ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q6NFN4 | MNNAPIGIFDSGVGGLTVARVIMEQLPNESVIYIGDTANSPYGPKPIAQVRELSLAIGEELVRRGCKMIVIACNTATSAALRDLRERFDVPVLGVILPAVRRAVSTTRNGKIGVIGTEGTIKSGAYQELFAASPSVEVHAQACPSFVSFVERGITSGRQILGVAQGYVEPLQAAGVDTLVLGCTHYPLLTGVIQLAMGDRVTLVSSAEETAKDVFKTLSMTDMLASEDSTPVRTFESTGDPVLFAQLAERFLGPHVTNVEKFAGM | Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Catalytic Activity: L-glutamate = D-glutamate
Sequence Mass (Da): 28097
Sequence Length: 265
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 5.1.1.3
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Q8FMU6 | MIERPIPGADAPIGIFDSGVGGLTVARTIIDQLPHESIIYIGDTANGPYGPLPIARVREHALRIADELVERGCKMIVIACNTASAAFLRDARERYDVPVVEVILPAVRRAVAATRNGKVGVIGTVGTINSGAYQDLFAASPSIEVHAAACPRFVDFVERGITSGRQILNIAEGYLEPLQAQGVDTLVLGCTHYPLLSGVIQLAMGDHVTLVSSAEETAKDVLRILSQNDLLADPTMHPTPTYSFESTGDPELFSQLSRRFLGPVVTQIRHNMV | Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Catalytic Activity: L-glutamate = D-glutamate
Sequence Mass (Da): 29305
Sequence Length: 273
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 5.1.1.3
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Q9XDZ7 | MIERPVPGADAPIGIFDSGVGGLTVARTIIDQLPHESVIYIGDTANGPYGPLPIAKVREHAIRIADELVERGCKMIVIACNTASAAFLRDARERYSVPVVEVILPAVRRAVASTRNGKVGVIGTVGTINSGAYQDLFSASPSIVVNAVACPRFVDFVERGITSGRQILNIAQDYLEPLQAEGVDTLVLGCTHYPLLSGVIQLAMGDHVSLVSSAEETAKDVLRILSQQDLLADPDMHPEPSYSFESTGDPEIFAQLSRRFLGPIVSQVRQNEG | Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Catalytic Activity: L-glutamate = D-glutamate
Sequence Mass (Da): 29230
Sequence Length: 273
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 5.1.1.3
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Q46Z37 | MPNVNPAPIGVFDSGLGGLSVLREIRALLPHESLLYLADSKYAPYGEKPEAFVQARTLQACEWLLAQGCKALVIACNTATGHAVELLRQTLPVPIIGVEPGLKPAAAASQSKVVGVLATANTLKSGKFARLLASLDGESRFICEAGLGLVPLIEQGDIDGPDIRGRLDNYLTPMLEAGADTLVLGCTHYPFLSDTIRDMVGNQLTLVDTGSAIARQLARKLVEHDLAVAPGAVPQDRFVSTKDAAHLRQMAAALLHIETQAETVAIEPAPAF | Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Catalytic Activity: L-glutamate = D-glutamate
Sequence Mass (Da): 28759
Sequence Length: 272
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 5.1.1.3
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Q9RU10 | MPPVSFAAASDPAPRSALPIGVFDSGAGGLSVLAELQRALPQEDVLYLADTAHVPYGARSDEDIRDLTARAVAELVRRGVKAVVVACNTASAFSLTHLRERFELPIIGLVPAVKPAVAATKSGVVGVLATPGTLRGTLLADVIRQWAEPAGVRVMQAVSTELVPLVEAGKADSPEARVVLRDVLEPLAEAGADQLVLGCTHYPFLAGSIRAEFGDTFALVDSGAAVARHTRNVLSRGGLLRGGDRTGEVSYLTTSDPAHLRALLMTLRPGGADGASLPDPPSPRIELTTT | Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Catalytic Activity: L-glutamate = D-glutamate
Sequence Mass (Da): 30144
Sequence Length: 290
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 5.1.1.3
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B1I4X2 | MAKGTVGLFDSGVGGLTVVREVSVILPGKRVIYFGDTAHVPYGDKSVDELLSYAERIIGFLCSQGADYIIFACNTSSAVSLRLMRDRFQVPMIGLIEPGAAEAVRLSATGRIGLIATEATVKAGAYARAVSALNRNCQVFSQAAPRLVPLVESGESDTPKAEQAVREYLEPLREQGIDTLILGCTHYPFLRDVIERVLGPEVVLVDPAAATVRAARLDMLRRGFSADNPGAQGEQDTVSLRYFVSGSADAFRAVAGQFLGREPEPVTEICLLR | Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Catalytic Activity: L-glutamate = D-glutamate
Sequence Mass (Da): 29306
Sequence Length: 273
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 5.1.1.3
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A6QBL4 | MRVGVFDSGLGGLTVVQALSRVIKGADIFYVADTKHAPYGEKTPEQILQYSLNITAYFLDEHQIDVLIIACNTATSAAVKTLRERYPELIIIGTEPGIKPALEQTRTKNIGVLATPATLVGEKYQDLVNVLSAKEEVTLYEQACPGLVEQIENGEIESGKTHDMLEGWLHPMRENDVDTIVLGCTHYPLVAHKIEEIMKREMNLIHTGDAIAKRLLALAEEKGYENRGKFSLCIMSTAKIDQEIIKQIIPEYDCFKFISVKTSNF | Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Catalytic Activity: L-glutamate = D-glutamate
Sequence Mass (Da): 29526
Sequence Length: 265
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 5.1.1.3
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Q67SL6 | MTQYIPDTQRPIGLFDSGEGGLTVARAVADLLPQENLIYACDTAHFPYGPRPLAEVRAFFRRFMEFFVEQNCKLVIVACNTATAAAIDLLLADAFPIPALGVVQPGAAMAAEASVTGRIGVAATQGTCDSGIYPQTIRLFRPDAYVVQQACPILVIRAEEGVISGPEVRREVERCLAPILAERVDTLVLGCTHFPHMAKVIQDVVGPAVRLVDPGKATAVQVADLLRRRGLLNPGPGPGQRRAFTTGDPQRFLEVACRLWPGGVDAAAHIHLWSQQE | Function: Provides the (R)-glutamate required for cell wall biosynthesis.
Catalytic Activity: L-glutamate = D-glutamate
Sequence Mass (Da): 29860
Sequence Length: 277
Pathway: Cell wall biogenesis; peptidoglycan biosynthesis.
EC: 5.1.1.3
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Q2S6G3 | MPRMPDSSSLFDELQDLATEQQNPHSTHIDTASVEEILRVINTEDHKVPIAVRRELPHIAEAVEIVVEAFEADGRLFYVGAGTSGRLGVVDASECPPTFGTDPERVQGIIAGGREAVFRSQEGAEDVPERGAQALKGQGVTENDVVCGIASSGRTPFVVGAVEHARDAIGCPTLFVTTIPREELDVDPDVAICPVVGPEVIMGSTRMKSGTAQKLVLNMITTAAMVRLGKVYENMMVDLRRTSEKLVERGIRTVMMVTGVDYDAADAVLTRCDGHVKTALVMILADVEVDEARRRLDATDGFVRPAIEGDE | Function: Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate.
Catalytic Activity: H2O + N-acetyl-D-muramate 6-phosphate = (R)-lactate + N-acetyl-D-glucosamine 6-phosphate
Sequence Mass (Da): 33551
Sequence Length: 311
Pathway: Amino-sugar metabolism; N-acetylmuramate degradation.
EC: 4.2.1.126
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A8GI17 | MNLGALVSETRNPATMGLDEMSTLEMVSCFNQEDRKVPEAIEKVLPAIAQAVDLAAAALKAGGRLIYLGAGTSGRLGVLDASECPPTFGVPHGMVIGLIAGGPGALLKAVEGAEDDAALGEADLVALDLTATDMVVGLAASGRTPYVIGALRYARQLGCPTAAISCNPDSPIAHEVQVAISPVVGPEALTGSTRLKSGTAQKLVLNMLSTGAMVKLGKVYENLMVDVKATNVKLVDRACRIVVEATGAERSQAEAALTQTGFEVKPAILMILAGIDAQEAQQRLQQHDGYLRAALTR | Function: Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate. Together with AnmK, is also required for the utilization of anhydro-N-acetylmuramic acid (anhMurNAc) either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling.
Catalytic Activity: H2O + N-acetyl-D-muramate 6-phosphate = (R)-lactate + N-acetyl-D-glucosamine 6-phosphate
Sequence Mass (Da): 30727
Sequence Length: 297
Pathway: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation.
EC: 4.2.1.126
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Q50559 | MKSSASAPAKAILFGEHAVVYSKPAIAAAIDRRVTVTVSESSSTHVTIPSLGIRHSSERPSGGILDYIGRCLELYHDASPLDIRVEMEIPAGSGLGSSAALTVALIGALDRYHGRDHGPGETAARAHRVEVDVQGAASPLDTAISTYGGLVYLDSQRRVRQFEADLGDLVIAHLDYSGETARMVAGVAERFRRFPDIMGRIMDTVESITNTAYRELLRNNTEPLGELMNLNQGLLDSMGVSTRELSMMVYEARNAGAAGSKITGAGGGGSIIAHCPGCVDDVVTALNRNWKAMRAEFSVKGLI | Function: Catalyzes the phosphorylation of (R)-mevalonate (MVA) to (R)-mevalonate 5-phosphate (MVAP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds such as archaeal membrane lipids.
Catalytic Activity: (R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+)
Sequence Mass (Da): 32225
Sequence Length: 303
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.36
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Q980D2 | MMVEAKVPLKLTLFGEHAVVYDRPAIAMTISESLKVKVSENDKFLIISPSLNIKGVKLDLNEMKIESDEAKKVLRYVFEVLNYFEMKKPVKIEINSTVEPSVGLGTSAAVIVGTVAAYSKYLGIDLSRDEIAKISHNIELKVQGIASRMDTYTETYGGLIYFPAGGKGFEKIDTNFELTAGYIRRSMSTADVLWRVRTLKESNKEVFENILDVIGEITNRAKSLIVEQNFEELGLLMYVNHGLLFSLGITSPEADEIVSRAKQLGIKGCKISGGGAGGSIICIKSVEAEVLLRSYNARIVNSTLTKDGVIFSIL | Function: Catalyzes the phosphorylation of (R)-mevalonate (MVA) to (R)-mevalonate 5-phosphate (MVAP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds such as archaeal membrane lipids.
Catalytic Activity: (R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+)
Sequence Mass (Da): 34542
Sequence Length: 314
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.36
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Q5JJC6 | MSVKRVLASAPAKIILFGEHSVVYGKPAIAAAIDLRTYVSAEFNDTGAIKIEAHDIRTPGLIVSFTEDSIYFESDYGKAAEVLGYVRQAIELVREEADVNGKGITVSITSQIPVGAGLGSSAAVAVATIGAVSRLLGLELSNEEVGKLGHKVELLVQGASSGIDPTVSAIGGFIHYQKGKFEHLPFMELPLVVGYTGSSGSTKELVAMVRKNYEEMPEIFEPILNSMGRLVEKAREVITSDLDRELKFQTLGKLMNINHGLLDALGVSTKKLSELVYAARTAGALGAKITGAGGGGCMYALAPGKQSEVATAITIAGGTPMITKISREGMRIEEVEE | Function: Catalyzes the phosphorylation of (R)-mevalonate (MVA) to (R)-mevalonate 5-phosphate (MVAP). Functions in the mevalonate (MVA) pathway leading to isopentenyl diphosphate (IPP), a key precursor for the biosynthesis of isoprenoid compounds such as archaeal membrane lipids.
Catalytic Activity: (R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+)
Sequence Mass (Da): 35598
Sequence Length: 337
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.7.1.36
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P49283 | MSSNEAYHEPGAGGDGPGGSSGASGGGSQRSNQLHHQQILNETTYLKPAAKQAYFSDEKVLIPDDDSTNVGFSFRKLWAFTGPGFLMSIAYLDPGNIESDMQSGAAAKYKILWVLLWATVLGLLMQRLAARLGVVTGLHLAEMCYRQYKRLPRWILWIMIEIAIIGSDMQEVIGTAIAIYLLSNKVVPLWGGVLITIVDTFTFLFLDKYGLRKLEFLFGTLITIMAVSFGYEYIVSAPNQGEVLEGMFVPWCSNCNSNVLLQAVGVVGAVIMPHNLYLHSALVKSRDIDRRQTKKVSEANFYFFIEASVALFVSFIINLFVVAVFAHGMYGKTNNDVVEVCKDKSMYEDAKMSFVDNVNGTAIIDADLYKGGLFLGCTFGAVAMYIWGVGILAAGQSSTMTGTYAGQFSMEGFLNLQWPRWCRVLVTRCIAIIPTFCLAMFSKMEDLTSMNDILNAVMSLQLPFAAIPTIAFTSCAAIMGEFVNGLGNKIVSILLTIVVIGVNLYFVVVQVENMEIKGGLLALVCIFAILYILFNLYLVIHMAACMGNQRLMNSRWVQRFVLPSQNSFSIKNANSTYARIATSSDQEPEGLAGEDA | Function: Putative transporter required for normal taste behavior. May be a nitrite/nitrate transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65466
Sequence Length: 596
Subcellular Location: Membrane
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Q9RHG4 | MASYKVNIPAGPLWSNAEAQQVGPKIAAAHQGNFTGQWTTVVESAMSVVEVELQVENTGIHEFKTDVLAGPLWSNDEAQKLGPQIAASYGAEFTGQWRTIVEGVMSVIQIKYTF | Function: Carbohydrate-binding protein that binds oligomannosides such as Man(6)GlcNAc(2) with sub-micromolar affinities. The specificity of MVL is unique in that its minimal target comprises the Man-alpha-(1->6)-Man-beta-(1->4)-GlcNAc-beta-(1->4)-GlcNAc tetrasaccharide core (Man(2)A) found in N-linked oligomannosides. Displays hemagglutininating activity on rabbit, horse and hen erythrocytes. This activity is inhibited by yeast mannan. Does not bind mono- and disaccharides. Inhibits HIV-1 envelope-mediated cell fusion at nanomolar concentrations through carbohydrate-mediated interactions with high-mannose residues on the surface of the HIV envelope glycoprotein gp120.
