ids
stringlengths 6
10
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stringlengths 11
1.02k
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stringlengths 108
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P59436 | MIIRFILSFFTSLLLMLIFGPHLINWLNKYKIQQIIRNFGPKSHFNKKNTPTMGGILIIFSIIISTIIWTKLSNPYVWLTLTILIGYGIIGFIDDNMKIYYKNSKGLSSLHKFSLLSILACIIIFLIYYIINDHSTIKLIVPFSKNIIFNTKMICILISYFAIIGTSNAVNLTDGLDGLAIVPIIFVTTNLSIISFISGNVNLSYYFNTIYIPYSNELTIICAAIIGSSLGFLWFNTYPAQIFMGDVGSLSLGGTIGIISVLLRQEILLIIVGGLFVIETLSVIIQVLYYKITKKKLFKMTPIHHHYELNGCPETRLIIRFWIISFILMLLGLLMLKVHQ | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Catalytic Activity: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38570
Sequence Length: 340
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell membrane
EC: 2.7.8.13
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O25235 | MLYSLLYGYFNINLFQYLTFRAGLGFFIAFFLTLFLMPKFILWAKAKKANQPISSFVPSHQNKKDTPTMGGIVFVFATIVASVLCASLGNLYVLLGLIVLVGFSFVGFRDDYTKINQQSNAGMSAKMKFGMLFILSLIVSVLLSLKGLDTFLYAPFLKNPLFEMPTMLAVGFWVLVFLSTSNAVNLTDGLDGLASVPSIFTLLSLSIFVYVAGNAEFSKYLLYPKVIDVGELFVVSLALVGSLFGFLWYNCNPASVFMGDSGSLALGGFIAYNAIVSHNEILLVLMGSIFVIETLSVILQVGSYKTRKKRLFLMAPIHHHFEQKGWAENKVIVRFWIISMLSNLVALLSLKVR | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Catalytic Activity: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39170
Sequence Length: 353
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.7.8.13
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Q0BXT9 | MLYELLAADSGLFNLLNYITFRTGAAVVTAFLVTVLFGDMLINFLRARQGKGQPIRDLSLEMQLSKQGTPTMGGFLIWLGLIVGVALWGNLQNPYVWVTLFVTFSYAILGFLDDYAKVTKQSTDGVSAGARLIAGFGIAALACAIIMGLHGAHTPAGHAEWGPFNPLAEWIAGFAPQTSVEPADPNFSGGVAVPFVNNYFLPLGGFFILFGMIVIVGAANAVNFTDGLDGLAIVPMTFAAAAYAMIAYLTGNFVFASYLGIQFAPGAGELAVLLGALIGSGMGFLWYNAYPAKVFMGDTGSLGLGGMLGVVAVATKHEFALVVIGGLFVIEAVSVLTQIGWFKITKRLTGEGKRIFLMAPLHHHFQKKNWPETRVVVRFWILSVLFALAGLATLKLR | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Catalytic Activity: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42416
Sequence Length: 397
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.7.8.13
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A8GP69 | MLYNLLLPHIHNSHIANLFHYITFRSGLAIIITLSLSFIMGPILIKFLRSLQKNGQPIRSDGPESHQTKAGTPTMGGIMIILSSGLSTLLLADLTNQYIWITLFGFISFGIIGFMDDYAKVTKNNHYGVRGKSKLVLQGIISLIICVLLEYLDKNPSHLLNVPFFKNLNLDLGYFYIVFAIFVIVGSSNAVNLTDGLDGLATVPIAFTAGSFALISYLVGNLIYSHYLQLTYIPNTGELTVLCAGLVGSCLGFLWFNAQPAEVFMGDTGSLSLGGVLGIISVITKHEIVLAIVGGLFVIETASVILQVYYFKATQGKRIFKMAPLHHHFEKHGWAESKVVIRFWIISVIFALIGLSSLKLR | Function: Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I.
Catalytic Activity: di-trans,octa-cis-undecaprenyl phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine = di-trans-octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39700
Sequence Length: 361
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.7.8.13
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Q8TDS7 | MNQTLNSSGTVESALNYSRGSTVHTAYLVLSSLAMFTCLCGMAGNSMVIWLLGFRMHRNPFCIYILNLAAADLLFLFSMASTLSLETQPLVNTTDKVHELMKRLMYFAYTVGLSLLTAISTQRCLSVLFPIWFKCHRPRHLSAWVCGLLWTLCLLMNGLTSSFCSKFLKFNEDRCFRVDMVQAALIMGVLTPVMTLSSLTLFVWVRRSSQQWRRQPTRLFVVVLASVLVFLICSLPLSIYWFVLYWLSLPPEMQVLCFSLSRLSSSVSSSANPVIYFLVGSRRSHRLPTRSLGTVLQQALREEPELEGGETPTVGTNEMGA | Function: May regulate nociceptor function and/or development, including the sensation or modulation of pain. Functions as a specific membrane receptor for beta-alanine. Beta-alanine at micromolar doses specifically evoked Ca(2+) influx in cells expressing the receptor. Beta-alanine decreases forskolin-stimulated cAMP production in cells expressing the receptor, suggesting that the receptor couples with G-protein G(q) and G(i).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36118
Sequence Length: 321
Subcellular Location: Cell membrane
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Q91ZB8 | MNSTLDSSPAPGLTISPTMDLVTWIYFSVTFLAMATCVGGMAGNSLVIWLLSCNGMQRSPFCVYVLNLAVADFLFLFCMASMLSLETGPLLIVNISAKIYEGMRRIKYFAYTAGLSLLTAISTQRCLSVLFPIWYKCHRPRHLSSVVSGALWALAFLMNFLASFFCVQFWHPNKHQCFKVDIVFNSLILGIFMPVMILTSTILFIRVRKNSLMQRRRPRRLYVVILTSILVFLTCSLPLGINWFLLYWVDVKRDVRLLYSCVSRFSSSLSSSANPVIYFLVGSQKSHRLQESLGAVLGRALRDEPEPEGRETPSTCTNDGV | Function: May regulate nociceptor function and/or development, including the sensation or modulation of pain. Functions as a specific membrane receptor for beta-alanine. The receptor couples with G-protein G(q) and G(i) (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36126
Sequence Length: 321
Subcellular Location: Cell membrane
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Q86SM8 | MMEPREAGQHVGAANGAQEDVAFNLIILSLTEGLGLGGLLGNGAVLWLLSSNVYRNPFAIYLLDVACADLIFLGCHMVAIVPDLLQGRLDFPGFVQTSLATLRFFCYIVGLSLLAAVSVEQCLAALFPAWYSCRRPRHLTTCVCALTWALCLLLHLLLSGACTQFFGEPSRHLCRTLWLVAAVLLALLCCTMCGASLMLLLRVERGPQRPPPRGFPGLILLTVLLFLFCGLPFGIYWLSRNLLWYIPHYFYHFSFLMAAVHCAAKPVVYFCLGSAQGRRLPLRLVLQRALGDEAELGAVRETSRRGLVDIAA | Function: Orphan receptor. May regulate nociceptor function and/or development, including the sensation or modulation of pain.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34286
Sequence Length: 312
Subcellular Location: Cell membrane
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Q91ZB7 | MTSLSVHTDSPSTQGEMAFNLTILSLTELLSLGGLLGNGVALWLLNQNVYRNPFSIYLLDVACADLIFLCCHMVAIIPELLQDQLNFPEFVHISLTMLRFFCYIVGLSLLAAISTEQCLATLFPAWYLCRRPRYLTTCVCALIWVLCLLLDLLLSGACTQFFGAPSYHLCDMLWLVVAVLLAALCCTMCVTSLLLLLRVERGPERHQPRGFPTLVLLAVLLFLFCGLPFGIFWLSKNLSWHIPLYFYHFSFFMASVHSAAKPAIYFFLGSTPGQRFREPLRLVLQRALGDEAELGAGREASQGGLVDMTV | Function: Orphan receptor. May regulate nociceptor function and/or development, including the sensation or modulation of pain.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34588
Sequence Length: 310
Subcellular Location: Cell membrane
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Q96AM1 | MAGNCSWEAHPGNRNKMCPGLSEAPELYSRGFLTIEQIAMLPPPAVMNYIFLLLCLCGLVGNGLVLWFFGFSIKRNPFSIYFLHLASADVGYLFSKAVFSILNTGGFLGTFADYIRSVCRVLGLCMFLTGVSLLPAVSAERCASVIFPAWYWRRRPKRLSAVVCALLWVLSLLVTCLHNYFCVFLGRGAPGAACRHMDIFLGILLFLLCCPLMVLPCLALILHVECRARRRQRSAKLNHVILAMVSVFLVSSIYLGIDWFLFWVFQIPAPFPEYVTDLCICINSSAKPIVYFLAGRDKSQRLWEPLRVVFQRALRDGAELGEAGGSTPNTVTMEMQCPPGNAS | Function: Orphan receptor. May bind to a neuropeptide and may regulate nociceptor function and/or development, including the sensation or modulation of pain (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38171
Sequence Length: 343
Subcellular Location: Cell membrane
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Q8VCJ6 | MAGNCSWEAHSTNQNKMCPGMSEARELYSRGFLTIEQIATLPPPAVTNYIFLLLCLCGLVGNGLVLWFFGFSIKRTPFSIYFLHLASADGMYLFSKAVIALLNMGTFLGSFPDYIRRVSRIVGLCTFFTGVSLLPAISIERCVSVIFPTWYWRRRPKRLSAGVCALLWMLSFLVTSIHNYFCMFLGHEAPGTVCRNMDIALGILLFFLFCPLMVLPCLALILHVECRARRRQRSAKLNHVVLAIVSVFLVSSIYLGIDWFLFWVFQIPAPFPEYVTDLCICINSSAKPIVYFLAGRDKSQRLWEPLRVVFQRALRDGAEPGDAASSTPNTVTMEMQCPSGNAS | Function: Orphan receptor. May bind to a neuropeptide and may regulate nociceptor function and/or development, including the sensation or modulation of pain.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38523
Sequence Length: 343
Subcellular Location: Cell membrane
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Q91ZB5 | MFSIFNIWGTFNKVLFFLSLTVSLAGLVGNALLLWHLGLHIKKGPFNTYLLHLAAADFLFLSCQVGFSIATIVSGHEDTLYFPVTFLWFAVGLWLLAAFSVDCCLAYMFPSFCSPNRRPRFTSVVLCLVIWALTMPAVLLPANACGLLKNGMSLLVCLKYHWTSVTWLAVLSGMACGASKFLLIFGNCCSSQPPPKFCKLAQCSGILLFFCRLPLVVYWCLRPVLKFLLPFFFPLATLLACIDSSAKPLLYYMKGRQLRKDPLQVALNRALGEESQSGLGGLSLPMHQV | Function: Orphan receptor. May regulate nociceptor function and/or development, including the sensation or modulation of pain.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32028
Sequence Length: 289
Subcellular Location: Cell membrane
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Q7TN39 | MLSIFNIWGTFNRVLFFLSLTVSLAGLAGNTLLLWHLGLRIKKGPFNTYLLHLAAADFLFLSCQVGFSIAKIASGYEDTLYFPVTFLWFAVGLWLLAAFIVDCCLSYMFPSFCGPNCRPRYTSFVLCLVIWALTMLAVLLPANACGLLYNRMSLLVCLKYHWVSVVWLGVLASTACGASMFLLVFGNCCSSQPPSKFCKLAQCSGILLFFCRLPLVFYWCLRPVIKFLLPFFFPLATLLACIDSSAKPLLYYLKGRQLRKEPLQVALNRALGEESQSSSGGISLPMSRV | Function: Orphan receptor. May regulate nociceptor function and/or development, including the sensation or modulation of pain.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32212
Sequence Length: 289
Subcellular Location: Cell membrane
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Q7TN38 | MEPLATTLCPQECTQTTRNETPNETTWSSEHVTKYTYISISLVICSLGLVGNGLLIWFLIFCIKRKPFTIYILHLAFADFMVLLCSSIIQLVNTFHIYDSTLVSYAVLFMIFGYNTGLHLLTAISVERCLSVLYPIWYHCRRPKHQSTVACTLLWALSVLVSGLENFFCILEVKPQFPECRYVYIFSCTLTFLVFVPLMVFSNLILFIQVCCNLKPRQPAKLYVIIMATVILFLVFAMPMKVLLIIGYYSNSTDASVWKSLPYLNMLSTINCSINPIVYFVVGSLRRKRSRKSLKEALQKVFEEKPVVASRENEVQFSLPL | Function: Orphan receptor. May regulate nociceptor function and/or development, including the sensation or modulation of pain.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36780
Sequence Length: 321
Subcellular Location: Cell membrane
