLLWALGFVFLFTVGGLTGVILANSSIDIVLHDTYYVVAHFHYVLSMGAVFAIMAGFIQWFPLFTGLSMNNKLLKIQFIVMFFGVNLTFFPQHFLGLSGMPRRYSDYPDAYTSWNVVSSIGSTISFIGVLLFIYIIWESFISQRLVIFSNQMPTSIEWFQNYPPAEHSYSELPMLSNF | Pathway: Energy metabolism; oxidative phosphorylation.
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Catalytic Activity: 4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O
EC: 7.1.1.9
Subcellular Location: Membrane
Sequence Length: 293
Sequence Mass (Da): 32912
Location Topology: Multi-pass membrane protein
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A0A804I7W6 | MSGGETSTVSKHGNPAQFHDCKHPHGQRGTGDSGSPSLLSAVQTNQLLQQKDMLAANHGLADNVVAALETGSQADVQWSTWGLPPRYPSIARNVSEATYEGGNYNKQEYMNILGGTGSGSHDALVLHEHPSEWSIESMPNSEGSMIFRPKGSHPYPGQGFEDTRNNPSATSPPNNEELLKQNNYGEPSKYLFAGMLASASTAVPSAATTPLCAEGLDPFTFAAVTPTTEFTKKVIHETGGFGKKQHTRGPGPDRTCLIPHVITIRTNEDIYSKIISFCQKSGSYAVCILSANGTVSRVTLLKPAASLGTITYEGQFDIVKLSGSFMPLESCNQSRHSGELRVMLARADGHVFGGGLAGPMMAASSVLIVLGRFLPNGGNVAMLANNLFMV | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Subcellular Location: Nucleus
Sequence Length: 390
Domain: The PPC domain mediates interactions between AHL proteins.
Sequence Mass (Da): 41453
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A0A8D8GFB0 | MHGRLKVRTSAEEAARKQKERNAKAAAFRAGMERILAKKERAELDEELLVLTGKILSANPDVATLWNLRRQCLQTFAKADEETGGQSLFDKDLSFTEMCLQVNPKSYCAWHHRCWVLENCPTPNWDKEVELCTKYLKMDERNFHCWDYRRYVVAKANVPPSKELEFCTEKIQNNFSNYSSWHYRSKLLPILHPNQEDASRPISEEKLKEELELVLTAAFTDPG | Function: Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to cysteines occuring in specific C-terminal amino acid sequences.
EC: 2.5.1.60
Catalytic Activity: geranylgeranyl diphosphate + L-cysteinyl-[protein] = diphosphate + S-geranylgeranyl-L-cysteinyl-[protein]
Sequence Length: 223
Sequence Mass (Da): 25924
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A0A8B8DN19 | MWLSLVIALPVLQMVAAFPLNMINNRPIIGVLAQESFKGSPAATYIPSPYVKWLESAGARVIPVRLFRENDLKAHCYYKKLFDSMNGILFPGGGVDIINSQFAKTAMIFYKLARHAKDSNGDLFPLWGTCQGFELITALVSKQNLLTNVDAEDLPLPLNFTSEATDSTLFGNLPKDVYIPLKTENVTANYHHWALSPKNFSENNDLKSFFKVLSTNRDRNGKEFISSIEAYKYPVYALQWHPEKNNYVWMPGAKINHDAHAVRVSQYFADFLVAQARKSQHRFPSVKDENEALVNNYHPIFDRKSSLENYFFDFLNETALTSFSSDCKHL | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + (n-1) H2O = (6S)-5,6,7,8-tetrahydrofolate + (n-1) L-glutamate
EC: 3.4.19.9
Subcellular Location: Secreted
Sequence Length: 330
Sequence Mass (Da): 37533
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A0A804IQ13 | MLMDKYIFIIHKWFVIDVRLGHLLQVYVTFFFFFFFFFFLTGSCFHGDAGTMRKRAKEEQQWKSSTVSITSTKHMLYGFKKKKEEYGKLQKAEMSRWDCIELLNEIVDESDQDLDEPQIEHLLQSAEAVRRDYPDQDWLHLTALIHDLGTVLMNPTFGDAFPLGCALDESIVHHNYFKENPLLQTRLGVYTENCGLDKVTMSWGHDEYIYLVMKGNETKLPPASFFIMRFHSL | Cofactor: Binds 2 iron ions per subunit.
Pathway: Polyol metabolism; myo-inositol degradation into D-glucuronate; D-glucuronate from myo-inositol: step 1/1.
Catalytic Activity: myo-inositol + O2 = D-glucuronate + H(+) + H2O
EC: 1.13.99.1
Subcellular Location: Cytoplasm
Sequence Length: 233
Sequence Mass (Da): 27419
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A0A1I7RQD7 | MQVDVFGRCGGKPCDKACYKRNSLEYRFYLAFENTACEDYASEKFFNFNSLVPIVLKREYYPNSPPKSFIALDDFPSIHELSTYLARLMTDDALYAQHLLWSYDLQRKPRSRHQMMCDVCEYVLQRPAKKVYKEIGEYSNANKKLKKIANISATAVNKTRILLWTPRNRWYDPGFLEDVHTKCGSTCEFTMDRGKYNSSDGVMFFPFYMRHYNTTYPKRHSPKQTLIMYEREPPTRVPGSHLPNDYFNATATFMMHSDIPYPYGYLQEITRDITRSQYHADLLRKIKEDKKHGIFKVFSHCQTASRREDVIAELQNDEADPVTKRYHFASGKYQKMWLKAEIATAPEAPALSGSGSEPGARAGAGNFGVGSGSRAQSRSQASQWSEKYLDIDLFGKCVNRSCDNDCYKEKMKSYRFYLAFENSVCLDYITEKFYQFHELVPIVLKKDDYRNLPPKSFIALDDFASFKSFASFIKYLMTDDEAYAEYLMWKYDYEKRHTGTGDQFCTICQYVARNRSPKSYKNIQSFWNSTKTCDRDHTKRLLENNKDMSG | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 550
Sequence Mass (Da): 64189
Location Topology: Single-pass type II membrane protein
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A0A804IK48 | MGSPLHSLLLAFFFAFFASHRASRSLVLAQKSPASVDVGVVLDLGTETGKRSRTSISMAIDDFYALHGDHATRVVLHVRDSDKDAVGAAAAAVDLLKNVRVKAIIGPMTSTEAAFLIQLGDRTHVPVLSFSATNPALCPAHTPYFVRTTTNDSSQVAAIASVVQHFGWREAVLVYADTEYGTGIVPFLTDALQSVDARVPYRGVIPSEATDAQLDGVLRELKAAEARVFIVHMLPYLALRLFRRAKKLGMMSRGYVWIATDGVTSVLELLDRQDVLEAMQGLIGVRHYVNRSKEVTNFTARFRWRFRQDNPTVKPADPSVIQLWAYDTAWAVAMAVEKLHPARSAFKNSRSGNDSTDLSRLGVSQTGLALRNAIFDTRFRGLAGEFQLVDGQLQSSAFEIVNVDGEGETTVAFWTPENGISEHLNSTASAGLKSVVWPGDSTEVPKGWEIPTDGKRLRIAVPVKHGFDQFVRVETDAMTNRTSVTGFCIDVFQAVIDSLPYAVTFDYIPVANSSKSYDNFVYQVFLKNFDAVVGDTTIIANRSQFVDFTMPYTDSGVSMVVRVKDAKSKDLWIFLEPLPIDLWLGSLAFFVFTGLMVWVIERQENPEFAGKPLDQLGTIFYFAFSILVFTHKEKLTSNLTRFAVIMCTFVVLILTSSYTASLTSILTVQQLQPTVTDVNQLLSTGAYIGHQDGSYAVGLLKRMGFQDHKFKNYSTPDQYAEALSKGSANGGVDAVFDEIPYLKLFLSQHCADFTMVGPIYKTDGFGFVFPRGSQLVPDVSRAILNVTEGEKMAAIEKKWFGDRTNCTPQSNSLSSSSLAFWSFGGLFLITGAVSGLALLIGLAKFIYHEWDGLRTAASEKTSLWKKIVAVLKHYHDVDGPRPCLTLKMDDYGELDDEDLNKIARPGDAAGLHGSVGSQSPVSVSDRSDFSFASPEEGMSSTEPSSPYHYATVEMAEIREAA | Function: Glutamate-gated receptor that probably acts as non-selective cation channel.