Sequence Mass (Da): 12368
Sequence Length: 114
Domain: Each monomer contains 2 structurally homologous domains with high sequence similarity connected by a short five-amino acid residue linker. Intriguingly, a water-filled channel is observed between the 2 monomers.
Subcellular Location: Cytoplasm
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Q75CC3 | MMDLDSQELWGRGPSMESPNNAWASVQRTPADSARTQQIVSPVVRQAESLGSLTLTDSSLSAEVKETMRNNYNERKMYEPGTPALEQTVWGAPPSQLDASISGLDTSMAPVASQSSMCDELHSEDLENWMNSRRKTYNPLAKNIVVVEEIPEREGILFKHTNYLVKHLVVLPNTNPSSNQTVIRRYSDFNWLQEVLLKKYPFRMIPELPPKKIGAQNADPIFLARRRKGLCRFINLVIMHPVLKQDDLVLTFLTVPTDLGSWRKQANYDTTEEFTDQKIDKAFISLWHKELSNQWNKADAKIDELLESWIKTSVLVERYERRMRQVSEERRLLGRVIEEFADNSVTLYPLEEGTIHDINSHISTISKHLNSLADTSKKERQEVEEHLSVKFKTFIDIIIALKGVFDRYKIMAGNNIAHLQRRVEINMDKLQSMESNPDVKGAEYDKLRQTIQRDKRTIAEQLNRSWLIRKCILEEFVIFQETQFCITHVFQEWAKMHVKYANETTESWEKVYANLQDMPLSRS | Function: Required for vacuolar protein sorting.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 60619
Sequence Length: 523
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Subcellular Location: Cytoplasm
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Q4WZF1 | MSLFGTSPDDPSMGDSVHQRSRSSLFADEPLPGGAGAGNSANLGSSSLFADDDGFQSSSPWNSNANKRAARHELVKTLLPDADVPESYIDAYDLVLNEGDRVGGVVGLTSVREILSSSGLSASDQAKIFNLVVSGDGDSANGLGRGQFNVLLALIGLAQEGEDLTFDAVDDRRKKLPLPKSSYLDRLRDRQQPSAPSHPEERPTTPPPPPAAINDPPSARSRQSRETLGGLDADPWGSPQLHRGHNHVQTEPEPPVLNGFGSVRSATNAWSSGAGEDETQHEVPSGLRANGRTDGAPSTSSGSGWGGSYRNTTAGDGFGGPIRAGLGNLGAPSSGQEEPNARRRLGIGISTSSQVEETVTVNLLPEKEGMFMFQHRNYEVKSSRRGSTVIRRYSDFVWLLDCLQKRYPFRQLPLLPPKRIAADSNSFLEKRRRGLVRFTNALVRHPVLSQEQLVVMFLTVPTELSVWRKQATISVQDEFTGRVLPPDLEDSLPANLTDIFETVRSGVKRSAEIYINLCTLLERLAKRNEGLAADHLRFSLALQSLTEVTKDTYAVDTNDVPILNEGIMATARHLSNSQSLLEDEARAWENGILEDLKFQRDCLVSVREMFDRRDRYARNNIPQLERRIESNERKLEELRTRPQGAVKPGEIEKVEESIFKDKESIVQQHARGVFIKECIRDELVHFQRSQYHISRLHQDWSQERVKYSELQADNWRSLSDQVEGMPLGE | Function: Required for vacuolar protein sorting.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 80642
Sequence Length: 729
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Subcellular Location: Cytoplasm
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Q3MPQ4 | MNSNIEDDPWSSGWNDDNDNNNNNNTSINDPLTGATATTTPYQSSYLTSSQLFTSTGGGGSGSGGGYNSGVNTYNTTIPPNLINVPSSYETIYSHFITKYNNNNNNNNSNSTFTLNDFEINIIDKLISLNYLTNYQKQKILDIIYENNLLPINQSFKFYQILGLLALEIDVPGTGDYVTLQFRLNNNLPDLPEKFINEIINEENEQEEQTSGLLGNRNRSIQSHSHFGPNNQDDWNIDDSTTISGGGGGGGGNFGDPLLVDHSYIHDDLIDESRSVGGTQPQQGGGGGSGGGSGSGSGTIAPNVDSSYIEKYINDIKDQFKPLFSGIDLIKIKEVPEKEGIIFKHINYMITHDLKIGGTSSGTKKVIRRYSDFVWLMEYLLEKYPFRVIPGLPPKKFTGASPDSQFLQRRRRGLHRFLNQLIKHPILSQEPIVQSFLTVPTDLTTWKKQAKIDSSLEFKGQKIQTDFINVIWPIMGEPFLKKWRQAEENIQFIIDKWVKIIILVERYERRQQQISFDNGKFAEMLNGFSKLNTKIYPDNEDNNNSTRNDVNVNVVVVDNNENYKQDFDFNSSGDIININQCLNSIGEFFNKSSQVLIDESYIINTKTLEKFKNYLDYLNSLQELFERTKQLSINQIDLLDKRIKDQEIKFKKISEENPDIKGGELIKLRQSIINDKQEIFQQLNKDWLIKQCCLQEFIIFQETQFLITELWVEWCKDRLKCQEKLVGLYDNLNQEIIHDMPLER | Function: Required for vacuolar protein sorting.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 84897
Sequence Length: 744
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Subcellular Location: Cytoplasm
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Q6FNH2 | MDTYSGQNGWADTSNASPWGDTNDTMPIDNSLSNSLSGLQLNEDINTVRANLTESIWGTERTGAPNNVETGLEAKDSLNVSTNFNELNTAILSPTSSTSNIEEQNSFTESLESWINEVRKTYNPQQLDIISIEEIPEREGLLFKHANYSVKHLIDLPNTEPPKNRTVVRRYSDFLWLQEVLLKRYPFRMIPDLPPKKIGSQNLDPVFLNKRRIGLSKFINLVMKHPKLSKDDLVLTFLTVPTDLTSWRKQVSYDTADEFTDKRISKDFVKIWKKDLAEIWNNTANCIDELIDKWTKISILVDRHEKRLQIIANERKIMNDLIHDVGNLTKSVYPIDQNPTILDINSGMTVISKHIEKTNENYNQQALDTKQKVLPKFRMYTDILRALKNVFERYKMLATNNVSMLQKHIDLNLQKLEDMKGKPDASGQEYDRIKTTIRKDRKIMYEQSNRAWLIRECILEEFTIFQETQFMITGCFQEWAKVQSTYSSLNLNEWENVTNHILEMPLSRE | Function: Required for vacuolar protein sorting.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 59105
Sequence Length: 509
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Subcellular Location: Cytoplasm
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P0CR59 | MFNAPRPMASSYSYTDPLSNSAAAGAAFGELDPWSSAPSPAGSVTPARATASASEGRNIAANGNKEEGLNGLINDPPALYVSLLDQLDTSGTGEVSLAAVHRLLGTSKLPAVVVEKIIHLTSRDKSTLTRPEFFCALALVSLAQSSPDPNDISIEKLSFSLSNLPLPKLKPSDPPSVSSGVAASTAAATGFNAWDGTINKGTTYSANNSTFRSTDPMVDNAEDRWWKDQERIVVTLIPEKEGWFLQKYRIESDKRGEGPVARRYSDFVWLMDVLEKRYPFRILPPLPPKRINPSSAFLEARRLALIRLLSFLTAHPVLRTDACLNIFLTSSSFESWRKRTPVSTDEESLSKKLTTAQEMSIPSDLELKLDNLRERLPAMLGHYTRLVVMAERSLVRLQVQAAEAARMAMSTQSIGELVPRCCWRSVQGDDGESGRGVARECGLCEGVGRGWGDVGDGWVSVGEELEKGVQLLQKHIESLKSQRDLYSSFHALFYRHNKLSLDNVDVLRKRVDSRFSKIESLKSAKKPGWEGEVDKLASQSDRDTAEIQRLLARRVFVRACMWHELSVVFHSMQAAQGTMGWKDFVKDQKERTKRLNGVWQGLEETLESMPLE | Function: Required for vacuolar protein sorting.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 67744
Sequence Length: 612
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization.
Subcellular Location: Cytoplasm
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P11691 | MDTEYEQVNKPWNELYKETTLGNKLTVNVGMEDQEVPLLPSNFLTKVRVGLSGGYITMRRIRIKIIPLVSRKAGVSGKLYLRDISDTTGRKLHCTESLDLGREIRLTMQHLDFSVSTRSDVPIVFGFEELVSPFLEGRELFSISVRWQFGLSKNCYSLPQSKWKVMYQEDALKVLRPSKKKASKTDSSV | Function: Transports viral genome to neighboring plant cells directly through plasmosdesmata, without any budding. The movement protein allows efficient cell to cell propagation, by bypassing the host cell wall barrier. Displays RNA-binding activity.
PTM: Phosphorylated.
Sequence Mass (Da): 21608
Sequence Length: 189
Subcellular Location: Host membrane
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P0CK09 | MALIFGTVNANILKEVFGGARMACVTSAHMAGANGSILKKAEETSRAIMHKPVIFGEDYITEADLPYTPLHLEVDAEMERMYYLGRRALTHGKRRKVSVNNKRNRRRKVAKTYVGRDSIVEKIVVPHTERKVDTTAAVEDICNEATTQLVHNSMPKRKKQKNFLPATSLSNVYAQTWSIVRKRHMQVEIISKKSVRARVKRFEGSVQLFASVRHMYGERKRVDLRIDNWQQETLLDLAKRFKNERVDQSKLTFGSSGLVLRQGSYGPAHWYRHGMFIVRGRSDGMLVDARAKVTFAVCHSMTHYSDKSISEAFFIPYSKKFLELRPDGISHECTRGVSVERCGEVAAILTQALSPCGKITCKRCMVETPDIVEGESGESVTNQGKLLAMLKEQYPDFPMAEKLLTRFLQQKSLVNTNLTACVSVKQLIGDRKQAPFTHVLAVSEILFKGNKLTGADLEEASTHMLEIARFLNNRTENMRIGHLGSFRNKISSKAHVNNALMCDNQLDQNGNFIWGLRGAHAKRFLKGFFTEIDPNEGYDKYVIRKHIRGSRKLAIGNLIMSTDFQTLRQQIQGETIERKEIGNHCISMRNGNYVYPCCCVTLEDGKAQYSDLKHPTKRHLVIGNSGDSKYLDLPVLNEEKMYIANEGYCYMNIFFALLVNVKEEDAKDFTKFIRDTIVPKLGAWPTMQDVATACYLLSILYPDVLRAELPRILVDHDNKTMHVLDSYGSRTTGYHMLKMNTTSQLIEFVHSGLESEMKTYNVGGMNRDVVTQGAIEMLIKSIYKPHLMKQLLEEEPYIIVLAIVSPSILIAMYNSGTFEQALQMWLPNTMRLANLAAILSALAQKLTLADLFVQQRNLINEYAQVILDNLIDGVRVNHSLSLAMEIVTIKLATQEMDMALREGGYAVTSEKVHEMLEKKLCKGFEGCMGRINLVGKILRNQAFKKALEIWAKAFNHEKHRRLRRTYRLVCEIAFQVPLGTPEGNHLKSRKWWRKKGKSSEECHDKRGFSQNLQHAS | Function: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May have RNA-binding activity.
PTM: Potyviral RNA is expressed as two polyproteins which undergo post-translational proteolytic processing. Genome polyprotein is processed by NIa-pro, P1 and HC-pro proteinases resulting in the production of at least ten individual proteins. P3N-PIPO is cleaved by P1 and HC-pro proteinases resulting in the production of three individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically (By similarity).
Catalytic Activity: Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.
Sequence Mass (Da): 115451
Sequence Length: 1016
Domain: The N-terminus of helper component proteinase is involved in interaction with stylets. The central part is involved in interaction with virions and the C-terminus is involved in cell-to cell movement of the virus (By similarity).
Subcellular Location: Host cell junction
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Q9SCU7 | MVRPPCCDKGGVKKGPWTPEEDIILVTYIQEHGPGNWRAVPTNTGLLRCSKSCRLRWTNYLRPGIKRGNFTEHEEKMIVHLQALLGNRWAAIASYLPQRTDNDIKNYWNTHLKKKLNKVNQDSHQELDRSSLSSSPSSSSANSNSNISRGQWERRLQTDIHLAKKALSEALSPAVAPIITSTVTTTSSSAESRRSTSSASGFLRTQETSTTYASSTENIAKLLKGWVKNSPKTQNSADQIASTEVKEVIKSDDGKECAGAFQSFSEFDHSYQQAGVSPDHETKPDITGCCSNQSQWSLFEKWLFEDSGGQIGDILLDENTNFF | Function: Transcription factor that binds specifically to the DNA sequence 5'-AACAAAC-3' . Acts as a positive regulator of hypersensitive cell death . Acts as a positive regulator of salicylic acid synthesis . Regulates very-long-chain fatty acid biosynthesis . Acts cooperatively with BZR2 to promote expression of a subset of brassinosteroids target genes . Transcriptional activity and hypersensitive response control negatively regulated by PLA2-ALPHA . Involved in the regulation of abscisic acid (ABA) signaling . Increased levels of MYB30 can accelerate flowering both in long and short days through the regulation of FT .
PTM: Ubiquitinated by MIEL1.
Sequence Mass (Da): 35919
Sequence Length: 323
Domain: The N-terminus (11-116) contains a fully active minimal DNA-binding domain.
Subcellular Location: Nucleus
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P01106 | MDFFRVVENQQPPATMPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA | Function: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3' . Activates the transcription of growth-related genes . Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis . Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells (By similarity). Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity). Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform .
PTM: Phosphorylated by PRKDC . Phosphorylation at Ser-344 by PIM2 leads to the stabilization of MYC (By similarity). Phosphorylation at Ser-77 by CDK2 prevents Ras-induced senescence . Phosphorylated at Ser-77 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-73 . Phosphorylation at Thr-73 and Ser-77 by GSK3 is required for ubiquitination and degradation by the proteasome . Dephosphorylation at Ser-77 by protein phosphatase 2A (PPP2CA) promotes its degradation; interaction with PPP2CA is enhanced by AMBRA1 .