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Q96LB2 | MDPTISTLDTELTPINGTEETLCYKQTLSLTVLTCIVSLVGLTGNAVVLWLLGCRMRRNAFSIYILNLAAADFLFLSGRLIYSLLSFISIPHTISKILYPVMMFSYFAGLSFLSAVSTERCLSVLWPIWYRCHRPTHLSAVVCVLLWALSLLRSILEWMLCGFLFSGADSAWCQTSDFITVAWLIFLCVVLCGSSLVLLIRILCGSRKIPLTRLYVTILLTVLVFLLCGLPFGIQFFLFLWIHVDREVLFCHVHLVSIFLSALNSSANPIIYFFVGSFRQRQNRQNLKLVLQRALQDASEVDEGGGQLPEEILELSGSRLEQ | Function: Orphan receptor. Probably involved in the function of nociceptive neurons. May regulate nociceptor function and/or development, including the sensation or modulation of pain. Potently activated by enkephalins including BAM22 (bovine adrenal medulla peptide 22) and BAM (8-22). BAM22 is the most potent compound and evoked a large and dose-dependent release of intracellular calcium in stably transfected cells. G(alpha)q proteins are involved in the calcium-signaling pathway. Activated by the antimalarial drug, chloroquine. May mediate chloroquine-induced itch, in a histamine-independent manner.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36250
Sequence Length: 322
Subcellular Location: Cell membrane
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Q8CIP3 | MDPTISSHDTESTPLNETGHPNCTPILTLSFLVLITTLVGLAGNTIVLWLLGFRMRRKAISVYILNLALADSFFLCCHFIDSLLRIIDFYGLYAHKLSKDILGNAAIIPYISGLSILSAISTERCLCVLWPIWYHCHRPRNMSAIICALIWVLSFLMGILDWFSGFLGETHHHLWKNVDFIITAFLIFLFMLLSGSSLALLLRILCGPRRKPLSRLYVTIALTVMVYLICGLPLGLYLFLLYWFGVHLHYPFCHIYQVTAVLSCVNSSANPIIYFLVGSFRQHRKHRSLKRVLKRALEDTPEEDEYTDSHLHKTTEISESRY | Function: Orphan receptor activated by neuropeptides terminating in Arg-Phe or Arg-Phe-amide. Mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. May regulate the function of nociceptive neurons by modulation of pain perception.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36810
Sequence Length: 322
Subcellular Location: Cell membrane
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Q4QXU0 | MDPTTPAWRTESTTMNGNDQALPLLCGKEILISVFLILFIALVGLVGNGFVLWLLGFRMRRNAFSVYVLSLAGADFLFLCFQIINCLVYLSNFFCSSSINFPSFFTTVMTCAYLAGLSMLSTISTERCLSVLWPIWYRCRRPRHLSAVACVLLWALSLLLSILEGKFCGLFGDGDSGWCQTFDLITAAWLIFLFMVLCGSSLALLVRILCGSRGLPLTRLYLTILLTVLVFLLCGLPFGIQWFLILWIWKNSDVLFCHIHPVSVVLSSLNSSANPIIYFFVGSFRKQWQLQQPILKLALQRALQDIAEVDHSEGCFRQGTPEMSRSSLV | Function: Mast cell-specific receptor for basic secretagogues, i.e. cationic amphiphilic drugs, as well as endo- or exogenous peptides, consisting of a basic head group and a hydrophobic core. Recognizes and binds small molecules containing a cyclized tetrahydroisoquinoline (THIQ), such as non-steroidal neuromuscular blocking drugs (NMBDs), including tubocurarine and atracurium. In response to these compounds, mediates pseudo-allergic reactions characterized by histamine release, inflammation and airway contraction.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36936
Sequence Length: 329
Subcellular Location: Cell membrane
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Q9K2S2 | MQLLHLAILSPFLFAFIIPFLAKYAKRVHTGWFVLILPVLLFIYFLPMIRMTQSGETLRSVLEWIPSLGINFTVYIDGLGLLFALLITGIGSLVTLYSIFYLSKEKEQLGPFYVYLLMFMGAMLGVVLVDNVMVLYMFWELTSLSSFLLIGYWYKREKSRYGAAKSLLITVSGGLCMLGGFILLYLITDSFSIREMVHQVQLIAGHELFIPAMILILLGAFTKSAQFPFYIWLPDAMEAPTPVSAYLHSATMVKAGIYVIARFSPIFAFSAQWFWIVSLVGLFTMVWGSFHAVKQTDLKSILAFSTVSQLGMIISMLGVSAAALHYGHTEYYTVAAMAAIFHLINHATFKGSLFMAVGIIDHETGTRDIRKLGGLMAIMPITFTISLIGTFSMAGLPPFNGFLSKEMFFTSMLRVTHFDLFNVQTWGVLFPLFAWIGSVFTFIYSMKLLFKTFRGNYQPEQLEKQAHEAPVGMLVPPVILVALAVSLFFFPNILSYSLIEPAMNSIYPTLLDGHEKFHVHISQWHGVTTELLMTAGIVVIGTIGYLSLNKWKGIYKLFPSKLTLNRLYDKLLTMMEKGSYRVTKQYMTGFLRDYLLYIFAGFIILIGGAFAIKGGFSFKTEGMAKIGVYEIILTLVMISATVATVFARSRLTAIIALGVVGYTLALFFVIFRAPDLALTQLVIETISVALFLLCFYHLPKLRLKTKTRTFRMTNFIISLGVGVIVTLLGIASSSQRTKDSIASFFVKHSHDLGGGDNVVNVILVDFRGFDTMFEITVLTIAALGIYSMIKTKVKEEGKSGE | Function: Mrp complex is a Na(+)/H(+) antiporter that is considered to be the major Na(+) excretion system in B.subtilis. Has a major role in Na(+) resistance and a minor role in Na(+)- and K(+)-dependent pH homeostasis as compared to TetB. MrpA may be the actual Na(+)/H(+) antiporter, although the six other Mrp proteins are all required for Na(+)/H(+) antiport activity and Na(+) resistance. MrpA is required for initiation of sporulation when external Na(+) concentration increases. Also transports Li(+) but not K(+), Ca(2+) or Mg(2+).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 89531
Sequence Length: 801
Subcellular Location: Cell membrane
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Q6PD99 | MGAQLTKGEATVEGKAVADKANGQENGHVKTNGDVSTKPDGEAVAADGNGTAEVAKDEAPKTEEGDGIEAAPATEAEASKSDGEAAKETKKKKKFSLKNSFKFKGISLKKNKKASEEAAEAVATPTTAEDKPEENGQAATETKEEEPAAETNETPAPEAEAEPKVEEAEPKAEEPAQQTETAPTEETTKSEESPAPVEETTPTESSDPEPAAE | Function: Involved in the control of cell movement by regulating actin cytoskeleton homeostasis and filopodium and lamellipodium formation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22094
Sequence Length: 213
Subcellular Location: Cytoplasm
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O05259 | MNEQKTNDLILQTATKLVSFIILLFSFYLFLSGHNAPGGGFVGGLITSSSIVLLLLAYDLKTVRSLLPVNFIYVAGAGLLLAVLTGVGSFVFGAPFLTHTFGYFQLPILGKTELATATIFDLGVYLVVVGITMTIIQTIGEEE | Function: Mrp complex is a Na(+)/H(+) antiporter that is considered to be the major Na(+) excretion system in B.subtilis. Has a major role in Na(+) resistance and a minor role in Na(+)- and K(+)-dependent pH homeostasis as compared to TetB. MrpA may be the actual Na(+)/H(+) antiporter, although the six other Mrp proteins are all required for Na(+)/H(+) antiport activity and Na(+) resistance. MrpA is required for initiation of sporulation when external Na(+) concentration increases. Also transports Li(+) but not K(+), Ca(2+) or Mg(2+).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15294
Sequence Length: 143
Subcellular Location: Cell membrane
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A7I339 | MSFIKEFKEFAVKGNVIDMAVGVVIGSAFGKIVSSLVGDVIMPVVGVLTGGVNFTDLKITIKEAVGENAAVTINYGNFIQVTIDFLIIAFCIFLAIKAINQLKKPEKQEPKAPAEPNDEVKLLSEIRDLLKK | 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): 14296
Sequence Length: 132
Subcellular Location: Cell inner membrane
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B0T274 | MSIVKEFREFIARGNVVDLAVGVIIGAAFNGIVKSLVDGVIMPPIGLVTGGLDFSKLQWVLKPEDPVTEAVELVAIQYGAFINTVIQFLIVAVVVFLLVKLVNHIRRADAAEPAPEAPAAPTPEERLLTEIRDLLAKPATVTAAPKAAAAPVAKPKTKPKA | 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): 17036
Sequence Length: 161
Subcellular Location: Cell inner membrane
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A9WJI9 | MIKEFREFISRGNVIDLAVGVIVGAAFTAIINSLVNDIINPLIGLLVGGRADFSNYFIPLAGQTATTLAEAQAAGPVLAYGSFLTAVINFLLIAFVVFMIVRTVNRMRSKPEAVPPAPPEPTPSERLLAEIRDLLARQG | 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): 14894
Sequence Length: 139
Subcellular Location: Cell membrane
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A1BFW8 | MLKEFKDFAVRGNVVDMAVGIIIGAAFTTIINTLVNEVVMPPIGVLLGGVDFSDFYLLLKEGSKAAPYESLAAAKSAGAVTLSYGIFVNACISFLIVTFVMFLSVKGINRLRAKEDAAPDPAVRECPFCCSPVSVKAKRCPMCTSELK | 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): 15803
Sequence Length: 148
Subcellular Location: Cell inner membrane
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Q8KD14 | MLKEFREFALKGNVVDMAVGIIIGGAFGALVNSLVNDLLMPPLGLLLKGVDFSNLFVVLKEGTPPGPYIALADAKTAGAVTLNYGLFVNALIGFLIMAFAVFLLVRSINRLRSLSEKSAAPAVAPQTKECPFCFSIIPLKAVRCPNCTSQL | 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): 16057
Sequence Length: 151
Subcellular Location: Cell inner membrane
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Q7NYB4 | MSVLKEFKEFAVKGNVIDLAVGVVIGGAFGSIVKSLVDDVIMPPIGLLIGNVDFSNLFFVLKDGAKQAGPYVSVAAAKQAGATTLNLGLFINALVSFTIVAFAIFMLVKAINRLKREEAAPAPAAPATKECRYCLSAIPEKATRCPCCTSQLD | 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): 16094
Sequence Length: 153
Subcellular Location: Cell inner membrane
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A0JZ09 | MTLIRRVAFLSLHTSPMEQPGSGDAGGMNVYVRALASALAASGVEVEIFTRSTSSGQPAVEHPDPGVCVHNVISGPPRKLPKEELPELLHSMVAEIERIRQRQPHGRYDLIHSHYWVSGVAGLELSRLWGVPLVHTMHTMAKVKNLLLQSGEKPEPRRREDGELRIVDGATRLIANTPAEAAELVSHYNADFDHIDVAPPGVDLTVFTPAFRPRSRAQLGVPAGKFHLLFAGRIQRLKGPQVLVKAAALLRSRRPDIDLQVTILGALSGAKDFDLKSLISAAGMDDVVTHHPPVNAPELAGWFRSADVVVMPSYSESFGLVALEAQACGTPVVATRVGGLSRAIFDGRTGLLVDGHKAADWADVLEALYDDPATRGDMGRAAALHAQGFGWQRTAAITLESYHAAVDQYIDSHRIPVGHSP | Function: Catalyzes the transfer of a N-acetyl-glucosamine moiety to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2-deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis pathway.
Catalytic Activity: 1D-myo-inositol 3-phosphate + UDP-N-acetyl-alpha-D-glucosamine = 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside 3-phosphate + H(+) + UDP
Sequence Mass (Da): 45443
Sequence Length: 421
EC: 2.4.1.250
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Q8FSH1 | MRVAMISMHTSPLQQPGVGDSGGMNVYILSTGTELARQGVEVDIFTRATRPSQGEVVQVAPNLRVINIVAGPYEGLAKEELSTQLAAFAGGVLEFTRRGGIEYDLIHSHYWLSGQVGWLMRDLWRIPLVHTAHTLAAVKNSYRADEDTPESEARRICEQQLVDNADVLAVNTQEELADLVHHYDADPDRISVVSPGADIALYTPGNDRATERSRRELGVPLHAKVVAFVGRLQPFKGPQVLIHAVAELLERDPQRNLRVLICGGPSGPSATPETYRNLAVELGVDKRIRFLDPRPPEELVAVYRAADIIAVPSYNESFGLVAMEAQATGTPVVAARVGGLPVAVAEGETGLLVDGHDPALWADTLATLLDDDETRIRMGQDAVEHARNFSWAATATQLSSLYSEATTAECDGGIPRRADGARWD | Function: Catalyzes the transfer of a N-acetyl-glucosamine moiety to 1D-myo-inositol 3-phosphate to produce 1D-myo-inositol 2-acetamido-2-deoxy-glucopyranoside 3-phosphate in the mycothiol biosynthesis pathway.