Subcellular Location: Membrane
Sequence Length: 961
Sequence Mass (Da): 105535
Location Topology: Multi-pass membrane protein
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A0A7R9QIK4 | MTTHWTVFAINRTIGAIVTTSGHKKYVFIGAVDASDGRTERRDGTAVWEHQTIXLSGGTELLFGNTRQLVVSLDTSDHKTCDLKQLIDCLKTNHLKERPELFVSGDTVRPGILVLINEVDWDLLGQHHYVLQPNDRVLFISTLHGG | PTM: C-terminal thiocarboxylation occurs in 2 steps, it is first acyl-adenylated (-COAMP) via the hesA/moeB/thiF part of the MOCS3/UBA4 homolog, then thiocarboxylated (-COSH) via the rhodanese domain of the MOCS3/UBA4 homolog.
Pathway: tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis.
Function: Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by the MOCS3/UBA4 homolog. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates.
Subcellular Location: Cytoplasm
Sequence Length: 146
Sequence Mass (Da): 16302
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A0A349VQ55 | MAAEKVLFDTTKDGRAVNEYVITRPNGESFSIIDYGALIHTLKVLDKDGKIDDVILGFDTIAAYQASGSGHGSIIGRTANRIKGGAFTIDGVDYQLPKNEGENNLHGGPGNFQNSFWEGKIVSRDEAETFIGDLKIKNNWTIETEGVLMSFLLADGVCGVPGNMDMKVLYTWATDGTLIITYRAVSDKKTIFAPTNHSYFNIDGQAAGRIGEQLLWIDADQVTEKDMDNVPNGKFIDVAGTEFDFRTPCATEKVLVETSSNPQLNCSRGADSNYVLKTTQDQVSLVASVESARSGRKMEVLTNFPGVQLYCACNLNEVGKGGVHYHPYEAICLETQMFPDAIHHDNFASAVIDKDEVKGFLCGYRFSVK | Pathway: Carbohydrate metabolism; hexose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-glucose = beta-D-glucose
Sequence Length: 369
Sequence Mass (Da): 40401
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A0A1I7SMC9 | MIRFIFFVLLFHASYVQCAPDRSNESKEKGFSWKCMACRGGVEVLRFLFERNSTSDKIIRAAEYFCKEFANQNTQICKGLTSQFREQFLYVLEQMVLSPRQFCGLMLDECGIPNNPFDGNWTLNLPPKPDIFKDRPAKQADQENRPIFRVLQVSDLHFDFEYENGTEADCGKPVCCQGAPVPVPKKSAGYWGTLAACDIPLRTVESMFAHIAGTHMTDSDKKIDYIMLTGDYMPHNDWVYNKDSHLYVISNLTQLINTYFPDTPVFWGVGNHEGVPVNSFAPHTMPSRFWPDWIYKALTDAGERWIPPEQIASANFRGSFSVKLTDKLKLINLNTNFCETTNFFLYLNQTDPDSALQWLIEELKEAEEQGVVVHIMAHIPPGDGECLEGWARNYYRIVNRFEYTIRAQFFGHVHTDSFTVFYENMNNFHSRPTNVLYSAPSVTTFESVNPAYRIYEVDGNYEHSTYEILDYKTYFLNLSRPQPYPNPEWELLYSAKAEYNLPDLSASSWSTLGERIRGDDVLYKKFLKNYARRDDYPCDAKCRDELLCSLRRGHHNESALCPESTLIKRTFPFIDRSNIEPSILDQFTRDEFISGAKTALWNKVVGWIGK | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Converts sphingomyelin to ceramide.
EC: 3.1.4.12
Catalytic Activity: a sphingomyelin + H2O = an N-acylsphing-4-enine + H(+) + phosphocholine
Subcellular Location: Secreted
Sequence Length: 610
Sequence Mass (Da): 70488
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A0A450YXZ7 | MGIGKTKFDVLENLLRKPARKRRHIHYFVGAHRPGKNAIDQPPKDIFDVSTNKEISKIITERLRARNVSFFANQSIADHISDEERRQLLQEVTQKVRDLLRGLIIDIDNDPNARNTAHRMARTYLDEAMRGRYHKAPPVVEFPNARQLDEIYTVGPITVRSTCSHHLVPVLGSVWIGVVPSARGLIGLSKFNRITDWIMSRPHIQEEAVIMLADYLEKKLEPKGLAIMMRAKHLCMSWRGVKDSDTSMTSQVMRGDFLTDVDLERRFIDTIRTQDF | Pathway: Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1.
EC: 3.5.4.16
Catalytic Activity: GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)
Sequence Length: 276
Sequence Mass (Da): 31765
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S9U4A4 | MKGSKKRQVTKAEEAGGDTKKLKHSHHTENVETHHVFFEYFLKVSRSEFFKTYFEKKHLLCSHGDPHHFSSGNEKLHIPPIQWSTELMLKHAKNRPLHFGTDISVVRFDKEKGCRVTYKSEGVTTPAELKQCMDSGWSVRFLRPHEYMESDSAFISLMEREFGCYCGLNSYWTPAGTQGFAPHYDDVDVFLFQMEGEKEWRLYDPLDEVGVLTRHSSEDFQLDEYPEPKYFFTLKAGDVLYMPRGMVHQGRTTARTHSLHVTFSANQMNTWADVMQQVAAYSVGVLAANRLEWRKTVPLDLPRVLGIANSDTFRETAGVTPLTELQKSKRETFLLQLRERVAEMTLLMTEETNLDTSVDVYVKESIRKLQPPSAQYAHTVPASVELDAAARVRLVSATCCRLMMQYEGEAQVVHCGTNSHVCLQTEIGELRFEAVFAPAVATLLSRYPKFTQVSSLPFPDFDDPAEVAENQLLLVETLRDSNILQKE | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase.
EC: 1.14.11.-
Subcellular Location: Nucleus
Sequence Length: 487
Sequence Mass (Da): 55621
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A0A7R9M3I5 | MIIKSLLLSKVGTSLAKRNDMKRIFISLNIFALILLLLYVMISVAVFMNNVSVPTIAVNTVPDKYDSVLNAIDAEIQTLDLYLDGLTLRSQHLTKNSSQLIFPAEVQDMTRTAAIAKGWCTPRLGADLQVLVMVLNRVDDFQRRATLRHTWAQDFQSPNRSKLYFAVGLSRDETVQRRLVAEDLMHHDIIQWSYYESYYNCSIKSLAILRWTATNCPLVKYVLKADDDSLIRSDKLIDFVRQTPGADTIYGHMWTKPGVFRTGNKWSINTSDYTDDYYPDYIGGPWLIPGPKVMVLYSTAILKSLPALPFEDAYITGIVASKANVNRESMPGIMYLDYRSNCDIERLDLCWYDRYSIFWQGINDSSMTLFYNRITRFDAKSCTKFSFHYLYN | EC: 2.4.1.-
Subcellular Location: Golgi apparatus membrane
Sequence Length: 392
Sequence Mass (Da): 45060
Location Topology: Single-pass type II membrane protein
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A0A7Z7QQ86 | MGKILKVVKIFGGFFKGIISKSFNGVKGIIGTSLKFIWSIISTIFKRILTFTKGIFTILREFISSIWRSIKNIITNHAKGLFNNIKGVFTSLYRFTRSIFSSLKNWLSNIWRSIKNTVTRYASALWSNVKRIFTNLFNGSRSIFNRLKSWLISLWSSLKKRVVNIASSLWSNVKRIFTNLFNGTRSIFNRVKSIIVNIWNSIKRSVTGIASSLWKTVRRTFNNMANGLKSIIGRIKDHITGMVKAIKDGLNGLIKGLNWVGSKLSLPKIPKLSTGTQRINRHIRTTSDGRLKQGTMAVVGDKGPGNGKGLDGRRELIQYPNGRTALTPAKDTTTWLPKGSRVISGSMRQQYEEAEGAGMYPRFSVGTWLGKSTNWLADKTGAIGSAIKKSASWLTDKIGDVMDFIDSPGKLFNKVMSLMGVDFGSLTKGMGIVGQIARAAFAKIKKGAIDWIKGGFDAQAGDGSVFDGFRILQPYSAPPKAPNPNYPFNGGVHHGVDYDTPVGTPIRTPMGGRVRSWYDNYGGGKAITVQKGRTFLWFMHLSEQLRRTGEQIKAGQLIGKSGNTGSMTNYRHLHFQVNQGGEANRFSTDPIPWLRKNDKTGGGKGYPAGSGAAYASRVISQAQSILGGRYKSRYIHDQMMRVAKRESNYQPNVVNNWDINALRGDPSRGLFQIIGSTFRANAKSGYTNFNNPLHQAISAMRYIVARYGWGGFKRAGDYAYATGGKVYNGLYNLGEEGYPEWIIPTDPSRASDAAKLLALASKDISKNKRPKNFNSGSIGNDDTRNSKLESKLDTMIGLLIKLVGSNDTIADKDFSPVIDNFGLSDFINSTVDKRERNNSRKSRFKPGCALI | Function: Is able to cleave peptidoglycan.