Sequence Mass (Da): 50565
Sequence Length: 454
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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P01108 | MDFLWALETPQTATTMPLNVNFTNRNYDLDYDSVQPYFICDEEENFYHQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVATSFSPREDDDGGGGNFSTADQLEMMTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSTSLSPARGHSVCSTSSLYLQDLTAAASECIDPSVVFPYPLNDSSSPKSCTSSDSTAFSPSSDSLLSSESSPRASPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQTPAKRSESGSSPSRGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRAKLDSGRVLKQISNNRKCSSPRSSDTEENDKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSIQADEHKLTSEKDLLRKRREQLKHKLEQLRNSGA | Function: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes. Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis. Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release . Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (By similarity).
PTM: Phosphorylated by PRKDC (By similarity). Phosphorylation at Ser-344 by PIM2 leads to the stabilization of MYC . Phosphorylation at Ser-77 by CDK2 prevents Ras-induced senescence. Phosphorylated at Ser-77 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-73. Phosphorylation at Thr-73 and Ser-77 by GSK3 is required for ubiquitination and degradation by the proteasome. Dephosphorylation at Ser-77 by protein phosphatase 2A (PPP2CA) promotes its degradation; interaction with PPP2CA is enhanced by AMBRA1 (By similarity).
Sequence Mass (Da): 50678
Sequence Length: 454
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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P09416 | MNFLWEVENPTVTTMPLNVSFANRNYDLDYDSVQPYFICDEEENFYHQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVATSFSPREDDDGGGGNFSTADQLEMMTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSTSLSPARGHSVCSTSSLYLQDLTAAASECIDPSVVFPYPLNDSSSPKSCTSSDSTAFSSSSDSLLSSESSPRATPEPLVLHEETPPTTSSDSEEEQDDEEEIDVVSVEKRQPPAKRSESGSSPSRGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRAKLDSGRVLKQISNNRKCSSPRSSDTEENDKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQADEHKLISEKDLLRKRREQLKHKLEQLRNSGA | Function: Transcription factor that binds DNA in a non-specific manner, yet also specifically recognizes the core sequence 5'-CAC[GA]TG-3'. Activates the transcription of growth-related genes . Binds to the VEGFA promoter, promoting VEGFA production and subsequent sprouting angiogenesis (By similarity). Regulator of somatic reprogramming, controls self-renewal of embryonic stem cells. Functions with TAF6L to activate target gene expression through RNA polymerase II pause release (By similarity). Positively regulates transcription of HNRNPA1, HNRNPA2 and PTBP1 which in turn regulate splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform (By similarity).
PTM: Phosphorylated by PRKDC (By similarity). Phosphorylation at Ser-343 by PIM2 leads to the stabilization of MYC (By similarity). Phosphorylation at Ser-76 by CDK2 prevents Ras-induced senescence. Phosphorylated at Ser-76 by DYRK2; this primes the protein for subsequent phosphorylation by GSK3B at Thr-72. Phosphorylation at Thr-72 and Ser-76 by GSK3 is required for ubiquitination and degradation by the proteasome. Dephosphorylation at Ser-76 by protein phosphatase 2A (PPP2CA) promotes its degradation; interaction with PPP2CA is enhanced by AMBRA1 (By similarity).
Sequence Mass (Da): 50561
Sequence Length: 453
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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Q599T9 | MAEGVPRAGSALPAASLSSLPLAALNVRVRRRLSLFLNVRAPVAADWTVLAEAMDFEYLEIQQLEKYADPTSRLLDDWQRRPGASVGRLLELLAKLGRDDVLMELGPSIEEDCQKYILKQQQEASEKPLQVDSIDSSITRINDMAGITIRDDPLGQKPECFDAFICYCPSDIEFVHEMIRQLEQTNYRLKLCVSDRDVLPGTCVWSIASELIEKRCRRMVVVVSDEYLQSKECDFQTKFALSLSPGAHQKRLIPIKYKPMKKEFPSILRFITVCDYTNPCTQNWFWTRLAKALSMP | Function: Adapter protein involved in the Toll-like receptor and IL-1 receptor signaling pathway in the innate immune response. Acts via IRAK1, IRAK2 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response. Increases IL-8 transcription. Involved in IL-18-mediated signaling pathway. Activates IRF1 resulting in its rapid migration into the nucleus to mediate an efficient induction of IFN-beta, NOS2/INOS, and IL12A genes . Upon TLR8 activation by GU-rich single-stranded RNA (GU-rich RNA) derived from viruses, induces IL1B release through NLRP3 inflammasome activation (By similarity). MyD88-mediated signaling in intestinal epithelial cells is crucial for maintenance of gut homeostasis and controls the expression of the antimicrobial lectin REG3G in the small intestine (By similarity).
PTM: Ubiquitinated; undergoes 'Lys-63'-linked polyubiquitination. OTUD4 specifically hydrolyzes 'Lys-63'-linked polyubiquitinated MYD88.
Sequence Mass (Da): 33709
Sequence Length: 296
Domain: The intermediate domain (ID) is required for the phosphorylation and activation of IRAK.
Subcellular Location: Cytoplasm
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Q63357 | MAEQESLEFGKADFVLMDTVSMPEFMANLRLRFEKGRIYTFIGEVVVSVNPYKVLNIYGRDTIEQYKGRELYERPPHLFAIADAAYKAMKRRSKDTCIMISGESGAGKTEASKYIMQYIAAITNPSQRAEIERVKNMLLKSNCVLEAFGNAKTNRNDNSSRFGKYMDINFDFKGDPIGGHINNYLLEKSRVIVQQPGERSFHSFYQLLQGGSEQMLHSLHLQKSLSSYNYIRVGAQLKSSINDAAEFKVVADAMKVIGFKPEEIQTVYKILAAILHLGNLKFIVDGDTPLIENGKVVSVIAELLSTKADMVEKALLYRTVATGRDIIDKQHTEQEASYGRDAFAKAIYERLFCWIVTRINDIIEVKNYDTTVHGKNTVIGVLDIYGFEIFDNNSFEQFCINYCNEKLQQLFIQLVLKQEQEEYQREGIPWKHIDYFNNQIIVDLVEQQHKGIIAILDDACMNVGKVTDGMFLEALNSKLGKHGHFSSRKTCASDKILEFDRDFRIRHYAGDVVYSVIGFIDKNKDTLFQDFKRLMYNSSNPVLKNMWPEGKLSITEVTKRPLTAATLFKNSMIALVDNLASKEPYYVRCIKPNDKKSPQIFDDERCRHQVEYLGLLENVRVRRAGFAFRQTYEKFLHRYKMISEFTWPNHDLPSDKEAVKKLIERCGFQDDVAYGKTKIFIRTPRTLFTLEELRAQMLVRVVLFLQKVWRGTLARMRYKRTKAALTIIRYYRRYKVKSYIHEVARRFHGVKNMRDYGKHVKWPTPPKVLRRFEEALQSIFNRWRASQLIKTIPASDLPQVRAKVAAMEMLKGQRADLGLQRAWEGNYLASKPDTPQTSGTFVPVANELKRKDKYMNVLFSCHVRKVNRFSKVEDRAIFVTDRHLYKMDPTKQYKVMKTIPLYNLTGLSVSNGKDQLVVFHTKDNKDLIVCLFSKQPTHESRIGELVGVLVNHFKSEKRHLQVNVTNPVQCSLHGKKCTVSVETRLNQPQPDFTKNRSGFILSVPGN | Function: Unconventional myosin that functions as actin-based motor protein with ATPase activity . Plays a role in endosomal protein trafficking, and especially in the transfer of cargo proteins from early to recycling endosomes (By similarity). Required for normal planar cell polarity in ciliated tracheal cells, for normal rotational polarity of cilia, and for coordinated, unidirectional ciliary movement in the trachea. Required for normal, polarized cilia organization in brain ependymal epithelial cells .
Sequence Mass (Da): 116095
Sequence Length: 1006
Domain: Binds a calmodulin chain via each of the two IQ domains . IQ domain 1 mediates interaction with calmodulin both in the presence and in the absence of Ca(2+). IQ domain 2 mediates interaction with calmodulin in the presence of Ca(2+) .
Subcellular Location: Cytoplasm
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P37301 | MALGAIGDGRLLLLLVGLLSASGPSPTLAIHVYTPREVYGTVGSHVTLSCSFWSSEWISEDISYTWHFQAEGSRDSISIFHYGKGQPYIDDVGSFKERMEWVGNPRRKDGSIVIHNLDYTDNGTFTCDVKNPPDIVGKSSQVTLYVLEKVPTRYGVVLGSIIGGVLLLVALLVAVVYLVRFCWLRRQAVLQRRLSAMEKGKLQRSAKDASKRSRQPPVLYAMLDHSRSAKAAAEKKSKGAPGEARKDKK | Function: Is an adhesion molecule necessary for normal myelination in the peripheral nervous system. It mediates adhesion between adjacent myelin wraps and ultimately drives myelin compaction.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 27467
Sequence Length: 249
Subcellular Location: Cell membrane
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P20938 | MFRDLKPAYLFCCSVLYAFSVLRPSQGISVSTHHNLHKTVGSDVTLYCGFWSNEYVSDLTTLSWRFRPDNSRDIISIFHYGNGVPYIEKWGQFRGRVEWVGDISKHDGSIVIRNLDYIDNGTFTCDVKNPPDVVGTSSDVHLTVYDKIPPVGAGVVSGAIIGTFLGIILLIVGGLYLFRYIVRRRARSETSFLQRRRSAAERGKVSGKAGTVSKGPVLYATLDQSKSGKGASEKKSKLSESKRDKK | Function: Creation of an extracellular membrane face which guides the wrapping process and ultimately compacts adjacent lamellae.
PTM: N-glycan is sulfated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 27335
Sequence Length: 246
Subcellular Location: Cell membrane
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Q6WEB5 | MAPGAPSSSPSPILAALLFSSLVLSPAQAIVVYTDKEVYGAVGSRVTLHCSFWSSEWVSDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTFKERIQWVGDPQWKDGSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYVFEKVPTRYGVVLGAVIGGVLGVVLLVLLLFYVVRYCWLRRQAALQRRLSAMEKGKLHKPGKDTSKRGRQTPVLYAMLDHSRSTKAASEKKAKGLGESRKDKK | Function: Is an adhesion molecule necessary for normal myelination in the peripheral nervous system. It mediates adhesion between adjacent myelin wraps and ultimately drives myelin compaction.
PTM: N-glycosylated; contains sulfate-substituted glycan.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 27485
Sequence Length: 248
Subcellular Location: Cell membrane
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P25189 | MAPGAPSSSPSPILAVLLFSSLVLSPAQAIVVYTDREVHGAVGSRVTLHCSFWSSEWVSDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTFKERIQWVGDPRWKDGSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYVFEKVPTRYGVVLGAVIGGVLGVVLLLLLLFYVVRYCWLRRQAALQRRLSAMEKGKLHKPGKDASKRGRQTPVLYAMLDHSRSTKAVSEKKAKGLGESRKDKK | Function: Is an adhesion molecule necessary for normal myelination in the peripheral nervous system. It mediates adhesion between adjacent myelin wraps and ultimately drives myelin compaction.
PTM: N-glycosylated; contains sulfate-substituted glycan.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 27555
Sequence Length: 248
Subcellular Location: Cell membrane
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P06907 | MAPGAPSSSPSPILAALLFSSLVLSPTLAIVVYTDREVYGAVGSQVTLHCSFWSSEWVSDDISFTWRYQPEGGRDAISIFHYAKGQPYIDEVGTFKERIQWVGDPSWKDGSIVIHNLDYSDNGTFTCDVKNPPDIVGKTSQVTLYVFEKVPTRYGVVLGAVIGGILGVVLLLLLLFYLIRYCWLRRQAALQRRLSAMEKGKFHKSSKDSSKRGRQTPVLYAMLDHSRSTKAASEKKSKGLGESRKDKK | Function: Is an adhesion molecule necessary for normal myelination in the peripheral nervous system. It mediates adhesion between adjacent myelin wraps and ultimately drives myelin compaction.