Catalytic Activity: 1D-myo-inositol 3-phosphate + UDP-N-acetyl-alpha-D-glucosamine = 1D-myo-inositol 2-acetamido-2-deoxy-alpha-D-glucopyranoside 3-phosphate + H(+) + UDP
Sequence Mass (Da): 46017
Sequence Length: 424
EC: 2.4.1.250
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D2B7W7 | MNARVEHRGRLDEREVAAVLTVVEAATEADGVRPLNEHVMLHLRYGGDERAGAVLLYVGDDLAGYAHVDPTDPVEGPSGELVIHPAFRGQGHGRHLLEAVLDRTGGRLRLWAHGGHPGAEALALSTGFTKIRSLWQMRRSLFAAIPGFELPDGVRLRTFAPGSPDEEAWVALNAKAFAHHPEQGSWTLEDLKRREQEPWFDPAGFFLAERPTGSGDGDVADGGSTDGGPADSGSADGGAGEGGTGDGNRLIGFHWTKVHGDGGHGHEPIGEVYVVGVDPAEQGGGLGRSLTLAGLSHLRARGLAQVMLYVDESNTAAIRLYEKLGFTRWDVDVMYRK | 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): 36078
Sequence Length: 337
EC: 2.3.1.189
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D1A4F4 | MDERALVFSDGLTDPQISQVLALAEAATRHDGVAPLSEQALLTLRAGRSRSLLSLEDGVIAGYAHLDPAPDGAGASGEVVVHPGRRRRGHGRALLRALRERARGPLRVWAHGDLAPAAALAAAEGMARVRVLLQMRRPLQDSPLPEVTVPDGVTIRTFEPGRDETAWLRVNGRAFADHPEQGAWTLEDLRARQAEPWFDPAGLFLAERDGRLIGFHWTKVHPDPIGEVYVVGVDPSAQGLGLGRVLTLIGLHHLRDRGLPAVMLYVDESNRPALRLYESLGFTRYAVDVMYQSPPPH | 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): 32430
Sequence Length: 297
EC: 2.3.1.189
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D5UXA4 | MAEVVHGPVADPGAVLALVAEAQAADGIGPLSEQFRLGVAGPGPHVVAEGGYAGIVIPPAGGPGAVEAVVAPSHRGRGLGRELVATALDVAGAGATVWAHGDLTPARAVAARLGLTPVRTLLNLRRPLADLDPAPSAPDGVTVRTYAGPADDTALLAVNNAAFAWHPEQGGWGPEQIAERTGADWFDPAGLFLAIGSGSGSDEADGRLLGFHWTKVADPATGLGEVYVVAVAPEGQGRGLGRLLTSVGLHYLADRKLDTVELYVEGDNAAALHTYTKLGFSEHERHVAYAHS | 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): 29798
Sequence Length: 292
EC: 2.3.1.189
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D1BV84 | MPVPLQIGPLGPSDVEGVRGLARAAETADGVAPLSEQPLLRLSSDEGWLTHVVARSKAGQVIGYAQVDRGGEDASAELVVHPEHRRAGVGGLLLRTAERDATLPQFGGTAGHHGKRLRVWAHGNLEPARAFAAAAGYVVVRELLFLTKPFPPVVAPVEPTPPVTEPVEPAPPVVEPVEPAPPVVEPVETTSASTSGVVSTGSTTGGGSTTGGGYRVRAFVPGVDDDAWVALNARAFAAHPEQGRLTVADLHDRMAEPWFDPAGFFLAEAPDGTLAGSLWTKVEGDDGEIYAVGVDPAHQGRGLGATLTAVGLDHLATRARRATLYVDGDNAAALATYARAGFVPTAVDVQYGKATGGTPVPRALPSR | 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): 37960
Sequence Length: 367
EC: 2.3.1.189
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B2DEV1 | MDHATRAHFTMTVGEVDPLLADALASERGRQQNQIELIASENIVSRAVLDALGHEITNKTLEGYPGNRFHGGGQFVDIAEQAAIDRAKQLFNCGYANVQPHSGTQANLAVFFLLLKPGEKVLSLDLAAGGHLSHGMKANLSGRWFDATNYNVNPQNEVIDLDEMERLAEEIRPKLLITGGSAYPRELDFERMSRIAKKVGAYFLVDMAHIAGLVAGGVHPSPFPHADIVTCTTTKTLRGPRGGLILTNNEEWYKKLQAAVFPGVQGSLHSNVLAAKAICLGEAMLDDFKVYARQVVANAKVLANTLAERGVRIVSGGTDTHIVLLDLASKGLLGKQAETLLAKANITSNKNPIPGDSPRPPEWVGMRLGSSAATTRGLKEAEFRVLGTVIADLIDAEVAGKADDVVEGAKAKIAELTNTFPVYGQ | Function: Catalyzes the reversible interconversion of alpha-methyl-L-serine to D-alanine with tetrahydrofolate (THF) serving as the one-carbon carrier. Cannot use alpha-methyl-D-serine, L-serine, D-serine or L-alanine.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + D-alanine + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-methylserine
Sequence Mass (Da): 45600
Sequence Length: 425
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.7
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B2DEU7 | MNELTRTFFNSSVHDTDPLIAQALDDERARQKNQIELIASENIVSQAVLDALGHEMTNKTLEGYPGNRFHGGGQFVDVVEQAAIDRAKQLFNCGYANVQPHSGTQANLAVFFLLVKPGDRILSLDLAAGGHLSHGMKGNLSGRWFEAHNYNVDPQNEVINYDEMERIAEEVKPKLLITGGSAYPRELDFARMAQIAKKVGAFFMVDMAHIAGLVAGGAHPSPFPHADIVTCTTTKTLRGPRGGLILTNNEEWYKKLQTAVFPGVQGSLHSNVLAAKAICLGEALRPEFRDYVAQVVKNAKVLAETLTSRGIRIVSGGTDTHIVLLDLSSKGLNGKQAEDALARANITSNKNPIPNDSPRPAEWVGMRLGVSAATTRGMKEDEFRKLGNVVADLLEAESAGNGPEAAEKAKVTVRELTEAFPVYAH | Function: Catalyzes the reversible interconversion of alpha-methyl-L-serine to D-alanine with tetrahydrofolate (THF) serving as the one-carbon carrier. Cannot use alpha-methyl-D-serine, L-serine, D-serine or L-alanine.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + D-alanine + H2O = (6S)-5,6,7,8-tetrahydrofolate + 2-methylserine
Sequence Mass (Da): 46056
Sequence Length: 425
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Cytoplasm
EC: 2.1.2.7
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P13827 | MKIIFFLCSFLFFIINTQCVTHESYQELVKKLEALEDAVLTGYSLFQKEKMVLNEGTSGTAVTTSTPGSKGSVASGGSGGSVASGGSVASGGSGNSRRTNPSDNSSDSDAKSYADLKHRVRNYLLTIKELKYPQLFDLTNHMLTLCDNIHGFKYLIDGYEEINELLYKLNFYFDLLRAKLNDVCANDYCQIPFNLKIRANELDVLKKLVFGYRKPLDNIKDNVGKMEDYIKKK | PTM: Merozoite surface antigen contain the sequence of 83 kDa, 42 kDa and 19 kDa antigens which are the major surface antigens of merozoites. The maturation take place during schizont.
Location Topology: Lipid-anchor
Sequence Mass (Da): 26051
Sequence Length: 233
Subcellular Location: Cell membrane
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P13820 | MKIIFFLCSFLFFIINTQCVTHESYQELVKKLEALEDAVLTGYSLFQKEKMVLNEEEITTKGASAQSGASAQSGASAQSGASAQSGTSGPSGPSGTSPSSRSNTLPRSNTSSGASPPADASDSDAKSYADLKHRVRNYLFTIKQLKYPESLDLPNHMLTLCDNIHGFKYLIDGYEEINELLYKLNFYFSLLRAKLNDVCANDYCQIPFNLKIRANELDVLKKLVFGYRKPLDNIKDNVGKMEDYIKKNKTTIANINELIEGSKKTIDQNKNADNEEGKKKI | PTM: Merozoite surface antigen contain the sequence of 83 kDa, 42 kDa and 19 kDa antigens which are the major surface antigens of merozoites. The maturation take place during schizont.
Location Topology: Lipid-anchor
Sequence Mass (Da): 31226
Sequence Length: 281
Subcellular Location: Cell membrane
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P87320 | MGISWFLSRFRIRTVAPSSFLKPRGLVYRPSQIRRRVSLLSLSGFHPYRAYSILGPKTPTAFNSANTVRFFSFSSISRLVFRSLRLPVAGFSLVAGGAAYIGAQVQRASDYTKDIFDKTFGILDSTWEKTRETVASVTNVQLPEISMPLWLEKILRLDEESAERRRVLQAERAKEHRSNSNDKQKSSDNDEDPNDTTVGIGAALAASILSVDSVDGEDTLTADEKRKLAQESKEDRMMLFTKKMIEIRNILQDIQDNNSAVTLPSIVVIGSQSSGKSSVLEAIVGHEFLPKGSNMVTRRPIELTLVHSADTAIPYGEFSGVQLGKITDFSKIQHILTDLNMAVPSSQGVDDNPIRLTIYASHIPNLSLIDLPGYIQIHSEDQPADLDMKISKLCEKYIREPNIILAVCAADVDLANSAALRASRRVDPLGLRTIGVVTKMDLVPPSKAISILHNNNYPLHYGYIGVISRIVPTGRFSAGQNLTDLVSTQENSYFSTHQQFADARIGNYLGIQSLRKCLINVLEYTMSKNLQHTADSIRTELEECNYQYKVQYNDRVLTADSYIAEGLDIFKAAFKEFTQKFGKSEVRDLLKSSLNEKVMDLLAERYWTDDDISNWSKHTNALDEHWKYKLDSCVSTLTRMGLGRVSTLLVTDSISKCIDEITKASPFADHPAAMQYIMNAAQDILRRRFHATSEQVENCVKPYKYDVEVNDDEWKSSRGQAEKLLQRELGLCQSALEKIKNAVGSRRMNQVLQYLEEQKTSSEPLPASYSTALLEQGRMLQYLKMREDILKLRISVLKSRACKHKEAKYTCPEIFLNAVSDKLVNTAVLFINIELLSEFYYQFPRELDQRLIHSLSSEQLNAFVNENPRLKSQLQLQHKRQCLELALQKINSLVILEQQADSD | Function: Dynamin-related GTPase required for mitochondrial fusion. Coordinates interaction between the inner and outer mitochondrial membrane to promote the formation of the double membrane (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 101901
Sequence Length: 903
Subcellular Location: Mitochondrion inner membrane
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P28737 | MSRKFDLKTITDLSVLVGTGISLYYLVSRLLNDVESGPLSGKSRESKAKQSLQWEKLVKRSPALAEVTLDAYERTILSSIVTPDEINITFQDIGGLDPLISDLHESVIYPLMMPEVYSNSPLLQAPSGVLLYGPPGCGKTMLAKALAKESGANFISIRMSSIMDKWYGESNKIVDAMFSLANKLQPCIIFIDEIDSFLRERSSTDHEVTATLKAEFMTLWDGLLNNGRVMIIGATNRINDIDDAFLRRLPKRFLVSLPGSDQRYKILSVLLKDTKLDEDEFDLQLIADNTKGFSGSDLKELCREAALDAAKEYIKQKRQLIDSGTIDVNDTSSLKIRPLKTKDFTKKLRMDATSTLSSQPLD | Function: Outer mitochondrial translocase required to remove mislocalized tail-anchored transmembrane proteins on mitochondria . Specifically recognizes and binds exposed hydrophobic surfaces of mistargeted tail-anchored transmembrane proteins . Acts as a dislocase that mediates the ATP-dependent extraction of mistargeted tail-anchored transmembrane proteins from the mitochondrion outer membrane . Able to unfold protein substrates by processive threading through its central pore . Once extracted from the mitochondrion outer membrane, substrate proteins are then transferred to the endoplasmic reticulum, where they are ubiquitinated and degraded by the proteasome . Also mediates extraction of excess tail-anchored proteins from the peroxisomal membrane . In normal conditions, MSP1 translocase activity is inhibited by PEX3 at peroxisomes; only catalyzes removal of excess tail-anchored proteins .
