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stringlengths 6
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I3R635 | MGLVKMTRWRTLVLATAAFNLSFLIWFSFAPFTGQIAAEFGLSLTDLGILASAAIWSAPPGRILTGWLSDRFGASTVFGIVLAYVGIFSMASAFATSYEVFFVERVVVASAGITFVVGIQHVSQWFPEEELGTAEGIYAGIGNAGAAGGALILPRAFGNWSGPLFSTGWRAAFFYTGVVAILMAIVYVVFGQDAATKARAAATSESATLSTWVHTATRYGVVALALGYVMSFGLEISMNGWLPTYFREGFGSNLVIASTFAATFSLAAGLLRPIGGYVSDRLVRDQRDILPFFAGRYREQWTVLCMTFIVVSMTGLTFAGQTGNVLLTVAAGFLVGMSCAFTEGAIFAQVPAMFPNRSGAAAGIVGGIGTFGGIGFPLVYSFAAAEGMIHTGYVIVAALMIPILALNAFISRPHIASRAHVDGFFDGSRFESSQSDD | Function: Is likely responsible for nitrate uptake in the nitrate assimilation pathway.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46239
Sequence Length: 437
Subcellular Location: Cell membrane
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P42434 | MTERLLRYFRDKQQDVQSEKTYDTQCPFCSMQCKMQLVEQTIVTRKKYTAIGIDNPTTQGRLCIKGMNAHQHALNSSRITRPLLKKNGEFMPVSWEEALNHIKDQVTMIQTEHGHDAMAVYGSASITNEEAYLLGKFARVGLQTKYIDYNGRLCMSAAATAANQTFGADRGLTNPLSDIPHTRVIILAGTNIAECQPTIMPYFEKAKENGAYFIAIDPRETATTKIADLHLKIKPGTDAALANGLVKIIIDEQLINEDFIQSRTNGFEELKQHTDSLDLNDIAEQTSVSLVDIRKAAVKFAKETSGMLFTARGIEQQTDGTAAVKGFLNMVLITGKIGKPYSGYGAITGQGNGQGAREHGQKADQLPGYRSIENEEHRAHIAKVWGIHQDELPRKGVSAYEMMEKINDGDIKGLFLMCSNPAVSSPNANLVKKALRRLTFFVAIDLFISETAKYADVILPASSYLEDEGTMTNVEGRVTLREASRPCPGEAKHDWQIICDLASALGKGRYFSYTSAEDIFNELREASRGGIADYSGISYGRLRREGGIHWPCPESDHPGTGRLFTESFAHPDQKAALSVIPNEPPVPKEKPTADYPLYLTTGRVMSHYLTGVQTRKSAALAARHFESFMEIHPQTAATYNIEDRVLVKIESPRGSITVRSKLSEQIRKDTVFVPIHWADAQNVNDLIGEALDPACKMPGFKVCAVRIIPI | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria.
Sequence Mass (Da): 78622
Sequence Length: 710
Pathway: Nitrogen metabolism; nitrate reduction (denitrification); dinitrogen from nitrate: step 1/4.
EC: 1.7.-.-
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I3R636 | MAEQSSRNLDTGRAGIILAGGRSRRFDGIDKATAPVGGRPMIHRVAASLDPAVDELVINCRADQRDTFAAALSDFDVRFAEDSHPDHGPVFGLRTAVRASNAEYAAILPCDMPLVPTGFISHLFGRVQGGTGVIPSVSETPVPLPSVVHCRAGEVACTETIRAGSDRLKDVMSTLGVNVLDGREVQAHAGLDAFSNVNTIDDLRALSSRR | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 22257
Sequence Length: 210
Domain: The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein.
Subcellular Location: Cytoplasm
EC: 2.7.7.77
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P42435 | MGKKQLVLVGNGMAGVRAIEEILSVAKDEFQITIFGAEPHPNYNRILLSKVLQGDTDIKDITLNDWDWYEENNIQLYTNETVIKVDTENKTVITDADRIQPYDELILATGSVPFILPIPGADKKGVTAFRDIKDTDTMLAASKQYKKAAVIGGGLLGLEAARGLLNLGMDVSVIHLAPFLMERQLDATAGRLLQNELEKQGMTFLLEKQTEEIVGDDRVEGLRFKDGTSIEADLVVMAVGIRPNTTLGAESGIPVNRGIIVNDYMQTEIPHIYAVGECAEHRGIAYGLVAPLYEQAKVLAKHMCGIETKPYEGSVLSTQLKVSGVEVFSAGDFNESEEKKAIKVFDEQDGIYKKIVLRGNQIVGAVLFGDSSEGNRLFSMIQKEADISETSKISILQPLSQEAGTSITAAMSDDEIICGCNGVSKGAIIQAIQEKGCSSTDEIKACTGASRSCGGCKPLVEEILQHTLGSDFDASAQKEAICGCTTLSRDEVVEEIKAKGLSHTREVMNVLGWKTPEGCSKCRPALNYYLGMINPTKYEDDRTSRFVNERMHANIQKDGTYSVVPRMYGGVTNSTDLRKIADVVDKYEIPLVKMTGGQRIDLIGVKKEDLPKVWEDLDMPSGYAYGKTLRTVKTCVGEQFCRFGTQDSMALGIALEKKFEGLNTPHKVKMAVSACPRNCAESGIKDLGVVGIDGGWELYVGGNGGTHLRAGDLLMKVKTNEEVLEYAGAYLQYYRETANYLERTSAWLERVGLSHVQSVLNDPEKRQELNGRMNETLSVHKDPWKDFLEDKQTSKELFENVVTTS | Cofactor: Binds 1 siroheme per subunit.
Function: Required for nitrite assimilation.
Catalytic Activity: 2 H2O + 3 NADP(+) + NH4(+) = 5 H(+) + 3 NADPH + nitrite
Sequence Mass (Da): 88432
Sequence Length: 805
Pathway: Nitrogen metabolism; nitrate reduction (assimilation).
EC: 1.7.1.4
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I3R637 | MASKKEQWKSDLYGDAVRDELEAFAEEGFESIPEDERDKWFTRFKFWGVFQQRTGQESYFMMRLTNANGVLEPGQLRTIAEVARDYATGPVDNPEFGNGWVDLTTRQSIQLHWLELEDIPEIWEQLESVGVTSRSAGGDTMRNITGCPVAGKDTHELVESKPLLDRFQSELREDDALSNMPRKFNISVTGCREGCAQDSINDIGLEPARKEVDGEVITGFNVRVGGGLGSRKPRVARSLDVFVADEERAYEVVRGFVELYHDHGNRDVRARARSRFFVDDWGTEKIRDRLESEYLDFELQSAGEDIRDEYTYNAGRPQSAGKSDHVGVHEQSDGRYYVGLSVAVGRLTAADALELADLADKYGSGKIRLTRRQNPIVMDVPAGALDDLLAEPLLSKHTPEPNPFQRGTVACTGTEFCSLALTETKARTARMLRWLRDNVEVPDDVHQLKIHYSGCTADCGQANTADIGLFGMRAQKDGEMVEAMDIGVGGGIGDEPSFVEWIHQRVPADEVPGAIASLVEAFAAHRTAGQTFRQWVEAEGPDAVAEYCEPIETDFEAPYMHDAKQSWYPFADEDEPPKTEQPMTSD | Cofactor: Binds 1 siroheme per subunit.
Function: Catalyzes the reduction of nitrite to ammonium in the nitrate assimilation pathway, using ferredoxin as the electron donor. Can use reduced methyl viologen but neither NADPH nor NADH as electron donors.
Catalytic Activity: 2 H2O + NH4(+) + 6 oxidized [2Fe-2S]-[ferredoxin] = 8 H(+) + nitrite + 6 reduced [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 65438
Sequence Length: 586
Pathway: Nitrogen metabolism; nitrate reduction (assimilation).
EC: 1.7.7.1
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P39459 | MKPLIQVQGVSQRFSTASGEFLALQNVSFDIYEGETISLIGHSGCGKSTLLNLIAGIALPTEGGLLCDNREIAGPGPERAVVFQNHSLLPWLTCFDNVALAVDQVFRRSMSKGERKEWIEHNLERVQMGHALHKRPGEISGGMKQRVGIARALAMKPKVLLLDEPFGALDALTRAHLQDAVMQIQQSLNTTIVMITHDVDEAVLLSDRVLMMTNGPAATVGEILDVNLPRPRNRVQLADDSRYHHLRQQILHFLYEKQPKAA | Function: Probably part of a high-affinity binding-protein-dependent transport system for nitrate. Probably responsible for energy coupling to the transport system.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28996
Sequence Length: 262
Subcellular Location: Cell membrane
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P42436 | MVNKDVTKVCIGKIEELPEQLGKTVYIEDKELAVFKLSDGSIRAIENRCPHKGGVLAEGIVSGQYVFCPMHDWKISLEDGIVQEPDHGCVKTYETLIEGEHVYLVY | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Required for nitrite assimilation. Required for activity of the reductase (By similarity).
Catalytic Activity: 2 H2O + 3 NADP(+) + NH4(+) = 5 H(+) + 3 NADPH + nitrite
Sequence Mass (Da): 11895
Sequence Length: 106
Subcellular Location: Cytoplasm
EC: 1.7.1.4
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A0A0H3JXA8 | MNNFNNEIKLILQQYLEKFEAHYERVLQDDQYIEALETLMDDYSEFILNPIYEQQFNAWRDVEEKAQLIKSLQYITAQCVKQVEVIRARRLLDGQASTTGYFDNIEHCIDEEFGQCSITSNDKLLLVGSGAYPMTLIQVAKETGASVIGIDIDPQAVDLGRRIVNVLAPNEDITITDQKVSELKDIKDVTHIIFSSTIPLKYSILEELYDLTNENVVVAMRFGDGIKAIFNYPSQETAEDKWQCVNKHMRPQQIFDIALYKKAAIKVGITDV | Function: Catalyzes the nucleophilic attack of one alpha-aminobutanoate moiety from SAM onto D-histidine to produce the intermediate (2S)-2-amino-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate. Functions in the biosynthesis of the metallophore staphylopine, which is involved in the acquisition of nickel, cobalt, zinc, copper, and iron, and thus enables bacterial growth inside the host, where metal access is limited. Therefore, this enzyme probably contributes to staphylococcal virulence . Appears to be specific for D-histidine as substrate .
Catalytic Activity: D-histidine + S-adenosyl-L-methionine = (2S)-2-amino-4-{[(1R)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 31126
Sequence Length: 272
EC: 2.5.1.152
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A0A0H2ZHV3 | MQGRTPLLETLRELECEIRLLTVYARECCGCYEILRRKLDRLSGLIGEDCSRAQWQADSDDPALQALGLRLRDAAVQALCELEKHLCQGVLHEPGEMGRYLGSLLESIRGELDSAGIDADARVLFVGSGALPTSALVLAREVGAHLCCLDIDEEALGYAREIARCQGLEARMQFSSLPPAELAFSRDATHFLIASLVQQKSAVLAQIRQVMRADAKVLLRHGSGIKGLFNYPVEPAELEGWQVCAERVSQPLYDTLILEKAGR | Function: Catalyzes the nucleophilic attack of one alpha-aminobutanoate moiety from SAM onto L-histidine to produce the intermediate (2S)-2-amino-4-{[(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate. Functions in the biosynthesis of the metallophore pseudopaline, which is involved in the acquisition of nickel and zinc, and thus enables bacterial growth inside the host, where metal access is limited. Therefore, this enzyme probably contributes to Pseudomonas virulence. Cannot use D-histidine in place of L-histidine as substrate.
Catalytic Activity: L-histidine + S-adenosyl-L-methionine = (2S)-2-amino-4-{[(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 28932
Sequence Length: 263
EC: 2.5.1.-
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Q8D035 | MYTLMKADVLAQLAGLQQEISQLHDNAQQNQSHFVLLERRFSRLQSFNDEPQLQDYRLQLEHDDAVVKQIAQLRQVANAALCDYEKHQVCALCSPSSKTDDYLTSFNQSLQQEIKLAGMQMGEKVLLVGSGALPTTALVLVAKLGATVFCYDHDPAAQQLARQLVQSLGLEKQVQFIDNLKELTDRPVDHIIVASLVADKQALLAQLVPYVTRSSKLVMRYGNGLKSIFNCPYCHEVNCSHWRTASKPVTTGLYDLIILEPNHHA | Function: Catalyzes the nucleophilic attack of one alpha-aminobutanoate moiety from SAM onto L-histidine to produce the intermediate (2S)-2-amino-4-{[(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate. Functions in the biosynthesis of the metallophore yersinopine, which is involved in metal acquisition and thus enables bacterial growth inside the host, where metal access is limited. Therefore, this enzyme probably contributes to Yersinia virulence.
Catalytic Activity: L-histidine + S-adenosyl-L-methionine = (2S)-2-amino-4-{[(1S)-1-carboxy-2-(1H-imidazol-4-yl)ethyl]amino}butanoate + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 29686
Sequence Length: 265
EC: 2.5.1.-
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Q9DE07 | MWKLVPAAGPGEPFRLLVGTEYVVGRKNCAFLIQDDQSISRSHAVLTVSRPETTHSQSVSVPVLTIKDTSKYGTFVNGSKLSGASRSLQSGDRVNFGVFESKFRVEYESLVVCSSCLDVAQKTALNEAIQQLGGLVVNEWTKECTHLIMESVKVTVKTICALICGRPIVKPEFFSELMKAVQSRQQLPTPESFYPSVDEPAIGIDNMDLSGHPERKKIFSGKTFVFLTAKQHKKLGPAVILGGGEAKLMAEERKETSLLVSPEVCVVDVGVTNSQILGSESMRNWTDSILAVLESNNLRAIPEAEIGLAVIFMSTEIYCNPQRQPDNKAVTASTASKVRPVSSQSSTVDETIMPTAAADYSTLNVADTEIEEQTCMEIERTTSQTTRREKVAFQQAAVRENPSTSGTVNAGMLISRVNRTSGFGQKNHPHSPSKILEVDKPRECTPRQQSNSITNYFHVARKRERAEEGEETSLSKQAKLEKKPLPVSECTESSASSAWNSEKEQHGKGNNIQLGRESGELASDKTDIKITFSENPAPKKRKELDDVSEDVETLEMVFESRDLDWEEQTANGDQEAQSNKRKKRCLETKGSRTEEGNTKQREENEMLRKEEVGSVLTLEDKSKIKEESSVSIRNKLINHNKLEDDSSRLPSKLLLTEFRSLVVSCPRSNSPTMRNTKCRGQNNFKTFRKVPYPGAGQLPYIIGGSDLVAHQARKNSELEEWLREELEEQNRRAREESLADDLFRYDPNVKRRR | Function: Component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity . The complex is involved in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity, cell cycle checkpoint control and meiosis . The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11 (By similarity). RAD50 may be required to bind DNA ends and hold them in close proximity (By similarity). NBN modulate the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-PKcs to the DNA damage sites and activating their functions (By similarity). It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX (By similarity). NBN also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation (By similarity). NBN is a major player in the control of intra-S-phase checkpoint and there is some evidence that NBN is involved in G1 and G2 checkpoints (By similarity). The roles of NBS1/MRN encompass DNA damage sensor, signal transducer, and effector, which enable cells to maintain DNA integrity and genomic stability (By similarity). Forms a complex with RBBP8 to link DNA double-strand break sensing to resection (By similarity).