PTM: N-glycosylated; contains sulfate-substituted glycan.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 27571
Sequence Length: 248
Subcellular Location: Cell membrane
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F4J3T8 | MTPPRPPSGRVRSLRDYSSESEKMDGTGSWDTLEWTKLDSTSGSGSFSNLSCLLESERVIVEGYGVVLINTDEAGTLLVTNFRILFLSEGTRKVIPLGTIPLATIEKFNKMVLKVQSSPRQSDKIPPRRLLQVTGKDMRIIVYGFRPRTKQRRNVFDALLKCTKPERVWDLYTFACGPSKFGNANPKERLLNEYFRLLGKSSIRASMDMIEDGAFTLSNELWRISDLNSNYNLCQTYPFAFMIPKSISDAELLQACSFRARCRLPVITWCQPGSGAVIARSSQPLVGLMMNMRSNLDEKLVAAFCSQLPGAKGERRKLYIADARPRKNALANGAMGGGSESSSNYFQSEIVFFGIDNIHAMRESFSRVRDYLDMHGTTSSDGRSSFLRHGGWTWGGGNLSSMSASVSLLGDSGWLIHIQSVLAGAAWIAARVAMESASVLVHCSDGWDRTTQLVSLACLLLDPYYRTFAGFQALVEKDWLAFGHPFSDRVGMPNISGSGNFDFPRQSSSAGSFPSSPVRQSSGSAASQSSSSSHGHNNYSPIFMQWIDSVSQLMRMYPCAFEFSPTFLVDFMDCLLSCRFGNFLCNSEKEREQCGIADACGCLWAYLTDLRSFSATSHVHCNPFYDPLKYDGPLLPPAASLAPTLWPQFHLRWACPEEAKAADIGVQCRAMTVKYSEMQKEKEAAERRVDEISFAMESLSAELLRERHLSWVARESANRATKEYAALTRAVQSLGCKINFTTSDVEDDPRSSLENNPRRRNRHGNNSDVSVSISLMPEENTSGNPKGRVCEALCPLRTREGVCRWPEVGCAHVGSQFVGLKANFDAFDRLAIYDSYFQPK | Function: Phosphatase with phosphoinositide 3'-phosphatase activity that can use phosphatidylinositol-3-phosphate (PtdIns3P) and phosphatidylinositol-3,5-diphosphate (PtdIns3,5P(2)) as substrates and produces phosphatidylinositol-5-phosphate (PtdIns5P); participates in pathway(s) that transfer gene regulatory signals to the nucleus. Required for recovery after water deprivation, via the accumulation of PtdIns5P upon dehydration; high PtdIns5P levels mediate ATX1 cytoplasmic localization, thus down-regulating the expression of ATX1-dependent genes. Confers sensitivity to soil-water-deficit stress.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + H2O = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 93378
Sequence Length: 840
Subcellular Location: Cytoplasm
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P0CAP1 | MLRSTSTVTLLSGGAARTPGAPSRRANVCRLRLTVPPESPVPEQCEKKIERKEQLLDLSNGEPTRKLPQGVVYGVVRRSDQNQQKEMVVYGWSTSQLKEEMNYIKDVRATLEKVRKRMYGDYDEMRQKIRQLTQELSVSHAQQEYLENHIQTQSSALDRFNAMNSALASDSIGLQKTLVDVTLENSNIKDQIRNLQQTYEASMDKLREKQRQLEVAQVENQLLKMKVESSQEANAEVMREMTKKLYSQYEEKLQEEQRKHSAEKEALLEETNSFLKAIEEANKKMQAAEISLEEKDQRIGELDRLIERMEKERHQLQLQLLEHETEMSGELTDSDKERYQQLEEASASLRERIRHLDDMVHCQQKKVKQMVEEIESLKKKLQQKQLLILQLLEKISFLEGENNELQSRLDYLTETQAKTEVETREIGVGCDLLPSQTGRTREIVMPSRNYTPYTRVLELTMKKTLT | Function: Plays a role in cellular signaling via Rho-related GTP-binding proteins and subsequent activation of transcription factor SRF (By similarity). Targets TJP1 to cell junctions. In cortical neurons, may play a role in glutaminergic signal transduction through interaction with the NMDA receptor subunit GRIN1 (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54206
Sequence Length: 466
Subcellular Location: Cytoplasm
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B1B3P3 | MGSMLLASFPGASSITTGGSCLRSKQYAKNYDASSYVTTSWYKKRKIQKEHCAAIFSKHNLKQHYKVNEGGSTSNTSKECEKKYVVNAISEQSFEYEPQTRDPESIWDSVNDALDIFYKFCRPYAMFTIVLGATFKSLVAVEKLSDLSLAFFIGWLQVVVAVICIHIFGVGLNQLCDIEIDKINKPDLPLASGKLSFRNVVIITASSLILGLGFAWIVDSWPLFWTVFISCMVASAYNVDLPLLRWKKYPVLTAINFIADVAVTRSLGFFLHMQTCVFKRPTTFPRPLIFCTAIVSIYAIVIALFKDIPDMEGDEKFGIQSLSLRLGPKRVFWICVSLLEMTYGVTILVGATSPILWSKIITVLGHAVLASVLWYHAKSVDLTSNVVLHSFYMFIWKLHTAEYFLIPLFR | Function: Involved in the biosynthesis of sophoraflavanone G (SFG). Can use flavanones (naringenin, liquiritigenin and hesperetin) as substrates, but not flavonols or isoflavones. Shows a strict specificity for dimethylallyl diphosphate.
Catalytic Activity: (2S)-naringenin + dimethylallyl diphosphate = diphosphate + sophoraflavanone B
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46159
Sequence Length: 410
Subcellular Location: Plastid
EC: 2.5.1.70
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Q8H115 | MDFALFSSISIFEINHKDPPIRRFIKTQNRILSTRKQQGTFPKMKAELNLPAGFRFHPTDEELVKFYLCRRCASEPINVPVIAEIDLYKFNPWELPEMALYGEKEWYFFSHRDRKYPNGSRPNRAAGTGYWKATGADKPIGKPKTLGIKKALVFYAGKAPKGIKTNWIMHEYRLANVDRSASTNKKNNLRLDDWVLCRIYNKKGTMEKYLPAAAEKPTEKMSTSDSRCSSHVISPDVTCSDNWEVESEPKWINLEDALEAFNDDTSMFSSIGLLQNDAFVPQFQYQSSDFVDSFQDPFEQKPFLNWNFAPQG | Function: May be involved in regulation of seed germination under flooding.
Sequence Mass (Da): 35999
Sequence Length: 312
Domain: The NAC domain includes a DNA-binding domain and a dimerization domain.
Subcellular Location: Nucleus
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Q01728 | MLRLSLPPNVSMGFRLVTLVALLFTHVDHITADTEAETGGNETTECTGSYYCKKGVILPIWEPQDPSFGDKIARATVYFVAMVYMFLGVSIIADRFMSSIEVITSQEKEITIKKPNGETTKTTVRIWNETVSNLTLMALGSSAPEILLSVIEVCGHNFTAGDLGPSTIVGSAAFNMFIIIALCVYVVPDGETRKIKHLRVFFVTAAWSIFAYTWLYIILSVSSPGVVEVWEGLLTFFFFPICVVFAWVADRRLLFYKYVYKRYRAGKQRGMIIEHEGDRPASKTEIEMDGKVVNSHVDNFLDGALVLEVDERDQDDEEARREMARILKELKQKHPDKEIEQLIELANYQVLSQQQKSRAFYRIQATRLMTGAGNILKRHAADQARKAVSMHEVNMDVVENDPVSKVFFEQGTYQCLENCGTVALTIIRRGGDLTNTVFVDFRTEDGTANAGSDYEFTEGTVIFKPGETQKEIRVGIIDDDIFEEDENFLVHLSNVRVSSEVSEDGILDSNHVSAIACLGSPNTATITIFDDDHAGIFTFEEPVTHVSESIGIMEVKVLRTSGARGNVIIPYKTIEGTARGGGEDFEDTCGELEFQNDEIVKTISVKVIDDEEYEKNKTFFIEIGEPRLVEMSEKKALLLNELGGFTLTEGKKMYGQPVFRKVHARDHPIPSTVISISEEYDDKQPLTSKEEEERRIAEMGRPILGEHTKLEVIIEESYEFKSTVDKLIKKTNLALVVGTNSWREQFIEAITVSAGEDDDDDECGEEKLPSCFDYVMHFLTVFWKVLFAFVPPTEYWNGWACFIVSILMIGLLTAFIGDLASHFGCTIGLKDSVTAVVFVALGTSVPDTFASKVAATQDQYADASIGNVTGSNAVNVFLGIGVAWSIAAIYHAANGEQFKVSPGTLAFSVTLFTIFAFINVGVLLYRRRPEIGGELGGPRTAKLLTSSLFVLLWLLYIFFSSLEAYCHIKGF | Function: Mediates the exchange of one Ca(2+) ion against three to four Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes . Contributes to Ca(2+) transport during excitation-contraction coupling in muscle. In a first phase, voltage-gated channels mediate the rapid increase of cytoplasmic Ca(2+) levels due to release of Ca(2+) stores from the endoplasmic reticulum. SLC8A1 mediates the export of Ca(2+) from the cell during the next phase, so that cytoplasmic Ca(2+) levels rapidly return to baseline. Required for normal embryonic heart development and the onset of heart contractions (By similarity).
Catalytic Activity: Ca(2+)(in) + 3 Na(+)(out) = Ca(2+)(out) + 3 Na(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 108185
Sequence Length: 971
Domain: The cytoplasmic Calx-beta domains bind the regulatory Ca(2+). The first Calx-beta domain can bind up to four Ca(2+) ions. The second domain can bind another two Ca(2+) ions that are essential for calcium-regulated ion exchange.
Subcellular Location: Cell membrane
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Q84TE6 | METEEEMKESSISMVEAKLPPGFRFHPKDDELVCDYLMRRSLHNNHRPPLVLIQVDLNKCEPWDIPKMACVGGKDWYFYSQRDRKYATGLRTNRATATGYWKATGKDRTILRKGKLVGMRKTLVFYQGRAPRGRKTDWVMHEFRLQGSHHPPNHSLSSPKEDWVLCRVFHKNTEGVICRDNMGSCFDETASASLPPLMDPYINFDQEPSSYLSDDHHYIINEHVPCFSNLSQNQTLNSNLTNSVSELKIPCKNPNPLFTGGSASATLTGLDSFCSSDQMVLRALLSQLTKIDGSLGPKESQSYGEGSSESLLTDIGIPSTVWNC | Function: Transcriptional activator that mediates auxin signaling to promote lateral root development. Activates the expression of two downstream auxin-responsive genes, DBP and AIR3.
PTM: Ubiquitinated (Probable). The interaction with SINAT5 mediate its proteasome-dependent degradation .
Sequence Mass (Da): 36569
Sequence Length: 324
Domain: The NAC domain includes a DNA-binding domain and a dimerization domain.
Subcellular Location: Nucleus
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Q10S65 | MAAAVAVAGPSMEVEQDLPGFRFHPTEEELLDFYLSRVVLGKKLHFNIIGTLNIYRHDPWDLPGMAKIGEREWYFFVPRDRKAGNGGRPNRTTERGFWKATGSDRAIRSSGDPKRVIGLKKTLVFYQGRAPRGTKTDWVMNEYRLPDYGAARAAAPPPKEDMVLCKIYRKATPLKELEQRASAMEEMQRGSSHGDYTATRASLVHDASASTGDDYFSSDDVHDSGFLIQSSSSSAAPSGSSSKNGGAGAPREAKKEEADVTVTVASATSLQLPAVSQLPSLQLPAMDWLQDPFLTQLRSPWQDQHCLSPYAHLLYY | Function: Transcription activator that binds sequence-specific DNA motifs. Involved in stress response. Plays a positive role in drought and salt stress tolerance through the modulation of abscisic acid-mediated signaling.
Sequence Mass (Da): 34927
Sequence Length: 316
Domain: The NAC domain includes a DNA binding domain and a dimerization domain.
Subcellular Location: Nucleus
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B8AE67 | MAMTPQLAFSRMPPGFRFQPTDEQLVVDYLQRRTAAQPCVTPDITDIDVYNVDPWQLPAMAMYGSDHDRYFFTMAAREAQARRTTPSGFWKPTGTKKTIFVVAGGHEVPTAVKRRFVFYLGHHQPSGSSNNNKTSWIMHEYRLMNSPRAAVPSSSSVNRLPTDDLTEEMVLCRISNKDLPKPPFIHNGLLQFSSVGLNGDGYNYLILDHLEPPAMEYPNVDIGNVDDAAAADDDPGDLDEEIDDSMQRNHGG | Function: Transcription factor involved in the regulation of seed size . Possesses transactivation activity in yeast .
Sequence Mass (Da): 28192
Sequence Length: 252
Domain: The NAC domain includes a DNA binding domain and a dimerization domain.
Subcellular Location: Nucleus
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Q8GY42 | MENMGDSSIGPGHPHLPPGFRFHPTDEELVVHYLKKKADSVPLPVSIIAEIDLYKFDPWELPSKASFGEHEWYFFSPRDRKYPNGVRPNRAATSGYWKATGTDKPIFTCNSHKVGVKKALVFYGGKPPKGIKTDWIMHEYRLTDGNLSTAAKPPDLTTTRKNSLRLDDWVLCRIYKKNSSQRPTMERVLLREDLMEGMLSKSSANSSSTSVLDNNDNNNNNNEEHFFDGMVVSSDKRSLCGQYRMGHEASGSSSFGSFLSSKRFHHTGDLNNDNYNVSFVSMLSEIPQSSGFHANGVMDTTSSLADHGVLRQAFQLPNMNWHS | Function: Transcription factor of the NAC family. May be associated with anther development and pollen production (Probable). Required for normal seed development and morphology .
Sequence Mass (Da): 36313
Sequence Length: 323
Domain: The NAC domain includes a DNA-binding domain and a dimerization domain.
Subcellular Location: Nucleus
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O49255 | MEVTSQSTLPPGFRFHPTDEELIVYYLRNQTMSKPCPVSIIPEVDIYKFDPWQLPEKTEFGENEWYFFSPRERKYPNGVRPNRAAVSGYWKATGTDKAIHSGSSNVGVKKALVFYKGRPPKGIKTDWIMHEYRLHDSRKASTKRNGSMRLDEWVLCRIYKKRGASKLLNEQEGFMDEVLMEDETKVVVNEAERRTEEEIMMMTSMKLPRTCSLAHLLEMDYMGPVSHIDNFSQFDHLHQPDSESSWFGDLQFNQDEILNHHRQAMFKF | Function: Transcription activator that binds to, and transactivates the promoter of the abscisic aldehyde oxidase AAO3. Promotes chlorophyll degradation in leaves by enhancing transcription of AAO3, which leads to increased levels of the senescence-inducing hormone abscisic acid (ABA) . Involved in the control of dehydration in senescing leaves. Binds to the DNA sequence 5'-CACGTAAGT-3' of SAG113 promoter. SAG113 acts as negative regulator of ABA signaling for stomatal closure in leaves, and controls water loss during leaf senescence . Transcription factor of the NAC family involved in senescence. May function in the transition between active cell division and cell expansion . Required for normal seed development and morphology .
Sequence Mass (Da): 31426
Sequence Length: 268
Domain: The NAC domain includes a DNA-binding domain and a dimerization domain.
