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stringlengths 6
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stringlengths 11
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stringlengths 108
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Q9GZQ4 | MSGMEKLQNASWIYQQKLEDPFQKHLNSTEEYLAFLCGPRRSHFFLPVSVVYVPIFVVGVIGNVLVCLVILQHQAMKTPTNYYLFSLAVSDLLVLLLGMPLEVYEMWRNYPFLFGPVGCYFKTALFETVCFASILSITTVSVERYVAILHPFRAKLQSTRRRALRILGIVWGFSVLFSLPNTSIHGIKFHYFPNGSLVPGSATCTVIKPMWIYNFIIQVTSFLFYLLPMTVISVLYYLMALRLKKDKSLEADEGNANIQRPCRKSVNKMLFVLVLVFAICWAPFHIDRLFFSFVEEWSESLAAVFNLVHVVSGVFFYLSSAVNPIIYNLLSRRFQAAFQNVISSFHKQWHSQHDPQLPPAQRNIFLTECHFVELTEDIGPQFPCQSSMHNSHLPAALSSEQMSRTNYQSFHFNKT | Function: Receptor for the neuromedin-U and neuromedin-S neuropeptides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47696
Sequence Length: 415
Subcellular Location: Cell membrane
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Q8BZ39 | MGKLENASWIHDSLMKYLNSTEEYLAYLCGPKRSDLSLPVSVVYALIFVVGVIGNLLVCLVIARHQTLKTPTNYYLFSLAVSDLLVLLLGMPLEVYELWHNYPFLFGPVGCYFKTALFETVCFASILSVTTVSIERYVAIVHPFRAKLESTRRRALRILSLVWSFSVVFSLPNTSIHGIKFQQFPNGSSVPGSATCTVTKPIWVYNFIIQATSFLFYILPMTLISVLYYLMGLRLKRDESLEADKVTVNIHRPSRKSVTKMLFVLVLVFAICWTPFHVDRLFFSFVDEWTESLAAVFNLIHVVSGVFFYLSSAVNPIIYNLLSRRFRAAFRNVVSPSCKWCHPQHRPQGPPAQKVIFLTECHLVELTEDAGPQFPCQSSIHNTQLTTVPCVEEVP | Function: Receptor for the neuromedin-U and neuromedin-S neuropeptides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44827
Sequence Length: 395
Subcellular Location: Cell membrane
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B2KES3 | MKTVTSQKMRELETAAVKEFGIDEDVLMEHAGRSAAEEILNCFLSENKEKKVIIVCGHGGNGGDGLVCGRYLMERGVDVYCYIIPPFQGSYKGLVLKNLKRAFFSHLSVKEIYQNLSDLKNSVADAYIVIDALLGIGFKGEVKKNYKETIEVLNSSPSIKIAFDIPSGLNADSGQNEGAVFKADYTYAMGFAKQGCLKAKDICGEIKVLNIGLPKELLSKV | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 24171
Sequence Length: 221
EC: 5.1.99.6
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C4M2B8 | MQYLTQEQAIKLDEELMGKYKYSLVQLMEIAGLAVAQVVTKEYPIEKGNKRVLILCGPGNNGGDGLVCGRYLSLFGYEVTVFYPKQSKNEHLQLLIKQLEIQDIPVVTELSSFEYDAIVDAVFGFSFKGPVRGIFKDIFSHINSLKVPIISVDIPSGWDVEQGYLQDGIQRCDVLISLSAPKLGVKNFKGIHYLGGRFIPLELKDKLHLILPYKENELIVKIN | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 25079
Sequence Length: 223
EC: 5.1.99.6
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B0RZQ3 | MIYVTAEQMRQIDHYTIHEIGIPSIVLMENAKAQISKHILDKNFSKAYVFASVGNNGGDGLAVARDIYNAKKYVKVYVIGKLEKASTDFKINYDILKKLDVEIEFVDENTKFDITENDLIVDSIFGTGLKRDIEGIYKGVIDMINDSQAFVVSVDMPSGLDSDENKIHNVAVKADLLVTLQLPKKSLQDYEGEYVVEPIGIPEKSIKHVLNNAS | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 23914
Sequence Length: 214
EC: 5.1.99.6
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C7Z508 | MAIKTLGAKAAAALDQELMSTGAFSIDQLMELAGLAVSQAVYRLQPLESGRRILVACGPGNNGGDGLVAARHLRHYGYNPTVFYPKRSKNDLYQRLAKQLEDLDVPFVDDFSSAVSSTDHIVDAIFGFSFSGEVREPFPAVIQALQETKLPVTSVDAPSSWDIENGPPESGLGSSFMPTALVSLTAPKPLVNHFRGRHFIGGRFVTPAIASKYGFEVPEYKGIDQVVEVETTGQKL | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 25471
Sequence Length: 236
Subcellular Location: Cytoplasm
EC: 5.1.99.6
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A8BQZ5 | MQQAQQKPFIPTIPAYQALKLDEDLINKCNYSIEQLMEIAGTAVAQATTHYIESTSSVSKAGVLVVCGPGNNGGDGLVAARHLSSGSMSSATVRVWLPKEPSSSVNKRMLSIAKHAGVVFIKDTNEEALHAILEFINSCESFYLVDAIFGFSFHGGPIKPPYDTVINTLLQMQTSMAIGPKTRIVSVDVPSGWSVDAQEWGLNTDKELIPDGLLRPDALISLTVPKNCSLWLPPGTAHYLGGNFLTPLLAMEYDVQEIQHYWSGVSSLFVVLS | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX (By similarity).
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 29580
Sequence Length: 273
EC: 5.1.99.6
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Q8NCW5 | MSRLRALLGLGLLVAGSRVPRIKSQTIACRSGPTWWGPQRLNSGGRWDSEVMASTVVKYLSQEEAQAVDQELFNEYQFSVDQLMELAGLSCATAIAKAYPPTSMSRSPPTVLVICGPGNNGGDGLVCARHLKLFGYEPTIYYPKRPNKPLFTALVTQCQKMDIPFLGEMPAEPMTIDELYELVVDAIFGFSFKGDVREPFHSILSVLKGLTVPIASIDIPSGWDVEKGNAGGIQPDLLISLTAPKKSATQFTGRYHYLGGRFVPPALEKKYQLNLPPYPDTECVYRLQ | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX. Accelerates cholesterol efflux from endothelial cells to high-density lipoprotein (HDL) and thereby regulates angiogenesis .
PTM: Undergoes physiological phosphorylation during sperm capacitation, downstream to PKA activation.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 31675
Sequence Length: 288
Subcellular Location: Mitochondrion
EC: 5.1.99.6
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E8R1E4 | MIRGRKRDGTVHARPDVCLSSMDDFFLRKPPAMDESPRLRPLSRAEARNLDLRAVRELGLPTLVLMENAGRSAARWFLEDWLSQGKGNLTDHKVLILCGPGSNGGDGGVMARWLDLAGVLVRVAWVSGPVPRLPAGDAAIQRDALAKAGFDQQDWVLPEDNAKLAKSLSWCTWVVDALLGTGLTRPIDGAFRTAVEMINDSGKPVYALDLPSGLDADTGEPLGVALRATATATFVAPKLACQYKEAEEYLGEVAVLPIGLPYALLEDYIEED | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 29448
Sequence Length: 272
EC: 5.1.99.6
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B7QDG3 | MEKSEKKPMRFSFRRRPKSVSVDRSEAHAADVSIGQYLEKLNYVSQEEAIKIDQELFSEYAYSVDQLMELAGLSVATAVAKSYPRGPMPKGGTVLVCCGPGNNGGDGLVCARHLKLFGYEPSVFYPKQSNKPLFQNLTKQCQEMEVPFLSFLPDSQLVSDSYNLVVDALFGFSFKPPVRPEFNDVMDKLKKVKIPVVSIDIPSGWDVETGGDADSLQPECLVSLTAPKRCSRNFKGRFHWLGGRFVPPALAAKYELNLPPYPGTDCCLLLTPPPS | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 30463
Sequence Length: 275
EC: 5.1.99.6
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Q5ZRQ9 | MDYYFTKGKPQLVNMKTPVYLVTQFQQLMDLMQNQYQVSCLELMQRSGKAACDFLVYRWPKVKKISIFCGRGDNGGQGYVLAQQAKKMGMIPTVWQVGHQMSMSKPPQMHEEVWYEMNSCHQQGILLHTYSPDIDLGDPELIVDALFGVGLYGHVRPEIASLLQRLQQFTVPILAIEVPTGINASTGEIAGNALAATATITFLCMKLGLLINDGKIYSGEIAFDDLLAPEAIYQQVKGIEKSSLLDSSTCFSKKIWYRNKTQKGWQLSIN | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 30300
Sequence Length: 270
EC: 5.1.99.6
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F4FTW6 | MTQAITVEESRELDDKTINKIGIPSLVLMERAGLKIYENMLDNKDLDLSNVLILAGTGNNGGDGLVVARLLATHGYQVSILTVGNPDHASEDHLAQARICNYYQIPKVFMNADFNKFTTLVDALFGSGLSRNVGGDFATIIDKANASTAKIHAIDIPSGLNGDTGDVMGTAIKAISTSTVAYPKVGMLKDQAKPYTGKIYVDDIGIYRGNAFENE | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 23070
Sequence Length: 215
EC: 5.1.99.6
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B1MW95 | MQLVTAAEMQQIDSYTIETIGMPQNVLIERAAMSVIDVIGAGHFNLDHILVLAGLGNNGADGIAIARLLYTQGFNVSLQFVGNVSRAKASVQQQLQIIENYGLIRAEKSDFNEATLIVDAIFGVGLNNTLPEGLQKMIKAANHIEKTVIAVDIPTGIDATTGEVRGAALKAHTTVTFGYNKVGLTQNVGGYLSGNVIVKDIGLRLPEDFTFTTVTPDNIATT | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
Catalytic Activity: (6R)-NADHX = (6S)-NADHX
Sequence Mass (Da): 23656
Sequence Length: 222
EC: 5.1.99.6
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A8JQX3 | MDQKTTGLRENYGHRRQPALGKAMPVTALLLNLESNPLDYSRNDIGAELLEDDDKPPQLFSVTDEPPSPNEEDYKPPNHHEDDGKLAGERHREIPCSNCLKTAPGHLIDRQSAINEMCQRLCGPECRRPQGLTLDGVRQDFLRQYEIAEAVAKTSAMTSTVQMKQRLAARKLEFEKEMEMDEQLGVASPRNDINLGQSSTVAATGMGEFEFEPPRDLLLYLVRMGSFNSAPKINNVDSQDDGLVLPSGLSTPALLQHVQQLRGGGIEQPSLLTRGFLKPLLADEDVADGLRCLKLNSVSRVCSAPVEGDDIRLLQWNILSQTLGQHNDGFVRCPEEALTWEHRKYLIVQEILQNQPDVICLQEVDHFKFLQTVLGSQNYAGIFFPKPDSPCLYIEQNNGPDGCAIFYKRDKLQLQGYDTRILEVWRVQSNQVAIAARLRMRSSGREFCVATTHLKARHGALLAKLRNEQGRDLIRFVKQFAGDTPLLLCGDFNAEPVEPIYATILGCDLLRLGSAYADVKLDREEILHPNADVGEFVAKSMKREPPYTTWKIREEGEECHTIDYVFYTPDRLKIKNCLDFPAGEQIGKNRTPSFQYPSDHFSLVCDFELLPPTENGKESGSGSGSDGENETEVEGSKHGSIQ | Cofactor: Binds 2 magnesium ions, but the ions are only loosely bound to the protein.
Function: Phosphatase which catalyzes the conversion of NADP(+) to NAD(+) and of NADPH to NADH . Shows a small preference for NADPH over NADP(+) . Because of its association with the CCR4-NOT complex, has a role in mRNA deadenylation and decay . Required at the pupal stage for proper wing morphogenesis after eclosion .
Catalytic Activity: H2O + NADP(+) = NAD(+) + phosphate
Sequence Mass (Da): 71880
Sequence Length: 642
Subcellular Location: Cytoplasm
EC: 3.1.3.-
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O35710 | MYQSPRRLCSALLLRDAPGLRRTLVPGPRRTLAPPVLGSRPKSPQLQAAAASGAARSRPRTVSSMGNGTSRLYSALAKTVNSSAAAQHPEYLVSTDPEHLEPIDPKELLEECRAVLHTRPPRYQRDFVDLRTDCSSSHSPIRVMQWNILAQALGEGKDNFVQCPVEALKWEERKCLILEEILAYQPDILCLQEVDHYFDTFQPLLSRLGYQGTFFPKPWSPCLDVEHNNGPDGCALFFLQNRFKLISSTNIRLTAMTLKTNQVAIAQTLECKESGRQFCIAVTHLKARTGWERFRSAQGCDLLQNLQNITQGAKIPLIVCGDFNAEPTEEVYKHFASSSLNLNSAYKLLSPDGQSEPPYTTWKIRTSGECRHTLDYIWYSRHALSVTSALDLLTEEQIGPNRLPSFHYPSDHLSLVCDFSFNEEPHELF | Cofactor: Binds 2 magnesium ions, but the ions are only loosely bound to the protein.
Function: Phosphatase which catalyzes the conversion of NADP(+) to NAD(+) and of NADPH to NADH (By similarity). Shows a small preference for NADPH over NADP(+) (By similarity). Represses translation and promotes degradation of target mRNA molecules (By similarity). Plays an important role in post-transcriptional regulation of metabolic genes under circadian control . Exerts a rhythmic post-transcriptional control of genes necessary for metabolic functions including nutrient absorption, glucose/insulin sensitivity, lipid metabolism, adipogenesis, inflammation and osteogenesis . Plays an important role in favoring adipogenesis over osteoblastogenesis and acts as a key regulator of the adipogenesis/osteogenesis balance . Promotes adipogenesis by facilitating PPARG nuclear translocation which activates its transcriptional activity . Regulates circadian expression of NOS2 in the liver and negatively regulates the circadian expression of IGF1 in the bone . Critical for proper development of early embryos .
Catalytic Activity: H2O + NADP(+) = NAD(+) + phosphate
Sequence Mass (Da): 48301
Sequence Length: 429
Subcellular Location: Cytoplasm
EC: 3.1.3.108
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P79942 | MDAQLTYTMGLLEQGYLSARVCSMGNSTSRLYSALAKTLSSSAAVSQELLEASQHDQSEPLDPKELLDECQVALQDRPARLHRDFFSLRSESSSQQPRTFRVMQWNILAQALGEGKDNFIMCPMEALKWEERKYLILEEILMYQPDVLCLQEVDHYFDTFQPILSRLGYQCTFLAKPWSPCLDVEHNNGPDGCALFFLQDRFQLVNSAKIRLSARTLKTNQVAIAETLQCCETGRQLCFAVTHLKARTGWERFRLAQGSDLLDNLESITQGATVPLIICGDFNADPTEEVYKRFASSSLNLNSAYKLLSEDGESEPPYTTWKIRTTGESCHTLDYIWYSQHALRVNAALGLPTEEQIGPNRLPSFNYPSDHLSLVCDFSFNEDPARLL | Cofactor: Binds 2 magnesium ions, but the ions are only loosely bound to the protein.