PTM: Phosphorylated by ATM in response of ionizing radiation, and such phosphorylation is responsible intra-S phase checkpoint control and telomere maintenance.
Sequence Mass (Da): 83987
Sequence Length: 753
Domain: The FHA and BRCT domains are likely to have a crucial role for both binding to histone H2AX and for relocalization of MRE11/RAD50 complex to the vicinity of DNA damage.
Subcellular Location: Nucleus
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Q5I2W8 | MWKLQPTESGGESVILLAGQEYVVGRKNCEILLTNDQSISRVHAVLTVTEQAVTLKDSSKYGTFVNGEKLESGSTKTLQTGYKITFGVFQSKFSLEKECIVVCSSCVDNEGKVTLSQDIRSVGGRLVSSWTSDCTHLVMPTVKVTIKTICALLCCRPIVKPAFFSALSKAVQQKLPLPKAERFRPQIDEPSLARDDVDLSARPERKSLFKGKTFLFLSSKQMKRLSVAVSCGGGVSQLLDEGALPVSLLESSSTCVLDMISGNSQPVISPASKKWLDSVGQILHRKGLRFITESEVGLAAIHVSNQTYCNPCSSLQSESVKTNPVFASATLSQSTAVDETALAAPSQNITAYVVNTEISQDQSRMVTSGISAVGETPEKTNPTQKASTTNKPLSLGQEPSSTRIVQETVMSSESFSVVESEQKMKKGSVVSARGRVEGPVKQKAPSSGNTTLKHSPQKQTALTSFFQPSSKKRPRESSASSVQPEPKFFKKDIKDNEDDIQQSFSVNRSHKTSSEETSLGQACGTGQNSSSKKRKEPEQDTLLGAEEPTAADDLEMSLEELEFLMSDEMDEPPQTAANKKQRLESGLTSKINSEQLSNQQEVTESKGRKGEKNQQSSSSNIQSMQLDRAGPAVTNQDTQTQSKRSPPDLEAHSSANKGPSKNKTPELEEVKKEEVSFVVNSRPQNGISQTSEAVLKQEMQASTSNSGPKNDPDLPRKLLQVQFMSLTVNNSSRSRPGPLQTHNPNDKNVKRFRKKNVPGFDGLPKIIGGSDLVAHNRSKHSELEEWLRQAAEEEKLNEREETLGDDLFRYNPRPAKKR | Function: Component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The complex is involved in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity, cell cycle checkpoint control and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity (By similarity).
Sequence Mass (Da): 89407
Sequence Length: 818
Domain: The EEXXXDDL motif at the C-terminus is required for the interaction with atm and its recruitment to sites of DNA damage and promote the phosphorylation of atm substrates, leading to the events of DNA damage response.
Subcellular Location: Nucleus
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O60934 | MWKLLPAAGPAGGEPYRLLTGVEYVVGRKNCAILIENDQSISRNHAVLTANFSVTNLSQTDEIPVLTLKDNSKYGTFVNEEKMQNGFSRTLKSGDGITFGVFGSKFRIEYEPLVACSSCLDVSGKTALNQAILQLGGFTVNNWTEECTHLVMVSVKVTIKTICALICGRPIVKPEYFTEFLKAVESKKQPPQIESFYPPLDEPSIGSKNVDLSGRQERKQIFKGKTFIFLNAKQHKKLSSAVVFGGGEARLITEENEEEHNFFLAPGTCVVDTGITNSQTLIPDCQKKWIQSIMDMLQRQGLRPIPEAEIGLAVIFMTTKNYCDPQGHPSTGLKTTTPGPSLSQGVSVDEKLMPSAPVNTTTYVADTESEQADTWDLSERPKEIKVSKMEQKFRMLSQDAPTVKESCKTSSNNNSMVSNTLAKMRIPNYQLSPTKLPSINKSKDRASQQQQTNSIRNYFQPSTKKRERDEENQEMSSCKSARIETSCSLLEQTQPATPSLWKNKEQHLSENEPVDTNSDNNLFTDTDLKSIVKNSASKSHAAEKLRSNKKREMDDVAIEDEVLEQLFKDTKPELEIDVKVQKQEEDVNVRKRPRMDIETNDTFSDEAVPESSKISQENEIGKKRELKEDSLWSAKEISNNDKLQDDSEMLPKKLLLTEFRSLVIKNSTSRNPSGINDDYGQLKNFKKFKKVTYPGAGKLPHIIGGSDLIAHHARKNTELEEWLRQEMEVQNQHAKEESLADDLFRYNPYLKRRR | Function: Component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. The complex is involved in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity, cell cycle checkpoint control and meiosis. The complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11. RAD50 may be required to bind DNA ends and hold them in close proximity. NBN modulate the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-PKcs to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. NBN also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. NBN is a major player in the control of intra-S-phase checkpoint and there is some evidence that NBN is involved in G1 and G2 checkpoints. The roles of NBS1/MRN encompass DNA damage sensor, signal transducer, and effector, which enable cells to maintain DNA integrity and genomic stability. Forms a complex with RBBP8 to link DNA double-strand break sensing to resection. Enhances AKT1 phosphorylation possibly by association with the mTORC2 complex.
PTM: Phosphorylated by ATM in response of ionizing radiation, and such phosphorylation is responsible intra-S phase checkpoint control and telomere maintenance.
Sequence Mass (Da): 84959
Sequence Length: 754
Domain: The FHA and BRCT domains are likely to have a crucial role for both binding to histone H2AX and for relocalization of MRE11/RAD50 complex to the vicinity of DNA damage.
Subcellular Location: Nucleus
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Q93NF6 | MGDTDLPCVTGVLLAAGAGKRLGRGPKALLPYRGRTLVEDAAETMLVGGCHEVVIVLGANAQAVCARANLEPYRIVVNHDWSSGMGSSYLAGDAAAHTKNHILVALVDQPGLSVTTVGRLLVSHRPGRISSAAYSSLDSPRVLRRGHPMVIDAGLRPAVASTVSGDAGARVFLRQKPWLVDLIDCSDESTGEDVDTVEQMYRLL | Function: Catalyzes the reduction of nicotine blue to its hydroquinone form. Nicotine blue is the name given to the compound formed by the autocatalytic condensation of two molecules of 2,3,6-trihydroxypyridine, an intermediate in the nicotine degradation pathway. May play a role in preventing the intracellular formation of nicotine blue semiquinone radicals, which by redox cycling would lead to the formation of toxic reactive oxygen species. Besides nicotine blue, several other quinones are reduced by nboR.
Catalytic Activity: 3,3'-bipyridine-2,2',5,5',6,6'-hexol + NADP(+) = (E)-2,2',5,5'-tetrahydroxy-6H,6'H-(3,3'-bipyridinylidene)-6,6'-dione + 3 H(+) + NADPH
Sequence Mass (Da): 21537
Sequence Length: 204
Pathway: Alkaloid degradation; nicotine degradation.
EC: 1.1.1.328
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P03416 | MSFVPGQENAGGRSSSVNRAGNGILKKTTWADQTERGPNNQNRGRRNQPKQTATTQPNSGSVVPHYSWFSGITQFQKGKEFQFAEGQGVPIANGIPASEQKGYWYRHNRRSFKTPDGQQKQLLPRWYFYYLGTGPHAGASYGDSIEGVFWVANSQADTNTRSDIVERDPSSHEAIPTRFAPGTVLPQGFYVEGSGRSAPASRSGSRSQSRGPNNRARSSSNQRQPASTVKPDMAEEIAALVLAKLGKDAGQPKQVTKQSAKEVRQKILNKPRQKRTPNKQCPVQQCFGKRGPNQNFGGSEMLKLGTSDPQFPILAELAPTVGAFFFGSKLELVKKNSGGADEPTKDVYELQYSGAVRFDSTLPGFETIMKVLNENLNAYQKDGGADVVSPKPQRKGRRQAQEKKDEVDNVSVAKPKSSVQRNVSRELTPEDRSLLAQILDDGVVPDGLEDDSNV | Function: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication.
PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion during infection.
Sequence Mass (Da): 49729
Sequence Length: 454
Subcellular Location: Virion
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P04134 | MANQGQRVSWGDESTKTRGRSNSRGRKNNNIPLSFFNPITLQQGSKFWNLCPRDFVPKGIGNRDQQIGYWNRQTRYRMVKGQRKELPERWFFYYLGTGPHADAKFKDKLDGVVWVAKDGAMNKPTTLGSRGANNESKALKFDGKVPGEFQLEVNQSRDNSRSRSQSRSRSRNRSQSRGRQQFNNKKDDSVEQAVLAALKKLGVDTEKQQQRSRSKSKERSNSKTRDTTPKNENKHTWKRTAGKGDVTRFYGARSSSANFGDTDLVANGSSAKHYPQLAECVPSVSSILFGSYWTSKEDGDQIEVTFTHKYHLPKDDPKTGQFLQQINAYARPSEVAKEQRKRKSRSKSAERSEQDVVPDALIENYTDVFDDTQVEIIDEVTN | Function: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication.
PTM: ADP-ribosylated. The ADP-ribosylation is retained in the virion during infection.
Sequence Mass (Da): 43521
Sequence Length: 382
Subcellular Location: Virion
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P04665 | MSNMDIDSINTGTIDKTPEELTPGTSGATRPIIKPATLAPPSNKRTRNPSPERTTTSSETDIGRKIQKKQTPTEIKKSVYKMVVKLGEFYNQMMVKAGLNDDMERNLIQNAQAVERILLAATDDKKTEYQKKRNARDVKEGKEEIDHNKTGGTFYKMVRDDKTIYFSPIKITFLKEEVKTMYKTTMGSDGFSGLNHIMIGHSQMNDVCFQRSKGLKRVGLDPSLISTFAGSTLPRRSGTTGVAIKGGGTLVDEAIRFIGRAMADRGLLRDIKAKTAYEKILLNLKNKCSAPQQKALVDQVIGSRNPGIADIEDLTLLARSMVVVRPSVASKVVLPISIYAKIPQLGFNTEEYSMVGYEAMALYNMATPVSILRMGDDAKDKSQLFFMSCFGAAYEDLRVLSALTGTEFKPRSALKCKGFHVPAKEQVEGMGAALMSIKLQFWAPMTRSGGNEVSGEGGSGQISCSPVFAVERPIALSKQAVRRMLSMNVEGRDADVKGNLLKMMNDSMAKKTSGNAFIGKKMFQISDKNKVNPIEIPIKQTIPNFFFGRDTAEDYDDLDY | Function: Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.
PTM: Late in virus-infected cells, may be cleaved from a 56-kDa protein to a 53-kDa protein by a cellular caspase. This cleavage might be a marker for the onset of apoptosis in infected cells or have a specific function in virus host interaction.
Sequence Mass (Da): 61770
Sequence Length: 560
Subcellular Location: Virion
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Q6I7C0 | MSDRRQNRKTPDEQRKANALIINENIEAYIAICKEVGLNGDEMLILENGIAIEKAIRICCDGKYQEKREKKAREAQRADSNFNADSIGIRLVKRAGSGTNITYHAVVELTSRSRIVQILKSHWGNELNRAKIAGKRLGFSALFASNLEAIIYQRGRNAARRNGSAELFTLTQGAGIETRYKWIMEKHIGIGVLIADAKGLINGKREGKRGVDANVKLRAGTTGSPLERAMQGIEKKAFPGPLRALARRVVKANYNDAREALNVIAEASLLLKPQITNKMTMPWCMWLAARLTLKDEFANFCAYAGRRAFEVFNIAMEKIGICSFQGTIMNDDEIESIEDKAQVLMMACFGLAYEDFSLVSAMVSHPLKLRNRMKIGNFRVGEKVSTVLSPLLRFTRWAEFAQRFALQANTSREGAQISNSAVFAVERKITTDVQRVEELLNKVQAHEDEPLQTLYKKVREQISIIGRNKSEIKEFLGSSMYDLNDQEKQNPINFRSGAHPFFFEFDPDYNPIRVKRPKKPIAKRNSNISRLEEEGMDENSEIGQAKKMKPLDQLTSTSSNIPGKN | Function: Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the host nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals that are responsible for the active RNP import into the nucleus through cellular importin alpha/beta pathway. Later in the infection, nclear export of RNPs are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that nucleoprotein binds directly host exportin-1/XPO1 and plays an active role in RNPs nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmasks nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.
PTM: Late in virus-infected cells, may be cleaved from a 56-kDa protein to a 53-kDa protein by a cellular caspase. This cleavage might be a marker for the onset of apoptosis in infected cells or have a specific function in virus host interaction.