Subcellular Location: Nucleus
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Q9UPR5 | MAPLALVGVTLLLAAPPCSGAATPTPSLPPPPANDSDTSTGGCQGSYRCQPGVLLPVWEPDDPSLGDKAARAVVYFVAMVYMFLGVSIIADRFMAAIEVITSKEKEITITKANGETSVGTVRIWNETVSNLTLMALGSSAPEILLSVIEVCGHNFQAGELGPGTIVGSAAFNMFVVIAVCIYVIPAGESRKIKHLRVFFVTASWSIFAYVWLYLILAVFSPGVVQVWEALLTLVFFPVCVVFAWMADKRLLFYKYVYKRYRTDPRSGIIIGAEGDPPKSIELDGTFVGAEAPGELGGLGPGPAEARELDASRREVIQILKDLKQKHPDKDLEQLVGIANYYALLHQQKSRAFYRIQATRLMTGAGNVLRRHAADASRRAAPAEGAGEDEDDGASRIFFEPSLYHCLENCGSVLLSVTCQGGEGNSTFYVDYRTEDGSAKAGSDYEYSEGTLVFKPGETQKELRIGIIDDDIFEEDEHFFVRLLNLRVGDAQGMFEPDGGGRPKGRLVAPLLATVTILDDDHAGIFSFQDRLLHVSECMGTVDVRVVRSSGARGTVRLPYRTVDGTARGGGVHYEDACGELEFGDDETMKTLQVKIVDDEEYEKKDNFFIELGQPQWLKRGISALLLNQGDGDRKLTAEEEEARRIAEMGKPVLGENCRLEVIIEESYDFKNTVDKLIKKTNLALVIGTHSWREQFLEAITVSAGDEEEEEDGSREERLPSCFDYVMHFLTVFWKVLFACVPPTEYCHGWACFGVSILVIGLLTALIGDLASHFGCTVGLKDSVNAVVFVALGTSIPDTFASKVAALQDQCADASIGNVTGSNAVNVFLGLGVAWSVAAVYWAVQGRPFEVRTGTLAFSVTLFTVFAFVGIAVLLYRRRPHIGGELGGPRGPKLATTALFLGLWLLYILFASLEAYCHIRGF | Function: Mediates the electrogenic exchange of Ca(2+) against Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes. Contributes to cellular Ca(2+) homeostasis in excitable cells. Contributes to the rapid decrease of cytoplasmic Ca(2+) levels back to baseline after neuronal activation, and thereby contributes to modulate synaptic plasticity, learning and memory. Plays a role in regulating urinary Ca(2+) and Na(+) excretion.
Catalytic Activity: Ca(2+)(in) + 3 Na(+)(out) = Ca(2+)(out) + 3 Na(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 100368
Sequence Length: 921
Domain: The cytoplasmic Calx-beta domains bind the regulatory Ca(2+). The first Calx-beta domain can bind up to four Ca(2+) ions. The second domain can bind another two Ca(2+) ions that are essential for calcium-regulated ion exchange.
Subcellular Location: Cell membrane
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Q8K596 | MAPLALMGVVLLLGVPHCLGEATPTPSLPPPTANDSDASPEGCQGSYRCQPGVLLPVWEPEDPSLGDKVARAVVYFVAMVYMFLGVSIIADRFMASIEVITSKEKEITITKANGETSVGTVRIWNETVSNLTLMALGSSAPEILLTVIEVCGHNFQAGELGPGTIVGSAAFNMFVVIAVCVYVIPAGESRKIKHLRVFFVTASWSIFAYVWLYLILAVFSPGVVQVWEALLTLIFFPVCVVFAWMADKRLLFYKYVYKRYRTDPRSGIIIGAEGDPPKSIELDGTFVGTEVPGELGALGTGPAEARELDASRREVIQILKDLKQKHPDKDLEQLMGIAKYYALLHQQKSRAFYRIQATRLMTGAGNVLRRHAADAARRPGATDGAPDDEDDGASRIFFEPSLYHCLENCGSVLLSVACQGGEGNSTFYVDYRTEDGSAKAGSDYEYSEGTLVFKPGETQKDLRIGIIDDDIFEEDEHFFVRLLNLRVGDAQGMFEPDGGGRPKGRLVAPLLATVTILDDDHAGIFSFQDRLLHVSECMGTVDVRVVRSSGARGTVRLPYRTVDGTARGGGVHYEDACGELEFGDDETMKTLQVKIVDDEEYEKKDNFFIELGQPQWLKRGISALLLNQGNGDKKITAEQEEAQRIAEMGKPVLGENNRLEVIIEESYDFKNTVDKLIKKTNLALVIGTHSWREQFIEAVTVSAGDEEEDEDGPREERLPSCFDYVMHFLTVFWKVLFACVPPTEYCNGWACFGVCILVIGVLTALIGDLASHFGCTVGLKDSVNAVVFVALGTSIPDTFASKVAALQDQCADASIGNVTGSNAVNVFLGLGVAWSVAAVYWAVQGRPFEVRAGTLAFSVTLFTVFAFVCIAVLLYRRRPQIGGELGGPRGPKLATTALFLGLWFLYILFSSLEAYCHIRGF | Function: Mediates the electrogenic exchange of Ca(2+) against Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes . Contributes to cellular Ca(2+) homeostasis in excitable cells . Contributes to the rapid decrease of cytoplasmic Ca(2+) levels back to baseline after neuronal activation, and thereby contributes to modulate synaptic plasticity, learning and memory . Plays a role in regulating urinary Ca(2+) and Na(+) excretion .
Catalytic Activity: Ca(2+)(in) + 3 Na(+)(out) = Ca(2+)(out) + 3 Na(+)(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 100711
Sequence Length: 921
Domain: The cytoplasmic Calx-beta domains bind the regulatory Ca(2+). The first Calx-beta domain can bind up to four Ca(2+) ions. The second domain can bind another two Ca(2+) ions that are essential for calcium-regulated ion exchange.
Subcellular Location: Cell membrane
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Q75HE5 | MGMGMRRERDAEAELNLPPGFRFHPTDDELVEHYLCRKAAGQRLPVPIIAEVDLYKFDPWDLPERALFGAREWYFFTPRDRKYPNGSRPNRAAGNGYWKATGADKPVAPRGRTLGIKKALVFYAGKAPRGVKTDWIMHEYRLADAGRAAAGAKKGSLRLDDWVLCRLYNKKNEWEKMQQGKEVKEEASDMVTSQSHSHTHSWGETRTPESEIVDNDPFPELDSFPAFQPAPPPATAMMVPKKESMDDATAAAAAAATIPRNNSSLFVDLSYDDIQGMYSGLDMLPPGDDFYSSLFASPRVKGTTPRAGAGMGMVPF | Function: Transcription factor that possesses transactivation activity . Transcription activator involved in response to abiotic stresses. Plays a positive role during dehydration and salt stress. Binds specifically to the 5'-CATGTG-3' motif found in promoters of stress-responsive genes .
Sequence Mass (Da): 35178
Sequence Length: 316
Domain: The NAC domain includes a DNA binding domain and a dimerization domain.
Subcellular Location: Nucleus
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O67730 | MVQLALKEEKELTKEEIKELQKEVRRLAKEKNAVILAHYYQRPEVQDIADFVGDSLELARKASQTDADIIVFCGVRFMCETAKIVNPEKKVLHPNPESGCPMADMITAKQVRELREKHPDAEFVAYINTTADVKAEVDICVTSANAPKIIKKLEAKKIVFLPDQALGNWVAKQVPEKEFIIWKGFCPPHFEFTYKELEKLKEMYPDAKVAVHPECHPRVIELADFVGSTSQILKYATSVDAKRVIVVTEVGLKYTLEKINPNKEYIFPQSMNYCGTVYCCTMKGITLPKVYETLKNEINEVTLPKDIIERARRPIERMLELS | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 36804
Sequence Length: 322
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.72
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Q9FGS4 | MALALSVAPTSSSLSSLLSRTPNPSPNFRTTHLNFGSQRRIYTINPLLRSFKCLQSSSRDVNASPFSISAIASSSSSSQTTELVPYKLQRLVKEFKSLTEPIDRLKWVLHYASLLPQMPESSKTESNRVMGCTARVWLDAELGQDGKMRFCADSDSDVSKGMCSCLIQVLDEASPVEVMELKTEDLAELNVGLLGGERSRVNTWYNVLVSMQKKTRRLVAEREGKVPSFEPFPSLVLTAHGIEAKGSFAQAQAKYLFPEESRVEELVNVLKEKKIGVVAHFYMDPEVQGVLTAAQKHWPHISISDSLVMADSAVTMAKAGCQFITVLGVDFMSENVRAILDQAGFEKVGVYRMSDETIGCSLADAASAPAYLNYLEAASRSPPSLHVVYINTSLETKAFAHELVPTITCTSSNVVQTILQAFAQMPELTVWYGPDSYMGANIVKLFQQMTLMTNEEIANIHPKHSLDSIKSLLPRLHYFQEGTCIVHHLFGHEVVERIKYMYCDAFLTAHLEVPGEMFSLAMEAKKREMGVVGSTQNILDFIKQKVQEAVDRNVDDHLQFVLGTESGMVTSIVAVIRSLLGSSANSKLKVEVVFPVSSDSMTKTSSDSSNSIKVGDVALPVVPGVAGGEGCSIHGGCASCPYMKMNSLSSLLKVCHKLPDLENVYGGFIAERFKRQTPQGKLIADVGCEPILHMRHFQANKELPDKLVHQVLSCESKR | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate. Can complement nadA-deficient E.coli mutant. Essential for the de novo synthesis of NAD. Participates also in cysteine desulfurization mediated by NFS2. Can activate the cysteine desulfurase activity of NFS2 in vitro.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 78934
Sequence Length: 718
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1.
Subcellular Location: Plastid
EC: 2.5.1.72
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Q4WL81 | MIFTNAILVISALLPATVLSLQHTEDSLFPARCWPDPCAGITFQNDTYVCGDPRLGPVVLPQKFPLNNELRTYARFGALCPAEFLDKWATDVAPNGTYIYPPANGFALDTEEQPILGNATLPVGMKLDRFGSEYGTFLAPLGAPYIERSLPPSNLNTFDGMYPYNYHVYQVTKEFVVGLGPIAPWFEQPGMGTQFVTYTNVLGLIDDGYLRRLDESEYDEKVEYSNPYTPGPNQ | Function: Conidial surface nicotinamide adenine dinucleotide glycohydrolase that cleave NAD(+) and NADP(+) but not their reduced counterparts, NADH and NADPH . Lacks both ADP-ribosyl cyclase and base exchange activity and does not mediate synthesis of calcium messengers cADPR or NAADP . Plays a role in pathogenicity by depleting the host's NAD(+) pool .
PTM: N-glycosylated.
Catalytic Activity: H2O + NAD(+) = ADP-D-ribose + H(+) + nicotinamide
Sequence Mass (Da): 26022
Sequence Length: 234
Domain: The C-terminus contains also a calcium binding site (residues 215-224) that might be involved in NADase activity regulation . The calcium-binding site is not alweays present since it emerged in the order Eurotiales, which includes Aspergillus species .
Subcellular Location: Secreted
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Q6UEF0 | MARAGQAVDPSPLGQPLEFHFARRSAPNRFLKAGMSERMCSWTEENPSARGIPSRELIETYRTWGRGNIGAIVTGNVMIDPNHIEAEGNPTIPPNALFSGERFDQFANLAAAARANGSLILAQISHPGRQTPSHRQPEPISASDVPLDTENMGNTFAVPRAATENEIKNIITGFAHAAEFLDRAGYDGVELHAAHGYLLNQFLSRATNLRTDKYGGTLTNRMRLILEIRAAITEKVRPGFIVGIKINSVEFQPNGIVPDEACELCCALEEHRFDFVELSGGKYKNLEEDDNAKHIISKRHEAFFLDVAQKVVSSLTKMKSYLTGGFRSTAGMVDGLQTVDGIGLARPFCQEPYLCHDILRGKIPGAIIPVMDQLNYQLTVAAACIQMRQIGNKVQPVDLSSQDAVDAITAAAEGWLKRKAIDRSEEAFKPPLLSGDAAPLSVEA | Function: NADH-dependent flavin oxidoreductase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins . The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2) . Within the aflatoxin pathway, the NADH-dependent flavin oxidoreductase nadA is specifically required for the last steps in which OMST is converted specifically to aflatoxin G1 . The biosynthesis of aflatoxins begins with the norsolorinic acid synthase aflC that combines a hexanoyl starter unit produced by the fatty acid synthase aflA/aflB and 7 malonyl-CoA extender units to synthesize the precursor NOR. The second step is the conversion of NOR to averantin and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN. The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway. The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen. Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2. Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring-opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring. The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O-methylsterigmatocystin (DHOMST), respectively. Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 .
Sequence Mass (Da): 48459
Sequence Length: 444
Subcellular Location: Cytoplasm
EC: 1.-.-.-
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Q817V8 | MSILEQVQPIETMLPERYYTMSTEDMEKRVREIKEKMGKMLFIPGHHYQKDEVVQFSDAVGDSLQLAQVAASNKDAKYIVFCGVHFMAETADMLTTDDQVVILPDMRAGCSMADMADIEQTERAWKELTKLFGDTMIPLTYVNSTAAIKAFCGRNGGATVTSSNAKQMVSWAFTQKERLVFLPDQHLGRNTAYDLGIPLDKMAVWDPHTDSLEYDGDIEEIQVILWKGHCSVHQNFTVKNIESVRKNHSDMNIIVHPECCYEVVAASDYAGSTKYIIDMIESAPPGSKWAIGTEMNLVNRIIQQHPDKEIVSLNPFMCPCLTMNRIDLPHLLWALETIERGEEINVISVDKQVTAEAVLALNRMLERV | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 41569
Sequence Length: 368
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.72
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Q9PC58 | MEEAHNMREIRLREIVVNHAVLSSCLDKCGDCFASEAARIKFDNDIEAIFELKRKRNAVILAHNYQTPEIFHGVADIVGDSLALARKAIDVDADVIVLAGVHFMAETAKLLNPEKTVLIPDMEAGCSLAESITPEDVALLRQTYPGIPIVTYVNTSAAVKAASDICCTSGNAKKVVEALGVPKVLMIPDEYLARNVAKETEVQIISWHGHCEVHELFSASDILQLRENHPGVTVLAHPECPPDVVAAADFAGSTAAMSDYVTTKQPKRVVLLTECSMSDNIAVHHPDVEFISSCNLCPHMKRITLANIRTALEENRHEVTVDAKIAAPARRAVERMLAI | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the condensation of iminoaspartate with dihydroxyacetone phosphate to form quinolinate.