Function: Phosphatase which catalyzes the conversion of NADP(+) to NAD(+) and of NADPH to NADH (By similarity). Shows a small preference for NADPH over NADP(+) (By similarity). Component of the circadian clock or downstream effector of clock function . Exhibits a high amplitude circadian rhythm with maximal levels in early evening . In constant darkness or constant light, the amplitude of the rhythm decreases .
Catalytic Activity: H2O + NADP(+) = NAD(+) + phosphate
Sequence Mass (Da): 43941
Sequence Length: 388
Subcellular Location: Cytoplasm
EC: 3.1.3.-
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A9N0D9 | MSILVKNNIHWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRSEIDLADIDYIIINHAEEDHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWNFKVVKTGDTLDIGNGKQLIFVETPMLHWPDSMMTYMTGDAVLFSNDAFGQHYCDERLFNDEVDQTELFEQCQRYYANILTPFSRLVTPKITEILGFNLPVDMIATSHGVVWRDNPTQIVELYLKWAADYQEDRITIFYDTMSNNTRMMADAIAQGINEVDPNVAVKIFNVARSDKNEILTNVFRSKGVLVGTSTMNNVMMPKIAGLVEEMTGLRFRNKRASAFGSHGWSGGAVDRLSTRLQDAGFEMSLSLKAKWRPDLDALELCRQHGRDIARQWALAPLPETTQKTAPVEETTTCAAADLGPKMQCSVCQWIYDPALGEPLQDVAPGTPWSDVPDNFLCPECSLGKDVFDVLATEAK | Cofactor: Binds 3 Fe cations per monomer.
Function: Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron center; electrons enter from the NorW at rubredoxin and are transferred sequentially to the FMN center and the di-iron center. Also able to function as an aerobic oxygen reductase.
Sequence Mass (Da): 54136
Sequence Length: 479
Pathway: Nitrogen metabolism; nitric oxide reduction.
Subcellular Location: Cytoplasm
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A0A0B4KGY6 | MESIMKVAMDKAAEQLIQQFGFDYLQQQLQLQHQNQHNSSPQQPQHQQLEPENEHLTYQYQQSKPTHMQQLACNYQPRHSTTTSSPSSTHSLASGGGSSSNSSNSSSSDSSSINISHISNISNISNIGNISNSNHSNAAYSLAVHSYQKQIESPANPSHVPHHQMDLSPLSENGSPNGTPGAQTPTATASGNTAAALASAAAAAAAATSGGNGSSITNCNSNNSSSSSNAQQQLQLGNYKTNSCWCYGESVCSGIEVEIENNNNNHIHHGETTYHMKILVPAVASGAIIGKGGETIASLQKDTGARVKMSKSHDFYPGTTERVCLITGSTEAIMVVMEFIMDKIREKPDLTNKIVDTDSKQTQERDKQVKILVPNSTAGMIIGKGGAFIKQIKEESGSYVQISQKPTDVSLQERCITIIGDKENNKNACKMILSKIVEDPQSGTCLNVSYADVSGPVANFNPTGSPYATNQNAINSSTASLNSTLGTTIGGANSAASLLVNGTGINLSINLGSPNPAPNLAVATQLLEHIKVAMRGSGYSETVTNEVVAALSVLAKYGVLGMGVGVSHTNGAHSTLGNFLGVTTLDQQTAAAASAATASNVFGAVGQVNLEQYAAAVASAAAASRPTQSQLDAAAVQFDPFRHLGSATAPAATPVSLNNNSFGLTATTGTATTAQLGGLSKSPTPGDLSSKDSKNVEVPEVIIGAILGPSGRSLVEIQHVSGANVQISKKGIFAPGTRNRIVTITGQPSAIAKAQYLIEQKINEEETKRARQIPLTTVVN | Function: Functions to regulate alternative splicing in neurons by binding pre-mRNA in a sequence-specific manner to activate exon inclusion (By similarity). Plays a role in long-term memory formation by processing the unspliced Orb2-isoform A (Orb2A) mRNA and thereby controlling Orb2A protein abundance .
Sequence Mass (Da): 81403
Sequence Length: 780
Domain: The KH domain consists of approximately 70 amino acids and includes a conserved hydrophobic core, an invariant Gly-X-X-Gly motif, and an additional variable segment. The third KH domain (KH3) binds a hairpin RNA loop containing the 5'-UCAY-3' motif on targeted molecules. RNA binding by KH3 requires residues C-terminal to the KH domain.
Subcellular Location: Nucleus
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Q9L9G2 | MRTAVIIGTGMIGTSIGLALRKQGVDSYLMDTSPVALRIAEAVGAGTAEEPPETVDLAVVAVPPVHVAPVIASHQSRGTARFYVDVAGVKVSTRRELDALGCDLATVVGGHPLVGRPGSGPLAARGDLFDGRPWALVPAVGTDAAALNRALELVAACGAIPVVLDAEAHDRAIALGTLVPQIALTLVAARLTEADSGALRLLGSVWSEIPQLVGVDSATSWTQVLAANAAPVVGELEKLSRDLASLLETLRGVADGDGSLAEPDGRLLEFIQRGIDGSNRVPGRYGIPTETALADVDVSVDDRPAELARLFDDVAGAGVVMRGIDISQRPDSPDRTVTISVTPRDAENLLHELRRRKWPANS | Function: Probable prephenate dehydrogenase that produces 4-hydroxyphenylpyruvate (4HPP) in the novobiocin biosynthesis pathway. Novobiocin is an aminocoumarin family antibiotic that targets bacterial DNA gyrases.
Catalytic Activity: NAD(+) + prephenate = 3-(4-hydroxyphenyl)pyruvate + CO2 + NADH
Sequence Mass (Da): 37636
Sequence Length: 362
Pathway: Antibiotic biosynthesis; novobiocin biosynthesis.
EC: 1.3.1.12
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Q9L9G0 | MFNTRANKASDQSPTIPTESATLAELWERTVRSRPSSPAIVTNGETLSYDEVNARANRLARLLLDEGAGPGRLVALALPRSSHLVISVLAVAKAGAVFLPLDVNHPRERLSYQLADARPALLCTVRSAAARLPDGIEMPRVLLDSPERTAVLDALPDTDLTDDERGGPLAATDLAYVIYTSGSTGRPKGVALTGAGLPALAAAKVAAMRVTGDSRVLQFASPGFDAYLTELLAAFTAGATLVVPGTDTLAGDPLRRALRDGRVSHAVLPPAAVATMSPDAVPDLRVLVVAGEACPAGLVERWAPGRLLINAYGPTECTVCATMTGPLTPTDEVTIGRPIPGVSVYILDAERRPAAPGEIGELYLSGAGLAQGYLNSPDLTAQMFVPNPFAADGERMYRTGDLASRRADGDILFHGRIDDQVELRGFRVELGEVESVLSQHPDVAQAVAALWTDPAEGPQLVTYVVPAPGTTPSAGELREHAGRFLPDFMVPSAFTTIDAVPLTPGGKTDRAGLPDPVKATQPAGLGPRTPAEKVLCDIFRDLFDLVEIDVRSNFFEMGGNSILAVDLIQRAQEAGLTLMPRTVIDHPTIEQLAAIATLEE | Function: Together with NovI, involved in the formation of a beta-OH-Tyr intermediate in the novobiocin biosynthesis pathway, an aminocoumarin family antibiotic that targets bacterial DNA gyrases. The ATP-dependent AMP-binding region activates L-Tyr as L-tyrosyl-AMP and then transfers the L-tyrosyl group to the acyl carrier domain through thioester formation to form a tyrosyl-S intermediate that is covalently tethered to NovH (L-Tyr-S-NovH).
Sequence Mass (Da): 63315
Sequence Length: 600
Pathway: Antibiotic biosynthesis; novobiocin biosynthesis.
EC: 6.-.-.-
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Q9L9F9 | MSTRPTVSPSELEQIDLASPVLHAEYELDEIFRHLRADEPVYWQQPRNEQPGFWVISRHADVNEVYKDKEHFTTEHGNALATLLTGGDSASGAMLAVTDGVRHHQVRNVLSRGFSARMLDLIAHTLQETVDGLLLAALERGECDAAQDIAADVPLGAICDLLEIPHADRKYLLGLTSHAWSTDYADEPPEESWVAKNEILLYFSKLLKERRGGVREDMVSLLANCRIDGDPLKAAEQMANCYGLMIGGDETGRHAITGTILALIQNPDQWRALKNGDVDLNTATEEALRWTVPSLHGGRKATGDVVINGRRINAGDVVSVWISSANRDETVFDAPDEFNLARTPNKHFTFAYGSHYCLGHYLGRMEVYAVLDGLRRLVGDLEQIGEERWIYSSILHGMSSLPIRITG | Function: Together with NovH, involved in the formation of a beta-OH-Tyr intermediate in the novobiocin biosynthesis pathway, an aminocoumarin family antibiotic that targets bacterial DNA gyrases. Acts as a cytochrome P450-type monooxygenase with specificity for the tyrosyl-S-NovH acyl enzyme (L-Tyr-S-NovH) to form the beta-OH-Tyr intermediate (L-beta-OH-Tyr-S-NovH).
Sequence Mass (Da): 45176
Sequence Length: 407
Pathway: Antibiotic biosynthesis; novobiocin biosynthesis.
EC: 1.14.-.-
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Q9L9F8 | MTSPADATTEVAVSQESVAMVTGAGRGIGAATAERLAAEGMAVIVVDRTEQDTRATVAAIRTAGGRARGIGCDVAVAQAVTAAVATAVEEFGRIDVLVNCAGINRDRLLLTMGDQEWDTVLDVNLGGTMRCSFAVGRHMRRQGHGRIINFSSVAARGNAGQTNYATAKGAIAGFTRTLAAELGPHGVTVNAIAPGFVATPMVDELAERLGGDRDSVMSEAAKSSAVGRIGTPEEIAATVVFVARPESGYLTGETVHVDGGRP | Function: Catalytic subunit of the NovJ(2)K(2) heterotetramer that catalyzes the NADPH-dependent reduction of the tyrosyl moiety of L-beta-OH-Tyr-S-NovH intermediate to yield the tethered beta-ketotyrosyl-S-NovH in the novobiocin biosynthesis pathway. Novobiocin is an aminocoumarin family antibiotic that targets bacterial DNA gyrases.
Sequence Mass (Da): 26850
Sequence Length: 262
Pathway: Antibiotic biosynthesis; novobiocin biosynthesis.
EC: 1.1.1.-
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Q9L9F6 | MANKDHAPEHYVTRILAEATLDGARPVVRWRDTVITGTQLDRSVRRVVTALREAGVARDHAVAVLTQVNSPWMLIVRYAAHLVGASVVYITGANHGIVTHELPVATRVRMLREAGASVLVFDESNAQLAETVDETVRDKLVLCGLGHPASGTVSVDGRPVDDVSVDFTPEAPELAMVLYTSGTTGQPKGVCRSFGSWNAAALRGAAYPRPVFLTMTAVSQTVAMIVDTVLAAGGSVLLRERFDPADFLRDVGEHRVTETFMGVAQLYAILGHPDARTADLSSLRHVLYLGCPASPERLREAAALLPGVLAQSYGSTEAGRITVLRAADHERPELLATVGRAVPGVTIAIRDPETGHDLPVGEIGEVVVHGPEVMAGYVADPEHTARVIRDGWVHTGDFGSVDERGYVRLFGRMREVVKVQDTRVSPTEVEKVLVGCPGVVDACVYGHRGPDLIEELHAAVVLGTEGAPSFDTLRDHVARAMTPTHAPIRFVRWRRFPINNTGKVNRLRVREVSAEARGDSPDVLVDR | Function: Catalyzes the formation of an amide bond between 3-dimethylallyl-4-hydroxybenzoate (ring A of novobiocin) and 3-amino-4,7-dihydroxycoumarin (ring B of novobiocin) in an ATP-dependent reaction in the novobiocin biosynthesis pathway. Novobiocin is an aminocoumarin family antibiotic that targets bacterial DNA gyrases.
Catalytic Activity: 3-amino-4,7-dihydroxycoumarin + 3-dimethylallyl-4-hydroxybenzoate + ATP = 8-desmethylnovobiocic acid + AMP + diphosphate
Sequence Mass (Da): 56921
Sequence Length: 527
Pathway: Antibiotic biosynthesis; novobiocin biosynthesis.
EC: 6.3.1.15
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Q9L9F5 | MRVLLTSLPGIGHLFPMVPLGWALQAAGHTVLVATDREFLPVVTGAGLSATAVLDPVDPVELFKPVEPFGDPLSPAERTGHRCAEAGVRALPAMRALVDVWHPDLVIAEPMELAGPAAATNAGVPWVRHSYGLIPPGPLLSVAAEVLDAELAVLGLSALAKPARTIDVCPDSLRPSDGVATVPMRYVPYNGPAGVPDWLLAGPPARPRVCLTLGTSLPRRDPHVAPLWRLLLDELVALGQEVVIAIDESHRPLLGHLPDGVRAARIPLCDLLPTCTAIVHHGGSGSTMAAASFGVPQLVVPHFADHFTNAERLTAVGAGLSLPHDTDDLARISAACELITGDGPHRAISRRLADENARRPTPAVVAEGLAAEQRSMTPA | Function: Catalyzes the transfer of L-noviose from dTDP-4-O-demethyl-beta-L-noviose to the phenolic oxygen of novobiocic acid, creating the full ABC ring system in the novobiocin biosynthesis pathway. Novobiocin is an aminocoumarin family antibiotic that targets bacterial DNA gyrases. Also shows activity with variant coumarin aglycones, suggesting it may be a promiscuous catalyst for noviosylation of a range of planar scaffolds. Does not show activity with TDP-L-rhamnose.
Catalytic Activity: dTDP-4-O-demethyl-beta-L-noviose + novobiocic acid = desmethyldescarbamoylnovobiocin + dTDP + H(+)
Sequence Mass (Da): 39698
Sequence Length: 379
Pathway: Antibiotic biosynthesis; novobiocin biosynthesis.
