ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P59436 | MIIRFILSFFTSLLLMLIFGPHLINWLNKYKIQQIIRNFGPKSHFNKKNTPTMGGILIIFSIIISTIIWTKLSNPYVWLTLTILIGYGIIGFIDDNMKIYYKNSKGLSSLHKFSLLSILACIIIFLIYYIINDHSTIKLIVPFSKNIIFNTKMICILISYFAIIGTSNAVNLTDGLDGLAIVPIIFVTTNLSIISFISGNVNLSYYFNTIYIPYSNELTIICAAIIGSSLGFLWFNTYPAQIFMGDVGSLSLGGTIGIISVLLRQEILLIIVGGLFVIETLSVIIQVLYYKITKKKLFKMTPIHHHYELNGCPETRLIIR... | 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 ... |
O25235 | MLYSLLYGYFNINLFQYLTFRAGLGFFIAFFLTLFLMPKFILWAKAKKANQPISSFVPSHQNKKDTPTMGGIVFVFATIVASVLCASLGNLYVLLGLIVLVGFSFVGFRDDYTKINQQSNAGMSAKMKFGMLFILSLIVSVLLSLKGLDTFLYAPFLKNPLFEMPTMLAVGFWVLVFLSTSNAVNLTDGLDGLASVPSIFTLLSLSIFVYVAGNAEFSKYLLYPKVIDVGELFVVSLALVGSLFGFLWYNCNPASVFMGDSGSLALGGFIAYNAIVSHNEILLVLMGSIFVIETLSVILQVGSYKTRKKRLFLMAPIHHH... | 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 ... |
Q0BXT9 | MLYELLAADSGLFNLLNYITFRTGAAVVTAFLVTVLFGDMLINFLRARQGKGQPIRDLSLEMQLSKQGTPTMGGFLIWLGLIVGVALWGNLQNPYVWVTLFVTFSYAILGFLDDYAKVTKQSTDGVSAGARLIAGFGIAALACAIIMGLHGAHTPAGHAEWGPFNPLAEWIAGFAPQTSVEPADPNFSGGVAVPFVNNYFLPLGGFFILFGMIVIVGAANAVNFTDGLDGLAIVPMTFAAAAYAMIAYLTGNFVFASYLGIQFAPGAGELAVLLGALIGSGMGFLWYNAYPAKVFMGDTGSLGLGGMLGVVAVATKHEFA... | 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 ... |
A8GP69 | MLYNLLLPHIHNSHIANLFHYITFRSGLAIIITLSLSFIMGPILIKFLRSLQKNGQPIRSDGPESHQTKAGTPTMGGIMIILSSGLSTLLLADLTNQYIWITLFGFISFGIIGFMDDYAKVTKNNHYGVRGKSKLVLQGIISLIICVLLEYLDKNPSHLLNVPFFKNLNLDLGYFYIVFAIFVIVGSSNAVNLTDGLDGLATVPIAFTAGSFALISYLVGNLIYSHYLQLTYIPNTGELTVLCAGLVGSCLGFLWFNAQPAEVFMGDTGSLSLGGVLGIISVITKHEIVLAIVGGLFVIETASVILQVYYFKATQGKRIF... | 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 ... |
Q8TDS7 | MNQTLNSSGTVESALNYSRGSTVHTAYLVLSSLAMFTCLCGMAGNSMVIWLLGFRMHRNPFCIYILNLAAADLLFLFSMASTLSLETQPLVNTTDKVHELMKRLMYFAYTVGLSLLTAISTQRCLSVLFPIWFKCHRPRHLSAWVCGLLWTLCLLMNGLTSSFCSKFLKFNEDRCFRVDMVQAALIMGVLTPVMTLSSLTLFVWVRRSSQQWRRQPTRLFVVVLASVLVFLICSLPLSIYWFVLYWLSLPPEMQVLCFSLSRLSSSVSSSANPVIYFLVGSRRSHRLPTRSLGTVLQQALREEPELEGGETPTVGTNEMG... | 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 ... |
Q91ZB8 | MNSTLDSSPAPGLTISPTMDLVTWIYFSVTFLAMATCVGGMAGNSLVIWLLSCNGMQRSPFCVYVLNLAVADFLFLFCMASMLSLETGPLLIVNISAKIYEGMRRIKYFAYTAGLSLLTAISTQRCLSVLFPIWYKCHRPRHLSSVVSGALWALAFLMNFLASFFCVQFWHPNKHQCFKVDIVFNSLILGIFMPVMILTSTILFIRVRKNSLMQRRRPRRLYVVILTSILVFLTCSLPLGINWFLLYWVDVKRDVRLLYSCVSRFSSSLSSSANPVIYFLVGSQKSHRLQESLGAVLGRALRDEPEPEGRETPSTCTNDG... | 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 L... |
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 | MAGNCSWEAHPGNRNKMCPGLSEAPELYSRGFLTIEQIAMLPPPAVMNYIFLLLCLCGLVGNGLVLWFFGFSIKRNPFSIYFLHLASADVGYLFSKAVFSILNTGGFLGTFADYIRSVCRVLGLCMFLTGVSLLPAVSAERCASVIFPAWYWRRRPKRLSAVVCALLWVLSLLVTCLHNYFCVFLGRGAPGAACRHMDIFLGILLFLLCCPLMVLPCLALILHVECRARRRQRSAKLNHVILAMVSVFLVSSIYLGIDWFLFWVFQIPAPFPEYVTDLCICINSSAKPIVYFLAGRDKSQRLWEPLRVVFQRALRDGAEL... | 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 | MAGNCSWEAHSTNQNKMCPGMSEARELYSRGFLTIEQIATLPPPAVTNYIFLLLCLCGLVGNGLVLWFFGFSIKRTPFSIYFLHLASADGMYLFSKAVIALLNMGTFLGSFPDYIRRVSRIVGLCTFFTGVSLLPAISIERCVSVIFPTWYWRRRPKRLSAGVCALLWMLSFLVTSIHNYFCMFLGHEAPGTVCRNMDIALGILLFFLFCPLMVLPCLALILHVECRARRRQRSAKLNHVVLAIVSVFLVSSIYLGIDWFLFWVFQIPAPFPEYVTDLCICINSSAKPIVYFLAGRDKSQRLWEPLRVVFQRALRDGAEP... | 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 | MEPLATTLCPQECTQTTRNETPNETTWSSEHVTKYTYISISLVICSLGLVGNGLLIWFLIFCIKRKPFTIYILHLAFADFMVLLCSSIIQLVNTFHIYDSTLVSYAVLFMIFGYNTGLHLLTAISVERCLSVLYPIWYHCRRPKHQSTVACTLLWALSVLVSGLENFFCILEVKPQFPECRYVYIFSCTLTFLVFVPLMVFSNLILFIQVCCNLKPRQPAKLYVIIMATVILFLVFAMPMKVLLIIGYYSNSTDASVWKSLPYLNMLSTINCSINPIVYFVVGSLRRKRSRKSLKEALQKVFEEKPVVASRENEVQFSLP... | 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 | MDPTISTLDTELTPINGTEETLCYKQTLSLTVLTCIVSLVGLTGNAVVLWLLGCRMRRNAFSIYILNLAAADFLFLSGRLIYSLLSFISIPHTISKILYPVMMFSYFAGLSFLSAVSTERCLSVLWPIWYRCHRPTHLSAVVCVLLWALSLLRSILEWMLCGFLFSGADSAWCQTSDFITVAWLIFLCVVLCGSSLVLLIRILCGSRKIPLTRLYVTILLTVLVFLLCGLPFGIQFFLFLWIHVDREVLFCHVHLVSIFLSALNSSANPIIYFFVGSFRQRQNRQNLKLVLQRALQDASEVDEGGGQLPEEILELSGSRL... | 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... |
Q8CIP3 | MDPTISSHDTESTPLNETGHPNCTPILTLSFLVLITTLVGLAGNTIVLWLLGFRMRRKAISVYILNLALADSFFLCCHFIDSLLRIIDFYGLYAHKLSKDILGNAAIIPYISGLSILSAISTERCLCVLWPIWYHCHRPRNMSAIICALIWVLSFLMGILDWFSGFLGETHHHLWKNVDFIITAFLIFLFMLLSGSSLALLLRILCGPRRKPLSRLYVTIALTVMVYLICGLPLGLYLFLLYWFGVHLHYPFCHIYQVTAVLSCVNSSANPIIYFLVGSFRQHRKHRSLKRVLKRALEDTPEEDEYTDSHLHKTTEISES... | 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 mo... |
Q4QXU0 | MDPTTPAWRTESTTMNGNDQALPLLCGKEILISVFLILFIALVGLVGNGFVLWLLGFRMRRNAFSVYVLSLAGADFLFLCFQIINCLVYLSNFFCSSSINFPSFFTTVMTCAYLAGLSMLSTISTERCLSVLWPIWYRCRRPRHLSAVACVLLWALSLLLSILEGKFCGLFGDGDSGWCQTFDLITAAWLIFLFMVLCGSSLALLVRILCGSRGLPLTRLYLTILLTVLVFLLCGLPFGIQWFLILWIWKNSDVLFCHIHPVSVVLSSLNSSANPIIYFFVGSFRKQWQLQQPILKLALQRALQDIAEVDHSEGCFRQGT... | 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 b... |
Q9K2S2 | MQLLHLAILSPFLFAFIIPFLAKYAKRVHTGWFVLILPVLLFIYFLPMIRMTQSGETLRSVLEWIPSLGINFTVYIDGLGLLFALLITGIGSLVTLYSIFYLSKEKEQLGPFYVYLLMFMGAMLGVVLVDNVMVLYMFWELTSLSSFLLIGYWYKREKSRYGAAKSLLITVSGGLCMLGGFILLYLITDSFSIREMVHQVQLIAGHELFIPAMILILLGAFTKSAQFPFYIWLPDAMEAPTPVSAYLHSATMVKAGIYVIARFSPIFAFSAQWFWIVSLVGLFTMVWGSFHAVKQTDLKSILAFSTVSQLGMIISMLGVS... | 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 protei... |
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 protei... |
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 | MTLIRRVAFLSLHTSPMEQPGSGDAGGMNVYVRALASALAASGVEVEIFTRSTSSGQPAVEHPDPGVCVHNVISGPPRKLPKEELPELLHSMVAEIERIRQRQPHGRYDLIHSHYWVSGVAGLELSRLWGVPLVHTMHTMAKVKNLLLQSGEKPEPRRREDGELRIVDGATRLIANTPAEAAELVSHYNADFDHIDVAPPGVDLTVFTPAFRPRSRAQLGVPAGKFHLLFAGRIQRLKGPQVLVKAAALLRSRRPDIDLQVTILGALSGAKDFDLKSLISAAGMDDVVTHHPPVNAPELAGWFRSADVVVMPSYSESFGL... | 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-acetam... |