Catalytic Activity: dihydroxyacetone phosphate + iminosuccinate = H(+) + 2 H2O + phosphate + quinolinate
Sequence Mass (Da): 37015
Sequence Length: 339
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from iminoaspartate: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.5.1.72
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A7HJZ9 | MTSFSKSDTCVIFGGSFNPPHIGHTVILSYALDYFNADFYIIPTKTPPHKVVDIDFDKRFEWVMKSFKCFDTYKKNQIFLWDLEKHIFGVNYAIKNVEYFRKYYSNTIILVGEDALGNIEKWYKYEELLNITTFAIYPRTRDGSLYKRGQQILGNLYSNVIELRDFPLIEISSSDIRKRIVEGKSIIGFVDGEILEDVTNTYLMHHKSHGGNWNE | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 25157
Sequence Length: 215
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
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A6GVY8 | MKIGLYFGTFNPIHIGHLIIANHMAENSDLDQVWMVVTPHNPLKKKDTLLDDYQRLHLVNLATEDYPKLKPSDIEFKLPQPNYTVNTLAHLQDKFPSYEFSLIMGEDNLNSLHKWKNYEAILQNHQIYVYPRLNTDTIDNQFINHQKIHIIKAPIVEISSTFIRENIKNKKNIQPLLPPKVWKYIDHSNFYKK | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22787
Sequence Length: 193
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
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Q2JDN2 | MGGTFDPVHNGHLVAASEVAALFDLDEVVFVPSGQPWQKIHRKVSAAEDRYLMTFLATAGNPQFTVSRIEIDRGGATYTIDTLRDLRAARPDDELFFITGADALAQIFTWRDHRELFELAHFVGVNRPGYHLALDAGLPTGAVSLLEVPALAISSSDIRERVGRRAPIWYLTPDGVVRYIAKRRLYQGAS | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 21035
Sequence Length: 190
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
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Q8REH1 | MKIAIYGGSFNPMHIGHEKIVDYVLKNLDMDKIIIIPVGIPSHRENNLEQSDTRLKICKEIFKNNKKVEVSDIEIKAEGKSYTYDTLLKLIEIYGKDNEFFEIIGEDSLKNLKTWRNYKELLNLCKFIVFRRKDDKNIEIDNEFLNNKNIIILENEYYNISSTEIRNKVKNKEDISGLVNKKVKKLIEKEYID | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22779
Sequence Length: 193
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
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C1A4H9 | MRLGLFGGSFDPPHVGHLLVAQDALEALRLDHLLIIPAAQQPLKGAHQTSAHHRLAMVRACFEGVQGIEVDPVEIERGGLSFMVDTVEAVRRRWPDAHLHLLVGRDVVPTLPRWHDVDRLLSMVRLVVLTRDAAPQEGPLLIDAESDSGVVAEVLSTRQVDMSSTEIRSRVRDGRSIRGFVPDAVATYIASTGLYREYPRGSADTERSERA | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 23277
Sequence Length: 211
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
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Q747Q5 | MKTGILGGTFNPVHVAHLRIAEEVRDTFALDRVLFIPAASPPHKAMEGEVPFETRCAMVRLATADNHAFAVSDMEGGRPGKSYSVDTIRALKEEYPGDEFFFIIGSDSFLDIGSWYDYEAIFASCNLVVAARPGAEAADLLAALPVAITAQFCYYPAEKRLAHRSGYSVYWLAGVPLDISSRSIRGLARLGRSIRYLVPEAVERYINEQRIYAHDG | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 23849
Sequence Length: 216
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
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Q7NE64 | MGERLGIFGGTFNPVHRGHLAMARAARDRCGLDQILWVPAAQPPHKPLAGGASIGDRVEMVRLAIAGEAGMALSLVDARRPGPSYAIDTLRLLEEQYPQAQWHWLLGQDGLADLPGWYRAAELIPRCRWIVVPRPGSGADPKQAMADLTERFGAVFVPLSDFECDISSTRVREQLAAGRAGWEALLPEQVVSYIHKRGLYDVPAGA | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 22456
Sequence Length: 206
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
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A9HC14 | MSSIAAWGDGRRTRIGVLGGSFNPVHDGHLQLARRALRHLRLDQVWLMISPGYPLKPVQGMAPFDVRLASVAARFDGRRLVATDIERRLGTRYTVDTLGLLRLRFPHAAFVWLMGADGLADLARWRDWRRIVSLVPFAVLPRPTYNPGALRGEAAVALARWRRPARQAPILADCAPCAWAFLPAPQIGISATELRASALRQRSRHPTHKHTTHQE | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 24049
Sequence Length: 215
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
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Q5FRT1 | MRIGLLGGSFNPAHAGHLMLARRALRALRLDQVWLMVSPGNPLKPSKGMAPFRVRLASAERIADGRRIVATDIESRLGQRFTVKTVGLLKQRFPHVRFVWLMGADGLAQLSHWKRWRRLAAMVPIAVLPRPGSVSPALRGAAASVLRHQRRPSRESPVLAERKGNAWTFLSAPQNDISATALRESGQFRPDSDQE | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 21647
Sequence Length: 195
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
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Q2SA28 | MQEHSPIVLLGGTFDPIHFGHLRTALELQQHFGESAEVRLIPCGDPRHRSAPKASGEHRLAMLRLALEGEPSLRIDEVEVRRTGASYTVDTLLELRQEVGNLRPLIFVMGTDAFESLPKWRRWLEIIQLAHIMVVNRPGWSFCEQGELGDFLRQHSAESNNDLIRQPAGKVGFITLTQMGISSSKVRELIGLRLSPRFLLPDSVWRYIRQHRLYGAVNA | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 24863
Sequence Length: 219
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
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Q9KD91 | MKRIGLLGGTFDPPHIGHLLLAQEAIHCADLDEVWFVPVGIPPHKEREEIASNDDRLAMIKRAIKGKETLFNICTIELEREGKSYTIDTVRTLTKKHPDVRFFFIIGGDMVKSLPTWKGIDELLATVTFIGFKRPGVLLDSPYQDQLMLVEGPEVNVSSTMIRERMTEGKPISYLLPLDVERYIYEKGLYKTNESRKSPSVSKTSSN | Function: Catalyzes the reversible adenylation of nicotinate mononucleotide (NaMN) to nicotinic acid adenine dinucleotide (NaAD).
Catalytic Activity: ATP + H(+) + nicotinate beta-D-ribonucleotide = deamido-NAD(+) + diphosphate
Sequence Mass (Da): 23434
Sequence Length: 207
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; deamido-NAD(+) from nicotinate D-ribonucleotide: step 1/1.
EC: 2.7.7.18
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Q5DZX4 | MQQQIVEEMKVKVSIDPVEEIKKRVDFIKGKLLEAHCKSLILGISGGVDSTTCGRLAQLAVNELNLETQSSDYQFIAVRLPYGIQQDEDEAQLALQFIQPTHSISINIKNGVDGLHSANHIALKDTGLLPTDSAKIDFVKGNVKARARMIAQYEVAGYVGGLVLGTDHSAENITGFYTKFGDGACDLAPLFGLNKRQVREVAAQLGAPEQLVKKVPTADLEELAPQKADEDALSVSYDQIDDFLEGKKIDADAEDRLIKIYQMSQHKRKPIPTIYD | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 30351
Sequence Length: 276
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
A6TQC4 | MEIAMKVERVVAWLREQVEESGTTGLVVGISGGIDSAVVANLIYRAFPNQSLGVILPIRSHQDDIDDGLAVAIACGIKHTTVNLDNEHENVLSKAINALQKLELYDENKLRISDANLRARLRMSTLYTIANNVNSLVVGTDNAAELHTGYFTKYGDGGVDILPIAGLTKREVYQWGEYLGVPQSVLNREPSAGLWEGQTDEKEMGTTYEMIDDFLEGKEVPQKDKEIIERLHGISHHKRVMPPLPNI | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 27347
Sequence Length: 247
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
O67091 | MLNLTLAQLNFTVGDVEGNKEKILKVIDEYSEKSHIIAFPELSLSGYPPEDLLLQPHFLKECEKAFDQIIHHTRNYDVIVAVGLPYYEFDLYNALAVIHRGEVLGIYKKHFLPNYSVFDEYRYFRKGEEPLMIEVNGHKVSFSICEDIWYPDGVERQTALSGAELIVNVNASPYHVNKYSFKESFLKSRAEDNLCFVAYVNLVGGQDELVFDGRSIVISPFGKLVARAKAFEEDILTVTLDLGEAKRKRLLDLRWREGSYGREKVNVKRSVSLPDKEFFRGRIEENPKEEEEIYAALKLSLRDYVRKNGFEKVVLGLSGGIDSSFVACLAVDALGRENVKGVYMPSQFSSKESYEDAKALAQNLGIEFHVIPIKEIYRAYFNEFEKEICEITFDVADENIQARIRANILFYFSNKFRYLVLSTSNKSETAVGYTTIYGDMAGGFAPIKDVYKTWVYKLARYRNSISPDIPERVFKKPPSAELRPNQTDQDVLPPYEILDQILMLYIEENLSPEEIIRKGLPRDAVYKTINMIRKNEYKRKQAPIGPKITSRAFGKDWRMPVTNKFFK | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) + L-glutamate + NAD(+)
Sequence Mass (Da): 65272
Sequence Length: 567
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (L-Gln route): step 1/1.
EC: 6.3.5.1
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Q9C723 | MRLLKVATCNLNQWAMDFESNMKNIKASIAEAKAAGAVIRLGPELEVTGYGCEDHFLELDTVTHAWECLKELLLGDWTDDILCSIGMPVIKGAERYNCQVLCMNRRIIMIRPKMWLANDGNYRELRWFTAWKQREELEEFQLPIEISEALEQKSVPFGYGYIQFIDTAVAAEVCEELFSPLPPHAELALNGVEVFMNASGSHHQLRKLDIRLNAFMGATHARGGVYMYSNQQGCDGSRLYYDGCACIVVNGNVVAQGSQFSLRDVEVIISQVDLDAVASLRGSISSFQEQASCKVKVSSVAVPCRLTQSFNLKMTLSSPKKIIYHSPQEEIAFGPACWMWDYLRRSGASGFLLPLSGGADSSSVAAIVGCMCQLVVKEIAKGDEQVKADANRIGNYANGQFPTDSKEFAKRIFYTVFMGSENSSEETKRRSKQLADEIGAWHLDVCIDGVVSAVLSLFQTVTGKRPRYKVDGGSNAENLGLQNIQARMRMVLAFMLASLLPWVHSKPGFYLVLGSSNVDEGLRGYLTKYDCSSADINPIGSISKMDLRLFLKWAATNLGYPSLAEIEAAPPTAELEPIRSDYSQLDEVDMGMTYEELSVYGRMRKIFRCGPVSMFKNLCYKWGTKLSPAEVAEKVKYFFKYYSINRHKMTVLTPSYHAESYSPEDNRFDLRQFLYNSKWPYQFKKIDEIVDSLNGDSVAFPEEEANSNKEIGVVAANSGDPSAGL | Catalytic Activity: ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) + L-glutamate + NAD(+)
Sequence Mass (Da): 80900
Sequence Length: 725
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (L-Gln route): step 1/1.
EC: 6.3.5.1
|
O29262 | MNFEKVVERICDFIRGVVSSSGSTGVVLGLSGGVDSATVAYLCVRALGSERVFALIMPETGVTPEQDVEDAINVAESLGMEYKLIEINDIVRVFKEKAGEGSKIAEANLKPRIRMVLNYYHANSMNRLVAGTGNKSELMVGYFTKYGDGGVDFLPIGDLYKTEVFQLAAYLGVPRRIIEKKPSARLWPGQTDEEEMGISYAELDEILKLIEKGERRDDEKFRRVVQMVERSRHKREMPPVARVRDLL | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 27653
Sequence Length: 247
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
Q8ZXL4 | MFVYDVVNALDYEKARSIITAFISQYVQRAGSRGVVVGISGGVDSTVAAALAVEALGRQRVLGLLMPSLYTPPEDLKDALDVINALGVEWKRVDITPIYDAFVKTLPDFSQENRVAAGNILPRIRMTVLYYYANKYNLLVMGTGDRSELLLGYFTKYGDGGVDFLPIGSLFKLQVRELAARLGFADIAKKPSSPRLWQGHTAEGELGASYEVIDQVLYAVFDLKKPPEEVRGFFGEVVDIVITRVKKNIHKLTPPAYPDITPARRNV | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 29517
Sequence Length: 267
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
O57921 | MRILDYDKVIERILEFIREKGNNGVVIGISGGVDSATVAYLATKALGKEKVLGLIMPYFENKDVEDAKLVAEKLGIGYKVINIKPIVDSFVENLELNLDRKGLGNIMSRTRMIMLYAHANSLGRIVLGTSNRSEFLTGYFTKWGDGASDYAPIINLYKTEVWEIAKRIGVPERIVKKKPSAGLWEGQTDEDELGISYNLLDEILWRMIDLKIGKEEIAKDLGIPLSLVERVEELIKKSEHKRRLPIGPSFEDLIVGP | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 28862
Sequence Length: 257
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
Q92TY6 | MNIRPDQNRLVFSADTLKIDEAAEADRIVAGLRAQLRSLRKRGLVLGLSGGIDSSVSVALAVRAVGAKNVFCLFMPENDSDPESLRLGRLVAETFGVEAVVEDIGPTLDAMGCYQRRDAFIRELVPDYGPGWASKIVIANALEGDGYNISSLVVQDPEGKQTKLRMPPSVYLGIVAATNMKQRTRKQIEYYHADRLNFAVLGTPNRLEYDQGFFVKNGDGAADVKPIAHLYKSQVYALAGHLGIPEEIRRRPPTTDTYSLEQTQEEFYFSLPYDRMDLCLFGLNNGLSADEVGRAANLGVAQVKRVWADIAAKRKATRYLHLGPQLVQPVEEIE | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 36913
Sequence Length: 334
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
Q03638 | MTDRFRITLAQLNPTVGALAANAEKAMAAWQAGRAAGADLVALPEMFLTGYQTQDLVLKPAFLRDAMAAMAALAAQVVDGPALGIGGPYVDETGSYNAWWVLKDGRVIARALKHHLPHDDVFDEMRLFDQGPVSDPLRLGPVALGVPVCEDAWHPDVAGALAAAGAEVLMVPNGSPYRRGKLDLRRQVTGARVAETGLPLLYLNMVGGQDDQLFDGASFVLNPDGSVAVQLPAFEEAVVHVDLERGAADWRAVPADIVAPPGDIEQDYRAMVLGLQDYLRKSGFSRVVLGLSGGIDSALVAVIAADALGAGNVHCVMLPSRYTSQGSLDDAADLARRLGARLDTVEIEGPRAAVEGALAHVLAGTAPDVTEENIQSRLRGVILMAISNKFGAMLLTTGNKSEVAVGYCTIYGDMAGGYNPLKDLYKTRVFETCRWRNATHRPWMQAPAGEIIPVAIIDKPPSAELRENQTDQDSLPPYEVLDAILERLVEGDQSVDQIVAAGFDRATVKRIEHLLYISEWKRFQSAPGPRLTTRAFWLDRRYPMVNRWRDQS | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + H2O + L-glutamine = AMP + diphosphate + H(+) + L-glutamate + NAD(+)
Sequence Mass (Da): 59706
Sequence Length: 552
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (L-Gln route): step 1/1.
