ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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E0Y3X0 | MAIEEKSTSAEPGPYDALSRFSSLTGEDDRKWWEHTGPVLEKVMRDSGYELQSQYIYLYFVQQHLIPYLGKFPTRGQDDHRWQSNLTPYKVPYELSWNVSHKVVRISWDPVCDASGTENDAFNKKAIHDCTRQLAELDSTVILDRYRLLHKDLVITDEEEQQLLRRDVLPKSGRGQHNLAVDFQEGGITLKVYFYPYMKFLATGTPIEELFFSAIEKLRIADIDEAVGMLKCFLSPKSDDGKPSVDEKVFPSLLACDLCDPSKSRIKYYVIDKWVKWERIANLWTIGGRRLEDPYCAKGLALLKELWDLLAIPEGDRGDIWPNLVLGQPPTHLMTTIANYTLSPASRFPEPQVYLTTFGLNDMAIIDALTAFYERVGFTDMAKSYKKNVQSYYPNLDLNQTNWVHEAVSFSYRNSKPYLSVYYSPF | Function: Prenyltransferase; part of the gene cluster that mediates the biosynthesis of notoamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first step of notoamide biosynthesis involves coupling of L-proline and L-tryptophan by the bimodular NRPS notE, to produce cyclo-L-tryptophan-L-proline called brevianamide F . The reverse prenyltransferase notF then acts as a deoxybrevianamide E synthase and converts brevianamide F to deoxybrevianamide E via reverse prenylation at C-2 of the indole ring leading to the bicyclo[2.2.2]diazaoctane core . Deoxybrevianamide E is further hydroxylated at C-6 of the indole ring, likely catalyzed by the cytochrome P450 monooxygenase notG, to yield 6-hydroxy-deoxybrevianamide E (Probable). 6-hydroxy-deoxybrevianamide E is a specific substrate of the prenyltransferase notC for normal prenylation at C-7 to produce 6-hydroxy-7-prenyl-deoxybrevianamide, also called notoamide S . As the proposed pivotal branching point in notoamide biosynthesis, notoamide S can be diverted to notoamide E through an oxidative pyran ring closure putatively catalyzed by either notH cytochrome P450 monooxygenase or the notD FAD-linked oxidoreductase (Probable). This step would be followed by an indole 2,3-epoxidation-initiated pinacol-like rearrangement catalyzed by the notB FAD-dependent monooxygenase leading to the formation of notoamide C and notoamide D . On the other hand notoamide S is converted to notoamide T by notH (or notD), a bifunctional oxidase that also functions as the intramolecular Diels-Alderase responsible for generation of (+)-notoamide T (Probable). To generate antipodal (-)-notoaminide T, notH' (or notD') in Aspergillus versicolor is expected to catalyze a Diels-Alder reaction leading to the opposite stereochemistry (Probable). The remaining oxidoreductase notD (or notH) likely catalyzes the oxidative pyran ring formation to yield (+)-stephacidin A (Probable). The FAD-dependent monooxygenase notI is highly similar to notB and is predicted to catalyze a similar conversion from (+)-stephacidin A to (-)-notoamide B via the 2,3-epoxidation of (+)-stephacidin A followed by a pinacol-type rearrangement (Probable). Finally, it remains unclear which enzyme could be responsible for the final hydroxylation steps leading to notoamide A and sclerotiamide (Probable).
Catalytic Activity: 6-hydroxydeoxybrevianamide E + dimethylallyl diphosphate = diphosphate + notoamide S
Sequence Mass (Da): 49102
Sequence Length: 426
Pathway: Alkaloid biosynthesis.
EC: 2.5.1.-
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L7WR40 | MRDIRELLLVLFTSCLALGSVPSSFDGDRYCRCQPGEACWPSLADWQALNMSIQGTLVEVRPIGHVCHEPTYNKADCERVSKLSSNGTWRASQPGAQQEHAWEVSLSRNESCYVGPANPAEPCGQGRIPRYSAMVETTEQAQKAIRFARERRLRLVIKNTGHDSGGRSSAVDSFQILTQRLKDISFIEEFTPTLAETRGPSVRIGAGVLTKELYAVADEHGYTAMGGECATVGVAGGYIQGGGVSTALTPMMGLAADLVQEFEVISAEGSLVIANEFQNQDLFWALRGGGGGTVGLVTSITMPVFGAIPANISELSFESQQPDEAFWTAVKEMIYVTRDITTGGNSGQYWVGRGPTGSYFVRQTLFFLGETDIEPADKMGSLLRVLQDQEIAFRFNVTAYPRLSSFLAIPQGEFVGGIAFHQENILIPQGFYDSPEGPAQLVDRLAEVKLNPGDMWVANTLGGQVMANKDVDNAMHSGWRTASVLLVGNRIFEPALKSQLDVQERLTAVEGPLLHSIGQPAPEAIYLNEADADLENWQDWFWGEKYARLRDIKSKWDPDDLFLVRHGVGSEDWDEDGMCRMQLSPQECPVREHSRCTCKFFECAMLHVPGLL | Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of notoamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first step of notoamide biosynthesis involves coupling of L-proline and L-tryptophan by the bimodular NRPS notE', to produce cyclo-L-tryptophan-L-proline called brevianamide F (Probable). The reverse prenyltransferase notF' then acts as a deoxybrevianamide E synthase and converts brevianamide F to deoxybrevianamide E via reverse prenylation at C-2 of the indole ring leading to the bicyclo[2.2.2]diazaoctane core (Probable). Deoxybrevianamide E is further hydroxylated at C-6 of the indole ring, likely catalyzed by the cytochrome P450 monooxygenase notG', to yield 6-hydroxy-deoxybrevianamide E (Probable). 6-hydroxy-deoxybrevianamide E is a specific substrate of the prenyltransferase notC' for normal prenylation at C-7 to produce 6-hydroxy-7-prenyl-deoxybrevianamide, also called notoamide S (Probable). As the proposed pivotal branching point in notoamide biosynthesis, notoamide S can be diverted to notoamide E through an oxidative pyran ring closure putatively catalyzed by either notH' cytochrome P450 monooxygenase or the notD' FAD-linked oxidoreductase (Probable). This step would be followed by an indole 2,3-epoxidation-initiated pinacol-like rearrangement catalyzed by the notB' FAD-dependent monooxygenase leading to the formation of notoamide C and notoamide D (Probable). On the other hand notoamide S is converted to notoamide T by notH' (or notD'), a bifunctional oxidase that also functions as the intramolecular Diels-Alderase responsible for generation of (-)-notoamide T (Probable). To generate antipodal (+)-notoaminide T, notH (or notD) in Aspergillus strain MF297-2 is expected to catalyze a Diels-Alder reaction leading to the opposite stereochemistry (Probable). The remaining oxidoreductase notD' (or notH') likely catalyzes the oxidative pyran ring formation to yield (-)-stephacidin A (Probable). The FAD-dependent monooxygenase notI' is highly similar to notB' and is predicted to catalyze a similar conversion from (-)-stephacidin A to (+)-notoamide B via the 2,3-epoxidation of (-)-stephacidin A followed by a pinacol-type rearrangement (Probable). Finally, it remains unclear which enzyme could be responsible for the final hydroxylation steps leading to notoamide A and sclerotiamide (Probable).
Sequence Mass (Da): 67308
Sequence Length: 612
Pathway: Alkaloid biosynthesis.
EC: 1.-.-.-
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I4AY86 | MTAPELRAPAGHPQEPPARSSPAQALSSYHHFPTSDQERWYQETGSLCSRFLEAGQYGLHQQYQFMFFFMHHLIPALGPYPQKWRSTISRSGLPIEFSLNFQKGSHRLLRIGFEPVNFLSGSSQDPFNRIPIADLLAQLARLQLRGFDTQCFQQLLTRFQLSLDEVRQLPPDDQPLKSQGAFGFDFNPDGAILVKGYVFPYLKAKAAGVPVATLIAESVRAIDADRNQFMHAFSLINDYMQESTGYNEYTFLSCDLVEMSRQRVKIYGAHTEVTWAKIAEMWTLGGRLIEEPEIMEGLARLKQIWSLLQIGEGSRAFKGGFDYGKASATDQIPSPIIWNYEISPGSSFPVPKFYLPVHGENDLRVARSLAQFWDSLGWSEHACAYPDMLQQLYPDLDVSRTSRLQSWISYSYTAKKGVYMSVYFHSQSTYLWEED | Function: Deoxybrevianamide E synthase; part of the gene cluster that mediates the biosynthesis of notoamide, a fungal indole alkaloid that belongs to a family of natural products containing a characteristic bicyclo[2.2.2]diazaoctane core . The first step of notoamide biosynthesis involves coupling of L-proline and L-tryptophan by the bimodular NRPS notE', to produce cyclo-L-tryptophan-L-proline called brevianamide F (Probable). The reverse prenyltransferase notF' then acts as a deoxybrevianamide E synthase and converts brevianamide F to deoxybrevianamide E via reverse prenylation at C-2 of the indole ring leading to the bicyclo[2.2.2]diazaoctane core . Deoxybrevianamide E is further hydroxylated at C-6 of the indole ring, likely catalyzed by the cytochrome P450 monooxygenase notG', to yield 6-hydroxy-deoxybrevianamide E (Probable). 6-hydroxy-deoxybrevianamide E is a specific substrate of the prenyltransferase notC' for normal prenylation at C-7 to produce 6-hydroxy-7-prenyl-deoxybrevianamide, also called notoamide S (Probable). As the proposed pivotal branching point in notoamide biosynthesis, notoamide S can be diverted to notoamide E through an oxidative pyran ring closure putatively catalyzed by either notH' cytochrome P450 monooxygenase or the notD' FAD-linked oxidoreductase (Probable). This step would be followed by an indole 2,3-epoxidation-initiated pinacol-like rearrangement catalyzed by the notB' FAD-dependent monooxygenase leading to the formation of notoamide C and notoamide D (Probable). On the other hand notoamide S is converted to notoamide T by notH' (or notD'), a bifunctional oxidase that also functions as the intramolecular Diels-Alderase responsible for generation of (-)-notoamide T (Probable). To generate antipodal (+)-notoaminide T, notH (or notD) in Aspergillus strain MF297-2 is expected to catalyze a Diels-Alder reaction leading to the opposite stereochemistry (Probable). The remaining oxidoreductase notD' (or notH') likely catalyzes the oxidative pyran ring formation to yield (-)-stephacidin A (Probable). The FAD-dependent monooxygenase notI' is highly similar to notB' and is predicted to catalyze a similar conversion from (-)-stephacidin A to (+)-notoamide B via the 2,3-epoxidation of (-)-stephacidin A followed by a pinacol-type rearrangement (Probable). Finally, it remains unclear which enzyme could be responsible for the final hydroxylation steps leading to notoamide A and sclerotiamide (Probable).
Catalytic Activity: brevianamide F + dimethylallyl diphosphate = deoxybrevianamide E + diphosphate
Sequence Mass (Da): 49567
Sequence Length: 435
Pathway: Alkaloid biosynthesis.
EC: 2.5.1.109
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A6R538 | MAPARPILLRFESRNGQFRLTVNPTDEFPSLLPKVLDNLPKNTAPPSIVLSNKPIGTGGQERNISTLKGVTIQRVGLSHGDKLFIGYEEETAVVNGSSSEHPSSISKSQNAPRRLDGVAVRQQEQAPPVPTPTSETLIKNPWEAVKQSPLDDRLDRKDGKISRGLDHKMCRHGPKGMCDYCMPLEPYAPEYLAEKKIKHLSFHSYLRKINSSTNKPELKSSYIPPLSEPDYRVKRDCPSGHPAWPEGICTKCQPSAITLQPQPFRMVDHVEFSSPDLINSLLDFWRKSGTQRLGFLYGTYEEYTEVPLGIKAVVQAIYEPPQVGEVDGVTLHEWGNEKDVDEVAKFCGLEKIGVIFTDLLDAGAGDEIVFAAQLQARYPKATKWSETGRFGSNFVTCVLSGDEDGAISISAYQASNSAVEMVKADIIEPSADPGVMLVQQENHSDDDASKARYIPEVFYRKVNEYGANVQENAKPSFPVEYLLVTLTHGFPTDPDVMFNNSTFPIENREVIGESQDLRMLADKLVSHGDPNKTICGVSDFHLLCFLNSLGILNKDEEFLLCTVARSHDTADGMQLINTSGWATLVTILQESGERPPKRSWPFQSQTFISSHQRSKHPQAPKSEHPQSDSEQLAKRFKGASLG | Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 71205
Sequence Length: 642
Subcellular Location: Cytoplasm
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Q74ZJ1 | MILRFRSKHGMQRVNCEGSEQFGTVLDRWVKLVHERAPREAMEVGVAERQIETRIAAEMAQKTVEQLGLKHGDMLSVSFKETGGSLAVAAAPERSSELAVDRELAREEGLIRRSHSRLCRHGDRGMCEYCSPLPPWDRGYQQEQNLKHISFHAHVKELNEHTNKKASGSTYIPPLSPPDFHVNKHCPAPHEPWPRGICSKCQPSAISLQQQEFRMVDHVEFQHSELVNEFINTWRSTGMQRFGYLYGRYARYDNTPLGIKAVVEAIWEPEQHDEQDGLTMDTVAVRVSVAAVDAIAADMGLMRLGMIFTDLTDSGSGDGSVFCKRHKDSFFLSSLEVITAARHQLHHRNACRFSDQGFYSSKFVTCVVSGNLQGEIDVAAYQVSTDAEALVDADIISGSTHPSMAYINEPSAERYVPEIFYMRRNEYGITIKENAKPAFPVDYLIVSLTHGFPVAADTPPTFQAHTGFPWANRQAMGQSQDYLELRRVLLPSIAAGDYTELHRRLSSFHLLLYLHSLQILDASEWRRLVTVATTPAPRGVEAVYDLISGPGWQTLVMILQEAA | Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 63253
Sequence Length: 563
Subcellular Location: Cytoplasm
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A1CS06 | MAATRPIILRFESRNGQFRLSVSPQELFPTLKQKILENLPKDVEPSSITLSNKPIGTGGEERSLDGLEGVSIEQVGLKHGDKLFVGYQERKGGETTPAKAHAAADSLRRLNGALVPQTETVTFRPPTSSSATVKNPWEVVQQSPLDDKLDKKDGKIQRPRDMKMCKHGPKGMCDYCMPLEPYDPKYLAEKKIKHLSFHSYMRKINAATNKAELKSSFMPPLSEPYYRVRHDCPSGHPPWPEGICTKCQPSAISLQPQEFRMVDHVEFSSPDLINSLLDFWRKSGSQRLGFLYGTYEEYTEVPLGVKAVVQAIYEPPQVDEVDGVTLHEWPNEKEVDEVARLCGLEKVGVIFTDLLDAGRGDGSVVCKRHIDSYYLSSLEIAFASRLQAQYPKTTKWSRTGRFGSNFVTCVLSGDEEGAITISSYQASVSAVEMVRADIVEPSAEPSVMLVQSEDDDSDNKSRYIPEVFYRKINEYGVSAQQNAKPSFPVEFLLVTLTHGFPTESNPLFTKSTFPIENREVIGESQDLRSVAKKLVSHRDSNEVIPEVSDFHLLCYLHSLSTFSKTNANRLHSKITRTVTTNLMTPQDEEKLLCRVATSHDPTEGLKLINTPGWATLVTILQESGERPPKRPWLNPADPPRPLSQQGKRHLSSRPESPKSESEQLAKRFKGASLE | Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 75417
Sequence Length: 674
Subcellular Location: Cytoplasm
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Q5AA50 | MSSIILRFRSKDGMFRITTDSSSNFTLVLEQLIEKLSQSGNNGNGNGNNNKIDLQSLTIANKPQDKGKSSYEFQNQTVNELGLKNGDMLYVNYESVTNDSGPTTTATNTTTNTASGNTIPITGPVPSIPINSVVTSHGPLKVEELPIDQELDKEDGLITRPLSSMCRHGPKGMCEYCSPLPPWDENYRKDHAIKHISFHAYLKQQLEKLKSSGGSYFPPLDPVDYSIDLTCNQGHKPYPNGICSKCQPSPITLQLQKFRMVDHLEFADSFILNDFINVWRVSGVQRFGYLYGRYAKSEKTPLGIKAIVETIIEPPQHDELDGITLLDWDQQEEKMVDQVANKFGLYKVGIIFTDLTDAGTKNGKVLCKRHKDSYFLTNLEIIMAAKFQLKYPNISKYSTAKNNGQFSSKFVTCVISGGLNGEIEPRSYQVSTSAEALVKADIITGCTQPSQIYVNESNNHRYVPDIQYSKINKYGLEVKSNAKPTFPGEFLLVSLTDSFPLQPTPIFTNSYVIENREFLGDENHDIQSLKTLHNYLKSNNDQIFNFHFILHLIKTHILNDQEIDLLIEYIKSKNLEDYLKLVESNGWMTLMTILEQSV | Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 67354
Sequence Length: 598
Subcellular Location: Cytoplasm
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P0CP30 | MLLRIRSPAGTARLTVQPETTGEDFAEAILNTIPAADPQPDPATLALSNQPGAAGESVPFHALSGRTVGDMGFSHGDLLFLSYKPRAADPDSHPAMQATAPHPQPAQPDPSHPKTHTDPPMPNTIPLRDLSSVQEPEIDQYWEKQTGKIERKRDPAFCRHGDKAMCDYCMPLEPYDPKFQSEHQIKHLSYHAYLRKLLSSRPPTASSATDLPPLSPTSLSVITPCPTGAHPSFPDGICSTCQPSAVTLQSQPFRMVDHIEFASPSIIEGLLSAWRRTGTQRIAFLIGREDKYEKVPMGIKVIVEAVWEPKQEGELDGLTVETPWSDESRVQEIAKWCDKGLSVVGMIYTDLTPSPDDITKTLYKRHAQSYTASSLEMLLSAAYQLSHPLSTRMSPTGHYSSRFVTCCLTGDKDGGVDILAWQASEHAEAMVKAGIVEASVDPAVVRVRKPGEGEYVPEVFYSYKNEYGLQVKMPAKPTFPVEYLYVNITHGFPLAPSPLFLSNAFPTENRPGLHDQSMQVVITQLAAILKTSDAEIGDAGTWPGRIKKDVEKWLSDWHLVTFLCMQGLFSLKEQQILCRAATAHAHPNDTHALEELFASGGWQTLLTIVDSEASANARSNPPPTSSFNNLGIDSPAFAGPSTESSAPPSGPDSVGAGAGAGAGGGRERVCPHCTFVNEHGGSDCEICGLPLDG | Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 75103
Sequence Length: 693
Subcellular Location: Cytoplasm
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Q8TAT6 | MAESIIIRVQSPDGVKRITATKRETAATFLKKVAKEFGFQNNGFSVYINRNKTGEITASSNKSLNLLKIKHGDLLFLFPSSLAGPSSEMETSVPPGFKVFGAPNVVEDEIDQYLSKQDGKIYRSRDPQLCRHGPLGKCVHCVPLEPFDEDYLNHLEPPVKHMSFHAYIRKLTGGADKGKFVALENISCKIKSGCEGHLPWPNGICTKCQPSAITLNRQKYRHVDNIMFENHTVADRFLDFWRKTGNQHFGYLYGRYTEHKDIPLGIRAEVAAIYEPPQIGTQNSLELLEDPKAEVVDEIAAKLGLRKVGWIFTDLVSEDTRKGTVRYSRNKDTYFLSSEECITAGDFQNKHPNMCRLSPDGHFGSKFVTAVATGGPDNQVHFEGYQVSNQCMALVRDECLLPCKDAPELGYAKESSSEQYVPDVFYKDVDKFGNEITQLARPLPVEYLIIDITTTFPKDPVYTFSISQNPFPIENRDVLGETQDFHSLATYLSQNTSSVFLDTISDFHLLLFLVTNEVMPLQDSISLLLEAVRTRNEELAQTWKRSEQWATIEQLCSTVGGQLPGLHEYGAVGGSTHTATAAMWACQHCTFMNQPGTGHCEMCSLPRT | Function: The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. The NPLOC4-UFD1-VCP complex regulates spindle disassembly at the end of mitosis and is necessary for the formation of a closed nuclear envelope (By similarity). Acts as a negative regulator of type I interferon production via the complex formed with VCP and UFD1, which binds to RIGI and recruits RNF125 to promote ubiquitination and degradation of RIGI .