Catalytic Activity: Hydrolysis of the -Gly-|-Gly- bond in the pentaglycine inter-peptide link joining staphylococcal cell wall peptidoglycans.
EC: 3.4.24.75
Subcellular Location: Secreted
Sequence Length: 851
Sequence Mass (Da): 94189
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A0A6U9PGN7 | MGASVQPSVDMDDRPGPTFVQADNGRNTAVGYTIPEQPRTFTSSNASLSPSNQSIPLPKSPQGFSPVVAFGDEVDEPCEQMMMLSAKSLPKSKTLVRDSGFPFGCVLSPLAARTPVPSTTDEPEFCASCGAALNLYANLDFDRNVWTCPICSKVNQIDAWPNSFLGEESPYLTCNALDFEGFGTSSDTNELMQLESYSDMTMFPTLFLIDAYLDEEDLEELKESLLSAFRALPGCCQVGIITFGSSVSVYDLNDASQVVADVLPGRESPTFSDLKPILMSSRVPILPVDQAREVAESIILSLRPFKNPQNVPARLRPRCLGSALEVAISLIKNYGKAHETGELGSDMLDQRVGSNQREFLGGRVLVMTSGPCTLGPGSVVLDDDVDHNQGSVQRSSIKYFTRVAEEARSRGVVIDVLCGGLGVAPGVSYMLPLVQETGGALLLHEGFGKLACSTIKTASCQPVFTNASFDVRLSPGIRVTQLIGPITEVGVSKSQKPARNALSGNAVQVLGLSNSTGIVVCFDPSGCKNVEYAYMQCMTRWTQPGGNNVTRILTKRMPCTDSKDQFLEGICGQAAALILAKKVAVSEDMFTDVEAVREGVEKCVGSIARVFVRKADTERGKLPRLPEELSTMAEGLYNLHRGALVGPAFGHTDERMALASQFIATNYELSQMMVVPVVYQSWGSKFEILPPVDMVMQTSCSFLLDCGAHVYIWIGQNSSKAAKEECRKLANKLCGGRWPTPVVKEAREGSSAQRYVTARLWPMRRESWGEQVHRIPNLADLDPEECYKMVEPYFRTEEPSFYEWLRELGFRPPDPVYAAPYYHYQALAP | Function: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
Subcellular Location: Cytoplasmic vesicle
Sequence Length: 829
Sequence Mass (Da): 90540
Location Topology: Peripheral membrane protein
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S9WCU5 | MVLTAVEGELVRQGRLPPAGFGGVCAIFQRIWRKEGWAGLLRGVLTDFVFALPAGLVDALASNSVFMLLQAVIPQQHAQSMGVAEVLLLSMVATGAAVYVASPYNGVRKTVTTNYVADIVAPTAEPKEQKEAEGDAEAPLVEEAYRYGTSTEAAARLAKKGGWRIFYRGATLDPFIIMTYRGLYIAASMLVPETVQVAHPYLVARGLALVADVVSQPLEVLSRRLVLTASDEVNAPYDGAIDCARQIAAKEGVTALWAGLRFRIVVSFVTMGLRAAIGALVFGSEGQS | Function: Catalyzes the exchange of ADP and ATP across the membrane.
Subcellular Location: Membrane
Sequence Length: 288
Sequence Mass (Da): 30716
Location Topology: Multi-pass membrane protein
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A0A922G2C1 | MSGVSLSAEAAQGRKDPPQSASSAERPTDVDNIVISPRSPCAMNGLVGQMTIFYCGKLNVFDGVPTDKARAIMHLAASPSHLLQDDILGRAAALWSFPCHLQTVTDRDRLIPPSTTTSLIMQTEKMTEYAQQFGGNGNSNRDPEIPRWPGTIVPHRLVVILLVALYIYIYMYVCMYMF | Function: Repressor of jasmonate responses.
Subcellular Location: Nucleus
Sequence Length: 178
Domain: The jas domain is required for interaction with COI1.
Sequence Mass (Da): 19621
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A0A350BCI3 | MVAGNRHRMMKVKFTPATLRKEHPKKWCYGIIAKINPLMNEDKQTNQINIVRDAEIHGRHRPKRVNRKYLINIAIVLLITILVLYFNLRDNLTAVMEAMVHVDYRFILLATGLVLLTFLLDGFILFILARLYTTRFTIGKGLGNALIGIFYNNVTPGHSGGQFAQAYTFKKQGLEISSAASILVMHFLLNQMALVTWGILAVSFKLKDFINIIQPITLLGINFPTISLAIIGFSLNFIVIVGIIFLAYSKWIHNFVINGLVGLLGKMKIIKHPEVTKSNLHLQIENFRIELRRLQSNIRVTIFLYILFMFRYFVIYSLPMVIAKSLPTITISGTLWDGIFMTSYLYVITNLAPLPGSAGVSELFFSHLFQTIFGSYAATLAPQLIWRTTTFYLTLIVSGFASAFYRSAPQEDNFRSDRRTFVELQKSTYAIRKLSSDTMWETSQLSRKDMIKEVTGDFLGIKARRKKAEELKKKQQEDARASAERKMKERLTLETDEFLIDPDDPVK | Function: Catalyzes the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), a major component of the bacterial membrane with a positive net charge. LPG synthesis contributes to bacterial virulence as it is involved in the resistance mechanism against cationic antimicrobial peptides (CAMP) produces by the host's immune system (defensins, cathelicidins) and by the competing microorganisms.
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + L-lysyl-tRNA(Lys) = 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys)
EC: 2.3.2.3
Subcellular Location: Cell membrane
Sequence Length: 507
Sequence Mass (Da): 57989
Location Topology: Multi-pass membrane protein
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A0A804ISA4 | MVSLIFFAMLSLAVAKAQWLPGHATFYGANQDPTSLGGACGYDNTIHAGFGINTAALSGALFRQGEACGACFEIACDAGADPQWCLGHATVTVTATNFCPPNNNGGWCDPPRRHFDMSLPAFSRIARVGSEGIVPVLYRRVACKRSGGVRFTLKGQGNFNLVMFSNVGGSGDVKAAWIRGSRASTWSAMQRNWGANWQTNADYRNQRLSFRLALGDGKTLEFSGVVPSSWSPGETFVSQTQFS | Function: Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found.
Subcellular Location: Secreted
Sequence Length: 243
Sequence Mass (Da): 26048
Location Topology: Peripheral membrane protein
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A0A7J3I9A8 | MVQTYIAQSIGFWEIAFLIILIVLILVVPSRLPQIMRDLGRAIREFRRALHETEETAEEVKKATEEVGKSLKSEKEKEE | Function: Part of the twin-arginine translocation (Tat) system that transports large folded proteins containing a characteristic twin-arginine motif in their signal peptide across membranes. TatA could form the protein-conducting channel of the Tat system.
Subcellular Location: Cell membrane
Sequence Length: 79
Sequence Mass (Da): 9156
Location Topology: Single-pass membrane protein
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A0A7R9M0G1 | MSTTMDSKANPLSNKINKILNQPMDRETLEALVSVSDVLQDNNLQSRRHLRTDIERQSLKITEEFVNCFDALKHSLNDLFSNVNQMNQNCKQMIERIETTRTQTSHLLKQTNQLSEELKGIEVKELVTNRFINEFQLKPEELMTINNTNDDIDDHFFEIIAKVRKIHEKSKLLLTNSQHTTGIEIMDSMALHEEAANERLYRWTLNILRGISSDVIEVHPQLFRAMACLEEREILFKYCLDEYVTVRRSAVVRNFIEALTRGRPNANSPPIESHSHDVIRYVGDMFAFLHQSVANEREMIDTLLKLCDKQKLSTSGLANTCIASITEGLCRPLKVRVEQSLISDNTSAAKSGPSVYYGIKNIIGFYVHTLTQTQLLTPDSPFIYTLKELQTLSDKIFYNSLNYSVARIGKSEATSDVEVPASDLKPTQSVTQIVAVLKEVLLCQNSSLTSDEEREREVQQILSTVIEPLIHSCIISASKLTALEMAVFLVNCLFAINETLSNHRFTDRFKDMITQQTDGHIDTLVNEQISHIISYLGLSPLQNAIQQKDDLMIPLSQLSGCDSLAIRSAMLKMDSFISRPTDLVLSQSSHLIDSNTKQLVWKRSLEAICLIYEEMYELVTNGVNQYVDPLSLMNYKPDQMKMLLLSAIIGKRLHRQYCRYRHYGTDTPFVRTLDGQAFIRDVREREEIGGYDTDEELDLLDTKYFTPQTLDLLAIKLTEDTNDCPLLPNPYIKTADHYL | Function: Required for normal Golgi function.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 739
Sequence Mass (Da): 84424
Location Topology: Peripheral membrane protein
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A0A804JLV2 | MKLAAISVVLFLALLNSATSNGDEKEPEFGYKQGTKTGPDNWGRIRNDWITCGKGKSQSPIDLRDKMVRRLPRLRRFRTSYVPADAAIKNRGHDIAVMWNGHEAGGITINGTEYKLKQLHWHSPSEHSINRRRFSLEMHMVHQSADNKTAVVGFLYKTGPPDPFIHKLERSIEKVKDKQDKEEELGAVDPSHASRRMGQRYYRYMGSLTTPPCSEGVIWTILRKVKTVSKKQLRLLRRAVDDDYENNSRPRQPINGRLIGLYRPPKHEN | Function: Reversible hydration of carbon dioxide.