Catalytic Activity: [protein]-with a C-terminal TM segment(out) + ATP + H2O = [protein]-with a C-terminal TM segment(in) + ADP + H(+) + phosphate
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 40343
Sequence Length: 362
Subcellular Location: Mitochondrion outer membrane
EC: 7.4.2.-
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Q9PHN0 | MKNIVLGGGCFWCVEAVFERLKGVINTEVGYSGGKPNPSYESVCNGDGNIEVVKINYDEKQISLLEILTLFFKIHDPTSIDKQGGDIGIQYRSIIFYENEEDKILAQNFIEEQQKIFSKKIVTKISRLQTYYKAENYHQHYFINNPDQGYCQAVIAPKLQKIQSD | 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)-S-oxide-[protein]
Sequence Mass (Da): 18896
Sequence Length: 165
EC: 1.8.4.11
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Q7NVL7 | MEKAILGGGCFWCLEAAFSQLKGVERVVSGYCGGHTDSPDYRQVCSGDSGHVEVVEISYDPALIDYATLLQVFFAVHDPTTLNRQGHDVGTQYASAIFYLDETQRECARRVIAQLDAEQIFDAPIVTRVESAPRFHPAEDYHQNYYAQNQQQNYCQLVISPKLAKIRRRFSHLLQN | 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)-S-oxide-[protein]
Sequence Mass (Da): 19904
Sequence Length: 176
EC: 1.8.4.11
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A5CQY7 | MQTFILAGGCFWCLDAVYRTLDGVQDVISGYIGGHTAHPSYDAVCTGATGHAEAVKVVFDEEVIPADVILDVFFTLHDPRQLNRQGADVGTQYRSAMFPADAAQEQLFRDAISRAGELWDGTAVTTIEPVGTWYDAEDYHQDFFAKNPGQGYCNAVAVPKVNKVRKSFAQYVRAA | 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)-S-oxide-[protein]
Sequence Mass (Da): 19172
Sequence Length: 175
EC: 1.8.4.11
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A4X3E5 | MFLRRTKAQLISPEEALPGRPVATPVTEPHEVLGTPLTGPFPEGTAVAVFGMGCFWGAERLFWTLPGVLTTSVGYAGGYTPNPSYDEVCSGRTGHAEVVHVRYDPTKITYEDLLKVFWENHDPTQGMRQGNDVGTQYRSAIYPTTDEQLTTARASRDAFAPVVARAGKGEITTEISPLGDYYLAEGYHQQYLAPTKNPGGYCNHGPNGLSCPVGVARTTD | 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)-S-oxide-[protein]
Sequence Mass (Da): 23854
Sequence Length: 220
EC: 1.8.4.11
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Q09859 | MQIAIIAAGCFWGVQEVYLRKFIPAAAILKTSVGYTGGITADPTYKEVCTNTTNHAEALKIEFDEKLTSYDKIIEFFFAMHDPTTSNQQGNDIGTQYRSAIFTTNPEQATIAKRVMNEVQAKHYPNKKIVTQILPAGKWWDAEDYHQLYLEKNPDGYRCSSHFLRWNVFE | 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 + L-methionyl-(S)-S-oxide-[protein]
Sequence Mass (Da): 19437
Sequence Length: 170
Subcellular Location: Cytoplasm
EC: 1.8.4.11
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A6T7R0 | MANKPTPEELKNGLSEMQFYVTQHHGTEPPFTGRLLHNKKNGVYHCLVCDAPLFNSQTKYDSGCGWPSFYEPVSAEAIRYLTDNSHGMQRIEIRCGNCDAHLGHVFPDGPQPTGERYCVNSASLSFTDEQNGEQIKG | 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): 15292
Sequence Length: 137
EC: 1.8.4.12
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Q6ADJ8 | MDAGKGEYQIAKSDEEWRRELTPEQYGVLRQAGTEQPWTGELLDESRAGVYACAACGAELFRSGTKFDSGCGWPSFYESVRPEAVELLEDTRLGITRTEVRCANCGSHLGHVFPDGFRTPTGDRYCMNSISLDFQPEDE | 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): 15510
Sequence Length: 139
EC: 1.8.4.12
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Q72NN2 | MNYEVNKSDEDWKKELTPEQYRILRQKGTEMAFTGALYKNQDKGTYVCAACGAVLFSSDTKYESGSGWPSFYQPVKDGVVDKQKDSSHGMERTEILCSKCGGHLGHVFNDGPRPTGLRYCINSASLKFQKE | 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): 14717
Sequence Length: 131
EC: 1.8.4.12
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Q87MS5 | MPKIVKKEPKFVEQSGKKVTKSDEQWREQLSDEEFRVCREQGTEPPFSGKLLHNKETGVYACTCCNAPLFISDNKYDSGCGWPSFDAPLNNEAIRYLEDLSHGMVRTEIRCASCDSHLGHVFEDGPKTTGERYCVNSVSLIFNKSDE | 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): 16644
Sequence Length: 147
EC: 1.8.4.12
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Q7MMC4 | MHKKSSTLIRKREISDVTKESKVVLKSDQQWREQLSEQEYHVCREQGTEPPFSGKLLHNKDSGEYACTCCYAPLFSSVNKYDSGCGWPSFDAPINETAVLYLDDFSHGMKRVEIRCARCDSHLGHVFPDGPKTTGERFCVNSVSLIFNKIETNE | 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): 17527
Sequence Length: 154
EC: 1.8.4.12
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Q9PF29 | MNVAFDLTPPSPSQREALIATLNAEEHRILLQHGTEAPFCNRLLDNNQLGTYTCRFCGLPLFHSNAKFKSGTGWPSFFEPYTHAHIRKQHDTSHGMIRTEILCARCNSHLGHLFPDGPPPTYERYCLNSVSLTFIPTGTLLPDQLHRGDNTAYRT | 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): 17493
Sequence Length: 155
EC: 1.8.4.12
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P76270 | MNKTEFYADLNRDFNALMAGETSFLATLANTSALLYERLTDINWAGFYLLEDDTLVLGPFQGKIACVRIPVGRGVCGTAVARNQVQRIEDVHVFDGHIACDAASNSEIVLPLVVKNQIIGVLDIDSTVFGRFTDEDEQGLRQLVAQLEKVLATTDYKKFFASVAG | Function: Catalyzes the reversible oxidation-reduction of the R-enantiomer of free methionine sulfoxide to methionine. Specific for free L-methionine-(R)-S-oxide.
Catalytic Activity: [thioredoxin]-disulfide + H2O + L-methionine = [thioredoxin]-dithiol + L-methionine (R)-S-oxide
Sequence Mass (Da): 18122
Sequence Length: 165
EC: 1.8.4.14
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Q7BHL7 | MDKETNDNEYRRQSEHRTSAPKRKKKKKIRKLPIILLIVVILLIALVVYIVHSYNSGVEYAKKHAKDVKVHQFNGPVKNDGKISILVLGADKAQGGQSRTDSIMVVQYDFINKKMKMMSVMRDIYADIPGYGKHKINSAYALGGPELLRKTLDKNLGINPEYYAVVDFTGFEKMIDELMPEGVPINVEKDMSKNIGVSLKKGNHRLNGKELLGYARFRHDPEGDFGRVRRQQQVMQTLKKEMVNFRTVVKLPKVAGILRGYVNTNIPDSGIFQTGLSFGIRGEKDVKSLTVPIKNSYEDVNTNTDGSALQINKNTNKQAIKDFLDED | Function: Involved in SarA attenuation. Affects resistance to oxacillin and teicoplanin, as well as the synthesis of virulence factors.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 36971
Sequence Length: 327
Subcellular Location: Cell membrane
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K7R4D4 | MNSMEIRQAFAGLLTLSMFIMLGNMIKKDHFDYPAEEVEIQTTEVSQHDLATVSHISQKSKQNDKALKPCWNPPTLKEVEQSKGFIIFSLTNGPEYHIAQVADAVVVAKYLGATLVLPDIKNSKSGNSMNLGDIYDVENVLNKLNGLVKVTKTLPPHVSTRNTPIVRVPNKVSQDYIMKKLKPIYQAKGIIKIESYFPSKNTISRNNNSLESLLCQTMFGGTLELKKEIQEEAESIVQKLETWSQESNGPFVAVDLRIEGLKNECNGKDGKGRKQCYQGHEIGEFLKRIGFGQETVIYVTQTKWSPDLNSLRYMFPKTYTKENIMSSTKKEKFINSESIEFEKAIDFYICSESDVFVPSILGPFYENVAGMRIVSGKNEIIVPSEVVSPSASASEHMSPYVTKKNHLAYKCFC | Function: Glycosyltransferase involved in mannan biosynthesis.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 46439
Sequence Length: 413
Pathway: Glycan biosynthesis.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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A4IGU3 | MALVPYTDSGVQSLKRFHDSSASFKFVNHNIEIKQDWKQLGVAAVVWDAALVLCMYLESEGIHLQNSSVIELGAGTGLVGIVAALLGAQVTITDRDLAMEFLRMNVRDNIPKDSLHRVSVRALNWGKSLEEFSTYDFILGADIIYLEETFPDLLQTFLHLSSQQSVILLSSRLRYQRDHDFLEMMKLHFTIADVYYDKNTDVHIFRAQLRQRKEL | Function: Protein-lysine methyltransferase that selectively trimethylates residues in heat shock protein 70 (HSP70) family members.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 24579
Sequence Length: 215
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q5VZV1 | MDVCLSSAQQPGRRGEGLSSPGGWLEAEKKGAPQKDSTGGVLEESNKIEPSLHSLQKFVPTDYASYTQEHYRFAGKEIVIQESIESYGAVVWPGAMALCQYLEEHAEELNFQDAKILEIGAGPGLVSIVASILGAQVTATDLPDVLGNLQYNLLKNTLQCTAHLPEVKELVWGEDLDKNFPKSAFYYDYVLASDVVYHHYFLDKLLTTMVYLSQPGTVLLWANKFRFSTDYEFLDKFKQVFDTTLLAEYPESSVKLFKGILKWD | Function: Protein-lysine methyltransferase.
Sequence Mass (Da): 29565
Sequence Length: 264
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q8BLU2 | MDQHLHIAQQPLLSGTPQEDGFAGPSVEFDRIESSLRSIQKFVPTDYASYTQEHYQFAGKKIIIQESIENYGTVVWPGATALCQYLEDHTEELNLQDAKILEIGAGAGLVSIVSSLLGAQVTATDLPDVLGNLQYNILKNTLECTAHLPEVRELVWGEDLEQSFPKSTCCYDYVLASDVVYHHYFLDKLLATMVYLSQPGTVVLWANKFRFSADYEFLGKFKQAFDTTLLAEYSESSVKLFKGILKWE | Function: Protein-lysine methyltransferase.