Sequence Mass (Da): 68120
Sequence Length: 608
Domain: Binds ubiquitinated proteins via its RanBP2-type zinc finger.
Pathway: Protein degradation; proteasomal ubiquitin-dependent pathway.
Subcellular Location: Cytoplasm
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A4RN19 | MLLRLRGPDGMLRIELDPKDTFNKLGQELMGKLPPTVDPATITVSNAPGSQGDKKLLKDIAKYKVEAIGLKHGDLIFVDYKHQGAEADGTANSDGASQPLTSTTNRLNGQPVLPTEDLPIDPLPTPAPGATIKNPWEVVRQSPLDDRLDKKDGKIPRKRDAMCRHGPKGMCDYCQPLDPFDAKFLAEKKIKYLSMHAHLRKINSATNKPELGSSFIPPLSEPYFRVKHDCPSGHPQWPEGICSKCQPSAITLQPQPFRMVDHVEFASPSIVDSFINTWRRTGGQRYGIMYGKYSEYEEVPLGIKAVVQAIYEPPQVDEVDGVSLNSWDNEKDVNQVARLCGLEPVGAIWTDLLDAGAGDGSVVCKRHADSYFLSSLEVCFAARLQAQHPKPSKWSDTGRFGSNFVTCIISGNEQGEIAISSYQVSNEAVEMVRADIMEPSADPTVMLVREEEEDDGSTSRTRYIPDVFYRRINEYGANVQENAKPSFPVEYLFVTLTHGFPDVAKPMFSDEGAFPIENREYMGESQEHSAAAKALKVHEKASSGSSKDGMKVSNFHLLCFLHQMSVLSKDEESLLCRVATQHDLADAFQLRSTTGWQTLMAILQSTGERIPKRSRQTDVLAADPAASSYPGRRGIDDSDERLAKRFASVRLNARGDGRNGRDRPSAHET | Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 74006
Sequence Length: 669
Subcellular Location: Cytoplasm
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Q9UTK3 | MSEPAVVSILDTDLYKLTMLQAVLEHYPDAQVSYKYTNRSPKMALNQEAYNWLREQIRGLRNLHLLPEEEQWLRKNCPYLKESFYEFMHEFEFDPENSISLNYDSETKDLSIFIHGLWKNTIFYEIPLLALVSESYFKFVDKDWSPEGQFEKAYEKGKRLIRAGCAFTDFGTRRRRDPHTQEIVLQGLMKAQEDFKGPGSFLGTSNVYFAAKYNLNVSGTVAHEWYMGIAAITQNYKQANRIASLKWVQTFGTSLLIALTDTFSTDVFLKSFTANSADDLANVFHGVRQDSGCAEEYIEKVVKHYKSIGVDPSTKVIVHSDALNVDRCIELYKYCEKCGIKSAFGIGTNLTSDFQKVSNPSEVSKPMNIVIKLFSAEGTKAVKISDDIMKNTGDRDAVIQAKHQLCLPIA | Cofactor: Activity is highest with Mn(2+).
Function: Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate. Helps prevent cellular oxidative stress via its role in NAD biosynthesis.
PTM: Transiently phosphorylated on a His residue during the reaction cycle. Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production. Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release.
Catalytic Activity: 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate
Sequence Mass (Da): 46694
Sequence Length: 410
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.
EC: 6.3.4.21
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P39683 | MSEPVIKSLLDTDMYKITMHAAVFTNFPDVTVTYKYTNRSSQLTFNKEAINWLKEQFSYLGNLRFTEEEIEYLKQEIPYLPSAYIKYISSSNYKLHPEEQISFTSEEIEGKPTHYKLKILVSGSWKDTILYEIPLLSLISEAYFKFVDIDWDYENQLEQAEKKAETLFDNGIRFSEFGTRRRRSLKAQDLIMQGIMKAVNGNPDRNKSLLLGTSNILFAKKYGVKPIGTVAHEWVMGVASISEDYLHANKNAMDCWINTFGAKNAGLALTDTFGTDDFLKSFRPPYSDAYVGVRQDSGDPVEYTKKISHHYHDVLKLPKFSKIICYSDSLNVEKAITYSHAAKENGMLATFGIGTNFTNDFRKKSEPQVKSEPLNIVIKLLEVNGNHAIKISDNLGKNMGDPATVKRVKEELGYTERSWSGDNEAHRWT | Function: Catalyzes the first step in the biosynthesis of NAD from nicotinic acid, the ATP-dependent synthesis of beta-nicotinate D-ribonucleotide from nicotinate and 5-phospho-D-ribose 1-phosphate . Essential for growth under anaerobic conditions .
PTM: Transiently phosphorylated on a His residue during the reaction cycle (By similarity). Phosphorylation strongly increases the affinity for substrates and increases the rate of nicotinate D-ribonucleotide production . Dephosphorylation regenerates the low-affinity form of the enzyme, leading to product release (By similarity).
Catalytic Activity: 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O + nicotinate = ADP + diphosphate + nicotinate beta-D-ribonucleotide + phosphate
Sequence Mass (Da): 49019
Sequence Length: 429
Pathway: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D-ribonucleotide from nicotinate: step 1/1.
Subcellular Location: Cytoplasm
EC: 6.3.4.21
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Q06495 | MLSYGERLGSPAVSPLPVRGGHVMRGTAFAYVPSPQVLHRIPGTSAYAFPSLGPVALAEHTCPCGEVLERHEPLPAKLALEEEQKPESRLVPKLRQAGAMLLKVPLMLTFLYLFVCSLDMLSSAFQLAGGKVAGDIFKDNAILSNPVAGLVVGILVTVLVQSSSTSTSIIVSMVSSGLLEVSSAIPIIMGSNIGTSVTNTIVALMQAGDRTDFRRAFAGATVHDCFNWLSVLVLLPLEAATGYLHHITRLVVASFNIHGGRDAPDLLKIITEPFTKLIIQLDESVITSIATGDESLRNHSLIQIWCHPDSLQAPTSMSRAEANSSQTLGNATMEKCNHIFVDTGLPDLAVGLILLAGSLVLLCTCLILLVKMLNSLLKGQVAKVIQKVINTDFPAPFTWVTGYFAMVVGASMTFVVQSSSVFTSAITPLIGLGVISIERAYPLTLGSNIGTTTTAILAALASPREKLSSAFQIALCHFFFNISGILLWYPVPCTRLPIRMAKALGKRTAKYRWFAVLYLLVCFLLLPSLVFGISMAGWQVMVGVGTPFGALLAFVVLINVLQSRSPGHLPKWLQTWDFLPRWMHSLKPLDHLITRATLCCARPEPRSPPLPPRVFLEELPPATPSPRLALPAHHNATRL | Function: Involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane . The cotransport has a Na(+):Pi stoichiometry of 3:1 and is electrogenic (By similarity).
Catalytic Activity: 3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68937
Sequence Length: 639
Subcellular Location: Apical cell membrane
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Q06496 | MMSYSERLGGPAVSPLPVRGRHMVHGAAFAYVPSPQVLHRIPGTTTYAISSLSPVALTEHSCPYGEVLECHDPLPAKLAQEEEQKPEPRLSQKLAQVGTKLLKVPLMLGFLYLFVCSLDVLSSAFQLAGGKVAGDIFKDNAILSNPVAGLVVGILVTVLVQSSSTSTSIIVSMVSSGLLEVSSAIPIIMGSNIGTSVTNTIVALMQAGDRTDFRRAFAGATVHDCFNWLSVLVLLPLEAATGYLHHVTGLVVASFNIRGGRDAPDLLKVITEPFTKLIIQLDKSVITSIAVGDESLRNHSLIRIWCQPETKEASTSMSRVEAIGSLANTTMEKCNHIFVDTGLPDLAVGLILLAGSLVVLCTCLILLVKMLNSLLKGQVANVIQKVINTDFPAPFTWVTGYFAMVVGASMTFVVQSSSVFTSAITPLIGLGVISIERAYPLTLGSNIGTTTTAILAALASPREKLSSSFQIALCHFFFNISGILLWYPLPCTRLPIRMAKALGKRTAKYRWFAVLYLLVCFLLLPSLVFGISMAGWQAMVGVGTPFGALLAFVVLVNVLQSRSPGHLPKWLQTWDFLPRWMHSLQPLDGLITRATLCYARPEPRSPQLPPRVFLEELPPATPSPRLALPAHHNATRL | Function: Involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane . The cotransport has a Na(+):Pi stoichiometry of 3:1 and is electrogenic .
Catalytic Activity: 3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68707
Sequence Length: 637
Subcellular Location: Apical cell membrane
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O97704 | MISYGENLGGRAVSPLPVRGGHMMHGAAFAYVPSPQVLHRIPGTSAYGFPSVGPMALPEHGCPYGEVVEHHDPLPAKLALEDERKPEPGLIQKLRRAGVTLLKVPLMLSFLYLFVCSLDVLSSAFQLAGGKVAGDIFKDNAILSNPVAGLVVGILVTVLVQSSSTSTSIVVSMVSSGLLEVSSAIPIIMGSNIGTSVTNTIVALMQAGDRTDFRRAFAGATVHDCFNWLSVLVLLPLEAATGYLHHITRLVVASFNIRGGRDAPDLLKIITEPFTKLIIQLDKSVITSLASGDESLRNHSLIRVWCYPNPTEVPTPMPRAEANTSRMLRNATLEKCNHIFVDTGLPDLAVGLILLAGSLALLCTCLILLVKMLNSLLKGQVAKVIQKVINTDFPTPFTWATGYFAMVVGASMTFVVQSSSVFTSAITPLIGLGVISIERAYPLTLGSNIGTTTTAILAALASPREKLSSAFQIALCHFFFNISGILLWYPVPCTRLPIRMAKALGKRTAKYRWFAVLYLLLCFLLLPSMVFGLSMAGWRAMVGVGAPFGALLAFVVLVSALQHRSPGCLPKWLQTWDFLPLWVHSLKPLDHLITRATLCCARPEPRSPPLPTRVFLEELPPATPSPRLAMPHHHDATRL | Function: Involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane. The cotransport has a Na(+):Pi stoichiometry of 3:1 and is electrogenic.
Catalytic Activity: 3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69023
Sequence Length: 639
Subcellular Location: Apical cell membrane
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O95436 | MAPWPELGDAQPNPDKYLEGAAGQQPTAPDKSKETNKTDNTEAPVTKIELLPSYSTATLIDEPTEVDDPWNLPTLQDSGIKWSERDTKGKILCFFQGIGRLILLLGFLYFFVCSLDILSSAFQLVGGKMAGQFFSNSSIMSNPLLGLVIGVLVTVLVQSSSTSTSIVVSMVSSSLLTVRAAIPIIMGANIGTSITNTIVALMQVGDRSEFRRAFAGATVHDFFNWLSVLVLLPVEVATHYLEIITQLIVESFHFKNGEDAPDLLKVITKPFTKLIVQLDKKVISQIAMNDEKAKNKSLVKIWCKTFTNKTQINVTVPSTANCTSPSLCWTDGIQNWTMKNVTYKENIAKCQHIFVNFHLPDLAVGTILLILSLLVLCGCLIMIVKILGSVLKGQVATVIKKTINTDFPFPFAWLTGYLAILVGAGMTFIVQSSSVFTSALTPLIGIGVITIERAYPLTLGSNIGTTTTAILAALASPGNALRSSLQIALCHFFFNISGILLWYPIPFTRLPIRMAKGLGNISAKYRWFAVFYLIIFFFLIPLTVFGLSLAGWRVLVGVGVPVVFIIILVLCLRLLQSRCPRVLPKKLQNWNFLPLWMRSLKPWDAVVSKFTGCFQMRCCCCCRVCCRACCLLCDCPKCCRCSKCCEDLEEAQEGQDVPVKAPETFDNITISREAQGEVPASDSKTECTAL | Function: Involved in actively transporting phosphate into cells via Na(+) cotransport.
