ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q5ACZ2 | MVSLQQLTISILLLFTASVQSLDINVDDKDSICSAAKYVVQGIWNYYEGLKYGGTVGMFAPPNYWWNAGEAFGGLVDFYTYCQSDNSTLEKLIYNGMYHQAGENYNYIPSNQSMTEGNDDQGVWGMAIMEAVERNFTEPESHSWLEMVQAVFNTMNARWDADNCGGGLRWQIFTWNSGYDYKNSISNGCLFHLAARLARYTGNSSVYVDTAEKVWKWMEDVGFLTEEDNGDVRIYDGAKITNNCSSVTDLRWSYTYGVFMAGCAYLYNFTGDDVWLTRTNEIVQASLSYFFANKIMQETTCQPQNKCNNDQRSFRCLFSRCLGLTTQLAPETKDRIREVLEASAEGAAKSCSGGSDGVTCGENWAIDKWDGVYGLGEQTSALEVMMALIVEPPLSVKTGGTNRTDYSAGTNSEDNANKNELTITGKDKAGAGVLTAIVLAVILGGAIWMIF | Function: Required for normal synthesis of the cell wall and alkaline pH-induced hypha formation.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer.
Location Topology: Lipid-anchor
Catalytic Activity: Random hydrolysis of (1->6)-alpha-D-mannosidic linkages in unbranched (1->6)-mannans.
Sequence Mass (Da): 50031
Sequence Length: 451
Subcellular Location: Secreted
EC: 3.2.1.101
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Q05031 | MIVNISAKMILSICFTFLSFFKATHAMDLDTTSKTSICDATALIQGGMLDYYEGTRYGGTVGMFQSPYYWWHAGEAFGGMLENWFLCENDTYQELLYDALLAQTGSNYDYIPSNQTMVEGNDDQGIWGITVMGAVERNFTDPGDGKPGWLAMVQAVFNTMYSRWDSEHCGGGLRWQIFTWNSGYNYKNTVSNACLFQIAARLGRYTGNTTYLEVAEQVFDWLVDVGYVVLNDTANVFDGAEIDTNCTDITKIEWTYNHGIVLGGLAYMYNATNGTGEWETSLTKILNGAKSYFFKDSIMYESACQDYGTCNTDQRTFKSIFSRMLGLTSVMAPFTRDTIDDLIKTSAEAAAKSCNGGTDGHTCGLNWQKQTNDGYYGLGEQMSALEVIQNLLIHDRPAPYKEDNGGTSKGDANAGMNSSTTNVLQNNLNIKKGDRAGAAIITAVILSVLTGGAVWMLF | Function: Required for normal synthesis of the cell wall.
PTM: N-glycosylated.
Location Topology: Lipid-anchor
Catalytic Activity: Random hydrolysis of (1->6)-alpha-D-mannosidic linkages in unbranched (1->6)-mannans.
Sequence Mass (Da): 50541
Sequence Length: 458
Subcellular Location: Cell membrane
EC: 3.2.1.101
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Q5AFI4 | MEKLSINNNNNNRRYQSRRFDGITIIRIVVLVFIVTVSTYFVNSYTCNQPHHNHSTRPSHYLPINGTHGLMNNDDSLHNKGAIGHYNTTVSLERRADENNSTTNGLFPSTSSSTFIFTPSSSSSSTFQQSRSSPQTTSTSSFVATTSSFQQETSQTSIPDTTTDFSFSSFSEAPTTSTTSSTSEFSSTPQETSNTVTSTSSTSTSSSSSPTSSPATTSASQHVTTFSSVDNGKTIVVTRTSVISSSPTASNSNNNKNNDNGGGLSHTNRIVVGVVVGVGGSILIGLLAVLFYLRKRNNRDYEGGWTFWRKNEKLGSDEFFNGELGVRDRNINQGSNF | Function: Cell-surface associated glycoprotein that acts as a plasma membrane receptor-type protein which senses the presence of matrix. Binds to calmodulin in response to environmental conditions and initiates a signaling cascade that activates CEK1, thus promoting invasive filamentation. Involved in the maintenance of the cell wall.
PTM: Cross-linked to the carbohydrate polymers of the cell wall.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36489
Sequence Length: 337
Domain: The GxxxG glycophorin motif in the transmembrane domain is required for CEK1 activation and subsequent invasive filamentation on agar medium.
Subcellular Location: Cell membrane
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P37530 | MNTAPFIAIEGPIGAGKTTLATMLSQKFGFPMINEIVEDNPYLDKFYDNIKEWSFQLEMFFLCHRYKQLEDTSDHFLKKGQPVIADYHIYKNVIFAERTLSPHQLEKYKKIYHLLTDDLPKPNFIIYIKASLPTLLHRIEKRGRPFEKKIETSYLEQLISDYEVAIKQLQEADPELTVLTVDGDSKDFVLNKSDFERIAAHVKELIV | Function: Plays an essential role in generating the deoxyribonucleotide precursors dGTP for DNA metabolism. Highly specific toward deoxyguanosine (dGuo) and deoxyinosine (dIno). Only marginal activity is observed with guanosine. UTP is slightly more efficient as phosphate donor than CTP, ATP and GTP.
Catalytic Activity: 2'-deoxyguanosine + ATP = ADP + dGMP + H(+)
Sequence Mass (Da): 24145
Sequence Length: 207
EC: 2.7.1.113
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Q54UT2 | MFRRSLMFMISNNKNTNMVSSINTTNKVNNFSKIIILEGNISAGKTYLSSKLGDLLGYKVFLEPTATNPYLSLFYKEPSKYALIMQKWLLNQRYNTFLNALQYSLENEQGVILDRSVYSDWVFAENCRSEGLISAEGFKEYNSIRDRFLSNIPIPNVTLFLDVDPKQCLQRIQNRKRDCEQSIPLSYLSGLDNCYKKFLIEMKSKGSNVIILDWNNFGDINLVLNEINNDNFNNFNNSNNSKFNDVNYKKQQLISDIENEKNNLKEMKFFLNENNNNNNQEKIKS | Function: Purine-specific deoxyribonucleoside kinase that phosphorylates preferentially deoxyguanosine, as part of the deoxyribonucleotide salvage pathway.
Catalytic Activity: 2'-deoxyguanosine + ATP = ADP + dGMP + H(+)
Sequence Mass (Da): 33193
Sequence Length: 285
Subcellular Location: Cytoplasm
EC: 2.7.1.113
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Q8NCG7 | MPGMVLFGRRWAIASDDLVFPGFFELVVRVLWWIGILTLYLMHRGKLDCAGGALLSSYLIVLMILLAVVICTVSAIMCVSMRGTICNPGPRKSMSKLLYIRLALFFPEMVWASLGAAWVADGVQCDRTVVNGIIATVVVSWIIIAATVVSIIIVFDPLGGKMAPYSSAGPSHLDSHDSSQLLNGLKTAATSVWETRIKLLCCCIGKDDHTRVAFSSTAELFSTYFSDTDLVPSDIAAGLALLHQQQDNIRNNQEPAQVVCHAPGSSQEADLDAELENCHHYMQFAAAAYGWPLYIYRNPLTGLCRIGGDCCRSRTTDYDLVGGDQLNCHFGSILHTTGLQYRDFIHVSFHDKVYELPFLVALDHRKESVVVAVRGTMSLQDVLTDLSAESEVLDVECEVQDRLAHKGISQAARYVYQRLINDGILSQAFSIAPEYRLVIVGHSLGGGAAALLATMLRAAYPQVRCYAFSPPRGLWSKALQEYSQSFIVSLVLGKDVIPRLSVTNLEDLKRRILRVVAHCNKPKYKILLHGLWYELFGGNPNNLPTELDGGDQEVLTQPLLGEQSLLTRWSPAYSFSSDSPLDSSPKYPPLYPPGRIIHLQEEGASGRFGCCSAAHYSAKWSHEAEFSKILIGPKMLTDHMPDILMRALDSVVSDRAACVSCPAQGVSSVDVA | Function: Lipase that catalyzes the hydrolysis of arachidonic acid (AA)-esterified diacylglycerols (DAGs) to produce the principal endocannabinoid, 2-arachidonoylglycerol (2-AG) which can be further cleaved by downstream enzymes to release arachidonic acid (AA) for cyclooxygenase (COX)-mediated eicosanoid production . Preferentially hydrolyzes DAGs at the sn-1 position in a calcium-dependent manner and has negligible activity against other lipids including monoacylglycerols and phospholipids . Plays a key role in the regulation of 2-AG and AA pools utilized by COX1/2 to generate lipid mediators of macrophage and microglia inflammatory responses. Functions also as a polyunsaturated fatty acids-specific triacylglycerol lipase in macrophages. Plays an important role to support the metabolic and signaling demands of macrophages (By similarity).