Q8FSH1 | MRVAMISMHTSPLQQPGVGDSGGMNVYILSTGTELARQGVEVDIFTRATRPSQGEVVQVAPNLRVINIVAGPYEGLAKEELSTQLAAFAGGVLEFTRRGGIEYDLIHSHYWLSGQVGWLMRDLWRIPLVHTAHTLAAVKNSYRADEDTPESEARRICEQQLVDNADVLAVNTQEELADLVHHYDADPDRISVVSPGADIALYTPGNDRATERSRRELGVPLHAKVVAFVGRLQPFKGPQVLIHAVAELLERDPQRNLRVLICGGPSGPSATPETYRNLAVELGVDKRIRFLDPRPPEELVAVYRAADIIAVPSYNESFGL... | 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-acetam... |
D2B7W7 | MNARVEHRGRLDEREVAAVLTVVEAATEADGVRPLNEHVMLHLRYGGDERAGAVLLYVGDDLAGYAHVDPTDPVEGPSGELVIHPAFRGQGHGRHLLEAVLDRTGGRLRLWAHGGHPGAEALALSTGFTKIRSLWQMRRSLFAAIPGFELPDGVRLRTFAPGSPDEEAWVALNAKAFAHHPEQGSWTLEDLKRREQEPWFDPAGFFLAERPTGSGDGDVADGGSTDGGPADSGSADGGAGEGGTGDGNRLIGFHWTKVHGDGGHGHEPIGEVYVVGVDPAEQGGGLGRSLTLAGLSHLRARGLAQVMLYVDESNTAAIRL... | 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 | MPVPLQIGPLGPSDVEGVRGLARAAETADGVAPLSEQPLLRLSSDEGWLTHVVARSKAGQVIGYAQVDRGGEDASAELVVHPEHRRAGVGGLLLRTAERDATLPQFGGTAGHHGKRLRVWAHGNLEPARAFAAAAGYVVVRELLFLTKPFPPVVAPVEPTPPVTEPVEPAPPVVEPVEPAPPVVEPVETTSASTSGVVSTGSTTGGGSTTGGGYRVRAFVPGVDDDAWVALNARAFAAHPEQGRLTVADLHDRMAEPWFDPAGFFLAEAPDGTLAGSLWTKVEGDDGEIYAVGVDPAHQGRGLGATLTAVGLDHLATRAR... | 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 | MDHATRAHFTMTVGEVDPLLADALASERGRQQNQIELIASENIVSRAVLDALGHEITNKTLEGYPGNRFHGGGQFVDIAEQAAIDRAKQLFNCGYANVQPHSGTQANLAVFFLLLKPGEKVLSLDLAAGGHLSHGMKANLSGRWFDATNYNVNPQNEVIDLDEMERLAEEIRPKLLITGGSAYPRELDFERMSRIAKKVGAYFLVDMAHIAGLVAGGVHPSPFPHADIVTCTTTKTLRGPRGGLILTNNEEWYKKLQAAVFPGVQGSLHSNVLAAKAICLGEAMLDDFKVYARQVVANAKVLANTLAERGVRIVSGGTDT... | 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-tet... |
B2DEU7 | MNELTRTFFNSSVHDTDPLIAQALDDERARQKNQIELIASENIVSQAVLDALGHEMTNKTLEGYPGNRFHGGGQFVDVVEQAAIDRAKQLFNCGYANVQPHSGTQANLAVFFLLVKPGDRILSLDLAAGGHLSHGMKGNLSGRWFEAHNYNVDPQNEVINYDEMERIAEEVKPKLLITGGSAYPRELDFARMAQIAKKVGAFFMVDMAHIAGLVAGGAHPSPFPHADIVTCTTTKTLRGPRGGLILTNNEEWYKKLQTAVFPGVQGSLHSNVLAAKAICLGEALRPEFRDYVAQVVKNAKVLAETLTSRGIRIVSGGTDT... | 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-tet... |
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 | MGISWFLSRFRIRTVAPSSFLKPRGLVYRPSQIRRRVSLLSLSGFHPYRAYSILGPKTPTAFNSANTVRFFSFSSISRLVFRSLRLPVAGFSLVAGGAAYIGAQVQRASDYTKDIFDKTFGILDSTWEKTRETVASVTNVQLPEISMPLWLEKILRLDEESAERRRVLQAERAKEHRSNSNDKQKSSDNDEDPNDTTVGIGAALAASILSVDSVDGEDTLTADEKRKLAQESKEDRMMLFTKKMIEIRNILQDIQDNNSAVTLPSIVVIGSQSSGKSSVLEAIVGHEFLPKGSNMVTRRPIELTLVHSADTAIPYGEFSG... | 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
Subcellu... |
P28737 | MSRKFDLKTITDLSVLVGTGISLYYLVSRLLNDVESGPLSGKSRESKAKQSLQWEKLVKRSPALAEVTLDAYERTILSSIVTPDEINITFQDIGGLDPLISDLHESVIYPLMMPEVYSNSPLLQAPSGVLLYGPPGCGKTMLAKALAKESGANFISIRMSSIMDKWYGESNKIVDAMFSLANKLQPCIIFIDEIDSFLRERSSTDHEVTATLKAEFMTLWDGLLNNGRVMIIGATNRINDIDDAFLRRLPKRFLVSLPGSDQRYKILSVLLKDTKLDEDEFDLQLIADNTKGFSGSDLKELCREAALDAAKEYIKQKRQL... | 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 mistarge... |
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)... |
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)... |
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)... |