EC: 2.4.1.302
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Q9L9F4 | MLILGLNGNVSAAGADVVPNLNELYMHDAAATLVRDGVLVAAVEEERLNRIKKTTKFPSNAIRECLAAAGAKPADVDAIAYYFPEDFFDDIFQQLYTEHPSVPTRYSREMILERLRVDLGWAAPPDILHYVPHHLAHAMSTYYRSGMREALVVVMDGAGERNCTTIYRSDGAELFEIASYPVPKSLGMFYLYGTRHLGYGFGDEYKVMGLAPYGDPSTYRDVFSTLYSLGPNGTYELIPRGGVVFRMTTILREHGLQPRRRGEPFTQAHMDFAASVQETTEQIAMHVIGYWARSTGLRNLAFGGGVAHNSTLNGRILTSGLFDEVFVHPASHDAGSSEGAALVVARERGERVWPLPRLTNASLGPDLGDVDSLERTLKSWSPLVDVERPDDIVEATAHLLAAGEAIGWAHGRSEFGPRALGNRSILADARPKENQTRINAMVKKRESFRPFAPVVTAEAAGDYFDLPETVGHHDFMSFVVQVRADRRELLGAVTHVDGSARVQVVTEETNPRFHRLVTRFGELTGTPVLLNTSFNNHAEPIVQSVDDVLTSYLTTSLDVLVIEDFVVRRRTELPLALEDFTIGFRPVTRLVRRLADVSAGRPGAPEVSHEIYLDHTSGPRATISAAMYELLTHADGVTPLGSLGIELTGELLTELYDLWQGRFVTVAPVGDGAGSAP | Function: Carbamoyltransferase that mediates 3'-carbamoylation of the noviosyl ring to produce novobiocin, the final step in the novobiocin biosynthesis pathway. Novobiocincin is an aminocoumarin family antibiotic that targets bacterial DNA gyrases.
Catalytic Activity: carbamoyl phosphate + descarbamoylnovobiocin = novobiocin + phosphate
Sequence Mass (Da): 74340
Sequence Length: 677
Pathway: Antibiotic biosynthesis; novobiocin biosynthesis.
EC: 2.1.3.12
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Q9L9F2 | MAPIVETAKETNSDSSLYLDLMIKVLAGTVYEDPAHRENFSHRDSTYREEVRNEGRDWPANAHTMIGIKRLENIRQCVEDVIGNNVPGDLVETGVWRGGACILMRGILRAHDVRDRTVWVADSFQGIPDVGEDGYAGDRKMALHRRNSVLAVSEEEVRRNFRNYDLLDEQVRFLPGWFKDTLPTAPIDTLAVLRMDGDLYESTWDTLTNLYPKVSVGGYVIVDDYMMCPPCKDAVDEYRAKFDIADELITIDRDGVYWQRTR | Function: S-adenosyl-L-methionine-dependent O-methyltransferase that methylates at 4-OH of the noviose moiety, the penultimate step in the novobiocin biosynthesis pathway. Novobiocin is an aminocoumarin family antibiotic that targets bacterial DNA gyrases.
Catalytic Activity: desmethyldescarbamoylnovobiocin + S-adenosyl-L-methionine = descarbamoylnovobiocin + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 29967
Sequence Length: 262
Pathway: Antibiotic biosynthesis; novobiocin biosynthesis.
EC: 2.1.1.285
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Q9L9E8 | MRILVTGGAGFIGSEFVRATLRGTLPGSSGTQVTVLDKLTYSGNVLNLAPIADLRNYRFVRGDICDQDLVDDVVAGHDAIVHFAAETHVDRSIGSAASFVRTNAMGTQVLLEAASRHRLGRFVHISTDEVYGSIPEGAWDEESPVAPNAPYAAAKAAGDLLALAWHRTHGLDVVVTRCTNNYGPYQYPEKLIPLFTTNVMDGQQVPVYGEGHNRRQWLHVSDHCRAIQLVLLGGRAGEVYHIGGGTELTNLELAEQILKSCGAGWDMVRHVPDRPGHDFRYSLDTTKIRTELGFSPRVAFADGLVETVEWYRDNRAWWEPLKSPDEATGSPGDAGR | Cofactor: Binds 1 NAD(+) per subunit.
Function: dTDP-glucose 4,6-dehydratase involved in the generation of the deoxysugar in the novobiocin biosynthesis pathway, an aminocoumarin family antibiotic that targets bacterial DNA gyrases.
Catalytic Activity: dTDP-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-alpha-D-glucose + H2O
Sequence Mass (Da): 36731
Sequence Length: 336
Pathway: Antibiotic biosynthesis; novobiocin biosynthesis.
EC: 4.2.1.46
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P55209 | MADIDNKEQSELDQDLDDVEEVEEEETGEETKLKARQLTVQMMQNPQILAALQERLDGLVETPTGYIESLPRVVKRRVNALKNLQVKCAQIEAKFYEEVHDLERKYAVLYQPLFDKRFEIINAIYEPTEEECEWKPDEEDEISEELKEKAKIEDEKKDEEKEDPKGIPEFWLTVFKNVDLLSDMVQEHDEPILKHLKDIKVKFSDAGQPMSFVLEFHFEPNEYFTNEVLTKTYRMRSEPDDSDPFSFDGPEIMGCTGCQIDWKKGKNVTLKTIKKKQKHKGRGTVRTVTKTVSNDSFFNFFAPPEVPESGDLDDDAEAILAADFEIGHFLRERIIPRSVLYFTGEAIEDDDDDYDEEGEEADEEGEEEGDEENDPDYDPKKDQNPAECKQQ | Function: Histone chaperone that plays a role in the nuclear import of H2A-H2B and nucleosome assembly . Participates also in several important DNA repair mechanisms: greatly enhances ERCC6-mediated chromatin remodeling which is essential for transcription-coupled nucleotide excision DNA repair . Stimulates also homologous recombination (HR) by RAD51 and RAD54 which is essential in mitotic DNA double strand break (DSB) repair . Plays a key role in the regulation of embryonic neurogenesis (By similarity). Promotes the proliferation of neural progenitors and inhibits neuronal differentiation during cortical development (By similarity). Regulates neurogenesis via the modulation of RASSF10; regulates RASSF10 expression by promoting SETD1A-mediated H3K4 methylation at the RASSF10 promoter (By similarity).
PTM: Monoglycylated on glutamate residues. Cannot be polyglycylated due to the absence of functional TTLL10 in human (By similarity).
Sequence Mass (Da): 45374
Sequence Length: 391
Domain: The NAP1L motif is required for the histone chaperone activity.
Subcellular Location: Nucleus
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Q9Z2G8 | MADIDNKEQSELDQDLEDVEEVEEEETGEETKIKARQLTVQMMQNPQILAALQERLDGLVDTPTGYIESLPKVVKRRVNALKNLQVKCAQIEAKFYEEVHDLERKYAVLYQPLFDKRFEIINAIYEPTEEECEWKPDEEDEVSEELKEKAKIEDEKKDEEKEDPKGIPEFWLTVFKNDLLSDMVQEHDEPILKHLKDIKVKFSDAGQPMSFILEFHFEPNEYFTNEVLTKTYRMRSEPDDSDPFSFDGPEIMGCTGCQIDWKKGKNVTLKTIKKKQKHKGRGTVRTVTKTVSKTSFFNFFAPPEVPENGDLDDDXEAILAADFEIGHFLRERIIPRSVLYFTGEAIEDDDDDYDEEGEEADEEGEEEGDEENDPDYDPKKDQNPAECKQQ | Function: Histone chaperone that plays a role in the nuclear import of H2A-H2B and nucleosome assembly. Participates also in several important DNA repair mechanisms: greatly enhances ERCC6-mediated chromatin remodeling which is essential for transcription-coupled nucleotide excision DNA repair. Stimulates also homologous recombination (HR) by RAD51 and RAD54 which is essential in mitotic DNA double strand break (DSB) repair (By similarity). Plays a key role in the regulation of embryonic neurogenesis (By similarity). Promotes the proliferation of neural progenitors and inhibits neuronal differentiation during cortical development (By similarity). Regulates neurogenesis via the modulation of RASSF10; regulates RASSF10 expression by promoting SETD1A-mediated H3K4 methylation at the RASSF10 promoter (By similarity).
PTM: Polyglycylated by TTLL10 on glutamate residues, resulting in polyglycine chains on the gamma-carboxyl group. Both polyglutamylation and polyglycylation modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally.
Sequence Mass (Da): 45314
Sequence Length: 390
Domain: The NAP1L motif is required for the histone chaperone activity.
Subcellular Location: Nucleus
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Q99733 | MADHSFSDGVPSDSVEAAKNASNTEKLTDQVMQNPRVLAALQERLDNVPHTPSSYIETLPKAVKRRINALKQLQVRCAHIEAKFYEEVHDLERKYAALYQPLFDKRREFITGDVEPTDAESEWHSENEEEEKLAGDMKSKVVVTEKAAATAEEPDPKGIPEFWFTIFRNVDMLSELVQEYDEPILKHLQDIKVKFSDPGQPMSFVLEFHFEPNDYFTNSVLTKTYKMKSEPDKADPFSFEGPEIVDCDGCTIDWKKGKNVTVKTIKKKQKHKGRGTVRTITKQVPNESFFNFFNPLKASGDGESLDEDSEFTLASDFEIGHFFRERIVPRAVLYFTGEAIEDDDNFEEGEEGEEEELEGDEEGEDEDDAEINPKV | Function: Acts as histone chaperone in nucleosome assembly.
PTM: Phosphorylated at the G0/G1 boundary but it is not phosphorylated in S-phase. Phosphorylated protein remains in the cytoplasm in a complex with histones during the G0/G1 transition, whereas dephosphorylation triggers its transport into the nucleus at the G1/S-boundary.
Sequence Mass (Da): 42823
Sequence Length: 375
Subcellular Location: Nucleus
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P12927 | MEKNLPDIFFFPNCVNVFSYKYSQDEFSNMSKTERDSFSLAVFPVIKHRWHNAHVVKHKGIYKVSTEARGKKVSPPSLGKPAHINLTAKQYIYSEHTISFECYSFLKCITNTEINSFDEYILRGLLEAGNSLQIFSNSVGKRTDTIGVLGNKYPFSKIPLASLTPKAQREIFSAWISHRPVVLTGGTGVGKTSQVPKLLLWFNYLFGGFSTLDKITNFHERPVILSLPRIALVRLHSNTILKSLGFKVLDGSPISLRYGSIPEELINKQPKKYGIVFSTHKLSLTKLFSYGTLIIDEVHEHDQIGDIIIAVARKHHTKIDSMFLMTATLEDDRERLKVFLPNPAFIHIPGDTLFKISEVFIHNKINPSSRMAYIEEEKRNLVTAIQMYTPPDGSSGIVFVASVAQCHEYKSYLEKRLPYDMYIIHGKVLDIDEILEKVYSSPNVSIIISTPYLESSVTIRNVTHIYDMGKVFVPAPFGGSQEFISKSMRDQRKGRVGRVNPGTYVYFYDLSYMKSIQRIDSEFLHNYILYANKFNLTLPEDLFIIPTNLDILWRTKEYIDSFDISTETWNKLLSNYYMKMIEYAKLYVLSPILAEELDNFERTGELTSIVREAILSLNLRIKILNFKHKDDDTYIHFCKILFGVYNGTNATIYYHRPLTGYMNMISDTIFVPVDNN | Function: NTP-dependent helicase that catalyzes unidirectional unwinding of 3'tailed duplex RNAs and plays an important role during transcription of early mRNAs, presumably by preventing R-loop formation behind the elongating RNA polymerase. Might also play a role in the export of newly synthesized mRNA chains out of the core into the cytoplasm. Required for replication and propagation of viral particles.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 77600
Sequence Length: 676
Subcellular Location: Virion
EC: 3.6.4.13
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Q8RQP9 | MTETAGELDPEVTPLHLRKALGRFASGVTIVTTAECEDEDSVHGMTANAFTSVSLDPPLVLVSISTRAKMDTKIRETGTYGISILAGDQEPVSLHFAGAAHEPDRVRFVWRRGVPLLEGALVHLACTVVASHPAGDHTLHVGRVEQLWYDDGHPLVFYTGSFRSLELLGRDEPWGF | Function: Catalyzes the reduction of FAD with the concomitant oxidation of NADH. NAD is the physiological electron donor. Subsequently, the reduced flavins diffuse to the oxygenase component NphA2.
Catalytic Activity: a reduced flavin + NAD(+) = an oxidized flavin + 2 H(+) + NADH
Sequence Mass (Da): 19174
Sequence Length: 176
EC: 1.5.1.36
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Q9TU19 | GEEEDEEEEEEEESEEGGGEEEESEEEEEEKQENESHHQATSKEYIAVGDFTAQQAGDLTFKKREILLIIEKKPDGWWIAKNAKGNKGLIPRTYVEPYNKEEGQDTSEEEDSEEDVEVGDQTAGGEEVKQRTDSHWSAVQKAISEQINTVDVLTTMGAIPAGFRPSTLFQLLEEGNQFRASYFLQPELTPSQLAFRDLMWDAKTGTIRSRPSRVSFILTLWSCKMIPLPGTSIQVLSRHVRLCIFDGNKVLSNIHTVRATWQSKKPKTWTFSPQVTGILPCLLDGDCFIRSNSSSPDLGILFELGISYIRNSTGERGELSCGWVFLKLFDASGIPIPAKTYELFLNGGTPYEKGVEVDPSVSRRAYGSVFHQMMTMRRQPQLLVKLRSLNRRSRDLLSLLPETLIGSMCTIHLLIFYRQILGDVLLKDRTSMQSADLISNPVLATFPKLLEQPDMMDALRSSWAEKESTLKRSEKRDKEFLKAMFLLVYHDCVVPLLHSTLLPPFRWAEEETEAARWKVIADFLKQNQENGGALQALLSPDGVHEPFDISEQTYDLLGEIRKNVA | Function: Together with BCAR1 it may play a role in the control of epithelial cell polarity (By similarity). Involved in the organization of apical junctions in kidney cells together with NPHP4 and RPGRIP1L/NPHP8 (By similarity). Does not seem to be strictly required for ciliogenesis (By similarity). Seems to help to recruit PTK2B/PYK2 to cell matrix adhesions, thereby initiating phosphorylation of PTK2B/PYK2 and PTK2B/PYK2-dependent signaling (By similarity). May play a role in the regulation of intraflagellar transport (IFT) during cilia assembly (By similarity). Required for normal retina development (By similarity). In connecting photoreceptor cilia influences the movement of some IFT proteins such as IFT88 and WDR19. Involved in spermatogenesis (By similarity).
Sequence Mass (Da): 63961
Sequence Length: 565
Domain: The SH3 domain mediates the stable interaction with Cas.
