ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9XFM6 | MALELWQTLKEAIHAYTGLSPVVFFTALALAFAIYQVISGWFASPFDDVNRHQRARSLAQEEEPPIPQPVQVGEITEEELKQYDGSDPQKPLLMAIKHQIYDVTQSRMFYGPGGPYALFAGKDASRALAKMSFEEKDLTWDVSGLGPFELDALQDWEYKFMSKYAKVGTVKVAGSEPETASVSEPTENVEQDAHVTTTPGKTVVDKSDDAPAETVLKKEE | Function: MSBP1 can bind to multiple steroid compounds with different affinities. Negatively regulates cell elongation and brassinosteroid signaling. May act as a coreceptor with BAK1 and enhances its endocytosis.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 24405
Sequence Length: 220
Dom... |
Q9FVZ7 | MAAAVAELWETLKQAIVAYTGLSPAAFFTAVAAAAALYHVVSGIFAGPPPPPPPRPRDEPEAEPLPPPVQLGEVSEEELRQYDGSDPKKPLLMAIKGQIYDVTQSRMFYGPGGPYALFAGKDASRALAKMSFEPQDLTGDISGLGPFELDALQDWEYKFMGKYVKVGTVKKTVPVEDGAPSTSPETTETAAAAEPEKAPATEEKPREVSSEEVKEKEDAVAAAAPDEGAKES | Function: Binds multiple steroid compounds (By similarity). May act as a coreceptor with SERL2 and enhance its endocytosis (Probable).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 24635
Sequence Length: 232
Domain: The cytochrome b5 heme-binding domain lacks the conserved iron-binding His... |
Q03455 | MNLQELLAKVPLLLSYPTIILSSNLIVPSHNDLISRAASTSAAEYADEKLIFFSTDHAIRLIFLPTFVASSFNLFAHYFNFINYSSRRKYYVLFTAIYFLSILTAIFHPIQSTCITLLIIKLLTTADESSPKIALNFKTILKTFVPFITLTLVILRWDPSFDASSGDVNKISTSLAAYALLILTLRYASPLILSTLSSSIGVVSKDTSVAQHSISRNKRFPLILVLPIFSFVLLYLMTIVNKTYNIQLLMVFVFFGCLSIFFLSLKDLFTEDGNQKKGGQEDEYCRMFDIKYMISYLWLTRFTILLTGIMAIVVHFLSFN... | Function: Probably act as a zinc ion transporter moving zinc from the nucleus/endoplasmic reticulum to the cytoplasm. Involved in zinc ion homeostasis and cellular distribution.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80578
Sequence Length: 724
Subcellular Location: Endoplasmic reticulum memb... |
Q74ZL3 | MVHLPLSRSRSGRRAVPDLSRYQQFYEADAADGYSTGSGLSSAAASVASLRRPGVGMGRTQSLTGYGRTRSLGAARPSYLGAPPRTYSMSSQRRANSLRSNNGFGPPAVAAGNTITVKTTETKDLQGRTRTVTRQTVKHINGVRYVETTTTMTMPDGEYPDDFYGFEGDFTAKQTSSGHVYQNARGAPDISDIAEEESLEEYLDARDTAPALRIQLRAPPRVQQQRQLQRQRRLSDTNFPARRSAKSSPARQSSEEPPATTKPHRIRFDETPQIVGIDPPTQKKAPKKQMTEQEMYMHALDAARKKVYGEISQPALEAKQ... | Function: May be involved in the control of meiotic sister-chromatid recombination.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 81930
Sequence Length: 751
Subcellular Location: Cell membrane
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Q6FX33 | MGFLTKKERRVPDLSRYDYHYQNKPAVDSSKYYVPREYGGKRLSASAAAAAIYTNPNPNATGVSRSYSLMHSYNPAAARQPPAGRTYSLRSDRASSITSNSRRPAAGKAQVRRASTQQRRASVDQELGTGVNQPRTNSITVTTTKVRDPQGRTKSITKKTVRRINGYEVVETTTTTTTTEPLPTQNGKMPANMDLVSVEDGTDVEEEHDDGLPSPQAHFDEFSGDFVAEDDLSSEVLQHQQQQYIEDIVEEETEEEEDPGHTGTKRLPGEFNEPPRTNIAARRSNSLTGSLSSLGAKKTISEEVPLDQTSSVSKFSDAME... | Function: May be involved in the control of meiotic sister-chromatid recombination.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 89322
Sequence Length: 834
Subcellular Location: Cell membrane
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Q6CK58 | MVFGMNLGNRRKATRVPDLSRYDYHYNGSGGNSVNQGDNYLKSHELSADAAFAASARAGSLVNYPERGYTNISRANSLRMGHPGQQQQQSSYIPRSYSFTARGAYAPRTGNVGNRRSVSAIPRTGTASSRGVGSRTGSMTGSVARVGSRTGSFAGGGNGSIIIKTQEVKDMMGRTQSITTQTIRRINGMEYVETTTQTAGLVEDPQFHFQQFAENDEFPISDELSATPPAAPLSESQPRTNQRLANFNSNAINNSAANNIRSDSEEEGEEHFTDASDVVEESGAFAEDDQDHFLAKVNKVDVDNNSKSYTSRKPLVQKQG... | Function: May be involved in the control of meiotic sister-chromatid recombination.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 71450
Sequence Length: 652
Subcellular Location: Cell membrane
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Q05812 | MVFGFTKRDRRVPDLSRYDYYYQNHEDYNKSPQLSAAAASAASAASPDRTNYSRSHSLVSHAPSIPRQRSSVKSPGRRLSTSSAAPPTSRAAAKQYSQKTYSLRSQRSGEYHLHPPGYTTNGSRMNSMTSGANVRRNYGKNKSTAGNNNDSRANSITVKTTQVTDPSGRTQSITKKTIRKINGYEYVETTTTTKNLVPLGDSQRHFDEFSENYMLQDDDILEEQASDNIHDIIEENETDNEKPYSPVSESHLQDDSELNVEKPDFPLGSYFHHKYSTDVMPLEEESSLSNFSDALDYIPPTHQTSSKYIHNKRKQASTTR... | Function: May be involved in the control of meiotic sister-chromatid recombination.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 80530
Sequence Length: 728
Subcellular Location: Cell membrane
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Q5ZSH7 | MSLLKEFKEFAMRGNVMDLAVAVVMGVAFNKIVTALVDGIIMPCVGLLLGGINIAGLSFTVGDVQIKWGNFLQNVIDFIIVAFAIFVLIKLINLLQRKKANEPEPVTPEIQLLTEIRDLLARNSSKI | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13941
Sequence Length: 127
Subcellular Location: Cell inner membrane
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B1MZU9 | MLSEFKTFIMRGNVLDLAVGVIIGGAFTGIVKSLTNNLISPIITFFTGGTSDLQNLKLVVTKELTFKYGAFLNDVINFLITAFVVFLLVKFVNRILRTNKKEEVKANPELEVLAEIRDLLEAQKKA | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14023
Sequence Length: 126
Subcellular Location: Cell membrane
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Q03SF6 | MLKEFKEFIARGNVMDLAVGVIVGAAFTAIVNSLVTNIINPLLGIFVGSIDFSNLVFTVGSAHFRYGAFINSVINFLIIAFVVFLLIKLINKLIAKPAEEPEEAVPSQEEKYLQEIVELLKQDKIEH | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14079
Sequence Length: 127
Subcellular Location: Cell membrane
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Q1WVR1 | MLKEFKEFISRGNVMDLAVGVIIGGAFTAIVNSLVKYIINPFLGLFVGAIDFSDLVFKIGNATFRVGSFLNAVINFLIIAFVVFLMVKGINKVLRQDKKEEAPAPKDPQLEVLEEIRDSLKKLDK | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13891
Sequence Length: 125
Subcellular Location: Cell membrane
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Q929V3 | MKKMLVEFRDFALKGNVLDLAVAVVIGAAFGKIVSSLVNNIIMPFVGVLLGGLDFSDLSFKVGKSVIQYGAFIQSIVDFVIIAFAIFIFVKVLTSFIKKKEQPTEETPVPPTEEYLKEIRDLLKEQQK | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14242
Sequence Length: 128
Subcellular Location: Cell membrane
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Q5NNP2 | MSILTDFKNFISKGNVLGLGIAVIMGDAFNKIISSVTGDLLMPIIGAVFGGVDFSGFFIRLGAVPAGYTGSLTSYNDLKKAGVPLFGYGQFLTVVVNFVIVAFILFMIMKLAAKLQKELDKTEAKKEEKIAEAAPTPEDIVLLREIRDELRGKK | Function: Channel that opens in response to stretch forces in the membrane lipid bilayer. May participate in the regulation of osmotic pressure changes within the cell.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16679
Sequence Length: 154
Subcellular Location: Cell inner membrane
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Q8R6L9 | MWADIYHKLVEIYDIKAVKFLLDVLKILIIAFIGIKFADFLIYRFYKLYSKSKIQLPQRKIDTLTSLTKNAVRYIIYFLAGASILKLFNIDMTSLLAVAGIGSLAIGFGAQNLVKDMISGFFIIFEDQFSVGDYVTINGISGTVEEIGLRVTKIRGFSDGLHIIPNGEIKMVTNLTKDSMMAVVNIAFPIDEDVDKIIEGLQEICEEVKKSRDDLIEGPTVLGITDMQDSKLVIMVYAKTQPMQKWAVERDIRYRVKKMFDQKNISFPYPRTTVILSEKKTN | Function: Mechanosensitive ion channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Has high selectivity for anions, and may contribute to resistance to hypoosmotic shock.