Catalytic Activity: a 1,2-diacyl-sn-glycerol + H2O = a 2-acylglycerol + a fatty acid + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73732
Sequence Length: 672
Subcellular Location: Cell membrane
EC: 3.1.1.116
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Q6BF16 | MQWQTKLPLIAILRGITPDEALAHVGAVIDAGFDAVEIPLNSPQWEQSIPAIVDAYGDKALIGAGTVLKPEQVDALARMGCQLIVTPNIHSEVIRRAVGYGMTVCPGCATATEAFTALEAGAQALKIFPSSAFGPQYIKALKAVLPSDIAVFAVGGVTPENLAQWIDAGCAGAGLGSDLYRAGQSVERTAQQAAAFVKAYREAVQ | Function: Involved in the degradation of galactose via the DeLey-Doudoroff pathway. Catalyzes the reversible, stereospecific retro-aldol cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) to pyruvate and D-glyceraldehyde-3-phosphate. In the synthetic direction, it catalyzes the addition of pyruvate to electrophilic aldehydes with re-facial selectivity. It can use a limited number of aldehyde substrates, including D-glyceraldehyde-3-phosphate (natural substrate), D-glyceraldehyde, glycolaldehyde, 2-pyridinecarboxaldehyde, D-ribose, D-erythrose and D-threose. It efficiently catalyzes aldol addition only using pyruvate as the nucleophilic component and accepts both stereochemical configurations at C2 of the electrophile.
Catalytic Activity: 2-dehydro-3-deoxy-6-phospho-D-galactonate = D-glyceraldehyde 3-phosphate + pyruvate
Sequence Mass (Da): 21391
Sequence Length: 205
Pathway: Carbohydrate acid metabolism; D-galactonate degradation; D-glyceraldehyde 3-phosphate and pyruvate from D-galactonate: step 3/3.
EC: 4.1.2.21
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Q92RN8 | MDRIPLPPMERPLIAILRGLKPEEAEGVVGALIETGFTAIEIPLNSPDPFRSIETAVKMAPAGCLIGAGTVLTTAQVERLADVGGRLMVSPNVEPAVIRLAATKGMVTMPGVFTPTEALAAAAAGASGLKFFPASVLGPSGITAIRAVLPGDLEIAAVGGVSEVNFADYAAIGIRSFGLGSSLYKPGMSAGDVRQRAIATLAAYDAVYGGQQ | Function: Involved in the degradation of galactose via the DeLey-Doudoroff pathway. Catalyzes the reversible, stereospecific retro-aldol cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) to pyruvate and D-glyceraldehyde-3-phosphate (By similarity).
Catalytic Activity: 2-dehydro-3-deoxy-6-phospho-D-galactonate = D-glyceraldehyde 3-phosphate + pyruvate
Sequence Mass (Da): 21588
Sequence Length: 212
Pathway: Carbohydrate acid metabolism; D-galactonate degradation; D-glyceraldehyde 3-phosphate and pyruvate from D-galactonate: step 3/3.
EC: 4.1.2.21
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P09788 | MSEQNNAVLPKGVTQGEFNKAVQKFRALLGDDNVLVESDQLVPYNKIMMPVENAAHAPSAAVTATTVEQVQGVVKICNEHKIPIWTISTGRNFGYGSAAPVQRGQVILDLKKMNKIIKIDPEMCYALVEPGVTFGQMYDYIQENNLPVMLSFSAPSAIAGPVGNTMDRGVGYTPYGEHFMMQCGMEVVLANGDVYRTGMGGVPGSNTWQIFKWGYGPTLDGMFTQANYGICTKMGFWLMPKPPVFKPFEVIFEDEADIVEIVDALRPLRMSNTIPNSVVIASTLWEAGSAHLTRAQYTTEPGHTPDSVIKQMQKDTGMGAWNLYAALYGTQEQVDVNWKIVTDVFKKLGKGRIVTQEEAGDTQPFKYRAQLMSGVPNLQEFGLYNWRGGGGSMWFAPVSEARGSECKKQAAMAKRVLHKYGLDYVAEFIVAPRDMHHVIDVLYDRTNPEETKRADACFNELLDEFEKEGYAVYRVNTRFQDRVAQSYGPVKRKLEHAIKRAVDPNNILAPGRSGIDLNNDF | Cofactor: Binds 1 FAD covalently per subunit.
Function: Catalyzes the azurin dependent hydroxylation of the methyl group of 4-methylphenol to form 4-hydroxybenzaldehyde.
Catalytic Activity: 4-methylphenol + H2O + 4 oxidized [azurin] = 4-hydroxybenzaldehyde + 4 H(+) + 4 reduced [azurin]
Sequence Mass (Da): 57945
Sequence Length: 521
Pathway: Aromatic compound metabolism; p-cresol degradation.
EC: 1.17.9.1
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Q2FYJ2 | MLVAVVKELKQGEGRVACTPENVRKLTDAGHKVIVEKNAGIGSGFSNDMYEKEGAKIVTHEQAWEADLVIKVKEPHESEYQYFKKNQIIWGFLHLASSKEIVEKMQEVGVTAISGETIIKNGKAELLAPMSAIAGQRSAIMGAYYSEAQHGGQGTLVTGVHENVDIPGSTYVIFGGGVAATNAANVALGLNAKVIIIELNDDRIKYLEDMYAEKDVTVVKSTPENLAEQIKKADVFISTILISGAKPPKLVTREMVKSMKKGSVLIDIAIDQGGTIETIRPTTISDPVYEEEGVIHYGVPNQPGAVPRTSTMALAQGNIDYILEICDKGLEQAIKDNEALSTGVNIYQGQVTNQGLASSHDLDYKEILNVIE | Function: May play a role in cell wall synthesis as L-alanine is an important constituent of the peptidoglycan layer.
Catalytic Activity: H2O + L-alanine + NAD(+) = H(+) + NADH + NH4(+) + pyruvate
Sequence Mass (Da): 40225
Sequence Length: 372
Pathway: Amino-acid degradation; L-alanine degradation via dehydrogenase pathway; NH(3) and pyruvate from L-alanine: step 1/1.
EC: 1.4.1.1
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Q2THW0 | MPSGSMSGGVSGPTSPPHPTVPSRPLRPSRYVPVSAATAFLVGSTTLFFCFTCPWLSEQFSVAVPIYNGVMFMFVLANFCMATFMDPGIFPRAEEDEDKEDDFRAPLYKTVEIRGIQVRMKWCSTCRFYRPPRCSHCSVCDNCVEDFDHHCPWVNNCIGRRNYRYFFLFLLSLTAHIMGVFGFGLLFILYHTQQLDRVHSAVTMAVMCVAGLFFIPVAGLTGFHVVLVARGRTTNEQVTGKFRGGVNPFTNGCLRNVSHVLCSSQAPRYLGRKRKAQTVSVQPPFLRPQLTEAQLAAKVLDNGIQGDLHRSKSSLEMMESQSADAEPPPPPKPELRYPGLSRGPAGHSEESSLLNKAPPTPTMFKYRPTYSSPGKNHTALTHAYANQSSQQPGYRSEPSLDGREGGGAERSGAERTGGGPGGPPGSGIPGYSLGGRSYPSFSDPTVLAERASRSSSVRSTHNAPPSEATTSTSYKSLANQTPPQAARNGSLSYDSLLTPSESPDFESAAPEMSPGRPRTPVVGYSSPFLSAQIAHQREAELHQPVASSSALMASPQHAVFLRGSGSPPVPPERERERLLHDSQAQHHHHHHHHHHHHRPPRFSRPPLLSDSGPPQPSYPYRTRSTDTTHPPRSPHPPPLGKSLSYSSAAAAEMQYRLVRKASASVAGGGIQAPKDEIQMKSYSRTNGQPKPSSTPSSPTHPISVSTRPGQAHSSAGSSQSPAHKPGGGVKKVTGVGGTTYEISV | Function: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and is involved in a variety of cellular processes.
Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80501
Sequence Length: 744
Domain: The DHHC domain is required for palmitoyltransferase activity.
Subcellular Location: Cell membrane
EC: 2.3.1.225
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E7FBS9 | MPVGLSVGGALGDPSPSRPFRPSRYVPVSAATAFLVGATTLFLCFTCPWLSEKFSSFIPLYNVVVFLFTLANFCMATFMDPGVFPRAEEDEDKEDDFRAPLYKTVEVRGIQVRMKWCSTCRFYRPPRCSHCSVCDNCVEEFDHHCPWVNNCIGRRNYRYFFLFLLSLTVHIMDVFGFSLLYILHHTKQLDLVQSGVTMAVMCVAGLFFVPVAGLTGFHVVLVARGRTTNEQVTGKFRGGVNPFTHGCFKNIAHVLCSSQAPRYLGRLRKPQSVQVQPPFLRPPLSEAQLAAKVLDNGIQQSKSSLEIMESQSTDADPPPPPKPEHRYPGLPHTQNEECSLLTEAPPTPSLYKYRPAYSSPGKNHTASTHSSKMSRGNSMTESPSVPVTTGQPSYRSDPSLSSRGAAGCRGGAEGGRSGSGGLGGASAFGGRSYPSFTDTLLQSAAASCSSSLRSAHTAHNALGPLISEGTTSTSYKSLANQTRNGSLSYESLLTPSESPEFESAAHELSPPRPHPPHSLSTAAGAAPILGYTSPFLSAQQREGSLQACPAPLRPSPNRAFLRPISSPPSRAPPLSPRARSLGSPPPGPAPGHTPLGKSMSYGGGAELQHRPSSSGGGTSMPNSTIKQNVANHNTHSHKPARGVKKVSGVGGTTYEISV | Function: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and is involved in a variety of cellular processes.
Catalytic Activity: hexadecanoyl-CoA + L-cysteinyl-[protein] = CoA + S-hexadecanoyl-L-cysteinyl-[protein]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70489
Sequence Length: 658
Domain: The DHHC domain is required for palmitoyltransferase activity.
Subcellular Location: Cell membrane
EC: 2.3.1.225
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Q9UBM7 | MAAKSQPNIPKAKSLDGVTNDRTASQGQWGRAWEVDWFSLASVIFLLLFAPFIVYYFIMACDQYSCALTGPVVDIVTGHARLSDIWAKTPPITRKAAQLYTLWVTFQVLLYTSLPDFCHKFLPGYVGGIQEGAVTPAGVVNKYQINGLQAWLLTHLLWFANAHLLSWFSPTIIFDNWIPLLWCANILGYAVSTFAMVKGYFFPTSARDCKFTGNFFYNYMMGIEFNPRIGKWFDFKLFFNGRPGIVAWTLINLSFAAKQRELHSHVTNAMVLVNVLQAIYVIDFFWNETWYLKTIDICHDHFGWYLGWGDCVWLPYLYTLQGLYLVYHPVQLSTPHAVGVLLLGLVGYYIFRVANHQKDLFRRTDGRCLIWGRKPKVIECSYTSADGQRHHSKLLVSGFWGVARHFNYVGDLMGSLAYCLACGGGHLLPYFYIIYMAILLTHRCLRDEHRCASKYGRDWERYTAAVPYRLLPGIF | Function: 7-dehydrocholesterol reductase of the cholesterol biosynthetic pathway reducing the C7-C8 double bond of cholesta-5,7-dien-3beta-ol (7-dehydrocholesterol/7-DHC) and cholesta-5,7,24-trien-3beta-ol, two intermediates in that pathway.
Catalytic Activity: cholesterol + NADP(+) = 7-dehydrocholesterol + H(+) + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54489
Sequence Length: 475
Pathway: Steroid biosynthesis; cholesterol biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.3.1.21
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Q5UQI4 | MNSYQTNTATSWGRNHIPTLLDNLTTAAMFMFCPFIILVFYLITYGEYLGSIGDFYLDIINGDWQTIWSNIPSFKINVLGACLLWIVFQLILSKLPDTIHRFVPHYVGGIKAGHITPAGNLVYYNINGLQAFIITHVLVIMSCYYGLFSPTIIMDNWGSIFWSVNIIGYLITFLAYFKALTFSSHPSDNKFTGKLFYDIVMGIEFNPEIFGTDLKLFFNGRPGIIAWNLINLSCAMKQYENFGYVSNSMILVIILQLIYIVDFFYNENWYVHTVDIAHDHFGWMLAWGDTVWLPFGYTLQAGYLMNNPIDLSTGFFNLVFVMGIIGYIIFRTANYQKDKYRSNTQGVKYIPCTYQTADGLNRASKLIYSGLWGVSRHMNYTGDIILSTAYCLACGFSHFIPYFYCVYMTILLVTRCLRDEQRCSRKYGKYWKMYTKRVPYRFIPGIY | Function: Production of cholesterol by reduction of C7-C8 double bond of cholesta-5,7-dien-3beta-ol (7-dehydrocholesterol/7-DHC).
Catalytic Activity: cholesterol + NADP(+) = 7-dehydrocholesterol + H(+) + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51692
Sequence Length: 447
Pathway: Steroid biosynthesis; cholesterol biosynthesis.
Subcellular Location: Membrane
EC: 1.3.1.21
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Q6P4M0 | MGERRRANASRGDKKVANGEKPHVGQWGRAWEVDYFSLAAVLFLLAFAPLIVYYFVMSCDQYQCALTAPVLDLYWGKAQLSDIWDKTPALTWGAAKIYIVWVSFQVFLYMLVPDILHKFVPGYEGGVQEGARTPAGLINKYQVNGLQAWTITHLLWFANAYHFHWFSPTIIIDNWVPLLWCANLLGYSVATFALLKAYFFPTNAHDCKFTGNFFYDYMMGIEFNPRIGKWFDFKLFFNGRPGIVAWTLINLSYAAKQQELYGQVTNSMILVNVLQAIYVVDFFWNESWYLKTIDICHDHFGWYLGWGDCVWLPYLYTLQGLYLVYNPVELSTATAVGVLLLGLIGYYIFRMTNHQKDLFRRTNGNCKIWGKKPKSIECSYTSADGKRHYSKLMISGFWGVARHLNYTGDLMGSLAYCLACGFDHLLPYFYFTYMTILLVHRCIRDEHRCSSKYGKDWKLYTDAVPYRLLPGLF | Function: 7-dehydrocholesterol reductase of the cholesterol biosynthetic pathway reducing the C7-C8 double bond of cholesta-5,7-dien-3beta-ol (7-dehydrocholesterol/7-DHC) and cholesta-5,7,24-trien-3beta-ol, two intermediates in that pathway.
Catalytic Activity: cholesterol + NADP(+) = 7-dehydrocholesterol + H(+) + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54785
Sequence Length: 473
Pathway: Steroid biosynthesis; cholesterol biosynthesis.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.3.1.21
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Q86SQ9 | MSWIKEGELSLWERFCANIIKAGPMPKHIAFIMDGNRRYAKKCQVERQEGHSQGFNKLAETLRWCLNLGILEVTVYAFSIENFKRSKSEVDGLMDLARQKFSRLMEEKEKLQKHGVCIRVLGDLHLLPLDLQELIAQAVQATKNYNKCFLNVCFAYTSRHEISNAVREMAWGVEQGLLDPSDISESLLDKCLYTNRSPHPDILIRTSGEVRLSDFLLWQTSHSCLVFQPVLWPEYTFWNLFEAILQFQMNHSVLQKARDMYAEERKRQQLERDQATVTEQLLREGLQASGDAQLRRTRLHKLSARREERVQGFLQALELKRADWLARLGTASA | Cofactor: Binds 1 magnesium ion per subunit.