Subcellular Location: Cell junction
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O15259 | MLARRQRDPLQALRRRNQELKQQVDSLLSESQLKEALEPNKRQHIYQRCIQLKQAIDENKNALQKLSKADESAPVANYNQRKEEEHTLLDKLTQQLQGLAVTISRENITEVGAPTEEEEESESEDSEDSGGEEEDAEEEEEEKEENESHKWSTGEEYIAVGDFTAQQVGDLTFKKGEILLVIEKKPDGWWIAKDAKGNEGLVPRTYLEPYSEEEEGQESSEEGSEEDVEAVDETADGAEVKQRTDPHWSAVQKAISEAGIFCLVNHVSFCYLIVLMRNRMETVEDTNGSETGFRAWNVQSRGRIFLVSKPVLQINTVDVLTTMGAIPAGFRPSTLSQLLEEGNQFRANYFLQPELMPSQLAFRDLMWDATEGTIRSRPSRISLILTLWSCKMIPLPGMSIQVLSRHVRLCLFDGNKVLSNIHTVRATWQPKKPKTWTFSPQVTRILPCLLDGDCFIRSNSASPDLGILFELGISYIRNSTGERGELSCGWVFLKLFDASGVPIPAKTYELFLNGGTPYEKGIEVDPSISRRAHGSVFYQIMTMRRQPQLLVKLRSLNRRSRNVLSLLPETLIGNMCSIHLLIFYRQILGDVLLKDRMSLQSTDLISHPMLATFPMLLEQPDVMDALRSSWAGKESTLKRSEKRDKEFLKSTFLLVYHDCVLPLLHSTRLPPFRWAEEETETARWKVITDFLKQNQENQGALQALLSPDGVHEPFDLSEQTYDFLGEMRKNAV | Function: Together with BCAR1 it may play a role in the control of epithelial cell polarity (By similarity). Involved in the organization of apical junctions in kidney cells together with NPHP4 and RPGRIP1L/NPHP8 (By similarity). Does not seem to be strictly required for ciliogenesis (By similarity). Seems to help to recruit PTK2B/PYK2 to cell matrix adhesions, thereby initiating phosphorylation of PTK2B/PYK2 and PTK2B/PYK2-dependent signaling (By similarity). May play a role in the regulation of intraflagellar transport (IFT) during cilia assembly. Required for normal retina development (By similarity). In connecting photoreceptor cilia influences the movement of some IFT proteins such as IFT88 and WDR19. Involved in spermatogenesis (By similarity).
PTM: Phosphorylation by CK2 is required for the interaction with PACS1 and the targeting to the base region of cilia.
Sequence Mass (Da): 83299
Sequence Length: 732
Domain: The SH3 domain mediates the stable interaction with Cas.
Subcellular Location: Cell junction
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Q9QY53 | MLARRPRDPLQALRRRGQELKLQVDSLVTESQLTGALEPSKRREIYQRCIQLKQAVDENKNTLQKLNKADEAAPVGNYEQRKEEEHSLLEKLACQLQELAVSISRKDALKVEAHSDKEEDDTTEDDEEETGGEEEESEGDGEGKQEQASPKQAETETVTYIALGDFAAQQTGDLTFKKGDVLHIIEKKPDGWWLAKDAEGVEGLIPRTYLEPYNKEDKLESSEGSEEGGEEDGEEDVEVVDETADGAQVKQRTDSHWSAVRKAISEQINTVDVLATMGAIPAGFRPSTLSQLLDEAGNQFRASYFLQPELTTSQLAFRDLTWDAKAGTIMSRPSRVSLILTLWSCKMIPLPGTSIQVLSRHIRLCLFDGSKVLSNIHTVRAVWQPKKPKTWTFSPQVTGILPCLLDGDCFIRSNSSTPDLGILFELGISYIRNSTGERGELSCGWVFLKLFDASGVPIPAKTYELFLNGGTPYEKGVEVDPSVSRRAQGSVFRQMISVRRQPQLLVKLRSLNRRSRAMLSLLPETLVGSMCSAHLLIFYRQILGDVLLRDRTNLQSADLISHPVLATFPLLLEQPDVMDALRSSWSEKESTLKRAEKRDKELLKAEFLLVYHDCVLPLLHSTLLPPFRWAEEETEAARWKAIADFLKQSRENEGSLKALLSPDGVHKPFDLSEQTFDFLGEIRKNSG | Function: Together with BCAR1 it may play a role in the control of epithelial cell polarity. Involved in the organization of apical junctions in kidney cells, together with NPHP4 and RPGRIP1L/NPHP8 . Does not seem to be strictly required for ciliogenesis . Seems to help to recruit PTK2B/PYK2 to cell matrix adhesions, thereby initiating phosphorylation of PTK2B/PYK2 and PTK2B/PYK2-dependent signaling . May play a role in the regulation of intraflagellar transport (IFT) during cilia assembly . Required for normal retina development . In connecting photoreceptor cilia influences the movement of some IFT proteins such as IFT88 and WDR19 . Involved in spermatogenesis; required for the differentiation of early elongating spermatids into spermatozoa .
Sequence Mass (Da): 77035
Sequence Length: 687
Domain: The SH3 domain mediates the stable interaction with Cas and is involved in establishing tight junctions in epithelial cells.
Subcellular Location: Cell junction
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Q99463 | MEVSLNHPASNTTSTKNNNSAFFYFESCQPPSPALLLLCIAYTVVLIVGLFGNLSLIIIIFKKQRKAQNFTSILIANLSLSDTLVCVMCIHFTIIYTLMDHWIFGDTMCRLTSYVQSVSISVSIFSLVFTAVERYQLIVNPRGWKPSVTHAYWGITLIWLFSLLLSIPFFLSYHLTDEPFRNLSLPTDLYTHQVACVENWPSKKDRLLFTTSLFLLQYFVPLGFILICYLKIVICLRRRNAKVDKKKENEGRLNENKRINTMLISIVVTFGACWLPRISSMSSLTGIMRC | Function: When expressed, is unable to bind pancreatic polypeptide (PP), neuropeptide Y (NPY), or peptide YY (PYY), suggesting that either it is functionally inactive or that it may have acquired a pancreatic polypeptide-independent function.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33180
Sequence Length: 290
Subcellular Location: Membrane
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P01303 | MLGNKRLGLSGLTLALSLLVCLGALAEAYPSKPDNPGEDAPAEDMARYYSALRHYINLITRQRYGKRSSPETLISDLLMRESTENVPRTRLEDPAMW | Function: NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone.
PTM: The neuropeptide Y form is cleaved at Pro-30 by the prolyl endopeptidase FAP (seprase) activity (in vitro).
Sequence Mass (Da): 10851
Sequence Length: 97
Subcellular Location: Secreted
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A6X0U8 | MVKVLVLYYSAYGHMEKMAKAAAEGAREGGAEVTIKRVPELVPPDVAKASHYKIDQDAPIATPAELADYDAIIIGTATRYGMMAAQMKNFLDQTGGLWAKGALINKVGSVMVSTATQHGGAELALISTQWQMQHQGMIIVPLSYAYQGQMGNDVVRGGAPYGMTTTADGDGSRQPSEQELDGARFQGKRVAEITAKLNS | Cofactor: Binds 1 FMN per monomer.
Catalytic Activity: a quinone + H(+) + NADH = a quinol + NAD(+)
Sequence Mass (Da): 21222
Sequence Length: 199
EC: 1.6.5.2
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Q9HZK8 | MANQESTTRTLLVALVVCLVSSVFVAGAAVALKPTQAENRLLDKQRSILAIAGLGEPGMSGKEVKALFDSRITAKVVDLQSGTFSDAQDPLGYDPLKAAKDPALSDALPAAEDIASIKRRERYTTVYLVETDGKLDTLILPVRGYGLWSTLYGFLALKGDLNTVAGFGFYQHGETPGLGGEVDNPKWKALWVGKTLYDAQGDLAVQIIKGSVDPQSAKATHQVDGLAGATLTSKGVDNLLHFWLGKDGFDAFLANLRKGEA | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Catalytic Activity: a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 27780
Sequence Length: 261
Subcellular Location: Cell inner membrane
EC: 7.2.1.1
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Q56582 | MASNNDSIKKTLGVVIGLSLVCSIIVSTAAVGLRDKQKANAVLDKQSKIVEVAGIDANGKKVPELFAEYIEPRLVDLETGNFTEGNASTYDQREASKDAERSIALTPEEDVADIRRRANTAVVYLVKDQDEVQKVILPMHGKGLWSMMYAFVAVETDGNTVSAITYYEQGETPGLGGEVENPSWRDQFIGKKLYNEDHQPAIKVVKGGAPQGSEHGVDGLSGATLTSNGVQHTFDFWLGDKGFGPFLAKVRDGELN | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Catalytic Activity: a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 27703
Sequence Length: 256
Subcellular Location: Cell inner membrane
EC: 7.2.1.1
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Q75R62 | MASNNDSIKKTLFVVIALSLVCSIIVSTAAVGLRDKQKVNAVLDKQSKIVEVAGINESGSVPELFAKYIEPRLIDFKTGNFVDGDATAYDQRKASKDPAQSIKLTAEQDKAKIIRRANTGVVYLVKSGDEISKVIVPVHGNGLWSMMYAFVAVETDGNTVSGITYYEQGETPGLGGEVENPSWRAQFVGKKLFDDNHQPAIKVVKGGAPAGSEHGVDGLSGATLTSNGVQHTFDFWLGDMGFGPFLAKVRDGGLN | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Catalytic Activity: a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 27251
Sequence Length: 255
Subcellular Location: Cell inner membrane
EC: 7.2.1.1
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A5F5Y7 | MASNNDSIKKTLFVVIALSLVCSIIVSAAAVGLRDKQKENAALDKQSKILQVAGIEAKGSKQIVELFNKSIEPRLVDFNTGDFVEGDAANYDQRKAAKEASESIKLTAEQDKAKIQRRANVGVVYLVKDGDKTSKVILPVHGNGLWSMMYAFVAVETDGNTVSGLTYYEQGETPGLGGEVENPAWRAQWVGKKLFDENHKPAIKIVKGGAPQGSEHGVDGLSGATLTSNGVQNTFDFWLGDMGFGPFLTKVRDGGLN | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Catalytic Activity: a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 27619
Sequence Length: 257
Subcellular Location: Cell inner membrane
EC: 7.2.1.1
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Q8ZBZ2 | MASDKPRNNDSIGKTLLVVVILCLVCSVVVAGAAVGLKAKQQEQRLLDKQRNILAVAGLLQPRMLAEEVQQAFATRIEPRLLDLQSGEFLKQDPATFDRSQALRDNQMSIALTPAQDIAGIRRRANVVEIYLVRGDGGQINKVILPIYGSGLWSMMYAFVAIDTDGKTVRGITYYDHGETPGLGGEIENPIWRNQWIGKRLFDDQGQPAIRIVKGRAPANDPHAVDGLSGATLTSNGVQNSFNFWLGENGFGPFLKKVREGALKNG | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Catalytic Activity: a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 29067
Sequence Length: 266
Subcellular Location: Cell inner membrane
EC: 7.2.1.1
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A0KHC9 | MADKSEMKKLLLTPVLGNNPIALQVLGVCSALAVTSQMKTAFVMTLAVTAVTAFSNLFISLIRNQIPNSVRIIAQMAVIASLVIVVDQVLKAYAYDISKQLSVFVGLIITNCIVMGRAEAYAMKSAPLPSFLDGIGNGLGYGAVLLTVATVREILGSGTWFGIELLPLVNNGGWYVPNGLLLLPPSAFFIIGLIIWGVRTKDPKQVEAKD | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Catalytic Activity: a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22408
Sequence Length: 210
Subcellular Location: Cell inner membrane
EC: 7.2.1.1
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Q9Z8B4 | MTSKKSYKSYFFDPLWSNNQILIAILGICSALAVTTTVQTAITMGIAVSIVTGCSSFFVSLLRKFTPDSVRMITQLIIISLFVIVIDQFLKAFFFDISKTLSVFVGLIITNCIVMGRSESLARHVTPIPAFLDGFASGLGYGWVLLVIGVIRELFGFGTLMGFRIIPQFVYASETHPDGYQNLSLMVLAPSAFFLLGIMIWLVNIRDSKKRKR | Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. NqrA to NqrE are probably involved in the second step, the conversion of ubisemiquinone to ubiquinol.
Catalytic Activity: a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23657
Sequence Length: 213
Subcellular Location: Cell inner membrane
EC: 7.2.1.1
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A5F5Y4 | MSTIIFGVVMFTLIILALVLVILFAKSKLVPTGDITISINGDPEKAIVTQPGGKLLTALAGAGVFVSSACGGGGSCGQCRVKIKSGGGDILPTELDHISKGEAREGERLACQVAVKADMDLELPEEIFGVKKWECTVISNDNKATFIKELKLAIPDGESVPFRAGGYIQIEAPAHHVKYADFDVPEKYRGDWDKFNLFRYESKVDEPIIRAYSMANYPEEFGIIMLNVRIATPPPNNPNVPPGQMSSYIWSLKAGDKCTISGPFGEFFAKDTDAEMVFIGGGAGMAPMRSHIFDQLKRLKSKRKMSYWYGARSKREMFYVEDFDGLAAENDNFVWHCALSDPQPEDNWTGYTGFIHNVLYENYLKDHEAPEDCEYYMCGPPMMNAAVINMLKNLGVEEENILLDDFGG | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: NQR complex catalyzes the reduction of ubiquinone-1 to ubiquinol by two successive reactions, coupled with the transport of Na(+) ions from the cytoplasm to the periplasm. The first step is catalyzed by NqrF, which accepts electrons from NADH and reduces ubiquinone-1 to ubisemiquinone by a one-electron transfer pathway.
Catalytic Activity: a ubiquinone + H(+) + n Na(+)(in) + NADH = a ubiquinol + n Na(+)(out) + NAD(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 45067
Sequence Length: 408
Subcellular Location: Cell inner membrane
EC: 7.2.1.1
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Q6XV52 | MNPNQKIITIGVVNTTLSTIALLIGVGNLIFNTVIHEKIGDHQTVVYPTITAPVVPNCSDTIITYNNTVINNITTTIITEAERHFKPSLPLCPFRGFFPFHKDNAIRLGENKDVIVTREPYVSCDNDNCWSFALAQGALLGTKHSNGTIKDRTPYRSLIRFPIGTAPVLGNYKEICVAWSSSSCFDGKEWMHVCMTGNDNDASAQIIYAGKMTDSIKSWRRDILRTQESECQCIDGTCVVAVTDGPAANSADHRVYWIREGKVIKYENVPKTKIQHLEECSCYVDTDVYCVCRDNWKGSNRPWMRINNETILETGYVCSKFHSDTPRPADPSTVSCDSPSNVNGGPGVKGFGFKTGDDVWLGRTVSTNGRSGFEIIKVTEGWINSPNHAKSVTQTLVSNNDWSGYSGSFIVENNGCFQPCFYIELIRGRTNKNDDVSWTSNSIVTFCGLDNEPGSGNWPDGSNIGFMPK | Function: Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moieties on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Catalytic Activity: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Sequence Mass (Da): 51894
Sequence Length: 469
Domain: Intact N-terminus is essential for virion morphogenesis. Possesses two apical sorting signals, one in the ectodomain, which is likely to be a glycan, and the other in the transmembrane domain. The transmembrane domain also plays a role in lipid raft association.
Subcellular Location: Virion membrane
EC: 3.2.1.18
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P06820 | MNPNQKIITIGSVSLTIATVCFLMQIAILVTTVTLHFKQHECDSPASNQVMPCEPIIIERNITEIVYLNNTTIEKEICPKVVEYRNWSKPQCQITGFAPFSKDNSIRLSAGGDIWVTREPYVSCDPVKCYQFALGQGTTLDNKHSNDTVHDRIPHRTLLMNELGVPFHLGTRQVCIAWSSSSCHDGKAWLHVCITGDDKNATASFIYDGRLVDSIGSWSQNILRTQESECVCINGTCTVVMTDGSASGRADTRILFIEEGKIVHISPLAGSAQHVEECSCYPRYPGVRCICRDNWKGSNRPVVDINMEDYSIDSSYVCSGLVGDTPRNDDRSSNSNCRNPNNERGTQGVKGWAFDNGNDLWMGRTISKDLRSGYETFKVIGGWSTPNSKSQINRQVIVDSDNRSGYSGIFSVEGKSCINRCFYVELIRGRKQETRVWWTSNSIVVFCGTSGTYGTGSWPDGANINFMPI | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moieties on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.