Locati... |
P0C0S2 | MEDLNVVDSINGAGSWLVANQALLLSYAVNIVAALAIIIVGLIIARMISNAVNRLMISRKIDATVADFLSALVRYGIIAFTLIAALGRVGVQTASVIAVLGAAGLAVGLALQGSLSNLAAGVLLVMFRPFRAGEYVDLGGVAGTVLSVQIFSTTMRTADGKIIVIPNGKIIAGNIINFSREPVRRNEFIIGVAYDSDIDQVKQILTNIIQSEDRILKDREMTVRLNELGASSINFVVRVWSNSGDLQNVYWDVLERIKREFDAAGISFPYPQMDVNFKRVKEDKAA | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
T0DVE4 | MDEIKTLLVDFFPQAKHFGIILIKAVIVFCIGFYFSFFLRNKTMKLLSKKDEILANFVAQVTFILILIITTIIALSTLGVQTTSIITVLGTVGIAVALALKDYLSSIAGGIILIILHPFKKGDIIEISGLEGKVEALNFFNTSLRLHDGRLAVLPNRSVANSNIINSNNTACRRIEWVCGVGYGSDIELVHKTIKDVIDTMEKIDKNMPTFIGITDFGSSSLNFTIRVWAKIEDGIFNVRSELIERIKNALDANHIEIPFNKLDIAIKNQDSSK | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
P0DKS1 | MNIYKEIDNASNWISDNHILFIKYISNIILSLIILIVGYSASKVTQKIIKNFMIKKNIDIIISEFFCSIIKYSILIFTIVTSLGCIGIQTTSIIAVIGAAGIAIGLALQGSLSNFAAGVLLVTLRYFRTGDYVNLCGVKGKIKTVQIFCTKIKTKDGKIIIIPNNKIISSNIINYSEELHRLMEVIISTEYTSDIKNVKEIIIDVLKKETRIVKEKKITVRLKNLGESSLDFLVRGWVYKKELKQTTSDILEKIKIELDKNKINIPYKQIDVNLKYSKEK | Function: Mechanosensitive channel that participates in the regulation of osmotic pressure changes within the cell, opening in response to stretch forces in the membrane lipid bilayer, without the need for other proteins. Contributes to normal resistance to hypoosmotic shock. Forms an ion channel of 1.0 nanosiemens con... |
A6W733 | MTTTPQPPPQPDETPEGAAGAATAGRDPLEIAADLVDDVSRELDPAELASLERLDQPRRILFVHAHPDDESIGTGATMARYAEAGAGVVLLTATRGELGEVIPPELAHLDPDALAEHRTGELATAMEALGVSDHRFLTRPDGTGYRDSGMVWLEPGRAAAGDDVDPRSLAAADPEEVAARIAEVVREVRPQVVVTYEPGGGYGHPDHVRVHEATVRALVLAAGDGSRGAGGAVPWQVAKVYEIVQPERPVREALRRLAETGAEGAGDPEGPLPSVVVPDGEVTTVVDGTGQVPAKIAALRAHATQVTLDLDAAVPAMRLS... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deacetylation of 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside (GlcNAc-Ins) in the mycothiol biosynthesis pathway.
Catalytic Activity: 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O = 1D-myo-inositol 2-amino-2-deoxy-alpha-D... |
D2PN56 | MSELPDRRLLLVHAHPDDETINNGATMARYVAEGAHVTLVTCTLGEEGEVLVPELAHLAADQSDQLGRHRIGELAAAMDELGVTDHRFLGGPGRYRDTGMIYDEQGNAAVPPDTRPDSFWQADLVTAANDLVTVIREVRPQVLVTYDEFGNYGHPDHVQAHRVATYAAALAAARSYREDLGPAWDIPKIYWTAISETAMRSSLRRLRESGDHTTFEGMDPDGPLGPMITPDRFIDCVIPADGYLDRKMNAMKAHATQITVDGPFFALSNNDGNEIFGDEFYRLVKGTAAPGSDGLEHDLFAGL | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deacetylation of 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside (GlcNAc-Ins) in the mycothiol biosynthesis pathway.
Catalytic Activity: 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O = 1D-myo-inositol 2-amino-2-deoxy-alpha-D... |
A0R2I7 | MSSHESPRLLFVHAHPDDETLTTGGTIAHYVARSAEVHVVTCTLGEEGEVIGERYAQLAVDHADQLGGYRIAELTAALQSLGLRGPRYLGGAGHWRDSGMAGTPSRGRQRWVDADLDEAVGALVAVIGEVRPHVVVTYDPNGGYGHPDHIQTHVVTTRAVAAAPEAVGWTVPKFYWTVTAISAMTAGLQALGDVPSEWIRVNAEDIPFGFGDDQIDAVVDVTAELPAKVGAMRAHATQITVAPDGRAFALSNNIALPVLGEEHYVLVSGEAGPRDSRGWETDLLAGLDLE | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deacetylation of 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside (GlcNAc-Ins) in the mycothiol biosynthesis pathway.
Catalytic Activity: 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside + H2O = 1D-myo-inositol 2-amino-2-deoxy-alpha-D... |
D1BS17 | MRTWPTPDVPPLPRTGAPAPVLVHDSTTQSLVEAAPGATATLYACGITPYDATHLGHANTYLAFDLLQRAWLDAGKTVVYTSNVTDVDDPLLERATATGVDWRELAREQTELYRTDMTALRMLPPATWTGAVESIPAVVEAVTALLDAGAAYRVDADVYADLSADPGFGRVAGLDDATMRALFAERGGDPDRPGKKHPLDPALWRGEQPGEPSWDGGKLGPGRPGWHIECAVIARDGLGLPFDVQGGGADLLFPHHEMSTSHARLLAGGAARVHVHAGLLAYDGHKMSKSRGNLVFVSRLLAAGTDPMTVRLALLAHHYR... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the ATP-dependent condensation of GlcN-Ins and L-cysteine to form L-Cys-GlcN-Ins.
Catalytic Activity: 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + ATP + L-cysteine = 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + AMP + diph... |
A0LWI8 | MTVLPASIRIEPHGRLAPALLPRVFALVDDATDTDGVQPLSEHVVLHLRYGGDERGCNLLLWVDDDEPRLAGYAHLDATDPVEAPSAELVIAPDFRGRGLGTMLVEAILARTGGRLRLWAHGELPAAQAMARRLGFARRRVLLQMRRDLFAPLPPVTLPDDVQIRTFRPGADDDAWIALNARAFADHPEQGSWTLEDLHRRMQESWFDPDGFFLAERDGELVGFHWTKVHGSPAGQASNGSSGHGHEPLGEVYILGVDPKAQGLGLGRALTIVGLRYLRSRRLPHVMLYVDATNAPAIRLYESLGFRHWGTDVLFERGGT... | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 35940
Sequence Length: 327
EC: 2.3.1.189
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C7M077 | MHALTTVENPSARLLPGVLALIRDVEAADGHEVLEAHRWIDLANADAESLHGIAVTLDDDTVVGYVHLRRHHRHGIELELLVAPDHRDEAASIVGALVEAASASLETLGPHEIFAWVPRHSRQVIDALEGLGFRADRAVRQLRRPLPLESDHPARPIDCPPFRTFRPGEDEDAWLEVNNRAFAWHPDQGDWDLETLLARERESWFDPAGFLLAEQDGRLVGFCWTKVHAPRSSSALGEIYVIATDPERAPRGLGSCLLVAGLDYLAHHDIPTASLYVEDTNERALRLYDRFGFVVDHEDVRLVWRLPAAS | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 34642
Sequence Length: 310
EC: 2.3.1.189
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Q5EDG0 | MSGDGEWRQELDEQQLEDVRRLLLAVREADGRPEVEPAGALPGEFDGGEHLVACVEGEVVGYAHLNTTGNSFGHQVAELFVHPAHRNRGYGAKLLQALDERAAVGFRVWAHGDHPAARKLALKTGLERKRELLILHVDVEGADWPEPILRDGVSLRTFVPGQDEDAVVRVNARAFDWHPEQGALTVEDVRADERRAWFDEDGFFLAEERGEVIGFHWTKVHEPTPGRFGGERVGEVYVVGVDPAAQGGGLGRALTLAGLRYLASRGLRQIILYVEGDNAAALAVYTKLGFTRHETDVQYGR | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 33223
Sequence Length: 301
EC: 2.3.1.189
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C5C246 | MQAYDDEIVGTALASNVLALADRVRTADGVEALSEQHRLALEHPGLRAHHLVVTDPAGAVVGYASVLGSSVEMLVDAAHRGEGVGHRLAEAALAVEPTLAFWAHGDLPGAAQLAEAIGLRRVRELWHLGRDLAPAGAGGDEAALLATPLPGGERLRTFGGTEAEEHAWLALNARAFASHPEQGAMTLEDLRVREGETWFDPSLLWLVHDDGDGALLASMWLKVPDAATGEIYVLGVDPGAQGRGLGRALTDRALDVLRARGVDRVELYVEGENARARALYEHSGFTPVAVHAQYGIP | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 31485
Sequence Length: 297
EC: 2.3.1.189
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C7MGB3 | MITTTALVPARRSAVRTLLATVTEHDGVSPLDEAALLALDGEDARHLLLTADGAATDTHAAEATAGSAASADPADPADPAAPADPADPADETLLGYVSVLGDGTVQGMVDPAHRRRGHGSALLRAALALRPDAGVWVHGALEGSLAFLTDAGLTETRRLLTLRRDLGGAQPLPSAPAPTLEGLRLDTFEESRDAEAWVAVNVRAFADHPEQGALTRADLEQRLAQPWFDAEDMLVALRDETLVGFVWIKREQPGATDRDAEIYVVATDPSVQGHRVAGHLMATVLERLERDGVPGVELYVEADNAPALRLYENWGFEVSG... | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 35181
Sequence Length: 331
EC: 2.3.1.189