EC: 4.2.1.1
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Length: 269
Sequence Mass (Da): 30882
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A0A3C1H059 | MLKERALEMKDISLTRRFAAYVQKDAAYALALRTMYFDMATIAPKKGAAYRSNLLSILSGEAFAHATSKSTIALLQKVADQSDDRFAQDQAKAILKDLEKIRFIPKKQYVEFNKLCNDAEVEWELAREEKDFSRFAPYLHRLIEGTKANVKTRRRTECDYDVLLGDYEPNMTQVEYDRFFAVVKEKLVPFLHRLLTEGVKPDTSFLYKVYPVDKQKQFMEILKEALCVDPKSSYLATSAHPFSSSLSKFDNRITVRYLADNVASAIFSLIHEVGHATYNHQVDQVYEGTVFFDNMSMGMHESQSRMMENMLGRNKSFWVNLYPKLVALFPENLSEVSLDQWVAAINAVEPGFIRTEADELTYPLHILLRYEVERGFFDGSVTVDNVEAVWNQKIHDFLGLNVKDSAEGVLQDIHWSSASFGYFPTYALGSAYSAQWMVAMRKDLNVEQLLEEGRMDLIKQWLMEKIHTYGGKRQADELLKEVTGESFNPMHYVDYLIDKYSALYQLK | Cofactor: Binds 1 zinc ion per subunit.
Function: Broad specificity carboxypetidase that releases amino acids sequentially from the C-terminus, including neutral, aromatic, polar and basic residues.
EC: 3.4.17.19
Catalytic Activity: Release of a C-terminal amino acid with broad specificity, except for -Pro.
Sequence Length: 507
Sequence Mass (Da): 58437
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A0A7C5EHH1 | MTEEKLESRLKKMVVRRLFMKIDPDSIDAGKSLVDDYGVDSVSLLELVVGLEEEFGIKVEDQEFDVNNFRTIEALAEFVRSKQQPS | PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine of apo-ACP by AcpS. This modification is essential for activity because fatty acids are bound in thioester linkage to the sulfhydryl of the prosthetic group.
Pathway: Lipid metabolism; fatty acid biosynthesis.
Function: Carrier of the growing fatty acid chain in fatty acid biosynthesis.
Subcellular Location: Cytoplasm
Sequence Length: 86
Sequence Mass (Da): 9852
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A0A7R9QRM8 | MSDNNMEGKDCLLSLETMNQRIRRMEYAVRGAIPMRATELEKELKSGLKKPFDEVIRANIGDCHAMDQRPLTFFRQVLSGVLNPNECLSNPNIPEDVKQRVTLLLDGCGGRSVGAYSDASGVEIIRRHVAEYIEERDQIASDWLNIVLTTGASEGAKAMLSFINSGSNDGIPTGVMVPIPQYPLYSATICELGMHLISYYLDEQNEWALSIDELSRALEESKNHCKPKAIVVINPGNPTGSVLTRHNIEDIIRFAKQNNLIIIADEVYQHNVWKNGAKFYSFKKVMHELEVKLELVSMMSASKGFMGECGLRGGYLEITNFEPQVKAMFFKMLSARLCSSILGQIAMDCVVKPPTIGEPSYEIFIKEKEEVLESLRKRAKLTADTFNSIPGIVSNPVAGAMYAFPKIVLPDKAIKAAEERGQKPDFFYVMTLLEKTGICVVPGSGFGQIPGTYHFRTTILPQTDKLERMMKKYTTMHSMAKSCDTFVVLPPMTAHKLTIFGKNSDRPNGEVQEIVYYPRNTYESGSKTECTYISIESTPQTYAVMLSKPSWMWGSEMGSNEFGLCVGNEAVWTQLNGPNDEEERLLGMDL | Pathway: Amino-acid degradation; L-alanine degradation via transaminase pathway; pyruvate from L-alanine: step 1/1.
EC: 2.6.1.2
Catalytic Activity: 2-oxoglutarate + L-alanine = L-glutamate + pyruvate
Sequence Length: 590
Sequence Mass (Da): 65930
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A0A2V6U2B3 | MTRRGRTVLKAWVWIGCLSPLLALLYRYWTNDLTANPVSFLTNTLGDWTLRLLLTSLALTPLRIMFGIGWQMPLRRLVGLFAFFYASLHFAVWLVIDQFFDWHAMLADILKRPFVTAGMCALTLLLPLAVTSTAGMVKRLGARAWTRLHRLVYVIGILGVVHFIWLAKVGRVTPYSYAGILALLLGIRAVDMLRRLVRRRWNSPSHLNGDRRMRTSMREWARGLVVLAGSAFLVGGCAHSMTADEKMMDKGMMSDDGGMAKDAGMSTDKEMMQDKGTMQDQGTEKK | Cofactor: Binds 1 FMN per subunit.
Function: Part of the MsrPQ system that repairs oxidized cell envelope proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated cell envelope proteins from methionine oxidation. MsrQ provides electrons for reduction to the reductase catalytic subunit MsrP, using the quinone pool of the respiratory chain.
Subcellular Location: Cell membrane
Sequence Length: 286
Sequence Mass (Da): 32243
Location Topology: Multi-pass membrane protein
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A0A7R9MDI4 | ILKFQTFLLVVLLFICSCTYLHGVFPACEGAKELLWQARLLKESEELWARCEELSGAHERAHSSNKLPFSWPSGSGALVHYLISNWIAYCSRYIMTSDWCISSRDILDSISWQDFCSCSQTWQINFGKVRKRDRPFRVSEQQADQSTSPTGSSSLTTTLSFQLPLTTFAISNTIAWLPKPAAATYRCFVCSCCFLFQQLLQLHLAFVAYYKADMRASLYVRPLSFFFATVGLLYHDTTHTTGRKCKTFYRAKGFSSSLLRTHFHSQHTLSTYPIPPTTLSQRSVVLDLSILLQLDSIAKMSSYLSHLNTHVLPTRHEYLQRLFVQRIRLSSDFIDKEKTCMLCQTPFTQHIVNKDDCELQPALIHGNHHACRMCVLKWLVQERKNKCPFCRLPLYRQDRCIMTYDAENGHGNEEDENYHRLDYQRYHVNDSDKDILTQLRHSPFAPDFATAVQSRAWHYEQGQLTVDRPDYAAYSAHLQTTLPDGIRATRYRTLHADRLSEAVRAAYYQLLRDDLRRSRPTIASHPVATLAAGDMIKTLFEALNGQRMTVRQLSSAIYTGLDSTHFDIWVRKLIREQSLPEGYMDYCCDLIEAIMYDFAGKDAVAVLKQNRLERKRQRRAYLRDPARRQRQRVRKMILRPKLELNIVQYSPNDDISAE | Function: Involved in the early part of the secretory pathway.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 658
Sequence Mass (Da): 76210
Location Topology: Single-pass type I membrane protein
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A0A3E2GU15 | MAYLPVSLISTTLAFVALVAAHGHVSNIVVNGIYYQNYDPTSFPYIPIPPIVIGWTAGDSDNGFISPDAYQDPDICHKDATNAGGHASVAAGDSISIQWTPWPDSHHGPVIDYLANCNGPCETVDKTMLEFFKIDGGGVISGGNPGTWFSDSLIADNNTWLVQIPPDLTPGNYVLRHEIIALHASGSPNGSQNYP | Function: Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds. Involved in the degradation of complex natural cellulosic substrates.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
EC: 3.2.1.4
Subcellular Location: Secreted
Sequence Length: 195
Domain: Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.
Sequence Mass (Da): 20793
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A0A8K0YBY1 | DKVPFHPYYTIKDILGIILMIALLMILVLFFPDLLGDPDNYTPANPLNTPPHIKPEWY | Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis.