Function: With NUS1, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Both subunits contribute to enzymatic activity, i.e. condensation of multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol phosphate which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER) . Synthesizes long-chain polyprenols, mostly of C95 and C100 chain length . Regulates the glycosylation and stability of nascent NPC2, thereby promoting trafficking of LDL-derived cholesterol .
Catalytic Activity: (2E,6E)-farnesyl diphosphate + n isopentenyl diphosphate = di-trans,poly-cis-polyprenyl diphosphate + n diphosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38657
Sequence Length: 333
Domain: The catalytic site at NUS1-DHDDS interface accomodates both the allylic and the homoallylic IPP substrates to the S1 and S2 pockets respectively. The beta-phosphate groups of IPP substrates form hydrogen bonds with the RXG motif of NUS1 and four conserved residues of DHDDS (Arg-85, Arg-205, Arg-211 and Ser-213), while the allylic isopentenyl group is pointed toward the hydrophobic tunnel of the S1 pocket where the product elongation occurs.
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.5.1.87
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F1QLP1 | MEDFAVSFWIYIGVMSIFVGGAVKKFLAFNIGAMPSVVVWLGATLLVERLCALCMPAVLARLVLCVCCWLYFTWATPKPSLPVEDKAVFITGCDSGFGNATAKKLDAMGFEVFATVLNLEGEGAKHLRKVCSSRLTLLQVDITQPQQVQQALLDTKAKLGIRDLWGLVNNAGWCVNIGDAELSLMSNYRGCMEVNFFGTVTVTRTFLPLLRQSKGRIVTISSPSGEHPFPCLASYGASKAALNLFINTLRHELDPWGVKVSTILPSAYKTGQSSNAEYWEKQYKSLLQGLSPNLLEEYGEEYLLETKELFQNYAKTANEDLSPVIDTIVEALLSPQPQVRYYAGPGLILMYFICSYLPLSISDRFLQKLFVQKKVMPRALIKQQGLSPNDNNNSIKENMNDSSSNNSNFTKCID | Function: Catalyzes the conversion of biologically active 11beta-hydroxyglucocorticoids (11beta-hydroxysteroid) such as cortisol, to inactive 11-ketoglucocorticoids (11-oxosteroid) such as cortisone, in the presence of NAD(+) . Cortisol is the primary glucocorticoid in teleosts and is released to increase glucose bioavailability in order to meet the increased energy demands in response to stress . Functions as a dehydrogenase (oxidase), thereby decreasing the concentration of active glucocorticoids, regulating the hypothalamus-pituitary-interrenal (HPI) axis function in adult fish . Decreasing the excess glucocorticoids may be of relevance to brain function and neural proliferation . Plays a key role by catalyzing the oxidation of 11beta-hydroxytestosterone (11beta,17beta-dihydroxyandrost-4-ene-3-one) to 11-ketotestosterone (17beta-hydroxyandrost-4-ene-3,11-dione), the major fish androgen, that activates androgen receptor transcriptional activity . Catalyzes the conversion of 11beta-hydroxyandrostenedione (11beta-hydroxyandrost-4-ene-3,17-dione) to 11-ketoandrostenedione (androst-4-ene-3,11,17-trione), which can be further metabolized to 11-ketotestosterone . Exerts a dual role in fish by inactivating glucocorticoids and activating androgens .
Catalytic Activity: an 11beta-hydroxysteroid + NAD(+) = an 11-oxosteroid + H(+) + NADH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45902
Sequence Length: 414
Pathway: Steroid metabolism.
Subcellular Location: Membrane
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P80365 | MERWPWPSGGAWLLVAARALLQLLRSDLRLGRPLLAALALLAALDWLCQRLLPPPAALAVLAAAGWIALSRLARPQRLPVATRAVLITGCDSGFGKETAKKLDSMGFTVLATVLELNSPGAIELRTCCSPRLRLLQMDLTKPGDISRVLEFTKAHTTSTGLWGLVNNAGHNEVVADAELSPVATFRSCMEVNFFGALELTKGLLPLLRSSRGRIVTVGSPAGDMPYPCLGAYGTSKAAVALLMDTFSCELLPWGVKVSIIQPGCFKTESVRNVGQWEKRKQLLLANLPQELLQAYGKDYIEHLHGQFLHSLRLAMSDLTPVVDAITDALLAARPRRRYYPGQGLGLMYFIHYYLPEGLRRRFLQAFFISHCLPRALQPGQPGTTPPQDAAQDPNLSPGPSPAVAR | Function: Catalyzes the conversion of biologically active 11beta-hydroxyglucocorticoids (11beta-hydroxysteroid) such as cortisol, to inactive 11-ketoglucocorticoids (11-oxosteroid) such as cortisone, in the presence of NAD(+) . Functions as a dehydrogenase (oxidase), thereby decreasing the concentration of active glucocorticoids, thus protecting the nonselective mineralocorticoid receptor from occupation by glucocorticoids . Plays an important role in maintaining glucocorticoids balance during preimplantation and protects the fetus from excessive maternal corticosterone exposure (By similarity). Catalyzes the oxidation of 11beta-hydroxytestosterone (11beta,17beta-dihydroxyandrost-4-ene-3-one) to 11-ketotestosterone (17beta-hydroxyandrost-4-ene-3,11-dione), a major bioactive androgen . Catalyzes the conversion of 11beta-hydroxyandrostenedione (11beta-hydroxyandrost-4-ene-3,17-dione) to 11-ketoandrostenedione (androst-4-ene-3,11,17-trione), which can be further metabolized to 11-ketotestosterone . Converts 7-beta-25-dihydroxycholesterol to 7-oxo-25-hydroxycholesterol in vitro . 7-beta-25-dihydroxycholesterol (not 7-oxo-25-hydroxycholesterol) acts as ligand for the G-protein-coupled receptor (GPCR) Epstein-Barr virus-induced gene 2 (EBI2) and may thereby regulate immune cell migration . May protect ovulating oocytes and fertilizing spermatozoa from the adverse effects of cortisol (By similarity).
Catalytic Activity: an 11beta-hydroxysteroid + NAD(+) = an 11-oxosteroid + H(+) + NADH
Sequence Mass (Da): 44127
Sequence Length: 405
Pathway: Steroid metabolism.
Subcellular Location: Microsome
EC: 1.1.1.-
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P51976 | MERWPWPSGGAWLLVAARALIQLLRADLRLGRPLLAALALLAALDWLCQSLLPPSAALAVLAAAGWIALSRLARPQRLPVATRAVLITGCDSGFGKETAKKLDAMGFTVLATVLEMNGPGALELRACCSPRLKLLQMDLTKPADISRALEFTKAHTTSTGLWGLVNNAGHNDVVADVELSPVATFRNCMEVNFFGALELTKGLLPLLHHSRGRIVTLGSPAGEMPYPCLAAYGTSKAAMALLMDAFSCELLPWGVKVSVIQPGCFKTESVSNVSHWEQRKQLLLANLPGELRQAYGEDYIEHLHREFLHSLRLALPDLSPVVDAITDALLAARPRPRYYPGRGLGLMYFIHYYLPEGLRRRFLQSFFIIPCLPRALRPGQPGATPAPDTAQDNPNPNPDPSLVGAR | Function: Catalyzes the conversion of biologically active 11beta-hydroxyglucocorticoids (11beta-hydroxysteroid) such as corticosterone, to inactive 11-ketoglucocorticoids (11-oxosteroid) such as 11-dehydrocorticosterone, in the presence of NAD(+) . Functions as a dehydrogenase (oxidase), thereby decreasing the concentration of active glucocorticoids, thus protecting the nonselective mineralocorticoid receptor from occupation by glucocorticoids (By similarity). Plays an important role in maintaining glucocorticoids balance during preimplantation and protects the fetus from excessive maternal corticosterone exposure (By similarity). Catalyzes the oxidation of 11beta-hydroxytestosterone (11beta,17beta-dihydroxyandrost-4-ene-3-one) to 11-ketotestosterone (17beta-hydroxyandrost-4-ene-3,11-dione), a major bioactive androgen. Catalyzes the conversion of 11beta-hydroxyandrostenedione (11beta-hydroxyandrost-4-ene-3,17-dione) to 11-ketoandrostenedione (androst-4-ene-3,11,17-trione), which can be further metabolized to 11-ketotestosterone. Converts 7-beta-25-dihydroxycholesterol to 7-oxo-25-hydroxycholesterol in vitro. 7-beta-25-dihydroxycholesterol (not 7-oxo-25-hydroxycholesterol) acts as ligand for the G-protein-coupled receptor (GPCR) Epstein-Barr virus-induced gene 2 (EBI2) and may thereby regulate immune cell migration (By similarity). May protect ovulating oocytes and fertilizing spermatozoa from the adverse effects of cortisol (By similarity).