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C7QKH8 | MTGISIGVVRRPNEADVATIRSLAEAAERADGVAPLPEQVLLHLKRSGDADADADTDAWHFVARRLSPQGSELTGYAFLDKSNAEEGPTAEVVVLPDARRQGVGGALLDALRMKVRRGDKPIRVWSHGALPAAAALAAKRGLEPVRELWVMSRPLADVPPAPTPPDGIRIATFRPGVDDEAWVEVNARAFAHHPEQGSMTVQDLRDRMAEPWFDPEGFFLAWRGAKLAGFHWTKVHDHSAYGDGPVGEVYVVGLDPAEQGHGLGRTLTEVGLRHLHDRGLGEVILYVEADNTPAVAVYTKLGFTRRSADVMYQL | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 34116
Sequence Length: 314
EC: 2.3.1.189
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D5UJR1 | MSSDIEAPTSLTSMRGALPPAVADDVRALHLTTVRHDGVPPLSEQPLLWLSDQEAPVVHVLAWHAVTGGAQELVGYAQVDVGSSTTARAELVVAPGHRRRGTGRSLLAHAAQEAASIPGRRLHVWAHGDLPAARATAAATGLVVVRELWRMAVDVTQHPPGAPQLPPGVAVRAFVPGQDEDAWRRVNARAFAHHPEQGRMTSADLRARESEPWFDPAGFLLAERDGQLLGSVWTKVHPGSEAPDGAPGEEVGEIYVVGVDPDAQGLGMGRALTALGLAHLRDRGLRTVILYTGAENTVAVHTYRRAGFARTAVDVMYGPP... | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 36655
Sequence Length: 348
EC: 2.3.1.189
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B0RAV5 | MSAFPPPPEPDAPRVAHVEPAPDAVRGILALADRARADDGVAPFNEQTRLTLGADGGPTLLLAHGTDDDPLGAAVVAHGDAGIEAELVVDPAHRRRGVGRALLDAVLAEAAGSPVSVWAHGDHPAARALADATGLDRARELLQLRASVAEARTGLGERQMPAGVALSSFTADDADDWVALNARAFASHPEQGRMTRGDLDDRVAEAWFDPASLLLARDADGRLAGFHWLKVDGGQAEVYVLGVDPDRAARGLGSALLAAGLDLLAERGHDEVDLYVEADNTPALALYRRAAFRDAAVDVQYRRA | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 31915
Sequence Length: 304
EC: 2.3.1.189
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C3PIU4 | MNIETNTVPQNLDLAQRVEELAAAAETHDGVAPLSEQFLIGLRDDRLGHRHLLAIEGDEVLGVAALDGQTVELFVGVDNRGRGIGKALVDALPASPQIWAHGNLPAAQALAKRNEMDVVRRLLVMAIEGRDLRAAEEAPTTVDGLEIQTYTESVERFGREHVEAEWVRTNNEAFSWHPEQGGWDLERLHRGMEAEWFDPADVLFLWDSHGGAHSAPTMAGFHWLKWHAEDTPAFGEVYVVGLAEDYRGRGLGGPLLTAGLQRMVEKGADKVILYVEADNDPAVKAYERLGFSIAEEHCVWAKSD | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 33540
Sequence Length: 304
EC: 2.3.1.189
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Q6NFH9 | MKMIETSLASASAALRDRVDEILAAATREDGCAPLSESFLNGLRRADDGHVHSCVMDSHDQVVGVAARDGDSAEVVVDPAFRRQGYGSFLIRHVVSQGVKNVWAHGDGAGAKAVAKALQLEQTRQLLVMAVEGDRLVESAQLQVPSGFRVLALNEAYESIPDIEQQWLRVNNEAFEWHPEQGGWDSARLAQARDTQWFRESDVLFLIDTAKRTVAGFHWTKRHGDLAEGADGEVYVVGLGSAYRRRGLGDLLIRMGLHHLEYEHARRVILYVEGDNESARRAYDALGFHVVESHVTYSPQSSS | Function: Catalyzes the transfer of acetyl from acetyl-CoA to desacetylmycothiol (Cys-GlcN-Ins) to form mycothiol.
Catalytic Activity: 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + acetyl-CoA = CoA + H(+) + mycothiol
Sequence Mass (Da): 33488
Sequence Length: 303
EC: 2.3.1.189
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Q96DH6 | MEANGSQGTSGSANDSQHDPGKMFIGGLSWQTSPDSLRDYFSKFGEIRECMVMRDPTTKRSRGFGFVTFADPASVDKVLGQPHHELDSKTIDPKVAFPRRAQPKMVTRTKKIFVGGLSANTVVEDVKQYFEQFGKVEDAMLMFDKTTNRHRGFGFVTFENEDVVEKVCEIHFHEINNKMVECKKAQPKEVMFPPGTRGRARGLPYTMDAFMLGMGMLGYPNFVATYGRGYPGFAPSYGYQFPGFPAAAYGPVAAAAVAAARGSGSNPARPGGFPGANSPGPVADLYGPASQDSGVGNYISAASPQPGSGFGHGIAGPLIA... | Function: RNA binding protein that regulates the expression of target mRNAs at the translation level. May play a role in the proliferation and maintenance of stem cells in the central nervous system (By similarity).
PTM: Phosphorylated.
Sequence Mass (Da): 35197
Sequence Length: 328
Subcellular Location: Cytoplasm
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Q920Q6 | MEANGSPGTSGSANDSQHDPGKMFIGGLSWQTSPDSLRDYFSKFGEIRECMVMRDPTTKRSRGFGFVTFADPASVDKVLGQPHHELDSKTIDPKVAFPRRAQPKMVTRTKKIFVGGLSANTVVEDVKQYFEQFGKVEDAMLMFDKTTNRHRGFGFVTFENEDVVEKVCEIHFHEINNKMVECKKAQPKEVMFPPGTRGRARGLPYTMDAFMLGMGMLGYPNFVATYGRGYPGFAPSYGYQFPGFPAAAYGPVAAAAVAAARGSVLNSYSAQPNFGAPASPAGSNPARPGGFPGANSPGPVADLYGPASQDSGVGNYISAA... | Function: RNA binding protein that regulates the expression of target mRNAs at the translation level. May play a role in the proliferation and maintenance of stem cells in the central nervous system.
PTM: Phosphorylated.
Sequence Mass (Da): 36939
Sequence Length: 346
Subcellular Location: Cytoplasm
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O22469 | MAAEEGKDEAGLDQVEEEFSIWKRNTPFLYDLMISHPLEWPSLTLHWVPSTPIPYSKDPYFAVHKLILGTHTSGGAQDFLMVADVVIPTPDAEPGLGGRDQEPIVPKVEIKQKIRVDGEVNRARCMPQKPTLVGAKTSGSEVFLFDYARLSGKPQTSECDPDLRLMGHEQEGYGLAWSSFKEGYLLSGSQDQRICLWDVSATATDKVLNPMHVYEGHQSIIEDVAWHMKNENIFGSAGDDCQLVIWDLRTNQMQHQVKVHEREINYLSFNPFNEWVLATASSDSTVALFDLRKLTAPLHVLSKHEGEVFQVEWDPNHETV... | Function: Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA.
Sequence Mass (Da): 47983
Sequence Length: 424
Domain: The DWD box is required for interaction with DDB1A... |
O22607 | MESDEAAAVSPQATTPSGGTGASGPKKRGRKPKTKEDSQTPSSQQQSDVKMKESGKKTQQSPSVDEKYSQWKGLVPILYDWLANHNLVWPSLSCRWGPQLEQATYKNRQRLYLSEQTDGSVPNTLVIANCEVVKPRVAAAEHISQFNEEARSPFVKKYKTIIHPGEVNRIRELPQNSKIVATHTDSPDVLIWDVETQPNRHAVLGAANSRPDLILTGHQDNAEFALAMCPTEPFVLSGGKDKSVVLWSIQDHITTIGTDSKSSGSIIKQTGEGTDKNESPTVGPRGVYHGHEDTVEDVAFSPTSAQEFCSVGDDSCLILW... | Function: Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of the flowering autonomous pathway which positively regulates flowering by promoting transcrip... |
Q9SU78 | MESEAAATVQATRPRRAPRTPVTAILTDKRRRKPKSNNESQLPFLLQQSQKATVDDTYSQWKTLLPILYDSFVNHTLVWPSLSCRWGPQLEQAGSKTQRLYLSEQTNGSVPNTLVIANCETVNRQLNEKAHSPFVKKYKTIIHPGEVNRIRELPQNSKIVATHTDSPDILIWNTETQPDRYAVLGAPDSRPDLLLIGHQDDAEFALAMCPTEPFVLSGGKDKSVILWNIQDHITMAGSDSKSPGSSFKQTGEGSDKTGGPSVGPRGIYNGHKDTVEDVAFCPSSAQEFCSVGDDSCLMLWDARTGTSPAMKVEKAHDADL... | Function: Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA (By similarity). Acts together with PDP1 and MSI4/FVE to regulate the function of the PRC2 complex on FLC ... |
Q9L0Q1 | MATVTFDKATRVYPGSTKPAVDGLDIDIADGEFLVLVGPSGCGKSTSLRMLAGLEDVNGGAIRIGDRDVTHLPPKDRDIAMVFQNYALYPHMSVADNMGFALKIAGVNKAEIRQKVEEAAKILDLTEYLDRKPKALSGGQRQRVAMGRAIVREPQVFLMDEPLSNLDAKLRVSTRTQIASLQRRLGITTVYVTHDQVEAMTMGDRVAVLKDGLLQQVDSPRNMYDKPANLFVAGFIGSPAMNLVEVPITDGGVKFGNSVVPVNRDALKAASDKGDRTVTVGVRPEHFDVVELNGGAAKTLSKDSADAPAGLAVSVNVVEE... | Function: Part of the ABC transporter complexes DasABC-MsiK and NgcEFG-MsiK involved in N,N'-diacetylchitobiose ((GlcNAc)2) uptake. Responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40396
Sequence Length: 378
Subcellular Location: Cell membrane
E... |
Q40518 | MTSVGLAPVSGLRESSSHSVGVDRLPEEMNDMRIRDDKEIEAAIVDGNGTETGHIIVTTIGGRHGQPKQTISYMAERIVGQGSFGVVFQAKCLETGETVAIKKVLQDKRYKNRELQTMRLLDHPNVVCLKHCFFSTTEKDEVYLNLVLEYVPETVHRVIKHYNKLNQRMPLILVKLYTYQIFRALSYIHHTIGVCHRDIKPQNLLVNPHTHQVKLCDFGSAKVLVKGEPNISYICSRYYRAPELIFGATEYTTAIDIWSAGCVLAELLLGQPLFPGESGVDQLVEIIKVLGTPTREEIKCMNPNYNEFKFPQIKAHPWHK... | Function: May mediate extracellular signals to regulate transcription in differentiating cells.