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)... |
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 +... |
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... |
Q7BHL7 | MDKETNDNEYRRQSEHRTSAPKRKKKKKIRKLPIILLIVVILLIALVVYIVHSYNSGVEYAKKHAKDVKVHQFNGPVKNDGKISILVLGADKAQGGQSRTDSIMVVQYDFINKKMKMMSVMRDIYADIPGYGKHKINSAYALGGPELLRKTLDKNLGINPEYYAVVDFTGFEKMIDELMPEGVPINVEKDMSKNIGVSLKKGNHRLNGKELLGYARFRHDPEGDFGRVRRQQQVMQTLKKEMVNFRTVVKLPKVAGILRGYVNTNIPDSGIFQTGLSFGIRGEKDVKSLTVPIKNSYEDVNTNTDGSALQINKNTNKQAI... | 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 | MNSMEIRQAFAGLLTLSMFIMLGNMIKKDHFDYPAEEVEIQTTEVSQHDLATVSHISQKSKQNDKALKPCWNPPTLKEVEQSKGFIIFSLTNGPEYHIAQVADAVVVAKYLGATLVLPDIKNSKSGNSMNLGDIYDVENVLNKLNGLVKVTKTLPPHVSTRNTPIVRVPNKVSQDYIMKKLKPIYQAKGIIKIESYFPSKNTISRNNNSLESLLCQTMFGGTLELKKEIQEEAESIVQKLETWSQESNGPFVAVDLRIEGLKNECNGKDGKGRKQCYQGHEIGEFLKRIGFGQETVIYVTQTKWSPDLNSLRYMFPKTYT... | 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 Len... |
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):... |
Q81F14 | MKTTYVNATIVTMNEQNEVIENGYIIVENDQIIDVKSGEFANDFEVDEVIDMKGKWVLPGLVNTHTHVVMSLLRGIGDDMLLQPWLETRIWPLESQFTPELAVASTELGLLEMVKSGTTSFSDMFNPIGVDQDAIMETVSRSGMRAAVSRTLFSFGTKDDEKKAIEEAEKYVKRYYNESDMLTTMVAPHSPYTCSTELLEECARIAVENQTMVHIHLSETEREVRDIEAQYGKRPVEYAASCGLFKRPTVIAHGVVLNDDERAFLAEHDVRVAHNPNSNLKLGSGIANVKAMLEAGIKVGIATDSVASNNNLDMFEEMRI... | 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-hom... |
Q8R9L4 | MNLLIKNVNLLSMEEDKVLEGVNVYVEGDTIKHIGELLPDVKVDVVIEGKDKLAMPGLINAHTHLGMSLFRNYANDVPLFDWLTKYIWPLEARLTAEDVYWGSLLSMIEMIYSGTTTYCDMYFFMEEVAKATEEIGIRGVISRGIIEEQDAKVNEEKLKDTENLYNAWNGKAEGRIKVMVGPHAPYTCGPTYLKEILDLAKRLGTGIHIHVSETKREVEESLEKYGKTPVQHLKDLGIFEVPTVAAHCVHLTDEDIEVLKEMKVSPVYNPTSNLKLASGFAPVEKMLKKGINVALGTDGPASNNNLNMFEEIHFAATINK... | 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-hom... |
A4XJI3 | MDLLIKGATIITLDGENEVLKGDILIENGKISEISQSIELSKEKMFATKVINAENLIALPGFINAHTHCGQTILRSYADDLPLYEWLFEKIFPAEEKLTKEIVYYSSLLGIAEMLKCGTTMFFDMYFHEDMTAKAALETGIKAVLSRGLQTDERQQQRLDETKELIYNYSSDKIKVFFGPHSVYTCSYELLEKVAELSEEFNTGIMIHLSESEDEVNQCYEKYDMSPVKLCQKAGLFTRPCIAAHCVYVDDEDIEILAENGVTAVYNPTSNLKLGNGFAPVFNLIKSGVNVAIGTDSAASNNNLNILEEIHIAALLEKGM... | 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-hom... |
Q3AC64 | MVNELTILIKNTTVLDLNKFAAVENDILIEGNKISKIGVDIEVNDKENLKIIDGSNKVALPGLINGHTHVAMTLFRGASDDLPLMDWLNNVIWPSESRLTGEDVYWGSLLGIVEMIKSGTTTFCDMYFFMDEVAHAVEQSGIRAILSRGMVALDPENGEKGLKESIDFIEKWQGKANGRITTALAPHAPYTCPPEFLKDVIWEAKRLNVPINIHISETLDEISIIKERYGTTPVRHLESLGLFEVKTIGAHLVHVDDEEIQILKRYQVGAIHNPQSNMKLASGIAPVAKMLEAGVLVGLGTDGAASNNDLDMIEELRAAS... | 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-hom... |
Q891Y7 | MSILIENVMIVTMDEEQDVIKEGYILIKEDKIKEVNLGAYLGNKENLYIINGEGRCAIPGLVNAHTHAGMTIFRGYGEGLPLMRWLNEKIWPIESKLKGEHVKIATELAALEMLRSGTTCFNDMYFYEEQVVKVAKEFNIRGIIGVSIMGDSWEHQLKEAIDIDKKIKEDKSGLLDSMIAPHSPYTLSKEALESIGKEAKLQNKNIHIHISETQDEVNIIKEKYNKTPCEFLQSVGIFNSKVAAAHCVYLTDEDMNILKQNGTSVIYNPQSNMKLASGIAKIAEMIDMDINVCLGTDGTSSNNNLNMIEEMETGTILQKL... | 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-hom... |