Sequence Mass (Da): 27892
Sequence Length: 248
Subcellular Location: Nucleus
EC: 2.1.1.-
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Q9H867 | MADTLESSLEDPLRSFVRVLEKRDGTVLRLQQYSSGGVGCVVWDAAIVLSKYLETPEFSGDGAHALSRRSVLELGSGTGAVGLMAATLGADVVVTDLEELQDLLKMNINMNKHLVTGSVQAKVLKWGEEIEGFPSPPDFILMADCIYYEESLEPLLKTLKDISGFETCIICCYEQRTMGKNPEIEKKYFELLQLDFDFEKIPLEKHDEEYRSEDIHIIYIRKKKSKFPS | Function: Protein N-lysine methyltransferase that specifically trimethylates 'Lys-315' of VCP/p97; this modification may decrease VCP ATPase activity.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 25807
Sequence Length: 229
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q81F14 | MKTTYVNATIVTMNEQNEVIENGYIIVENDQIIDVKSGEFANDFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWLETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMFNPIGVDQDAIMETVSRSGMRAAVSRTLFSFGTKDDEKKAIEEAEKYVKRYYNESDMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKRPVEYAASCGLFKRPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMFEEMRIATLLQKGIHQDATALPVETALSLATKGAAEVIGMKQTGSLEAGKCADFITIDPSNKPHLQPADEVLSHLVYAASGKDISDVIINGKHVVWNGECKTLDEERIIFEASRYKRGLQR | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
Catalytic Activity: H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine
Sequence Mass (Da): 48123
Sequence Length: 435
EC: 3.5.4.28
|
Q8R9L4 | MNLLIKNVNLLSMEEDKVLEGVNVYVEGDTIKHIGELLPDVKVDVVIEGKDKLAMPGLINAHTHLGMSLFRNYANDVPLFDWLTKYIWPLEARLTAEDVYWGSLLSMIEMIYSGTTTYCDMYFFMEEVAKATEEIGIRGVISRGIIEEQDAKVNEEKLKDTENLYNAWNGKAEGRIKVMVGPHAPYTCGPTYLKEILDLAKRLGTGIHIHVSETKREVEESLEKYGKTPVQHLKDLGIFEVPTVAAHCVHLTDEDIEVLKEMKVSPVYNPTSNLKLASGFAPVEKMLKKGINVALGTDGPASNNNLNMFEEIHFAATINKALNEDALSVPAFEALKMATVSGARALLWEREIGTIEVGKKADVILIDLNKPHLHPKNDLISALAYSVQGSDVDTVIVNGKVIMEKREIKTVDVERVYYEVEKRAQNLIRGEIS | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
Catalytic Activity: H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine
Sequence Mass (Da): 48350
Sequence Length: 433
EC: 3.5.4.28
|
A4XJI3 | MDLLIKGATIITLDGENEVLKGDILIENGKISEISQSIELSKEKMFATKVINAENLIALPGFINAHTHCGQTILRSYADDLPLYEWLFEKIFPAEEKLTKEIVYYSSLLGIAEMLKCGTTMFFDMYFHEDMTAKAALETGIKAVLSRGLQTDERQQQRLDETKELIYNYSSDKIKVFFGPHSVYTCSYELLEKVAELSEEFNTGIMIHLSESEDEVNQCYEKYDMSPVKLCQKAGLFTRPCIAAHCVYVDDEDIEILAENGVTAVYNPTSNLKLGNGFAPVFNLIKSGVNVAIGTDSAASNNNLNILEEIHIAALLEKGMYRLPEILKAQEVLKMATVNAAMAADIHNTGRLKKGFSADIVLIKANDLNMLPCYNTISNIVYSSNPSNVYATIVDGEILYMDGRLLTIDEEALIKEIKSIEKILEESIE | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
Catalytic Activity: H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine
Sequence Mass (Da): 47854
Sequence Length: 429
EC: 3.5.4.28
|
Q3AC64 | MVNELTILIKNTTVLDLNKFAAVENDILIEGNKISKIGVDIEVNDKENLKIIDGSNKVALPGLINGHTHVAMTLFRGASDDLPLMDWLNNVIWPSESRLTGEDVYWGSLLGIVEMIKSGTTTFCDMYFFMDEVAHAVEQSGIRAILSRGMVALDPENGEKGLKESIDFIEKWQGKANGRITTALAPHAPYTCPPEFLKDVIWEAKRLNVPINIHISETLDEISIIKERYGTTPVRHLESLGLFEVKTIGAHLVHVDDEEIQILKRYQVGAIHNPQSNMKLASGIAPVAKMLEAGVLVGLGTDGAASNNDLDMIEELRAASYLQKVSSMNPEALNAKTSIAMATSLGARALGLTEVGLLKEGYKADIILLNTNETNFYPRHNIFNLIAYSAKGADVDTVIVDGEIIMEKRQLTRLDEEKIKFEANKRGLKLVAG | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
Catalytic Activity: H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine
Sequence Mass (Da): 47617
Sequence Length: 433
EC: 3.5.4.28
|
Q891Y7 | MSILIENVMIVTMDEEQDVIKEGYILIKEDKIKEVNLGAYLGNKENLYIINGEGRCAIPGLVNAHTHAGMTIFRGYGEGLPLMRWLNEKIWPIESKLKGEHVKIATELAALEMLRSGTTCFNDMYFYEEQVVKVAKEFNIRGIIGVSIMGDSWEHQLKEAIDIDKKIKEDKSGLLDSMIAPHSPYTLSKEALESIGKEAKLQNKNIHIHISETQDEVNIIKEKYNKTPCEFLQSVGIFNSKVAAAHCVYLTDEDMNILKQNGTSVIYNPQSNMKLASGIAKIAEMIDMDINVCLGTDGTSSNNNLNMIEEMETGTILQKLYYKDATKLSAKKALEMATYNGAKALINNKKLGKIKKDYLADIALLDLNKPNMLPVNDIHSNIVFSANGSEIDYVIVNGSVVMEKGEFKHIDEEKVLYNFKEMCKDIFNN | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
Catalytic Activity: H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine
Sequence Mass (Da): 48177
Sequence Length: 429
EC: 3.5.4.28
|
B1I2P4 | MRLLIRNAYVIPVAGSDFTGDVAVEEGRIVFAGPTGAVPGTFEADETIDATGMVATPGLVNCHTHAAMTLFRGYADDLPLMEWLTRKIWPVENLLTGDDIYWGSLLAGLEMLKSGTTTFADQYFEMDRVAQAVEEIGLRASLCRGLIGVSEHAEKALAEGCEFVRRWHGAAAGRISAMLGPHAPYTCPPAYLKKVVAASEELDVGLHIHLSETRTEIEQIKAEYGCSPIALMEETGLFHRPVLAAHCVHLSEADIKILARRGVGVAHNPQSNMKLASGIAPVVRMLAAGVRVGIGTDGAASNNDLNMVEEMRTAALLQKVAQGDPTVLPAGLVLEMATAGGARVLGLEDRIGTLEVGKRADVVLWRVNQPHLCPAHNYQAHLVYSAGRADVDTVIVDGHVVMRGRRVLTVDEETVLRQAERTARRLIESV | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
Catalytic Activity: H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine
Sequence Mass (Da): 46329
Sequence Length: 430
EC: 3.5.4.28
|
A4J675 | MNRLLIRGATILTMEGPEAIIETGELLIEDGWITHVGLPGSASGSFDMDEVIEADGQVAMPGFINCHTHAAMTLLRGYADDLPLMTWLSEKIWPFEGRMTNEDIYWGTMLACLEMIKSGTTCFGDMYDCMHDVARAVEKTGMRAMLSRGMIGIAPTADKALIEAEELARNWNGKADGRITVMVAPHAPYTCPPDYLDKAMNLAAKHKLGINIHLAETLTEFEDIKKQYGKTPVKHLDQLGLFKLPVLAAHCVHLDEEDMDILAQKAMGVAYNPQSNMKLASGIAPVAKLLELGATVGIGTDGTASNNNLDMLEELRAGSFLQKVSTMNPEVIPAYRALQMATIDGALCMGLGDRVGLIKEGMRGDVILLDTQQPHMCPRHNLVANIAYAANSSDVRTVVIDGKVVMLDRVVKTIDEERVMYEVRERAARLAGK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
Catalytic Activity: H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine
Sequence Mass (Da): 47327
Sequence Length: 433
EC: 3.5.4.28
|
Q72B14 | MPLPCDTILQAALIVTQDDARTVIEDGAIAIHEGRIAAVGQRDAIVGNWHGVTVIDMGESLIMPGLVNAHTHASMTLLRGLADDLPLMDWLTGHIFPVEKGLTGELVELGALLGCAEMLRTGTTAFSDMYLIEDATLRAVDRAGLRCLAGEAIFAFPSPAYADPETAFDLVRAQHDRWKHHARAALAVAPHAVYTSTPAILARCRDLAEELGLPIHLHLAETATETAQCIEQHGARPVPYCDGLGLLTPRTTLAHCVDLTEGEIDLLAERGVTVAHCPESNMKLASGIAPATAMLGRGMTLGLGTDGAASNNSLNMFTEMTSCALLHKVHHMDPTCAPASAVLDMATRGGAHALHMQGIGRIEAGCPADIIALDLRAPNMQPIFNPASHLVYAATGHETRLTMVGGEVLYLDGCYTRFDMDDLLKEVRKARTWAMEQVRAAR | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
Catalytic Activity: H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine
Sequence Mass (Da): 47285
Sequence Length: 442
EC: 3.5.4.28
|
B8E183 | MRILIENVSVFQEGDILNNKNILIENDIIKEISEDKNFEKIDYVIEGKNKIALPGLVNTHTHLAMTLFRGFADDLPLKEWLEEKIWPQEAKLTAEDVYWGSLLGICEMIKGGTIAFADMYFFMDEVAKAVSESGVKASLSVGMIGVSGNENEILNRGVNFAQNWHNAENGRIKVMLAPHAPYTCPPSFLEKVINKAVEMNLSIHTHLSETYLEVENIKNIYGLTPVRLMDRIGLFNVPVLAAHCVFVDDEEIEILSEKGVGVAHNPQSNLKLASGVAPVKKMVEKRVKIGLGTDGPASNNNLDLWEEIRLVATLHKGVEKDPVCIPAKEALNMATKNGMEILGFENSGIIKEGYKADLILVNINKPHFYPRHNLISHLVYSALSSDVDTVIVDGKVLMEKRELKILDEEKIMFEAEKRAFDLIKKR | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
Catalytic Activity: H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine
Sequence Mass (Da): 47673
Sequence Length: 426
EC: 3.5.4.28
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Q9KC82 | MGTIVKNVSIVTGQAEAPFIRHGYFKFADGVIVSVAEGTPSPEEIDRVEVIDGKGKWVMPGMINTHGHLGMSLLRGHSDDLPLQSWLTEKMWPFEGKMDREAVHHARQLAMAEMIKSGTTTFLEMYHLYMDDLAEAVVEQGPRAVLMRSMIGLCSESEQREKLKEAVTFATTWNGDGNGRITTMMAPHAPYTCPPSFIEMIVDEADRIDLPLHTHMAETQREVEEHRKTYGVHPLVHFEQLGFLKDRHWLLAHCVHLGEEELDILEQHPSVHVSHNPMSNLKLGSGIANVQSMLERGINICLGTDSVASNNHLDLVEEMRIAALLQKGAVLDPTAIPAETAIAMATKNGAKALRLPQVGTIEAGKRADFIMIDPQCLHLQPHEHVMSHLVYALKGADVQDVFVEGAPLMLNKELKTFDEEKLQFEANAHYQRICEKLK | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
Catalytic Activity: H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine
Sequence Mass (Da): 48874
Sequence Length: 438
EC: 3.5.4.28
|
B8CX03 | MKILIKNVDVIYTADSNRSIIKNGYIIIQDNKIKEINDMDNLVYQSNDFDDVISGKGKMALPGLVNAHTHSAMTLLRGFADDMPLHKWLQEKIWPFEKTLIPEDIYWGAKLAILEMIKTGTTTFADMYFEMGQVAKVVEEGGLRAVLSQGLIEANDGEEGLNRALKFCLEWNNRADGRILTMLAPHAPYTCSPDFFRRVVDLSQEYNLGIHTHIAETKEEFQQIREKYDCTPLQYLEKTGALKRPVLAAHCIYITEEDMDLMAQKPIGVAYNPQSNMKLGSGIAPVTRMLSKGIKVGIGTDGTSSNNNLDLIEEARSGSFLQKVNDLDSTALPVDTVLKMLTVNGAKILGFDKLGVLKEGYLADIILIGLNESTFYYPHYNNLSNLFYAGSGNDVTTVIVNGRVIMKDREVLTINEEEVYYKIEEIARRKL | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deamination of 5-methylthioadenosine and S-adenosyl-L-homocysteine into 5-methylthioinosine and S-inosyl-L-homocysteine, respectively. Is also able to deaminate adenosine.