PTM: Autophosphorylated mainly on threonine and serine residues.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 46309
Sequence Length: 409
EC: 2.7.11.1
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Q9LYG9 | MAEQKSSNGGGGGGDVVINVPVEEASRRSKEMASPESEKGVPFSKSPSPEISKLVGSPNKPPRAPNQNNVGLTQRKSFARSVYSKPKSRFVDPSCPVDTSILEEEVREQLGAGFSFSRASPNNKSNRSVGSPAPVTPSKVVVEKDEDEEIYKKVKLNREMRSKISTLALIESAFFVVILSALVASLTINVLKHHTFWGLEVWKWCVLVMVIFSGMLVTNWFMRLIVFLIETNFLLRRKVLYFVHGLKKSVQVFIWLCLILVAWILLFNHDVKRSPAATKVLKCITRTLISILTGAFFWLVKTLLLKILAANFNVNNFFDR... | Function: Mechanosensitive channel that opens in response to stretch forces in the membrane lipid bilayer.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83032
Sequence Length: 734
Subcellular Location: Cell membrane
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Q8VZL4 | MAGVRLSLLKSIQRSIKPHATAKSCSGLLNSHARAFTCGNLLDGPKASPSMISFSSNIRLHNDAKPFNYLGHSSYARAFSSKSDDFGSIVASGVTGSGDGNGNGNDWVEKAKDVLQTSVDAVTETAKKTKDVSDEMIPHVQQFLDSNPYLKDVIVPVSLTMTGTLFAWVVMPRILRRFHTYAMQSSAKLLPVGFSNEDVPYEKSFWGALEDPARYLVTFIAFAQIAAMVAPTTIAAQYFSPTVKGAVILSLVWFLYRWKTNVITRMLSAKSFGGLDREKVLTLDKVSSVGLFAIGLMASAEACGVAVQSILTVGGVGGVA... | Function: Mechanosensitive channel that opens in response to stretch forces in the membrane lipid bilayer.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53884
Sequence Length: 497
Subcellular Location: Mitochondrion membrane
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Q6PDM1 | MTMRSAVFKAAAAPAGGNPEQRLDYERAAALGGPEDESGAAEAHFLPRHRKLKEPGPPLASSQGGSPSPSPAGCGGGKGRGLLLPAGAAPGQQEESWGGSVPLPCPPPATKQAGIGGEPVAAGAGCSPRPKYQAVLPIQTGSIVVAAAKEPTPWAGDKGGAAPPAATASDPAGPPPLPLPGPPPLAPTATAGTLAASEGRWKSIRKSPLGGGGGSGASSQAACLKQILLLQLDLIEQQQQQLQAKEKEIEELKSERDTLLARIERMERRMQLVKRDNEKERHKLLQGYEPEEREEAELSEKIKLERQPELCETSQALPSK... | Function: Component of histone acetyltransferase complex responsible for the majority of histone H4 acetylation at 'Lys-16' (H4K16ac) which is implicated in the formation of higher-order chromatin structure . Greatly enhances MSL2 E3 ubiquitin ligase activity, promoting monoubiquitination of histone H2B at 'Lys-35' (H2... |
Q2W5W8 | MSLWGPSKTVMVSADKALPGRASEIRVPERHYVLDTLLKPPFPVGMEVACFGMGCFWGAERLFWKTGGVYSTSVGYTGGFTLNPTYEEVCSAQTGHTEAVLVAFDPAEVSYTALLRLFWEGHNPTQGMRQGNDIGTQYRSAIYWTTPEQQAAAEASAKAYGEALRRAGFGAITTEIAPAGRFYWAEGYHQQYLAKEPGGYCGLGGTGVRYG | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)... |
B3PND9 | MKKIYVAGGCFWGVQGFLKTIKGIKKTTVGYANSLLENPTYELVKSHVTDAVETVEVIYDENILSLKDIVKKLFAVIDPTARNYQGPDHGRQYRNGFYFVDQEDGVMLRELMLEFSKKYEKPLATEILPLDNYYLAEDYHQDYFDKHPNAVCHIKF | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)... |
Q8TQV6 | MEGNEKAEQKNATSEESTDIFENPGEGLEKATFAAGCFWGIEEAFRQVKGVVATAVGYSGGHFEKPTYEQVCTLDTGHAEAVRVIFDPKVVSYKNLLDVFWKIHDPTTKNRQGPDVGKQYRSVIFYHNEEQKAAALASKEELEKAGVFKNPIVTEIVPVSEFYMAEDYHQQYFEKKGFLQNILRSFKK | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)... |
Q12TP4 | MERATFAAGCFWGVEAAFSKVEGVISTKVGYTGGTLKDPTYKDVSTGSTGHAESIDIIFDESVITYGELLEVLWNTHDPTTKDSQGPDHGSQYRSAIFYHDDAQREAALRSREQLERSGKYDSTIKTEIVKASEFSPAEDYHQKYFQKLQFKR | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)... |
Q2FQ35 | MGIAFFAGGCFWGIEAGFQKVPGVINTKVGYMGGHTIEPTYQEVCSDTTGHAETIALEYDDTAITYRKLLEIFFSLHNPTEVNRQGPDVGSQYRSVIFYTSPEQKEEAEMFIAEMNQSGRYHAAIATEVVPAETFWPAEEYHQSYFLKIGQRYGRSLF | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)... |
A9AB97 | MTNTETAVFGMGCFWSAEELFRKINGVISTEVGFMGGNIKNPTYGQVCRGRSGHIEVVNIIYNPKILKYDDLLELFWNNHDPTTPNRQGWDVGEQYSSHIFYFTEEQKLLAEKSFEKIQKNSELKIVTAIRKASDFFPAEEYHQKYFMKKNNCILNF | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)... |
A3CUG3 | MAPEKSLERATFGAGCFWGVEEAFRRVPGVVETAVGFMGGTVENPTYPEVCTGRTGHAEVVQVTYDPGTVSYRALLDTFWDAHDPTTPNRQGPDIGTQYRSVIFVHTPEQEAEARASKEEMDQSGKFRRPIVTAIEPAGTFWRAEEYHQQYFAKRGGGQCRTVW | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)... |
Q6LYY1 | MKNIKTTVFGMGCFWGAEEVFRKINGVVSTEVGFMGGTIKNPTYGQVCRGKSGHIEVVKIDYDPEIISYDELLDLFWNNHNPTTPNKQGWDVGEQYSSYIFYFDDEQKLIAEKSLEKMQENTDLKIVTIIEKAGSFYPAEEYHQKYFMKKNNSILNF | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)... |
O26635 | MMCLSRYEKATFGAGCFWGVEDAFRKVDGVVSTRVGYMGGHLENPTYEDVCTGLTGHAEVVEVTFDPDVVGYSDLLDVFWSIHDPTTLNRQGPDVGEQYRSVIFYHSDEQRRAAIESRRRLEESGRFRDRIVTAIEPAGTFYEAEEYHQQYLEKNPRRRCYLMRLLSTR | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol +... |
Q9D6Y7 | MLSASRRALQLLSSANPVRRMGDSASKVISAEEALPGRTEPIPVTAKHHVSGNRTVEPFPEGTQMAVFGMGCFWGAERKFWVLKGVYSTQVGFAGGHTRNPTYKEVCSEKTGHAEVVRVVYRPEHISFEELLKVFWENHDPTQGMRQGNDFGTQYRSAVYPTSAVQMEAALRSKEEYQKVLSKHNFGPITTDIREGQVFYYAEDYHQQYLSKNPDGYCGLGGTGVSCPMAIKK | Function: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)... |
Q6AUK5 | MGVQHLLKLRMASPHPHPHPGAPLAARPLSALASFFLARPSSTAAAPPPRHVTLSCSRPHCNHNQWAASRCRGTAGRRRLQVVVAMSSSAPPPPPGSVQKSEEEWEAILSPEQFRILRLKGTEYPGTGEYDKLFAEGVYECAGCGTPLYKSSTKFNSGCGWPAFYEGFPGAIARTPDPDGRRIEITCAACGGHLGHVFKGEGFNTPTDERHCVNSISLKFIPASEDSKL | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. MSRB family specifically reduces the MetSO R-enantio... |
Q9M0Z5 | MADLVTVVKKTEEEWRAVLSPEQFRILRQKGTETPGTEEYDKFFEEGIFSCIGCKTPLYKSTTKFDAGCGWPAFFEGLPGAINRAPDPDGRRTEITCAVCDGHLGHVHKGEGYSTPTDERLCVNSVSINFNPAKPSSIT | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. MSRB family specifically reduces the MetSO R-enantio... |
Q84JT6 | MPTSATAVAPSTGSVQKKDQDWRAILSPEQFRVLREKGTENRGKGEYTKLFDDGIYSCAGCATPLYKSTTKFDSGCGWPSFFDAIPGAIKQTPEAGGRRMEITCAACDGHLGHVVKGEGFPTATDERHCVNSVSLKFSEISSQ | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the reduction of methionine sulfoxide (MetSO) to methionine in proteins. Plays a protective role against oxidative stress by restoring activity to proteins that have been inactivated by methionine oxidation. MSRB family specifically reduces the MetSO R-enantio... |