Sequence Mass (Da): 63625
Sequence Length: 565
Subcellular Location: Virion
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B1YBH2 | MKVAVASRNPNKVRAVEEAYRLFGIPARVSSVDKPPSLPPQPVGLEAVVAGAVERAKAALAAAGEAEHGVGIEAGALEAGGRHLDVTVAAVADRGGLVTLGFGPAFQIPDVFLGDVLRGVELGVLAERHFGKAAVGYREGIIGLLTRGRVTRLDLNVVAVAMALVPRLPANAQLYRFWKTAP | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = H(+) + phosphate + XDP
Sequence Mass (Da): 18929
Sequence Length: 182
EC: 3.6.1.73
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Q97WI6 | MVTIALGSKNPVKISATKEALEILRLNWDLIATDIDSGVDKQPFCDQTYVGARNRALNAIKATNADIGLGIEGGVCNVYGKFIANAVVYVITKEGVENFAISSSFTLPSSIVSLILQGKELGEASDIIFKTINSKTKEGAVGLLTNNIIDRKTLYVQPIILALYPIYNTIINNTLF | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = H(+) + phosphate + XDP
Sequence Mass (Da): 19011
Sequence Length: 176
EC: 3.6.1.73
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P39432 | MHQVISATTNPAKIQAILQAFEEIFGEGSCHITPVAVESGVPEQPFGSEETRAGARNRVDNARRLHPQADFWVAIEAGIDDDATFSWVVIDNGVQRGEARSATLPLPAVILDRVRQGEALGPVMSQYTGIDEIGRKEGAIGVFTAGKLTRSSVYYQAVILALSPFHNAVYR | Cofactor: Binds 1 divalent metal cation per subunit; can use either Mg(2+) or Mn(2+).
Function: Phosphatase that hydrolyzes non-canonical purine nucleotides such as XTP and ITP to their respective diphosphate derivatives. Probably excludes non-canonical purines from DNA/RNA precursor pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions.
Catalytic Activity: H2O + XTP = H(+) + phosphate + XDP
Sequence Mass (Da): 18519
Sequence Length: 171
EC: 3.6.1.73
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P16603 | MPFGIDNTDFTVLAGLVLAVLLYVKRNSIKELLMSDDGDITAVSSGNRDIAQVVTENNKNYLVLYASQTGTAEDYAKKFSKELVAKFNLNVMCADVENYDFESLNDVPVIVSIFISTYGEGDFPDGAVNFEDFICNAEAGALSNLRYNMFGLGNSTYEFFNGAAKKAEKHLSAAGAIRLGKLGEADDGAGTTDEDYMAWKDSILEVLKDELHLDEQEAKFTSQFQYTVLNEITDSMSLGEPSAHYLPSHQLNRNADGIQLGPFDLSQPYIAPIVKSRELFSSNDRNCIHSEFDLSGSNIKYSTGDHLAVWPSNPLEKVEQFLSIFNLDPETIFDLKPLDPTVKVPFPTPTTIGAAIKHYLEITGPVSRQLFSSLIQFAPNADVKEKLTLLSKDKDQFAVEITSKYFNIADALKYLSDGAKWDTVPMQFLVESVPQMTPRYYSISSSSLSEKQTVHVTSIVENFPNPELPDAPPVVGVTTNLLRNIQLAQNNVNIAETNLPVHYDLNGPRKLFANYKLPVHVRRSNFRLPSNPSTPVIMIGPGTGVAPFRGFIRERVAFLESQKKGGNNVSLGKHILFYGSRNTDDFLYQDEWPEYAKKLDGSFEMVVAHSRLPNTKKVYVQDKLKDYEDQVFEMINNGAFIYVCGDAKGMAKGVSTALVGILSRGKSITTDEATELIKMLKTSGRYQEDVW | Cofactor: Binds 1 FAD per monomer.
Function: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis. Has NADPH-dependent ferrireductase activity on the plasma membrane.
Catalytic Activity: NADPH + 2 oxidized [cytochrome P450] = H(+) + NADP(+) + 2 reduced [cytochrome P450]
PTM: Phosphorylated by the cyclin-CDK PCL1-PHO85.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 76772
Sequence Length: 691
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.6.2.4
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Q8VYY5 | MKMRVETALAILLVLISIQQCYGGVSNYTCTCFSSGNRSDILESNCSTSCNCRPDRDQWVCLCPANGFPVIAIGGSNSSCFTSCNCSAGATKSSKKQYLSRKLVIVILLFCGVLISLAFLASMICYICRKDKFSGQTPSVSSDRESSWHSSANLINRKSSVSQSKISISSSVAGCFFQNASLFCVSKPETIHGAIFQFSYTELEQATNKFSSNSVIGHGGSSCVYRGQLKDGKTAAIKRLNTPKGDDTDTLFSTEVELLSRLHHYHVVPLIGYCSEFHGKHAERLLVFEYMSYGSLRDCLDGELGEKMTWNIRISVALGAARGLEYLHEAAAPRILHRDVKSTNILLDENWHAKITDLGMAKCLSSDGLQSGSSSPTTGLQGTFGYFAPEYAIAGCASQMSDVFSFGVVLLELITGRKPIQKPSNNKGEESLVIWAVPRLQDSKRVIEELPDPRLNGKFAEEEMQIMAYLAKECLLLDPESRPTMREVVQILSTITPDTSSRRRNFPINYLFQSNEKKKESKVGWSRGGSKSGQEEETVDLTEPRFESFCLPNVKPVLLEPSAHI | PTM: Phosphorylated.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 62192
Sequence Length: 565
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9LZD0 | MVSNCLSLSLHLNLHPHKHNRHSLSSLRSRTKAKLYQHVSFTDSSHKSSYTSCVSTFDIQRKSSKHYELGKHSFSPILPGDNLVLSRSGVIRPRLSAMTGSEINDHGYDESQFDPSLTNDDLKPTTPSQRTFSWLDMSSLWIGLVVGVPTYYLAGSLVDLGMAWWQGIATVVTANLILLVPLVLTAQPGTLYGISFPVLARSSFGIRGAHIPTLLRALVGCGWYGIETWIGGEAIFLLLPGHIKKSALSHTLPWLGTSPLEFSCFIVFWLAQLCIVWRGMDGIRKLEKYSAPILISLTSCLLAWSYLKAGGFGHMLSLSSKLTSAQFWTLFFPSLTANISFWATLALNIPDFSRFAKSQTDQIIGQVGLPVFMGLFTFVGVAVTSSTSIIFGRVISNPIELLGQIGGLATTLLAIVGISLATLTTNIAANVVAPANALVNLNPKFFTFGRGAFLTAVLGIVFQPWRLLKSSESFVYTWLIGYSALLGPIGGIILVDYYLIKKMKLNIGDLYSLSPSGEYYFSKGYNVAAVVALVAGIIPVVPGFLHKISALSKISNGFVVVYDNALFFSFIIAGFVYWIIMSRLGRKQSSLSSSSHPLL | Function: Nucleobase-proton symporter that facilitates the uptake of nucleobases in the cells. Can transport adenine, guanine and uracil . Contributes to uracil import into plastids for plastidic uracil salvage which is essential for plant growth and development .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65356
Sequence Length: 599
Subcellular Location: Plastid
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Q2V8Y7 | MGKSNSKLKPEVVEELTRKTYFTEKEVQQWYKGFIKDCPSGQLDAAGFQKIYKQFFPFGDPTKFATFVFNVFDENKDGRIEFSEFIQALSVTSRGTLDEKLRWASKLYDLDNDGYITRNEMLDIVDAIYQMVGNTVELPEEENTPEKRVDRIFAMMDKNADGKLTLQEFQEGTKADPSIVQALSLYDGLV | Function: Neuronal calcium sensor, regulator of G protein-coupled receptor phosphorylation in a calcium dependent manner. Directly regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for calmodulin (By similarity). Stimulates PI4KB kinase activity (By similarity). Involved in long-term synaptic plasticity through its interaction with PICK1 (By similarity). May also play a role in neuron differentiation through inhibition of the activity of N-type voltage-gated calcium channel (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21833
Sequence Length: 190
Subcellular Location: Golgi apparatus
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P36608 | MGKGNSKLKSSQIRDLAEQTYFTEKEIKQWYKGFVRDCPNGMLTEAGFQKIYKQFFPQGDPSDFASFVFKVFDENKDGAIEFHEFIRALSITSRGNLDEKLHWAFKLYDLDQDGFITRNEMLSIVDSIYKMVGSSVQLPEEENTPEKRVDRIFRMMDKNNDAQLTLEEFKEGAKADPSIVHALSLYEGLSS | Function: Neuronal calcium sensor, regulator of G protein-coupled receptor phosphorylation in a calcium dependent manner. Can substitute for calmodulin and directly activate PDE, NO synthase, and calcineurin. Regulates associative learning and memory in a calcium dependent manner.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22022
Sequence Length: 191
Subcellular Location: Membrane
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A2A1A0 | MSKNLTGVGGSLPVENVQVLAGKELKNLPNRYVRPELEHDDVVPIDNSLEIPVIDLSRLLDQQYACDELAKFHSACLDWGFFQLINHGVREEVIEKMKVDTEDFFRLPFKEKNAYRQLPNGMEGYGQAFVTSEEQKLDWADMHFLITKPVQERNMRFWPTSPTSFRETMEKYSMELQKVAMCLTGMMAKNLGLESEILTKPLRTVFNREDELLPSMSSCGEGLGLSPHSDATGLTLLIQVNEVNGLHIKKDEKWVPIKPILGAFVVNIGDVIEIMSNGIYKSIEHRAVINTDKERLSIAAFHDPEYGTKIGPLPDLVKENGVKYKTIDYEDYLIRSSNIKLDGKSLLDQMKL | Cofactor: Binds 1 Fe cation per subunit.
Function: Involved in the biosynthesis of the common precursor of all benzylisoquinoline alkaloids such as morphine, sanguinarine, codeine or berberine. Condenses dopamine and phenylacetaldehyde, 3,4-dihydrophenylacetaldehyde or 4-hydroxyphenylacetaldehyde.
Catalytic Activity: (4-hydroxyphenyl)acetaldehyde + dopamine = (S)-norcoclaurine + H2O
Sequence Mass (Da): 39964
Sequence Length: 352
EC: 4.2.1.78
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P62166 | MGKSNSKLKPEVVEELTRKTYFTEKEVQQWYKGFIKDCPSGQLDAAGFQKIYKQFFPFGDPTKFATFVFNVFDENKDGRIEFSEFIQALSVTSRGTLDEKLRWAFKLYDLDNDGYITRNEMLDIVDAIYQMVGNTVELPEEENTPEKRVDRIFAMMDKNADGKLTLQEFQEGSKADPSIVQALSLYDGLV | Function: Neuronal calcium sensor, regulator of G protein-coupled receptor phosphorylation in a calcium dependent manner. Directly regulates GRK1 (RHOK), but not GRK2 to GRK5. Can substitute for calmodulin (By similarity). Stimulates PI4KB kinase activity (By similarity). Involved in long-term synaptic plasticity through its interaction with PICK1 (By similarity). May also play a role in neuron differentiation through inhibition of the activity of N-type voltage-gated calcium channel (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 21879
Sequence Length: 190
Subcellular Location: Golgi apparatus
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Q4QTJ2 | MSKLITTEPLKSMAEVISNYAMKQQSVSERNIPKKQSLLRKEITYETEVQTSADSIWNVYSSPDIPRLLRDVLLPGVFEKLDVIAGNGGVGTVLDIAFPLGAVPRRYKEKFVKINHEKRLKEVVMIEGGYLDMGCTFYMDRIHIFEKTPNSCVIESSIIYEVKEEYAGKMAKLITTEPLESMAEVISGYVLKKRLQVFGFEIKPKLRFNLLLCLIICLVIAGGMFVAGVPL | Function: Involved in the biosynthesis of (S)-coclaurine, the common precursor of all benzylisoquinoline alkaloids such as morphine, sanguinarine, codeine or papaverine. Condenses dopamine and 4-hydroxyphenylacetaldehyde.
Catalytic Activity: (4-hydroxyphenyl)acetaldehyde + dopamine = (S)-norcoclaurine + H2O
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 26015
Sequence Length: 231
Pathway: Alkaloid biosynthesis; (S)-reticuline biosynthesis.
Subcellular Location: Membrane
EC: 4.2.1.78
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Q09711 | MGKSQSKLSQDQLQDLVRSTRFDKKELQQWYKGFFKDCPSGHLNKSEFQKIYKQFFPFGDPSAFAEYVFNVFDADKNGYIDFKEFICALSVTSRGELNDKLIWAFQLYDLDNNGLISYDEMLRIVDAIYKMVGSMVKLPEDEDTPEKRVNKIFNMMDKNKDGQLTLEEFCEGSKRDPTIVSALSLYDGLV | Function: Negatively regulates sporulation perhaps by controlling Ca(2+)-dependent desensitization of git3.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22033
Sequence Length: 190
Subcellular Location: Membrane
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Q9SKT7 | MSFHSFYQRASSLFKAYPSTSKILLLSTFSGGGGVLVYSDSNPLKRILHADATLDSDGNPIRKKKVVVLGSGWSGYSFLSYLNNPNYDVQVVSPRNFFLFTPLLPSVTNGTVEARSIVEPIRGLMRKKGFEYKEAECVKIDASNKKIHCRSKEGSSLKGTTEFDMDYDILILAVGAKPNTFNTPGVEEHAYFLKEAEDALNIRHSVIDCFERASLPNLTEEERKKILHFVVVGGGPTGVEFSAELHDFLVQDVAKIYPKVQEFTKITLLEAGDHILNMFDKRITAFAEEKFQRDGIDLKTGSMVVGVTADEISTKERETGKIVSEPYGMVVWSTGIGSRPVIKDFMQQIGQGQRRVLATDEWLRVEGCDGVYALGDTATINQRRVMEDIAAIFNKADKGNTGTLKKKDFNSVVKDICQRYPQVELYLKKNKLKNIANLLKSANGEDTQVNIEKFKQALSEVDSQMKNLPATAQVASQQGKYLAKCFNKMEKCEKKPEGPLRFRGEGRHRFQPFRYRHFGSFAPLGGEQTAAELPGDWVSIGHSSQWLWYSVYASKLVSWRTRMLVISDWTRRFVFGRDSSSI | Cofactor: Binds 1 FAD per subunit.
Function: Alternative NADH-ubiquinone oxidoreductase which catalyzes the oxidation of mitochondrial NADH does not translocate protons across the inner mitochondrial membrane (By similarity). NAD(P)H dehydrogenase; more efficient on NADH.