Subcellular Location: Membrane
Sequence Length: 58
Sequence Mass (Da): 6709
Location Topology: Multi-pass membrane protein
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A0A7R9QNZ4 | MPLKTEVYNKAHNINEYTLSNSTGGLVVRIIDYGATITHLFVKDKNGQPRDVVLGWDDLDGYLGNKGRNPYFGAAIGRCGNRITNGKFELNGQTYQLALNNGPNALHGGVKGFDKRKWTLIGSTDDSITLELISEDGDEGYPGRLRVALTYTVTDDNELRLEYTARLTDNQSVETVVNLTNHSYFNLNGCTRGEELDVLNHTVRMTATNYLDINENFQPTGKILSTKTDTPVMDFATGDGQPRHTIGERIAQVLPNGYDHCYVIDTDDKTYNIAGNEEIREAVVEVSSPLTGVRLTFSTTEPGFQFYTGNNVGSGQTTKTSQSSPALELRKNSGFCLESQRFPNAINEGKWRPQVLLSPNATYSQTTAYKFGLI | Pathway: Carbohydrate metabolism; galactose metabolism.
EC: 5.1.3.3
Catalytic Activity: alpha-D-galactose = beta-D-galactose
Sequence Length: 374
Sequence Mass (Da): 41363
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A0A154MVJ6 | MMCYVVFGCRCALIVVFAMSAMSKSRNRESFAAFRRATVELVPAARGHGTSLAVSVVVAELLVVAGLVVPNTATVGLLAASALCTAFTVAIAAALRRGVTASCRCFGGSATPLGARHLVRNALLIVLAVLALVLPGRDDVGSDPAALLLAAGAGVVVASLVISFDALADLFLGGPPPSTITKGSPHDRPVRRRRARRDAVPARPRAHPRRHPPAA | Pathway: One-carbon metabolism; methylamine degradation.
Function: May be specifically involved in the processing, transport, and/or maturation of the MADH beta-subunit.
Subcellular Location: Cell membrane
Sequence Length: 215
Sequence Mass (Da): 22185
Location Topology: Multi-pass membrane protein
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A0A1I7SUW1 | MQDEAVETDPEEPVVRTYTKIQKILWLLVMCVLLFGFVLFTVLIGHFSRDIAAWSQKKVTAKTILLWNDPCKTCGQVGYENGTEFSDLLSDTCGKKCVFVSDWALQNSSDAVIVFPRTIENVDNKFPNRSFPTQKLVLFEKEPPSKDNTQKSSVLVPDGLFNWVASYVPDADIVLPYGRLVKRLPPYKHDRDFKDDLVDIVNRKTDGVFAYTTNCGTNSNKERIFEELRKYIQVDVYSKCGNSSCDSKCFKSNLKKYRFYLAFESTVCDNYVTEKFFRTDNKIVPVVLRRKDYLDFGANHDFIALDDFPNPASLANYLKELMQDNDAYMKYFEWSKEWKKITQPLPYSLCSVCDYIHQPSRSRSVLGEQSFSDWYSPKRRCDSDFIDDFLNPDL | Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
Subcellular Location: Golgi apparatus
Sequence Length: 394
Sequence Mass (Da): 45654
Location Topology: Single-pass type II membrane protein
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A0A2E4HQ82 | MIKLTWIKRWFIEMGSPPHFFTWSSRLLPWLYPLSFLVLLCGIIWGVFIAPTDYKQGDIYRIIFIHVPSAILAQSIYIMMSVFGAICLIWRVKLAGMFLRSAAVLGGSFTLIALVSGSIWGKPTWGTWWVWDARLTSTLILLFLYAGIISLYSSIDNKQKGDRAASLISIVGVAIVPIIKKSVDWWQTLHQPSTFTLTSAPSMTADMYLPLLVCVLGFYLVFFSILFNKIQVEILIRERNTSWVKNYFLEKEDGTNI | Function: Required for the export of heme to the periplasm for the biogenesis of c-type cytochromes.
Subcellular Location: Cell inner membrane
Sequence Length: 257
Sequence Mass (Da): 29318
Location Topology: Multi-pass membrane protein
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A0A2E6M391 | MECASMLNQKSSANSYSEESLPSEVCTFPPEKRILKSDEFGRVFKTGNHRIRQDSLQLIALTHQHDISRLGLVVPKKMLKRAVHRNRLKRLVREAFRQWKSPVPCDVVISLKQKIDPQLLYSDSMAVSIQQVFQKLDRYSSRPPKRKKG | Function: RNaseP catalyzes the removal of the 5'-leader sequence from pre-tRNA to produce the mature 5'-terminus. It can also cleave other RNA substrates such as 4.5S RNA. The protein component plays an auxiliary but essential role in vivo by binding to the 5'-leader sequence and broadening the substrate specificity of the ribozyme.
EC: 3.1.26.5
Catalytic Activity: Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Sequence Length: 149
Sequence Mass (Da): 17261
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J2JRD3 | MNRARSTRKRSRKRAALQMSTVVVATAALAASGATAGPATAATGGPTPVPAQSAGSATATGHGIRVGTVKITTRLRNGRYELTDPTRGGLTVKDYLNNEYFGDLELSKPFTGKDNVWGNGTTSSRESAAVDAHFAAEQAWDYFKNTFHRLGPRGDNKGPTLYVHFKKNFSHAQAIDDPMAAFFGDGKDNKKPVTSLDAVAHEYTHLVSDATAKFGYSAESDALNEATSDIFAAMVEFQANLPSDPPDYLFEEKVYGKSTPLRYMDKPSRDGKSPDFWKPGIRSGKDGDIHFLAGIANHFFYLLAEGSGKKTINGVAYNSPTIDGRKVAGIGRAKAARIWYEALTTQFNSATGFKQARTGTLKAAARLYGTSSPDYAAVQKAWAAVNVK | Function: Extracellular zinc metalloprotease.
EC: 3.4.24.-
Subcellular Location: Secreted
Sequence Length: 388
Sequence Mass (Da): 41711
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A0A7C4RBZ1 | MQQTYVYKWLDLNIVFKIGGHVIFNGDELNINLLKVYSNIFRETYDGGRWVIVVGGGKPARKYVESARKLGLNEGLCDEIGIKITRINAMILSSLLGELAYPVIPENLEQVRAYSTSGRIVVMGGLQPGQSTIAVSALVAETINAEKLVIATDVDGIYTEDPKKNPDAKLLREISVNELTKKLIEYSHEAGEYKLADLQGLKIISRSHITTIYLNGRNPENLRKALKGEQVGTLLKS | Pathway: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1.
Function: Catalyzes the reversible phosphorylation of UMP to UDP.
Catalytic Activity: ATP + UMP = ADP + UDP
EC: 2.7.4.22
Subcellular Location: Cytoplasm
Sequence Length: 237
Sequence Mass (Da): 26245
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A0A6N9FHT3 | MLLLRRISRLPASIDRGCAVTIGGFDGMHVGHQEVLRRVIRAARERNLASVVFSFEPSAKEFMARGTPPPRLMTLREKCAALNTAGVDAIYCPPFNDSIRTLSPDDFMRKLLSGLLNARHVIQGPDFRFGYRRSGGMDELAAGGRRLGFSVEQAPPVSVDGERVSSTGVRRALAASDLAQAAKLLGRRYCMGGRVIHGLKIGAAKLGYPTANIALKGRVSPIDGIFAVRVHGVEDEPLAGVASIGYRPTVGGTEKILEAHIFDFSGDLYGRFLDIEPVAKLRDEVHFKNLEELRVQMDRDADQARELLRAA | Pathway: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.
Function: Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD.
Catalytic Activity: ATP + FMN + H(+) = diphosphate + FAD
Sequence Length: 311
Sequence Mass (Da): 33961
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G8YVP9 | MDAETNINSGLPYNLRDRKHRIKLSSNGADSSGGLRNQLFIQASHMKSNINHRKKRNIIFQYNYTNIVTVLILPILTIIYLAKFSTTILPQNHRILIFTFIYYNFTILAFISGYHKCYTHNSFRSRSVLLHYYFAIFGSSLGLGSIKWWSTLHKAHHQFTDNTEKDPYSIKRGFFWAHTGWLLVRFKHHALSESSENNHAERVAKEKLDDVSNEALYENDELDDDNDSLDENYDEYCKQLIKWQERCYLLFFIITSVAIPTAVTVCYLKDTFLNGLIYPGIVRMILCQQSILSTESICHMGYFNISIHSQPFSDKNSSQNCSNPLVSILTYGQAEQNFHHEFPHDYRNSPSSYSFDPTKWFIWVLHKFSFVDQLCVTPKALVMQLQIQQQQEIINRMKSRLIWGTPISRLPLIKPRDFKKIIASASQTGRIYIIIQNVIHDITPFMEQHPGGVQLLKASHGKDATKAFFGGVYGHSTAATNLLATMRIGLLDVGNNEEIWRRMVKEEGDMDDSNSRRENGSYKTAEAA | Cofactor: Expected to bind 2 Fe(2+) ions per subunit.