B0BYW4 | MEKVQKTEQEWEAQLTPEQFRVTRHHGTERAFTGEYHDLKAAGTYQCVCCGTELFTSDTKFDSGTGWPSFWAPADKTHVEEKTDRSLFMVRTEVLCAVCDAHLGHVFNDGPKPTGLRYCMNSAALKFVPKS | Cofactor: Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Mass (Da): 14807
Sequence Length: 131
EC: 1.8.4.12
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Q6FAL8 | MGKLNKTEREWQRELSPEEYRITRQKGTEPAFTGQYWNTKQSGTYVCRCCGTELFSSISKYDSGCGWPSFYKPINTTAIEEHDDFSHGMVRTEIVCHHCDAHLGHVFEDGPQPTGLRYCVNSASLQLKTDEKNDEETYP | Cofactor: Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Mass (Da): 15964
Sequence Length: 139
EC: 1.8.4.12
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Q8UGX7 | MSDLTSPKVNKSDADWREQLTPEQYHILREHGTERPFTGPYWNSTEKGLYRCAACDEPLFLSDTKFDAGCGWPSYFEPVKPGAVTEHRDSTHGMVRTEIRCANCGGHLGHVFPDGPPPTGLRYCINGHSMVFEPV | Cofactor: Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Mass (Da): 15140
Sequence Length: 135
EC: 1.8.4.12
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Q0A706 | MVEVEKSDAEWRAQLTDEQYAVCRQGGTEQPFSGAYYHCKEPGTYHCVCCDAPLFSSRAKYDSGSGWPSFWAPISDDHLRILEDRSLGMVREEVRCARCDAHLGHVFPDGPMPTGLRYCINSVCLDLKRSG | Cofactor: Binds 1 zinc ion per subunit. The zinc ion is important for the structural integrity of the protein.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(R)-S-oxide-[protein]
Sequence Mass (Da): 14724
Sequence Length: 131
EC: 1.8.4.12
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Q8PLY8 | MSFRDALNLPSSEITDESVYRDRRRLLQLLALTPALGVAGCAEADPPPPPKTVVTPAQARSGFRTAEELTRLEDVTSYNNFYEFGTDKTDPSKAAKTLKLSPWTVKVGGECEKPGSLSLDELLKGIASEERIYRLRCVEGWSMVIPWTGVPLGEVLKRFAPTSKAKYVAFTTLADPQQMPGVRYRSINWPYREGLRIDEAMHPLTLLATGLYGKPLPQQNGAPLRLVVPWKYGFKSIKSIVEIRFVEKMPETAWHDLQPSEYGFFSNVNPAVDHPRWSQKTERRIAGTASKLFAERIATKPFNGYADQVASLYAGMDLKK... | Cofactor: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxy... |
Q8ZAW9 | MHNTFTHTKNNTHTKNNTQAKNSGSQTKSNAVSLNKPRKLTEADVTPESIFYQRRKVLQALGITAATLALPASAQADLLAWFKGNEPPKAPSGKPLTFTPSAAYHPDLALTPEDKVTGYNNFYEFGLDKADPAANAGTLKTEDWQIKIDGDVVKPMTLDMDYLMKCFPLEERIYRLRCVEAWSMVVPWIGFELGKLLKLAEPTSNARYVAFQTLYAPDQMPGQKNRFIGGGLDYPYVEGLRLDEAMHPLAFMVVGVYGKTLPPQNGAPLRLMTPWKYGFKSIKSIVHIRLTRDQPPTTWNLSAPNEYGFYANVNPHVDHP... | Cofactor: Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxy... |
P58769 | MAFALSLPSLPKRYQPAAIWSLYVIGLCPGLWYFYLAATGGLGFNPVKDFEHLLGIWALRFLCLGLLVTPLRDLFNVNLIAYRRALGLIAFYYVLAHFTVYLVLDRGLILGSIAGDILKRPYIMLGMAGLIILIPLALTSNRWSIRRLGSRWNTLHKLVYLVLIVGVLHFVLARKSITLEPVFYISTMVVLLGYRLVRPSIMTMKRNKRARPVRT | Cofactor: Binds 1 FMN per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic 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 generated by t... |
G8QMC1 | MTFQPTPRQLSAIKAALFLLTLLPALHYAHGLWSDSLGANPIEALTRGMGIWTLNFLFLTLCVSPLRKLSGWHWLLRLRRMLGLTAFAYGCLHLLTYLWLDQFWDVDAIARDIWKRPFITVGATAFLLMLPLALTSSHAAIRSLGGKRWQSLHRAVYAVAILGVVHYLWLVKRVALLDPIIYALVLAILLGWRVVERIRLNGPWPTRSTPPAVQPVVFMKRDAVAALGEPKKR | Function: Part of the MsrPQ system that repairs oxidized periplasmic 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 generated by the host defense mechanisms. MsrPQ i... |
Q7WD13 | MPAAPLTARAIGRIKPLLFVAGLLPFARWFWLGANDGLSANPVEFLTRSSGTWTLVCLLVTLAITPLRRLTGQPALVRLRRMCGLFAFFYGSLHFLAWVWWDRGLDPVSMLQDVGERPFITVGFAAFVLMAALAATSTQWAMRKLGKRWQVLHRAVYAIGLLAILHFWWHKAGKNDLQQPLLYGSVLALLLGWRVAAWWRRRGAAR | Cofactor: Binds 1 FMN per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic 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 generated by t... |
A6WYN0 | MAAAAQTGKKKTVRPGEWKIWLLYAVGFVPAVWTFYLGASGNLGADPVKTFEHTLGLWALRFLILTLMVTPIRDLTGMAFLRYRRALGLLAFYYALMHFATYMVLDQGLNISAIVTDIVRRPFITIGMISLVLLVPLALTSNNWSIRKLGRRWNSLHKLVYVAIAGGAIHFIMSVKSWPAEPVIYAGIVSALLLWRLVRPHARNRKPVSRPRGEAMAVKK | Cofactor: Binds 1 FMN per subunit.
Function: Part of the MsrPQ system that repairs oxidized periplasmic 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 generated by t... |
J4KLK4 | MALVEKIQLTDDFSVYANPAAKLEVEFIHKEIFIDKCYDVAPFPDDSFIVDAGGNIGMFTLYMKRKYPQSTILAFEPAPATFSTFQRNMELHNVSGVQAHQCGLGREDASLALTFYPQMPGNSTLYAEDKTNQMKSVDQNHPIAKLMQETHEVQVDVKRLSDFLGEVPNLKRVNLLKVDVEGAEMDVLRGLDDEHWDLIDNVVVELCDSKGDFATAKTLLESKGFAVAVERPDWAPPDLKMYMLIAKRN | Function: Methyltransferase; part of the pathway that mediates the biosynthesis of tenellin-type 2-pyridones, iron-chelating compounds involved in iron stress tolerance, competition with the natural competitor fungus Metarhizium robertsii and insect hosts infection . Methylates pyridovericin-N-O-(beta-D-glucopyranoside... |
P19888 | MKIKFVDLFAGIGGIRIGFERAAKRFELETECVLSSEIDKKACETYALNFKEEPQGDIHEITSFPEFDFLLAGFPCQPFSYAGKQQGFGDTRGTLFFEVERVLRDNRPKAFLLENVRGLVTHDKGRTLKTIISKLEELGYGVSYLLLNSSTFGVPQNRVRIYILGILGSKPKLTLTSNVGAADSHKYKNEQISLFDESYATVKDILEDSPSEKYRCSDEFIGQLSKVVGNNFELLHGYRLIDYRGGNSIHSWELGIKGDCTKEEIEFLNQLIANRRKKIYGTHQDGKALTLEQIRTFYNHDQLEVIIKSLLQKGYLREEE... | Function: A methylase, recognizes the double-stranded sequence 5'-GGYRCC-3', methylates C-4 on both strands, and protects the DNA from cleavage by the BanI endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequen... |
O30640 | MAEYTPKERLYRALRKQQVDRMPAVCFTQTATVEQMEACGAYWPEAHSDAEKMATLAEAAHTVVGFEAVRVPFDITAEAEFFGCGIKAGDLKQQPSVIKPSVKNLEDLEKLKNYNLKEGRIAVVLEAVKILSEKYGKELPIIGSMIGPFSLAQHINGDAWFGNLFTGEEVVPALLDFCSDFNVAYAKAMVENGADTIAIIDPTASYELIGGEFYEKYALPYQKKIVDAMKELDVATVLHICGNTTNGLGIMDKTGVNGISVDQKVDIKTATGSVKNAIIVGNLDPVAVLWNGTPEEIAEASKKALDAGVGLLTVGCGTVS... | Function: Methyltransferase involved in methanogenesis from methylamines methanol pathway. Catalyzes the transfer of the methyl group from the methylated corrinoid protein MtmC (MtmC1 or MtmC2) or MtbC to coenzyme M, forming the substrate for coenzyme-B sulfoethylthiotransferase.