Catalytic Activity: an 11beta-hydroxysteroid + NAD(+) = an 11-oxosteroid + H(+) + NADH
Sequence Mass (Da): 44182
Sequence Length: 406
Pathway: Steroid metabolism.
Subcellular Location: Microsome
EC: 1.1.1.-
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P50233 | MERWPWPSGGAWLLVAARALLQLLRSDLRLGRPLLAALALLAALDWLCQRLLPPPAALVVLAGAGWIALSRLARPPRLPVATRAVLITGCDTGFGKETAKKLDAMGFTVLATVLDLNGPGALELRARCSPRLKLLQMDLTKPEDISRVLEITKAHTASTGLWGLVNNAGLNMVVADVELSPVVTFRECMEVNFFGALELTKGLLPLLRHSRGRIVTVGSPAGDMPYPCLAAYGTSKAAIALLMDTFSCELLPWGIKVSIIQPGCFKTEAVTNVNLWEKRKQLLLANLPRELLQAYGEDYIEHLHGQFLNSLRMALPDLSPVVDAIIDALLAAQPRSRYYTGRGLGLMYFIHHYLPGGLRRRFLQNFFISHLLPRALRPGQPGPVHDTTQDPNPSPTVSAL | Function: Catalyzes the conversion of biologically active 11beta-hydroxyglucocorticoids (11beta-hydroxysteroid) such as corticosterone, to inactive 11-ketoglucocorticoids (11-oxosteroid) such as 11-dehydrocorticosterone, in the presence of NAD(+) . Functions as a dehydrogenase (oxidase), thereby decreasing the concentration of active glucocorticoids, thus protecting the nonselective mineralocorticoid receptor from occupation by glucocorticoids . Plays an important role in maintaining glucocorticoids balance during preimplantation and protects the fetus from excessive maternal corticosterone exposure . Catalyzes the oxidation of 11beta-hydroxytestosterone (11beta,17beta-dihydroxyandrost-4-ene-3-one) to 11-ketotestosterone (17beta-hydroxyandrost-4-ene-3,11-dione), a major bioactive androgen (By similarity). Catalyzes the conversion of 11beta-hydroxyandrostenedione (11beta-hydroxyandrost-4-ene-3,17-dione) to 11-ketoandrostenedione (androst-4-ene-3,11,17-trione), which can be further metabolized to 11-ketotestosterone (By similarity). Converts 7-beta-25-dihydroxycholesterol to 7-oxo-25-hydroxycholesterol in vitro (By similarity). 7-beta-25-dihydroxycholesterol (not 7-oxo-25-hydroxycholesterol) acts as ligand for the G-protein-coupled receptor (GPCR) Epstein-Barr virus-induced gene 2 (EBI2) and may thereby regulate immune cell migration (By similarity).
Catalytic Activity: an 11beta-hydroxysteroid + NAD(+) = an 11-oxosteroid + H(+) + NADH
Sequence Mass (Da): 43726
Sequence Length: 400
Pathway: Steroid metabolism.
Subcellular Location: Microsome
EC: 1.1.1.-
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Q59660 | MRYITPRKAAEGLGSAHEGTQHHWAMTVSAVALTVLTPLFMIVVARAIGLSQEQLLAYFGRPFPALITALFVIVGMVHFIKGTRIMIDDYFQGGTRKAAIIFSVIFGWAVIAAAVYALARMGLGAIVVL | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13934
Sequence Length: 129
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Cell inner membrane
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A5GZW8 | MATLWRLSVLCGARGGGALVLRTSVVRPAHVSAFLQDRHTPGWCGVQHIHLSPSHQASSKAASLHWTGERVVSVLLLGLLPAAYLNPCSAMDYSLAAALTLHGHWGIGQVVTDYVRGDALQKVAKAGLLALSAFTFAGLCYFNYHDVGICKAVAMLWKL | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17005
Sequence Length: 159
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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P80479 | MYKTLLAQVFFHSIAKKKLYFFWLPRLFSLLLVPGFLFDIEILFLFHPIILLHASLGLSVIIEDYIHIETIKFQYLSLIKLLLVLLINLNILYLL | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 11265
Sequence Length: 95
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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P80482 | MTEKLLHFIRTKSGSMHWWLQRFLAILLAPIILYLLFDVAIYIGQQSDPTVMMFLNRIFNHNSIFIFITSVILIWHVRGGMEVIIEDYVHGEKTRIVSIFLIRVIAIEIMEYLYKCSIIF | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14222
Sequence Length: 120
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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P41086 | MIYDFKAEIIKAKNSSFSKSGSHHWLLQRVTGVILALCSFWLIYFMFTNKNNDINIIMWEFKKPFNIVILLITVTISLYHSVLGMRVVIEDYINCHKLRNTLIIIVKLFCILTIVSFVVAIFYSG | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14555
Sequence Length: 125
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Cell inner membrane
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Q9P7X0 | MLQTRLGLGALRQGRLLFAVKSFSTTSVAKIFPPPPQTIKGTVNDAAVFPHHSKLHGSYHWDFERIIAIAMVPQVMIPLFTGTSHPLMDAALACTLITHAHLGFESCVIDYFPARRFKKLSPLMHWILRGCTVLTLIGVYEFNTNDIGLTEGIKKLWKS | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17744
Sequence Length: 159
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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Q08717 | MAETEKMKYGSLNRFAQAVTGLFLLFFLGVHLYVAHIDFGHPVAFFSSVINQLHNPWWLAFFLIFVYIITYHGINGLNHIVADTSISEKAKRNIGIALMVIYVITIIYGTILALLVARMTVPT | Cofactor: The heme is bound between the two transmembrane subunits.
Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13874
Sequence Length: 123
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Cell membrane
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Q6P355 | MATLLRVSSLCRANRASAFKSLLIRPVPCLTQDHHMVQTSQIHTSPNHHAGSKAASMHWTSERALSVALLGLLPAAYLYPGAAMDYSLAAALTLHGHWGLGQVVTDYVHGDAKIKMANTSLFALSALTFAGLCYFNYHDVGICKAVSMLWSL | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16424
Sequence Length: 152
Subcellular Location: Mitochondrion inner membrane
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P37298 | MMLPRSMKFMTGRRIFHTATVRAFQSTAKKSLTIPFLPVLPQKPGGVRGTPNDAYVPPPENKLEGSYHWYMEKIFALSVVPLATTAMLTTGPLSTAADSFFSVMLLGYCYMEFNSCITDYISERVYGVWHKYAMYMLGLGSAVSLFGIYKLETENDGVVGLVKSLWDSSEKDNSQKIEAKK | Function: Membrane-anchoring subunit of succinate dehydrogenase (SDH) that is involved in system II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). SDH3 and SDH4 form the membrane dimer that anchors the catalytic dimer formed by SDH1 and SDH2 to the matrix surface of the mitochondrial inner membrane. Electrons originating from the catalytic dimer enter the membrane dimer for ubiquinone reduction.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20249
Sequence Length: 181
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle.