Catalytic Activity: 3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75759
Sequence Length: 690
Subcellular Location: Apical cell membrane
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Q9JJ09 | MAPWPELENAHPNPNKFIEGASGPQSSIPDKDKGTSKTNDSGTPVAKIELLPSYSALVLIEEPPEGNDPWDLPELQDNGIKWSERDSKGKILCIFQGIGKFILLLGFLYLFVCSLDVLSSAFQLVGGKMAGQFFSNNSIMSNPVAGLVIGVLVTVMVQSSSTSSSIIVSMVASSLLSVRAAIPIIMGANIGTSITNTIVALMQAGDRNEFRRAFAGATVHDFFNWLSVLVLLPLEAATHYLEKLTNLVLETFSFQNGEDAPDILKVITDPFTKLIIQLDKKVIQQIAMGDSEAQNKSLIKIWCKTISNVIEENVTVPSPDNCTSPSYCWTDGIQTWTIQNVTEKENIAKCQHIFVNFSLPDLAVGIILLTVSLLILCGCLIMIVKLLGSVLRGQVATVIKKTLNTDFPFPFAWLTGYLAILVGAGMTFIVQSSSVFTSAMTPLIGIGVISIERAYPLTLGSNIGTTTTAILAALASPGNTLRSSLQIALCHFFFNISGILLWYPIPFTRLPIRLAKGLGNISAKYRWFAVFYLIFFFLLTPLTVFGLSLAGWPVLVGVGVPIILLILLVLCLRMLQARCPRILPLKLRDWNFLPLWMHSLKPWDNIISLATSCFQRRCCCCCRVCCRVCCMVCGCKCCRCSKCCKNLEEEEKEQDVPVKASGGFDNTAMSKECQDEGKGQVEVLGMKALSNTTVF | Function: Involved in actively transporting phosphate into cells via Na(+) cotransport.
Catalytic Activity: 3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75992
Sequence Length: 695
Subcellular Location: Apical cell membrane
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Q8N130 | MPSSLPGSQVPHPTLDAVDLVEKTLRNEGTSSSAPVLEEGDTDPWTLPQLKDTSQPWKELRVAGRLRRVAGSVLKACGLLGSLYFFICSLDVLSSAFQLLGSKVAGDIFKDNVVLSNPVAGLVIGVLVTALVQSSSTSSSIVVSMVAAKLLTVRVSVPIIMGVNVGTSITSTLVSMAQSGDRDEFQRAFSGSAVHGIFNWLTVLVLLPLESATALLERLSELALGAASLTPRAQAPDILKVLTKPLTHLIVQLDSDMIMSSATGNATNSSLIKHWCGTTGQPTQENSSCGAFGPCTEKNSTAPADRLPCRHLFAGTELTDLAVGCILLAGSLLVLCGCLVLIVKLLNSVLRGRVAQVVRTVINADFPFPLGWLGGYLAVLAGAGLTFALQSSSVFTAAVVPLMGVGVISLDRAYPLLLGSNIGTTTTALLAALASPADRMLSALQVALIHFFFNLAGILLWYLVPALRLPIPLARHFGVVTARYRWVAGVYLLLGFLLLPLAAFGLSLAGGMELAAVGGPLVGLVLLVILVTVLQRRRPAWLPVRLRSWAWLPVWLHSLEPWDRLVTRCCPCNVCSPPKATTKEAYCYENPEILASQQL | Function: Involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane . The cotransport has a Na(+):Pi stoichiometry of 2:1 and is electroneutral (By similarity).
Catalytic Activity: 2 Na(+)(out) + phosphate(out) = 2 Na(+)(in) + phosphate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63550
Sequence Length: 599
Subcellular Location: Apical cell membrane
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Q80SU6 | MPNSLAGGQVPNPTLDAFDLVDRSLRNAGISGSIPGLEEGGTDPWTFSPLKNADQLKEVGMASRLRRVVSSFLKACGLLGSLYFFICSLDILSSAFQLLGSKMAGDIFKDNVVLSNPVAGLVIGVLVTVLVQSSSTSSSIVVSMVASKLLTVQVSVPIIMGVNVGTSITSTLVSMAQSGDRDEFQRAFSGSAVHGIFNWLTVLVLLPLESATAALERLSELALGAASLQPGQQAPDILKALTRPFTHLIIQLDSSVITSGITSNTTNSSLIKHWCGFRGETPQGSSEGCGLFSSCTERNSSASPEEDRLLCHHLFAGSKLTDLAVGFILLAGSLLVLCVCLVLIVKLLNSVLKGRIAQAVKTVINADFPFPFGWLSGYLAILVGAGLTFLLQSSSVFTAAIVPLMGVGVIDLERAYPLFLGSNIGTTTTALLAALASPADMLIFAVQVALIHFFFNLAGILLWYLVPVLRLPIPLAKRFGNLTAQYRWVAIVYLLLTFLLLPLAAFGLSLAGGTVLAAVGGPLVGLVLLIILVNVLQQHRPSWLPRCLQSWAWLPLWLHSLEPWDRLVTACCPCRACSNSPMTSKVAHCYENPQVIASQQL | Function: Involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane . The cotransport has a Na(+):Pi stoichiometry of 2:1 and is electroneutral .
Catalytic Activity: 2 Na(+)(out) + phosphate(out) = 2 Na(+)(in) + phosphate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63939
Sequence Length: 601
Subcellular Location: Apical cell membrane
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Q5SZA1 | MDEKPTTRKGSGFCSLRYALALIMHFSNFTMITQRVSLSIAIIAMVNSTQHQDPANASTEGPVMDLLSNQSRGIKDFSTRAAVYQWSTETQGIIFSSISYGIILTLIPSGYLAGIFGAKQILGAGLLISSLLTLFTPLAADFGVILVIVIRTVQGMAQGMAWTGQFTIWAKWAPPLERSKLTSIAGSGAAFGSFIILCVGGLISQALGWPFIFYIFGSIGCVCCVLWFTVIYDDPMHHPCISVREKEHITSSVAQQSSSPRRSVPIKAMVRCLPLWAIFMGFFSHFWLCTIIITYLPTYISTVLHVNIRDSGVLSSLPFIAASSCTILGGQMADFLLSRNLLSLITVRKLFSSLGLLLPSLCAVALPFVTSSYIATIVLLILIPGTSNLCDSGFIINTLDVAPRYASFLMGISRGFGLTAGIISSTTTGFLISQDSESGWRNVFFLSAAVNMFGLIFYLIFGQAEIQSWAKERTLTRL | Function: Acts as a membrane potential-dependent organic anion transporter, the transport requires a low concentration of chloride ions . Mediates chloride-dependent transport of urate . Can actively transport inorganic phosphate into cells via Na(+) cotransport .
Catalytic Activity: 3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51965
Sequence Length: 478
Subcellular Location: Apical cell membrane
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P58796 | MVKVNIIFYSMYGHVYRMAEAVAAGAREVEGAEVGIYQVPETLPEEVLEKMGAIETKKLFAHIPVLTREMNEEVLAGADALIFGTPTRYGNMTAQMRAVLDGLGGLWNRDAFVGKVGSVFTSSGTQHGGQESTILTFHVTLLHLGMILVGLPYSEKRQTRMDEITGGSPYGVSTIAGGDGSRQPSENELAMARYQGRHVTLIAKKIAGK | Cofactor: Binds 1 FMN per monomer.
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Sequence Mass (Da): 22604
Sequence Length: 209
EC: 1.6.5.2
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Q1QX85 | MGIRNTLDKLEPHFHQGGKYEKFYALYEAVDTIFYSPPSVTKSTAHVRDGIDLKRIMITVWLCTFPAMFFGMYNAGLQANMAIGDGFGALGGWREAVTMALAGSHDPGSIWANFVLGATYFLPIYLVTFAVGGFWEVLFAVKRGHEVNEGFFVTSVLYALILPATIPLWQVALGITFGVVIGKEIFGGTGKNFLNPALTGRAFLYFAYPAQISGDSVWVAADGYTGATALSTAAQNGMSAVQQAYSWWDAFLGFIPGSVGETSTLAILIGAAVLLITRIASWRIMLGVFVGMALTAMLFTAIGSESNPMFGMPWYWHLVLGGFAFGMVFMATDPVSASMTDPGKLLFGFLIGVMTVLIRVVNPAFPEGIMLAILFANLFAPMIDHFFVQANIKRRMKRDAAYSPATNEETA | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Catalytic Activity: a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44600
Sequence Length: 411
Subcellular Location: Cell inner membrane
EC: 7.2.1.1
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Q7UWS1 | MVEQYLSVFLKAVFVENLALAFFLGMCTFLAVSKNVKTAIGLGIAVIAIETITVPANQLIYSLLLKKGALTWVNDYLISTDTYNFAEVDLTFLGFISYIGVIAAMVQILEMFLDRFMPSLYNALGIFLPLITVNCAILGASLFMEQREYPFGESVVFGFGCGVGWALAIMALAGIREKLKYSDVPPPLRGLGITFITVGLMSLAFMSFSGIQL | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Catalytic Activity: a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23262
Sequence Length: 213
Subcellular Location: Cell inner membrane
EC: 7.2.1.1
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Q56589 | MEHYISLLVKSIFIENMALSFFLGMCTFLAVSKKVKTSFGLGVAVVVVLTIAVPVNNLVYNLVLRENALVEGVDLSFLNFITFIGVIAALVQILEMVLDRFFPPLYNALGIFLPLITVNCAIFGGVSFMVQRDYNFAESIVYGFGSGVGWMLAIVALAGIREKMKYSDVPPGLRGLGITFITVGLMALGFMSFSGVQL | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
PTM: The N-terminus is blocked.
Location Topology: Multi-pass membrane protein
Catalytic Activity: a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+)
Sequence Mass (Da): 21540
Sequence Length: 198
Subcellular Location: Cell inner membrane
EC: 7.2.1.1
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Q68D85 | MTWRAAASTCAALLILLWALTTEGDLKVEMMAGGTQITPLNDNVTIFCNIFYSQPLNITSMGITWFWKSLTFDKEVKVFEFFGDHQEAFRPGAIVSPWRLKSGDASLRLPGIQLEEAGEYRCEVVVTPLKAQGTVQLEVVASPASRLLLDQVGMKENEDKYMCESSGFYPEAINITWEKQTQKFPHPIEISEDVITGPTIKNMDGTFNVTSCLKLNSSQEDPGTVYQCVVRHASLHTPLRSNFTLTAARHSLSETEKTDNFSIHWWPISFIGVGLVLLIVLIPWKKICNKSSSAYTPLKCILKHWNSFDTQTLKKEHLIFFCTRAWPSYQLQDGEAWPPEGSVNINTIQQLDVFCRQEGKWSEVPYVQAFFALRDNPDLCQCCRIDPALLTVTSGKSIDDNSTKSEKQTPREHSDAVPDAPILPVSPIWEPPPATTSTTPVLSSQPPTLLLPLQ | Function: Triggers NCR3-dependent natural killer cell activation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 50827
Sequence Length: 454
Domain: The C-terminal part is similar to retroviral Gag protein. This putative protein seems to be the result of a fusion between an Ig-like domain-containing protein and a ERV.
Subcellular Location: Cell membrane
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P22736 | MPCIQAQYGTPAPSPGPRDHLASDPLTPEFIKPTMDLASPEAAPAAPTALPSFSTFMDGYTGEFDTFLYQLPGTVQPCSSASSSASSTSSSSATSPASASFKFEDFQVYGCYPGPLSGPVDEALSSSGSDYYGSPCSAPSPSTPSFQPPQLSPWDGSFGHFSPSQTYEGLRAWTEQLPKASGPPQPPAFFSFSPPTGPSPSLAQSPLKLFPSQATHQLGEGESYSMPTAFPGLAPTSPHLEGSGILDTPVTSTKARSGAPGGSEGRCAVCGDNASCQHYGVRTCEGCKGFFKRTVQKNAKYICLANKDCPVDKRRRNRCQFCRFQKCLAVGMVKEVVRTDSLKGRRGRLPSKPKQPPDASPANLLTSLVRAHLDSGPSTAKLDYSKFQELVLPHFGKEDAGDVQQFYDLLSGSLEVIRKWAEKIPGFAELSPADQDLLLESAFLELFILRLAYRSKPGEGKLIFCSGLVLHRLQCARGFGDWIDSILAFSRSLHSLLVDVPAFACLSALVLITDRHGLQEPRRVEELQNRIASCLKEHVAAVAGEPQPASCLSRLLGKLPELRTLCTQGLQRIFYLKLEDLVPPPPIIDKIFMDTLPF | Cofactor: Binds 2 zinc ions.
Function: Orphan nuclear receptor. Binds the NGFI-B response element (NBRE) 5'-AAAGGTCA-3' . Binds 9-cis-retinoic acid outside of its ligand-binding (NR LBD) domain . Participates in energy homeostasis by sequestrating the kinase STK11 in the nucleus, thereby attenuating cytoplasmic AMPK activation . Regulates the inflammatory response in macrophages by regulating metabolic adaptations during inflammation, including repressing the transcription of genes involved in the citric acid cycle (TCA) (By similarity). Inhibits NF-kappa-B signaling by binding to low-affinity NF-kappa-B binding sites, such as at the IL2 promoter . May act concomitantly with NR4A2 in regulating the expression of delayed-early genes during liver regeneration (By similarity). Plays a role in the vascular response to injury (By similarity).
PTM: Phosphorylated at Ser-351 by RPS6KA1 and RPS6KA3 in response to mitogenic or stress stimuli.
Sequence Mass (Da): 64463
Sequence Length: 598
Domain: The NR LBD domain binds the lipid A moiety of lipopolysaccharide (LPS) in the cytosol.
Subcellular Location: Nucleus
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P12813 | MPCIQAQYGTPATSPGPRDHLTGDPLALEFGKPTMDLASPETAPAAPATLPSFSTFMDGYTGEFDTFLYQLPGTTQPCSSACSSASSTSSSSSSATSPASASFKFEDFQVYGCYPGTLSGPLDETLSSSGSEYYGSPCSAPSPSTPNFQPSQLSPWDGSFGHFSPSQTYEGLWAWTEQLPKASSGPPPPPTFFSFSPPTGPSPSLAQSSLKLFPPPATHQLGEGESYSMPAAFPGLAPTSPNRDTSGILDAPVTSTKSRSGASGGSEGRCAVCGDNASCQHYGVRTCEGCKGFFKRTVQKSAKYICLANKDCPVDKRRRNRCQFCRFQKCLAVGMVKEVVRTDSLKGRRGRLPSKPKQPPDASPTNLLTSLIRAHLDSGPSTAKLDYSKFQELVLPRFGKEDAGDVQQFYDLLSGSLDVIRKWAEKIPGFIELCPGDQDLLLESAFLELFILRLAYRSKPGEGKLIFCSGLVLHQLQCARGFGDWIDNILAFSRSLHSLGVDVPAFACLSALVLITDRHGLQDPRRVEELQNRIASCLKEHMATVAGDPQPASCLSRLLGKLPELRTLCTQGLQRIFCLKLEDLVPPPPIVDKIFMDTLSF | Cofactor: Binds 2 zinc ions.
Function: Orphan nuclear receptor. Binds the NGFI-B response element (NBRE) 5'-AAAGGTCA-3' . Binds 9-cis-retinoic acid outside of its ligand-binding (NR LBD) domain (By similarity). Participates in energy homeostasis by sequestrating the kinase STK11 in the nucleus, thereby attenuating cytoplasmic AMPK activation (By similarity). Regulates the inflammatory response in macrophages by regulating metabolic adaptations during inflammation, including repressing the transcription of genes involved in the citric acid cycle (TCA) . Inhibits NF-kappa-B signaling by binding to low-affinity NF-kappa-B binding sites, such as at the IL2 promoter . May act concomitantly with NR4A2 in regulating the expression of delayed-early genes during liver regeneration (By similarity). Plays a role in the vascular response to injury .
PTM: Phosphorylated at Ser-354 by RPS6KA1 and RPS6KA3 in response to mitogenic or stress stimuli.
Sequence Mass (Da): 64738
Sequence Length: 601
Domain: The NR LBD domain binds the lipid A moiety of lipopolysaccharide (LPS) in the cytosol.