Catalytic Activity: coenzyme M + methyl... |
O93661 | MATEYALRMGDGKRVYLTKEKIVSEIEAGTADAADLGEIPALSANEMDKLAEILMMPGKTVSVEQGMEIPVTHDIGTIRLDGDQGNSGVGIPSSRLVGCMTHERAFGADTMELGHIDYSFKPVKPVVSNECQAMEVCQQNMVIPLFYGAMPNMGLYYTPDGPFENPGDLMKAFKIQEAWESMEHAAEHLTRDTVWVMQKLFASGADGVNFDTTGAAGDGDMYGTLHAIEALRKEFPDMYIEAGMAGECVLGMHGNLQYDGVTLAGLWPHQQAPLVAKAGANVFGPVCNTNTSKTSAWNLARAVTFMKAAVEASPIPCHVD... | Function: Catalyzes the transfer of a methyl group from dimethylamine to the corrinoid cofactor of MtbC . The major or perhaps only DMA methyltransferase expressed under inducing conditions .
Catalytic Activity: Co(I)-[dimethylamine-specific corrinoid protein] + dimethylamine + H(+) = methyl-Co(III)-[dimethylamine-spec... |
P33563 | MTQILETVDKSRLTVNPLLKNKSELGQFFTPSSISIFMACLFSEDKLNNAKVLDAGAGIGSLTSAFLARLISENIGKADLHLLEIDEMLEPYLSETLALFKDYIEINSQIIIDDFIEWAAYSLLDEESLLAKDKQRFTHAILNPPYKKIKSNSKHRKLLRKAGIETVNLYSAFVALTVDLMSDGGEIVFIIPRSFCNGPYFRHFRQHLLNKTSIKHMHLFESRDKAFKDDEVLQENVISKLEKGTVQEDVKISISTDDSFSVIRSYRYPFEKIVQPNDIEKFIHINTTNEETLIEKHPNVCYSLEELNIEVSTGPVVDFR... | Function: A beta subtype methylase that recognizes the double-stranded sequence 5'-CTGCAG-3', methylates A-5 on both strands, and protects the DNA from cleavage by the BsuBI endonuclease.
Catalytic Activity: a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenos... |
Q9Y6C9 | MADAASQVLLGSGLTILSQPLMYVKVLIQVGYEPLPPTIGRNIFGRQVCQLPGLFSYAQHIASIDGRRGLFTGLTPRLCSGVLGTVVHGKVLQHYQESDKGEELGPGNVQKEVSSSFDHVIKETTREMIARSAATLITHPFHVITLRSMVQFIGRESKYCGLCDSIITIYREEGILGFFAGLVPRLLGDILSLWLCNSLAYLVNTYALDSGVSTMNEMKSYSQAVTGFFASMLTYPFVLVSNLMAVNNCGLAGGCPPYSPIYTSWIDCWCMLQKEGNMSRGNSLFFRKVPFGKTYCCDLKMLI | Function: Protein insertase that mediates insertion of transmembrane proteins into the mitochondrial outer membrane . Catalyzes insertion of proteins with alpha-helical transmembrane regions, such as signal-anchored, tail-anchored and multi-pass membrane proteins . Does not mediate insertion of beta-barrel transmembran... |
Q791V5 | MADAASQVLLGSGLTILSQPLMYVKVLIQVGYEPLPPTIGRNIFGRQVCQLPGLFCYAQHIASIDGRRGLFTGLTPRLCSGVLGTVVHGKVLQYYQESEKPEELGSVTVQKEYSSSFDRVIKETTREMIARSAATLITHPFHVITLRSMVQFIGRESKYCGLCDSIVTIYREEGIVGFFAGLIPRLLGDIISLWLCNSLAYLINTYALDSGVSTMNEMKSYSQAVTGFFASMLTYPFVLVSNLMAVNNCGLAGGSPPYSPIYTSWIDCWCMLQKAGNMSRGNSLFFRKVPCGKTYCYDLRMLI | Function: Protein insertase that mediates insertion of transmembrane proteins into the mitochondrial outer membrane. Catalyzes insertion of proteins with alpha-helical transmembrane regions, such as signal-anchored, tail-anchored and multi-pass membrane proteins. Does not mediate insertion of beta-barrel transmembrane ... |
G5ECI1 | MRSSLLLLVFFLSIGWARYCVHNEKSWCQGHNIWGWCFHNKSSGVFNCDDNAFCVSQEQLKNKKSSGCFLRDNSSICCCNDADGCNLGFIGVQPKYAHGQQCTNSMEVPNEDIRQFRPCDDPFCYSVLTAEDDGGPTTVTRGCHSRKMVMHHMSKNEDDKYQNNTKWRETKQIAEMPSCAEILKDQPKVNGTTSMCVDFTYDQEAEDGEEVDEPIKMKGRLCCCAGSNKCNEHAMWADEGISLTEMLEEIEARKVPVDSSAPVNIILSIAFSIFLIHF | Function: Plays a role in mechanosensory transduction (touch sensitivity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 31379
Sequence Length: 278
Subcellular Location: Cell membrane
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P05302 | MNIIDLFAGCGGFSHGFKMAGYNSILAIEKDLWASQTYSFNNPNVSVITEDITTLDPGDLKISVSDVDGIIGGPPCQGFSLSGNRDQKDPRNSLFVDFVRFVKFFSPKFFVMENVLGILSMKTKSRQYVKDIIAEEFSNVGYKVCVIILNACDYGVPQSRQRVFFIGLKSDRPLNQQILTPPSKVIESEYTSLEEAISDLPVIEAGEGGEVQDYPVAPRNKYQENMRKGSTCVYNHVAMRHTQRLVDRFAAIKFGQSVKHVSEEHSQRKRGDANSISGKVFSQNNMRPYPYKPCPTVAASFQSNFIHPFYNRNFTAREGA... | Function: A methylase that recognizes the double-stranded sequence 5'-CTNAG-3', methylates C-1 on both strands, and protects the DNA from cleavage by the DdeI endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Seq... |
Q86KU6 | MEEYKEIMQNKKGKVDVTPIANFFREEVKQQITKNCWKPRVVAFLTSDDQGAIDYSKWTKLACQKDGIEFILKRVERVDLEDLIIEANNDSCVHGILVYYPVFGGMMDSYLQDVVSPTKDIEGLSTQNRFNLYHNIRFMDGETATKKCVIPCTPLAMVKIIDNLGIYDKSLAMGEHLKGKTVTIVNRSEIVGRPLAAMLANDGAIVYSIDINGIIIFQSGKRHGTIKMSETNVTREEAISKSDILILGVPSPNYKVNSDLIQDGTIVINFAGCLNVDESIQEKSILVPTIGKVTIAMLERNLLRLFNNQISNK | Function: Catalyzes oxidation of cytoplasmic one-carbon units for purine biosynthesis.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NAD(+) = 5,10-methenyltetrahydrofolate + NADH
Sequence Mass (Da): 35069
Sequence Length: 313
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 1.5... |
P24600 | MKTIDLFAGCGGMSLGFMQAGFEIVAAVDNWRPAINTYQQNFTHPIHELDLAQIDAAVSLIKTHSPELIIGGPPCQDFSSAGKRDEGLGRANLTLDFAKIVLAIQPAWVIMENVERARLSKIHQQACSMLGDEGYSLAQVVLDASLCGVPQLRKRTFVIGHRHGSIADLANVLQQRLAKQSLTVRDYFGESLDTDYYYRHPRTYERRAIFSVNEPSPTIRGVNRPIPATYRMHPKDAGDVSLARPLTTKERSLIQTFPLDFKFVGTKSEQEQMIGNAVPVNLAFFLATSLQAYLNQPRMQQLSLLPSFF | Function: A methylase that recognizes the double-stranded sequence 5'-GRCGYC-3', methylates C-? on both strands, and protects the DNA from cleavage by the HgiDI endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
S... |
Q9RLM4 | MMSLKIQPAVPKKSDKPSATNRDCQNFKREKNNLPFQLTDKSCNLDISIRQERKKTLIFSFFSGAGFLDLGFELSGFDIAFVNEVHPPFLEAYKYSRSRMDIPKPKYGYFKGSIDECLYAEKAKDLAGWVKKEKQNGIIVGFIGGPPCPDFSIAGKNKGKDGENGKLSQSYVDLICKNQPDFFVFENVKGLYRTAKHREFFNALKRQLSDFGYVCTEKLINAIEYGVPQDRERIILVGFLSQHVDALQKFDWDAHISFPDALEKDWPTTEEVGRVVSQPANIYPELTVQYWFNRNGVDTHPNASKHFQPRAGLEKFQTIS... | Function: A methylase that recognizes the double-stranded sequence 5'-RCCGGB-3', methylates C-2 on both strands, and protects the DNA from cleavage by the NmeDI endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
S... |
Q9P786 | MSNTNKSEPNHSCKVVYASRVAETFVEQLKQHVNLFEFAPKLVGFLSNSDPAARMYADWTNKTCTEIGFQYELREVPKDDLEDAIVEANNDPSVNGIMIYFPVFNDGQDQYLQQVVSPDKDVEGLCHKYVMNMYHNIRHLDPEKTKKSILPCTPLAIVKILEYLGVYNKIINYGNRLYGKTITIVNRSEIVGRPLAALLANDGAKVYSVDIHNVQCFTRGAGIRSKKHDVADTNFKLEDVAPISDVIICGVPSANYKFPSNLVRDGAVCICFSSEKNFDAASLKEHAGIYVPSIGKVTIAMLLRNLIRLTSYQLNKPVDI | Function: Catalyzes oxidation of cytoplasmic one-carbon units for purine biosynthesis.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NAD(+) = 5,10-methenyltetrahydrofolate + NADH
Sequence Mass (Da): 35814
Sequence Length: 320
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcell... |
Q02046 | MSKPGRTILASKVAETFNTEIINNVEEYKKTHNGQGPLLVGFLANNDPAAKMYATWTQKTSESMGFRYDLRVIEDKDFLEEAIIQANGDDSVNGIMVYFPVFGNAQDQYLQQVVCKEKDVEGLNHVYYQNLYHNVRYLDKENRLKSILPCTPLAIVKILEFLKIYNNLLPEGNRLYGKKCIVINRSEIVGRPLAALLANDGATVYSVDVNNIQKFTRGESLKLNKHHVEDLGEYSEDLLKKCSLDSDVVITGVPSENYKFPTEYIKEGAVCINFACTKNFSDDVKEKASLYVPMTGKVTIAMLLRNMLRLVRNVELSKEK | Function: Catalyzes oxidation of cytoplasmic one-carbon units for purine biosynthesis.