Function: Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates.
EC: 1.14.19.1
Catalytic Activity: 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA = (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O
Subcellular Location: Membrane
Sequence Length: 528
Sequence Mass (Da): 60897
Location Topology: Multi-pass membrane protein
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A0A6N8UNR9 | MELFETVLLILLVVVSVSLGGLVLIQQSKGADIGAAFGSGAANTLFGSSGATSFIVKFTAALAIGYFLIAFGLAYTAKERADSLKSYEIESLPAMVEDGDAIPSDEGAVTTTDEQDTQDVQLPLEGDDMPDLQTPSMEGAQGSEDSSNTSDEDTEELPDF | Function: Involved in protein export. Participates in an early event of protein translocation.
Subcellular Location: Cell membrane
Sequence Length: 160
Sequence Mass (Da): 16724
Location Topology: Multi-pass membrane protein
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A0A1I0G0A6 | MNHIVLVHPAIPQNTGNIMRTCVATNTCLHIIKPMSFDLDDKKMKRAGLDYVKDLNLSVYESFEEFEQKNPGEYHFFTRYSHLCYTDQDFSDSAKEHYLFFGHEHDGIPKEILTKHLESCLRIPMSDKVRSLNLSNCAAICIYEVLRQQNYPNLSKVEVQKGEDFLYEL | Function: Could methylate the ribose at the nucleotide 34 wobble position in tRNA.
Catalytic Activity: 5-carboxymethylaminomethyluridine(34) in tRNA(Leu) + S-adenosyl-L-methionine = 5-carboxymethylaminomethyl-2'-O-methyluridine(34) in tRNA(Leu) + H(+) + S-adenosyl-L-homocysteine
EC: 2.1.1.207
Subcellular Location: Cytoplasm
Sequence Length: 169
Sequence Mass (Da): 19711
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A0A2E6LVE1 | MPIQFLHDEPQVVPGLKCAAVEANIKKPGRLDLVLFDLGENATSSCVTTTNALAASPVLLTRKHQQEMTSRYWVINTGYANAAMGQAGDKAALDVVTALAKELDAPVESILPFSTGVIGEPLPVEKITAAIPALKAGLGEENWLSAVQGIVTTDTQYKLISKTFVWQEQAFIMQGIAKGAGMIKPNMATMLGFVATNLKIPQATLEPMLKTAVDQSFNAISVDGDTSTNDCVAFAATGHSELSVENDEAFKDFVQECLNKVCLELSLQIVKDGEGATKILEITCSGASSVEVAKAVAESIGHSPLVKTACFASDPNWGRILMAIGKAPNANVDANNLDVSLGGKLLFTQGGRIEGYVESEFAAIMEEQHIKIDVDLKQGDAAFTCWTNDLSYEYVKINADYRS | Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1.
Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Catalytic Activity: L-glutamate + N(2)-acetyl-L-ornithine = L-ornithine + N-acetyl-L-glutamate
Subcellular Location: Cytoplasm
Sequence Length: 403
Sequence Mass (Da): 43066
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A0A132N502 | MAASTGTNPSVDKAFYVTTPIYYVNDAPHLGHAYTTVAADVLSRWHRQRGEQVWFLTGTDEHGQKIMRAAQANGVSPQEWADRLVETAWKPLWRHLDISNDDFIRTTERRHTERVQEFWQRLYDSGEVYKGSYEGPYCVACEEYKLPGDLIEGENGEKLCPVHGRPVEMLAEENYFFRLSAYADRLLQHYEEHPDFIEPETARNEVVQFVKQGLQDLSISRSTFDWGIPIPWDTGHVLYVWIDALLNYATAVGYGADPEKFERTWPADVHLVGKDILRFHAVIWPAMLMAAGLPLPRKVFAHGWLLVGGEKMSKSKLTGISPQQLTEHFGVDAYRYYFLRAIPFGQDGSFSWEDMTARYTSELANDFGNLASRVAAMVNKYFGGELPEAAAAGEAEARIAAGLEQAARLADERMCALDFQGGLVAVFDFIKQVNGYVTEQEPWQVAKADDAASRARLATILYTAAESLRGIAVLLNPVMPAACAKLWESLGAEPHLGPLDRQRVQDAGRWGQLPAGVRITKGEVLFPRLPEPKEDA | Cofactor: Binds 1 zinc ion per subunit.
Function: Is required not only for elongation of protein synthesis but also for the initiation of all mRNA translation through initiator tRNA(fMet) aminoacylation.
EC: 6.1.1.10
Catalytic Activity: ATP + L-methionine + tRNA(Met) = AMP + diphosphate + L-methionyl-tRNA(Met)
Subcellular Location: Cytoplasm
Sequence Length: 536
Sequence Mass (Da): 60142
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A0A948FW92 | QEEEQFAKTLEQGMKILEQDLADLSASQIPGDTVFRLYDTYGFPVDLTADIAREKGLSLDLDGFESAMEAQRTRARSASNFKVDLSDELALDGETAFSGYQSLVDDVVVKAILRDGQRVSSLKEGDTGIIILESSPFYGESGGQAGDSGYLTAEGVRFEVRDTHKSGGHHLHHGLVLSGVIAEGEELCAEVNNEVRQATALNHSATHLLHAALRKVLGEHVSQKGSLVDSQRLRFDFSHFEAVSKQELTEIETLVNQQIRLNTPVQTEVMDMESAGKRGAMMLFGEKYGDSVRVLSMGGDFSIELCGGTHVQRTGDIGLMRISAESGIAAGVRRIEAVTGAAALAAFDSAENELSNLAGLLKTGREKIADKVQQLLAQQKQLEKELSALKGKLASSAGNDLMSQVEEINGVKVLITKLDGADAKSLRDTVDQLKNKLGSGVLLLAADEGEKVSLVAGVTKDLTGRFKAGDIMKLAAEAVGGKGGGRPDMAQGGGTDSAAIPAALQAVRDYCLAK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the attachment of alanine to tRNA(Ala) in a two-step reaction: alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). Also edits incorrectly charged Ser-tRNA(Ala) and Gly-tRNA(Ala) via its editing domain.
EC: 6.1.1.7
Catalytic Activity: ATP + L-alanine + tRNA(Ala) = AMP + diphosphate + L-alanyl-tRNA(Ala)
Subcellular Location: Cytoplasm
Sequence Length: 514
Domain: Consists of three domains; the N-terminal catalytic domain, the editing domain and the C-terminal C-Ala domain. The editing domain removes incorrectly charged amino acids, while the C-Ala domain, along with tRNA(Ala), serves as a bridge to cooperatively bring together the editing and aminoacylation centers thus stimulating deacylation of misacylated tRNAs.
Sequence Mass (Da): 54704
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A0A182DXA1 | MREEMHMDVVATIIILFSLTLLARPAYGSAGDRHHIYLSCVKSCILKYGCPRRFDESGWIFSECFRCRYKCTWKTVKYFNDILHLSVPQFYGKWPFLAIWIPFIMPIPIQEFASVVFSILNLFTTFSMYRTVKRLRSSNRLKIVWTAYSVIGIIMWTCSAIFHWADFWLTEYLDYFTACAFIVFALFIDFDYGYNMKMCIACSLLTAVIYCVWLVQQWKLRDHSGRRSLLCLTVMVIWGLLSVLLEVLDFVPIYWIIDSHSLFHLATVPLPLLMTRFILLENAYEMQQQIGNIKQT | Function: Involved in the lipid remodeling steps of GPI-anchor maturation.