Catalytic Activity: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 52131
Sequence Length: 469
Domain: Intact N-terminus is essential for virion morphogenesis. Possesses two apical sorting signals, one in the ectodomain, which is likely to be a glycan, and the other in the transmembrane domain. The transmembrane domain also plays a role in lipid raft association.
Subcellular Location: Virion membrane
EC: 3.2.1.18
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Q6MNP6 | MKKQTLHSPSYFVSGGKNPESLFAWKNVNCEIRNRKGEVFFEMKNVEAPEGWSQLAIDIAASKYFRKVGVPKTGHETSVRQMVDRVVKAIVASAIRQGGYFATRKEADIFAKELKFILLSQRGAFNSPVWFNAGLWEAYKAQSPSEHFAWDEKKKSIQATKNAYERPQCSACFIQSVDDSIESIFDLAKTEAKLFKYGSGTGSNFSKIRSKYEATGSGGKSSGLISFLEVLDKGAGAIKSGGTTRRAAKMVVVDIDHPEVLDFIDWKMREEQKAHLLIAAGLSADFEGEAYRTVSGQNANNSVRVSDAFMKAVEQERPWKLKARLTGKVLREIPAGEVWNRITRAAWMCADPGIQFHDTINKWHTCPETDIIHSSNPCSEYMFLDDSACNLASINLVKFLNDTGDFDFESFIHTARTLFVAQEILVDYSSYPTQRVAQNSHDYRPLGLGFANLGSLLMRKGVAYDSDEGRAWAGALTSLMSGVAYLTSSEMARAKGPFAGYRKNSKSMLKVMKMHERALNQVAWKMLPAGIDKAVRNLWKGVLYNGEKYGYRNAQATVIAPTGTIGLLMDCDTTGIEPDFSLIKFKKLVGGGEIQIVNQSVDAALASLQYFEDERQAILKYVEENNSVVGAPQMHPEDLPVFDTATAMPGQRVLSPESHVKMMAAVQPFISGAISKTVNMPSTATEEDISRIYFLAWKLGVKAVAVYRDGSKQSQPLNLKEKPKVVEEVGVPNFTMKCPECGSDTVLTSGCYRCPNCGTTVGCS | Cofactor: 5'-deoxyadenosylcobalamine (coenzyme B12).
Function: Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen (By similarity).
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 84408
Sequence Length: 764
EC: 1.17.4.1
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O54196 | MTETTSGPARGSRTKGTKATKGLRIERVHTTPGVHPYDEVVWERRDVVMTNWRDGSVNFEQRGVEFPDFWSVNAVNIVTSKYFRGAVGTPQRETGLKQLIDRIVKTYRKAGEEYKYFASPADAEIFEHELAYALLHQIFSFNSPVWFNVGTPQPQQVSACFILSVDDSMESILDWYKEEGMIFKGGSGAGLNLSRIRSSKELLSSGGNASGPVSFMRGADASAGTIKSGGATRRAAKMVILDVDHPDIEGFIETKVKEEEKIRALRDAGFDMDLGGDDITSVQYQNANNSVRVNDEFMRAVESGSAFGLRARMTGEIIEQVDAKALFRKMAQAAWACADPGIQYDDTINRWHTCPESGRINGSNPCSEYMHLDNTSCNLASLNLMKFLTDDGEGNQSFDVERFAKVVELVITAMDISICFADFPTQKIGENTRAFRQLGIGYANLGALLMATGHAYDSDGGRAIAGAISSLMTGTSYRRSAELAAVVGPYDGYARNAAPHNQVMRQHADANDTAVRMDDLDTPIWAAATETWQDVLRLGEKNGFRNAQASVIAPTGTIGLAMSCDTTGLEPDLALVKFKKLVGGGSMQIVNGTVPQALRRLGYQAEQIEAIVEHIAEHGNVLDAPGLKTEHYKVFDCAMGERSISAMGHVRMMAAIQPWISGALSKTVNMPESATVEEVEEIYFEAWKMGVKALAIYRDNCKVGQPLSAKTKEKEQDGIAEKTEDTIRAAVEKVIEYRPVRKRLPKGRPGITTSFTVGGAEGYMTANSYPDDGLGEVFLKMSKQGSTLAGMMDAFSIAVSVGLQYGVPLETYVSKFTNMRFEPAGMTDDPDVRMAQSIVDNIFRRLALDFLPFETRSALGIHSAEERQRHLDTGSYEQVIEEDELDVEGLAQSAPRQQIPAVPAAPAEIPAPKQAHTSAELVEMQLGISADAPLCFSCGTKMQRAGSCYICEGCGSTSGCS | Cofactor: 5'-deoxyadenosylcobalamine (coenzyme B12).
Function: Catalyzes the reduction of ribonucleotides to deoxyribonucleotides. May function to provide a pool of deoxyribonucleotide precursors for DNA repair during oxygen limitation and/or for immediate growth after restoration of oxygen.
Catalytic Activity: [thioredoxin]-disulfide + a 2'-deoxyribonucleoside 5'-diphosphate + H2O = [thioredoxin]-dithiol + a ribonucleoside 5'-diphosphate
Sequence Mass (Da): 104791
Sequence Length: 961
EC: 1.17.4.1
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A1S3A0 | MVKKLTGKSFALSALVAASFVAAGAMASDKTEPRNDVYKDKFSKQYNSWHATAESEAITDALEQDPALVILWAGYGFAKDYNAPRGHMYALTDVRNTLRTGAPTSAEDGPMPMACWSCKSPDVPRLIEEQGESGYFTGKWAKGGAEVANTIGCSDCHEKGTPKLRLSRPFASRAMEAIGTPFDKASKQDKESMVCAQCHVEYYFEKTDDRKGFVKFPWDGGTTVENMEVYYDAIQFADWTHAVSKTPMLKAQHPGYETWKLGTHGQNNVSCVDCHMPKVTNEQGKKFTDHKVGNPFDRFEETCGTCHSQDKEHMLTVYKDNKSKVMELKSKAEAQLVAAHFEAGAAWKAGATEDEMKPILTNIRHAQWRWDYAIASHGVSAHAPAEALRVLGTAVDKAANARVQLAQLLATKGVKQPIELPDISTKAKAQAALGMDMDKMNADKAKFKQEMLPKWEADAKAREATYK | Cofactor: Binds 1 Ca(2+) ion per monomer.
Function: Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process.
Catalytic Activity: 6 Fe(III)-[cytochrome c] + 2 H2O + NH4(+) = 6 Fe(II)-[cytochrome c] + 8 H(+) + nitrite
Sequence Mass (Da): 51568
Sequence Length: 467
Pathway: Nitrogen metabolism; nitrate reduction (assimilation).
Subcellular Location: Periplasm
EC: 1.7.2.2
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Q8EAC7 | MMKKMTGKTFALSALVAASFMAAGAMASDKTEPRNEVYKDKFKNQYNSWHDTAKSEELVDALEQDPNMVILWAGYAFAKDYKAPRGHMYAVTDVRNTLRTGAPKNAEDGPLPMACWSCKSPDVPRLIEEQGEDGYFKGKWAKGGPEVTNTIGCSDCHEKGSPKLRISRPYVDRALDAIGTPFSKASKQDKESMVCAQCHVEYYFEKKEDKKGFVKFPWDMGVTVDQMEVYYDGIEFSDWTHALSKTPMLKAQHPEYETWKMGIHGKNNVSCVDCHMPKVTSPEGKKFTDHKVGNPFDRFEETCATCHSQTKEFLVGVTNERKAKVKEMKLKAEEQLVKAHFEAAKAWELGATEAEMKPILTDIRHAQWRWDLAIASHGVAAHAPEEALRVLGTSVNKAADARVKLAQLLAKKGLTDPVAIPDISTKAKAQAVLGMDMEKMNAEKEAFKKDMLPKWDAEAKKREATYK | Cofactor: Binds 1 Ca(2+) ion per monomer.
Function: Catalyzes the reduction of nitrite to ammonia, consuming six electrons in the process . Has very low activity toward hydroxylamine . Has even lower activity toward sulfite. Sulfite reductase activity is maximal at neutral pH (By similarity).
Catalytic Activity: 6 Fe(III)-[cytochrome c] + 2 H2O + NH4(+) = 6 Fe(II)-[cytochrome c] + 8 H(+) + nitrite
Sequence Mass (Da): 52334
Sequence Length: 467
Pathway: Nitrogen metabolism; nitrate reduction (assimilation).
Subcellular Location: Periplasm
EC: 1.7.2.2
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O35987 | MAEERQDALREFVAVTGAEEDRARFFLESAGWDLQIALASFYEDGGDEDIVTISQATPSSVSRGTAPSDNRVTSFRDLIHDQDEEEEEEEGQRFYAGGSERSGQQIVGPPRKKSPNELVDDLFKGAKEHGAVAVERVTKSPGETSKPRPFAGGGYRLGAAPEEESAYVAGERRRHSGQDVHVVLKLWKTGFSLDNGDLRSYQDPSNAQFLESIRRGEVPAELRRLAHGGQVNLDMEDHRDEDFVKPKGAFKAFTGEGQKLGSTAPQVLNTSSPAQQAENEAKASSSILINEAEPTTNIQIRLADGGRLVQKFNHSHRISDIRLFIVDARPAMAATSFVLMTTFPNKELADENQTLKEANLLNAVIVQRLT | Function: Reduces the ATPase activity of VCP . Necessary for the fragmentation of Golgi stacks during mitosis and for VCP-mediated reassembly of Golgi stacks after mitosis . May play a role in VCP-mediated formation of transitional endoplasmic reticulum (tER) . Inhibits the activity of CTSL (in vitro) (By similarity). Together with UBXN2B/p37, regulates the centrosomal levels of kinase AURKA/Aurora A during mitotic progression by promoting AURKA removal from centrosomes in prophase (By similarity). Also, regulates spindle orientation during mitosis (By similarity).
PTM: Phosphorylated during mitosis. Phosphorylation inhibits interaction with Golgi membranes and is required for the fragmentation of the Golgi stacks during mitosis.
Sequence Mass (Da): 40680
Sequence Length: 370
Subcellular Location: Nucleus
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P46461 | MAYILKATKCPTDELSLTNRAIVNVGDFPEEIKYADISPAPGQHFIFALEKTVEVPSGYVGFSLVQRKWAMVSINQELEVRPYRFDASSDVITCVSFETDFLQKKTVSQEPYDSDQMAKEFIMQFAGMALTVGQSLVFNFKDKKLLGLAVKSLEAIDPKSLGEGKDTAMRNVRFGRILGNTVVQFEKAENSSLNLQGKSKGKVVRQSIINPDWDFGKMGIGGLDKEFNSIFRRAFASRVFPPELVEQLGCKHVKGILLYGPPGTGKTLMARQIGTMLNAREPKIVNGPQILDKYVGESEANVRRLFAEAEEEEKRLGPNSGLHIIIFDEIDAICKQRGSVAGNSGVHDTVVNQLLTKIDGVDQLNNILVIGMTNRRDMIDEALLRPGRLEVQMEISLPNEQGRVQILNIHTKRMREFNKINDDVDNKEIAALTKNFSGAELEGLVRAAQSSAMNRLIKADAKVTVDPEAMEKLKVNRDDFLHSLEHDIKPAFGTAQEILDNMLARGVINWGAPVSNLLEDGMLYVQQAKAPESSGLVSVLVAGAPNSGKTALAAQLAKMSDFPFVKVCSPEDMVGYTESAKCLHIRKIFDDAYRSMLSCIVVDNVERLLDYGSIGPRYSNMTLQALLVLLKKQPPKGRKLLILCTSSRREVLEEMEMLTAFTSVLHVPNLSKPDHVLAVLENTDIFSKGEIQAIGKKMAGKRVFIGIKKLLGLIDMARQTEQSQRAIKFLSKMEEEGGLDMVARQ | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 82555
Sequence Length: 745
Subcellular Location: Cytoplasm
EC: 3.6.4.6
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P54351 | MSIEKAHRMRAIKCPTDELSLTNKAIVNVSDFTEEVKYVDISPGPGLHYIFALEKISGPELPLGHVGFSLVQRKWATLSINQEIDVRPYRFDASADIITLVSFETDFLQKKTTTQEPYDSDEMAKEFLMQFAGMPLTVGQTLVFQFKDKKFLGLAVKTLEAVDPRTVGDSLPKTRNVRFGRILGNTVVQFEKAENSVLNLQGRSKGKIVRQSIINPDWDFGKMGIGGLDKEFNAIFRRAFASRVFPPELVEQLGIKHVKGILLYGPPGTGKTLMARQIGTMLNAREPKIVNGPQILDKYVGESEANIRRLFAEAEEEEKRLGPNSGLHIIIFDEIDAICKARGSVAGNSGVHDTVVNQLLAKIDGVEQLNNILVIGMTNRRDMIDEALLRPGRLEVQMEISLPNEQGRVQILNIHTKRMRDFNKIASDVDNNEIAAKTKNFSGAELEGLVRAAQSTAMNRLIKADSKVHVDPEAMEKLRVTRADFLHALDNDIKPAFGAAQEMLENLLARGIINWGPPVTELLEDGMLSVQQAKATESSGLVSVLIEGAPNSGKSALAANLAQLSDFPFVKVCSPEDMVGFTESAKCLHIRKIFDDAYRSTLSCIVVDNVERLLDYGPIGPRYSNLTLQALLVLLKKQPPKGRKLLILCTSSRRDVLEEMEMLSAFTSVLHVSNLSTPENVLAVLDDSDLFSPEELQSIARKMAGKRLCIGIKKLLALIDMIRQSEPHQRVIKFLSKMEEEGGLEMDRVQGH | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin (By similarity).