PTM: The N-terminus is blocked.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NAD(+) = 5,10-methenyltetrahydrofolate + NADH
Sequence Mass (Da): 36240
Sequence Length: 320
Subcellular Location: Cytoplasm
EC: 1.5.1... |
Q9I6B7 | MLRSLFRRLFKYLLWFMAASVVLVAVLRWVPPPGTMVMVERKVGSWVDGQPIDLQRDWRSWEQLPDSLKVAVIAGEDQHFAEHHGFDLPAIQQALAHNERGGSIRGASTLSQQVAKNVFLWSGRSWLRKGLEAWFTLLIETLWTKQRILEVYLNSAEWGPGVFGAQAAARYHFGLDAERLSRTQASQLAAVLPSPLKWSAARPGPYVRQRAAWIRQQMWQLGGDDYLLRLER | Function: Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-c... |
Q88CS3 | MLSTLIRRLSRALLWFVAGSIVLVLVFRWVPPPGTALMVERKVQSWVNGEPIDLQRDWEPWENISDELKVAVIAGEDQKFASHWGFDLPAIQAALAHNERGGNIRGASTLTQQVAKNLFLWSGRSWFRKGLEAWFTALIELFWSKERILEVYLNSAEWGKGVFGAQAAARYHFGVDASRLSRQQAAQLAAVLPSPIKWSASRPSAYVASRAGWIRRQMSQLGGPSYLMQLDSSRKL | Function: Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-c... |
Q88AF9 | MLQIILRRLMKALLWFAAGSALVVLVLRWVPPPGTALMVERKVESWFDGEPIDLQRDWEPWDKISNNLKIAVIAGEDQKFAEHWGFDVDAIQAAILHNEQGGSIRGASTLSQQVSKNLFLWSGRSYLRKGLEAWFTMLIELLWSKERILEVYLNSVEWDEGIFGAQAAAQHHFRTNASALSEQQASYLAAVLPNPRQWSASHPSGYVSRRAGWIRQQMRQLGGDEYLQGLNSSRRW | Function: Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-c... |
Q2K330 | MPARRRWFENRPVLKRIVLAVLALVVLPYVLIFFYLLPFIHPVSTLMLRDLVLLRGYDRRWVSLDEISPVLVQSVMMSEDGQYCFHGGVDWAEMRMLVEDTLKGQATRGGSTIPMQTAKNLFLWNSRSFVRKAMELPLAVSTDFVLSKRRLMEIYLNIAEWGPGIYGIEAAAQHHFKVPASKLTRRQASLLAVSLPNPIDRKAGKPGRGLRRLAGVIERRAQGSGEYIKCIYE | Function: Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-c... |
Q8NJJ1 | MGKKAIQFGGGNIGRGFVAEFLHKAGYEVVFVDVMDKMVEALQQNKSYKVTEVSEEGEHTTTITNYRAINSKTHESDVIQEIATADVVTCAVGPHILKFIAPVIAKGIDARTESKPVAVIACENAIGATDTLHGFIKQHTSQDRVESLYDRAQFANSAIDRIVPQQAPNSGLDVRIEKFYEWAVEKTPFGSVGHPDIPAIHWVDNLEPYIERKLFTVNTSHATTAYFGHFRGKKMIADALEDEEIRGLVHKVLEETASLIVAKHDISEEEQKEYVKKIVSRISNPYLEDKVERVGRAPLRKLSRKERFIGPASQLAERGM... | Function: Catalyzes the NAD(H)-dependent interconversion of D-fructose 6-phosphate and D-mannitol 1-phosphate in the mannitol metabolic pathway. Has a strong preference for NADH over NADPH. Required for protection of conidiospores against exogenous stresses such as high temperatures and an oxidative environment.
Cataly... |
Q2UIM3 | MTLQAIKYSGGKLAIIDQLQLPHVEKYVTIHTSEEGWHAIKEMRVRGAPAIAIVAALALASELTTLIARNQLSSNAIETQTFITEKLHYLVSSRPTAVNLSDAAGKLETIVAESVKMPESTGHAVATAFIQAAEAMLAKDVEDNRMIGEYGAKWISENALSKNFTKATVLTHCNTGSLATAGFGTALGVIRALSSTDTLRHAYCTETRPYNQGSRLTAFELVHDRIPATLITDSMAAALLARAEIGVDAIVVGADRVAANGDTANKIGTYGLAVLAKYHGVKFLVAAPLTTIDLVTKSGNEITIEERPASEVTTVRGTCE... | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 40449
Sequence Length: 381
Pathway: Amino-acid biosynthesis; L-met... |
Q0CFY3 | MTLQAIKYNNGDLAIIDQLQLPHVEKYVTIHNSEEGWHAIKDMRVRGAPAIAIVAALALASELHGLMAHDKLSPEAEDVQTFVVEKLRYLVSSRPTAVNLSDAARKLEVVVAQSARAPGATGKTVATAFIQAAEEMLVKDVEDNKKIGEHGAQWILKNSLEGHGKATVLTHCNTGSLATSGYGTALGVIRSLASADSLQHAYCTETRPYNQGSRLTAFELVHDALPATLITDSMAAALLASKKAGVNAIVVGADRVAANGDTANKIGTYGLAVLAKYHNVKFLVAAPLTTIDLNTKSGDQIVIEERLASEVTSIRGPRDN... | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 40070
Sequence Length: 377
Pathway: Amino-acid biosynthesis; L-met... |
O31662 | MTHSFAVPRSVEWKETAITILNQQKLPDETEYLELTTKEDVFDAIVTLKVRGAPAIGITAAFGLALAAKDIETDNVTEFRRRLEDIKQYLNSSRPTAINLSWALERLSHSVENAISVNEAKTNLVHEAIQIQVEDEETCRLIGQNALQLFKKGDRIMTICNAGSIATSRYGTALAPFYLAKQKDLGLHIYACETRPVLQGSRLTAWELMQGGIDVTLITDSMAAHTMKEKQISAVIVGADRIAKNGDTANKIGTYGLAILANAFDIPFFVAAPLSTFDTKVKCGADIPIEERDPEEVRQISGVRTAPSNVPVFNPAFDIT... | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 38860
Sequence Length: 353
Pathway: Amino-acid biosynthesis; L-met... |
Q2NL31 | MTLEAIRYSRGSLQILDQLLLPQQSRYEAVGSVRQAWEAIRAMKVRGAPAIALVGCLSLAVELQAGAGGPGLAALVAFVQDALSFLVTARPTAVNMARAARDLADLAAQEAEREGATEEAVRERVICWAEDMLDKDLRDNRSIGDLGAHHLLKRAAPQGGKVTVLTHCNTGALATAGYGTALGVIRSLHNLGRLEHAFCTETRPYNQGARLTAFELVYEQIPATLIADSMAAAAMAHQGVSAVVVGADRVVANGDTANKVGTYQLAIAAKHHGIPFYVAAPSSSCDLRLETGREIVIEERPDQELTDVNGVRIAAPGIGV... | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 37826
Sequence Length: 358
Pathway: Amino-acid biosynthesis; L-met... |
Q0ITU1 | MGELGALQSIVYHRGSLRLLDQRKLPLEVDYIDVKCSGDGWNAIRDMVVRGAPAIAIAAALALAVEVSGLEDFTGTPAEAAVFVSEKLEYLVSSRPTAVNLSDAATKLRSLVSRTAETEKDAKAIFQAYIDAAETMLVDDVSDNKAIGSHGAEFLKQKLEVSKDISVLTHCNTGSLATAGYGTALGVIRALHSGGILEKAFCTETRPFNQGSRLTAFELVHDKVPATLIADSAAAALMKSGCIQAVIVGADRIAANGDTANKIGTYNLAISAKHHGVQFYVAAPITSIDLSLPSGEQIVIEERSPNELLNSEGGLGKQVA... | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 39508
Sequence Length: 374
Pathway: Amino-acid biosynthesis; L-met... |
A4S068 | MSSLEAIRYARGNLELLDQLALPLETKYIDVRDCNACWRCIKDMNVRGAPAIAIAAALALAVELEAKRGTLTTCEAAEAFVRERFDHMYTSRPTAVNLGEAKNRIQALAKRLSESGDVSGMIEGVIEGCEAMHAEDVASCRAIGDKGAAALLRACGAKDGENIKVMTCCNTGSLATAGYGTALGVIRALWESGRLERAYCLETRPYNQGSRLTAYELVYEKIPGTLICDNMAAALMARGDVDAIVVGADRVAANGDFANKIGTYSLAVNAKHHGVPMFTAAPVTTLDPETATGADIHIEERPGEEVTHSLGKRVAAEGID... | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 38658
Sequence Length: 365
Pathway: Amino-acid biosynthesis; L-met... |