EC: 6.3.5.1
|
Q97WN9 | MHEYIRKSLTIDCEAVTNYIVERIREYLEFSNKKGGVIGVSGGVDSAVTATLLAKATDNFFILLMPSSSTPKIDLDDSFEMIKFLNAQNKYKLINIDEIVKSFSNKIETENKYIIGNIKARVRMIILYAYAQMLDYLVVGTGDKSELLLGYFTKYGDGGVDVLPIGDLYKTQVRMLGKCLGLPERIVTKPSSPALWEGQTAEGELGIDYETIDSILYLRFDEMRSEDEIVKMLGIPIDIVKKVDRLVKISQHKRLPPEIFRLSGRAINSDWRFPRRWA | Function: Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses ammonia as a nitrogen source.
Catalytic Activity: ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) + NAD(+)
Sequence Mass (Da): 31593
Sequence Length: 278
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1.
EC: 6.3.1.5
|
Q2KW92 | MHFPIVALIGRYQDTGLDAPLRALAAMLTQAGRRVLVDADTARNTAVHEYPVATMQEIGESASLAVVMGGDGTVLGVARHLAPYGVPLIGINHGRLGFITDIPLQDAHDALARVLDGNFQIEERMLLQGSVWRGDALMYTASALNDVVLNRAGRGGMIEMRVELDGVYMYTQRADGLIIATPTGSTAYALSANGPLLHPGLNAMVLVPVAPQSLSNRPIVIPDTGVLNMTLTAIGRVETGASAHFDMQTWSDLQLGDRITVQRAPHTARLVHPQGYSFFSTLRRKLHWNQMPQVSDNIE | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 32320
Sequence Length: 299
Subcellular Location: Cytoplasm
EC: 2.7.1.23
|
O51291 | MKNKVLLCINTLKSGASILGNDVKVYLETKYFVEVVLIDVGRPLFSFPKENFLFLITLGGDGTVLLAVNLLLENENIDIPIISINMGNVGFLADIKIEDFKKVIDRFFNNSLVINKKFLLHVTVSQHGKDLISKYALNDIIIRSSVLNKMIYVDLMVNSESFLSYKSDGIIVSTPTGSTGYSFSAGGPILEADLEGFXLTPISPHSVYNRSFVFSKLSKLSISFSKEYFIAAASIFLDGINFGSFGVDVVFEFKISSQSLNFVSFCTDTFVKRLKNKLL | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 30967
Sequence Length: 279
Subcellular Location: Cytoplasm
EC: 2.7.1.23
|
Q8YGW9 | MKDTSLALHFVSSGTKESLSAQKDLVERYGHVAAEDADIIVALGGDGTMLQALRDFMNTGKPIYGMNRGSVGFLMNEFVIENLPERILAAQMETIRPLVMVAETDDAPPVEALAINEVSLFRQSYQAARIRITIDGKVRLQELVCDGVMVATPAGSTAYNLSAQGPILPLEAPLLALTPVSPFRPRRWGGALLPKHVTVRMDLLETEKRPVNAVADNNEVKSVTSVTVREAPNSQVTILFDKNHSWDERILTEQFRH | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 28261
Sequence Length: 257
Subcellular Location: Cytoplasm
EC: 2.7.1.23
|
P75508 | MKYKIFASTTPQTEPVLQKLKQVLKGCEAVEKGFDYLFVLGGDGFFVSTVANYNCHNCRVVGINTGHLGFYTSFNEKDLDDNFLQKLQQCHFQRISLLEVSVNGQQHLVLNELAVYTNTAYPINIFIDGEAWEFYRGSGLLIGPRTGSTALAKSAKGAVIFPGIDVLQIIEMNPLLHPNQVTIQSPIILPKETQVEFVVKKAFNPQQFPTFYCDGRKLELPNADTTLALKLVQSTPMFNISLKTQDFINKLKSTFIKQS | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 29034
Sequence Length: 259
Subcellular Location: Cytoplasm
EC: 2.7.1.23
|
B2A524 | MRSVGLIPNIQKDQVAEITSRMYKILSEHDIDVYLTHEGADLIGTESAGVSSDVMGEVAEMIIILGGDGTILKAAREYAPYDIPLLGINLGKMGFLAEIEANEVMAYLESLLTGNYTIEERMMLDATVLRDRKEITTFSALNDVIIAKGPFSRIIEVETKVGGNYLETYPGDGLIVTSPTGSTGYSFSAGGPIISSNLEVMMITPICPHLMHNRSVIISSDEVVTAKMKTNYAVVVLTVDGQQGFTLQDGDEIKVKKSNYKTKLVKLRRRSFYQLLNEKLTGGQEV | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 31323
Sequence Length: 286
Subcellular Location: Cytoplasm
EC: 2.7.1.23
|
Q82UK6 | MDSALFKTIALIGKHKNPDIVIPLLSLAEYLTDRGISVVLDSLTAAHISNSRYPILTLEEIGKQADLAIVLGGDGTMLNIARALVPFSVPLIGINQGRLGFLTDLTADTMHETLNDMLAGQFVVENRMLLTVEVTRNGESVFKELAFNDVVLHRGISSGMIELEVHINGEYVYSLRSDGLIIATPTGSTAYALSSGGPILHPGLNLMTLVPICPHTLSNRPIVIGADATIEIKVHFTTEIKIYTDSHSWFDLSEHDRVFIQRCPETIKLLHPVHHSYYRMLREKLGWSGILQKNSR | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 32659
Sequence Length: 296
Subcellular Location: Cytoplasm
EC: 2.7.1.23
|
Q3JBV4 | MAKPFKIIGLIGKQKDPRIAESLQQVADFLVAKGLTLMIDQETAALFPSHHWEAVTRHELGQRCDLAIVVGGDGTLLHVARSLADSGIPLLGIKLGRLGFLADVLPEALGTDLAAMLAGHYREEERFLLQAELEQESQSYLIGTALNDITTHIREVVRLIEFETYINGRFLNSQRSDGLVVATPTGSTAYALSAGGPILDVNLNAMVLVSICPHALSNRPLVIDADSLVEIVISEYNTTPGQVSCDGQPGIALKVGDKVKIYKRPGRVRLIHPTAHDHYSILRAKLHWGRKLG | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 31887
Sequence Length: 293
Subcellular Location: Cytoplasm
EC: 2.7.1.23
|
Q9PBQ0 | MEMMMTAAPRIAFLASTAEPAQRARQELMARYGDCSIEEADVLCALGGDGFMLRTLHRYGASGKPVYGMKLGSVGFLMNQYHDDLLERLQRAEPAKLRPLQMMAQTESGVSVESLAYNEVSLLRQTHQAAYISIDLNGQTRIDELTGDGVIVATPAGSTAYNYSAHGPILPLGSHTLALTPIAPYRPRRWRGAILKADTEIRFRVLDPYKRPVSVTADSHEIRDVVEVTIRESTEQRVTLLFDPEHNLEERIFSEQFAV | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 28852
Sequence Length: 259
Subcellular Location: Cytoplasm
EC: 2.7.1.23
|
Q8ZH09 | MNNRRFDCIGIVGHPRHPAALATHEILYHWLKARGYAVMVEQQIAHDLNLTDAITGSLADIGQKADLAVVVGGDGNMLGAARVLARYDIKVIGVNRGNLGFLTDLDPDNALQQLSDVLEGEYLSEQRFLLETHVRRTNQQSRISTAINEVVLHPGKVAHMIEFEVYIDDRFAFSQRSDGLIIATPTGSTAYSLSAGGPILTPTLDAIVLVPMFPHTLTARPLVISSSSTIRLKFSHITSDLEISCDSQIALPIQEGEEVLIRRSDFHLNLIHPKDYSYFNTLSTKLGWSKKLF | Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Catalytic Activity: ATP + NAD(+) = ADP + H(+) + NADP(+)
Sequence Mass (Da): 32398
Sequence Length: 293
Subcellular Location: Cytoplasm
EC: 2.7.1.23
|
Q58DX5 | MGENEASLPNTSLQGKKMAYQKVHADQRAPGHSQYLDNDDLQATALDLEWDMEKELEESGFDQFQLDGAENQNLGHSETIDLNLDSIQPATSPKGRFQRLQEESDYITHYTRSAPKSNRCNFCHVLKILCTATILFIFGILIGYYVHTNCPSDAPSSGTVDPQLYQEILKTIQAEDIKKSFRNLVQLYKNEDDMEISKKIKTQWTSLGLEDVQFVNYSVLLDLPGPSPSTVTLSSSGQCFHPNGQPCSEEARKDSSQDLLYSYAAYSAKGTLKAEVIDVSYGMADDLKRIRKIKNVTNQIALLKLGKLPLLYKLSSLEKAGFGGVLLYIDPCDLPKTVNPSHDTFMVSLNPGGDPSTPGYPSVDESFRQSRSNLTSLLVQPISAPLVAKLISSPKARTKNEACSSLELPNNEIRVVSMQVQTVTKLKTVTNVVGFVMGLTSPDRYIIVGSHHHTAHSYNGQEWASSTAIITAFIRALMSKVKRGWRPDRTIVFCSWGGTAFGNIGSYEWGEDFKKVLQKNVVAYISLHSPIRGNSSLYPVASPSLQQLVVEKNNFNCTRRAQCPETNISSIQIQGDADYFINHLGVPIVQFAYEDIKTLEGPSFLSEARFSTRATKIEEMDPSFNLHETITKLSGEVILQIANEPVLPFNALDIALEVQNNLKGDQPNTHQLLAMALRLRESAELFQSDEMRPANDPKERAPIRIRMLNDILQDMEKSFLVKQAPPGFYRNILYHLDEKTSRFSILIEAWEHCKPLASNETLQEALSEVLNSINSAQVYFKAGLDVFKSVLDGKN | Function: May be catalytically inactive.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 88682
Sequence Length: 795
Subcellular Location: Membrane
|
Q4JAT0 | MHRGLYPGRFQPFHIGHLEVVKWSMKHVDELIIVIGSAQESHTLSNPFTAGERIEMIRRTLDKENLDLSKVYIIPIPDIMMNSVWVSHIKTFAPNFDVIISRNPLVNRLFKEANVEVLQPPPFDRHKYNSTLIRRYIIEGNEEWKKLVPKSVLDYLLEIHGDERLRSIAGL | Catalytic Activity: ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate + NAD(+)
Sequence Mass (Da): 19935
Sequence Length: 171
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.1
|
Q6F999 | MYKFDYLVFIGRFQPFHFAHLQTIQIALQQSREVIIALGSAQPERNIKNPFLAEERQKMILANFSAEDQARIHFVNIIDVYNDQKWVEQVKQLVNAIIESRSHVGLIGHFKDESSYYLKLFPEWTMVELESLKESMSATPMREAYYEGKIIESAFPEGTIQFLKTFQDSEIYKQLQQKYRAQDSSNLI | Function: Dual substrate specificity enzyme that catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and the formation of deamido-NAD(+) (NaAD) from nicotinate mononucleotide (NaMN) . Shows nearly identical catalytic efficiency for both physiological substrates . Plays an essential role in all three routes of NAD biogenesis, de novo synthesis as well as the deamidating and nondeamidating salvage pathways .
Catalytic Activity: ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate + NAD(+)
Sequence Mass (Da): 22079
Sequence Length: 188
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
EC: 2.7.7.1
|
Q9YER8 | MKRLLVVGRFQPPHLGHLHTIKWALGRAEEVIVVVGSAQESYTLENPMTAGERVHALRLMLEELDDWCRRLMIAPVPDIAMNKVWVQYLKMLLPPFDGVVSGNELVLMLFEDMGLAALRPPMFRRGECSGTRIRRLMASGESGWEDCLHPQVRRYVEEIGLPERLRRLQEMR | Catalytic Activity: ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate + NAD(+)
Sequence Mass (Da): 19828
Sequence Length: 172
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.1
|
Q5V117 | MRGFYIGRFQPYHNGHHSMVERISEEVDELVLGIGSADDSHTTHDPFTAGERIMMITKAVAEYDLTTYVVPLEDINRNAVWVSHVESMCPDFDVAYSNNPLVVRLFEEAGIEVRQSPMFDRDRLEGSEIRQRMIDDESWRDRVPASVVEVIEEIHGIKRLQHVSDSDSLERYAATGESLPESLDDLDD | Catalytic Activity: ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate + NAD(+)
Sequence Mass (Da): 21482
Sequence Length: 188
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.1
|
B0R328 | MTRGFYIGRFQPFHTGHRRVIEQIATEVDELVVGIGSAGDSHSARNPFTAGERIMMITKALVEFNLVTYAVPIEDLERNAVWVSHVRSMCPKFEVAYSNNPLVIRLFNEAAVEVRQPPMYDRDVLEGAEIRRRMADGDDWESLVPDAVADVVAEIDGVERIQHVADTDANGHDSGLR | Catalytic Activity: ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate + NAD(+)
Sequence Mass (Da): 19820
Sequence Length: 177
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.1
|
A8AB26 | MRALFPGRFQPFHKGHLAVVKWSLERVDELVIVVGSAQESHTLQNPMTAGERVLAIRRALEDEGIDLRKVYIIPVPDILMNSAWVAHVRTYVPPFEAVVTRNPLVKVLFEEAGYEVLEPPPFGREKYVATNIRALMALGDPKWEEMVPRAVAEIIKELGIIRRMRELSKRD | Catalytic Activity: ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate + NAD(+)
Sequence Mass (Da): 19520
Sequence Length: 171
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from nicotinamide D-ribonucleotide: step 1/1.