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 83434
Sequence Length: 752
Subcellular Location: Cytoplasm
EC: 3.6.4.6
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Q9M0Y8 | MAGRYGSQVMTMTVTNTPSADLAFTNLAYCSSSDLRQFSVPGSDLFLANVADSFILSLCGHGSIRDGNIALNAIQRRHARVSTGDMVSVSRFVPPENFDLAMLTLELEFVKKGTKSEQVDAALLSTQLKRKYTNQVLTVGQKATFEYHGTNYILTVNRADVEGQDHTNGIERGLLSKDTYIVFEASNASGIKIVNQREAASSNIFKHKEFNLESLGIGGLGAEFADIFRRAFASRVFPPHVTSRLGIKHVKGMLLFGPPGTGKTLMARQIGKMLNGKDPKIVNGPEVLSKFVGETEKNVRDLFADAEQDQRTLGDASELHVIIFDEIDAICKSRGSTRDGTGVHDSIVNQLLTKIDGVEALNNVLLIGMTNRKDLLDEALLRPGRLEVQVEISLPDEAGRLQILQIHTNKMKENSFLGTDINLQELAARTKNYSGAELEGVVKSATSYALNRQLSMDDLTKPVEEENIKITMEDFLHAIYEVQPAFGASTDDLERCRLNGMVDCGHRHNHIYKRAMLLVEQVKVSTRSPLVTCLLEGPSGSGKTALAATIGIDSDFPYVKIVSAETMIGLSESTKCAHIVKVFEDAYKSPMSIIILDDIERLLEFIAIGPRFSNIISQTLMVLLKRLPPKGKKLLVFGTTSEVTFLESVGISDCFSVTHSVPTLQKEDAKKVLNQLNLFSEDDVDSAAEALNDMPIKKIYMLIEMAAQGENGGSAEAIYAGREKININHFYDCLGDFIRFTG | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Required for vesicle-mediated transport. Catalyzes the fusion of transport vesicles within the Golgi cisternae. Is also required for transport from the endoplasmic reticulum to the Golgi stack. Seems to function as a fusion protein required for the delivery of cargo proteins to all compartments of the Golgi stack independent of vesicle origin (By similarity). Required for maintaining the normal morphology of the Golgi apparatus .
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 81487
Sequence Length: 742
Subcellular Location: Cytoplasm
EC: 3.6.4.6
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P04512 | MEKLTDLNYTLSVITLMNNTLHTILEDPGMAYFPYIASVLTGLFALNKASIPTMKIALKTSKCSYKVVKYCIVTIFNTLLKLAGYKEQITTKDEIEKQMDRVVKEMRRQLEMIDKLTTREIEQVELLKRIYDKLTVQTTGEIDMTKEINQKNVRTLEEWESGKNPYEPREVTAAM | Function: Plays an essential role in the virus replication cycle by acting as a viroporin. Creates a pore in the host reticulum endoplasmic and as a consequence releases Ca(2+) in the cytoplasm of infected cell. In turn, high levels of cytoplasmic calcium trigger membrane trafficking and transport of viral ER-associated proteins to viroplasms, sites of viral genome replication and immature particle assembly.
PTM: The N-glycosyl content is primarily Man(9)GlcNAc, with a small amount of Man(8)GlcNAc.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 20267
Sequence Length: 175
Domain: Binds 1 calcium ion per tetramer.
Subcellular Location: Host rough endoplasmic reticulum membrane
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Q93XW5 | MCPVENKWLKVGQKGAGPGARSSHAMTVVGNKVYCFGGELKPTIHIDNDLYVFDLETQEWSIAPATGEAPFPCFGVSMVTIGSTIYVYGGRDDKRRYNGLHSYDTETNEWKLLAPVEEGLPGRSYHSMAGDDRKVYVFGGVTAKGRVNTLHAYDVVDQKWVEYPAAGEACKGRGAPGLVVVEGRIWVLFGFDGNELGDIHCFDLASEQWKAVETTGDVPAARSVFPAVSYGKYIVIYGGEEEPHELMHMGAGKMSGEVYQLDTETLVWERIVCGNEEEKPSQRGWCAFTKAVKDGEEGLLVHGGNSPTNERLDDLVFWGFSHLNVN | Function: Specifier protein that contributes to constitutive and herbivore-induced simple nitrile formation . Promotes simple nitriles, but not epithionitrile or thiocyanate formation . Converts allylglucosinolate (allyl-GSL), 2-propenylglucosinolate (sinigrin), indol-3-ylmethylglucosinolate (glucobrassicin), benzylisothiocyanate and benzylglucosinolate (glucotropaeolin) to their corresponding simple nitriles in the presence of myrosinase . Catalyzes mainly the conversion of benzylisothiocyanate when benzylglucosinolate is used as the initial substrate of myrosinase .
Catalytic Activity: a (Z)-N-(sulfonatooxy)alkanimidothioate = a nitrile + sulfate + sulfur
Sequence Mass (Da): 35853
Sequence Length: 326
EC: 4.8.1.5
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P30890 | MAEASEFNFNLRRKSRAVTASRRVKEEVKEKQKMDDSKSQVVDVDSVSVYSHESSRSNYSDAYEKLKREPVVEESNDARYRTFEFSEDEETFKPANKMSDKSQRNSKSKHTEGLECSDTVLEKISELTLEIEKVKQMNQPITVDAAFNMTLRNVDNLTTRQKQALVNSIINSMN | Function: Plays an essential role in the viral genome replication. Participates, together with NSP2, in the formation of viral factories (viroplasms) which are large inclusions in the host cytoplasm where replication intermediates are assembled and viral RNA replication takes place. Orchestrates the recruitment of viroplasmic proteins such as capsid proteins to these factories.
PTM: O-glycosylated.
Sequence Mass (Da): 20057
Sequence Length: 174
Subcellular Location: Host cytoplasm
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A0A2I1C3Y3 | MPAPADIQAATLNKFLAAWREGSAPDTMALWSDDFKQRLLPLSLGESSFRSRDQAALFYPGLVENLRNWELHIKEIVHDSARGTAAVYATSQADTPFSGEKWTNEYAIFLSFSEDGTKVCRLEEMMDSAFYQSFVPKFQRYLMGLGGLKK | Function: Monooxygenase; part of the gene cluster that mediates the biosynthesis of the tetrahydroxanthone dimer neosartorin, which exhibits antibacterial activity . The two different monomeric units appear to be synthesized by the same set of enzymes, among which the Baeyer-Villiger monooxygenase nsrF is the key enzyme for the divergence of the biosynthetic routes . The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase nsrB . The atrochrysone carboxyl ACP thioesterase nsrC then breaks the thioester bond and releases the atrochrysone carboxylic acid from AacuL . Atrochrysone carboxylic acid is decarboxylated by the decarboxylase nsrE, and oxidized by the anthrone oxygenase nsrD to yield emodin . Emodin is then reduced to emodin hydroquinone by the oxidoreductase nsrR . A-ring reduction by the short chain dehydrogenase nsrJ, dehydration by the scytalone dehydratase-like protein nsrI and probable spontaneous re-oxidation, results in overall deoxygenation to chrysophanol . The Baeyer-Villiger monooxygenase nsrF accepts chrysophanol as a substrate to insert one oxygen atom at two different positions to yield the precursors of both monomric units . NsrF is promiscuous/flexible in interacting with the 2 (non methylated and methylated) aromatic rings of chrysophanol, thus diverging the biosynthetic pathway at this point . After the hydrolysis of the lactones, methylesterification by the methyltransferase nsrG yields respectively moniliphenone and 2,2',6'-trihydroxy-4-methyl-6-methoxya-cyldiphenylmethanone . The next steps are the hydroxylation by the FAD-dependent monooxygenase nsrK, followed by isomerization by the monooxygenase nsrQ . The short chain dehydrogenase/reductase nsrO then catalyzes the C-5 ketoreduction to give the xanthone skeleton of blennolide C and 5-acetylblennolide A . The acetyltransferase nsrL has a strict substrate specificity and uses only blennolide A but not blennolide C to yield 5-acetylblennolide A as the single-acetylated product . In the final step of the biosynthesis, the heterodimerization of the 2 xanthones, blennolide C and 5-acetylblennolide A, is catalyzed by the cytochrome P450 monooxygenase nsrP . NsrP can utilize at least three different xanthones as its substrates to perform the dimerization reaction .
Sequence Mass (Da): 16911
Sequence Length: 150
Pathway: Secondary metabolite biosynthesis.
EC: 1.-.-.-
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Q8U1M0 | MEKKKVVIIGGGAAGMSAASRVKRLRPEWDVKVFEATEWVSHAPCGIPYVVEGIAPKEKLMHYPPEVFIKKRGIDLHLKAEVIEVETGYVRVRENGEEKSYEWDYLVFANGASPQIPEIEGVDLPGVFTADLPPDAVAITEYMEKNKVEDVVIIGTGYIALEMAEAFVTRGKNVTLIGRSERVLRKTFDKEITDIVEEKLRQHLNLRLHEKTLSIEGRERVEKVITDGGEYKADLVIIATGIKPNVELAKQLGVKIGETGAIWTNEKMQTSVENVYAAGDVAETKHVITGKRVWIPLAPAGNKMGYVAGSNIAGKEIEFPGVLGTSITKFMDLEIGKTGLTENEAVKEGYDVRTAFIKANTKPHYYPGGREIWLKGVVDNETNRLLGVQAVGAEILPRIDSAAAMITAGFTTKDVFFTDLAYAPPFAPVWDPLIVLARVLKF | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the CoA-dependent reduction of elemental sulfur (S(0)) to produce hydrogen sulfide . Can use both NADPH and NADH, but shows a preference for NADPH . May enable S(0) to be used, via sulfide, for iron-sulfur cluster synthesis by SipA (Probable). Also shows coenzyme A disulfide reductase (CoADR) activity with both NADH and NADPH . However, CoADR specific activity is about 20-fold lower than the sulfur reduction assay and CoADR activity appears to be an artifactual side reaction and is not thought to have any physiological relevance . Also shows NAD(P)H oxidase activity with both NADH and NADPH .
Catalytic Activity: hydrogen sulfide + NADP(+) = NADPH + sulfur
Sequence Mass (Da): 48720
Sequence Length: 442
Subcellular Location: Cytoplasm
EC: 1.8.1.18
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Q12908 | MNDPNSCVDNATVCSGASCVVPESNFNNILSVVLSTVLTILLALVMFSMGCNVEIKKFLGHIKRPWGICVGFLCQFGIMPLTGFILSVAFDILPLQAVVVLIIGCCPGGTASNILAYWVDGDMDLSVSMTTCSTLLALGMMPLCLLIYTKMWVDSGSIVIPYDNIGTSLVSLVVPVSIGMFVNHKWPQKAKIILKIGSIAGAILIVLIAVVGGILYQSAWIIAPKLWIIGTIFPVAGYSLGFLLARIAGLPWYRCRTVAFETGMQNTQLCSTIVQLSFTPEELNVVFTFPLIYSIFQLAFAAIFLGFYVAYKKCHGKNKAEIPESKENGTEPESSFYKANGGFQPDEK | Function: Plays a critical role in the sodium-dependent reabsorption of bile acids from the lumen of the small intestine . Transports various bile acids, unconjugated or conjugated, such as cholate and taurocholate . Also responsible for bile acid transport in the renal proximal tubules, a salvage mechanism that helps conserve bile acids (Probable). Works collaboratively with the Na(+)-taurocholate cotransporting polypeptide (NTCP), the organic solute transporter (OST), and the bile salt export pump (BSEP), to ensure efficacious biological recycling of bile acids during enterohepatic circulation .
Catalytic Activity: 2 Na(+)(out) + taurocholate(out) = 2 Na(+)(in) + taurocholate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37714
Sequence Length: 348
Subcellular Location: Membrane
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Q62633 | MDNSSVCSPNATFCEGDSCLVTESNFNAILSTVMSTVLTILLAMVMFSMGCNVEINKFLGHIKRPWGIFVGFLCQFGIMPLTGFILSVASGILPVQAVVVLIMGCCPGGTGSNILAYWIDGDMDLSVSMTTCSTLLALGMMPLCLFIYTKMWVDSGTIVIPYDSIGISLVALVIPVSIGMFVNHKWPQKAKIILKIGSIAGAILIVLIAVVGGILYQSAWIIEPKLWIIGTIFPIAGYSLGFFLARLAGQPWYRCRTVALETGMQNTQLCSTIVQLSFSPEDLNLVFTFPLIYTVFQLVFAAIILGMYVTYKKCHGKNDAEFLEKTDNDMDPMPSFQETNKGFQPDEK | Function: Plays a critical role in the sodium-dependent reabsorption of bile acids from the lumen of the small intestine . Transports various bile acids, unconjugated or conjugated, such as cholate and taurocholate. Also responsible for bile acid transport in the renal proximal tubules, a salvage mechanism that helps conserve bile acids. Works collaboratively with the Na(+)-taurocholate cotransporting polypeptide (NTCP), the organic solute transporter (OST), and the bile salt export pump (BSEP), to ensure efficacious biological recycling of bile acids during enterohepatic circulation (By similarity).
Catalytic Activity: 2 Na(+)(out) + taurocholate(out) = 2 Na(+)(in) + taurocholate(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38024
Sequence Length: 348
Subcellular Location: Membrane
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Q3UEZ8 | MDSLDNTTLLLAPSSLLPDNLTLSPNAGSPSASTLSPLAVTSSPGPGLSLAPSPSIGFSPEATPTPEPTSSSLTVGVAGQGSSAFPRPWIPHEPPFWDTPLNHGLNVFVGAALCITMLGLGCTVDVNHFGAHVRRPVGALLAALCQFGFLPLLAFLLALIFKLDEVAAVAVLLCGCCPGGNLSNLMSLLVDGDMNLSIIMTISSTLLALVLMPLCLWIYSRAWINTPLVQLLPLGAVTLTLCSTLIPIGLGVFIRYKYNRVADYIVKVSLWSLLVTLVVLFIMTGTMLGPELLASIPATVYVVAIFMPLAGYASGYGLATLFHLPPNCKRTVCLETGSQNVQLCTAILKLAFPPRFIGSMYMFPLLYALFQSAEAGVFVLIYKMYGSEILHKREALDEDEDTDISYKKLKEEEMADTSYGTVGTDDLVMMETTQTAL | Function: Transporter for bile acids.