Catalytic Activity: H(+) + H2O + S-adenosyl-L-homocysteine = NH4(+) + S-inosyl-L-homocysteine
Sequence Mass (Da): 48364
Sequence Length: 431
EC: 3.5.4.28
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P23941 | MRFFSVFDIVKNKANQLGYTETEMYAVLKNYNVNKKDLLAYKENGVIPTDKVLNGILSYLGMTKVELELKLGRIPAGLEDVFLNNTKEIAKILENKNSVKLNEFNSIQEIKPYFYTDLGKLYNGDCLELFKQVPDENVDTIFADPPFNLDKEYDEGVTDKNSFSGYLDWYYKWIDECIRVLKPGGSLFIYNIPKWNTYLSEYLNRKLNFRNWITVDMKFGLPIQNRLYPANYSLLYYVKGDKPKTFNVQRIPLQTCPHCGREIKDYGGYKNKMNPKGVTLSDVWSDIYPVRHSSSKNRKFNELSVKLLDRIITMSTNEGDVVLDPFGGSGTTFAVSEMLGRKWIGFELGNCEIIKERLKNKDKDKKLLGKVYEEKNKLFPNRVKELRKKNGLWIDDDFRQDHEGNSKGDKKNENNDQISLSLE | Function: A beta subtype methylase, recognizes the double-stranded sequence 5'-GGATCC-3', methylates C-5 on both strands, and protects the DNA from cleavage by the BamHI endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49136
Sequence Length: 423
EC: 2.1.1.113
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O68556 | MNNHSYLKKNSFHEGDARELLKCIEEESIALSVWSPPYHVGKKYEEGQTYEQWSSLLTKVIALHYPILKPGGFLVINIDDILAFPDPRMPRFQAVNLKKHRVSVTREDILNALKLEPELTKYQLAKKFNCSEQTIERRLKGNNIRGGKYNVQTKVKLAGPVLEKAAEEAGLYLYDRRIWAKDPAWQNSQWHSNSYKAVSEFEHLYIFWKPGETVIDRNKLSKEEWASWASRGIWYIPSVRKNDDHEAKFPLLLPQRLIKLLTQKGDTVLDCFMGSGTTAVAALSESRNFIGIEKEPKYIQLSNKNVETFYISRNKEASKIKETNHSVTDEKKKAEQLELLLEENENSL | Function: A beta subtype methylase, recognizes the double-stranded sequence 5'-GCCNNNNNGGC-3', methylates C-2 on both strands, and protects the DNA from cleavage by the BglI endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 40242
Sequence Length: 348
EC: 2.1.1.113
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P0DW08 | MIVIDLFSGAGGLSEGFHKHDFKIAAHVEKEYWACETIKTRLFYHFLKAQNDLELYHEYLRVSDNYRNIEQSRAFVFQRYPELREKLEMEVLNRKFGNPHNDPTATSSTQMIQLIQNSLQYSRATSVDLIIGGPPCQAYSLVGRSRMKDSVGKDSRNYLFQYYKRIVDEFKPKAFVFENVPGILTAKQGKVYQEIKESFDQIGYTVLSGTSQEDRSNVIDFADFGVPQRRKRVILFGFQKKLNYEYPNFERHKLSWNSPLTTRDVISDLPVLKPKQGHDLRLFEYDTTQGVDQLSPYELMMREDSIGFTNHFARPIKERDAEIYQIAIEHATQGRQIKYNELPERLKTHKNEKAFLDRFKVHWWDIIPHTVVAHISKDGHYNIHPDIEQCRSLTVREAARIQGFPDNYKFEGPRTAQYTQVGNAVPPLMSGIIARAVKDVINGHH | Function: Component of antiviral defense system DISARM (defense island system associated with restriction-modification), composed of DrmE, DrmA, DrmB, DrmC and DrmMII. DISARM is probably a multi-gene restriction module, this subunit is a DNA methylase. Expression of DISARM in B.subtilis (strain BEST7003) confers resistance to phages Nf, phi29, phi105, phi3T, SPO1, SPR and SPP1. Protection is over 10(7)-fold against phi3T, 10(4)-10(5)-fold against Nf, phi29, phi105 and SPR, 100-fold against SPO1 and 10-fold against SPP1. DISARM does not interfere with phage adsorption, but instead interferes with (phi3T) DNA replication early in its cycle, preventing replication, circularization and lysogeny and probably causes phage DNA degradation (DNA is degraded in SPP1-infected cells). Expression of this methylase alone leads to highly methylated phage, however they are still susceptible to the DISARM system.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 51787
Sequence Length: 445
Subcellular Location: Cytoplasm
EC: 2.1.1.37
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Q9LAI2 | MNWIFNTLIQFLEDLNIDPSVVSLIDEDAKKLEEQFPKALKHPVVDEEIVYKILCEKYNLNALNVKTISETLNKEYKFGRNSKTALKKYLDYGKEEYLIQFFNTLMLENNTYIDREYIESVLAFCEPVSKEKIKNEFIKLWNEANEVNEYGKLKDYLLGIYSKLFSMGLENLRLIEIYNSNESLIKKVFKYESTIKELKEYCLSNQESITAGLAIKMFNEKYMELMKKEYQQDAIALKLEEHMNQLYVDNNINEYPYIFDRGNDILLLPTEEYDFVYFHIDQDFFNRFQDENKFLDYVLSSIKQIYRVLANEKVFALKIDNIYNNEKNLKWELYPKLTIYSEHFIQTKETARFYKAYDIAKDLLSKHEFRLLENDSEKNRENILKEYFSGKISEDELFSLVHVNMKKEHFFEFLNRFKYVHYGFTFNDCLVLDRVDKSFANGELENVISNATEILLIFYKFRADQRRIPCPSCGSLNISGNSYPEINNRSWECKSPYCPDRSKSNRGKRYSKKSNYMQWGAIYPKSHDIIPRELIKKWRRDIIVINNEQEIFEMLVKYFSFTDEKLLFINTNELPSVVTERENRKVVILSQKLKEKAYTSNVVVKESLEGEIEFFKNGLYLKNFTELYLPEDQRRVSPEINNFLNSGGRLKLIQGDSYEVLKSVEDNTFAAAVTSPPYYNAREYSQWPNLYLYFNDMYNIIKECFRTLKPGSVFLYNIADIVDNENIIVKSSMGNKRIPLGAYTIYFFQKAGFELLDNIIWDKGEPQSNRQKNDGKFTPHYQKPLNAYEHMFIFKKTGAPLTLSDDWQSKRGSWIKNIVPFQPVFKINSKGENILGHTAPFPEDIPRFVANVFTKHDNDIILDPFSGSLTSAIASYKSNRIGLGIELSPDYVELSRDRALLEGVTTKILNFN | Function: A beta subtype methylase . Recognizes the double-stranded sequence 5'-CCN(7)GG-3', methylates C-2 on both strands, and protects the DNA from cleavage by the BslI endonuclease .
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 107439
Sequence Length: 912
EC: 2.1.1.113
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P34905 | MKFRKGELFCGPGGLALGAKEAKYMHPETGEVFEFEHAWANDIDEWACETFRTNICPDRPDSVVCGDVRELDIKSLGEKFGEIDAFTFGFPCNDYSIVGEHKGMEGNYGPLYSYGVKILNEYNPLVFIAENVGGLQSANEGKAFLGILNDLASAGKYGYKLVPHLYKFEEYGVPQRRHRIIIVGIRKDQDVAFRVPEPTHKEKYRTASEALADIPEDALNHEFTRHKKKVVEMLNHIAPGGNAWSESIPEELRLNVKKVRMSQIYRRLHPDQPSYTVTGSGGGGTHGYHWEEPRALTNRERARLQTFPDDYEFIGKKEMVRKQIGMAVPPDGAKIILEAVLKTFARIEYPSINSKWDFESVSAEQVIEEVQEIM | Function: A methylase, recognizes the double-stranded sequence 5'-GCAGC-3', methylates C-2 on both strands, and protects the DNA from cleavage by the BbvI endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42350
Sequence Length: 374
EC: 2.1.1.37
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P10283 | MKVLSLFSGCGGMDLGLEGGFLAHRSSINSDLYASYISDHDENYVYLKKTGFETVFANDILPFAKLAWCNFFKNRVNQPENIFHLESIVDVVNNIENKQFSFPNDIDVVTGGFPCQDFSFAGKRKGFDSHKDHNGIIYNEPTEATRGQLYLWLKKVVEITKPKVFIAENVKGLVTLGDVKDIIQKDFRNIDDGYVVLDAQVLNAKNYGVAQNRERVIFIGISKRYANKKILDELISLQEKSEVYPYPPYTHGTDPELKPYATLNQILAHLPEPELASTDKSQQSYSKAKLFKKTQGNIEVNMNGQAPTIRAEHHGNIEFRRLSKENGGTNLSELHLPQRRLTVRECALIQSFPPDYEFVFNYGKANSVSASAAYKIIGNAVPPLLGFAIGRHLSQIWDKLFKT | Function: A methylase, recognizes the double-stranded sequence 5'-CGCG-3', methylates C-1 on both strands, and protects the DNA from cleavage by the BepI endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 45466
Sequence Length: 403
EC: 2.1.1.37
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P70986 | METVQMSLDLQPEDTKANIECSSPDYEIKCFSHNQFAPQIERLKIEKKYIHIVEETETFNRKLVSYQANKNQSIHNWIRYKEGFSSELVQNLIEEFGLSKGDTILDPFLGSGTTSLTAKMLGINSIGIDILPISHIAFEPKSFIFEYNLEELDRAYKEIYEISPTKIEQKFNHLSITEGAFPEETENDLLFFTHWDNNSQYSYQTKTLIKLILVSILEEISYTRKDGQYLRWDYRSQKVIETNKKRLEQGKEPIKTILDKGELPTVKESLLNTLLTIKEDIKEIQQKCLPNESVHELIKDSALNALPKINDNTFDAVITSPPYCNRYDYTRTYALELAYLGVDEKKIRELRQAQLSCTVENKSKLKQLKDYYHSLFLESRYAEIERLVTGNEVLNEINYALRKRWENGEVNNKGILSMVDGYFTELTFIFYELFRTCKPGAKVAFVNDNVRYAGEIIPVDFLSTKIAEDIGFKPIKIYTLKQRKGNSSQQMGKYGRVALRKSITIWEKP | Function: An alpha subtype methylase that recognizes the double-stranded sequence 5'-CYCGRG-3', methylates C-1 on both strands, and protects the DNA from cleavage by the BsoBI endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 59144
Sequence Length: 509
EC: 2.1.1.113
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P25262 | MQQFRFIDLFAGIGGFRLGLEAVGGVCVASAEIDQQAIKVYRQNWPTDGVDHNLGDITAIQQLPAHDVLVGGVPCQPWSIAGKNQAFDDPRGQLWADVIRLVQINQPKAFIFENVKGLVDPRNRLCLEIILDSFKDLGYSVFYKLLNSFDFGVAQNRDRVFIVGIQQKLDLNGFSFPEYTESEQRLYHILDNLEVPETKLESIPIQRNLFGERIDVGYNKLTPRGAFNDFFILNDIRNGPTSIHSWEIYPTTEREKQICMIIMRNRRNSRYGDCDGNPMSYQDIAELVAGLAEKELQTLVEKRILRQYPDGKYEFFNRRLSGGIDGTYRIFLPNARFFGTLTARGMHDEIAEISVSGANAEEYKHNFIQQVLIPKRYRKITVSEAARLQGFPGSFQFHSNQSANFRLIGNSVAPPVIVALGKALQCVKLFEQELCEV | Function: A methylase that recognizes the double-stranded sequence 5'-GGWCC-3', methylates C-? on both strands, and protects the DNA from cleavage by the HgiBI endonuclease . This system is less active than isoschizomeric RM.HgiEI .
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 49627
Sequence Length: 437
EC: 2.1.1.37
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P13906 | MAIKINEKGRGKFKPAPTYEKEEVRQLLMEKINEEMEAVATATSDISNDEIQYKSDKFNVLSLFCGAGGLDLGFELAGLEQSLGTDKALEAFKDRDVYNAIRHESVFHTVYANDIFSEALQTYEKNMPNHVFIHEKDIRKIKEFPSANLVIGGFPCPGFSEAGPRLVDDERNFLYIHFIRCLMQVQPEIFVAENVKGMMTLGGGEVFRQIVEDFGAAGYRVEARLLNARDYGVPQIRERVIIVGVRNDIDFNYEYPEITHGNEEGLKPYVTLEEAIGDLSLDPGPYFTGSYSTIFMSRNRKKKWTDQSFTIQASGRQAPIHPGGLPMEKVDKNKWIFPDGEENHRRLSVKEIKRIQTFPDWYEFSDGGNMKVSVNNRLDKQYKQIGNAVPVFLARAVAKSIAQFAADYLKDNHPHEAPQMKLFI | Function: A methylase, recognizes the double-stranded sequence 5'-GGCC-3', methylates C-3 on both strands, and protects the DNA from cleavage by the BspRI endonuclease.