B1I2P4 | MRLLIRNAYVIPVAGSDFTGDVAVEEGRIVFAGPTGAVPGTFEADETIDATGMVATPGLVNCHTHAAMTLFRGYADDLPLMEWLTRKIWPVENLLTGDDIYWGSLLAGLEMLKSGTTTFADQYFEMDRVAQAVEEIGLRASLCRGLIGVSEHAEKALAEGCEFVRRWHGAAAGRISAMLGPHAPYTCPPAYLKKVVAASEELDVGLHIHLSETRTEIEQIKAEYGCSPIALMEETGLFHRPVLAAHCVHLSEADIKILARRGVGVAHNPQSNMKLASGIAPVVRMLAAGVRVGIGTDGAASNNDLNMVEEMRTAALLQKV... | 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-hom... |
A4J675 | MNRLLIRGATILTMEGPEAIIETGELLIEDGWITHVGLPGSASGSFDMDEVIEADGQVAMPGFINCHTHAAMTLLRGYADDLPLMTWLSEKIWPFEGRMTNEDIYWGTMLACLEMIKSGTTCFGDMYDCMHDVARAVEKTGMRAMLSRGMIGIAPTADKALIEAEELARNWNGKADGRITVMVAPHAPYTCPPDYLDKAMNLAAKHKLGINIHLAETLTEFEDIKKQYGKTPVKHLDQLGLFKLPVLAAHCVHLDEEDMDILAQKAMGVAYNPQSNMKLASGIAPVAKLLELGATVGIGTDGTASNNNLDMLEELRAGSF... | 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-hom... |
Q72B14 | MPLPCDTILQAALIVTQDDARTVIEDGAIAIHEGRIAAVGQRDAIVGNWHGVTVIDMGESLIMPGLVNAHTHASMTLLRGLADDLPLMDWLTGHIFPVEKGLTGELVELGALLGCAEMLRTGTTAFSDMYLIEDATLRAVDRAGLRCLAGEAIFAFPSPAYADPETAFDLVRAQHDRWKHHARAALAVAPHAVYTSTPAILARCRDLAEELGLPIHLHLAETATETAQCIEQHGARPVPYCDGLGLLTPRTTLAHCVDLTEGEIDLLAERGVTVAHCPESNMKLASGIAPATAMLGRGMTLGLGTDGAASNNSLNMFTEM... | 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-hom... |
B8E183 | MRILIENVSVFQEGDILNNKNILIENDIIKEISEDKNFEKIDYVIEGKNKIALPGLVNTHTHLAMTLFRGFADDLPLKEWLEEKIWPQEAKLTAEDVYWGSLLGICEMIKGGTIAFADMYFFMDEVAKAVSESGVKASLSVGMIGVSGNENEILNRGVNFAQNWHNAENGRIKVMLAPHAPYTCPPSFLEKVINKAVEMNLSIHTHLSETYLEVENIKNIYGLTPVRLMDRIGLFNVPVLAAHCVFVDDEEIEILSEKGVGVAHNPQSNLKLASGVAPVKKMVEKRVKIGLGTDGPASNNNLDLWEEIRLVATLHKGVEK... | 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-hom... |
Q9KC82 | MGTIVKNVSIVTGQAEAPFIRHGYFKFADGVIVSVAEGTPSPEEIDRVEVIDGKGKWVMPGMINTHGHLGMSLLRGHSDDLPLQSWLTEKMWPFEGKMDREAVHHARQLAMAEMIKSGTTTFLEMYHLYMDDLAEAVVEQGPRAVLMRSMIGLCSESEQREKLKEAVTFATTWNGDGNGRITTMMAPHAPYTCPPSFIEMIVDEADRIDLPLHTHMAETQREVEEHRKTYGVHPLVHFEQLGFLKDRHWLLAHCVHLGEEELDILEQHPSVHVSHNPMSNLKLGSGIANVQSMLERGINICLGTDSVASNNHLDLVEEMR... | 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-hom... |
B8CX03 | MKILIKNVDVIYTADSNRSIIKNGYIIIQDNKIKEINDMDNLVYQSNDFDDVISGKGKMALPGLVNAHTHSAMTLLRGFADDMPLHKWLQEKIWPFEKTLIPEDIYWGAKLAILEMIKTGTTTFADMYFEMGQVAKVVEEGGLRAVLSQGLIEANDGEEGLNRALKFCLEWNNRADGRILTMLAPHAPYTCSPDFFRRVVDLSQEYNLGIHTHIAETKEEFQQIREKYDCTPLQYLEKTGALKRPVLAAHCIYITEEDMDLMAQKPIGVAYNPQSNMKLGSGIAPVTRMLSKGIKVGIGTDGTSSNNNLDLIEEARSGSF... | 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-hom... |
P23941 | MRFFSVFDIVKNKANQLGYTETEMYAVLKNYNVNKKDLLAYKENGVIPTDKVLNGILSYLGMTKVELELKLGRIPAGLEDVFLNNTKEIAKILENKNSVKLNEFNSIQEIKPYFYTDLGKLYNGDCLELFKQVPDENVDTIFADPPFNLDKEYDEGVTDKNSFSGYLDWYYKWIDECIRVLKPGGSLFIYNIPKWNTYLSEYLNRKLNFRNWITVDMKFGLPIQNRLYPANYSLLYYVKGDKPKTFNVQRIPLQTCPHCGREIKDYGGYKNKMNPKGVTLSDVWSDIYPVRHSSSKNRKFNELSVKLLDRIITMSTNEGD... | 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-h... |