Subcellular Location: Cytoplasm
EC: 2.7.7.1
|
B1YJ30 | MKWMIVEKAEELANVSYQLLKQEIVRHPEGLTIGLATGSSPLGVYEEWRKDRVDCRHVTTVNLDEYVGLSPDHPHSYHTFMQEHLFDAVDFKESYVPIGSTADPREESDRYEALVRQLGIDIQLLGIGSNGHIAFNEPGTPFDAKTHVTKLTESTRQANQRFFDRLEDVPTEAITMGIGTIMEAKKILLVASSERKAEAIRDMMEGPATTDCPATILQRHADVMVVLDEEAASLLSDEAKRTGRAAYTNFMK | Function: Catalyzes the reversible isomerization-deamination of glucosamine 6-phosphate (GlcN6P) to form fructose 6-phosphate (Fru6P) and ammonium ion.
Catalytic Activity: alpha-D-glucosamine 6-phosphate + H2O = beta-D-fructose 6-phosphate + NH4(+)
Sequence Mass (Da): 28251
Sequence Length: 252
Pathway: Amino-sugar metabolism; N-acetylneuraminate degradation; D-fructose 6-phosphate from N-acetylneuraminate: step 5/5.
EC: 3.5.99.6
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O52380 | MVDFKTYFELLNLYSDYAMVCDSANWEKWPDFFIETGTYRLQPRENFEQGLPLCLLALESKAMIRDRVYGVKETMYHDPYYQRHIVGTPRVLSVERDADGERITAEASYAVIRTKYDGDSTIFNAGYYRDVIVRTPEGLKLKSRLCVYDSEMIPNSVIYPI | Function: Oxygenase component of the salicylate 5-hydroxylase (S5H) multicomponent enzyme system which catalyzes the 5-hydroxylation of salicylate to gentisate. Active only on substrates with a ring-substituted carboxylate group with an adjacent hydroxyl group. Primarily active against salicylate and substituted salicylates, but not against 2-hydroxycinnamate, 3-hydroxycinnamate, 2-hydroxyphenylacetate, 3-hydroxyphenylacetate, 2-hydroxybenzophenone, 1-hydroxy-2-naphthoate, 4-methoxysalicylate or 2-hydroxyacetophenone.
Catalytic Activity: H(+) + NADH + O2 + salicylate = 2,5-dihydroxybenzoate + H2O + NAD(+)
Sequence Mass (Da): 18813
Sequence Length: 161
Pathway: Aromatic compound metabolism; naphthalene degradation.
EC: 1.14.13.172
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Q9SCL7 | MATVTSNASPKSFSFTVSNPFKTLIPNKSPSLCYPTRNKNHHRLGFSIKATVSTPPSIATGNAPSPDYRVEILSESLPFIQKFRGKTIVVKYGGAAMTSPELKSSVVSDLVLLACVGLRPILVHGGGPDINRYLKQLNIPAEFRDGLRVTDATTMEIVSMVLVGKVNKNLVSLINAAGATAVGLSGHDGRLLTARPVPNSAQLGFVGEVARVDPSVLRPLVDYGYIPVIASVAADDSGQAYNINADTVAGELAAALGAEKLILLTDVAGILENKEDPSSLIKEIDIKGVKKMIEDGKVAGGMIPKVKCCIRSLAQGVKTASIIDGRRQHSLLHEIMSDEGAGTMITG | Function: Involved in the arginine biosynthetic pathway via the intermediate compound ornithine.
Catalytic Activity: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L-glutamyl 5-phosphate
Sequence Mass (Da): 36595
Sequence Length: 347
Pathway: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4.
Subcellular Location: Plastid
EC: 2.7.2.8
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Q54PM7 | MSKEIFIGIDGGGTKTSTVAVDSNGQELARHTSPCSNYHSVGEDLAKAAINEGIKYVIRKVKETITDDDNKEVTVGSICLGMSGVDREKDKLLVKSWVTELLGESINYSIHNDAIVALSSGTQGKLFGVVIICGTGCISLGFNREGVSGRSGGWGPLLGDYGSGYQIGYDILRHVLKAKDQVGPKTSLTQVLLEKLQLTKEEDLISWAYDPKTQSWQKFAQLSPLAFEQAQLGDEISNLILVDAANALYDLINSVIKKLGLDKEEKFPLVYTGGNIERKGILSDLLSKKIMENYPNAEILNTTCDPSMGAALLALNSKK | Function: Converts N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, into GlcNAc 6-phosphate. Also has ManNAc kinase activity (By similarity).
Catalytic Activity: ATP + N-acetyl-D-glucosamine = ADP + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Mass (Da): 34504
Sequence Length: 319
EC: 2.7.1.59
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Q8X8E1 | MYYGFDIGGTKIALGVFDSGRQLQWEKRVPTPRDSYDAFLDAVCELVAEADQRFGCKGSVGIGIPGMPETEDGTLYAANVPAASGKPLRADLSARLDRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLIFNGKPITGKSYITGEFGHMRLPVDALTMMGLDFPLRRCGCGQHGCIENYLSGRGFAWLYQHYYHQPLPAPEIIALYDQGDEQARAHVERYLDLLAVCLGNILTIVDPDLVVIGGGLSNFPAITTQLADRLPRHLLPVARVPRIERARHGDAGGMRGAAFLHLTD | Function: Catalyzes the phosphorylation of N-acetyl-D-glucosamine (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P.
Catalytic Activity: ATP + N-acetyl-D-glucosamine = ADP + H(+) + N-acetyl-D-glucosamine 6-phosphate
Sequence Mass (Da): 33012
Sequence Length: 303
Pathway: Cell wall biogenesis; peptidoglycan recycling.
EC: 2.7.1.59
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B5F8E5 | MGPVMLNVEGCELDAEEREILAHPLVGGLILFTRNYHDPEQLRELVRQIRAASRNHLVVAVDQEGGRVQRFREGFTRLPAAQSFFALHGLEEGGRLAQEAGWLMASEMIAMDIDISFAPVLDVGHISAAIGERSYHADPAKALAMATRFIDGMHDAGMKTTGKHFPGHGAVTADSHKETPCDPRPETDIRGKDMSVFRTLISENKLDAIMPAHVIYRAIDPRPASGSPYWLKTVLRQELGFDGVIFSDDLSMEGAAIMGSYAERAQASLDAGCDMILVCNNRKGAVSVLDNLSPIKAERVTRLYHKGSFSRRELMDSARWKTASAQLNQLHERWQEEKAGH | Function: Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 37698
Sequence Length: 341
Pathway: Cell wall biogenesis; peptidoglycan recycling.
Subcellular Location: Cytoplasm
EC: 3.2.1.52
|
Q080R9 | MSYLMMDLAGLTVSATETAQLQHPQVGGIILFSRNCENKNQLIELVKSVRSIRPELLIAVDHEGGRVQRFREGFSLIPAMGDILPAAKGDLTLAKQWAKECGFLMAVELLACDIDLSFAPVLDVNGISEVIGKRSFSAVPDEVSALAQQFIIGMNEAGMAAVGKHFPGHGSVAADSHIAMPVDPRTKEQVEAFDMQPFKHLIGSQQLQGVMPAHVVYSNIDPNPAGFSSYWLQTILRQQLGFDGVIFSDDLGMKGASFAGNYLGRAKAALDAGCDMILVCNDSVGVNALLTEFDWPAAEPTHTALSLKGNTAQASQALEQQTRWQAAQLLAMDITRIAQSL | Function: Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 36725
Sequence Length: 341
Pathway: Cell wall biogenesis; peptidoglycan recycling.
Subcellular Location: Cytoplasm
EC: 3.2.1.52
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Q8EEW2 | MSYLMLDLLSLDVSEAEAEMLRHPQVGGLILFSRNFTSREQLIALVQQIRQIRPEILIAVDHEGGRVQRFREGFTLIPAMGDILPAAKGDMALAKRWACELGFLMAIELLACDIDLSFAPVLDLNGISQVIGKRSFSANPDEVIALARSFIEGMAQAGMGAVGKHFPGHGSVAADSHIAQPIDEREGEVIFNQDILPFKELIFNGKLSGIMPAHVIYPKVDPNPAGFSSYWLKQILRKELGFNGVIFSDDLGMKGASFAGDYVGRAKAALDAGCDMILVCNDNPGVMTLLNGFVWPEAAPQHPASLLKPNMAQTALALENSARWENAKQLAEQIQLAQQAKV | Function: Plays a role in peptidoglycan recycling by cleaving the terminal beta-1,4-linked N-acetylglucosamine (GlcNAc) from peptide-linked peptidoglycan fragments, giving rise to free GlcNAc, anhydro-N-acetylmuramic acid and anhydro-N-acetylmuramic acid-linked peptides.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 37193
Sequence Length: 342
Pathway: Cell wall biogenesis; peptidoglycan recycling.
Subcellular Location: Cytoplasm
EC: 3.2.1.52
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Q52I78 | MNAAAEAEFNILLATDSYKVTHYKQYPPNTSKVYSYFECREKKTENSKIRKVKYEETVFYGLQYILNKYLKGKVVTKEKIQEAKEVYKEHFQDDVFNEKGWNYILEKYDGHLPIEVKAVPEGSVIPRGNVLFTVENTDPECYWLTNWIETILVQSWYPITVATNSREQKKILAKYLLETSGNLDGLEYKLHDFGYRGVSSQETAGIGASAHLVNFKGTDTVAGIALIKKYYGTKDPVPGYSVPAAEHSTITAWGKDHEKDAFEHIVTQFSSVPVSVVSDSYDIYNACEKIWGEDLRHLIVSRSTEAPLIIRPDSGNPLDTVLKVLDILGKKFPVTENSKGYKLLPPYLRVIQGDGVDINTLQEIVEGMKQKKWSIENIAFGSGGALLQKLTRDLLNCSFKCSYVVTNGLGINVFKDPVADPNKRSKKGRLSLHRTPGGNFVTLEEGKGDLEEYGHDLLHTVFKNGKVTKSYSFDEVRKNAQLNIELEAAPH | Function: Catalyzes the condensation of nicotinamide with 5-phosphoribosyl-1-pyrophosphate to yield nicotinamide mononucleotide, an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway. The secreted form behaves both as a cytokine with immunomodulating properties and an adipokine with anti-diabetic properties, it has no enzymatic activity, partly because of lack of activation by ATP, which has a low level in extracellular space and plasma. Plays a role in the modulation of circadian clock function. Plays a role in the modulation of circadian clock function. NAMPT-dependent oscillatory production of NAD regulates oscillation of clock target gene expression by releasing the core clock component: CLOCK-BMAL1 heterodimer from NAD-dependent SIRT1-mediated suppression.
Catalytic Activity: beta-nicotinamide D-ribonucleotide + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + H(+) + nicotinamide
Sequence Mass (Da): 55374
Sequence Length: 491
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinamide D-ribonucleotide from 5-phospho-alpha-D-ribose 1-diphosphate and nicotinamide: step 1/1.
Subcellular Location: Nucleus
EC: 2.4.2.12
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Q9SCP7 | MENESSESRNRARLAIMELANMISVPMSLNAAVRLGIADAIWNGGANSPLSAAEILPRLHLPSHTTIGGDPENLQRILRMLTSYGVFSEHLVGSIERKYSLTDVGKTLVTDSGGLSYAAYVLQHHQEALMRAWPLVHTAVVEPETEPYVKANGEAAYAQYGKSEEMNGLMQKAMSGVSVPFMKAILDGYDGFKSVDILVDVGGSAGDCLRMILQQFPNVREGINFDLPEVVAKAPNIPGVTHVGGDMFQSVPSADAIFMKWVLTTWTDEECKQIMKNCYNALPVGGKLIACEPVLPKETDESHRTRALLEGDIFVMTIYRTKGKHRTEEEFIELGLSAGFPTFRPFYIDYFYTILEFQK | Function: Involved in nicotinate detoxification in planta . Catalyzes the conversion of nicotinate to N-methylnicotinate, which is a detoxified form of endogenous nicotinate in planta .
Catalytic Activity: nicotinate + S-adenosyl-L-methionine = N-methylnicotinate + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39688
Sequence Length: 359
Subcellular Location: Cytoplasm
EC: 2.1.1.7
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I1M2U5 | MEKEESTEQRKQARLAIMELANMISVPMALNAVVRLNVADAIWQGGANNPLSAAEILPRLLPAGGGDAENLQRLLRMLASYGVFYEHLSAGERKYSLTDVGKTLVTDEQGLSYAHYVLQHHQDALMRAWPMVHEAVVDPTKEPFERANGEPAYGYYLKHPEMNDLMVRAMSGVSVPFIRAMLEGYDGFQGVEKLVDVGGSGGDCLRMILEKHPTIKEGINFDLPEVVAKAPQIPFVTHVGGDMFKFIPQGDAIFMKWVLTTWTDEECKHIMQNCHKALPEGGKLIACEPVLPEDSDESHRTRALLEGDIFVMTIYRAKGKHRTEEQFRQLAIDAGFPRFRAFHVDHFYTVLEFQK | Function: Involved in nicotinate detoxification in planta . Catalyzes the conversion of nicotinate to N-methylnicotinate, which is a detoxified form of endogenous nicotinate in planta .
Catalytic Activity: nicotinate + S-adenosyl-L-methionine = N-methylnicotinate + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39914
Sequence Length: 355
EC: 2.1.1.7
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