Subcellular Location: Nucleus
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Q04913 | MPCIQAQHGSLSQCAGPCDNYVPDILNSEFGKFTMDLVNSEIAASTSLPSFSTFMDGYTGEFDAFLYQIPSSNQQSSLKVEEFQVFGCYPGSFTNQLDETMSSSGSDYYGSPCSIPSPSTPGFQNPQLPTWECSYGAYSPTQNYDNMRHWTEQQKNSISQQTFFSFGTPAHSPNMAANPLKIAPATHRLDQQLVDTDVFALAQNSSAGFPAVPLGQAPGVLDSSVLLDSPLSPSKTRSPSSNEGRCAVCGDNASCQHYGVRTCEGCKGFFKRTVQKNAKYICLANKDCPVDKRRRNRCQFCRFQKCLVVGMVKEVVRTDSLKGRRGRLPSKPKQIAESSPVDLINSLVRAHIDSIPSSSKLDYSKFQETVPLQLEKESSVDVQQFYDLLSGSLEVIRKWAEKIQGFVDLPKEDQDLLLESAFLELFILRLAYRSRPEEGKLIFCNGVVLHRTQCVRGFGEWIDSIIEFSHSLQRMNIDVPSFSCLSALVIVTDRHGLKEPKKVEELQSQIINCLKEHIPSSMNEQNRPNCLSKLLGKLPELRTLCTQGLQRIFYLKLEDLVPPPPIVDKIFMDTLPF | Cofactor: Binds 2 zinc ions.
Function: Orphan nuclear receptor. Binds the NGFI-B response element (NBRE) 5'-AAAAGGTCA-3'.
Sequence Mass (Da): 64383
Sequence Length: 577
Domain: The NR LBD domain may bind the lipid A moiety of lipopolysaccharide (LPS) in the cytosol.
Subcellular Location: Nucleus
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P43354 | MPCVQAQYGSSPQGASPASQSYSYHSSGEYSSDFLTPEFVKFSMDLTNTEITATTSLPSFSTFMDNYSTGYDVKPPCLYQMPLSGQQSSIKVEDIQMHNYQQHSHLPPQSEEMMPHSGSVYYKPSSPPTPTTPGFQVQHSPMWDDPGSLHNFHQNYVATTHMIEQRKTPVSRLSLFSFKQSPPGTPVSSCQMRFDGPLHVPMNPEPAGSHHVVDGQTFAVPNPIRKPASMGFPGLQIGHASQLLDTQVPSPPSRGSPSNEGLCAVCGDNAACQHYGVRTCEGCKGFFKRTVQKNAKYVCLANKNCPVDKRRRNRCQYCRFQKCLAVGMVKEVVRTDSLKGRRGRLPSKPKSPQEPSPPSPPVSLISALVRAHVDSNPAMTSLDYSRFQANPDYQMSGDDTQHIQQFYDLLTGSMEIIRGWAEKIPGFADLPKADQDLLFESAFLELFVLRLAYRSNPVEGKLIFCNGVVLHRLQCVRGFGEWIDSIVEFSSNLQNMNIDISAFSCIAALAMVTERHGLKEPKRVEELQNKIVNCLKDHVTFNNGGLNRPNYLSKLLGKLPELRTLCTQGLQRIFYLKLEDLVPPPAIIDKLFLDTLPF | Function: Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development . It is crucial for expression of a set of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons (By similarity).
Sequence Mass (Da): 66591
Sequence Length: 598
Domain: the ligand-binding domain (LBD) contains no cavity as a result of the tight packing of side chains from several bulky hydrophobic residues in the region normally occupied by ligands. NR4A2 lacks a 'classical' binding site for coactivators .
Subcellular Location: Cytoplasm
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Q06219 | MPCVQAQYGSSPQGASPASQSYSYHSSGEYSSDFLTPEFVKFSMDLTNTEITATTSLPSFSTFMDNYSTGYDVKPPCLYQMPLSGQQSSIKVEDIQMHNYQQHSHLPPQSEEMMPHSGSVYYKPSSPPTPSTPSFQVQHSPMWDDPGSLHNFHQNYVATTHMIEQRKTPVSRLSLFSFKQSPPGTPVSSCQMRFDGPLHVPMNPEPAGSHHVVDGQTFAVPNPIRKPASMGFPGLQIGHASQLLDTQVPSPPSRGSPSNEGLCAVCGDNAACQHYGVRTCEGCKGFFKRTVQKNAKYVCLANKNCPVDKRRRNRCQYCRFQKCLAVGMVKEVVRTDSLKGRRGRLPSKPKSPQDPSPPSPPVSLISALVRAHVDSNPAMTSLDYSRFQANPDYQMSGDDTQHIQQFYDLLTGSMEIIRGWAEKIPGFADLPKADQDLLFESAFLELFVLRLAYRSNPVEGKLIFCNGVVLHRLQCVRGFGEWIDSIVEFSSNLQNMNIDISAFSCIAALAMVTERHGLKEPKRVEELQNKIVNCLKDHVTFNNGGLNRPNYLSKLLGKLPELRTLCTQGLQRIFYLKLEDLVPPPAIIDKLFLDTLPF | Function: Transcriptional regulator which is important for the differentiation and maintenance of meso-diencephalic dopaminergic (mdDA) neurons during development . It is crucial for expression of a set of genes such as SLC6A3, SLC18A2, TH and DRD2 which are essential for development of mdDA neurons .
Sequence Mass (Da): 66593
Sequence Length: 598
Domain: the ligand-binding domain (LBD) contains no cavity as a result of the tight packing of side chains from several bulky hydrophobic residues in the region normally occupied by ligands. NR4A2 lacks a 'classical' binding site for coactivators (By similarity).
Subcellular Location: Cytoplasm
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Q92570 | MPCVQAQYSPSPPGSSYAAQTYSSEYTTEIMNPDYTKLTMDLGSTEITATATTSLPSISTFVEGYSSNYELKPSCVYQMQRPLIKVEEGRAPSYHHHHHHHHHHHHHHQQQHQQPSIPPASSPEDEVLPSTSMYFKQSPPSTPTTPAFPPQAGALWDEALPSAPGCIAPGPLLDPPMKAVPTVAGARFPLFHFKPSPPHPPAPSPAGGHHLGYDPTAAAALSLPLGAAAAAGSQAAALESHPYGLPLAKRAAPLAFPPLGLTPSPTASSLLGESPSLPSPPSRSSSSGEGTCAVCGDNAACQHYGVRTCEGCKGFFKRTVQKNAKYVCLANKNCPVDKRRRNRCQYCRFQKCLSVGMVKEVVRTDSLKGRRGRLPSKPKSPLQQEPSQPSPPSPPICMMNALVRALTDSTPRDLDYSRYCPTDQAAAGTDAEHVQQFYNLLTASIDVSRSWAEKIPGFTDLPKEDQTLLIESAFLELFVLRLSIRSNTAEDKFVFCNGLVLHRLQCLRGFGEWLDSIKDFSLNLQSLNLDIQALACLSALSMITERHGLKEPKRVEELCNKITSSLKDHQSKGQALEPTESKVLGALVELRKICTLGLQRIFYLKLEDLVSPPSIIDKLFLDTLPF | Function: Transcriptional activator that binds to regulatory elements in promoter regions in a cell- and response element (target)-specific manner. Induces gene expression by binding as monomers to the NR4A1 response element (NBRE) 5'-AAAAGGTCA-3' site and as homodimers to the Nur response element (NurRE) site in the promoter of their regulated target genes (By similarity). Plays a role in the regulation of proliferation, survival and differentiation of many different cell types and also in metabolism and inflammation. Mediates proliferation of vascular smooth muscle, myeloid progenitor cell and type B pancreatic cells; promotes mitogen-induced vascular smooth muscle cell proliferation through transactivation of SKP2 promoter by binding a NBRE site (By similarity). Upon PDGF stimulation, stimulates vascular smooth muscle cell proliferation by regulating CCND1 and CCND2 expression. In islets, induces type B pancreatic cell proliferation through up-regulation of genes that activate cell cycle, as well as genes that cause degradation of the CDKN1A (By similarity). Negatively regulates myeloid progenitor cell proliferation by repressing RUNX1 in a NBRE site-independent manner. During inner ear, plays a role as a key mediator of the proliferative growth phase of semicircular canal development (By similarity). Mediates also survival of neuron and smooth muscle cells; mediates CREB-induced neuronal survival, and during hippocampus development, plays a critical role in pyramidal cell survival and axonal guidance. Is required for S phase entry of the cell cycle and survival of smooth muscle cells by inducing CCND1, resulting in RB1 phosphorylation. Binds to NBRE motif in CCND1 promoter, resulting in the activation of the promoter and CCND1 transcription (By similarity). Also plays a role in inflammation; upon TNF stimulation, mediates monocyte adhesion by inducing the expression of VCAM1 and ICAM1 by binding to the NBRE consensus site (By similarity) . In mast cells activated by Fc-epsilon receptor cross-linking, promotes the synthesis and release of cytokines but impairs events leading to degranulation (By similarity). Also plays a role in metabolism; by modulating feeding behavior; and by playing a role in energy balance by inhibiting the glucocorticoid-induced orexigenic neuropeptides AGRP expression, at least in part by forming a complex with activated NR3C1 on the AGRP- glucocorticoid response element (GRE), and thus weakening the DNA binding activity of NR3C1. Upon catecholamines stimulation, regulates gene expression that controls oxidative metabolism in skeletal muscle (By similarity). Plays a role in glucose transport by regulating translocation of the SLC2A4 glucose transporter to the cell surface . Finally, during gastrulation plays a crucial role in the formation of anterior mesoderm by controlling cell migration. Inhibits adipogenesis (By similarity). Also participates in cardiac hypertrophy by activating PARP1 (By similarity).
PTM: Phosphorylated by PRKDC.
Sequence Mass (Da): 68230
Sequence Length: 626
Domain: The AF-1 domain mediates transcription activation. The N-terminal region (1-292) directly interacts with the C-terminal LBD (380-627): the interaction is potentiated by AF-1-mediated recruitment of NCOA2.
Subcellular Location: Nucleus
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P51179 | MPCVQAQYSPSPPGSTYATQTYGSEYTTEIMNPDYAKLTMDLGSTGIMATATTSLPSFSTFMEGYPSSCELKPSCLYQMPPSGPRPLIKMEEGREHGYHHHHHHHHHHHHHHQQQQPSIPPPSGPEDEVLPSTSMYFKQSPPSTPTTPGFPPQAGALWDDELPSAPGCIAPGPLLDPQMKAVPPMAAAARFPIFFKPSPPHPPAPSPAGGHHLGYDPTAAAALSLPLGAAAAAGSQAAALEGHPYGLPLAKRTATLTFPPLGLTASPTASSLLGESPSLPSPPNRSSSSGEGTCAVCGDNAACQHYGVRTCEGCKGFFKRTVQKNAKYVCLANKNCPVDKRRRNRCQYCRFQKCLSVGMVKEVVRTDSLKGRRGRLPSKPKSPLQQEPSQPSPPSPPICMMNALVRALTDATPRDLDYSRYCPTDQATAGTDAEHVQQFYNLLTASIDVSRSWAEKIPGFTDLPKEDQTLLIESAFLELFVLRLSIRSNTAEDKFVFCNGLVLHRLQCLRGFGEWLDSIKDFSLNLQSLNLDIQALACLSALSMITERHGLKEPKRVEELCNKITSSLKDHQRKGQALEPSEPKVLRALVELRKICTQGLQRIFYLKLEDLVSPPSVIDKLFLDTLPF | Function: Transcriptional activator that binds to regulatory elements in promoter regions in a cell- and response element (target)-specific manner . Induces gene expression by binding as monomers to the NR4A1 response element (NBRE) 5'-AAAAGGTCA-3' site and as homodimers to the Nur response element (NurRE) site in the promoter of their regulated target genes . Plays a role in the regulation of proliferation, survival and differentiation of many different cell types and also in metabolism and inflammation. Mediates proliferation of vascular smooth muscle, myeloid progenitor cell and type B pancreatic cells; promotes mitogen-induced vascular smooth muscle cell proliferation through transactivation of SKP2 promoter by binding a NBRE site (By similarity). Upon PDGF stimulation, stimulates vascular smooth muscle cell proliferation by regulating CCND1 and CCND2 expression . In islets, induces type B pancreatic cell proliferation through up-regulation of genes that activate cell cycle, as well as genes that cause degradation of the CDKN1A . Negatively regulates myeloid progenitor cell proliferation by repressing RUNX1 in a NBRE site-independent manner. During inner ear, plays a role as a key mediator of the proliferative growth phase of semicircular canal development (By similarity). Mediates also survival of neuron and smooth muscle cells; mediates CREB-induced neuronal survival, and during hippocampus development, plays a critical role in pyramidal cell survival and axonal guidance. Is required for S phase entry of the cell cycle and survival of smooth muscle cells by inducing CCND1, resulting in RB1 phosphorylation. Binds to NBRE motif in CCND1 promoter, resulting in the activation of the promoter and CCND1 transcription (By similarity). Also plays a role in inflammation; Upon TNF stimulation, mediates monocyte adhesion by inducing the expression of VCAM1 and ICAM1 by binding to the NBRE consensus site (By similarity). In mast cells activated by Fc-epsilon receptor cross-linking, promotes the synthesis and release of cytokines but impairs events leading to degranulation. Also plays a role in metabolism; by modulating feeding behavior; and by playing a role in energy balance by inhibiting the glucocorticoid-induced orexigenic neuropeptides AGRP expression, at least in part by forming a complex with activated NR3C1 on the AGRP-glucocorticoid response element (GRE), and thus weakening the DNA binding activity of NR3C1. Upon catecholamines stimulation, regulates gene expression that controls oxidative metabolism in skeletal muscle (By similarity). Plays a role in glucose transport by regulating translocation of the SLC2A4 glucose transporter to the cell surface (By similarity). Finally, during gastrulation plays a crucial role in the formation of anterior mesoderm by controlling cell migration (By similarity). Also participates in cardiac hypertrophy by activating PARP1 .
PTM: Phosphorylated by PRKDC.
Sequence Mass (Da): 68564
Sequence Length: 628
Domain: The AF-1 domain mediates transcription activation. The N-terminal region (1-292) directly interacts with the C-terminal LBD (380-627): the interaction is potentiated by AF-1-mediated recruitment of NCOA2.
Subcellular Location: Nucleus
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P07071 | MTIEKEIEGLIHKTNKDLLNENANKDSRVFPTQRDLMAGIVSKHIAKNMVPSFIMKAHESGIIHVHDIDYSPALPFTNCCLVDLKGMLENGFKLGNAQIETPKSIGVATAIMAQITAQVASHQYGGTTFANVDKVLSPYVKRTYAKHIEDAEKWQIADALNYAQSKTEKDVYDAFQAYEYEVNTLFSSNGQTPFVTITFGTGTDWTERMIQKAILKNRIKGLGRDGITPIFPKLVMFVEEGVNLYKDDPNYDIKQLALECASKRMYPDIISAKNNKAITGSSVPVSPMGCRSFLSVWKDSTGNEILDGRNNLGVVTLNLPRIALDSYIGTQFNEQKFVELFNERMDLCFEALMCRISSLKGVKATVAPILYQEGAFGVRLKPDDDIIELFKNGRSSVSLGYIGIHELNILVGRDIGREILTKMNAHLKQWTERTGFAFSLYSTPAENLCYRFCKLDTEKYGSVKDVTDKGWYTNSFHVSVEENITPFEKISREAPYHFIATGGHISYVELPDMKNNLKGLEAVWDYAAQHLDYFGVNMPVDKCFTCGSTHEMTPTENGFVCSICGETDPKKMNTIRRTCGYLGNPNERGFNLGKNKEIMHRVKHQ | Function: Catalyzes the conversion of ribonucleotides into deoxyribonucleotides, which are required for DNA synthesis and repair.