PTM: In the absence of DNA, can self-methylate two cysteine residues.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 48212
Sequence Length: 424
EC: 2.1.1.37
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Q59603 | MYKTIDLFSGIGGIRLGFEKYGCTNVFSSEWDKYARQVYEANFGEKPFGDINGIDPSDIPDHDILLAGFPCQPFSIAGKGLGFEDTRGTLFFNIAEILKTKQPKAFLLENVKRLTTHDSGRTFRIVLETLKQLGYTVYFKVLNTLDFGLPQKRERIYIVGFSDNIPFYFPEPINQYRPLGELLENDRDVEPSYFLSDTLKQKRLAALKKAPPTPSIWHENIGGNVSALPYSCALRAGGSYNYLVVNGVRRLTGREMLRLQGFPDDFEINIPYSQVRKVAGNSVSVPVIEATRKICSLLFPARSNKKGNWIYWRQDDA | Function: A methylase, recognizes the double-stranded sequence 5'-RGCGCY-3', methylates C-5 on both strands, and protects the DNA from cleavage by the NgoBI endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 35949
Sequence Length: 317
EC: 2.1.1.37
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P18051 | MKENIGDCTIDLTVTSPPYDDLRNYNGYSFNFEETAQELYRVTKEGGVVVWVVGDKTHKGSETGSSFRQALYFKELGFNLHDTMIYEKDSISFPDKNRYYQIFEYMFIFSKGKPKTINLLADRKNKWYNGKKHIKGHYRKMDGEKVRHHKQNLLKEFGVRFNIWRIPNGHQKSTLDKIAFQHPAIFPEKLAEDHILSWSNEGDIVFDPFMGSGTTAKMAALNNRKYIGTEISKEYCDIANERLKNYIILHKRMEGKGYRLPQVHS | Function: A beta subtype methylase, recognizes the double-stranded sequence 5'-GGATCC-3', methylates C-? on both strands. No endonuclease has been identified for this methylase, although it is speculated it might protect against BamHI.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30981
Sequence Length: 265
EC: 2.1.1.113
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Q45489 | MSEDQYKQIKLHLGMEDDNEDLPNHIPSSFPKQHLNKIYNGDTMNMLLDIPDNSVDLVVTSPPYNINKFKNDRRPLEEYLKWQTEIIEQCHRVLKPSGSIFWQVGTYVNDSGAHIPLDIRFFPIFESLGMFPRNRIVWVRPHGLHANKKFAGRHETILWFTKTPEYKFFLDPIRVPQKYANKKHYKGDKKGELSGDPLGKNPGDVWAFRNVRHNHEEDTIHPTQYPEDMIERIVLSTTEPNDIVLDPFIGMGTTASVAKNLNRYFYGAEIEKEYVDIAYQILSGEPDENNNFPNLKTLRQYCEKNGIIDPSQYTFTRQRKGSKPSLDSKAHPEEHHKKEIVERIEFEAENSVYKKVQNEQ | Function: A beta subtype methylase, recognizes the double-stranded sequence 5'-AGATCT-3', methylates C-5 on both strands, and protects the DNA from cleavage by the BglII endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42043
Sequence Length: 360
EC: 2.1.1.113
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P22772 | MELTIEEMLIKQKETGAHYTPTDLGDIIAKRLINELKKSGISGTKKIRGLDPSCGDGELLLSLNRMGKFNNIDNIELIGIDEDKEAIKEADFRLNEMGINDAKLSGGDFLDMVDLEGNLSLFDDDLSKIEPVDLIIANPPYVRTQVLGADRAQKLAKLFNLKGRVDLYHAFLVAMTLQLKPGGLIGVITSNKYLANTTGESIRQFLAENYDIIEIMDLGDTKLFSGAVLQAIFFGTKKLNKGIRQTAPANFYKIYEETDPSKTEVSIKFETLFGLLESSNTGVFNVDEKFYSVSCGKLIVPDSFKEPWVMATDEEYNWITNINNNSYCTIQDLCDLKVGIKTTADKVFIKSTWEELPDEIKPEVEVLKLLISTDHASKWRPLERIGNQKILYTHENLNGKKKAIHFTQYPHALAYLETHRETLEGRKYVIKAKRNWYQIWLPQNPDHWALPKILFPDISPEPKFFYEDEGCCIDGNCYWIIPKEENNNDILFLILGISNTKYMTNYHDIAFNNKLYPGRTRYLTQYVSNYPLPNPEANYSQEIIDVLRELLFQNPNDERKIEIENQIENLTALAFGVERL | Function: A gamma subtype methylase, recognizes the double-stranded sequence 5'-ATCGAT-3', methylates A-5 on both strands, and protects the DNA from cleavage by the BanIII endonuclease.
Catalytic Activity: a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 66276
Sequence Length: 580
EC: 2.1.1.72
|
Q59605 | MQQIKFIDLFSGMSGIRKGFEQACRKQSVACECVFTSEIKPAALEVLKQNYPDEVPYGDITKIETGDIPDFDILLAGFPCQAFSFAGKRLGFEDTRGTLFFDVARILKAKKPKGFILENVEGLVTHDRKDSTQKIGRTLTVILETLEALGYYVSWKVLNAKEFGIPQNRKRIYLTGSLKSKPDLSFETSPSPKLKNILESGLPTESSPFIKKLLKKFPPSELYGKSVKDKRGGKNNIHSWDIELKGAVTEEEKQLLNILLKERRKKNGLQKIGIDWMDGMPLTKAQISTFYKHPDLQNILDSLTDKGYLVLEHPKQKIGGQRIKDESLPKGYNIVSGKKSFEINKILDPNDVAPTLFAMDMEHLFVVDNGGLRTLTGKEGLRLFGYPDDYPFDIPKKDRCDLLGNTVAVPVIKAVSERLLHTL | Function: A methylase, recognizes the double-stranded sequence 5'-GGNNCC-3', methylates C-5 on both strands, and protects the DNA from cleavage by the NgoBV endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 47571
Sequence Length: 423
EC: 2.1.1.37
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P43420 | MLQIASLFAGVGGIDLGFEQTGYFETVWANEYDKNAAITYQSNFKNKLIIDDIRNIKVEDVPDFDVLLSGFPCTSFSVAGYRKGFEDEKSGDLFFETLRLIVAKKPQVIFLENVKNLVGHDNGNTFKVIYEALESNGYHIKYQVLNAKDFGNIPQNRERIYIVGFRNIEHYKNFNFPMPQPLTLTIKDMINLSDKLDDRFYYTEDKCSFYSPLQEQMTSDETIYQWRRKYVRENKSNVCPTLTANMGTGGHNVPLVKTKHGIRKLTPRECFNFQGYPEDFILPELAPTHLYKQAGNSVVVPVIRRIAENIYKSML | Function: A methylase that recognizes the double-stranded sequence 5'-GCNGC-3', methylates C-? on both strands, and protects the DNA from cleavage by the Bsp6I endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 36315
Sequence Length: 315
EC: 2.1.1.37
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P04043 | MKIKEIKKVTLQPFTKWTGGKRQLLPVIRELIPKTYNRYFEPFVGGGALFFDLAPKDAVINDFNAELINCYQQIKDNPQELIEILKVHQEYNSKEYYLDLRSADRDERIDMMSEVQRAARILYMLRVNFNGLYRVNSKNQFNVPYGRYKNPKIVDEELISAISVYINNNQLEIKVGDFEKAIVDVRTGDFVYFDPPYIPLSETSAFTSYTHEGFSFADQVRLRDAFKRLSDTGAYVMLSNSSSALVEELYKDFNIHYVEATRTNGAKSSSRGKISEIIVTNYEK | Function: An alpha subtype methylase that recognizes the double-stranded sequence 5'-GATC-3', methylates A-2 on both strands, and protects the DNA from cleavage by the DpnII endonuclease.
Catalytic Activity: a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32907
Sequence Length: 284
EC: 2.1.1.72
|
P09358 | MKNNEYKYGGVLMTKPYYNKNKMILVHSDTFKFLSKMKPESMDMIFADPPYFLSNGGISNSGGQVVSVDKGDWDKISSFEEKHEFNRKWIRLAKEVLKPNGTVWISGSLHNIYSVGMALEQEGFKILNNITWQKTNPAPNLSCRYFTHSTETILWARKNDKKARHYYNYDLMKELNDGKQMKDVWTGSLTKKVEKWAGKHPTQKPEYLLERIILASTKEGDYILDPFVGSGTTGVVAKRLGRRFIGIDAEKEYLKIARKRLEAENETN | Function: A beta subtype methylase that recognizes the single- or double-stranded sequence 5'-GATC-3', methylates A-2 on one or both strands (respectively), and protects the DNA from cleavage by the DpnII endonuclease. Further methylates DNA that is already methylated at 5'-GATC-3' sites. Essential for establishment of a previously unmethylated plasmid transformed into the cell as single-stranded DNA, enhances plasmid transfer to DpnII-containing strains of Streptococcus pneumoniae.
Catalytic Activity: a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 30922
Sequence Length: 268
EC: 2.1.1.72
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Q9H903 | MTVPVRGFSLLRGRLGRAPALGRSTAPSVRAPGEPGSAFRGFRSSGVRHEAIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTDGEHERPGGDATVTIAHRYTPKEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDPVTGKTKLVGDVDFEAVKKKAGFITPVPGGVGPMTVAMLLKNTLLAAKKIIY | Function: Bifunctional mitochondrial folate-interconverting enzyme that has both NAD/NADP-dependent methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase activities.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NAD(+) = 5,10-methenyltetrahydrofolate + NADH
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37315
Sequence Length: 347
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Mitochondrion inner membrane
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D3ZUA0 | MATRARGLSLLRGRLGRGPARAPGVAERAWRGFGSSSRRHEAVIISGTEMAKQIRRELQQGVESWLALGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELIVKPKNVSQEELLDITDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKNVGMPIAMLLHTDGEHERPGGDATVTIAHRHTPREQLKAHTQLAEIIIVAAGIPGLITADMVREGATVIDVGINYVQDPVTGKTKLVGDVDFEAVKKKASFITPVPGGVGPMTVAMLLKNTLLAAKNITY | Function: Bifunctional mitochondrial folate-interconverting enzyme that has both NAD/NADP-dependent methylenetetrahydrofolate dehydrogenase and methenyltetrahydrofolate cyclohydrolase activities.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 36426
Sequence Length: 338
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
Subcellular Location: Mitochondrion inner membrane
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P25265 | MVGAVIDLFCGVGGLTHGLILEGFGVLAGIDNDPSCKYAYEQNNRTRFIEKSISEVDGRELNALYPNNQHKILVGCAPCQDFSQYTKKSRTGTKWQLLTEFSRLIREIEPDIISMENVPEVRTFNRGEVFNNFIQSLEQLGYHVSHSVVHCPDYGIPQQRDRLVLFAAKQGVIKIIPPTHTPENYRTVRDVIGSLATNYSGGHWEGDSMHAASRLEDINLRRIQHSVPGGTWADWPEELIAECHKKESGESYGSVYGRMEWDKVAPTITTQCNGYGNGRFGHPEQDRAISLREAALLQTFPRSYQFAPEGQLKFKTVSRQIGNAVPVALGRVIAKSIKRFLEGLHERQRVRIII | Function: A methylase that recognizes the double-stranded sequence 5'-GTCGAC-3', methylates C-? on both strands and protects the DNA from cleavage by the HgiDII endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39853
Sequence Length: 354
EC: 2.1.1.37
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P55818 | MSKKLLFQFDTDATPSVFDVVVGYDGGADHITGYGNVTPDNVGAYVDGTIYTRGGKEKQSTAIFVGGGDMAAGERVFEAVKKRFFGPFRVSCMLDSNGSNTTAAAGVALVVKAAGGSVKGKKAVVLAGTGPVGMRSAALLAGEGAEVVLCGRKLDKAQAAADSVNKRFKVNVTAAETADDASRAEAVKGAHFVFTAGAIGLELLPQAAWQNESSIEIVADYNAQPPLGIGGIDATDKGKEYGGKRAFGALGIGGLKLKLHRACIAKLFESSEGVFDAEEIYKLAKEMA | Function: Catalyzes the dehydrogenation of methylene-H(4)MPT. Can also catalyze the reversible dehydrogenation of methylene-H(4)F with 20-fold lower catalytic efficiency.
Catalytic Activity: 5,10-methylenetetrahydromethanopterin + NADP(+) = 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + NADPH
Sequence Mass (Da): 29736
Sequence Length: 288
Pathway: One-carbon metabolism; formaldehyde degradation; formate from formaldehyde (H(4)MPT route): step 2/5.
Subcellular Location: Cytoplasm
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O85012 | MARSILHMLTPLKHMSPFDVNMAIDAGFETLIPYTGVDLTDVVSLTQDSIFSRAPQDGVRTGIFIGGKNAELALDMVDRAKKAFVPPFVNHVFADPAGSFTTGAAMVAEVNRALKARFSTDLKGKRIVIFGGAGVVAYVAAVIGALEGAQTVLVGHDGEERVSKIAFTMKWRFGIDVGAVDGTLPEARRAAITDADVILSAGPAGVSILTAEDLESAPKLLVASDVNAVPPAGIAGIDVNAVDVPLPTGKGVGIGALAVGNVKYQTQCRMFRKMLEAQEPLCLDFRDAYKLAVEIAG | Function: Catalyzes the dehydrogenation of methylene-H(4)MPT.
Catalytic Activity: 5,10-methylenetetrahydromethanopterin + NAD(+) = 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + NADH
Sequence Mass (Da): 31151
Sequence Length: 297
Pathway: One-carbon metabolism; formaldehyde degradation; formate from formaldehyde (H(4)MPT route): step 2/5.