O68556 | MNNHSYLKKNSFHEGDARELLKCIEEESIALSVWSPPYHVGKKYEEGQTYEQWSSLLTKVIALHYPILKPGGFLVINIDDILAFPDPRMPRFQAVNLKKHRVSVTREDILNALKLEPELTKYQLAKKFNCSEQTIERRLKGNNIRGGKYNVQTKVKLAGPVLEKAAEEAGLYLYDRRIWAKDPAWQNSQWHSNSYKAVSEFEHLYIFWKPGETVIDRNKLSKEEWASWASRGIWYIPSVRKNDDHEAKFPLLLPQRLIKLLTQKGDTVLDCFMGSGTTAVAALSESRNFIGIEKEPKYIQLSNKNVETFYISRNKEASKI... | 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... |
P0DW08 | MIVIDLFSGAGGLSEGFHKHDFKIAAHVEKEYWACETIKTRLFYHFLKAQNDLELYHEYLRVSDNYRNIEQSRAFVFQRYPELREKLEMEVLNRKFGNPHNDPTATSSTQMIQLIQNSLQYSRATSVDLIIGGPPCQAYSLVGRSRMKDSVGKDSRNYLFQYYKRIVDEFKPKAFVFENVPGILTAKQGKVYQEIKESFDQIGYTVLSGTSQEDRSNVIDFADFGVPQRRKRVILFGFQKKLNYEYPNFERHKLSWNSPLTTRDVISDLPVLKPKQGHDLRLFEYDTTQGVDQLSPYELMMREDSIGFTNHFARPIKERD... | 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 resist... |
Q9LAI2 | MNWIFNTLIQFLEDLNIDPSVVSLIDEDAKKLEEQFPKALKHPVVDEEIVYKILCEKYNLNALNVKTISETLNKEYKFGRNSKTALKKYLDYGKEEYLIQFFNTLMLENNTYIDREYIESVLAFCEPVSKEKIKNEFIKLWNEANEVNEYGKLKDYLLGIYSKLFSMGLENLRLIEIYNSNESLIKKVFKYESTIKELKEYCLSNQESITAGLAIKMFNEKYMELMKKEYQQDAIALKLEEHMNQLYVDNNINEYPYIFDRGNDILLLPTEEYDFVYFHIDQDFFNRFQDENKFLDYVLSSIKQIYRVLANEKVFALKID... | 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-... |
P34905 | MKFRKGELFCGPGGLALGAKEAKYMHPETGEVFEFEHAWANDIDEWACETFRTNICPDRPDSVVCGDVRELDIKSLGEKFGEIDAFTFGFPCNDYSIVGEHKGMEGNYGPLYSYGVKILNEYNPLVFIAENVGGLQSANEGKAFLGILNDLASAGKYGYKLVPHLYKFEEYGVPQRRHRIIIVGIRKDQDVAFRVPEPTHKEKYRTASEALADIPEDALNHEFTRHKKKVVEMLNHIAPGGNAWSESIPEELRLNVKKVRMSQIYRRLHPDQPSYTVTGSGGGGTHGYHWEEPRALTNRERARLQTFPDDYEFIGKKEMV... | 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
Sequenc... |
P10283 | MKVLSLFSGCGGMDLGLEGGFLAHRSSINSDLYASYISDHDENYVYLKKTGFETVFANDILPFAKLAWCNFFKNRVNQPENIFHLESIVDVVNNIENKQFSFPNDIDVVTGGFPCQDFSFAGKRKGFDSHKDHNGIIYNEPTEATRGQLYLWLKKVVEITKPKVFIAENVKGLVTLGDVKDIIQKDFRNIDDGYVVLDAQVLNAKNYGVAQNRERVIFIGISKRYANKKILDELISLQEKSEVYPYPPYTHGTDPELKPYATLNQILAHLPEPELASTDKSQQSYSKAKLFKKTQGNIEVNMNGQAPTIRAEHHGNIEFR... | 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... |
P70986 | METVQMSLDLQPEDTKANIECSSPDYEIKCFSHNQFAPQIERLKIEKKYIHIVEETETFNRKLVSYQANKNQSIHNWIRYKEGFSSELVQNLIEEFGLSKGDTILDPFLGSGTTSLTAKMLGINSIGIDILPISHIAFEPKSFIFEYNLEELDRAYKEIYEISPTKIEQKFNHLSITEGAFPEETENDLLFFTHWDNNSQYSYQTKTLIKLILVSILEEISYTRKDGQYLRWDYRSQKVIETNKKRLEQGKEPIKTILDKGELPTVKESLLNTLLTIKEDIKEIQQKCLPNESVHELIKDSALNALPKINDNTFDAVITS... | 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-adenos... |
P25262 | MQQFRFIDLFAGIGGFRLGLEAVGGVCVASAEIDQQAIKVYRQNWPTDGVDHNLGDITAIQQLPAHDVLVGGVPCQPWSIAGKNQAFDDPRGQLWADVIRLVQINQPKAFIFENVKGLVDPRNRLCLEIILDSFKDLGYSVFYKLLNSFDFGVAQNRDRVFIVGIQQKLDLNGFSFPEYTESEQRLYHILDNLEVPETKLESIPIQRNLFGERIDVGYNKLTPRGAFNDFFILNDIRNGPTSIHSWEIYPTTEREKQICMIIMRNRRNSRYGDCDGNPMSYQDIAELVAGLAEKELQTLVEKRILRQYPDGKYEFFNRRL... | 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'... |