Catalytic Activity: a ribonucleoside 5'-triphosphate + formate + H(+) = a 2'-deoxyribonucleoside 5'-triphosphate + CO2 + H2O
Sequence Mass (Da): 67957
Sequence Length: 605
EC: 1.1.98.6
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P28903 | MTPHVMKRDGCKVPFKSERIKEAILRAAKAAEVDDADYCATVAAVVSEQMQGRNQVDINEIQTAVENQLMSGPYKQLARAYIEYRHDRDIEREKRGRLNQEIRGLVEQTNASLLNENANKDSKVIPTQRDLLAGIVAKHYARQHLLPRDVVQAHERGDIHYHDLDYSPFFPMFNCMLIDLKGMLTQGFKMGNAEIEPPKSISTATAVTAQIIAQVASHIYGGTTINRIDEVLAPFVTASYNKHRKTAEEWNIPDAEGYANSRTIKECYDAFQSLEYEVNTLHTANGQTPFVTFGFGLGTSWESRLIQESILRNRIAGLGKNRKTAVFPKLVFAIRDGLNHKKGDPNYDIKQLALECASKRMYPDILNYDQVVKVTGSFKTPMGCRSFLGVWENENGEQIHDGRNNLGVISLNLPRIALEAKGDEATFWKLLDERLVLARKALMTRIARLEGVKARVAPILYMEGACGVRLNADDDVSEIFKNGRASISLGYIGIHETINALFGGEHVYDNEQLRAKGIAIVERLRQAVDQWKEETGYGFSLYSTPSENLCDRFCRLDTAEFGVVPGVTDKGYYTNSFHLDVEKKVNPYDKIDFEAPYPPLANGGFICYGEYPNIQHNLKALEDVWDYSYQHVPYYGTNTPIDECYECGFTGEFECTSKGFTCPKCGNHDASRVSVTRRVCGYLGSPDARPFNAGKQEEVKRRVKHLGNGQIG | Function: Catalyzes the conversion of ribonucleotides into deoxyribonucleotides, which are required for DNA synthesis and repair . Can reduce each of the four common ribonucleoside triphosphates .
Catalytic Activity: a ribonucleoside 5'-triphosphate + formate + H(+) = a 2'-deoxyribonucleoside 5'-triphosphate + CO2 + H2O
Sequence Mass (Da): 80023
Sequence Length: 712
Domain: Modulators bind to two classes of sites, one that binds ATP and dATP and regulates pyrimidine ribonucleotide reduction ('pyrimidine site'), the other that binds dATP, dGTP, and dTTP and regulates purine ribonucleotide reduction ('purine site').
EC: 1.1.98.6
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Q9L646 | MTPHVMKRDGCKVPFKSERIKEAILRAAKAAGVDDADYCATVAEVVSSQMNARSQVDINEIQTAVENQLMSGPYKQLARAYIEYRHDRDIQREKRGRLNQEIRGLVEQTNSALLNENANKDSKVIPTQRDLLAGIVAKHYARQHLLPRDVVQAHERGDIHYHDLDYSPFFPMFNCMLIDLKGMLTQGFKMGNAEIEPPKSISTATAVTAQIIAQVASHIYGGTTINRIDEVLAPFVTESYNKHRKTADEWQIPDAEGYARSRTEKECYDAFQSLEYEVNTLHTANGQTPFVTFGFGLGTSWESRLIQASILRNRIAGLGKNRKTAVFPKLVFAIRDGLNHKFGDPNYDIKQLALECASKRMYPDILNYDQVVKVTGSFKTPMGCRSFLGVWENENGEQIHDGRNNLGVISLNLPRIALEAKGDETAFWKLLDERLALARKALMTRIARLEGVKARVAPILYMEGACGVRLKADDDVSEIFKNGRASISLGYIGIHETINALFGGEHLYDSEQLRAKGIAIVERLRQAVDQWKDETGYGFSLYSTPSENLCDRFCRLDTAEFGVVPGVTDKGYYTNSFHLDVEKKVNPYDKIDFEAPYPPLANGGFICYGEYPNIQHNLKALEDVWDYSYQHVPYYGTNTPIDECYECGFTGEFECTSKGFTCPKCGNHDAARVSVTRRVCGYLGSPDARPFNAGKQEEVKRRVKHLGNGQIG | Function: Catalyzes the conversion of ribonucleotides into deoxyribonucleotides, which are required for DNA synthesis and repair.
Catalytic Activity: a ribonucleoside 5'-triphosphate + formate + H(+) = a 2'-deoxyribonucleoside 5'-triphosphate + CO2 + H2O
Sequence Mass (Da): 79959
Sequence Length: 712
EC: 1.1.98.6
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P07075 | MNYDRIYPCDFVNGPGCRVVLFVTGCLHKCEGCYNRSTWNARNGQLFTMNTVKELASHLSKSYIQGLTLTGGDPLYPQNREEISNLVSWVKARFPEKDIWLWTGYKFEDIKQLEMLKYVDVIIDGKYEKNLPTKKLWRGSDNQRLWSNTDGVWKHD | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine.
Catalytic Activity: glycyl-[protein] + reduced [flavodoxin] + S-adenosyl-L-methionine = 5'-deoxyadenosine + glycin-2-yl radical-[protein] + H(+) + L-methionine + semiquinone [flavodoxin]
Sequence Mass (Da): 18247
Sequence Length: 156
EC: 1.97.1.-
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P45080 | MNYLQYYPTDVINGEGTRCTLFVSGCTHACKGCYNQKSWSFSAGVLFDDVMEQQIINDLKDTRIKRQGLTLSGGDPLHPLNVETLLPFVQRVKRECPDKDIWVWTGYKLDELDKQQRAMLPYIDVLIDGKFIQEQADPSLVWRGSANQIIHRFKL | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Activation of anaerobic ribonucleoside-triphosphate reductase under anaerobic conditions by generation of an organic free radical, using S-adenosylmethionine and reduced flavodoxin as cosubstrates to produce 5'-deoxy-adenosine.
Catalytic Activity: glycyl-[protein] + reduced [flavodoxin] + S-adenosyl-L-methionine = 5'-deoxyadenosine + glycin-2-yl radical-[protein] + H(+) + L-methionine + semiquinone [flavodoxin]
Sequence Mass (Da): 17856
Sequence Length: 155
Subcellular Location: Cytoplasm
EC: 1.97.1.-
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Q7WZY5 | MKSISNRDKLQDLLTQYYLNTNEKMVFLNSTGEVIALNEAAEEVFADDNDYSQMTNAVCRRCEGYSNEYDIMSCENCFLEALEIGKGSFQVFIRTKDNKIQPYTASYELIDHEKGIYAFTLHNVSPQIQRQERMYQRKMMQKTISAQENERKRISRELHDGIVQELINVDVELRLLKYQQDKDELIDNSKRIEGIMSRLIDDVRNLSVELRPSSLDDLGLDAAFRSYFKQFEKNYGIHVNYHTNFSAQRFDNEIETVVYRVVQEALFNALKYAQVDIVEVSLQLNENNIIAEVSDRGVGFKRGDDPKGTGLGLFGMNERAELVNGTVNIDSQINRGTIVTLEVPITD | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Member of the two-component regulatory system NreB/NreC involved in the control of dissimilatory nitrate/nitrite reduction in response to oxygen. NreB functions as a direct oxygen sensor histidine kinase which is autophosphorylated, in the absence of oxygen, probably at the conserved histidine residue, and transfers its phosphate group probably to a conserved aspartate residue of NreC. NreB/NreC activates the expression of the nitrate (narGHJI) and nitrite (nir) reductase operons, as well as the putative nitrate transporter gene narT.
PTM: Autophosphorylated.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 39953
Sequence Length: 347
Subcellular Location: Cytoplasm
EC: 2.7.13.3
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P46011 | MSMQQETSHMTAAPQTNGHQIFPEIDMSAGDSSSIVRATVVQASTVFYDTPATLDKAERLLSEAAENGSQLVVFPEAFIGGYPRGSTFELAIGSRTAKGRDDFRKYHASAIDVPGPEVERLALMAKKYKVYLVMGVIEREGYTLYCTVLFFDSQGLFLGKHRKLMPTALERCIWGFGDGSTIPVFDTPIGKIGAAICWENRMPSLRTAMYAKGIEIYCAPTADSRETWLASMTHIALEGGCFVLSANQFCRRKDYPSPPEYMFSGSEESLTPDSVVCAGGSSIISPLGIVLAGPNYRGEALITADLDLGDIARAKFDFDVVGHYSRPEVFSLNIREHPRKAVSFKTSKVMEDESV | Function: Highly specific for beta-cyano-L-alanine (Ala(CN)). Low activity with 3-phenylpropionitrile (PPN) or allylcyanide and no activity with indole-3-acetonitrile. Not associated with auxin production but may be involved in cyanide detoxification.
Catalytic Activity: a nitrile + 2 H2O = a carboxylate + NH4(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38895
Sequence Length: 355
Subcellular Location: Cell membrane
EC: 3.5.5.1
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Q6H849 | MAMVPSGSGGGPPVIAEVEMNGGADSGAATVRATVVQASTVFYDTPATLDKAERLIEEAAGYGSQLVVFPEAFVGGYPRGSTFGFGANISIGNPKDKGKEEFRKYHAAAIEVPGPEVTRLAAMAGKYKVFLVMGVIEREGYTLYCSVLFFDPLGRYLGKHRKLMPTALERIIWGFGDGSTIPVYDTPLGKIGALICWENKMPLLRTALYGKGIEIYCAPTADSRQVWQASMTHIALEGGCFVLSANQFCRRKDYPPPPEYVFSGLGEEPSPDTVVCPGGSVIISPSGEVLAGPNYEGEALITADLDLGEIVRAKFDFDVVGHYARPEVLSLVVNDQPHLPVSFTSAAEKTTAAKSDSTAKPY | Function: Highly specific for beta-cyano-L-alanine (Ala(CN)). Low activity with 3-phenylpropionitrile (PPN). Not associated with auxin production but may be involved in cyanide detoxification (By similarity).
Catalytic Activity: a nitrile + 2 H2O = a carboxylate + NH4(+)
Sequence Mass (Da): 38676
Sequence Length: 362
EC: 3.5.5.1
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P33036 | VSYNSKFLAATVQAEPVVLDA | Function: Acts on many kinds of nitrile compounds such as aliphatic, aromatic, and heterocyclic mononitriles or dinitriles. Prefers S-(-)-2-(4'-isobutylphenyl)-propionitrile to R-(+)-2-(4'-isobutylphenyl)-propionitrile as the substrate.
Catalytic Activity: a nitrile + 2 H2O = a carboxylate + NH4(+)
Sequence Mass (Da): 2223
Sequence Length: 21
EC: 3.5.5.1
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P20960 | MQTRKIVRAAAVQAASPNYDLATGVDKTIELARQARDEGCDLIVFGETWLPGYPFHVWLGAPAWSLKYSARYYANSLSLDSAEFQRIAQAARTLGIFIALGYSERSGGSLYLGQCLIDDKGQMLWSRRKLKPTHVERTVFGEGYARDLIVSDTELGRVGALCCWEHLSPLSKYALYSQHEAIHIAAWPSFSLYSEQAHALSAKVNMAASQIYSVEGQCFTIAASSVVTQETLDMLEVGEHNASLLKVGGGSSMIFAPDGRTLAPYLPHDAEGLIIADLNMEEIAFAKAINDPVGHYSKPEATRLVLDLGHREPMTRVHSKSVIQEEAPEPHVQSTAAPVAVSQTQDSDTLLVQEPS | Function: Nitrilase that acts mostly on arylacetonitriles.
Catalytic Activity: a nitrile + 2 H2O = a carboxylate + NH4(+)
Sequence Mass (Da): 38908
Sequence Length: 356
EC: 3.5.5.1
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P10045 | MDTTFKAAAVQAEPVWMDAAATADKTVTLVAKAAAAGAQLVAFPELWIPGYPGFMLTHNQTETLPFIIKYRKQAIAADGPEIEKIRCAAQEHNIALSFGYSERAGRTLYMSQMLIDADGITKIRRRKLKPTRFERELFGEGDGSDLQVAQTSVGRVGALNCAENLQSLNKFALAAEGEQIHISAWPFTLGSPVLVGDSIGAINQVYAAETGTFVLMSTQVVGPTGIAAFEIEDRYNPNQYLGGGYARIYGPDMQLKSKSLSPTEEGIVYAEIDLSMLEAAKYSLDPTGHYSRPDVFSVSINRQRQPAVSEVIDSNGDEDPRAACEPDEGDREVVISTAIGVLPRYCGHS | Function: Specific for the herbicide bromoxynil (3,5-dibromo-4-hydroxybenzonitrile); converts it to its metabolite 3,5-dibromo-4-hydroxybenzoic acid.
Catalytic Activity: a nitrile + 2 H2O = a carboxylate + NH4(+)
Sequence Mass (Da): 37802
Sequence Length: 349
EC: 3.5.5.1
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P54845 | MALPPSPLAMEYVNDFDLMKFEVKREPSEGRPGPPTASLGSTPYSSVPPSPTFSEPGMVGATEGTRPGLEELYWLATLQQQLGAGEALGLSPEEAMELLQGQGPVPVDGPHGYYPGSPEETGAQHVQLAERFSDAALVSMSVRELNRQLRGCGRDEALRLKQRRRTLKNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVARLARERDLYKARCDRLTSSGPGSGDPSHLFL | Function: Acts as a transcriptional activator which regulates the expression of several rod-specific genes, including RHO and PDE6B . Functions also as a transcriptional coactivator, stimulating transcription mediated by the transcription factor CRX and NR2E3 . Binds in a sequence-specific manner to the rhodopsin promoter .
PTM: Phosphorylated .
Sequence Mass (Da): 25940
Sequence Length: 237
Domain: The minimal transactivation domain (MTD) is conserved across the MAF family, it may activate transcription by recruiting TBP and associated factors at the promoters of target genes.
Subcellular Location: Cytoplasm
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P54846 | MAFPPSPLAMEYVNDFDLMKFEIKREPSEGRSGVPTASLGSTPYSSVPPSPTFSEPGMVGGGEAPRPGLEELYWLATLQQQLGSDEVLGLSPDEAVELLQNQGPVSMEGPLGYYSGSPGETGAQHVQLPERFSDAALVSMSVRELNRQLRGCGRDEALRLKQRRRTLKNRGYAQACRSKRLQQRRGLEAERARLAAQLDALRAEVARLARERDLYKARCDRLTSGGPGSDDHTHLFL | Function: Acts as a transcriptional activator which regulates the expression of several rod-specific genes, including RHO and PDE6B. Functions also as a transcriptional coactivator, stimulating transcription mediated by the transcription factor CRX and NR2E3. Binds in a sequence-specific manner to the rhodopsin promoter.
PTM: Disumoylated at Lys-20. Sumoylation modulates the transcriptional activity of NRL on RHO and NR2E3 promoters, and is required for normal rod differentiation.
Sequence Mass (Da): 26083
Sequence Length: 237
Domain: The minimal transactivation domain (MTD) is conserved across the MAF family, it may activate transcription by recruiting TBP and associated factors at the promoters of target genes.
Subcellular Location: Cytoplasm
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Q9VMA0 | MELVKRGFLRACKNHSYLSFELIDDILAPLCANHKTTKPGSKEAIRALVAEINDTISDLGQLLVFIKYPVKAEEYLVYAKTDATPDSVANTGLTAEECQYFSKLLDKIASEEDCHIAWNDAYNDIVLQASSKPLKKSRMQELLQKWIQMGYFMEVTDRIYLGPRSLVELSFYLSSNHADNIKNCTLCKCLVLWDIRCGSCNIQYHRGCIQTYLQRRDICPSCGNLWTTPIRRSIG | Function: Component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination . The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks (By similarity).