Subcellular Location: Cytoplasm
EC: 1.5.1.-
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Q04448 | MRFTSNMAQIIDGKAIAQEVRTQLAHELKGMEAAGYPKPHLTAVIVGEDPASEKYVANKMVACREVGISSETKRLPASTTQEELLQLIADLNKDPQVTGILVQLPVPEHINERTICNAVDVDKDVDGFNEVNIGRTALDMEANIPATPLGVKRLLEHMKIETLGRNAVVVGRSKNVSLPMAILLHADGKYATKAMDATVTICHRYTPPKELARHCRQADIIVVAVGKPGLITKDMVKPGACVIDVGINRIKDESTGQFKLVGDVDFEEVRQVAGHITPVPGGVGPMTVAMLMHNTLKAARKQFDDRKSS | Function: May play a role in spermatogenesis.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NAD(+) = 5,10-methenyltetrahydrofolate + NADH
Sequence Mass (Da): 33551
Sequence Length: 309
Subcellular Location: Mitochondrion
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P13995 | MAATSLMSALAARLLQPAHSCSLRLRPFHLAAVRNEAVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGENPASHSYVLNKTRAAAVVGINSETIMKPASISEEELLNLINKLNNDDNVDGLLVQLPLPEHIDERRICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDGAHERPGGDATVTISHRYTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVHDPVTAKPKLVGDVDFEGVRQKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRLEEREVLKSKELGVATN | Function: Although its dehydrogenase activity is NAD-specific, it can also utilize NADP at a reduced efficiency.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NAD(+) = 5,10-methenyltetrahydrofolate + NADH
Sequence Mass (Da): 37895
Sequence Length: 350
Subcellular Location: Mitochondrion
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Q1GYH8 | MIKQLFWRGLLLALVLVVLYQFWIFMHILWWVEHNPSSSAFMRASLSALQQDNPDAALKHQWVEYQRISIHLKRAVIAAEDAKFVGHEGFDWDGIQKAYEKNWKQGKIVAGGSTISQQLAKNLFLSTKRTPWRKLEEAVITWMLERMMSKRRIFEIYLNVIEWGNGVFGAEAAARHYYRTSASSLNVAQAARLAAMIPNPRYYDKHREARGLIRKARIIEARMRYAEVP | 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-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 26692
Sequence Length: 229
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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P0A0Z4 | MFRIIKWLIALPVGIFIFFNAYVYGNIITYRAVAPHRTAFMSMRMKQFEQEGRDVALDYRWMPYKRISTNLKKALIASEDARFAGHGGFDWGGIQNAIRRNRNSGKVKAGGSTISQQLAKNLFLNESRSYIRKGEEAAITAMMEAVTDKDRIFELYLNSIEWHYGVFGAEAASRYFYQIPAAKLTKQQAAKLTARVPAPLYYADHPKSKRLRNKTNIVLKRMGSAELPESDTD | 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-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 26603
Sequence Length: 233
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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Q2YBM4 | MFFKRWFWRIFLFFIAVIFVYQFWIFSQIVYWNYFNPSSSAFMQTRLETLREKNTKAALRTRWIPYEQISPHLKRAIIAAEDAKFLEHEGFDFDAIQKAYEKNLKKGRLIMGGSTISQQLAKNLFLSGDKTPWRKLQEAFITLMLEKVMSKRRILEIYLNVIEWGNVVFGAEAAARHYYGISASSVSREQAARLAAMVPSPRFYDENRNTPWLSKKTRMILGRMASASIP | 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-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 27020
Sequence Length: 230
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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Q13U46 | MTATRRVSRPGPVRWMFYLGAVVAIAWLATQAFYFAQIAVWNYVNPRTTSFMRSDAWRLSQDRPDLSVQHTWVPYDQISRNLKRAIIASEDANFVNNNGYETDAILQAWERNKAKGKIVRGGSTITQQLARNLFLSREKSYIRKGQELIITWMLETLMDKERIFEIYLNSVEWGNGVYGAEAAAHYYFKTSASKLTAAQSARLAVMLPQPKYFDEHRGSPYLAQRSRVIARRMGAAELPD | 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-cis-undecaprenyl diphosphate = [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n+1)-di-trans-octa-cis-undecaprenyl diphosphate + di-trans,octa-cis-undecaprenyl diphosphate + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 27552
Sequence Length: 240
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
Subcellular Location: Cell inner membrane
EC: 2.4.1.129
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Q17693 | MTNTGETKVIESHGTIKKIDSLSTMPYCGVETDENAVVEEKITLESGKSWSPKHYELLHERIERLIDEKQQFFSLEFFPPRFVNGVPNFLERVERLSEGGSVFVDMTWHMGSDPANVDKVTSSSSIAASMLDYCGVDTMLHMTCVQYNKADTLKHLEQAKAMGLRSILALRGDLPPGTELEDTHQFRALDMIRWIREEYGNYFSIGCAGYPLGHPQAPSYKADLMYLKAKCDAGANFVITQLFFEAETFEKFVRDCREIGITQPIIPGIMPIMGYESIKRIAKLSQLEIPQHILDDLEPIKHDDDAVQKYGTERCIEMCRRLLDNGTAPSIHLYTMNREGSIREILKSLGLWKLEGDRVFPWKNRSQHPIRCLESVRPIYWSFRPRSYITRTRDWDQFPNGRWGNSSSPAFGDVSSYYLSNLTTVRNADDRLAMFGANIESFEDVKRVFINYITQAPNADGVKVTVLPWTEAETGVQPETSLISEQLVWCNENGILTVNSQPSVNGAPSTDPLVGWGKPGGYCYQKAYLECFMTAELSDKLIQIIEREFPVRVNYHAINKDSTFDKTNSEETTPIAVTWGVFPGSEIAQPTVVDPLSFRAWRDEAYQMWMAQWGDFYPKESKSYGVIKAVHDEFRLVTLVDNDFQKPSVLFDVLQKALDELKK | Catalytic Activity: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADPH
Sequence Mass (Da): 75487
Sequence Length: 663
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 1.5.1.53
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P42898 | MVNEARGNSSLNPCLEGSASSGSESSKDSSRCSTPGLDPERHERLREKMRRRLESGDKWFSLEFFPPRTAEGAVNLISRFDRMAAGGPLYIDVTWHPAGDPGSDKETSSMMIASTAVNYCGLETILHMTCCRQRLEEITGHLHKAKQLGLKNIMALRGDPIGDQWEEEEGGFNYAVDLVKHIRSEFGDYFDICVAGYPKGHPEAGSFEADLKHLKEKVSAGADFIITQLFFEADTFFRFVKACTDMGITCPIVPGIFPIQGYHSLRQLVKLSKLEVPQEIKDVIEPIKDNDAAIRNYGIELAVSLCQELLASGLVPGLHFYTLNREMATTEVLKRLGMWTEDPRRPLPWALSAHPKRREEDVRPIFWASRPKSYIYRTQEWDEFPNGRWGNSSSPAFGELKDYYLFYLKSKSPKEELLKMWGEELTSEESVFEVFVLYLSGEPNRNGHKVTCLPWNDEPLAAETSLLKEELLRVNRQGILTINSQPNINGKPSSDPIVGWGPSGGYVFQKAYLEFFTSRETAEALLQVLKKYELRVNYHLVNVKGENITNAPELQPNAVTWGIFPGREIIQPTVVDPVSFMFWKDEAFALWIERWGKLYEEESPSRTIIQYIHDNYFLVNLVDNDFPLDNCLWQVVEDTLELLNRPTQNARETEAP | Function: Catalyzes the conversion of 5,10-methylenetetrahydrofolate to 5-methyltetrahydrofolate, a cosubstrate for homocysteine remethylation to methionine . Represents a key regulatory connection between the folate and methionine cycles (Probable).
PTM: Phosphorylation of an N-terminal serine-rich phosphorylation region increases sensitivity to S-adenosylmethionine and inhibition.
Catalytic Activity: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADPH
Sequence Mass (Da): 74597
Sequence Length: 656
Domain: Contains a serine-rich phosphorylation region at the N-terminal and an eukaryote-only S-adenosylmethionine (SAM)-binding domain at the C-terminal. Through asymmetric homodimerization, the two regions are positioned next to each other and N-terminal phosphorylation increases sensitivity to SAM binding and inhibition.
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 1.5.1.53
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P29567 | MNMDIASFFSGAGGLDLGFTKAGFNIVFANDNWKGCWKTFEKNHGIKINKKPIEWLKPSEIPDVVGFIGGPPCQSWSLAGSMCGADDPRGKTFYAYVDLVKEKDPLFFLAENVPGIVSRTHLPEFKRLVNSFIDIGYNVEYKVLNAKDYGVPQDRKRVFIVGYREDLNLKFEFPKPLNKKVTLRDAIGDLPEPKPALEKNRSNGENLEVPNHEYMTGTFSSRYMSRNRVRSWDEVSFTIQAGGRHAPCHPQANKMIKVGPDKFIFDPESPKPYRRLSVRECARIQGFPDDFIFYYKNVADGYTMVGNAVPVKLAEELAKKIKKDLEGVLN | Function: A methylase that recognizes the double-stranded sequence 5'-GGCC-3', methylates C-3 on both strands, and protects the DNA from cleavage by the MthTI endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = a 5-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 37360
Sequence Length: 330
EC: 2.1.1.37
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P29568 | MKTTHRIYFKNSADMNELKDKSINLVVTSPPYPMVEIWDRLFSELNPKIEETLIDEEDGLRSYNLMHEELEKVWHEVDRVTAPGGVVIINIGDATRKIGKKFQLYPNHVRTIDFFFDRGYQVLPFIIWRKQSNKPTKFMGSGMLPPNAYVTHEHEYILIFRKEGPRQFKTEEERKLRRESAYFWEERNQWFSDVWTDLTGVSQRLNHKNLRKRAAAYPFELAYRLINMYSIMGDWVLDPFLGTGTTMIAAACAGRNSIGYELDHNFKDLIESRINETLKLSNEIVMRRINDHIEFIREKNGKYYSENYKFKVTTRQEQDIRLYYPRTYKKIKNNEFEFFYQEVNPKKERQSKLNI | Function: A beta subtype methylase that recognizes the double-stranded sequence 5'-CTAG-3', methylates C-1 on both strands, and protects the DNA from cleavage by the MthZI endonuclease.
Catalytic Activity: a 2'-deoxycytidine in DNA + S-adenosyl-L-methionine = an N(4)-methyl-2'-deoxycytidine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42477
Sequence Length: 355
EC: 2.1.1.113
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O97148 | MKTLLVLRISTVILVVLVIQKSYADILECDYFDTVDISAAQKLQNGSYLFEGLLVPAILTGEYDFRILPDDSKQKVARHIRGCVCKLKPCVRFCCPHDHIMDNGVCYDNMSDEELAELDPFLNVTLDDGSVSRRHFKNELIVQWDLPMPCDGMFYLDNREEQDKYTLFENGTFFRHFDRVTLRKREYCLQHLTFADGNATSIRIAPHNCLIVPSITGQTVVMISSLICMVLTIAVYLFVKKLQNLHGKCFICYMVCLFMGYLFLLLDLWQISISFCKPAGFLGYFFVMAAFFWLSVISLHLWNTFRGSSHKANRFLFEHRFLAYNTYAWGMAVVLTGITVLADNIVENQDWNPRVGHEGHCWIYTQAWSAMLYFYGPMVFLIAFNITMFILTAKRILGVKKDIQNFAHRQERKQKLNSDKQTYTFFLRLFIIMGLSWSLEIGSYFSQSNQTWANVFLVADYLNWSQGIIIFILFVLKRSTWRLLQESIRGEGEEVNNSEEEISLENTTTRNVLL | Function: Involved in biological aging and stress response. Essential for adult survival. Required in the presynaptic motor neuron to up-regulate neurotransmitter exocytosis at larval glutamatergic neuromuscular junctions (NMJs). Regulates a step associated with docking and clustering of vesicles at release sites. SP/Acp70A and sun are agonists that activate mth in vitro.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59644
Sequence Length: 514
Subcellular Location: Cell membrane
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Q8TQX8 | MDEEAEVAEIAVLGGVGFNSHKDCESHPVTTPYGRITAYLTSIKGRSVVIIPRHAEEIHIPPHRVNYRGNIWAAHSLGAKRVISTNSVGSMRGHPVGSFVVLDDFIDFTRSRPSTFHDDKTVHVDVSEPYCPEIRASLRYSLEKRGISYTEGVYACTEGPRFETRAEIRMMSQFADVVGMTGVPEVVLAKELSLCYASLSIVTNQACGMTTQKLTADEVTEVVGKAQASIFKILSDAIGKIPETRNCMCRFAKEGACL | Function: Catalyzes the reversible phosphorylation of S-methyl-5'-thioinosine (MTI) to hypoxanthine and 5-methylthioribose-1-phosphate. Involved in the breakdown of S-methyl-5'-thioadenosine (MTA), a major by-product of polyamine biosynthesis. Catabolism of (MTA) occurs via deamination to MTI and phosphorolysis to hypoxanthine.
Catalytic Activity: phosphate + S-methyl-5'-thioinosine = hypoxanthine + S-methyl-5-thio-alpha-D-ribose 1-phosphate
Sequence Mass (Da): 28299
Sequence Length: 258
Pathway: Purine metabolism; purine nucleoside salvage.
EC: 2.4.2.44
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