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65372
Sequence Length: 582
Subcellular Location: Mitochondrion inner membrane
EC: 1.6.5.9
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Q94C12 | MGRKKGLPEFEESAPDGFDPENPYKDPVAMVEMREHIVREKWIQIEKAKILREKVKWCYRVEGVNHYQKCRHLVQQYLDSTRGVGWGKDHRPISLHGPKPEAVEAE | Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 12438
Sequence Length: 106
Subcellular Location: Mitochondrion inner membrane
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P73735 | MTDARPRICILGGGFGGLYTALRLGQLSWEGHTPPEIVLVDQRDRFLFAPFLYELVTEEMQTWEIAPPFVELLAESGVIFRQAEVTAIDFDHQKVLLNDQDKGTESLAFDQLVIALGGQTPLPNLPGLKDYGLGFRTLEDAYKLKQKLKSLEQADAEKIRIAIVGGGYSGVELAAKLGDRLGERGRIRIIERGKEILAMSPEFNRQQAQASLSAKGIWVDTETTVTAITATDVTLQFREQEDVIPVDLVLWTVGTTVSPLIRNLALPHNDQGQLRTNAQLQVEGKTNIFALGDGAEGRDASGQLIPTTAQGAFQQTDYCAWNIWANLTGRPLLPCRYQPLGEMLALGTDGAVLSGLGIKLSGPAALLARRLVYLYRFPTWQHQLTVGLNWLTRPLGDWLKNEPS | Cofactor: Binds 1 FAD per subunit.
Function: Bifunctional oxidoreductase probably ables to act both on prenyl naphthoquinones and on prenyl benzoquinones . Catalyzes the penultimate step in the biosynthesis of vitamin K1 .
Catalytic Activity: demethylphylloquinone + H(+) + NADPH = demethylphylloquinol + NADP(+)
Sequence Mass (Da): 44489
Sequence Length: 404
Pathway: Cofactor biosynthesis; phylloquinone biosynthesis.
EC: 1.6.5.12
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P84189 | MKMMIPVIFSILLLIFSLSSTAMSLEDEQENMEERAEIDFSGIPEDIIKQIKETNAKPPARFDPAAFEKSDD | Function: Agonist of the B2 bradykinin receptor (BDKRB2) . Potentiates the hypotensive effect of bradykinin (BK) and induces a direct vasorelaxing effect independent of BK, by endothelium- and nitric oxide (NO)-dependent mechanisms in rat aortic ring preparations . Also exerts proangiogenic, antiinflammatory, and antifibrogenic activities .
PTM: Hypotensin-1 undergoes enzymatic cleavages by carboxypeptidases, endopeptidases, and aminopeptidases resulting in at least 46 fragments of this protein.
Sequence Mass (Da): 8164
Sequence Length: 72
Subcellular Location: Secreted
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Q9BBN8 | MNVPATRKDLMIVNMGPHHPSMHGVLRLIVTLDGEDVIDCEPILGYLHRGMEKIAENRTIIQYLPYVTRWDYLATMFTEAITVNGPEQLGNIQVPKRASYIRVIMLELSRIASHLLWLGPFMADIGAQTPFFYIFREREFIYDLFEAATGMRMMHNFFRIGGVAADLPHGWIDKCFDFCNYFFTRVVEYQKLITRNPIFLERVEGVGVVGGEEVINWGLSGPMLRASGIQWDLRQVDNYECYEEFDWEVQWQKEGDSLARYLVRIGEMMESIKIIQQALEGIPGGPYENLEIRCFGREKEPEWNDFEYRFIGKKPSPTFELPKQELYVRVEAPKGELGIFLIGDQNGFPWRWKIRPPGFINLQILPQLVKRMKLADIMTILGSIDIIMGEVDR | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 45601
Sequence Length: 393
Subcellular Location: Plastid
EC: 7.1.1.-
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Q85FL7 | MNTVDKEKFNLKTRGRLSAWLTKHNFSHRPLGYDYRGVEILEVKSEEWLSTAVALYAYGFNYLRSQCAYDATPGGSLVSVYHLTQMQDQSDQPEEICVKVFVSRTNPQIPSVYWVWKSAEFQERESYDMLGIIYQGHPYLRRILMPESWIGWPLRKDYVVPNFYELQDAY | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 20052
Sequence Length: 170
Subcellular Location: Plastid
EC: 7.1.1.-
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P56754 | MQGTLSVWLAKRGLVHRSLGFDYQGIETLQIKPEDWHSIAVILYVYGYNYLRSQCAYDVAPGGLLASVYHLTRIEYGVNQAEEVCIKVFTHRSNPRIPSVFWVWKSTDFQERESYDMLGITYDSHPRLKRILMPESWIGWPLRKDYIAPNFYEIQDAY | Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 18558
Sequence Length: 158
Subcellular Location: Plastid
EC: 7.1.1.-
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Q9BBT7 | MNSIEFPLIDRTTQNSVISTTLNDLSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPESILDAITKLRKKISREIHEDQTSSLSSQRENRCFTTNHKFYVERSTHTGNYDQVLFHQPPSTSEISSDTFFRYQKVQYPPRNEIVN | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26102
Sequence Length: 230
Subcellular Location: Plastid
EC: 7.1.1.-
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P06670 | MSLIEFPLLDQTSSNSVISTTLNDLSNWSRLSSLWPLLYGTSCCFIEFASLIGSRFDFDRYGLVPRSSPRQADLILTAGTVTMKMAPSLVRLYEQMPEPKYVIAMGACTITGGMFSTDSYSTVRGVDKLIPVDVYLPGCPPKPEAVIDALTKLRKKIAREIIEDRTLCQSQKKNRSFTTRHKLYVRRSTHTGTYEQELLYQSPSTLDISSETFFKSKSSVSSYKLVN | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 25497
Sequence Length: 227
Subcellular Location: Plastid
EC: 7.1.1.-
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Q50KA9 | MANSERTFIAIKPDGVQRSLVGEIIKRFEQKGFRLIAMKLIQASEDLLKEHYIDLKDRPFFAGLVKYMQSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVESAEKEIGLWFQPEELVDYKSCAQNWIYE | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein-coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination. During GZMA-mediated cell death, works in concert with TREX1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 17180
Sequence Length: 152
Subcellular Location: Cytoplasm
EC: 2.7.4.6
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P15531 | MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPFFAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVESAEKEIGLWFHPEELVDYTSCAQNWIYE | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein-coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination. During GZMA-mediated cell death, works in concert with TREX1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 17149
Sequence Length: 152
Subcellular Location: Cytoplasm
EC: 2.7.4.6
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P15532 | MANSERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFLQASEDLLKEHYTDLKDRPFFTGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVKSAEKEISLWFQPEELVEYKSCAQNWIYE | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein-coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination. During GZMA-mediated cell death, works in concert with TREX1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 17208
Sequence Length: 152
Subcellular Location: Cytoplasm
EC: 2.7.4.6
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Q05982 | MANSERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFIQASEDLLKEHYIDLKDRPFFSGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVESAEKEISLWFQPEELVDYKSCAQNWIYE | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and farnesyl pyrophosphate kinase, histidine protein kinase and 3'-5' exonuclease activities. Involved in cell proliferation, differentiation and development, signal transduction, G protein-coupled receptor endocytosis, and gene expression. Required for neural development including neural patterning and cell fate determination. During GZMA-mediated cell death, works in concert with TREX1. NME1 nicks one strand of DNA and TREX1 removes bases from the free 3' end to enhance DNA damage and prevent DNA end reannealing and rapid repair (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 17193
Sequence Length: 152
Subcellular Location: Cytoplasm
EC: 2.7.4.6
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Q50KA8 | MAHQERTFIAIKPDGVQRGLVGDIVKRFEQKGFRLVAMKFLRASEDLLKEHYIDLKDRPFYPGLVKYMHSGPVVAMVWEGLNVVKTGRMMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVKSAEKEISLWFKPEELVDYKSCAFDWIYE | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (By similarity). Negatively regulates Rho activity by interacting with AKAP13/LBC. Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically. Binds to both single-stranded guanine- and cytosine-rich strands within the nuclease hypersensitive element (NHE) III(1) region of the MYC gene promoter. Does not bind to duplex NHE III(1). Has G-quadruplex (G4) DNA-binding activity, which is independent of its nucleotide-binding and kinase activity. Binds both folded and unfolded G4 with similar low nanomolar affinities. Stabilizes folded G4s regardless of whether they are prefolded or not. Exhibits histidine protein kinase activity (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 17366
Sequence Length: 152
Subcellular Location: Cytoplasm
EC: 2.7.4.6
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P22392 | MANLERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVAMKFLRASEEHLKQHYIDLKDRPFFPGLVKYMNSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVKSAEKEISLWFKPEELVDYKSCAHDWVYE | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate (By similarity). Negatively regulates Rho activity by interacting with AKAP13/LBC . Acts as a transcriptional activator of the MYC gene; binds DNA non-specifically . Binds to both single-stranded guanine- and cytosine-rich strands within the nuclease hypersensitive element (NHE) III(1) region of the MYC gene promoter. Does not bind to duplex NHE III(1) . Has G-quadruplex (G4) DNA-binding activity, which is independent of its nucleotide-binding and kinase activity. Binds both folded and unfolded G4 with similar low nanomolar affinities. Stabilizes folded G4s regardless of whether they are prefolded or not . Exhibits histidine protein kinase activity .
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 17298
Sequence Length: 152
Subcellular Location: Cytoplasm
EC: 2.7.4.6
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P85288 | MEQTFVAIKPDGVQRGLCGEVMKFIQPMKHYLDLKDMPFYAGLCKYMSSGPVFAMVWEGEGIVKMMLGETNPADSKPGSIRGDFCINIGRNIIHGSDTVENAKMEVGLWFKPEEFVAYAEKAKAWVYE | Function: Major role in the synthesis of nucleoside triphosphates other than ATP.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 14393
Sequence Length: 128
Subcellular Location: Cytoplasm
EC: 2.7.4.6
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Q3YQT1 | MLERTLSILKPDVVKRNITGQVNSYIENSGLKIVTQKMCLLTRFQAEEFYAIHKSQHFFIPLVDFMVSGPIIVQVLEGENAISLYRELMGATDPKKANPGTIRGDFAENIDANCVHGSDSLDNAVREIRFFFSDYELLSLK | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 15943
Sequence Length: 141
Subcellular Location: Cytoplasm
EC: 2.7.4.6
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B4RCP4 | MTERTFSIIKPDATRRNLTGKVNAVIEDAGLRIVAQKRIRMSRAQAEKFYEVHKERPFFGELVEFMTSAPVVVQVLEGENAVARYREVMGATNPAQAADGTIRKLYAESVGENSVHGSDSLENAKIEIAQFFTEDEIVG | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 15462
Sequence Length: 139
Subcellular Location: Cytoplasm
EC: 2.7.4.6
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Q6KZI4 | MERCLILVKPDGVERNLIGEVISRFERKGLAIKALKMMRVTREQAEDHYSVHRLKPFFDDLVSYLTSGPIVAMIVEGNNAIASSRMLAGATDGSKAAPGTIRGDFSLDIERNIVHASDSLESYEHEYKIFFNENEIMD | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 15520
Sequence Length: 138
Subcellular Location: Cytoplasm
EC: 2.7.4.6
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A9B9E7 | MVAERTFLAIKPDGVQRGLVGEILSRFERKGFKLIALKQLIPSRALAEQHYGVHRERPFFKGLVDFITSGPVIAMIWEGEGVILGARKLIGSTKPLDADPGTIRGDLAIDIGRNVIHGSDGPETASFEIGLWFESSELSDWNPSDQLWRVE | Function: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP
Sequence Mass (Da): 16726
Sequence Length: 151
Subcellular Location: Cytoplasm
EC: 2.7.4.6
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Q803Q2 | MDTEMMPKFSSKDEEIDYWKCLSLKYKKSCHDAQEELQEFQEGSRELEAELEAQLGQAEHRIRDLQSENQRLKSEVDILKEKLEQQYAQSYKQISMLEDDLLQTRGIKEQLHKYVRELEQANDDLERAKRATITSLEDFEQRLNQAIERNAFLESELDEKESLLVSVQRLKDEARDLRQELAVRERTSDVTRMSAPSSPTLDIDKTDSAVQASLSLPATPVGKTMEHPFIGTKALTNGCGNGSPLTPSARISALNIVGDLLRKVGALESKLAACRNFAKDQAARKNYTTGNGNLINSNATKFSHSLHTTYFDKTTMNGLDPGALSAAIASPRAVSPPGLLPLSV | Function: Required for organization of the cellular microtubule array and microtubule anchoring at the centrosome. Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end (By similarity).
PTM: Phosphorylated in mitosis.
Sequence Mass (Da): 38443
Sequence Length: 344
Subcellular Location: Cytoplasm
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Q0QLF2 | MGKDYQVLGKNKVKVDSLEKVMGTAKFAADYSFPDMLYAGVFRSTVPHARIVSLDLSKARAIDGVEAVLDYHAIPGKNRFGIIIKDEPCLVDDKVRRYGDAIAVVAAQTPDLVQEALDAITIEYEELEGIFTMERALEEDSPAIHGDTNIHQVKHLEYGDVDAAFKQCDIVVEDTYSTHRLTHMFIEPDAGVSYYDNEGMLTVVVSTQNPHYDRGEVAGMLALPNSKVRIIQATTGGGFGGKLDLSVQCHCALLTYHTKKPVKMVRSREESTTVSSKRHPMTMHCKTGATKDGRLQAVQVEMFGDTGAYASYGPAVITRATVHCMGPYVVPNVRVDAKFVYTNNPMSGAFRGFGVPQASVCHEGQMNALAKALGMDPIDIRILNAHQVGAKLATGQVLENSVGLIETLEKAREKAVEVMGYEKTR | Cofactor: Binds 1 Se-Mo-molybdopterin cytosine dinucleotide (Se-Mo-MCD) cofactor per heterotetramer. The cofactor is bound between the NdhL and NdhM subunits.
Function: Catalyzes the hydroxylation of nicotinate to 6-hydroxynicotinate. Also active against 2-pyrazinecarboxylic acid, but inactive against other nicotinate analogs.
Catalytic Activity: H2O + NADP(+) + nicotinate = 6-hydroxynicotinate + H(+) + NADPH
Sequence Mass (Da): 46488
Sequence Length: 425
Pathway: Cofactor degradation; nicotinate degradation; 6-hydroxynicotinate from nicotinate: step 1/1.