Subcellular Location: Mitochondrion inner membrane
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P17874 | XEEFDYDLVIIGAG | Function: Soluble hydrogenase catalyzes both production and consumption of hydrogen from suitable artificial electron donors or acceptors. This subunit (50 kDa) is required for hydrogen production with reduced methyl-viologen.
Sequence Mass (Da): 1552
Sequence Length: 14
Subcellular Location: Cytoplasm
EC: 1.12.-.-
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Q8Q051 | MHHNVFTNTPTIPIDVKDRSVSELMDGMLRTGFQGRKLAESVQAWSNMLKEKDTTVLMGLSGAMVPAGMRRVISYLIRERMIDCLVSTGANLFHDSHEALGRKHYVGSHLANDEKLFEHGVDRIYDVFAVEEEFRNADNLIADFAEEIGEISCSSREFMYLLGKELVRRGAAEDSIVVSAYRHNVPIFVPALSDSSIGIGLTIARRRGLKLEIDQIKDVDEITQIVEKSGHTGVVYVGGGVPKNFIQQTEVIASILGMDVPGHEYAIQYTSDSPHWGGLSGCTFDEAVSWGKVAAQAKKVQVFVDATIALPIVAHALHEKTRGVKRTAPVFSWDGPEGLEIAYNE | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Catalytic Activity: [eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine
Sequence Mass (Da): 38042
Sequence Length: 345
Pathway: Protein modification; eIF5A hypusination.
EC: 2.5.1.46
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Q38BX0 | MAELAKSAVLVSSCTDDLLGDAKQVVVGPNQEDLHSAEAVLNRYSTVGFQASNLARAFSICEMMLTPQSPSPSLMPTEGDQASESPVMVQPTLFVGVTANLFGTGCREAIRFLCTECVPLPNGVEPATPLDDMAGISCDGTGALKPSPCDSRALIHVLVVSGGAMEHDIRRACESYKLSRDGAEEEGEQFHHPVERDRSRSKGTDCHFGNVRYNSSGVASRNLFSCVMRCLVKRLAEAQRKEKANREAAPIPEAYYDVCSWAITPSTLWYMAGLWMADIFTEALQETGEVTDEKVASEEGLKRAKSTVLYWAARNGVPIFSPSLTDGDIMEFILTAGDTGVPLLQLDLVADIHRLNRLAMRSRRTGMMILGGGVVKHHVCNANLMRNGADYAVFLNNAQEFDGSDAGARPGEAVSWGKLRLDSTAVKVYSEVTIVFPLIVVHVFVAWVRMMRSKGKENIRS | Cofactor: The binding sites for NAD(+) are contained in the regulatory subunit DHSp.
Function: In association with the non-catalytic regulatory subunit DHSp, catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF5A precursor protein to form the intermediate deoxyhypusine residue. Regulates protein levels of its regulatory subunit DHSp. Required for cell growth and survival.
Catalytic Activity: [eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 50170
Sequence Length: 461
Pathway: Protein modification; eIF5A hypusination.
Subcellular Location: Membrane
EC: 2.5.1.46
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Q6EWQ6 | MEGPQEREVPAAALAAVLKHSSALPFETAQVRGYDFNRGVDYRALLEAFSTTGFQATNFGRAVQQVNAMIEKKLEPLSEDEDQHADLTQSRRPLTGCTIFLGYTSNLISSGIRETIRYLVQHNMVDVLVTTAGGVEEDFIKCLAPTYLGEFSLRGKELRENGINRIGNLLVPNDNYCKFEDWLMPILDQMVLEQNTEGVKWTPSKMIARLGKEINNPESVYYWAQKNHIPVLSPALTDGSLGDMIFFHSYKNPGLVLDIVEDLKLINTQAIFAKRTGMIILGGGMVKHHIANANLMRNGADYAVYINTAQEFDGSDSGARPDEAVSWGKIRMDAQPVKVYADASLVFPLLVAETFAQKVDAFMPEKNED | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a critical lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue. This is the first step of the post-translational modification of that lysine into an unusual amino acid residue named hypusine. Hypusination is unique to mature eIF-5A factor and is essential for its function.
Catalytic Activity: [eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine
Sequence Mass (Da): 41029
Sequence Length: 369
Pathway: Protein modification; eIF5A hypusination.
EC: 2.5.1.46
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Q6BJH5 | MSGSDKLPGLASDAVLKQSIPVPDSFVEIKGIDYSKDSAYNMKAVDLIESMKNMGFQASSVSQACEIINGMRSWRGKHIDSLPEHERTGEFDDEGYQKSTIFMGYTSNLISSGLRDTLRFLVQHKMVSAIVSSAGGIEEDLIKVLAPTYMGEFSLPGKGLRDQGMNRIGNLLVPNDNYCKFEEWIVPILDKCLEEQEEGMKKMGSDGLNADSPACWTPSKLINRLGKEINDESSVLYWAHKNDIPVFCPALTDGSIGDMLFFHTFKASPQQIRLDIVADIRKLNSMSMAASNAGMILLGGGLIKHHICNACLMRNGADYAVYINTGQEFDGSDAGARPDEAISWGKIKAEAKQVKVYADASIVFPLIVAATFASEKPN | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Catalytic Activity: [eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine
Sequence Mass (Da): 41355
Sequence Length: 378
Pathway: Protein modification; eIF5A hypusination.
EC: 2.5.1.46
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Q9AXQ8 | MEDANHDSVASAHSAAFKKSENLEGKSVKIEGYDFNQGVNYSKLLQSFASNGFQASNLGDAIEVVNHMLDWSLADEAPVDDCSEEERDPKFRESVKCKVFLGFTSNLISSGVRDTIRYLVQHHMVDVIVTTTGGIEEDLIKGRSIKCLAPTFKGDFALPGAQLRSKGLNRIGNLLVPNDNYCKFEDWIIPILDKMLEEQISEKILWTPSKLIGRLGREINDESSYLYWAFKNNIPVFCPGLTDGSLGDMLYFHSFRNPGLIVDVVQDIRAVNGEAVHAAPRKTGMIILGGGLPKHHICNANMMRNGADYAVFINTAEEFDGSDSGARPDEAISWGKISGSAKTVKVHCDATIAFPLLVAETFAAKREKERKSC | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue. Also able to produce homospermidine from putrescine (By similarity).
Catalytic Activity: [eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine
Sequence Mass (Da): 41126
Sequence Length: 373
Pathway: Protein modification; eIF5A hypusination.
EC: 2.5.1.46
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Q54MQ7 | MSTNTTTTNATPELAKESVFFQSNHEDLKNRPKVRGYDFNEGVDFSKLFETYKTIGYQASAVGEAIDEINRMISWRLVDEPLKEGEDDDEERKVTRCKIFLGYTSNLVSSGVREIIRYLVQHSMVDVIVSTAGGVEEDFIKCLAPTYMGEFHLEGEKLRRKGLNRIGNLLVPNDNYCKFEDWIMPILDQMVEEQKTKGTVWTPSRVINRLGKEINHEDSIYYWAWKNDIPVYSPALTDGSIGDMMYFHSYNTPGLVLDIISDIRAINNHAVYSKKSGMIILGGGVIKHHICNANLFRNGADYSVFVNTGNEFDGSDSGARPDEAVSWGKIKLDAKPVKVYSEASIVFPILVAETFAKTFKKKSPEELKLNKRSIFD | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a critical lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue. This is the first step of the post-translational modification of that lysine into an unusual amino acid residue named hypusine. Hypusination is unique to mature eIF-5A factor and is essential for its function.
Catalytic Activity: [eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine
Sequence Mass (Da): 42544
Sequence Length: 376
Pathway: Protein modification; eIF5A hypusination.