C1G9Q3 | MPLIAISYSHGKLSILNQLFLPHQTTYDPIYSACDAWHAIHDMRVRGAPAIAIVAALSLAVELYDLIQKGKLSDQAKEVEIFIREKLEYIASSRPTAVNLVEAAGRLGKIVVARSCGEGVTGREVAEEYIRAAEKMLEDDVKDNRGIGEFGAKWIMKQAIDGAEGKGKVAVLTHCNTGSLATAGYGTALGVIRSLHAANSLKHAYCTETRPYNQGSRLTAYELVHDNIPATLITDSMAAALLAHKSAGVGAIVVGADRVAANGDTANKIGTYGLAVLAKHHGVKFLVAAPRTTIDMNTKSGEGIAIEERPRQEMTRIRGP... | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 40893
Sequence Length: 382
Pathway: Amino-acid biosynthesis; L-met... |
A6LE92 | MRFNEQADGVIILDQTLLPGKEAYLTLTTAEEIWDAIYKLKVRGAPAIGVAAAYGIYVCARRIDTAEKSVFVNEFRKIKEYLAGSRPTAVNLVAALNRMERVLVAHPTLSVPEWKELLYKEAIAIREEDAAACRQIGENCLELLRPGMGILTHCNAGHLAVSEYGTALAPIYLGQERGYGFKVFADETRPLLQGARLTAYELSRAGVDVTLICDNMASVVMRKGWVHAVVVGCDRVAANGDVANKIGTSGVAILARHYKIPFYVLGPTSTIDGSCPDGDSIVIEERNPDEVTEMWYSRRMAPKDVKVYNPAFDITPHELI... | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 36938
Sequence Length: 335
Pathway: Amino-acid biosynthesis; L-met... |
Q7U4V1 | MTLPPSLRWTGDHLELLDQRRLPEEVSFLKLHQWRDVAEAIATMAVRGAPAIGVAAAWGVVLAAQANEDLDLAVSVLKSSRPTAVNLGWALDRIKASPAAQEPVDPQGLAAVAAALEADDRARTQTLVDHGVGLLASGSRVLHHCHTGAIATAGVGTALGVIAAGHARGVVRHAWLDETRPRLQGAALSAWELGCLGVPCTVIVDGASGLLMRRQEVDAVLVGCDRVAANGDVANKVGTYNLALVARAHGIPFYVCAPGSSMDRSTSDGDAITIEERPQEEITQHRGQRLAAPGAAAWNPAFDITPAHLVTALITEFGVI... | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 35488
Sequence Length: 337
Pathway: Amino-acid biosynthesis; L-met... |
A5D1G8 | MLDTMRWTGDGLLELLDQTRLPFEKSYIKCTEYTDVAEAIKRLAVRGAPAIGAAAAYGLVLAARKIRANTKKEFLTELEARARELAATRPTAVNLHWALNRMLRKMRLAEPEDAGLLCDLLLEEAQAIFREDITGNRRMARYGLELIPEGARILTHCNAGALATAGYGTALGLVRAAHEAGRRVSVYAGETRPLLQGARLTAWEMLQEGIPVTLITDSMAGYLLAKGKADLVVVGADRIAANGDVANKIGTYSLAVLAREHKIPFYVAAPVSTIDLSLASGEEIPIEERDSSEVTHLAGRPVAPEGVNVWNPAFDVTPAR... | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 39529
Sequence Length: 364
Pathway: Amino-acid biosynthesis; L-met... |
C0QUC0 | MRKIKDIRPIQLKDHKLYVINQLKLPKEKEWLELSTYQQVAEAIEKMIIRGAPLIGIVGAYGFAIGVKQILDEGRSLDDVRDVFDRLKNTRPTAVNLFWALERVWKKFERWTEEGRSGEELVNLLFKEAERIDLEDYHANKAIGGYGQVLLPERCNVLTHCNTGALATSGWGTALGVIRSAFENGKDITVYVDETRPYLQGSRLTAWELVEEGIPHYLITDNSAGFLMSKGIIDAIIVGADRITANGDVANKIGTYTLAVLAEAHGIPFYVAAPTSTFDLDTDSGKDIPIEERSQLEVKKCGGCDIAPEETEALNYSFDV... | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 39383
Sequence Length: 353
Pathway: Amino-acid biosynthesis; L-met... |
B2AML6 | MATLQAIKYSRGKLLVLDQLRLPHENHYDEVSTAEEAFDCIRSMRVRGAPAIAIVAALAHAVELHNGDCTATEPEEVIAHIEKRLDYLKESRPTAVDLSNAITLLKLATRAANLEGLAHPEAKEAILNTYIQTAEEILAKDLHNNTSIGSYGTAWLQQQYSASSEKPISVLTHCNTGSLATSGHGTALGIIRTLHSEGLLKHAYCTETRPYNQGSRLTSFELVFEGIPSTLITDSMAGALFNLHRERMNIGAVIVGADRVVRNGDTANKIGTYQLAVLARHHGVKFVVAAPTTSIDLETGNGSAIEIEERKREELTQISG... | Function: Catalyzes the interconversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P).
Catalytic Activity: S-methyl-5-thio-alpha-D-ribose 1-phosphate = S-methyl-5-thio-D-ribulose 1-phosphate
Sequence Mass (Da): 42785
Sequence Length: 395
Pathway: Amino-acid biosynthesis; L-met... |
A7MK09 | MSKESQLEALVAACHWIGAKGWAPATGGNMSLREDARWCWLSESGKDKGSLTTDDFLQVDIATNLAPSGRKPSAETGLHTLIYRLFPEANCVLHVHTVNATVLSRVEKSDALHLSGYEMQKSLAGQITHLDDVPVAIFDNDQDIDALAERIARHHRQFPLRYGFLLRGHGLTCWGSDVAVARRHLEGLEFLFECEMQRRLLERA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Catalytic Activity: S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O
Sequence Mass (Da): 22791
Se... |
Q66I75 | MSSVVNAAYAEYNGKEKGDQEDPRVLIPQLCRLFYELGWVTGTGGGISLRHGEHIYIAPSGVQKERIQPEDLFVCDIDEKDISCPPPQKKLKKSQCTPPFMNAYTMRGAQAVIHTHSKSAVMATLLFPGKEFRITHQEMIKGIRKGNSGTNFRYDDTLVVPIIENTPEEKDLKERMARAMDMYPDSCAVLVRRHGVYVWGETWEKAKTMCECYDYLFDIAVQMKQSGLDPSAFPTEEKGIV | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). Functions in the methionine salvage pathway. May play a role in apoptosis.
Catalytic Activity: S-methyl-5-thio-D-ribulose 1-phosphate = 5-... |
Q54NY7 | MSNFDSEHPRVLIPELCKLFYGNGWVTGTGGGISIKRDKEIYIAASGVQKERILGEDIFVMDENENEISTPPTEKKLKASQCTPLFFNAYKYRDAGAVIHTHSQHAVMVTLLYQTEFIITHQEMIKGILSGHGENAKYLQYFDRLVIPIIENTPHERDLKERMHKAMEKYPNANAVLVRRHGVYVWGPDWVKAKTMCECFDYLFEIAIKMKQMGLDPTEVPHANEECCYDC | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Catalytic Activity: S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O
Sequence Mass (Da): 26521
Se... |
B4M1W5 | MALSIFKDLPGEHPRNLIPSLCRQFYHLGWVTGTGGGMSIKYNNEIYIAPSGVQKERMQPEDLFVQDIDGKDLQLPPEIKGLSKSQCTPLFMLAYRHRNAGAVIHTHSQHAVMATLLWPGKTFRCTHLEMIKGVYDEADKRYLRYDEQLVVPIIENTPFERDLADSMYAAMMEYPGCSAVLVRRHGVYVWGQTWEKTKTMSECYDYLFSIAVQMKQAGLDPEKFENALQA | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P).
Catalytic Activity: S-methyl-5-thio-D-ribulose 1-phosphate = 5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O
Sequence Mass (Da): 26284
Se... |
Q8EKK8 | MGIRAIVVDTAGTTTDLTFIQDVLFPYSVKALPDFLAQNQHNVLVENCICDTRDIALEPDADLNRVTEILQQWVREDRKATPLKTLQGLIWKQGYAHDEFKGHIFPDFIEAVKRFSAQNLRIYSFSSGSVDAQKLLFSHSDGGDLTEMFNGHFDTRTGNKLDKQAYCNILNTISLSPKQVLFVSDVIEELKAADAAGMMTCQMVRDSKQRTGDFRTINSFDKLVIE | Cofactor: Binds 1 Mg(2+) ion per subunit.
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... |
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