EC: 1.17.1.5
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H9N289 | MEQAIINDEREYLRHFWHPVCTVTELEKAHPSSLGPLAVKLLNEQLVVAKLGDEYVAMRDRCAHRSAKLSLGTVSGNRLQCPYHGWQYDTHGACQLVPACPNSPIPNKAKVDRFDCEERYGLIWIRLDSSFDCTEIPYFSAANDPRLRIVIQEPYWWDATAERRWENFTDFSHFAFIHPGTLFDPNNAEPPIVPMDRFNGQFRFVYDTPEDMAVPNQAPIGSFSYTCSMPFAINLEVSKYSSSSLHVLFNVSCPVDSHTTKNFLIFAREQSDDSDYLHIAFNDLVFAEDKPVIESQWPKDAPADEVSVVADKVSIQYRKWLRELKEAHKEGSQAFRSALLDPVIESDRSYI | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Involved in the caffeine degradation, which is the essential first step for assimilating the carbon and nitrogen in caffeine. Catalyzes the N1-demethylation of caffeine to produce theobromine and formaldehyde. Also catalyzes the N1-demethylation of theophylline, paraxanthine, and 1-methylxanthine to 3-methylxanthine, 7-methylxanthine, and xanthine, respectively. NADH is the preferred substrate.
Catalytic Activity: caffeine + H(+) + NADH + O2 = formaldehyde + H2O + NAD(+) + theobromine
Sequence Mass (Da): 40203
Sequence Length: 351
Pathway: Alkaloid degradation.
EC: 1.14.13.178
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F0E1K6 | MHAENSFVIDDWYPVGALAETVSGRKYHTRILGTEIWYQLADGTVSAGLADNTAELASKSIYGLLWVSLSDNPRDVIAIPEFAEADRRVVSAGSIRVATSGLRVIENFLDMAHFPFVHTDILGAEPLTEVAAYDVEIDEAADEIRAVNCRFPQPKGSAAASEPVEMQYVYRIARPFIAILYKTCVIDANRLDVLGLFVQPVDQESSIAHTIMCYLDDINTDKQLRDFQQRIFGQDIMILINQVPKALPLNPRHETPVRADALSSAYRRWLNDRNVTFGTTRG | Function: Involved in the caffeine degradation, which is the essential first step for assimilating the carbon and nitrogen in caffeine. Probably catalyzes the N7-demethylation of 7-methylxanthine to produce xanthine and formaldehyde.
Catalytic Activity: 7-methylxanthine + H(+) + NADPH + O2 = formaldehyde + H2O + NADP(+) + xanthine
Sequence Mass (Da): 31473
Sequence Length: 282
EC: 1.14.13.128
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H9N291 | MNKLDVNQWFPIATTEDLPKRHVFHATLLGQEMAIWRDDSGSVNAWENRCPHRGLRLTLGANTGNELRCQYHGWTYESGTGGCTFVPAHRDAPPPNAARVNTFPVREKHGFIWTTLGQPPGEPISILDDAQLVNAVKTNLHSVVIDADIDGVVSVLRQNLSAFIDVFGAASAEDLHLKSMLQDRGILVTRSGSIAIHFYMQRSTISKCVVHAQVLTPGRPGYELQKNYSYAMNVIRRAAEAVATDLISITDISDQTIEKLEVVRENMTKAPPTHYICEVVTRTQETGDINSYWLKPIGYPLPAFSPGMHISITTPEGSIRQYSLVNGPDERESFIIGVKKEIQSRGGSRSMHEDVKVGTQLKVTLPRNGFPLVQTRKHPILVAGGIGITPILCMAQALDQQGSSYEIHYFARAFEHVPFQDRLTALGDRLNVHLGLGPDETRAKLPDIMEIHNAQDVDVYTCGPQPMIETVSAVALAHGIAEESIRFEFFSKKNDVPVSDEEYEVELKKTGQIFTVSPGSTLLQACLDNDVRIEASCEQGVCGTCITPVVSGDLEHHDTYLSKKERESGKWIMPCVSRCKSKKIVLDL | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Involved in the caffeine degradation, which is the essential first step for assimilating the carbon and nitrogen in caffeine. Catalyzes the oxidation of NADH and transfers electrons to NdmA and NdmB, which catalyze the N-demethylation reactions.
Sequence Mass (Da): 65089
Sequence Length: 588
EC: 1.-.-.-
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Q0QLF1 | MKKRGKGVGSMWYGIGNTGLPNPAAAFVEIHGDGSANVMFGAADIGQGSGTAMAQIAAEELGLDYEKIHVTWGDTMVTPDGGATSASRQTLITGNAVILACRQAKETLAKTAAEKLDCAPEELSFRDNTVFITADPERSMTYGELMAAMKAAGRMAVGAGSYNPNTTGLAPENMSGIPFEVYSYATTIAEVEVDTETGEVDVLKVVSAHDVGTPINRSMVEGQIEGGVTMGQGFVLMEEIEVNTKNGAIKNPSMSKYIIPSNRDVPEIHSILVESEGGPGPFGAKGVGEPALIPMIPAVVAAIEDALGTRFTHTPIMPKDIVAAVKAQEK | Cofactor: Binds 1 Se-Mo-molybdopterin cytosine dinucleotide (Se-Mo-MCD) cofactor per heterotetramer. The cofactor is bound between the NdhL and NdhM subunits.
Function: Catalyzes the hydroxylation of nicotinate to 6-hydroxynicotinate. Also active against 2-pyrazinecarboxylic acid, but inactive against other nicotinate analogs.
Catalytic Activity: H2O + NADP(+) + nicotinate = 6-hydroxynicotinate + H(+) + NADPH
Sequence Mass (Da): 34476
Sequence Length: 330
Pathway: Cofactor degradation; nicotinate degradation; 6-hydroxynicotinate from nicotinate: step 1/1.
EC: 1.17.1.5
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Q9SK66 | MQVVSRRLVQRPLVGGASIYSSSSLRSLYGVSNHLNGTDNCRYSSSLATKGVGHLARKGTGGRSSVSGIVATVFGATGFLGRYLVQQLAKMGSQVLVPFRGSEDSPRHLKLMGDLGQVVPMKFDPRDEDSIKAVMAKANVVINLIGREYETRNFSFEDANHHIAEKLALVAKEHGGIMRYIQVSCLGASVSSPSRMLRAKAAAEEAVLNALPEATIMRPATMIGTEDRILNPWSMFVKKYGFLPLIGGGTTKFQPVYVVDVAAAIVAALKDDGSSMGKTYELGGPDVFTTHELAEIMYDMIREWPRYVKLPFPIAKAMAAPRDFMVNKVPFPLPSPQIFNLDQINALTTDTLVSDNALKFQDLDLVPHKLKGYPVEFLIQYRKGGPNFGSTVSEKIPTDFYP | Cofactor: Binds 1 FAD per subunit.
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Sequence Mass (Da): 43936
Sequence Length: 402
Subcellular Location: Mitochondrion matrix
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Q559Z0 | MLKNLSKGFPSLINKRSFSTINENPLTRIHHGSRTQTTGLVATVFGATGFTGRYLVQLLARTGIQVVVPYRCEDEGFRDLKVLGELGQIIPVRFDIRDSESIERAISHSNIVINMAGRDYETRNFSLDDINVHAASRIADLSKNVEKYIHVSTLRASEDSPSHFSRSKAIGEKLTREIIPNCTVVRPSIIFGDEDKFINKWSKVSQNWPFIPRYNQQHKIQPLHCYDLASGILSILETPGTSGKVYEFAGDEVFTWDEFLDMIIDGTAQYSKLNIPVSNDFMKFISEHLLERFARNPNFIKDQIDYHNQDMTTTVGALTLKDLNVTTTPIQEKLIRLSRMYRPGKFFNAIANPQNK | Cofactor: Binds 1 FAD per subunit.
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Sequence Mass (Da): 40475
Sequence Length: 356
Subcellular Location: Mitochondrion matrix
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Q16795 | MAAAAQSRVVRVLSMSRSAITAIATSVCHGPPCRQLHHALMPHGKGGRSSVSGIVATVFGATGFLGRYVVNHLGRMGSQVIIPYRCDKYDIMHLRPMGDLGQLLFLEWDARDKDSIRRVVQHSNVVINLIGRDWETKNFDFEDVFVKIPQAIAQLSKEAGVEKFIHVSHLNANIKSSSRYLRNKAVGEKVVRDAFPEAIIVKPSDIFGREDRFLNSFASMHRFGPIPLGSLGWKTVKQPVYVVDVSKGIVNAVKDPDANGKSFAFVGPSRYLLFHLVKYIFAVAHRLFLPFPLPLFAYRWVARVFEISPFEPWITRDKVERMHITDMKLPHLPGLEDLGIQATPLELKAIEVLRRHRTYRWLSAEIEDVKPAKTVNI | Cofactor: Binds 1 FAD per subunit.
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Required for proper complex I assembly . Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
PTM: Acetylated on lysine residues. BLOC1S1 is required for acetylation . Acetylated by CLOCK in a circadian manner .
Sequence Mass (Da): 42510
Sequence Length: 377
Subcellular Location: Mitochondrion matrix
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Q9DC69 | MAAAVRFRVVRALPMSRPAITAAATSVFCGSSHRQLHHAVIPHGKGGRSSVSGVVATVFGATGFLGRYVVNHLGRMGSQVIIPYRCDVYDIMHLRLMGDLGQLTFLEWDARDKDSIRKAVQHSNVVINLIGREWETRNFDFEDVFVNIPRAIAQASKEAGVERFIHVSHLNASMKSSSKSLRSKAVGEKEVRSVFPEAIIIRPSDIFGREDRFLNHFANYRWFLAVPLVSLGFKTVKQPVYVADVSKGIVNATKDPDAVGKTFAFTGPNRYLLFHLVKYIFGMTHRTFIPYPLPLFVYSWIGKLFGLSPFEPWTTKDKVERIHISDVMPTDLPGLEDLGVQPTPLELKSIEVLRRHRTYRWLSSEIEETKPAKTVNY | Cofactor: Binds 1 FAD per subunit.
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
PTM: Acetylated on lysine residues. BLOC1S1 is required for acetylation. Acetylated by CLOCK in a circadian manner.
Sequence Mass (Da): 42525
Sequence Length: 377
Subcellular Location: Mitochondrion matrix
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P25284 | MAPLTAAMRSTPRIIVSNAFGFQRRAISDVTITRTGKPIIRNQGGRSSLGGHTATVFGATGQLGRYIVNRLARQGCTVVIPFRDEYNKRHLKVTGDLGKVVMIEFDLRNTQSIEESVRHSDVVYNLIGRDYPTKNFSFEDVHIEGAERIAEAVAKYDVDRFIHVSSYNADPNSECEFFATKARGEQVVRSIFPETTIVRPAPMFGFEDRLLHKLASVKNILTSNGMQEKYNPVHVIDVGQALEQMLWDDNTASETFELYGPKTYTTAEISEMVDREIYKRRRHVNVPKKILKPIAGVLNKALWWPIMSADEIEREFHDQVIDPEAKTFKDLGIEPADIANFTYHYLQSYRSNAYYDLPPATEKERREDREYIHML | Cofactor: Binds 1 FAD per subunit.
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Sequence Mass (Da): 42870
Sequence Length: 375
Subcellular Location: Mitochondrion matrix
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P80265 | ASNLATGGAGPLIXKGTGGRSS | Cofactor: Binds 1 FAD per subunit.
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Sequence Mass (Da): 1983
Sequence Length: 22
Subcellular Location: Mitochondrion matrix
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P54713 | LQYGPLAXILGE | Cofactor: Binds 1 FAD per subunit.
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Sequence Mass (Da): 1285
Sequence Length: 12
Subcellular Location: Mitochondrion matrix
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P91929 | MTAVFRVGLVRLVSRATQSPNLLQAQTNALPAAFQQRCSISGKTMRGGPRVPKAAPYPYKTKKYSVFNAIFDKTSKRFDENSKVICVEGPIAAGKSKFAKELAEELDMEYYPAVDLDLIYINSYGYDMRKLDPQLPPSCRSYDVRNFCLDPSHDLAAQFQIRMYMLRYSQYIDALQHVLSTGQGVVLERSPYSDFVFMEAMFRQGYLSRGARSVYNELRQNTIGELLKPHLVIYLDLPVDAVKKQIKARNVDYEVQSKVFSDAYLSDLEQLYKQQYLKDISTHAELLIYDWTAGGETEVVVEDIERIDFNQFEADIHNKKMLDWRFPLEAEWCEARIKYCHEKPDLMNYFNVPRFDVPELVRSADDGKVWRDVWFNAPGMKYRPGYNADMGDEGLLTKTKIGINQGI | Cofactor: Binds 1 FAD per subunit.
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Sequence Mass (Da): 46898
Sequence Length: 407
Subcellular Location: Mitochondrion matrix
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O95299 | MALRLLKLAATSASARVVAAGAQRVRGIHSSVQCKLRYGMWHFLLGDKASKRLTERSRVITVDGNICTGKGKLAKEIAEKLGFKHFPEAGIHYPDSTTGDGKPLATDYNGNCSLEKFYDDPRSNDGNSYRLQSWLYSSRLLQYSDALEHLLTTGQGVVLERSIFSDFVFLEAMYNQGFIRKQCVDHYNEVKSVTICDYLPPHLVIYIDVPVPEVQRRIQKKGDPHEMKITSAYLQDIENAYKKTFLPEMSEKCEVLQYSAREAQDSKKVVEDIEYLKFDKGPWLKQDNRTLYHLRLLVQDKFEVLNYTSIPIFLPEVTIGAHQTDRVLHQFRELPGRKYSPGYNTEVGDKWIWLK | Cofactor: Binds 1 FAD per subunit.
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
PTM: Phosphorylation at Ser-250 by PINK1 is required for the binding and/or reduction of the complex I substrate ubiquinone.