EC: 2.5.1.46
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Q9VSF4 | MSTEPSVAKDAVLKRSEALAENTPQVSGYDFNEGLDYSKLFESYVNTGFQATNLGLAIREINRMLDCRDQPLEADQIDSHETDDFIRRRSKCTVFLGYTSNLVSSGLRETIRFLAEHRMIDCIVTTAGGVEEDFIKCLAPTFMGSFELSGRDLRERGINRIGNLLVPNDNYCKFEDWVMPLLDEMLEEQKSQGTIWSPSKIIHRLGERIGDPSSIYYWAAKNQIPVFCPALTDGSLGDMMYFHSFRQPGLVVDILSDLRRLNTMAVKAVNSGMIIVGGGVIKHHICNANLMRNGADYSVFINTASEFDGSDSGARPDEAISWGKIRKDATPVKVYAEASLVFPLIVGETFAKRHHCAGKELPRETNQV | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Catalytic Activity: [eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine
Sequence Mass (Da): 41080
Sequence Length: 368
Pathway: Protein modification; eIF5A hypusination.
EC: 2.5.1.46
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Q8SQN2 | MDRPQNVKDLARKVKDNLSFSREVRGMDFEKEWDFMAIMRSFETMGFQGSNLYRAVEEIERMKNSKIFFGCTSNIISSGLRDVIATLVKRRHVHVLVITGGGIEEDIIKAFKPTFCADFRLDGAELRDNGLNRIGNLVIPSENYEHLESWLNNIVNDITEGYTAERPRILTPSSFIRILGERIDDESSILYWAAKNDIPVYSPAVVDGSLGDILSFHPRRKMLKLDIVEDVYRINCETIFCGETAAIILGCGVVKHHILNANLFKNGLEHCVLINNAQEFDGSDAGASLDEAVSWGKVKPGTRGVKVFGDATILFPLLVGATFMRKDKDVPKGE | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Catalytic Activity: [eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine
Sequence Mass (Da): 37447
Sequence Length: 334
Pathway: Protein modification; eIF5A hypusination.
EC: 2.5.1.46
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B0R5L2 | MTGDDADETHENVVPGSDEDLDTPDVRGYDFSGEFDFFELLDSYATTGFQASHLADAVDITREMREDDATIYLTLTSNIVSSGLREVVAHLVRENYVDVIITTSGSLTEDIIKTAKPFKMGEWDVDEAALREEGINRLGNIFVPSDRYVWLEEYLYDFFEEFFADQKVRTPTAFARELGATLDDEDSILKNAADNDIPVFCPALTDAEIGNFLYYYRQGYDSEVGIEILDDYDALIEEGLLADTTGLICVGAGVPKHHAIMTNLFRGGADYAVYISTGMEGDGSLSGAPPEEAVSWGKIKDEDAEPNYALIEAEATLVFPLLVAGAFENP | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a specific lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue.
Catalytic Activity: [eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine
Sequence Mass (Da): 36381
Sequence Length: 330
Pathway: Protein modification; eIF5A hypusination.
EC: 2.5.1.46
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P49366 | MEGSLEREAPAGALAAVLKHSSTLPPESTQVRGYDFNRGVNYRALLEAFGTTGFQATNFGRAVQQVNAMIEKKLEPLSQDEDQHADLTQSRRPLTSCTIFLGYTSNLISSGIRETIRYLVQHNMVDVLVTTAGGVEEDLIKCLAPTYLGEFSLRGKELRENGINRIGNLLVPNENYCKFEDWLMPILDQMVMEQNTEGVKWTPSKMIARLGKEINNPESVYYWAQKNHIPVFSPALTDGSLGDMIFFHSYKNPGLVLDIVEDLRLINTQAIFAKCTGMIILGGGVVKHHIANANLMRNGADYAVYINTAQEFDGSDSGARPDEAVSWGKIRVDAQPVKVYADASLVFPLLVAETFAQKMDAFMHEKNED | Function: Catalyzes the NAD-dependent oxidative cleavage of spermidine and the subsequent transfer of the butylamine moiety of spermidine to the epsilon-amino group of a critical lysine residue of the eIF-5A precursor protein to form the intermediate deoxyhypusine residue . This is the first step of the post-translational modification of that lysine into an unusual amino acid residue named hypusine. Hypusination is unique to mature eIF-5A factor and is essential for its function.
Catalytic Activity: [eIF5A protein]-L-lysine + spermidine = [eIF5A protein]-deoxyhypusine + propane-1,3-diamine
Sequence Mass (Da): 40971
Sequence Length: 369
Pathway: Protein modification; eIF5A hypusination.
EC: 2.5.1.46
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O60074 | MSNLEASLFQLKFAAKSLNKQSLKAAKEERAEREKVKKAITKGNSEIARIYASNAIRKQQESLNLLKLSSRIDAVSSRLQTAVTMRAVSGNMAGVVRGMDRAMKTMNLEMISQVMDKFEAQFDDVNVQTGYMNKAMGSVTAVDTPQEDVDLLMQTVADEAGLEFNQNMNNNLSVPAASVPTPAAPVEDDNLQERLRALRS | Function: Class E VPS protein implicated in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins will be targeted into the vacuole after fusion of the endosome with the vacuole (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 22000
Sequence Length: 200
Subcellular Location: Endosome membrane
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P69771 | MSRNSAAGLENTLFQLKFTSKQLQKQANKASKEEKQETNKLKRALNENEDISRIYASNAIRKKNERLQLLKLASRVDSVASRVQTAVTMRQVSASMGQVCKGMDKALQNMNLQQITMIMDKFEQQFEDLDTSVNVYEDMGVNSDAMLVDNDKVDELMSKVADENGMELKQSAKLDNVPEIKAKEVNVDDEKEDKLAQRLRALRG | Function: Class E VPS protein implicated in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins will be targeted into the vacuole after fusion of the endosome with the vacuole. Probably acts as a peripherally associated component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruits late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Regulates the membrane association of VPS4. Can stimulate VPS4 ATPase activity directly or via VTA1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23091
Sequence Length: 204
Subcellular Location: Endosome membrane
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O14177 | MGLTSWLFGGGKSPQEQLRAHQRSLGRAERELDRERTKLDQRERALIQEIKGSAKAGNTGAARIQARDLMRLRNSRKKMMNAKTQLQAISLRLQTMRTSEQMMQSMRGATRLLTGMNKSMNIPAMARITQQFERENEIMEQRQEMIDENMDDALEEDDEEEADELVNKVLDEIGVDLSQGLPDAATQIGTVPELKTEDNLQARLDELAKR | Function: Required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB). Acts a component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 23928
Sequence Length: 210
Subcellular Location: Cytoplasm
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P36108 | MSLFEWVFGKNVTPQERLKKNQRALERTQRELEREKRKLELQDKKLVSEIKKSAKNGQVAAAKVQAKDLVRTRNYIQKFDNMKAQLQAISLRIQAVRSSDQMTRSMSEATGLLAGMNRTMNLPQLQRISMEFEKQSDLMGQRQEFMDEAIDNVMGDEVDEDEEADEIVNKVLDEIGVDLNSQLQSTPQNLVSNAPIAETAMGIPEPIGAGSEFHGNPDDDLQARLNTLKKQT | Function: Required for the sorting and concentration of proteins resulting in the entry of these proteins into the invaginating vesicles of the multivesicular body (MVB). Acts a component of the ESCRT-III complex, which appears to be critical for late steps in MVB sorting, such as membrane invagination and final cargo sorting and recruitment of late-acting components of the sorting machinery. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complex assemblies. Can directly stimulate VPS4 ATPase activity. The DID4/VPS2-VPS24 subcomplex is required for the VPS4-dependent dissociation of ESCRT-III.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26291
Sequence Length: 232
Subcellular Location: Cytoplasm
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A7MAQ2 | MSSSTLLHLLLLSSLLFSCLSCLTNVEDEFSYIEGNPNGPENWGNLKPEWETCGKGMEQSPIQLRDNRVIFDQTLGKLRRNYRAVDARLRNSGHDVLVDFKGNAGSLSINRVEYQLKRIHFHSPSEHEMNGERFDLEAQLVHESQDQKRAVVSILFRFGRADPFLSDLEDFIKQFSNSQKNEINAGVVDPNQLQIDDSAYYRYMGSFTAPPCTEGISWTVMRKVATVSPRQVLLLKQAVNENAINNARPLQPTNFRSVFYFEQLKSKLGVI | Function: Storage protein of tuber. Involved in protection against oxidative stress (Probable). Has carbonate dehydratase, trypsin inhibitor, dehydroascorbate (DHA) reductase and monodehydroascorbate (MDA) reductase activities . Catalyzes the reactions of carbonate dehydratase and DHA reductase independently of zinc and glutathione (GSH). The coupled reaction is capable of recycling a plant antioxidant ascorbate using ubiquitous compounds H(2)O and CO(2) . Exhibits antioxidant activity. Able to scavenge 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical. Exhibits immunomodulatory activity. Activates Toll-like receptor 4 signaling pathways by up-regulating the gene expression of pro-inflammatory cytokines, such as tumor necrosis factor alpha, interleukin-1 beta and interleukin-6, and chemokines RANTES and MCP-1, in mouse RAW 264.7 macrophages. Stimulates the phagocytosis of E.coli by the LPS-treated mouse macrophages .