Subcellular Location: Golgi apparatus membrane
Sequence Length: 296
Sequence Mass (Da): 34869
Location Topology: Multi-pass membrane protein
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A0A2E6NND6 | MKRMRLSEIIAAVDGSPGAAGTDDPAITGVCTDSRKVEPGELFVPLCGEHHDGHDFIAGAFERGAAASLSSRDASAGSGRRIVKVSDTLTALEDLALYNRGELSFEVTAITGSVGKTTTKEFLKHILGTDFTACAAPKSFNNRLGVALTLLETDEDTEHLVVEMGTSGKGELSYLSKRVRPERIIITTVALAHLEGLEDLPGIIAAKAEIFEGLDPAGRAYLNPAAPGYEEFRACLDGEPRTYGTVGADFPLELIPAAGGAQAGYRFRVGAEEYTLDLPGEHNVTNASGAIAVALDLGVSPASIREGLARCRLPPGRLNVWTEAGVHFVDDSYNANPCSMKAALDTFEEYCAGIAEGRNIAVLGEMLELGPRSRHYHAEIGSLLAGKPVDLLVTIRGSSRYLGEAFTRERESSGRRGDAKTMHFEELSPAREYLSEEIRSGDKLLFKASNAVGLSGLAEELRETVGADERELPLV | Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Function: Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Catalytic Activity: ATP + D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminoheptanedioate = ADP + H(+) + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine
EC: 6.3.2.10
Subcellular Location: Cytoplasm
Sequence Length: 475
Sequence Mass (Da): 50662
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A0A8T7AWC3 | MMNNRELQRLIAGLFPDDVAVAGSVTCPTDAALLPEEQHQTTAMVAKRLREFTHGRHCARQAMQQLGHAPAPVLKHEDRSPVWPDQICGSISHTGDIAAAVVAHRDGYRSLGLDIETAEPLDESTHALILRPDERSADGAQAKLIFSAKEAIYKTLYPLVGSYLDFQEMVVEFDKADGTFAAQPHTDRVPPPLAAALQGRYQVTPDWVVAATWIRAAAD | Pathway: Siderophore biosynthesis; enterobactin biosynthesis.
Function: Involved in the biosynthesis of the siderophore enterobactin (enterochelin), which is a macrocyclic trimeric lactone of N-(2,3-dihydroxybenzoyl)-serine. The serine trilactone serves as a scaffolding for the three catechol functionalities that provide hexadentate coordination for the tightly ligated iron(2+) atoms. Plays an essential role in the assembly of the enterobactin by catalyzing the transfer of the 4'-phosphopantetheine (Ppant) moiety from coenzyme A to the apo-domains of both EntB (ArCP domain) and EntF (PCP domain) to yield their holo-forms which make them competent for the activation of 2,3-dihydroxybenzoate (DHB) and L-serine, respectively.
Catalytic Activity: apo-[aryl-carrier protein] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[aryl-carrier protein]
Sequence Length: 219
Sequence Mass (Da): 23943
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G8YQS8 | MLVNRAIGLSRTKRAAFIDKKVSILRATLGSSRKANGLLASSFPTRTIPSSLHFLHTSSLLRNNMDSRNHGPGGKVSKETLLASASSITSKLLVHIKWPLMRNNRPFSVDDFSAFLSWLMMGNILWIILGTTTFGLTTMYMVYAYDNIKGSVCDPEYDEKSGKRSIDRSTLASLTNKILSSGLGFQFEFEKGFVLPEMIDGKLRFSNLNVYYKNLITDNEENLDGEFVNFSGNINSMDISLSFRKWYEGRGLIEDVEIHGLKGNVLKGTNRMVDVIEEPTFTSSSVRNGGFADEEYTQVSENNDLIGTGNQRQLLFSPSYELSNFKLRDSHIEIYEEENEIPLRISIFNCDLPRLRGSQVLFDFLNSTSISGAINESLFTLYKRQNFNNSKGDGKVVRFTLNGINLGNITASSPKSRLNWIVNGKSEITTDITLPQLGDTESNFAVNTEYNRISQIFSQLLHEMISTPCEDKESNKASRYDSNLLKGALTAIYQTFTNDDQHVRDYNSNEKSSQYMMINVAIKFRDLKASLPSELPVAASSSVPFISLQNLRSLISYTNEISATRDSPITVKSTVIHKINDMNDLNDLYHNKILDEIVSDIYEELLRMVELEEQRIIKERSSLWSHSLSSQLLLLGLGVLA | Function: Involved in the organization of the mitochondrial membranes and the global structure of the mitochondria. Also required for mitochondrial distribution and mobility as well as for the maintenance of mitochondrial DNA nucleoids structures.
Subcellular Location: Mitochondrion inner membrane
Sequence Length: 641
Sequence Mass (Da): 72142
Location Topology: Multi-pass membrane protein
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A0A1N5VEH6 | MKSGKINRKVEFSIYQTFPYLEALALQRKINSEMINGSGRESIIICEHEPVYTCGIHQDGNTTNLEGVYFIERGGGITYHGPGQITAYFMINLNQRGINILDLINFVHEVEIQYLEQHGIVAHSRLKKETGVWVGNHKISSTGFALKGGFTLHGIGLNVNTDLQKFSLINPCGFDWSVMTSVSKLNGKTYHMEEEKGLFLKILKENLGI | Pathway: Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2.
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
EC: 2.3.1.181
Catalytic Activity: L-lysyl-[protein] + octanoyl-[ACP] = H(+) + holo-[ACP] + N(6)-octanoyl-L-lysyl-[protein]
Sequence Length: 209
Sequence Mass (Da): 23463
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A0A8S2CX87 | MCSKNIYYHGSKVTPEERVIAIGQRGAFHGSTVWLTGLPAFCLDGDNIRCGLNKNLGFSDVDREENIRRVAEVSKLFAEAGLMCIVSFISPFEKDRAHARRLHEECKLPFIEVFVDTPLAICEERDVKGLYQKARNGQIKNFTGIDGLYERPLDPDITIDTATTSAEKAIESIIALLAERGVLSPTLISSVRELFIDDLTKQQILVDLDDIPRLSITKVRYPTQLSPDRESFIPLLD | Pathway: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3.
Function: Catalyzes the synthesis of activated sulfate.
EC: 2.7.1.25
Catalytic Activity: adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)
Sequence Length: 237
Sequence Mass (Da): 26582
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G8YAE5 | MLALKPIWKPRTGFRPVVSVGNILTHRSNFSSGIVRYNSVAATTSKDVDLSAFKIETVKDLAQTGVFDKSITDSLSKEKFTQLTPVQQQVILPIVTHDKGLVCRAKTGTGKTLAFALPTLQDSIKHGRLGKVRTLVIAPTRDLALQIENEYLRLIKHMPVKYKKLLTPTVHIGGKRTIFNSKRISSIAIATPGRLNDNLNNEMFKEAFDSLRYRIYDEGDRLLDQGFERELYEINEKLRESRTVDSNLVPLLFSATVNDRVHNFALKSIGRNYDFINTVNENEPEAHENIEQILVKTDGIDESFKGALCFSVKTITESNGKVIVFLPTINAANWFFSAVKEAYFSGDRRKSRNRPAIVLLHGKKTQSAREIAVSKFRTNATGILVTTDVAARGLDFKDVSHVVQMTPSMSLSDYIHKIGRTARAGAHGQAILYSTRSEEKYVNALEKEKGIKFSHVVQYSDQAKEEDEVFFEQLGDLSPEFQDCIRSLLSYYKQVSSVFGIPFRKYLDSLLVYYRSILNDSSAKFPFGRKFSLGILSIPDRVASSYFSDGDRQFRSRDNFNQFTSYNKYGGRGDDRNRYDSRNKFDGRNKFDNGRRFDRPKKTFKRSNRFDD | Function: RNA helicase.
EC: 3.6.4.13
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Length: 612
Domain: The Q motif is unique to and characteristic of the DEAD box family of RNA helicases and controls ATP binding and hydrolysis.
Sequence Mass (Da): 69585
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A0A2E4N8Y3 | MLVSEEKLQDRVAELANQIQSNFKNSDLIVVGLLTGTIIFLADLIRKIDLPLRLDFIGVSSYRNGTESSKLVFTKELKIDVRDQDVLIVDDILDTGKTLKSVIDKIKAMHPRKISTCVLLSKKTRREYNIPADYIGFEIPNEFVVGYGLDYAEEYRNLPFIGALNN | Pathway: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1.
Catalytic Activity: diphosphate + IMP = 5-phospho-alpha-D-ribose 1-diphosphate + hypoxanthine
EC: 2.4.2.8
Subcellular Location: Cytoplasm
Sequence Length: 166
Sequence Mass (Da): 18809
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A0A1S8L1I5 | MVITVTLNPAMDKTLNIDDFNVGVVNRVGSIRYDIGGKGINVSKVLKNFNVESKCTGFIGGMWESSFKEELEKRKINNEFITINGDTRTNTKVVDDLNKVYTDINEAGPNISHDELEVFINKFKAMCNKDDIVVLSGGVAPGIEKNIYGTLTKIAKDNGAFVILDAEGELLSEGIKEKPYIIKPNDMEFELLLGKKFKNNDDIIEGAKEVIAKGVSNVLISLGSKGALFVTKDKAYYAKGLVVPVKSTVGAGDSMVAAFVYGIINGLNEMEILRFSIACGAASVSTEGTEACSLEDVQELLKRVEVEEV | Pathway: Carbohydrate metabolism; D-tagatose 6-phosphate degradation; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-phosphate: step 1/2.