Sequence Mass (Da): 40751
Sequence Length: 355
Subcellular Location: Mitochondrion matrix
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Q9TC96 | MAIEHASSIKKVKNFTLNFGPQHPAAHGVLRLVLELNGEVVARADPHIGLLHRGTEKLIEYKTYTQALPYFDRLDYVSMMCQEHAYSLAVEKLLHCEVPERAQYIRVLFSEITRILNHLLALTTHAMDVGALTPFLWAFEEREKLIEFYERVSGSRMHAAYIRPGGVACDLPANLCEDIYLFCQQFASRIDEMEEMLTNNRIWKQRLVDIGIVTAENAFAWGFSGVLLRGSGVAWDLRKTQPYDVYNRMIFDVPVGTQGDCYDRYLCRVEEMRQSIHIIMQCLNQLPKGMIKADDKKITPPSRSQMKQSMESLIHHFKLFTEGYTVPNSETYTSVEAPKGEFGVYLVSNGTNRPYRCKIRAPGFLHLQGLDMMSKNHMLADVVTIIGTQDIVFGEVDR | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). Component of the iron-sulfur (IP) fragment of the enzyme (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Sequence Mass (Da): 45476
Sequence Length: 398
Subcellular Location: Mitochondrion
EC: 7.1.1.2
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Q36450 | MTTKNRQIKNFTSNFGPQHPAAHGVSRSVLEMNGEVVERAEPHIGLLQRGTEKLIEYKTYLQALPYSDRSEYVSMMAQEHAHSSAVERLLNCEVPLRAQYIRVLFREITRISNHSLALTTHAMDVGASTPFLWAFEEREKLLEFYERVSGARMHASFIRPGGVAQDLPLGLCIDIDSFTQQFASRIDELEEMSTGNRIWKQRLVDIGTVTAQQAKDWGFSGVMLRGSGVCWDLRKAAPYDVHDQLDPDIPVGTRGDRYDRYCIRIEEMRQSVRIIVQCLNQMPSGMIKADDRKLCPPSRSRMKLSMESSIHHFEPYTEGFSVPAPSTYTAVEAPKGEFGVFLVSNGSNRPYRRKIRAPCFAHSQGLDSMSKHHMPADVVTIIGTQDIVSGEVDR | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). Component of the iron-sulfur (IP) fragment of the enzyme.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Sequence Mass (Da): 44522
Sequence Length: 394
Subcellular Location: Mitochondrion
EC: 7.1.1.2
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Q5DUX5 | MMRSSSLQKNIMLLRVGSKDSTRFRILILNFGPQHPASHGVLRLVIVIIGEVVTKLDPHIGFLHRGTERLVEEHSYMNAAVFMDRLDYTTVLTQTHAYCLAVEQALAKSRLCIRTQLLRTIFDELSRILNHLLSIATHALDIGTMAMLFWAFEDRERIMELYEYISGARMHTALYYPNQTLDHILTNELLAKILIFSRNSEKTYTEIYIALYNNRVWRLRLCGIGVVSTEISTSTTISGPVARSTGLQLDMRSGENYQYGYYASLTLRIFLGISGDSFDRFIIRLRELFESTRLIYNSLIELSAYINISVYNMCSYSNNPHLKIESLIELFRYSLGEYLLNISLVSGFVESGKGIFGIMLAANNTNRPYRLYIRSPAYMHLQLLPKLGAGHHIADLATLLGSIDVVFGEVDR | Function: Transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. Component of the iron-sulfur (IP) fragment of the enzyme.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Sequence Mass (Da): 46974
Sequence Length: 412
Subcellular Location: Hydrogenosome
EC: 7.1.1.2
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P15689 | MKAICVNFGPQHPAAHGVLRLILQLNGEVVEKMDIHIGLLHRGSEKLMETKPYLQSMPYFDRLDYVSMMVQEHAYCLAIEALLNTTNYTANFVLVRTMFDELTRILNHMLAIACHALDIGSMSSIFWAFEEREKIMEFYERVCGRRMHAAFYRPNEVNLNFLSVKLLTDILEFNNNCLTTLSEMHNILTYNKIWKQRLVNIGSISYKDCLDFGLTGVMARSTGIKRDLRMDAFDTYANYYYLNFRSYTGQAGDSYDRFLIRMNEMSESINIISQAIFKLTTSKNTCSPASILKALNKKKFISQTYKNEYSSMEKLITHFKYWSEGFKIQSNWTYQAVESPKGEFGVTLVSDGSNKPYRCKVRSPAYHHLQVLPKMSKGHLLADLSALIGTIDIVFGEIDR | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). Component of the iron-sulfur (IP) fragment of the enzyme. Component of the iron-sulfur (IP) fragment of the enzyme.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Sequence Mass (Da): 46077
Sequence Length: 400
Subcellular Location: Mitochondrion
EC: 7.1.1.2
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Q37619 | MALEKIITAPKYKNFTINFGPQHPAAHGVLRLVLEMNGEVVQRSDPHIGLLHRGTEKLIEYKNYLQALPYFDRLDYVSMMCQEHAYSLAVEKLLNISKDIPLRAQYIRVLFSEITRILNHLLAVTCHAMDVGALTPFLWGFEEREKLMEFYERVSGARMHAAYIRPGGVALDLPLGLCEDIYKFSKQFASRIDEIEEMLTSNRIWKQRLVDVGVVSAEQALDWSFSGVLLRGSGIAWDLRKTQPYEVYDRMKFNIPVGTRGDCYDRYLIRVQEMRESLRIVMQTINEMSKGIIRLDDRKITPPTRDQMKQSMESLIHHFKFYTGGFVVPAGETYTAVEAPKGEFGVYLVSNGTSKPYRCKIRAPGFAHLQGLDFMARNHMLADVVTIIGTQDIVFGEVDR | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). Component of the iron-sulfur (IP) fragment of the enzyme. Component of the iron-sulfur (IP) fragment of the enzyme.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Sequence Mass (Da): 45810
Sequence Length: 400
Subcellular Location: Mitochondrion
EC: 7.1.1.2
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P80264 | MTTKNRQIQNFTLNFGPQHPAAHGVLRLVLEMNGEVVERAEPHIGLL | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). Component of the iron-sulfur (IP) fragment of the enzyme.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 5278
Sequence Length: 47
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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P21301 | MLFLVVFLHLYRFTFGPQHPAAHGVLCCLLYFCGEFIVYIDCIIGYLHRGTEKLCEYKSVEQCLPYFDRLDYVSVCCNEHLLSLCFEYMLRCCLSLRCAFMRLLIVEFTRSFNGLLCISCMVLDLGCLSPLLWSFEERDKLMTFFDLCCGCRMHLAFMVLLGILDDFVFGFVDFLLLLIISCLFVMDCYDLLFVGNRLFYLRLRGLSFFDLYDLVFNSLSGVLSRSLGMVWDCRLFSCYELYFMFCYDYCFCFIGDAFDRLFLRLFDMRMSLLICKQCFFVGFFVFGFVCLFDYLYCDITIETIIMLFYSLWCCCLPGISFACVEHPKGEYCLLLCFCVGLCSRLRLRCADFLHICLLDVCLRGFLLHDLVAVLGNIDVVFGSVDR | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). Component of the iron-sulfur (IP) fragment of the enzyme. Component of the iron-sulfur (IP) fragment of the enzyme.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Sequence Mass (Da): 45098
Sequence Length: 386
Subcellular Location: Mitochondrion
EC: 7.1.1.2
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Q37383 | MGLNFFMSRKIYYIKLLTGLYKKFIKALIVKKNESNNAYLLVETANFYNLVFSLQRSSLTQFKVLNDVCIVDYPEKIDRFELSYNLSSIKYNFRIFIKTYTSAYVPSISTLFNSANWIERECWDMFGVFFTNHPDLRRILTDYGFEGFPLRKDFPLTGYIEIRYDDEKANIVYEPLELSQEYRLFNFTSPWEKIK | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Sequence Mass (Da): 23349
Sequence Length: 195
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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Q95748 | MDNQFIFKYSWETLPKKWVKKMERSEHGNRFDTNTDYLFQLLCFLKLHTYTRVQVLIDICGVDYPSRKRRFEVVYNLLSTRYNSRIRVQTSADEVTRISSVVSLFPSAGWWEREVWDMFGVSFINHPDLRRILTDYGFEGHPLRKDFPLSGYVEVRYDDPEKRVVSEPIEMTQEFRYFDFASPWEQRSDG | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22881
Sequence Length: 190
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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Q00673 | MISRTLLKRTVPASRLLRSFTTSNVRLSAHEEDLVNVNNLPRPKPTENYVPLINPTEKYKVQIEELHKFGTYIMSCLPKYIQQFSVWKDELTIYVAPSAIRPVMSYLKNHTSCQFKAVMDITAADYPSRTNRFDVVYNLLSDRHNSRIRVKTYANETSPVPSVTPLFNGANWYERETYDLFGVFFVGHPDLRRIMTDYGFEGHPLRKDFPTTGYTEVRYDEEKKRVIYEPLELTQAWRNFTVGSSVWEPVGEGKDFTPESFKLPTPQPEPEQEEKK | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). Essential for N-alkane assimilation.
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Sequence Mass (Da): 32158
Sequence Length: 276
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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Q2LCR4 | MKDYKNELKVKVDLGENLRGSIPGLIKKVMYKTQYLEIQVEKKNLLPVLRFLKESSKYQCTMLLDIVCIDCLNIEEIKIGRFKIIYVLNSIYNNTRVHISTYVENNGIIETTSGLFESSVWLEREIWDMFGIYFEKHPDLRRILTDYGFVGYPLKKDFPITGYLEVYYDVADKKIIYKPIELMQEYRNYNFGAVWGDYERKVYLENIIK | Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Catalytic Activity: a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+)
Sequence Mass (Da): 24881
Sequence Length: 209
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
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Q2YQ73 | MSLLKIYWRAMQYLAVERTATITMCVASVLVALVTLAEPVLFGRVIQSISDKGDIFSPLLMWAALGGFNIMAAVFVARGADRLAHRRRLGVMIDSYERLITMPLAWHQKRGTSNALHTLIRATDSLFTLWLEFMRQHLTTVVALATLIPVAMTMDMRMSLVLIVLGVIYVMIGQLVMRKTKDGQAAVEKHHHKLFEHVSDTISNVSVVQSYNRIASETQALRDYAKNLENAQFPVLNWWALASGLNRMASTFSMVVVLVLGAYFVTKGQMRVGDVIAFIGFAQLMIGRLDQISAFINQTVTARAKLEEFFQMEDATADRQEPENVADLNDVKGDIVFDNVTYEFPNSGQGVYDVSFEVKPGQTVAIVGPTGAGKTTLINLLQRVFDPAAGRIMIDGTDTRTVSRRSLRHAIATVFQDAGLFNRSVEDNIRVGRANATHEEVHAAAKAAAAHDFILAKSEGYDTFVGERGSQLSGGERQRLAIARAILKDSPILVLDEATSALDVETEEKVTQAVDELSHNRTTFIIAHRLSTVRSADLVLFMDKGHLVESGSFNELAERGGRFSDLLRAGGLKLEDKQPKQPVVEGSNVMPFPVKGAVA | Function: Involved in beta-(1-->2)glucan export. Its export to the periplasmic space is required to exert its action as a virulence factor. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation (Probable).
Catalytic Activity: [(1->2)-beta-D-glucosyl](n)(in) + ATP + H2O = [(1->2)-beta-D-glucosyl](n)(out) + ADP + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65951
Sequence Length: 599
Domain: In NdvA the ATP-binding domain (NBD) and the transmembrane domain (TMD) are fused.
Subcellular Location: Cell inner membrane
EC: 7.5.2.3
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P16009 | MEMISNNLNWFVGVVEDRMDPLKLGRVRVRVVGLHPPQRAQGDVMGIPTEKLPWMSVIQPITSAAMSGIGGSVTGPVEGTRVYGHFLDKWKTNGIVLGTYGGIVREKPNRLEGFSDPTGQYPRRLGNDTNVLNQGGEVGYDSSSNVIQDSNLDTAINPDDRPLSEIPTDDNPNMSMAEMLRRDEGLRLKVYWDTEGYPTIGIGHLIMKQPVRDMAQINKVLSKQVGREITGNPGSITMEEATTLFERDLADMQRDIKSHSKVGPVWQAVNRSRQMALENMAFQMGVGGVAKFNTMLTAMLAGDWEKAYKAGRDSLWYQQTKGRASRVTMIILTGNLESYGVEVKTPARSLSAMAATVAKSSDPADPPIPNDSRILFKEPVSSYKGEYPYVHTMETESGHIQEFDDTPGQERYRLVHPTGTYEEVSPSGRRTRKTVDNLYDITNADGNFLVAGDKKTNVGGSEIYYNMDNRLHQIDGSNTIFVRGDETKTVEGNGTILVKGNVTIIVEGNADITVKGDATTLVEGNQTNTVNGNLSWKVAGTVDWDVGGDWTEKMASMSSISSGQYTIDGSRIDIG | Function: Baseplate central spike complex-associated lysozyme that is essential for the localized hydrolysis of bacterial cell wall, so that the tail tube, through which the phage DNA is ejected, can penetrate to the host inner membrane . The tail lysozyme complex at the tip of the tail tube penetrates through the outer membrane into the periplasm and during that process, gp5* dissociates from gp5C and activated . Due to the lower pH in the periplasm, gp5* would dissociate from gp27 which probably still binds to the tip of the tube . This way, lysozyme domain is released and locally digests the peptidoglycan layer to make a hole to let the tube penetrate to the inner membrane . Involved in the tail assembly .
PTM: In the fully assembled virus, gp5 precursor is cleaved to form the mature tail lysozyme gp5*, and a C-terminus fragment, gp5C . The two fragments remain associated with the virion . The enzymatic activity of the precursor is about 10% of that of mature gp5* . PubMed:15342608 reported a cleavage at Val-390 but the cleavage has been mostly observed at Ser-351 .
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 63116
Sequence Length: 575
Subcellular Location: Virion
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Q9FLI7 | MAIIASTFGTGLSYAGELPFKPVTGGEVGRKQQRMVVVRAEGGGGINPEIRKNEDKVVDSVVVTELSKNITPYCRCWRSGTFPLCDGSHVKHNKANGDNVGPLLLKKQ | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Plays an important role in plant development, senescence, reactive oxygen homeostasis, and iron metabolism. Acts as an iron-sulfur transfer protein.
Sequence Mass (Da): 11626
Sequence Length: 108
Subcellular Location: Plastid
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O70903 | MGGKWSKSRMGGWSTIRERMRRAEPVAEGVGAVSRDLDRRGAVTINNTASTNRDAAWLEAQEDGEEVGFPVRPQVPLRPMTYKGAFDLSHFLKEKGGLDGLIYSKQRQDILDLWVYNTQGYFPDWQNYTPGPGERFPLTFGWCFKLVPVNPQEVEQANEGENNSLLHPMSLHGMEDDGREVLMWKFDSRLALTHLARVKHPEYKDC | Function: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells.
PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23498
Sequence Length: 206
Domain: The N-terminal domain is composed of the N-myristoyl glycine and of a cluster of positively charged amino acids. It is required for inner plasma membrane targeting of Nef and virion incorporation, and thereby for infectivity. This domain is also involved in binding to TP53.