PTM: Activated following N-terminal proteolytic cleavage by thrombin and/or proteases.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46642
Sequence Length: 437
Subcellular Location: Cell membrane
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Q5ZJH8 | MGLLERLRKEWFIAGIALVIAAARLEPAVGVKGGPLKPEITITYIAVSAIFFNSGLSLKTEELTSALMHVKLHLFVQIFTLVFFPTAIWLFLQLLSITPINEWLLKGLQTVGCMPPPVSSAVILTKAVGGNEAAAIFNSAFGSFLLGSSSSVPFTSIFSQLFMTVVVPLIIGQIVRRYIKDWLERRKPPFGTISSCVLLMIIYTTFCDTFANPNIDLDKFSLIIIVFIIFSVQMSFMFLTFLFSTRSNSGFTPADTVAIIFCSTHKSLTLGIPMLKIVFAGYEHLSLISVPLLIYHPAQILLGSLLVPTIKSWMVSRQKALKLTRQPKVPVKV | Function: Involved in teeth and skeletal development. Has an essential role in the biosynthesis and trafficking of glycosaminoglycans and glycoproteins to produce a proper functioning extracellular matrix. Required for extracellular matrix mineralization. Also involved in the regulation of cellular calcium homeostasis. Does not show transport activity towards bile acids or steroid sulfates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36777
Sequence Length: 333
Subcellular Location: Cell membrane
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Q6DHK8 | MGLIARVRKEWFIIGIVLVITFAKLQPSVGVKGGPLHPEITITYVAVSVIFFNSGLSLKTEELASALMHVKLHFFVQTFTLVFFPIAIWLLLKVLALTAINEWLLRGLQTVACMPPPVSSAVILTKAVGGNEAAAIFNSAFGSFLGIVVTPLLLLVFLGSSSSVPFTSIFSQLFMTVVVPLIVGQVCRRFLRECLDRRKPPFGAVSSVVLLMIIYSTFCDTFNNPNIELDHLSLLTVVFIIFSIQLSFMALIFFLSTRKSSGFSAADSVAIMFCATHKSLTLGIPMLKIVFEGYEHLSLISVPLLIYHPAQILLGSVLLPSIKTWMSGRQKTLTPI | Function: Involved in teeth and skeletal development . Has an essential role in the biosynthesis and trafficking of glycosaminoglycans and glycoproteins to produce a proper functioning extracellular matrix (By similarity). Required for extracellular matrix mineralization . Also involved in the regulation of cellular calcium homeostasis (By similarity). Does not show transport activity towards bile acids or steroid sulfates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36838
Sequence Length: 336
Subcellular Location: Cell membrane
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Q0GE19 | MRLLERMRKDWFMVGIVLAIAGAKLEPSIGVNGGPLKPEITVSYIAVATIFFNSGLSLKTEELTSALVHLKLHLFIQIFTLAFFPATIWLFLQLLSITPINEWLLKGLQTVGCMPPPVSSAVILTKAVGGNEAAAIFNSAFGSFLGIVITPLLLLLFLGSSSSVPFTSIFSQLFMTVVVPLIIGQIVRRYIKDWLERKKPPFGAISSSVLLMIIYTTFCDTFSNPNIDLDKFSLVLILFIIFSIQLSFMLLTFIFSTRNNSGFTPADTVAIIFCSTHKSLTLGIPMLKIVFAGHEHLSLISVPLLIYHPAQILLGSVLVPTIKSWMVSRQKGVKLTRPTV | Function: Involved in teeth and skeletal development. Has an essential role in the biosynthesis and trafficking of glycosaminoglycans and glycoproteins, to produce a proper functioning extracellular matrix. Required for extracellular matrix mineralization . Also involved in the regulation of cellular calcium homeostasis . Does not show transport activity towards bile acids or steroid sulfates (including taurocholate, cholate, chenodeoxycholate, estrone-3-sulfate, dehydroepiandrosterone sulfate (DHEAS) and pregnenolone sulfate).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37432
Sequence Length: 340
Subcellular Location: Cell membrane
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Q5PT53 | MRLLERARKEWFMVGIVVAIGAAKLEPSVGVNGGPLKPEITVSYIAVATIFFNSGLSLKTEELTSALVHLRLHLFIQIFTLAFFPAAIWLFLQLLSVTSINEWLLKGLQTVGCMPPPVSSAVILTKAVGGNEAAAIFNSAFGSFLGIVVTPVLLLLFLGSSSSVPFTSIFSQLFMTVVVPLVIGQIVRRYIKDWLERKKPPFGVVSSSVLLMIIYTTFCDTFSNPNIDLDKFSLILILFIIVSVQLSFMLLTFIFSTRNNSGFTPADTVAIIFCSTHKSLTLGIPMLKIVFAGHEHLSLISVPLLIYHPAQILLGSVLVPTIKSWMVSRQKGVKLTRPTV | Function: Involved in teeth and skeletal development. Has an essential role in the biosynthesis and trafficking of glycosaminoglycans and glycoproteins to produce a proper functioning extracellular matrix. Required for extracellular matrix mineralization . Also involved in the regulation of cellular calcium homeostasis (By similarity). Does not show transport activity towards bile acids or steroid sulfates (including taurocholate, cholate, chenodeoxycholate, estrone-3-sulfate, dehydroepiandrosterone sulfate (DHEAS) and pregnenolone sulfate).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37256
Sequence Length: 340
Subcellular Location: Cell membrane
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Q28HF8 | MGLLERLRKEWFIVGIILVIAAAKLEPTIGGKGGPLKPEITITYIAVSAIFFNSGLSLKTEELTNALMHVKLHLFVQLFTLVFFPTAIWVFLQVLSLTPINEWLLKGLQTVSCMPPPVSSAVILTKAVGGNEAAAIFNSAFGSFLGIVVTPLLLLLFLGSSSSVPFTSIFSQLFMTVVVPLIIGQIVRRYIKDWLERKKPPFGAISSCVLLMIIYTTFCDTFSNPNIDLDTFSLVIIVFIIFFIQLAFMLLTFLFSTSKNTGFTPADTVAIVFCSTHKSLTLGIPMLKIVFAGYEHLSLISVPLLIYHPAQILLGSVLVPTIKSWMLSRQKALKLTRQPKVPL | Function: Involved in teeth and skeletal development. Has an essential role in the biosynthesis and trafficking of glycosaminoglycans and glycoproteins to produce a proper functioning extracellular matrix. Required for extracellular matrix mineralization. Also involved in the regulation of cellular calcium homeostasis. Does not show transport activity towards bile acids or steroid sulfates.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37812
Sequence Length: 343
Subcellular Location: Cell membrane
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Q12311 | MNRGSLDDGPKLREEKHFQDFYPDLNADTLLPFIVPLVETKDNSTDTDSDDISNRNNREIGSVKSVQTKELIFKGRVTTEPLVLKKNEVEFQKCKITTNELKGKKNPYCVRFNESFISRYYHINKVRNRKSYKQQQKEFDGVEAPYFTKFSSKEAPNITISTSTKSAIQKFASISPNLVNFKPQYDMDEQDELYLHYLNKRYFKDQMSHEIFEILMTTLETEWFHIEKHIPSTNSLIARHNILRDCKNYELYGSDDGTGLSMDQACAVCLGTDSDNLNTIVFCDGCDIAVHQECYGIIFIPEGKWLCRRCMISKNNFATCLMCPSHTGAFKQTDTGSWVHNICALWLPELYFSNLHYMEPIEGVQNVSVSRWKLNCYICKKKMGACIQCFQRNCFTAYHVTCARRAGLYMSKGKCTIQELASNQFSQKYSVESFCHKHAPRGWQTSIEGINKARKYFSLLSTLQTETPQHNEANDRTNSKFNKTIWKTPNQTPVAPHVFAEILQKVVDFFGLANPPAGAFDICKYWSMKRELTGGTPLTACFENNSLGSLTEEQVQTRIDFANDQLEDLYRLKELTTLVKKRTQASNSLSRSRKKVFDIVKSPQKYLLKINVLDIFIKSEQFKALERLVTEPKLLVILEKCKHCDFDTVQIFKEEIMHFFEVLETLPGASRILQTVSSKAKEQVTNLIGLIEHVDIKKLLSRDFIINDDKIEERPWSGPVIMEEEGLSDAEELSAGEHRMLKLILNSG | Function: Component of the NuA3 histone acetyltransferase complex, that acetylates Lys-14 of histone H3. Recruitment of NuA3 to nucleosomes requires methylated histone H3. In conjunction with the FACT complex, NuA3 may be involved in transcriptional regulation.
Sequence Mass (Da): 86029
Sequence Length: 748
Domain: Residues 156 to 543 compose a region conserved in chromatin associated proteins.
Subcellular Location: Cytoplasm
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Q18411 | MRWRYTIRDQSPFEESSNCHRLTSSETANTFRWPMRTYNVYGFLLTCTCLLLILTIIPMSGGSSERVQRSVRSVVETKNNIKYGVICDAGSSGTRLFVYTLKPLSGGLTNIDTLIHESEPVVKKVTPGLSSFGDKPEQVVEYLTPLLRFAEEHIPYEQLGETDLLIFATAGMRLLPEAQKDAIIKNLQNGLKSVTALRVSDSNIRIIDGAWEGIYSWIAVNYILGRFDKENDSKVGMIDMGGASVQIAFEIANEKESYNGGNVYEINLGSIETNEDYKYKIYSTTFLGYGANEGLKKYENSLVKSGNSNDSCSPRGLNRLIGEFTVNGTGEWDVCLAQVSSLIGDKAQPSCPNPTCFLRNVIAPSVNLSTVQLYGFSEYWYTTSNFGSGGEYHYQKFTDEVRKYCQKDWNDIQDGFKRNEFPNADIERLGTNCFKAAWVTSVLHDGFNVDKTKHLFQSVLKIAGEEMQWALGAMLYHSKDLKFNLLEQLEVAQSTQQISNFFSFFVILIIVLAVALYRQLQSESTYKKYNFLRTDSKPDFLNV | Function: Seems to be able to hydrolyze CTP, ATP and UTP.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61239
Sequence Length: 543
Subcellular Location: Golgi apparatus membrane
EC: 3.6.1.15
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O72907 | MNTYAAYIDYALKKLDTFPVDMTGGNDNTVLLKDYQLFVAKVFLGLNSMNSILLFQETGVGKTITTVYMLKNLKKIYSEWTIIILVKKALIDDPWTHTILDYAPEVMKDCIIMNYDDQNFHNKFFTNIKSINVKSRIFIIIDECHNFISKSLTKEDNKKRNTKLVYNYIAKNLMQKNNKLICLSATPIVNDVREFQMLVNLLRPGILTPDKSLFYNKKLIDEKEIISKLGCICSYIVNNEASIFEDVENTTLFAKKTVHIKHVFMSKKQEELYLKARYLERKLGISVFKIYQRMASTFVFDDIPDKKKLTEEEYEKFVDSLSIDFKNTLYGKKISKQSLDILSAGGTINDIKDVKDIELYNYLYEHSCKFTFVCVSIIQSKGKCLVFEPFIRSSGIEILLQYFNVFGITYIEFSSRTKDIRSKSVSDFNKVDNTDGEITKVCVFSQSGNEGISFLSINDIFILDMTWNEASLKQIIGRAIRLNSHVNNPPERRYVNVYFVVAKLSSGRSSVDDILLDIIQSKSKEFSQLYKVFKHSSIEWIYSNYTDFQTVDDEKGFKKLISRNIILDENTITNKKKLTMGENIWYSFSSSLVSIHRGFKSMDNKIYDSEGFFITVLPDKPTIKIYEGKLIYILTVR | Function: DNA-dependent ATPase required for providing the needed energy to achieve the termination of early transcripts. Acts in concert with the RAP94 subunit of the virion RNA polymerase and the capping enzyme/VTF to catalyze release of UUUUUNU-containing nascent RNA from the elongation complex. NPH-I must bind ssDNA in order to exhibit ATPase activity (By similarity).
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 73774
Sequence Length: 637
Subcellular Location: Virion
EC: 3.6.1.15
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Q9YW39 | MHSIEHIVARHFNYALEKTKDLPKSINNEITNEIIILKDYQYLVSRIFIGLSELNSLLLFWDTGYGKTLTSVYIMKHLKLVFPQWFFVIFIKKSLYVDPWLNTLSKLGMKGQNIKFVLYDSSSSLKQFNVLYRTIISSINTKNRILIIIDEVHQVISRTIEKSSSTQRNFLSIFNKIVKLANSENNKLLCMSATPITNNVLEFKYLINLLRPKIIEFKEDFIVNNTLKNHEQLKNGLISITSYQKISEADSFTNTSYTEGFASKNIFYHNVTMTPEQSNIFNIADKHDKKSALGGLKTMRRLVSSFAFYDIKIKGSMSQIEYNKMVSEKLNEFKSIIGNFKFSNEFIDIFRNNDSFSNAKSSEIEIFDKIKQYSCKYIEACKIILNSNGKVLLYEPLVSFEGISTLKIYFNIFNISYVEYSSKTESTRDYNIDIFNKYDNLYGNKIKVCIFSAAGSEGISFSSINDIIILDLPWKESDIKQIIGRSIRLNSHEELPIEKRYVNVHFIIASTIDGKSVDKEIFDLIKSKQDKINVLNSFMKVISIEQIHSKYKYAEPVENEYIFNNIRHTKIDDVNENNVITKIIVSPIYYCSEDNLNIIYNGYLDKKTGIIYSNNIPIAKLILDENNIYKFFIKDDKLVYITKSIYE | Function: DNA-dependent ATPase required for providing the needed energy to achieve the termination of early transcripts. Acts in concert with the RAP94 subunit of the virion RNA polymerase and the capping enzyme/VTF to catalyze release of UUUUUNU-containing nascent RNA from the elongation complex. NPH-I must bind ssDNA in order to exhibit ATPase activity (By similarity).
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 75135
Sequence Length: 647
Subcellular Location: Virion
EC: 3.6.1.15
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Q08513 | MSSYHAAYIDYELRVTESMTDTMGTDTEITLKPYQHFVASVFLGLDKMHSLLLFHDTGVGKTITTTFIIKQLKNIYTNWSILLLVKKHL | Function: Serves two roles in transcription; it acts in concert with viral termination factor/capping enzyme to catalyze release of UUUUUNU-containing nascent RNA from the elongation complex, and it acts by itself as a polymerase elongation factor to facilitate readthrough of intrinsic pause sites.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 10240
Sequence Length: 89
EC: 3.6.1.15
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P05807 | MSKSHAAYIDYALRRTTNMPVEMMGSDVVRLKDYQHFVARVFLGLDSMHSLLLFHETGVGKTMTTVYILKHLKDIYTNWAIILLVKKALIEDPWMNTILRYAPEITKDCIFINYDDQNFRNKFFTNIKTINSKSRICVIIDECHNFISKSLIKEDGKIRPTRSVYNFLSKTIALKNHKMICLSATPIVNSVQEFTMLVNLLRPGSLQHQSLFENKRLVDEKELVSKLGGLCSYIVNNEFSIFDDVEGSASFAKKTVLMRYVNMSKKQEEIYQKAKLAEIKTGISSFRILRRMATTFTFDSFPERQNRDPGEYAQEIATLYNDFKNSLRDREFSKSALDTFKRGELLGGDASAADISLFTELKEKSVKFIDVCLGILASHGKCLVFEPFVNQSGIEILLLYFKVFGISNIEFSSRTKDTRIKAVAEFNQESNTNGECIKTCVFSSSGGEGISFFSINDIFILDMTWNEASLRQIVGRAIRLNSHVLTPPERRYVNVHFIMARLSNGMPTVDEDLFEIIQSKSKEFVQLFRVFKHTSLEWIHANEKDFSPIDNESGWKTLVSRAIDLSSNKNITNKLIEGTNIWYSNSNRLMSINRGFKGVDGRVYDVDGNYLHDMPDNPVIKIHDGKLIYIF | Function: DNA-dependent ATPase that acts as a 5' to 3' translocase on single-stranded DNA and thereby plays a role in transcription termination of viral early genes . Uses forward translocation in concert with the viral RNA polymerase RAP94/OPG109 subunit and the capping enzyme/VTF to catalyze release of UUUUUNU-containing nascent RNA from the elongation complex . In addition, acts as a positive elongation factor to assist transcription through problematic sequences .