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 26774
Sequence Length: 235
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q8WV22 | MQGSTRRMGVMTDVHRRFLQLLMTHGVLEEWDVKRLQTHCYKVHDRNATVDKLEDFINNINSVLESLYIEIKRGVTEDDGRPIYALVNLATTSISKMATDFAENELDLFRKALELIIDSETGFASSTNILNLVDQLKGKKMRKKEAEQVLQKFVQNKWLIEKEGEFTLHGRAILEMEQYIRETYPDAVKICNICHSLLIQGQSCETCGIRMHLPCVAKYFQSNAEPRCPHCNDYWPHEIPKVFDPEKERESGVLKSNKKSLRSRQH | Function: RING-type zinc finger-containing E3 ubiquitin ligase that assembles with melanoma antigen protein (MAGE) to catalyze the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. Within MAGE-RING ubiquitin ligase complex, MAGE stimulates and specifies ubiquitin ligase activity likely through recruitment and/or stabilization of the E2 ubiquitin-conjugating enzyme at the E3:substrate complex. Involved in maintenance of genome integrity, DNA damage response and DNA repair . NSMCE3/MAGEG1 and NSMCE1 ubiquitin ligase are components of SMC5-SMC6 complex and may positively regulate homologous recombination-mediated DNA repair . MAGEF1-NSMCE1 ubiquitin ligase promotes proteasomal degradation of MMS19, a key component of the cytosolic iron-sulfur protein assembly (CIA) machinery. Down-regulation of MMS19 impairs the activity of several DNA repair and metabolism enzymes such as ERCC2/XPD, FANCJ, RTEL1 and POLD1 that require iron-sulfur clusters as cofactors .
PTM: Ubiquitinated.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 30855
Sequence Length: 266
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q9D720 | MQGSTRRAGAMTDVHRRFLQLLMTHGVLEEWEVRRLQNHCYQVHDRNATVDKLEDFINNINSVLESLYIEIKKGVTEDDGRPIYALVNLATTSVSKMATDFAENELDLFRKALELIVDSETGFASSTNILNLVDQLKGKKMRKKEAEQVLQKFVQSKWLIEKEGEFTLHGRAILEMEQFIRESYPDSVKMCNICHGLLIQGQSCETCGIRMHLPCVAKYFQSIPEPHCPHCNDYWPHDIPEVYNPEKEREAGISKSSRKSLRTRQH | Function: RING-type zinc finger-containing E3 ubiquitin ligase that assembles with melanoma antigen protein (MAGE) to catalyze the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. Within MAGE-RING ubiquitin ligase complex, MAGE stimulates and specifies ubiquitin ligase activity likely through recruitment and/or stabilization of the E2 ubiquitin-conjugating enzyme at the E3:substrate complex. Involved in maintenance of genome integrity, DNA damage response and DNA repair. NSMCE3/MAGEG1 and NSMCE1 ubiquitin ligase are components of SMC5-SMC6 complex and may positively regulate homologous recombination-mediated DNA repair.
PTM: Ubiquitinated.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 30708
Sequence Length: 266
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q5RAZ5 | MQGSTRRMSVMTDVHRRFLQLLMTHGVLEEWDVKRLQRHCYKVHDRNATVDKLEDFINNINSVLESLYIEIKRGVTEDDGRPIYALVNLATTSISKMATDFAENELDLFRKALELIIDSETGFGSSTNILNLVDQLKGKKMRKKEAEQVLQKFVQNKWLIEKEGEFTLHGRAILEMEQYIRETYPDAVKICNICHSLLIQGQSCETCGIRMHLPCVAKYFQSNAEPRCPHCNDYWPHEIPKVFDPEKERESGVSKSNKKSLRSRQH | Function: RING-type zinc finger-containing E3 ubiquitin ligase that assembles with melanoma antigen protein (MAGE) to catalyze the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. Within MAGE-RING ubiquitin ligase complex, MAGE stimulates and specifies ubiquitin ligase activity likely through recruitment and/or stabilization of the E2 ubiquitin-conjugating enzyme at the E3:substrate complex. Involved in maintenance of genome integrity, DNA damage response and DNA repair. NSMCE3/MAGEG1 and NSMCE1 ubiquitin ligase are components of SMC5-SMC6 complex and may positively regulate homologous recombination-mediated DNA repair.
PTM: Ubiquitinated.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 30900
Sequence Length: 266
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q53EK2 | MEKERQDGLSDKHKFILQYIMCRTAGVDNEQVRELVQEQYGETATVEDVINELNNSLHNFDFKIKRVQDQLDGRLTLHFQNLSGDPVSQMATPYPPVQIELMRKIIEWIMKCDDYQYSLTTLQIQKLSRKEMGLAPSVIESHLHTFERDGWLRQREGIWTFTNHALAELDAYLHNEYESNLYECNACREIVIAGYVCDCGYCLHVYCCKHLAHVNCINCNTPWANATVIGRW | Function: Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Plays a critical role in meiosis.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 27052
Sequence Length: 232
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q6PAF4 | MADRINESHQRFLQALMSHGIMEGSAVRALHRHCCELHKVHYMHDKLDDFVGVLNRHLQPLFMTIEKGVGEEDGLTYYALVNRVENDITKMASDYAENELELFRKTMELIILSDNGFATSISILNLADELQSKKMKKKEVEQLLQSFVQEKWLIGRNGEYTLHTRCIMELEHYIRNTYQDVAKICNVCRKVAIQSQLCENCGIPLHLQCAGKYFHGKANPTCPNCNESWPHEIPDLNQVSSQGPSHSQTETVRGRNQRSKNTSTASRTSR | Function: RING-type zinc finger-containing E3 ubiquitin ligase that assembles with melanoma antigen protein (MAGE) to catalyze the direct transfer of ubiquitin from E2 ubiquitin-conjugating enzyme to a specific substrate. Within MAGE-RING ubiquitin ligase complex, MAGE stimulates and specifies ubiquitin ligase activity likely through recruitment and/or stabilization of the E2 ubiquitin-conjugating enzyme at the E3:substrate complex. Involved in maintenance of genome integrity, DNA damage response and DNA repair.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 30947
Sequence Length: 270
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q07913 | MEVHEEQVSAPVTGDATAKYLLQYILSARGICHENALILALMRLETDASTLNTEWSIQQWVDKLNDYINAINVKLNLLGYKIIRINHGIGRNAVTLKAKQNFESFEDNTAIRAHNNDYAVLQSIVLPESNRFFVYVNLASTEETKLATRFNQNEIEFMKWAIEQFMISGETIVEGPALETSIIVKEVNRILVAATGDSNLAKWRKFSTFTVGSTNLFQFQELTATDIEDLLLRLCELKWFYRTQEGKFGIDLRCIAELEEYLTSMYNLNTCQNCHKLAIQGVRCGNESCREENEETGENSLSQIWHVDCFKHYITHVSKNCDRCGSSLITEGVYVI | Function: Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 38335
Sequence Length: 336
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q8GYH7 | MASASSSDGVAGRIQNASLVLVSDNSSTLADIRKAVAMMKNIAVQLEKENQTDKVKDLENSVAELLDLHSDCNHRSTAIQSVANRYQPVEQLTDFKKLLDDEFTKLKATPSSVPQNDHLMRQFREAVWNVHHAGEPMPGDDDEDIVMTSTQCPLLNMTCPLSGKPVTELADPVRSMDCRHVYEKSVILHYIVNNPNANCPVAGCRGKLQNSKVICDAMLKFEIEEMRSLNKQSNRAEVIEDFTEDVDED | Function: E3 SUMO-protein ligase that modulates cell cycle progression and functions as a repressor of endocycle onset in meristems. May function downstream of the meristem patterning transcription factors PLETHORA 1 and 2 (PLT1 and PLT2) in root meristem development. Modulates the expression of the mitotic cyclins CYCB1-1 and CYCB1-2 and cyclin-dependent kinases CDKB1-1 and CDKB2-1 in root meristem. Involved in cytokinin signaling in root development.
PTM: Sumoylated, possibly via autosumoylation.
Sequence Mass (Da): 27717
Sequence Length: 249
Pathway: Protein modification; protein sumoylation.
Subcellular Location: Nucleus
EC: 2.3.2.-
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Q32KY9 | MPGRSTSSSSSGSTGFISFSGVESALSSLKTFQSCISSGMDTASSVALDLVETQTEVSSEYSMDKAMVEFAMMDRELNHYLKAVQSTINHVKEERSEKIPDLKLLVEKKFLALQNKNSDADFQNNEKFVQFKQQLKELKKQYGLQSDREADITEGVDEDMIVTQSQTNFICPITQLEMKKPVKNKVCGHTYEEEAIVRMIESKHERKKKACCPKIGCSHVDMRMSDLIQDEALRRAIESHKKRRRQSN | Function: E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a complex involved in DNA double-strand break repair by homologous recombination. Is not be required for the stability of the complex. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. Acts as an E3 ligase mediating SUMO attachment to various proteins such as SMC6L1 and TSNAX, the shelterin complex subunits TERF1, TERF2, TINF2 and TERF2IP, RAD51AP1, and maybe the cohesin components RAD21 and STAG2. Required for recruitment of telomeres to PML nuclear bodies. Required for sister chromatid cohesion during prometaphase and mitotic progression.
PTM: Sumoylated, possibly via autosumoylation.
Sequence Mass (Da): 28119
Sequence Length: 248
Pathway: Protein modification; protein sumoylation.
Subcellular Location: Nucleus
EC: 2.3.2.-
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Q96MF7 | MPGRSSSNSGSTGFISFSGVESALSSLKNFQACINSGMDTASSVALDLVESQTEVSSEYSMDKAMVEFATLDRQLNHYVKAVQSTINHVKEERPEKIPDLKLLVEKKFLALQSKNSDADFQNNEKFVQFKQQLKELKKQCGLQADREADGTEGVDEDIIVTQSQTNFTCPITKEEMKKPVKNKVCGHTYEEDAIVRMIESRQKRKKKAYCPQIGCSHTDIRKSDLIQDEALRRAIENHNKKRHRHSE | Function: E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a complex involved in DNA double-strand break repair by homologous recombination . Is not be required for the stability of the complex . The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks . The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs) . Acts as an E3 ligase mediating SUMO attachment to various proteins such as SMC6L1 and TSNAX, the shelterin complex subunits TERF1, TERF2, TINF2 and TERF2IP, RAD51AP1, and maybe the cohesin components RAD21 and STAG2 . Required for recruitment of telomeres to PML nuclear bodies . SUMO protein-ligase activity is required for the prevention of DNA damage-induced apoptosis by facilitating DNA repair, and for formation of APBs in ALT cell lines . Required for sister chromatid cohesion during prometaphase and mitotic progression .
PTM: Sumoylated, possibly via autosumoylation.
Sequence Mass (Da): 27932
Sequence Length: 247
Pathway: Protein modification; protein sumoylation.
Subcellular Location: Nucleus
EC: 2.3.2.-
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Q91VT1 | MPGRSSTSSGSTRYISFSGIESALSSLKNFQSCISSGMDTVSSVALDLVETQTEVSSEYSMDKAMVEFAKMDRELSHYVKAVQSTINHVKEERPEKVPDLKLLVEKKFLALQDKNSDADFKENEKFVQFKQQLRELKKQYGIHADRENDLTEGVDEDMIVTQSQTNFICPITQLEMKKPVKNKMCGHTYEEEAIVRMIESKHKRKKKACCPKIGCSHTDMRMSDLIPDEALRRAIESHNKKKKRHSE | Function: E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a complex involved in DNA double-strand break repair by homologous recombination. Is not be required for the stability of the complex. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. Acts as an E3 ligase mediating SUMO attachment to various proteins such as SMC6L1 and TSNAX, the shelterin complex subunits TERF1, TERF2, TINF2 and TERF2IP, RAD51AP1, and maybe the cohesin components RAD21 and STAG2. Required for recruitment of telomeres to PML nuclear bodies. Required for sister chromatid cohesion during prometaphase and mitotic progression.
PTM: Sumoylated, possibly via autosumoylation.
Sequence Mass (Da): 28231
Sequence Length: 247
Pathway: Protein modification; protein sumoylation.
Subcellular Location: Nucleus
EC: 2.3.2.-
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Q4PIR3 | MSEAQLKTSLEALSQNLLPGNQNHCSFDFQLKEIDDSIKQVIKCALVAAEIKNNECLDMLDSGIRELLDAKQRLLLMQQSVDTLANKTSENISDFENKSLLDIYTQIFKELIQEYEEKSDYGKYGTQGEYIEFKKTIWHEQNTDGSDFPSMKTFFNVMNTEEQEADEVMVYSATFDNRCPLTLQPIVHPILSTACNHFYEKDAILSLLNPTCVCPVVGCEARLQRSLLKEDEILERRLRRAQEISNLKEA | Function: Acts as an E3 ligase mediating SUMO/Smt3 attachment to other proteins. Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Plays a critical role in meiosis.
PTM: Autosumoylated.
Sequence Mass (Da): 28676
Sequence Length: 250
Pathway: Protein modification; protein sumoylation.
Subcellular Location: Nucleus
EC: 2.3.2.-
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Q7ZXH2 | MSGRSAPVVSFSSVDNSLSSLKNCQGYLHTGMDITVSVALDLLETGCESTEVDAMESVMLEYSAMERDLKQYIHAVEETVQKLRREQMEQVPDLQSLVQEKYATIQKKNDDEDLKKNDRFVQFKDQLREMRKQMGEKEEGDAAFENVDEDIAVLPSQQNLTCPITQMEMTNPVKNKVCGHTYEKEAIERMIQDRHQKKKRVKCPKVGCVHSDMQISDLVPDTALKRTIDILNKQKGRH | Function: E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a complex involved in repair of DNA double-strand breaks by homologous recombination. Is not be required for the stability of the complex. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The complex is required for telomere maintenance via recombination and mediates sumoylation of shelterin complex (telosome) components. Required for recruitment of telomeres to PML nuclear bodies. SUMO protein-ligase activity is required for the prevention of DNA damage-induced apoptosis by facilitating DNA repair. Required for sister chromatid cohesion during prometaphase and mitotic progression (By similarity).
Sequence Mass (Da): 27226
Sequence Length: 238
Pathway: Protein modification; protein sumoylation.
Subcellular Location: Nucleus
EC: 2.3.2.-
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P38632 | MALNDNPIPKSVPLHPKSGKYFHNLHARDLSNIYQQCYKQIDETINQLVDSTSPSTIGIEEQVADITSTYKLLSTYESESNSFDEHIKDLKKNFKQSSDACPQIDLSTWDKYRTGELTAPKLSELYLNMPTPEPATMVNNTDTLKILKVLPYIWNDPTCVIPDLQNPADEDDLQIEGGKIELTCPITCKPYEAPLISRKCNHVFDRDGIQNYLQGYTTRDCPQAACSQVVSMRDFVRDPIMELRCKIAKMKESQEQDKRSSQAIDVL | Function: Acts as an E3 ligase mediating SUMO/Smt3 attachment to SMC5 and YKU70. Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks.
Sequence Mass (Da): 30354
Sequence Length: 267
Pathway: Protein modification; protein sumoylation.
Subcellular Location: Nucleus
EC: 2.3.2.-
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Q9Y7U4 | MSQLSFTGKSSSKGRSRLTQEVRPTASQIIADEEASDLDEYEEDLEGSGNEDDFGPSMSRSSRGRKRRKGDPLELQSQFEERNETDAINFQLLVRNVVRYAICSQTSHNTITRKDIVQKAFPEGTSRNLFQSVFEEADRQLQLSFGFRLVAVTQSNRKKDMAVSQLRRPATSNANSSNLHRYWVLRSTLPMELQKDSRLIVDSVLDTAYYGFLMTVIAFIAVSHCSVGHSELQSFLQELLTEEETTPLHLDITRSLSLLVRQGYLDRVKDDTHNQFVYYIGSRAVTEISIEGLKSFVTEFFPDSDIDMDALLTEYRQEYQNQSSSSAA | Function: Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Plays a critical role in meiosis.
PTM: Sumoylated by nse2.
Sequence Mass (Da): 37276
Sequence Length: 328
Subcellular Location: Nucleus
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P03535 | MDKLADLNYTLSVITSMNDTLHSIIQDPGMAYFLYIASVLTVLFTLHKASIPTMKIALKTSKCSYKVIKYCIVTIINTLLKLAGYKEQVTTKDEIEQQMDRIVKEMRRQLEMIDKLTTREIEQVELLKRIHDNLITRPVDVIDMSKEFNQKNIKTLDEWESGKNPYEPSEVTASM | Function: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca(2+) in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication and immature particle assembly.
PTM: The N-glycosyl content is primarily Man(9)GlcNAc, with a small amount of Man(8)GlcNAc.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 20237
Sequence Length: 175
Domain: Binds 1 calcium ion per tetramer.