Subcellular Location: Host cell membrane
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P03407 | MGGKWSKRSMGGWSAIRERMRRAEPRAEPAADGVGAVSRDLEKHGAITSSNTAATNADCAWLEAQEEEEVGFPVRPQVPLRPMTYKAALDISHFLKEKGGLEGLIWSQRRQEILDLWIYHTQGYFPDWQNYTPGPGIRYPLTFGWCFKLVPVEPEKVEEANEGENNSLLHPMSLHGMEDAEKEVLVWRFDSKLAFHHMARELHPEYYKDC | Function: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells.
PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24042
Sequence Length: 210
Domain: The N-terminal domain is composed of the N-myristoyl glycine and of a cluster of positively charged amino acids. It is required for inner plasma membrane targeting of Nef and virion incorporation, and thereby for infectivity. This domain is also involved in binding to TP53.
Subcellular Location: Host cell membrane
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Q89842 | MGGKWSKRRAEGWQTIRERMRRAEPAEPAADGVGAVSRDLARHGAITSSNTNNADIAWLEAQEEGEVGFPVRPQVPLRPMTYKAAVDLSHFLKEKGGLEGLVHSQKRQDILDLWVYHTQGFFPDWQNYTPGPGIRYPLTFGWCYKLVPVEPDEGENNREDNSLLHPANQHGVEDSERQVLVWRFDSRLAFHHVARELHPEYFKN | Function: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells.
PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23382
Sequence Length: 204
Domain: The N-terminal domain is composed of the N-myristoyl glycine and of a cluster of positively charged amino acids. It is required for inner plasma membrane targeting of Nef and virion incorporation, and thereby for infectivity. This domain is also involved in binding to TP53.
Subcellular Location: Host cell membrane
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P03406 | MGGKWSKSSVVGWPTVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAATNAACAWLEAQEEEEVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGVRYPLTFGWCYKLVPVEPDKVEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC | Function: Factor of infectivity and pathogenicity, required for optimal virus replication . Alters numerous pathways of T-lymphocytes function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity . Alters the functionality of other immunity cells, like dendritic cells, monocytes/macrophages and NK cells .
PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23342
Sequence Length: 206
Domain: The N-terminal domain is composed of the N-myristoyl glycine and of a cluster of positively charged amino acids. It is required for inner plasma membrane targeting of Nef and virion incorporation, and thereby for infectivity. This domain is also involved in binding to TP53.
Subcellular Location: Host cell membrane
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Q1JQA5 | MAGPAPGRRLVALALIVALAVGLPTAGAGQAPRPAERGPPVRLFTEEELARYGGEEEDQPIYMAVKGVVFDVTSGKEFYGRGAPYNALTGKDSTRGVAKMSLDPADLTHDTTGLTAEELESLDDVFTRVYKAKYPIVGYTARRILNEDGSPNLDFKPEDQPHFDIKDEF | Function: Acts as a neurotrophic factor in postnatal mature neurons enhancing neuronal survival (By similarity). Promotes cell proliferation and neurogenesis in undifferentiated neural progenitor cells at the embryonic stage and inhibits differentiation of astrocytes (By similarity). Its neurotrophic activity is exerted via MAPK1/ERK2, MAPK3/ERK1 and AKT1/AKT pathways (By similarity). Neurotrophic activity is enhanced by binding to heme (By similarity). Acts also as an anorexigenic neurotrophic factor that contributes to energy balance (By similarity).
Sequence Mass (Da): 18313
Sequence Length: 169
Domain: The cytochrome b5 heme-binding domain was proven to bind heme, although it lacks the conserved iron-binding His residue at position 79.
Subcellular Location: Secreted
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Q923S6 | MGNNFSSVSSLQRGNPSRASRGHPQNLKDSIGGSFPVPSHRCHHKQKHCPPTLSGGGLPATPLLFHPHTKGSQILMDLSHKAVKRQASFCNAITFSNRPVLIYEQVRLKITKKQCCWSGALRLGFTSKDPSRIHPDSLPKYACPDLVSQSGFWAKALPEEFANEGNIIAFWVDKKGRVFYRINESAAMLFFSGVRTVDPLWALVDVYGLTRGVQLLDSELVLPDCLRPRSFTALRRPSLRCEADEARLSVSLCDLNVPGADGDDGAPPAGCPIPQNSLNSQHSRALPAQLDGDLRFHALRAGAHVRILDEQTVARLEHGRDERALVFTSRPVRVAETIFIKVTRSGGGRAGALSFGVTTCDPGTLRPADLPFSPEALVDRKEFWAVCRVPGPLHSGDILGLVVNADGELHLSHNGAAAGMQLCVDASQPLWMLFSLHGAITQVRILGSTIMTERGGPSLPCSPASTPTSPSALGIRLSDPLLSTCGSGPLGGSAGGTAPNSPVSLPESPVTPGLGQWSDECTICYEHAVDTVIYTCGHMCLCYSCGLRLKKALHACCPICRRPIKDIIKTYRSS | Function: Plays a role in hippocampal-dependent synaptic plasticity, learning and memory. Involved in the formation of spines and functional synaptic contacts by modulating the translational activity of the cytoplasmic polyadenylation element-binding protein CPEB3. Promotes ubiquitination of CPEB3, and hence induces CPEB3-dependent mRNA translation activation of glutamate receptor GRIA1 and GRIA2. Can function as an E3 ubiquitin-protein ligase to activate monoubiquitination of JAG1 (in vitro), thereby regulating the Notch pathway. Acts as a tumor suppressor; inhibits malignant cell transformation of medulloblastoma (MB) cells by inhibiting the Notch signaling pathway.
PTM: Myristoylation is a determinant of membrane targeting.
Location Topology: Peripheral membrane protein
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): 61778
Sequence Length: 574
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q9D0S4 | MADPSEHVGLGGPRSPARPEPPPTRFHQVHGANIRMDPSGTRATRVESFAHGVCFSREPLAPGQVFLVEIEEKELGWCGHLRLGLTALDPASLAAVPEFSLPDLVSLGHSWVFAITRHHNRVPREGQPEAEAAVPSGPQALLVEPYLRIEQFRIPRDRLVGRSRPGLYSHLLDQLYEQNVLPPTARRSRLGVLFCPREDGTADMHIIINGEDMGPSARGLPAAQPLYAVVDVFASTKSVRLVQLEYGLPSLQTLCRLVIHKRVVHRLAIDVLHLPKGLKDFCKYE | Function: Plays an important role in the process of myofiber differentiation and maturation. Probable substrate-recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex, which mediates the ubiquitination of proteins. Probably contributes to catalysis through recognition and positioning of the substrate and the ubiquitin-conjugating enzyme. During myogenesis, controls the ubiquitination and degradation of the specific pool of CTNNB1/beta-catenin located at the sarcolemma.
Sequence Mass (Da): 31537
Sequence Length: 285
Domain: The SOCS domain mediates the interaction with ELOB and ELOC, while the NHR domain may be involved in ubiquitination substrate binding.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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Q96EH8 | MGAQLCFEANAKAPREALRFHAEAKGAQVRLDTRGCIAHRRTTFHDGIVFSQRPVRLGERVALRVLREESGWCGGLRVGFTRLDPACVSVPSLPPFLCPDLEEQSPTWAAVLPEGCALTGDLVRFWVDRRGCLFAKVNAGCRLLLREGVPVGAPLWAVMDVYGTTKAIELLDPTASRLPTPMPWDLSNKAVPEPKATPGEECAICFYHAANTRLVPCGHTYFCRYCAWRVFSDTAKCPVCRWQIEAVAPAQGPPALRVEEGS | Function: E3 ubiquitin-protein ligase that plays a role in various biological processes such as lung development or innate immunity . Seems to utilize UBE2E1. Promotes innate antiviral response by catalyzing 'Lys-63'-linked ubiquitination of IRF7 . Inhibits also hepatitis C virus assembly by directly binding to viral E1 envelope glycoprotein to disrupt its interaction with E2 .
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): 28789
Sequence Length: 262
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q8CJC5 | MGSLLSPEANAEVPREALSFHGNATGAQVHLDDQRSTARRRSTFHDGIVFSQRPVWPGERVALRVLRHEEGWCGGLRVGFTRLDPAQVAASCLPPFVCPDLEEQSPTWAALLPEGFVRAGNVVCFWVNRRGWLFAKVNAGRPLLLRKDVLVQGAPLWAVMDVYGTTKAIELLDPKANAWIRSGEPVPESEVISGEECVICFHNTANTRLMPCGHSHFCGSCAWHIFKDTARCPICRWQIEEVAVVSSLKAEEGS | Function: E3 ubiquitin-protein ligase that plays a role in various biological processes such as lung development or innate immunity . Seems to utilize UBE2E1. Promotes innate antiviral response by catalyzing 'Lys-63'-linked ubiquitination of IRF7 .
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): 28040
Sequence Length: 254
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q02038 | MIVRCLSAARRLHRVGGSGILLRMTLGREAMSPLQAMSSYTVDGRNVLRWDLSPEQIKRRTEELIAQTKQVYDDIGMLDIEEVTYENCLQALADVEVKYIVERTMLDFPQHVSSDKEVRAASTEADKRLSRFDIEMSMREDIFLRIVRLKETCDLGKIKPEARRYLEKSVKMGKRNGLHLPEQVQNEIKAMKKRMSELCIDFNKNLNEDDTFLVFSKAELGALPDDFIDSLEKTDDNKYKITLKYPHYFPVMKKCCIPETRRKMEMAFNTRCKEENTIILQELLPLRAKVAKLLGYSTHADFVLEMNTAKSTHHVTAFLDDLSQKLKPLGEAEREFILNLKKKECEEKGFEYDGKINAWDLHYYMTQTEELKYSVDQEILKEYFPIEVVTEGLLNIYQELLGLSFEQVTDAHVWNKSVTLYTVKDKATGEVLGQFYLDLYPREGKYNHAACFGLQPGCLLPDGSRMMSVAALVVNFSQPRAGRPSLLRHDEVRTYFHEFGHVMHQICAQTDFARFSGTNVETDFVEVPSQMLENWVWDTDSLRRLSKHYKDGSPITDDLLEKLVASRLVNTGLLTLRQIVLSKVDQSLHTNTSLDAASEYAKYCTEILGVAATPGTNMPATFGHLAGGYDGQYYGYLWSEVFSMDMFYSCFKKEGIMNPEVGMKYRNLILKPGGSLDGMDMLQNFLKREPNQKAFLMSRGLHAP | Cofactor: Binds 1 zinc ion per subunit.
Function: Hydrolyzes oligopeptides such as neurotensin, bradykinin and dynorphin A. Acts as a regulator of cannabinoid signaling pathway by mediating degradation of hemopressin, an antagonist peptide of the cannabinoid receptor CNR1.
Catalytic Activity: Preferential cleavage in neurotensin: 10-Pro-|-Tyr-11.
Sequence Mass (Da): 80757
Sequence Length: 704
Subcellular Location: Mitochondrion
EC: 3.4.24.16
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Q9BT67 | MALALAALAAVEPACGSRYQQLQNEEESGEPEQAAGDAPPPYSSISAESAAYFDYKDESGFPKPPSYNVATTLPSYDEAERTKAEATIPLVPGRDEDFVGRDDFDDADQLRIGNDGIFMLTFFMAFLFNWIGFFLSFCLTTSAAGRYGAISGFGLSLIKWILIVRFSTYFPGYFDGQYWLWWVFLVLGFLLFLRGFINYAKVRKMPETFSNLPRTRVLFIY | Function: Activates HECT domain-containing E3 ubiquitin-protein ligases, including NEDD4 and ITCH, and consequently modulates the stability of their targets. As a result, controls many cellular processes. Prevents chronic T-helper cell-mediated inflammation by activating ITCH and thus controlling JUNB degradation (By similarity). Promotes pancreatic beta cell death through degradation of JUNB and inhibition of the unfolded protein response, leading to reduction of insulin secretion . Restricts the production of pro-inflammatory cytokines in effector Th17 T-cells by promoting ITCH-mediated ubiquitination and degradation of RORC (By similarity). Together with NDFIP2, limits the cytokine signaling and expansion of effector Th2 T-cells by promoting degradation of JAK1, probably by ITCH- and NEDD4L-mediated ubiquitination (By similarity). Regulates peripheral T-cell tolerance to self and foreign antigens, forcing the exit of naive CD4+ T-cells from the cell cycle before they become effector T-cells (By similarity). Negatively regulates RLR-mediated antiviral response by promoting SMURF1-mediated ubiquitination and subsequent degradation of MAVS . Negatively regulates KCNH2 potassium channel activity by decreasing its cell-surface expression and interfering with channel maturation through recruitment of NEDD4L to the Golgi apparatus where it mediates KCNH2 degradation . In cortical neurons, mediates the ubiquitination of the divalent metal transporter SLC11A2/DMT1 by NEDD4L, leading to its down-regulation and protection of the cells from cobalt and iron toxicity . Important for normal development of dendrites and dendritic spines in cortex (By similarity). Enhances the ubiquitination of BRAT1 mediated by: NEDD4, NEDD4L and ITCH and is required for the nuclear localization of ubiquitinated BRAT1 . Enhances the ITCH-mediated ubiquitination of MAP3K7 by recruiting E2 ubiquitin-conjugating enzyme UBE2L3 to ITCH (By similarity). Modulates EGFR signaling through multiple pathways. In particular, may regulate the ratio of AKT1-to-MAPK8 signaling in response to EGF, acting on AKT1 probably through PTEN destabilization and on MAPK8 through ITCH-dependent MAP2K4 inactivation. As a result, may control cell growth rate . Inhibits cell proliferation by promoting PTEN nuclear localization and changing its signaling specificity .
PTM: Ubiquitinated by NEDD4 and ITCH; mono-, di- and polyubiquitinated forms are detected. Ubiquitination regulates its degradation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24899
Sequence Length: 221
Domain: The PPxY motifs are required for E3 ubiquitin-protein ligase binding and activation and for ubiquitination.