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate
Sequence Mass (Da): 72310
Sequence Length: 631
Subcellular Location: Virion
EC: 3.6.1.15
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Q892M0 | MNFILASSSERRKELLKRIVENFEVIPSDYDEKEVAFNGNCSEYVMELSKGKALNVASKLKRDSGIIIASDTIVYFNGEVLGKPSSKEHAYEMLKSLSGEVHEVYSGIVIYDLSSKKIKADYSCSKVKFSNLDDKMIREYIKTGEPMDKAGSYGIQGYGGIFVEKIHGCYYNIVGLPINKLYFLLKEMGVNL | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 21586
Sequence Length: 192
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q1LQB1 | MTSILYLASQSPRRRELLTQLGVTYELLLADAGEDAEALEAVRPGESPDDYVQRVCALKADAALQRRARRGLPDAPILTSDTTVCRGGDILGKPADARDAAAMLASLSGTTHRVLTAVTVATSAGQRHALSISHVTFRPILAPEIERYVASGEPLGKAGAYGIQGRAAEFVERIDGSYSGIMGLPLFETAALLREAGLHF | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 21229
Sequence Length: 200
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q46Y94 | MHDYLYLASQSPRRRELLTQLGVRYELLLADDEEDAEALEVVQPGETPDDYVQRVCALKAEAALRRRERRALPDAPILTSDTTVCLGGEILGKPGDGADASAMLKALSGSTHRVLTAVTVVSTLGMHHALSISRVTFRAMTAAEIERYVDSGEPLGKAGAYGIQGRAAEFVERIEGSYSGIMGLPLFETAALLRQARLRF | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 21746
Sequence Length: 200
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q11VI6 | MFINHLHNTDIILASGSPRRKQLLEDAGINFRIHTKNVEENYPVYLQRSEIPLYLSKIKAHAVKADFPDSLIIAADTIVVQRRDVFNKPGSAEEAKDMLRKLSNNMHEVITGVTICYGEKERSFYDITEVFFKPLSETYINYYIENHKPFDKAGAYGIQEWLGMVGIKKIQGDFYNVMGLPVSKLIDELEKMFNPELELNQINSNRPEEPNKYLYFGI | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 25196
Sequence Length: 218
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q3Z7G4 | MPDCQNTNLPEIILASASPRRQQILREMGFTFSVCPSQAELHPDGSVAPAKFATLNAETKARDIARNTRQGLIIAADTVVVDTLGILGKPASPEEALNYLLRLGGKSHTVISGICLINTQNGQVRSGTCQSSLHMRPFTPAEAQRYVESGLPMDKAGAYGIQDREFEPVEKIEGCYLNVVGLPACTLVRLMKEMGFCPELHDNWQPEGDCTLCRIYRTGINQTC | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 24480
Sequence Length: 224
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q9RV24 | MPAETAPRVILASGSPRRRELLGNLGVPFEVVVSGEAEDSQETDPARLALELGQLKARAVAAQHPDAVVIAADTVVALGGTLLAKPADEAENAAFLRQQSGKTQQVYTGVCVISPAGEQSGVERTDVTFRALTEAEVTFYARSGEGLDKAGGYGIQGVGMALIERVEGDYSNIVGFPLALVLRLLRGAGVSAFGV | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 20263
Sequence Length: 195
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q24SM2 | MVTIWLGSGRMLVLASASPRRAMLLEAEGFSFIRVEADVSEVLPQGISPESAVKGLALRKAQAGLNRWLNHGGSREDIILGADTIVVLNQQILGKPRDEEEAEAMLTALSGQTHYVYTGVALVNGAGRQECGAVCTAVFFRSLTHEEILEYIATGEPVDKAGAYGIQGLGGHLVDHYEGSLSNVIGLPMEYVKERLSVWGMGLGDIALHEVKDGLPSVKGST | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 23686
Sequence Length: 222
Subcellular Location: Cytoplasm
EC: 3.6.1.9
|
Q6AMI5 | MYKCDKPLILASSSPRRKAFLDQLGLEYSVRVKSIDEFAQPEESPEAFVCRMALEKGSAVSYQHPDSWVIAADTIVCLDQKILGKPRDSEDAVAMLCRLAGRSHTVMTAFAIICEKEKISEVQLVETSVYFSSFGEVEARAYVATGEPLDKAGSYGIQGVGALFVRKIAGSYSNVVGLPLAELVERLLYYSVISI | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 21383
Sequence Length: 195
Subcellular Location: Cytoplasm
EC: 3.6.1.9
|
A4J7K7 | MRPIILASASPRRQELLKNLGLEFEVQVSDVDENLEENISSGQLVEKLAERKAAAVALIRTQGLVIGADTIVVLGDKPLGKPTNREEAVQMLSNLQGKSHEVFTGLAVIDASTGQRVVTHQVTEVNFKTLTKDQIERYVDTGEPMDKAGGYAVQGLASIFIDSIRGCYFSVVGLPISKLADALRMFGVEIV | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: dTTP + H2O = diphosphate + dTMP + H(+)
Sequence Mass (Da): 20695
Sequence Length: 191
Subcellular Location: Cytoplasm
EC: 3.6.1.9
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Q2SXV1 | MQHDASSLPRLILASSSRYRRELLERLRAPFDVVTPEVDETPLPGETPSATALRLAAAKARAAAERVRAPHGALVIGSDQVATFDGLQIGKPGTHERALAQLQAMRGRDVEFHSALCLYDSRCGQTQIEDVVTRVRFRTLTDVELDAYLRAETPYDVAGSAKSEGLGIALLDAIDSDDPTALVGLPLIALTRMLRAAGYPLFDAPASAADGANGQ | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP
Sequence Mass (Da): 22989
Sequence Length: 215
Subcellular Location: Cytoplasm
EC: 3.6.1.-
|
Q47EH5 | MPQKLILASTSPYRRELLSRLGLAFDVANPQTDESPIFGESPESMALRLSEAKARAAAQAYPDALIIGSDQVATVNGNIYGKPGTHERAVKQLRELSGKTVNFFTGLCLLNARTGEAEVRGIPTLVTFRELTDSEIDNYLRREPAYNCAGSAKSEGLGIALMSSMRGDDPNALVGLPLIALCDMLRKQSLGVL | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP
Sequence Mass (Da): 20796
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 3.6.1.-
|
Q54TC5 | MTSRPLILGSSSIWRKQVLIDMGYIFKTMSPDIDEKAIRDSDPKTLTLLISRAKAQALLKRIKESDDELDKKSIMICSDQVIVHNGVIREKPETEQQCREYLQSYEFHPAVAVVSVVVVNIETGKIVEGTDIATQHFKKISDEFIDKLIKQGDVMHCAGGFTVEHMADFTLQLEGEVETILGLPKTLTKNLISQVSQ | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP
Sequence Mass (Da): 22118
Sequence Length: 197
Subcellular Location: Cytoplasm
EC: 3.6.1.-
|
P58626 | MPKLILASTSPWRRALLEKLQISFECAAPEVDETPHSDESPRQLVLRLAQEKAQSLASRYPDHLIIGSDQVCVLDGEITGKPLTEENARLQLRKASGNIVTFYTGLALFNSANGHLQTEVEPFDVHFRHLSEAEIDNYVRKEHPLHCAGSFKSEGFGITLFERLEGRDPNTLVGLPLIALCQMLRREGKNPLMG | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP
Sequence Mass (Da): 21672
Sequence Length: 194
Subcellular Location: Cytoplasm
EC: 3.6.1.-
|
Q2SK56 | MTNKSPHPSIILGSTSPYRAALLQKLNLNFQQAAPYFDEQITPTSLAPRDIAINFAKEKAESLREQFPDHLIIGSDQTAALNGLLLRKPGDKATAIKQLAACSGESVTFYSGLALINTRLNTTRTCVDWQTVYFRDLSREEIERYIELEKPYDCVGSFKVEGLGISLFEKIEGKDPNTLIGLPLIELITLLKKEGLRIP | Function: Nucleoside triphosphate pyrophosphatase that hydrolyzes 7-methyl-GTP (m(7)GTP). May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: H2O + N(7)-methyl-GTP = diphosphate + H(+) + N(7)-methyl-GMP
Sequence Mass (Da): 22153
Sequence Length: 199
Subcellular Location: Cytoplasm
EC: 3.6.1.-
|
Q5LLN0 | MTVPLILASGSAIRAQLLENAAVPFTKDVPRVDEESVKAALLAESAPPRDIADALAEMKARKISDKHPGAMVLGCDQVLDFQGRLLSKPDSPETALAELKQMSGQRHMLLSAAVIYENGQPVWRHVGQVRLRMRALSDSYLSGYVARNWDSIRHAVGGYKLEEEGVRLFSTIDGDHFNVLGMPLLELLNFLALRGVIDT | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 21816
Sequence Length: 199
Subcellular Location: Cytoplasm
EC: 3.6.1.9
|
Q1GCM3 | MSTHILLASGSEIRAKLLRQAGVDFRVEVARVDEDAIKTALEADGASPRDIADTLAEAKARKVSGKFPEEMVLGCDQVLDFEGTLLSKPKDKNQALQQLKAMRGKRHMLLSAAVIYCDAKPLWRHVGQVRLVMRMASDAYLESYVERNWESIRHAVGAYKLEEEGVRLFTTIDGSYFNVLGLPMLELMNYLGLQGIIEQ | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 22239
Sequence Length: 199
Subcellular Location: Cytoplasm
EC: 3.6.1.9
|
A4X378 | MSGSLPLRLVLASASPARRKTLQAAGIEPDVLVSGVDESLVASDRADELCLELARLKAQAVLTRLRPAQDQRTLVIGCDSVLEFDGQIFGKPADSADAIHRWERMRGRSGVLHSGHCLVDVTAGRRAEAVASTTVHFAAVSDDEIATYVATGEPLVVAGAFTIDGLGGPFVERIEGDPGTVVGLSLPLLRRLLAELNLPITGLWSRGTSTHPTPGTSATPKPNPGA | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 23686
Sequence Length: 226
Subcellular Location: Cytoplasm
EC: 3.6.1.9
|
Q1GP76 | MTLILASQSSGRAAMLRAAGLAFETTAAHVDEEMLTASLRAAGQTPRNIADALAEAKAVKIASRLPGVTVIGADSTLALDDGSMLAKPETPEEAADHLRRMAGRRHRLFSAAVAARDGAPIWRAIGEAKLWIRPLSDAFIADYVAQNWDSIRWTVGCYEIEGAGVQLFDRVEGDPWTIIGMPMLPLLTWLRATGLAPQ | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 21261
Sequence Length: 198
Subcellular Location: Cytoplasm
EC: 3.6.1.9
|
Q82I23 | MTDQPRRRLVLASQSPARLNLLRQAGLDPEVIVSGFDEDRLSAPTPAELALALAEAKASVVAAKPEVQGALVIGCDSVLDLDGEALGKPADAEEATARWKAMRGRAGTLQTGHCIYDTASKRYASATASTVVRFGEPTDEEIAAYVASGEPLHVAGAFTLDGRSAPFIEGIDGDHGNVIGISLPTVRRLLGELGVGITQLWTPREK | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 21684
Sequence Length: 206
Subcellular Location: Cytoplasm
EC: 3.6.1.9
|
Q9EWV6 | MTPQPRRRLVLASQSPARLGLLRQAGLAPEVLVSGVDEEAVTAPTPAELALALAEAKASVVAAKPEVHGALVIGCDSVLDLDGQALGKPADAEEATARWKAMRGRAGTLQTGHCVWDTASGRHVSATASTVVRFGEPTDDEIAAYVASGEPLHVAGAFTLDGRSAPFIDGIDGDHGNVIGLSLPLLRRLLADLGTGITELWAPAED | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 21266
Sequence Length: 206
Subcellular Location: Cytoplasm
EC: 3.6.1.9
|
Q31RS8 | MTTPRLILASASPARRRLLATVGLTVEVQPSHFDESLVQLNDPPALVQELAFRKAASVARSQTEPALVLGCDSVLAINGEICGKPASPAEAIARWQQMRGQWGELHTGHALIDSASQRRWLACGTTRVRFAEVEDAEIKAYVATGEPLACAGAFALEGKGGLFIAEIQGCHTNVIGLSLPLLRELLLAADYPLLQAWQT | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 21335
Sequence Length: 199
Subcellular Location: Cytoplasm
EC: 3.6.1.9
|
Q0IBR4 | MLLLASASPARRRLLEQAQIPHQVMVSGVDEDQIHHPDPAQLVQLLAEAKASAVKLKVEQSAELNVSIKAVLGCDSVLAFEGEVFGKPVDAAEAVARWQRMRGKWAELHTGHCLIPPSFAPTTEGRAPEMQCTCVTTRVLFANLTDVEVEDYVASGEPLQCAGGFALEGRGGCCVEQLAGCYSNVIGLSLPLLRRWLSLS | Function: Nucleoside triphosphate pyrophosphatase. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Catalytic Activity: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate + H(+)
Sequence Mass (Da): 21533
Sequence Length: 200
Subcellular Location: Cytoplasm
EC: 3.6.1.9
|
P25706 | MIIDRVEVETINSFSKLELFKEIYGLIWILPIFALLLGITIEVLVIVWLEREISASIQQRIGPEYAGPLGLLQAIADGTKLLLKEDILPSRGDIPLFSIGPSIAVISILLSFLVIPLGYRFVLADLSIGVFLWIAISSIAPIGLLMAGYSSNNKYSFLGGLRAAAQSISYEIPLTFCVLAISLLSNSLSTVDIVEAQSKYGFFGWNLWRQPIGFLVFLISSLAECERLPFDLPEAEEELVAGYQTEYSGIKYGLFYLVSYLNLLVSSLFVTVLYLGGWNFSIPYISFFGFFQMNKIIGILEMVIGIFITLTKAYLFLFISITIRWTLPRMRMDQLLNLGWKFLLPISLGNLLLTTSFQLVSL | 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 (By similarity).
Catalytic Activity: a plastoquinone + (n+1) H(+)(in) + NADH = a plastoquinol + n H(+)(out) + NAD(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40511
Sequence Length: 362
Subcellular Location: Plastid
EC: 7.1.1.-
|
P19040 | LAETNRTPFDLAEGECQVSVGFNTEYMHSSVGFALIMLSESEYASILFMSLFSVMFCLVVYSYLWSRGSYPRYRYDNLMHLCWKTSFTYIFNIPVFLLKPFSSGLKNKDPWLYNQPYSAFKTDALIGQGV | 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: Multi-pass membrane protein
Sequence Mass (Da): 15014
Sequence Length: 130
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
|
Q37714 | MIYFIFLQVVMVLVSVAFLTLLERKILGYIQLRKGPNKVGFLGILQPFSDGVKLFCKEVSLPLVSNFMPYLVAPVFSLFLSFFLWTLVPFISYGAKFNLSFLLVICAMSVSVYSIMVAGWSSNSKYSLLGSIRAGAQTISYEVSLIIIILSPLMLFKKLDLEGYLVKSSYVGWPLYLCLPLGLCWFTTILAETNRTPFDLAEGESELVSGFNTEYMGVGFALIMLSEYASILFMSLLFSVVFGSMSFLMFCLVVYSYLWSRGSYPRYRYDNLMHLCWKSLLPTSLMFLCFYWSLSQGG | 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: Multi-pass membrane protein
Sequence Mass (Da): 33763
Sequence Length: 298
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.2
|
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