P13906 | MAIKINEKGRGKFKPAPTYEKEEVRQLLMEKINEEMEAVATATSDISNDEIQYKSDKFNVLSLFCGAGGLDLGFELAGLEQSLGTDKALEAFKDRDVYNAIRHESVFHTVYANDIFSEALQTYEKNMPNHVFIHEKDIRKIKEFPSANLVIGGFPCPGFSEAGPRLVDDERNFLYIHFIRCLMQVQPEIFVAENVKGMMTLGGGEVFRQIVEDFGAAGYRVEARLLNARDYGVPQIRERVIIVGVRNDIDFNYEYPEITHGNEEGLKPYVTLEEAIGDLSLDPGPYFTGSYSTIFMSRNRKKKWTDQSFTIQASGRQAPI... | 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-met... |
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
Seque... |
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)-me... |
Q45489 | MSEDQYKQIKLHLGMEDDNEDLPNHIPSSFPKQHLNKIYNGDTMNMLLDIPDNSVDLVVTSPPYNINKFKNDRRPLEEYLKWQTEIIEQCHRVLKPSGSIFWQVGTYVNDSGAHIPLDIRFFPIFESLGMFPRNRIVWVRPHGLHANKKFAGRHETILWFTKTPEYKFFLDPIRVPQKYANKKHYKGDKKGELSGDPLGKNPGDVWAFRNVRHNHEEDTIHPTQYPEDMIERIVLSTTEPNDIVLDPFIGMGTTASVAKNLNRYFYGAEIEKEYVDIAYQILSGEPDENNNFPNLKTLRQYCEKNGIIDPSQYTFTRQRK... | 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-h... |
P22772 | MELTIEEMLIKQKETGAHYTPTDLGDIIAKRLINELKKSGISGTKKIRGLDPSCGDGELLLSLNRMGKFNNIDNIELIGIDEDKEAIKEADFRLNEMGINDAKLSGGDFLDMVDLEGNLSLFDDDLSKIEPVDLIIANPPYVRTQVLGADRAQKLAKLFNLKGRVDLYHAFLVAMTLQLKPGGLIGVITSNKYLANTTGESIRQFLAENYDIIEIMDLGDTKLFSGAVLQAIFFGTKKLNKGIRQTAPANFYKIYEETDPSKTEVSIKFETLFGLLESSNTGVFNVDEKFYSVSCGKLIVPDSFKEPWVMATDEEYNWIT... | 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... |
Q59605 | MQQIKFIDLFSGMSGIRKGFEQACRKQSVACECVFTSEIKPAALEVLKQNYPDEVPYGDITKIETGDIPDFDILLAGFPCQAFSFAGKRLGFEDTRGTLFFDVARILKAKKPKGFILENVEGLVTHDRKDSTQKIGRTLTVILETLEALGYYVSWKVLNAKEFGIPQNRKRIYLTGSLKSKPDLSFETSPSPKLKNILESGLPTESSPFIKKLLKKFPPSELYGKSVKDKRGGKNNIHSWDIELKGAVTEEEKQLLNILLKERRKKNGLQKIGIDWMDGMPLTKAQISTFYKHPDLQNILDSLTDKGYLVLEHPKQKIGG... | 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
Seque... |
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
Se... |
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-adenos... |
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... |
Q9H903 | MTVPVRGFSLLRGRLGRAPALGRSTAPSVRAPGEPGSAFRGFRSSGVRHEAIIISGTEMAKHIQKEIQRGVESWVSLGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELILKPKDVSQEELLDVTDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRTGIQTFGKNVVVAGRSKNVGMPIAMLLHTDGEHERPGGDATVTIAHRYTPKEQLKIHTQLADIIIVAAGIPKLITSDMVKEGAAVIDVGINYVHDPVTGKTKLVGDVDFEAVKKKAGFIT... | 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 To... |
D3ZUA0 | MATRARGLSLLRGRLGRGPARAPGVAERAWRGFGSSSRRHEAVIISGTEMAKQIRRELQQGVESWLALGNRRPHLSIILVGDNPASHTYVRNKIRAASAVGICSELIVKPKNVSQEELLDITDQLNMDPRVSGILVQLPLPDHVDERTICNGIAPEKDVDGFHIINIGRLCLDQHSLIPATASAVWEIIKRAGIETFGKNVVVAGRSKNVGMPIAMLLHTDGEHERPGGDATVTIAHRHTPREQLKAHTQLAEIIIVAAGIPGLITADMVREGATVIDVGINYVQDPVTGKTKLVGDVDFEAVKKKASFITPVPGGVGPM... | 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 ... |
P25265 | MVGAVIDLFCGVGGLTHGLILEGFGVLAGIDNDPSCKYAYEQNNRTRFIEKSISEVDGRELNALYPNNQHKILVGCAPCQDFSQYTKKSRTGTKWQLLTEFSRLIREIEPDIISMENVPEVRTFNRGEVFNNFIQSLEQLGYHVSHSVVHCPDYGIPQQRDRLVLFAAKQGVIKIIPPTHTPENYRTVRDVIGSLATNYSGGHWEGDSMHAASRLEDINLRRIQHSVPGGTWADWPEELIAECHKKESGESYGSVYGRMEWDKVAPTITTQCNGYGNGRFGHPEQDRAISLREAALLQTFPRSYQFAPEGQLKFKTVSRQ... | 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