Subcellular Location: Host rough endoplasmic reticulum membrane
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Q45UF1 | MEGTSESPVLDEFEVNNNDYDNDFISRFSQNPLNAFSLFTDGNLQEYFMNNSLEKIVIHVVLIVISLCGIKAQTSKIIYVVRLLFWKIYNVINNLVNKVINREKIINHQVVDNRFREFEERFRLLLLQHDKNIAKQDDIVQYNKLDNFAESIKSEFNLKVAEMERRFQELKWRCDMIANKAMNTIVLANTVDSNNKDEKIVFDEGSVVQYNRE | Function: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca(2+) in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication and immature particle assembly.
PTM: The N-glycosyl content is primarily Man(9)GlcNAc, with a small amount of Man(8)GlcNAc.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 25111
Sequence Length: 213
Subcellular Location: Host rough endoplasmic reticulum membrane
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Q9YS17 | MEFINQTFFSDYSEGKIDTIPYALGIVLALTNGSRILKFINLLISLLRKFIITSKTVIGKFKIENNTSHQNDDIHKEYEEVMKQMREMRVHVTALFDSIHKDNMEWRMSESIRREKKREMKASTAENEVKIHTNDVNICDTSGLETEVCL | Function: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca(2+) in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication and immature particle assembly.
PTM: The N-glycosyl content is primarily Man(9)GlcNAc, with a small amount of Man(8)GlcNAc.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 17489
Sequence Length: 150
Subcellular Location: Host rough endoplasmic reticulum membrane
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Q9NPB1 | MIRLGGWCARRLCSAAVPAGRRGAAGGLGLAGGRALRVLVDMDGVLADFEGGFLRKFRARFPDQPFIALEDRRGFWVSEQYGRLRPGLSEKAISIWESKNFFFELEPLPGAVEAVKEMASLQNTDVFICTSPIKMFKYCPYEKYAWVEKYFGPDFLEQIVLTRDKTVVSADLLIDDRPDITGAEPTPSWEHVLFTACHNQHLQLQPPRRRLHSWADDWKAILDSKRPC | Function: Dephosphorylates specifically the 5' and 2'(3')-phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP.
Sequence Mass (Da): 25862
Sequence Length: 228
Subcellular Location: Mitochondrion
EC: 3.1.3.-
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Q8CHQ9 | MAAYHIRQYQEKDHKRVLELFSSGMKELIPAAIRQMLTLPHSLLLLPGVPVTIVLMSASWLLATLYSFLFLLCLWLIFWISCRNYVAKSLQADLADITKSYLNAHGSFWVAESGDQVVGMVGAQPVKDPPLGKKQMQLFRLSVSSQHRGQGIAKALVRTVLQFARDQGYSDVVLETGSVQHSAQALYQAMGFQKTGQYFVSISKKLMGLSILQFSYSLPFASGPGYSGKYLKKGPIPC | Function: Probable acetyltransferase (Probable). Has no detectable histone acetyltransferase activity towards histone H3 or H4.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26424
Sequence Length: 238
Subcellular Location: Membrane
EC: 2.3.1.-
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Q9JIY8 | MAPYHIRKYQDSDHRSVVDLFRRGMEEHIPATFRHMLLLPRTLLLLLGVPLTLFLASGSWLLVLLSILTLFLSLWFLAKYTWEKHVMNCLHTDMADITRTYLSSHSSCFWVAESRGQTVGMVAARPVKDPLLQKKQLQLLHLSVSLQHRREGLGKAMVRTVLQFAQMQGFSEVVLSTSMLQYAALALYQGMGFQKTGETFYTYLSRLRKSPMINLKYSLTSREGDL | Function: Has histone acetyltransferase activity in vitro, with specificity for histone H4.
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25956
Sequence Length: 226
Subcellular Location: Nucleus membrane
EC: 2.3.1.48
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Q9QXS4 | MAPYHIRKYQDSDHRSVVNLFCRGTEEHISASFRYMLLLPGTLLILLGVPLTLFLASGSWLLVLLSTLTLLVSLWLLAKYPWEKYTAMCLHSDMADIPRTYLSSHYSCFWVAESRGQMVGIIAVLPVKDPLLQRKQLQLRHLSVSLEHRREGIGRAMVRTALQFAEMQGFSEVVLVTSMLQYAALALYQSMGFQKTGEFFYTFVSRLRNSPMICLKYCLTSALNDLKT | Function: Has histone acetyltransferase activity in vitro, with specificity for histone H4.
Catalytic Activity: acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-lysyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26038
Sequence Length: 228
Subcellular Location: Nucleus membrane
EC: 2.3.1.48
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O60178 | MKFGCVQFFPKLGKVNENIVHLRQLLDQHSEALQSVKLLVFPEMCLTGYNFKNSESIQPFLENVTSNHCPSIQFAQEVSEQYRCYTIIGFPEFQNSNGISTLYNSTALISPKKELLNVYHKHFLFETDKSWATEGKGFSFEPCIPELGPISMAICMDINPYDFKAPFEKFEYANFILRELEHQQMVSSNVSRPIICLSMAWLVSDDKVIDASLPDIKNLHYWTTRLSPLINSNTDAIVLVANRWGKENDLNFSGTSCIMELSQGRAILHGVLKAAENGIVVGELEK | Function: Deamidates N-terminal Asn and Gln. Component of a targeting complex in the N-end rule pathway (By similarity).
Sequence Mass (Da): 32427
Sequence Length: 286
Subcellular Location: Cytoplasm
EC: 3.5.1.-
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P54989 | MGANKQMNLGFLFQISGVHYGGWRYPSAQPHRATDIQYYAEIVRTAERGKLDFCFLADSIAAYEGSADQQDRSKDALMAAEPKRLLEPFTLLAALAMVTEHIGLVTTATTTYNEPYTMARLFASLDHITNGRAGWNVVTSANLAEAHNFGRDGHVEHGDRYARAEEFINVVFKLWDSIEDGAYLRDKLAGRYGLSEKIHFINHIGEHFKVRGPLNVPRPPQGHPVIVQAGSSHPGKELAARTAEVVFTAQQTLADGKAFYSDVKGRMAKYGRSSENLKVLPGVVVYVAETESEAKAKYETVSNLVPPDFGLFMLSDLLGEIDLKQFDIDGPLPEDLPEAKGSQSRREVIINLARRENLTIRQLYQRVSGASGHRSIWGTPKQIADQFEQWVYEEAADGFNILPPYLPESMNDFVNFVVPELQRRGIFRTEYEGSTLRDHLGLARPKNSVAKPS | Function: Hydroxylation of nitrilotriacetate.
Catalytic Activity: FMNH2 + nitrilotriacetate + O2 = ammoniodiacetate + FMN + glyoxylate + H2O
Sequence Mass (Da): 50529
Sequence Length: 453
EC: 1.14.14.10
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P54990 | MADQIRSATEGGDPTSDPKGFRRALGTFPTGVTIVTAPGVDGPAGVTANSFASVSLDPPLVLWSIGHTSRSHSKFQQSATFAINILADDQVGVSQVFAGGSADKFSLVDWHTGRTGAPLIDNALAYFDCVCEARHEGGDHTIMIGRVVDFGRAEGSPLAFSQGRYGVTLDHPEAAKARDHKSEEYGLDDLPFLSLIAKAHYKEDADLEEQRSAAGCTPVGSKILAGLYGSAPLTADELARRMYLDRREVVDSLNEFVADGHVESCDSGRFALTESGKQRRRRMIEYVSRYQDEQLASISRSDLGVATRVLQAFLAGPGRGSS | Function: Catalyzes the NADH-dependent reduction of the FMN cofactor of the nitrilotriacetate monooxygenase subunit A.
Catalytic Activity: FMNH2 + NAD(+) = FMN + 2 H(+) + NADH
Sequence Mass (Da): 34496
Sequence Length: 322
EC: 1.5.1.42
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Q5S7W5 | MAQPELLWAAAGLMLLGVAVSACVRCQLYATKRGKDGSQGSRLERPQRFEVIRSCSAVTRRPERIKEPEHLARKAPEELSTSCHVGFESSAEPRYQNFLTEDCLHEDAAYVEPVPLDYYSHNRFFSPPNDEDSHSYQNVIIGDPCSSELDDAEDYENSTAIEVWKVQQAKAMLYAESQDEEPDYVNTDPTIDAVVLSK | Function: Involved in BCR (B-cell antigen receptor)-mediated signaling in B-cells. May also be involved in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells and FCGR1 (high affinity immunoglobulin gamma Fc receptor I)-mediated signaling in myeloid cells. Couples activation of these receptors and their associated kinases with distal intracellular events such as calcium mobilization through the recruitment of GRB2.
PTM: Phosphorylated on tyrosines following cross-linking of BCR; which induces the recruitment of GRB2.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 22277
Sequence Length: 198
Subcellular Location: Cell membrane
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Q9GZY6 | MSSGTELLWPGAALLVLLGVAASLCVRCSRPGAKRSEKIYQQRSLREDQQSFTGSRTYSLVGQAWPGPLADMAPTRKDKLLQFYPSLEDPASSRYQNFSKGSRHGSEEAYIDPIAMEYYNWGRFSKPPEDDDANSYENVLICKQKTTETGAQQEGIGGLCRGDLSLSLALKTGPTSGLCPSASPEEDEESEDYQNSASIHQWRESRKVMGQLQREASPGPVGSPDEEDGEPDYVNGEVAATEA | Function: Involved in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. May also be involved in BCR (B-cell antigen receptor)-mediated signaling in B-cells and FCGR1 (high affinity immunoglobulin gamma Fc receptor I)-mediated signaling in myeloid cells. Couples activation of these receptors and their associated kinases with distal intracellular events through the recruitment of GRB2.
PTM: Phosphorylated on tyrosines following cross-linking of BCR in B-cells, FCGR1 in myeloid cells, or FCER1 in mast cells; which induces the recruitment of GRB2.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 26550
Sequence Length: 243
Subcellular Location: Cell membrane
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Q9JHL0 | MSAELELLWPVSGLLLLLLGATAWLCVHCSRPGVKRNEKIYEQRNRQENAQSSAAAQTYSLARQVWPGPQMDTAPNKSFERKNKMLFSHLEGPESPRYQNFYKGSNQEPDAAYVDPIPTNYYNWGCFQKPSEDDDSNSYENVLVCKPSTPESGVEDFEDYQNSVSIHQWRESKRTMGAPMSLSGSPDEEPDYVNGDVAAAENI | Function: Involved in FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. May also be involved in BCR (B-cell antigen receptor)-mediated signaling in B-cells and FCGR1 (high affinity immunoglobulin gamma Fc receptor I)-mediated signaling in myeloid cells. Couples activation of these receptors and their associated kinases with distal intracellular events through the recruitment of GRB2.
PTM: Phosphorylated on tyrosines following cross-linking of BCR in B-cells, high affinity IgG receptor (FCGR1) in myeloid cells, or high affinity IgE receptor (FCER1) in mast cells; which induces the recruitment of GRB2.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 22876
Sequence Length: 203
Subcellular Location: Cell membrane
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O64876 | MIYVGGVQFLDESSSFSLSSSSQGSSLLVDVMSHPVITLASDSFKNLEEKNVSFDESDSESSTKDRYVYIFQREFAVVNPALVDFVGTDEATTCVGLVIRNRKSGMTSVAHMDSPEIVDLGISQMLLLVLQDDVDAELDVHMVGGYEDVDIKNADGVGDYAKPEGYSFPLCCKLVETLQKRRENFHIQTLFILGHNTKLDSQANTCPIFNGCLVNTSTGAILPASFNRTSRCPDEIVRRIRVSSSFEDSSWKGKLLDTYDTKTDRFIIAPCRWTMRLIEYVWELNQLTDEEILTNCSTSPSAEGPDFVNSLRRNWGYLLKYPEWSKTFPRRQPRVFERTVDGHWKKC | Function: N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by NTAN1 renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position (By similarity). Does not seem to be involved in immune response, unlike the N-terminal glutamine amidohydrolase NTAQ1 .
Catalytic Activity: H(+) + H2O + N-terminal L-asparaginyl-[protein] = N-terminal L-aspartyl-[protein] + NH4(+)
Sequence Mass (Da): 39174
Sequence Length: 347
EC: 3.5.1.121
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Q96AB6 | MPLLVEGRRVRLPQSAGDLVRAHPPLEERARLLRGQSVQQVGPQGLLYVQQRELAVTSPKDGSISILGSDDATTCHIVVLRHTGNGATCLTHCDGTDTKAEVPLIMNSIKSFSDHAQCGRLEVHLVGGFSDDRQLSQKLTHQLLSEFDRQEDDIHLVTLCVTELNDREENENHFPVIYGIAVNIKTAEIYRASFQDRGPEEQLRAARTLAGGPMISIYDAETEQLRIGPYSWTPFPHVDFWLHQDDKQILENLSTSPLAEPPHFVEHIRSTLMFLKKHPSPAHTLFSGNKALLYKKNEDGLWEKISSPGS | Function: N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by NTAN1/PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position, nor on acetylated N-terminal peptidyl Asn.
Catalytic Activity: H(+) + H2O + N-terminal L-asparaginyl-[protein] = N-terminal L-aspartyl-[protein] + NH4(+)
Sequence Mass (Da): 34677
Sequence Length: 310
Subcellular Location: Cytoplasm
EC: 3.5.1.121
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Q64311 | MPLLVDGQRVRLPRSAVELVRAHPPLEERARLLRGQSVQQVGPQGLLYVQQRELAVTSPKDGSISILGSDDATTCHIVVLRHTGNGATCLTHCDGSDTKAEVPLIMSSIKSFSEHAECGRLEVHLVGGFSDDRQLSQKLTHQLLSEFDKQDDDIHLVTLCVTELNDREENENHFPIIYGIAVNIKTAEIYRASFQDRGPEEQLRAARALAGGPMISIYDAKTEQLRIGPCSWTPFPQVDFWLQQDDKQILESLSTSPLAEPPHFVEHIRSTLMFLKKFPSPENILFPGNKALLYKKNKDGLWEKISSPGS | Function: N-terminal asparagine deamidase that mediates deamidation of N-terminal asparagine residues to aspartate. Required for the ubiquitin-dependent turnover of intracellular proteins that initiate with Met-Asn. These proteins are acetylated on the retained initiator methionine and can subsequently be modified by the removal of N-acetyl methionine by acylaminoacid hydrolase (AAH). Conversion of the resulting N-terminal asparagine to aspartate by NTAN1/PNAD renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. This enzyme does not act on substrates with internal or C-terminal asparagines and does not act on glutamine residues in any position.
Catalytic Activity: H(+) + H2O + N-terminal L-asparaginyl-[protein] = N-terminal L-aspartyl-[protein] + NH4(+)
Sequence Mass (Da): 34595
Sequence Length: 310
Subcellular Location: Cytoplasm
EC: 3.5.1.121
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Q9BV86 | MTSEVIEDEKQFYSKAKTYWKQIPPTVDGMLGGYGHISSIDINSSRKFLQRFLREGPNKTGTSCALDCGAGIGRITKRLLLPLFREVDMVDITEDFLVQAKTYLGEEGKRVRNYFCCGLQDFTPEPDSYDVIWIQWVIGHLTDQHLAEFLRRCKGSLRPNGIIVIKDNMAQEGVILDDVDSSVCRDLDVVRRIICSAGLSLLAEERQENLPDEIYHVYSFALR | Function: Distributive alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Gly/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of the exposed alpha-amino group of the Ala, Gly or Ser residue in the [Ala/Gly/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif. Some of the substrates may be primed by NTMT2-mediated monomethylation . Catalyzes the trimethylation of the N-terminal Gly in CENPA (after removal of Met-1). Responsible for the N-terminal methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET. Required during mitosis for normal bipolar spindle formation and chromosome segregation via its action on RCC1.