Function: Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.
EC: 2.7.1.144
Catalytic Activity: ATP + D-tagatofuranose 6-phosphate = ADP + D-tagatofuranose 1,6-bisphosphate + H(+)
Sequence Length: 309
Sequence Mass (Da): 33578
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A0A936AMI6 | MRPAGTARRIGVFGGTFDPVHNGHLRTALELVGALRLDELRLIPCHTPATRVLPATTPGQRLAMLRLAIADCPPLRCDDREIRRGGTSYTIDTLRSLRAELGASARLCLIIGADAFAALDSWKEWDRQVDLAHIAVLERPGERAAHSPALARWVAAHRADNIEQALGQAACGSILALQLTQLAISATRIRALLAAGDTPRFLLPDAVLDYIRQHHIYESATPAEEGASM | Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
EC: 2.7.7.18
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Length: 229
Sequence Mass (Da): 24812
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A0A2H1A691 | MSVDTSFLDNVKEPKNFNNNAPFDLLVSDLFLKLESTTSENKAPFDTVSAKKTHIIEEFVKTWRTHFGPNILPAVRLIFPNRDGRKYHVKDVALTRLVNKLLKLQPGSGDYQIIKNWKKSYQQKANLANDSERRQLGDLPLIIARIISRRRDQTVPVKSSVTVAEVNDVLDQLAQKTQSKEQLALLEPFVEKLTIPEVRYVFQMILKESMLSFFERAFFLAWHPDAYNLFKVCEDMKKIFWVLSDPEKRLLPTQLCVQPMYMFVPQSSQKLDISYDSLCKRMTVALQTENKDKKLVDLYKQEQIEGHFLIEEKIDGDRMLMHMVNGKFRWHTRRRRDYTLVYGENIHIGSLTKHLTDALDDKVHSIVLDGEMVAWSKDREMILPFGTLRSAAIQEALKQFDVIDVYEGNNSWPLFLIFDILHLNGRDLTGLPLFYRKSLINKVVKEVPHRFEILEWVKAKSPTDIKANMQRIVSERNEGIMVKSLLSKYRVYSRESTWIKVKPEYLENFGENLDLVVIGKIGRVKTSYICGLKDIEAEGCYKSFCMVANGFSNAVYRQIESKLVNFWHDYTVEKPPATLIQFGTKKPDYWINPANSIVLEIKARSIEVTAETPYAAGSTLHNLWCRAVREDKDYDECITLQEYQELKARYSTDIYKNQDVNRNRKRPGENSIIEKYEKVKKLKIAAESDLLTGIHFVIATDYKDPDESKSMSAEALKQLVRSHGGAIELNPKRNELHEKTVMVVGTNLTPRLQRWYKEGFDVISPRWIVESIRHEKLLPIEPSFIVASVNAGFMNLAHQNVDEFGDSYVVTATSSQGLLQHLMSLTVKKRLADDSIERCRRLFLEESDRESDPHWWMLFYGLKFHIVGSRSSITSHKAAAGSLSQRIARFGGECIGDVHQSHYIVVPEKVEKKHEVVAEVARVSRELGARYVEGKKIARVVRESFVVESVKEGVVVDAEDHNYSAD | Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
EC: 6.5.1.1
Subcellular Location: Nucleus
Sequence Length: 966
Sequence Mass (Da): 111330
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A0A3L7QL86 | MRFDVLTLFPDLFQGYLSQSLLKLAIQTEKVSINLWNIRDWAKGKHSKVDDRPFGGGPGMVMMPEPIFDCVEEVRLKVVENPGLLVMLTPAGEKLNQKLVEELSGHSRILLLCGRYEGFDERIRIGLKPREISIGDFICNGGEVPAMVLIDSVIRLVPGVLGDPESLTEETHNDPGVVEYPQYTRPRVFRGAEVPEVLLGGNHAAIASWRAEQSKLRSQGLIQ | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.228
Subcellular Location: Cytoplasm
Sequence Length: 223
Sequence Mass (Da): 24845
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A0A3C0KXD5 | MAIALTELDQDLWFPHPEQALDEPEGLLAMGGDLSQNRLRLAYRHGIFPWYEDDQPLLWWSPPDRAVVFPDRFKPSRSLARLLNQNVFQVTLDERFDAVIAGCQQHRVQQGLGTWITQEMITAYSLLFAAGDAHCIACYSKGRLVGGLYGISVGSVFCGESMFSLESNASKVAFSHLVRTCRTLGINLIDCQMPNPHLLSLGAEVLPRTTFLRLLADFADTAVDWSQLAGPLAAWNKDAGSSS | Function: Functions in the N-end rule pathway of protein degradation where it conjugates Leu, Phe and, less efficiently, Met from aminoacyl-tRNAs to the N-termini of proteins containing an N-terminal arginine or lysine.
Catalytic Activity: L-leucyl-tRNA(Leu) + N-terminal L-arginyl-[protein] = H(+) + N-terminal L-leucyl-L-arginyl-[protein] + tRNA(Leu)
EC: 2.3.2.6
Subcellular Location: Cytoplasm
Sequence Length: 243
Sequence Mass (Da): 26913
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A0A3A0CCN9 | MSLIQRNVVLASGSPYRKQLLEDAGVAFRVVVSHVDEDLHPHDEPHAYVRSLASRKAMAVVPSCPDALVIAADTICTWRGRIINKPADEADARRMIAEACDARLQRVITGVCVVDSRDMTTLSFAECSIVEMKPASAEQIDAYVRSGEPMGKCGALAIESSGSFVARYEGSYANIMGLPVERLLPVLLKLDA | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + H2O = a 2'-deoxyribonucleoside 5'-phosphate + diphosphate + H(+)
EC: 3.6.1.9
Subcellular Location: Cytoplasm
Sequence Length: 192
Sequence Mass (Da): 20815
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A0A959MIK5 | MHFDVLTVQPELLASPLQHSIMKRAQDKGLLTVEIHNLRKWAVNEYGMIDDYQYGGGAGMVMMCEPLANAIESLSQTKKYDEVIFLTPDGETFDQSMANQLSLKENILLICGHYKGIDERIREHFITKEISIGSFVLSGGELPAAILIDAIGRLLPGVLNDETSALTDSFQDNLLAPPVYTRPEDFRGWKVPDILLSGNHKKIEDWRQEEALKRTREKRPDLLK | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
EC: 2.1.1.228
Subcellular Location: Cytoplasm
Sequence Length: 224
Sequence Mass (Da): 25322
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A0A2J7QA37 | MSAMAVGEKRVKSIDDSFQNASKVLVDIEGTTTSISFVKDTLFPYIRSNLQSYLKAHWNDAEFQQDLLLLKEQAKQDEADKVDGAVLIPEDNEDNTMEAVAKNVLWQMDLDRKTKALKQLQGHIMREGYKNGNLKGHVYSDVVPALKSWAHSGRRIYVYSSGSVEAQKLLFGHSEEGDLLDLFAGHFDTEVGPKVEPDSYVNIVKKLDCRSEDIVFLTDVPREAEAAQKAGLKAVIVVREGTELLTEEDKVSFPVIKSFHDFVFEASAKRKKMCTNDESPANGPISETSESSITEKNKAVKKTEEVSPESAGSGNTVSSSDCEMMDVSSNDAQVTDMEPDKTKIESQSTDDKTMAVEDSDTKESEKVELEPDDSEVCKTESSAPESKTVGAPDVEKESPKVCSENAEECDGKEVSVTSLTKLSAEVSKVDIDVKLNDSKADKKDSEAGETEVDIKGIPANEEETKVDAEETEAVGMSTKDKNVEVRISENDSRDGAELETVSGGSKNKSVGTISNCLESESGALETGSEEGKIDSCDEVAEVNAGDKKKFCDSRSASGDVKGDSCNEDANLEETEADTQNKKTDVNNTETEEKMETNTTEIENVKGINDEDVKDTEKNDRDTLAAEMEDEITEEMESSAKLGKNDVALKKKIDMESGGTANGREKGENTKPSEDLSVSEESGVTKSESEVATKTESDILNQTSEKQSDIDFSADASPENTDASPEESKTEGISEDPESTDKMLQDKMEDVSDAVKNEDSELLATSDNDTVKEDANANEDTKPLDSKNEGDEESKTAEDTAKENGLAFTTENGKGDVTNKCPDTEQNGEVTDKEQDVKIKKLSIDGSGNTSMTKDDVATPAVASGSS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene).
EC: 3.1.3.77
Subcellular Location: Cytoplasm
Catalytic Activity: 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate
Sequence Length: 866
Sequence Mass (Da): 93930
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