Subcellular Location: Endosome membrane
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Q8R0W6 | MALALAALAAVEPACGSGYQQLQNEEEPGEPEQTAGDAPPPYSSITAESAAYFDYKDESGFPKPPSYNVATTLPSYDEAERTKTEATIPLVPGRDEDFVGRDDFDDTDQLRIGNDGIFMLTFFMAFLFNWIGFFLSFCLTTSAAGRYGAISGFGLSLIKWILIVRFSTYFPGYFDGQYWLWWVFLVLGFLLFLRGFINYAKVRKMPETFSNLPRTRVLFIY | Function: Activates HECT domain-containing E3 ubiquitin-protein ligases, including NEDD4 and ITCH, and consequently modulates the stability of their targets. As a result, controls many cellular processes. Prevents chronic T-helper cell-mediated inflammation by activating ITCH and thus controlling JUNB degradation . Promotes pancreatic beta cell death through degradation of JUNB and inhibition of the unfolded protein response, leading to reduction of insulin secretion . Restricts the production of pro-inflammatory cytokines in effector Th17 T-cells by promoting ITCH-mediated ubiquitination and degradation of RORC . Together with NDFIP2, limits the cytokine signaling and expansion of effector Th2 T-cells by promoting degradation of JAK1, probably by ITCH- and NEDD4L-mediated ubiquitination . Regulates peripheral T-cell tolerance to self and foreign antigens, forcing the exit of naive CD4+ T-cells from the cell cycle before they become effector T-cells . Negatively regulates RLR-mediated antiviral response by promoting SMURF1-mediated ubiquitination and subsequent degradation of MAVS (By similarity). Negatively regulates KCNH2 potassium channel activity by decreasing its cell-surface expression and interfering with channel maturation through recruitment of NEDD4L to the Golgi apparatus where it mediates KCNH2 degradation (By similarity). In cortical neurons, mediates the ubiquitination of the divalent metal transporter SLC11A2/DMT1 by NEDD4L, leading to its down-regulation and protection of the cells from cobalt and iron toxicity (By similarity). Important for normal development of dendrites and dendritic spines in cortex . Enhances the ubiquitination of BRAT1 mediated by: NEDD4, NEDD4L and ITCH and is required for the nuclear localization of ubiquitinated BRAT1 . Enhances the ITCH-mediated ubiquitination of MAP3K7 by recruiting E2 ubiquitin-conjugating enzyme UBE2L3 to ITCH . Modulates EGFR signaling through multiple pathways. In particular, may regulate the ratio of AKT1-to-MAPK8 signaling in response to EGF, acting on AKT1 probably through PTEN destabilization and on MAPK8 through ITCH-dependent MAP2K4 inactivation. As a result, may control cell growth rate (By similarity). Inhibits cell proliferation by promoting PTEN nuclear localization and changing its signaling specificity .
PTM: Ubiquitinated by NEDD4; mono-, di- and polyubiquitinated forms are detected. Ubiquitination regulates its degradation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24914
Sequence Length: 221
Domain: The PPxY motifs are required for E3 ubiquitin-protein ligase binding and activation and for ubiquitination.
Subcellular Location: Endosome membrane
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Q5U2S1 | MALALAALAAVEPACGTGYQQLQNEEEPGEREQTAGDAPPPYSSISAESAAYFDYKDESGFPKPPSYNVATTLPSYDEAERTKAEATIPLVPGRDEDFVGRDDFDDADQLRIGNDGIFMLTFFMAFLFNWIGFFLSFCLTTSAAGRYGAISGFGLSLIKWILIVRFSTYFPGYFDGQYWLWWVFLVLGFLLFLRGFINYAKVRKMPETFSNLPRTRVLFIY | Function: Activates HECT domain-containing E3 ubiquitin-protein ligases, including NEDD4 and ITCH, and consequently modulates the stability of their targets. As a result, controls many cellular processes. Prevents chronic T-helper cell-mediated inflammation by activating ITCH and thus controlling JUNB degradation. Promotes pancreatic beta cell death through degradation of JUNB and inhibition of the unfolded protein response, leading to reduction of insulin secretion. Restricts the production of pro-inflammatory cytokines in effector Th17 T-cells by promoting ITCH-mediated ubiquitination degradation of RORC. Together with NDFIP2, limits the cytokine signaling and expansion of effector Th2 T-cells by promoting degradation of JAK1, probably by ITCH- and NEDD4L-mediated ubiquitination. Regulates peripheral T-cell tolerance to self and foreign antigens, forcing the exit of naive CD4+ T-cells from the cell cycle before they become effector T-cells. Negatively regulates RLR-mediated antiviral response by promoting SMURF1-mediated ubiquitination and subsequent degradation of MAVS. Negatively regulates KCNH2 potassium channel activity by decreasing its cell-surface expression and interfering with channel maturation through recruitment of NEDD4L to the Golgi apparatus where it mediates KCNH2 degradation. In cortical neurons, mediates the ubiquitination of the divalent metal transporter SLC11A2/DMT1 by NEDD4L, leading to its down-regulation and protection of the cells from cobalt and iron toxicity. Important for normal development of dendrites and dendritic spines in cortex. Enhances the ubiquitination of BRAT1 mediated by: NEDD4, NEDD4L and ITCH and is required for the nuclear localization of ubiquitinated BRAT1. Enhances the ITCH-mediated ubiquitination of MAP3K7 by recruiting E2 ubiquitin-conjugating enzyme UBE2L3 to ITCH. Modulates EGFR signaling through multiple pathways. In particular, may regulate the ratio of AKT1-to-MAPK8 signaling in response to EGF, acting on AKT1 probably through PTEN destabilization and on MAPK8 through ITCH-dependent MAP2K4 inactivation. As a result, may control cell growth rate. Inhibits cell proliferation by promoting PTEN nuclear localization and changing its signaling specificity.
PTM: Ubiquitinated by NEDD4; mono-, di- and polyubiquitinated forms are detected. Ubiquitination regulates its degradation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24913
Sequence Length: 221
Domain: The PPxY motifs are required for E3 ubiquitin-protein ligase binding and activation and for ubiquitination.
Subcellular Location: Endosome membrane
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Q9NV92 | MARRRSQRVCASGPSMLNSARGAPELLRGTATNAEVSAAAAGATGSEELPPGDRGCRNGGGRGPAATTSSTGVAVGAEHGEDSLSRKPDPEPGRMDHHQPGTGRYQVLLNEEDNSESSAIEQPPTSNPAPQIVQAASSAPALETDSSPPPYSSITVEVPTTSDTEVYGEFYPVPPPYSVATSLPTYDEAEKAKAAAMAAAAAETSQRIQEEECPPRDDFSDADQLRVGNDGIFMLAFFMAFIFNWLGFCLSFCITNTIAGRYGAICGFGLSLIKWILIVRFSDYFTGYFNGQYWLWWIFLVLGLLLFFRGFVNYLKVRNMSESMAAAHRTRYFFLL | Function: Activates HECT domain-containing E3 ubiquitin-protein ligases, including ITCH, NEDD4, NEDD4L, SMURF2, WWP1 and WWP2, and consequently modulates the stability of their targets. As a result, may control many cellular processes. Recruits ITCH, NEDD4 and SMURF2 to endosomal membranes. Negatively regulates KCNH2 potassium channel activity by decreasing its cell-surface expression and interfering with channel maturation through recruitment of NEDD4L to the Golgi apparatus and multivesicular body where it mediates KCNH2 degradation . May modulate EGFR signaling. Together with NDFIP1, limits the cytokine signaling and expansion of effector Th2 T-cells by promoting degradation of JAK1, probably by ITCH- and NEDD4L-mediated ubiquitination (By similarity).
PTM: Ubiquitinated by NEDD4 and ITCH. Also ubiquitinated by NEDD4L. Ubiquitination by NEDD4 or NEDD4L does not affect turnover (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36390
Sequence Length: 336
Domain: The PPxY motifs are required for E3 ubiquitin-protein ligase activation and for ubiquitination.
Subcellular Location: Endosome membrane
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Q90932 | MYSPYCLTQDEFHPFIEALLPHVRAFSYTWFNLQARKRKYFKKHEKRMSKEEERAVKDELLGEKPEVKQKWASRLLAKLRKDIRPECREDFVLSVTGKKAPCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGVPLESTDGERLAKAPQCASPGLCVQPHHIGVTIKELDLYLAFFVQAPDSGQSDSSNPQGDADIKPLPNGHLSFQDCFVTSGVWNVTELVRVSQTPVATASGPNFSLADLESPGGYYNISPVTLGRRPLGPPTASGPKRPKALDEGDLEGPGDDVFYSGPGRSPAPGSSQGPWGGDVDTSPATLKKSGKLDFCSALSGHAASPRMAFGHHPLPVLAGVRPASALHFPSGSLLPQSGPYFAHPTIRYHHGQDSLKDFVQFVCADGAAQGPQHSQRPAPPLPPALSASDPATATF | Function: Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication.
Sequence Mass (Da): 46903
Sequence Length: 431
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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P70257 | MYSPYCLTQDEFHPFIEALLPHVRAFSYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLGEKPEIKQKWASRLLAKLRKDIRPEFREDFVLTITGKKPPCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLYKSPQCSNPGLCVQPHHIGVTIKELDLYLAYFVHTPESGQSDSSNQQGDADIKPLPNGHLSFQDCFVTSGVWNVTELVRVSQTPVATASGPNFSLADLESPSYYNINQVTLGRRSITSPPSTSSTKRPKSIDDSEMESPVDDVFYPGTGRSPAAGSSQSSGWPNDVDAGPASLKKSGKLDFCSALSSQGSSPRMAFTHHPLPVLAGVRPGSPRATASALHFPSTSIIQQSSPYFTHPTIRYHHHHGQDSLKEFVQFVCSDGSGQATGQPNGSGQGKVPGSFLLPPPPPVARPVPLPMPDSKTTSTAPDGAALTPPSPSFTTTGASSANRFVGIGPRDG | Function: Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication. Isoform NFIX1 acts as a transcriptional activator while isoform NFIX3 acts as a repressor.
Sequence Mass (Da): 53394
Sequence Length: 488
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular Location: Nucleus
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Q9YES5 | MNRREVRCAFSASKAARAQLLLRGKVRLEPLPTRPRTVLGLDASYSAKDGVGVGAAVLISLETLEPVDCRVYISRVCIPYIPGLLAFRELAVMAPAAAALSAEADVVMVDGHGIAHPRRFGIASHVGVILERPSIGVAKKKLVGTLVEGPGGMYVVQDGERLAIVLGTRPREVYVSPGHRITLEEAASIARATIRPGGWMPEPTRLADVISKALKTIIGGQSLINSALASLCRVKLGPRLEELERPLRRAGLEVE | Function: DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA.
Catalytic Activity: Endonucleolytic cleavage at apurinic or apyrimidinic sites to products with a 5'-phosphate.
Sequence Mass (Da): 27258
Sequence Length: 255
Subcellular Location: Cytoplasm
EC: 3.1.21.7
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Q0A5M1 | MGVSIRALHPWAVDAAEGRRLQQTLREQLCLKTPRGFRPRLVAGVDAGVVDGGRTIRAAVVVMSLPDLAVVTQSVARAPAIMPYVPGLLSFRELPGVVRALEQLDVTPELLLCDGQGIAHPRRLGIAAHLGLITDLPAIGVGKSRLVGTYREPRPEKGATSGLYDGHERIGTVLRSRDHVRPLYVSPGHRISHEDAVHWVLTCCTRYRLPEPQRAADRLASAKEAPA | Function: DNA repair enzyme involved in the repair of deaminated bases. Selectively cleaves double-stranded DNA at the second phosphodiester bond 3' to a deoxyinosine leaving behind the intact lesion on the nicked DNA.
Catalytic Activity: Endonucleolytic cleavage at apurinic or apyrimidinic sites to products with a 5'-phosphate.
Sequence Mass (Da): 24621
Sequence Length: 227
Subcellular Location: Cytoplasm
EC: 3.1.21.7
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P29378 | MTAHNPVQGTLPRSNEEIAARVKAMEAILVDKGLISTDAIDHMSSVYENEVGPQLGAKIVARAWVDPEFKQRLLTDATSACREMGVGGMQGEEMVVLENTGTVHNMVVCTLCSCYPWPVLGLPPNWYKYPAYRARAVRDPRGVLAEFGYTPDPDVEIRIWDSSAELRYWVLPQRPAGTENFTEEQLADLVTRDSLIGVSVPTTPSKA | Cofactor: Binds 1 Co(3+) ion per subunit.
Function: NHase catalyzes the hydration of various nitrile compounds to the corresponding amides.
Catalytic Activity: an aliphatic amide = a nitrile + H2O
Sequence Mass (Da): 22848
Sequence Length: 207
EC: 4.2.1.84
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A8EUK5 | MVKKYKVIDNFISKEALSGILLLFVTLFAIIVANSNFGDFYFNLWDKPLGVAIGDFIISMPLRLWINDGLMALFFLMVSLEIKRELLIGELASVSRAMFPFVASLGGMIVPASIYIALNPDNFIGFGIPMGTDTAFAIAMLILLGKRVNTALKLFLVALAVIDDLGAIIVVATVYTSELKLEYFLHAAFVYGLIWLLNYFDVKKLSFYLFLGIFLWIFIHETGVHATIAGVLLAFAIPISSRMNEKKFIEKTKADLEEFERCMDDKPILNHRQINALEGIAYGYDRVQNPLIRLEHDLHGFSAFFIMPIFAFSNAGVLLDFSTVWTNWMIVLGVALGLLVGKPLGIFGFTYAATKLNIIKKPKNISWFEIISVGFIAGIGFTMSIFIANLAFIDEDTISAIKIGIFTASFMATVIGMILISINYKFKISKA | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48002
Sequence Length: 431
Subcellular Location: Cell inner membrane
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A0RMW2 | MNIIKNFLQKESASGILIILAMILALILANNGVLNKFYSEILRLDSGIIFGEFKLIKPTILWVNDGLMAIFFFFIGLELKYEFLEGELNSISKVALPSIAGIGGVIVPAVIFYVLNHANRFDVNGWAIPTVSDTAFALAVLFLLGSRIPISLKLFLLSLAIIDDVAAIIIIAIFYTKTLSIISLFISFCAIVILTILNYKNNQNIYIYLLCGIVLWVSVLMSGIHATLAGIIASMFIPLRDEDGDPEHGMLQSVMHFLHPIVAFLILPIFAFSNAGVVFSEDSILNLTHPVPLGIIFGLFIGKQIGVFSFAFLAIKCKLAELPNGCGWLHLYGLSILTGVGMSMSLFIDGLAYAESDAFLYANKIAILLASTMCAVTGYFVLRKASKSQN | Function: Na(+)/H(+) antiporter that extrudes sodium in exchange for external protons.
Catalytic Activity: 2 H(+)(out) + Na(+)(in) = 2 H(+)(in) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42590
Sequence Length: 390
Subcellular Location: Cell inner membrane
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