Catalytic Activity: N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 25387
Sequence Length: 223
Subcellular Location: Nucleus
EC: 2.1.1.244
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Q8R2U4 | MTSEVIEDEKQFYSKAKTYWKQIPPTVDGMLGGYGHISNIDLNSSRKFLQRFLREGPNKTGTSCALDCGAGIGRITKRLLLPLFRVVDMVDVTEDFLAKAKTYLGEEGKRVRNYFCCGLQDFSPEPGSYDVIWIQWVIGHLTDQHLAEFLRRCKRGLRPNGIIVIKDNMAQEGVILDDVDSSVCRDLEVVRRIIRTAGLSLLAEERQENLPDEIYHVYSFALR | Function: Distributive alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Gly/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of the exposed alpha-amino group of the Ala, Gly or Ser residue in the [Ala/Gly/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif . Some of the substrates may be primed by NTMT2-mediated monomethylation. Catalyzes the trimethylation of the N-terminal Gly in CENPA (after removal of Met-1) (By similarity). Responsible for the N-terminal methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET. Required during mitosis for normal bipolar spindle formation and chromosome segregation via its action on RCC1 .
Catalytic Activity: N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 25420
Sequence Length: 223
Subcellular Location: Nucleus
EC: 2.1.1.244
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B8JM82 | MEFSGTHQAFRNRWAKTDDEMCKHSMSFHLHKTLRKEFFASYLYLLEQIPLVKLYALTCEYIKGEKQFYYRAQNFYKDVPPSEEGMMGDFVEISDIDLEGSRQFLKKFVGPGKAGTKCALDCGCGIGRVSKGVLFPVFESMEMLDMMEEFILHAHECYLGDYADRVESYYLYNLQEFIPPRKKYDVIWMQWVACHLTDKDLMEFLMRAKESLRPNGVIIIKDNMARQGCKLDPIDSSIIRHLDIMNGIIQRAGLNILDVEKQEGFPEAIVPVWMIAMR | Function: Alpha N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes monomethylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and Pro in the Pro-Pro-Lys motif. Predominantly functions as a mono-methyltransferase but is also able to di-/tri-methylate the GPKRIA peptide and di-methylate the PPKRIA peptide (in vitro). May activate NTMT1 by priming its substrates for trimethylation.
Catalytic Activity: N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N-terminal N-methyl-L-alanyl-L-prolyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32383
Sequence Length: 278
Subcellular Location: Nucleus
EC: 2.1.1.299
|
Q5VVY1 | MAHRGAHFAFRSRWQKTDDELCRHSMSFILHKAIRNDFFQSYLYLLEKIPLVKLYALTSQVINGEMQFYARAKLFYQEVPATEEGMMGNFIELSSPDIQASQKFLRKFVGGPGRAGTDCALDCGSGIGRVSKHVLLPVFNSVELVDMMESFLLEAQNYLQVKGDKVESYHCYSLQEFTPPFRRYDVIWIQWVSGHLTDKDLLAFLSRCRDGLKENGIIILKDNVAREGCILDLSDSSVTRDMDILRSLIRKSGLVVLGQEKQDGFPEQCIPVWMFALHSDRHS | Function: Alpha N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes monomethylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and Pro in the Pro-Pro-Lys motif . Predominantly functions as a mono-methyltransferase but is also able to di-/tri-methylate the GPKRIA peptide and di-methylate the PPKRIA peptide (in vitro) . May activate NTMT1 by priming its substrates for trimethylation .
Catalytic Activity: N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N-terminal N-methyl-L-alanyl-L-prolyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32400
Sequence Length: 283
Subcellular Location: Nucleus
EC: 2.1.1.299
|
B2RXM4 | MAHLGAHFAFRSRWQKTDDELCRHSMSFILHKAIRNDFFQSYLYLLEKIPLVKLYALTSQVIDGEMQFYARAKLFYQEVPATEEGMMGNFIELSNPDIQASREFLRKFVGGPGRAGTGCALDCGSGIGRVSKHVLLPVFSSVELVDMMESFLLEAQSYLQVNEDKVESYHCYSLQEFTPHLGRYDVIWIQWVSGYLTDKDLLAFLSRCRDGLKENGVIILKDNVAREGCIFDLSDSSVTRDMDILRSLIRKSGLVVLGQEKQEGFPEQCVPVWMFALHSDRHS | Function: Alpha N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes monomethylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and Pro in the Pro-Pro-Lys motif. Predominantly functions as a mono-methyltransferase but is also able to di-/tri-methylate the GPKRIA peptide and di-methylate the PPKRIA peptide (in vitro). May activate NTMT1 by priming its substrates for trimethylation.
Catalytic Activity: N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + S-adenosyl-L-methionine = H(+) + N-terminal N-methyl-L-alanyl-L-prolyl-L-lysyl-[protein] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 32313
Sequence Length: 283
Subcellular Location: Nucleus
EC: 2.1.1.299
|
Q5PP70 | MDICGVDSEGKEFNSVQEMWREEIGEGDETKKTQWYRDGVSYWEGVEASVDGVLGGYGHVNDADIIGSEVFLKTLLQERLVNNVGANQHLVALDCGSGIGRITKNLLIRYFNEVDLLEPVAQFLDAARENLASAGSETHKATNFFCVPLQEFTPAAGRYDVIWVQWCIGHLTDNDFVSFFNRAKGYLKPGGFFVVKENLAKNGFVLDKEDHSITRSDPYFKQLFRQCGLHLYRTKDQKGLPQELFAVKMYALTVDTPPKIHRTRSKTRSNRPQIIK | Function: Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif (By similarity).
Catalytic Activity: N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 31247
Sequence Length: 276
EC: 2.1.1.244
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Q9N4D9 | MSSSSSSRIHNGEDVYEKAEEYWSRASQDVNGMLGGFEALHAPDISASKRFIEGLKKKNLFGYFDYALDCGAGIGRVTKHLLMPFFSKVDMEDVVEELITKSDQYIGKHPRIGDKFVEGLQTFAPPERRYDLIWIQWVSGHLVDEDLVDFFKRCAKGLKPGGCIVLKDNVTNHEKRLFDDDDHSWTRTEPELLKAFADSQLDMVSKALQTGFPKEIYPVKMYALKPQHTGFTNN | Function: Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif.
Catalytic Activity: N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 26632
Sequence Length: 234
EC: 2.1.1.244
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Q55DH6 | MTIKNEEQQQQTNKLKYPKNLLSSGLDGEGNTYINIEDLWKKELEGKDNKMEDKWYKSADEYWKGVEATVDGMLGGLAQVSPIDVVASKVFIQDFIKGTDSRPPINLNLALDCGAGIGRVAKEFLLPIGFKNVDLVEQNKLFLDKAKSDNFKDDNRVENYYAVGLQDFTFEKKYDCIWIQWVIGHLHDLDFIEFLKKCMDSLTPNGIICIKDNCAKKRFIMDKEDNSVSRTEDHLKYLFDQAGCKLLKSMVQPNFPKELFPVLMFALERK | Function: Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif (By similarity).
Catalytic Activity: N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 31043
Sequence Length: 270
EC: 2.1.1.244
|
Q6NN40 | MTTTLEEQLSDKLQMMDETTDKVQGSSKQKDDSSIAASSDAKTASPSSSDSSTKVAAPESEFYNKAQKYWSEVPATVNGMLGGLGYISAIDIQGSNVFLREIRVPGNRLALDCGAGIGRVTRNLLIPRFSCVDLVEQDPAFADKAREYCTSEDGSRGKVGQIYNVGLQKFTPTQQYDLVWTQWVLGHLTDRDLVSFFRRIKQGLAPGAFLCLKENVSSSKKTVEDRNDSSVTRPLDSYEHFLKEAGFRIVRKVKQQNFPKGLFPVYMIACKPVSKE | Function: Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif (By similarity).
Catalytic Activity: N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 30602
Sequence Length: 276
EC: 2.1.1.244
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Q10CT5 | MDSRGFDSEGREFSSATEMWAHEIGAAADAPVSAAVAEPAPAPAAGSNGVAGEEEAGGGGKREEWYSKAIAYWQGVEASTEGVLGGYGCVNDVDVKGSDAFLRPLLAERFGAARRHLVALDCGSGIGRVTKNFLLRHFNEVDLVEPVSHFLEAAQENLTECMEVGEDTHKAANFYCVPLQDFTPDEGRYDVIWIQWCIGQLPDDDFISFFNRAKIGLKPNGFFVLKENIARNGFVLDKEDNSITRSDAYFKELFKKCGLYIHSIKDQSDLPKELFAVKMYALVTEKPKIQKNGKRRRPKNSPRMIRS | Function: Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif (By similarity).
Catalytic Activity: N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 33966
Sequence Length: 307
EC: 2.1.1.244
|
O13748 | MDPEKFYSDAIDYWNGVQPTVDGMLGGLGTGRIPQTDVVGSRTFLNRLNYRIGKIENLVAADCGAGIGRVTENVLLKIASHVDLVEPVENFISTAKKQLATKPCSFINVGLQNWTPEKNRYGLIWNQWCLSHLTDEDLIAYLSRCCEAIQEKGVICVKENVSSFEDTFDPIDSSVTRCEQSLKSLFKKANLVVVAETLQHGFPEELFPVKMYALVPHSS | Function: Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif (By similarity).
Catalytic Activity: N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 24388
Sequence Length: 219
Subcellular Location: Cytoplasm
EC: 2.1.1.244
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P38340 | MDVPADSHIKYEDAIDYWTDVDATVDGVLGGYGEGTVVPTMDVLGSNNFLRKLKSRMLPQENNVKYAVDIGAGIGRVSKTMLHKHAAKIDLVEPVKPFIEQMHVELAELKDKGQIGQIYEVGMQDWTPDAGKYWLIWCQWCVGHLPDAELVAFLKRCIVGLQPNGTIVVKENNTPTDTDDFDETDSSVTRSDAKFRQIFEEAGLKLIASERQRGLPRELYPVRMYALKPMPN | Function: Alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif. Responsible for the N-terminal methylation of the ribosomal proteins RPL12A, RPL12B, RPS25A and RPS25B.
Catalytic Activity: N-terminal L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N-terminal N,N,N-trimethyl-L-alanyl-L-prolyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 26068
Sequence Length: 232
Subcellular Location: Cytoplasm
EC: 2.1.1.244
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Q7NH22 | MTVRLLLASASPRRRELLSQIGVAFEVKPSAFEERMDPALPPEQLVVQNALGKALNVQKRAPAELILGADTVVVFNRRIYGKPTGPADAGRMLGELQGQWHTVYTGIALVEERRWRVAERATRVKLRAMTPAQIAAYVAGGEPLDKAGSYAIQGLGAALVEQIDGCYSNVVGLSLPLLVDLLAEFDRRVF | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 20692
Sequence Length: 190
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q5FS71 | MTASPSSAEGSSGLPDRPKLVLASASPRRLSLLEQIGIVPDAVVSADIDEEPRPGELPRPLAQRLARQKAEHVAAQRTDAALVLGADTVVSVGRRVLPKAEDEKTARACLKLLSGRRHKVLTAVVLRPSAGWPQGTPCERLVETSVIFHRLTDAQIDALIAQGDWQGKAGGYAIQGAAAAHIRQIGGSYSAVVGLPLFETAQLLRGQPVGKPSGGWIA | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 22919
Sequence Length: 218
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q0BTC5 | MMPDQPATACPLVLASASPRRAALLAQIGVIPALTLATDIDETPLKGEVPLKGEVPRLLSRRLAQGKADTAIRVLREQSDAPLAAPFILAADTVVAVGRRALPKAETEAEARQCLTLLSGRRHHVWTTVVVIAPDGKRAERIVESAVTFNRMTDLQQEAYIASGEWRGKAGGYAIQGLAAAYIRFLSGSYSNVVGLPLFETAQLLRGLGFRSL | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 22807
Sequence Length: 213
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q2SBH1 | MFDGNPGRRRLVLASGSPRRREMIAGLGCEFSIASADIDESVRPSEAAADYVERLAKEKATAVFEARGDQQDIVVLGADTTVVAGGDILGKPVDFDDAKAMLRRLSGTWHEVLTSVALVAAEGCKVTTTLSRVRFRELSEQEIQRYWDSGEPADKAGAYGIQGLAGSFVERVEGSYSSIVGLPLCETVVLLKEFGIKIWSD | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 21715
Sequence Length: 201
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q9K8H3 | MKPLILASGSPRRKQLLEQMNVPFTVCKSTIDETFDPTFPPDEVVQQLARQKAQDVAKKHEDSFILAADTIVVFQGRILGKPATEQEARQMLSQLSDQSHEVLTGVALLHQGQVETFVETTEVRFWPLTDTEIETYLQTGEPFDKAGAYGIQGLGAYLVKELKGDYYNVVGLPLSRTVRALKVHGFSTRF | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 21240
Sequence Length: 190
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q31FH4 | MKRRLYLSSSSPRRKELLDQAGIPFDLVNAPVEETGLPNESPESFVLRMAVEKALSGFNKVPGKNVWVLGSDTIILKDGKVFGKPKHKMDAYRMLMSFSGEEHTVMTSIAIVNDGAVYSDVCQTNVFFRPISDSEFEQYWATGEAEDKAGAYGIQGQAAKFIEKIEGSYSAVMGLPLYELDKLLRESNFYSE | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 21408
Sequence Length: 192
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q0C2H1 | MPGSAPLILASASPRRLELLAQIGIVPDRVAPTDIDETRRKAESPRELALRLAREKAAACDAEGAFVLAADTVVALGQRNLEKAADETEAADFLRLLSGRAHQCITGVAVRAPSGQIVSRAVLARVKMKRLTEAEIAAYVASGDWKGKAGGYGIQGAAGGFVTAINGSYTAIVGLPLYETKSLLEGLGYRR | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 20071
Sequence Length: 191
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q5QWE2 | MRLLLASSSPRRRELLTLLHRPFDCEVPEVEELRGANENAGDYVTRLAEEKAQTVAQRQQTPCLVIGSDTLISFKGQVLEKPESYEHFSQMMKQLSGQTHQVLTSVSVCQWNGHKVVARETALVTTQVEFAALSQGEIDAYWATGEPHDKAAGYGIQGYGGKFVKRIEGSYFAVVGLPLYETEQLLRMFEMTGEVDER | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 22184
Sequence Length: 198
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q1IV55 | MLRYNLGMGLILASASPRRSELLRKARMVFRVEPAHVPEVHTAGEDPKQYAQRLARDKARAVAAKYPNDFVIGADTIVVADAHVLEKPADEADAARMIRMLSGHTHEVTTGVCLCGPNVEIVETETTRVTVAEISDEEIADYIHTGEPMDKAGAYGIQGMFSRWVTGIEGDYFNVVGLPIARVYRMMRRAGVL | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 21268
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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A9KHL6 | MYQIVLASGSPRRKEILSQVGINFTVCVSNMEEITSETLPENIVMELSKMKAHDIAKQYETNTIIIGSDTIVAYKNQILGKPKNEDHAKEMLQLLSGVTHEVYTGVTVIIKNDSGEVEERTFFEISKVTVSDLTEEEIMDYIKSKEPMDKAGAYAVQGRFAAHVTRIEGDYYTIVGLPIARLYQEVKKFGIDLVKQM | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 22171
Sequence Length: 197
Subcellular Location: Cytoplasm
EC: 3.6.1.9
|
Q38YR2 | MFILASQSPRRQALLKRVVNDFEVQPAQIDEHETPLTAPGDYVQTLAQRKGEAVAVQYPTATILAADTAISFQGTLYGKPKDRQDAYEMLRQLSGQTHQVYTGLWLMKDGLVQQKVVQTDVTFWHLSTAEIEQYLDQNEYADKAGAYGIQGAGALLINKVNGDFYNVVGLPVSTVARMLQN | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 20092
Sequence Length: 181
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q1MQH1 | MTQQRVSSVFIETVPIVLASASPRRRSLLEQLGLLFKIVSVDSEPLPLSSEHPLEYVIRAAKVKAFAAAALEPRSVIIAADTVVIYTKDDVFEIIGKPQSGNDSFSMLSRFQGGKHQVITGCCIVWPLEENITSVQYEIFYDTASIQFGQWDKDILSSYVSTGESNDKAGAFSIQGIGAFLIDIIEGNYTTILGLPLPQLVKRLLKRKAIKVVLNKNSEETISSDFLTYSR | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 25506
Sequence Length: 231
Subcellular Location: Cytoplasm
EC: 3.6.1.9
|
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