S... |
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... |
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)... |
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 | MAATSLMSALAARLLQPAHSCSLRLRPFHLAAVRNEAVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGENPASHSYVLNKTRAAAVVGINSETIMKPASISEEELLNLINKLNNDDNVDGLLVQLPLPEHIDERRICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDGAHERPGGDATVTISHRYTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVHDPVTAKPKLVGDVDFEGVRQKAGYITPVPGGVGPMTVAML... | 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-c... |
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-c... |
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-c... |
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-c... |
Q17693 | MTNTGETKVIESHGTIKKIDSLSTMPYCGVETDENAVVEEKITLESGKSWSPKHYELLHERIERLIDEKQQFFSLEFFPPRFVNGVPNFLERVERLSEGGSVFVDMTWHMGSDPANVDKVTSSSSIAASMLDYCGVDTMLHMTCVQYNKADTLKHLEQAKAMGLRSILALRGDLPPGTELEDTHQFRALDMIRWIREEYGNYFSIGCAGYPLGHPQAPSYKADLMYLKAKCDAGANFVITQLFFEAETFEKFVRDCREIGITQPIIPGIMPIMGYESIKRIAKLSQLEIPQHILDDLEPIKHDDDAVQKYGTERCIEMCR... | 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
|
P42898 | MVNEARGNSSLNPCLEGSASSGSESSKDSSRCSTPGLDPERHERLREKMRRRLESGDKWFSLEFFPPRTAEGAVNLISRFDRMAAGGPLYIDVTWHPAGDPGSDKETSSMMIASTAVNYCGLETILHMTCCRQRLEEITGHLHKAKQLGLKNIMALRGDPIGDQWEEEEGGFNYAVDLVKHIRSEFGDYFDICVAGYPKGHPEAGSFEADLKHLKEKVSAGADFIITQLFFEADTFFRFVKACTDMGITCPIVPGIFPIQGYHSLRQLVKLSKLEVPQEIKDVIEPIKDNDAAIRNYGIELAVSLCQELLASGLVPGLHF... | 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 reg... |
P29567 | MNMDIASFFSGAGGLDLGFTKAGFNIVFANDNWKGCWKTFEKNHGIKINKKPIEWLKPSEIPDVVGFIGGPPCQSWSLAGSMCGADDPRGKTFYAYVDLVKEKDPLFFLAENVPGIVSRTHLPEFKRLVNSFIDIGYNVEYKVLNAKDYGVPQDRKRVFIVGYREDLNLKFEFPKPLNKKVTLRDAIGDLPEPKPALEKNRSNGENLEVPNHEYMTGTFSSRYMSRNRVRSWDEVSFTIQAGGRHAPCHPQANKMIKVGPDKFIFDPESPKPYRRLSVRECARIQGFPDDFIFYYKNVADGYTMVGNAVPVKLAEELAKK... | 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
Seq... |
P29568 | MKTTHRIYFKNSADMNELKDKSINLVVTSPPYPMVEIWDRLFSELNPKIEETLIDEEDGLRSYNLMHEELEKVWHEVDRVTAPGGVVIINIGDATRKIGKKFQLYPNHVRTIDFFFDRGYQVLPFIIWRKQSNKPTKFMGSGMLPPNAYVTHEHEYILIFRKEGPRQFKTEEERKLRRESAYFWEERNQWFSDVWTDLTGVSQRLNHKNLRKRAAAYPFELAYRLINMYSIMGDWVLDPFLGTGTTMIAAACAGRNSIGYELDHNFKDLIESRINETLKLSNEIVMRRINDHIEFIREKNGKYYSENYKFKVTTRQEQDI... | 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... |
O97148 | MKTLLVLRISTVILVVLVIQKSYADILECDYFDTVDISAAQKLQNGSYLFEGLLVPAILTGEYDFRILPDDSKQKVARHIRGCVCKLKPCVRFCCPHDHIMDNGVCYDNMSDEELAELDPFLNVTLDDGSVSRRHFKNELIVQWDLPMPCDGMFYLDNREEQDKYTLFENGTFFRHFDRVTLRKREYCLQHLTFADGNATSIRIAPHNCLIVPSITGQTVVMISSLICMVLTIAVYLFVKKLQNLHGKCFICYMVCLFMGYLFLLLDLWQISISFCKPAGFLGYFFVMAAFFWLSVISLHLWNTFRGSSHKANRFLFEHR... | 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/A... |
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 hypo... |
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