PTM: Not glycosylated.
Catalytic Activity: H(+) + hydrogencarbonate = CO2 + H2O
Sequence Mass (Da): 30876
Sequence Length: 271
EC: 1.6.5.4
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Q9LXV3 | MASLALSGSCSLAFPLKSRSLSLPRPPSSSLNLTKPLRSLDSRFSLLKSPLPVSLRRRSSTLVKASSTVASASSSPTPPLVPAPVPWQGAAIKPLLASIATGLILWFVPVPEGVTRNAWQLLAIFLATIVGIITQPLPLGAVALMGLGASVLTKTLTFAAAFSAFGDPIPWLIALAFFFARGFIKTGLGNRVAYQFVRLFGSSSLGLGYSLVFSEALLAPAIPSVSARAGGIFLPLVKSLCVACGSNVGDGTEHRLGSWLMLTCFQTSVISSSMFLTAMAANPLSANLAFNTIKQTIGWTDWAKAAIVPGLVSLIVVPFLLYLIYPPTVKSSPDAPKLAQEKLDKMGPMSKNELIMAATLFLTVGLWIFGAKLGVDAVTAAILGLSVLLVTGVVTWKECLAESVAWDTLTWFAALIAMAGYLNKYGLIEWFSQTVVKFVGGLGLSWQLSFGILVLLYFYTHYFFASGAAHIGAMFTAFLSVSTALGTPPYFAALVLAFLSNLMGGLTHYGIGSAPIFYGANYVPLAKWWGYGFLISIVNILIWLGVGGAWWKFIGLW | Function: 2-oxoglutarate/malate translocator involved with DIT2-1 in primary ammonia assimilation and in the re-assimilation of ammonia generated by the photorespiratory pathway. Imports 2-oxoglutarate into plastids as precursor for ammonia assimilation. 2-oxoglutarate is converted to glutamate, the end product of ammonia assimilation, which is exported to the cytosol by DIT2-1.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59213
Sequence Length: 557
Subcellular Location: Plastid
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Q90839 | MRRGEGPAPRRRWLLLLAVLAALCCAAAGSGGRRRAASLGEMLREVEALMEDTQHKLRNAVQEMEAEEEGAKKLSEVNFENLPPTYHNESNTETRIGNKTVQTHQEIDKVTDNRTGSTIFSETIITSIKGGENKRNHECIIDEDCETGKYCQFSTFEYKCQPCKTQHTHCSRDVECCGDQLCVWGECRKATSRGENGTICENQHDCNPGTCCAFQKELLFPVCTPLPEEGEPCHDPSNRLLNLITWELEPDGVLERCPCASGLICQPQSSHSTTSVCELSSNETRKNEKEDPLNMDEMPFISLIPRDILSDYEESSVIQEVRKELESLEDQAGVKSEHDPAHDLFLGDEI | Function: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (By similarity).
Sequence Mass (Da): 39209
Sequence Length: 350
Domain: The C-terminal cysteine-rich domain mediates interaction with LRP5 and LRP6.
Subcellular Location: Secreted
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Q9UBP4 | MQRLGATLLCLLLAAAVPTAPAPAPTATSAPVKPGPALSYPQEEATLNEMFREVEELMEDTQHKLRSAVEEMEAEEAAAKASSEVNLANLPPSYHNETNTDTKVGNNTIHVHREIHKITNNQTGQMVFSETVITSVGDEEGRRSHECIIDEDCGPSMYCQFASFQYTCQPCRGQRMLCTRDSECCGDQLCVWGHCTKMATRGSNGTICDNQRDCQPGLCCAFQRGLLFPVCTPLPVEGELCHDPASRLLDLITWELEPDGALDRCPCASGLLCQPHSHSLVYVCKPTFVGSRDQDGEILLPREVPDEYEVGSFMEEVRQELEDLERSLTEEMALREPAAAAAALLGGEEI | Function: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (By similarity).
PTM: N- and O-glycosylated.
Sequence Mass (Da): 38390
Sequence Length: 350
Domain: The C-terminal cysteine-rich domain mediates interaction with LRP5 and LRP6.
Subcellular Location: Secreted
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Q9QUN9 | MQRLGGILLCTLLAAAVPTAPAPSPTVTWTPAEPGPALNYPQEEATLNEMFREVEELMEDTQHKLRSAVEEMEAEEAAAKTSSEVNLASLPPNYHNETSTETRVGNNTVHVHQEVHKITNNQSGQVVFSETVITSVGDEEGKRSHECIIDEDCGPTRYCQFSSFKYTCQPCRDQQMLCTRDSECCGDQLCAWGHCTQKATKGGNGTICDNQRDCQPGLCCAFQRGLLFPVCTPLPVEGELCHDPTSQLLDLITWELEPEGALDRCPCASGLLCQPHSHSLVYMCKPAFVGSHDHSEESQLPREAPDEYEDVGFIGEVRQELEDLERSLAQEMAFEGPAPVESLGGEEEI | Function: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (By similarity).
Sequence Mass (Da): 38388
Sequence Length: 349
Domain: The C-terminal cysteine-rich domain mediates interaction with LRP5 and LRP6.
Subcellular Location: Secreted
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Q9UBT3 | MVAAVLLGLSWLCSPLGALVLDFNNIRSSADLHGARKGSQCLSDTDCNTRKFCLQPRDEKPFCATCRGLRRRCQRDAMCCPGTLCVNDVCTTMEDATPILERQLDEQDGTHAEGTTGHPVQENQPKRKPSIKKSQGRKGQEGESCLRTFDCGPGLCCARHFWTKICKPVLLEGQVCSRRGHKDTAQAPEIFQRCDCGPGLLCRSQLTSNRQHARLRVCQKIEKL | Function: Antagonizes canonical Wnt signaling by inhibiting LRP5/6 interaction with Wnt and by forming a ternary complex with the transmembrane protein KREMEN that promotes internalization of LRP5/6. DKKs play an important role in vertebrate development, where they locally inhibit Wnt regulated processes such as antero-posterior axial patterning, limb development, somitogenesis and eye formation. In the adult, Dkks are implicated in bone formation and bone disease, cancer and Alzheimer disease (By similarity).
PTM: Appears to be not glycosylated.
Sequence Mass (Da): 24876
Sequence Length: 224
Domain: The C-terminal cysteine-rich domain mediates interaction with LRP5 and LRP6.
Subcellular Location: Secreted
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Q9UK85 | MGEASPPAPARRHLLVLLLLLSTLVIPSAAAPIHDADAQESSLGLTGLQSLLQGFSRLFLKGNLLRGIDSLFSAPMDFRGLPGNYHKEENQEHQLGNNTLSSHLQIDKMTDNKTGEVLISENVVASIQPAEGSFEGDLKVPRMEEKEALVPIQKATDSFHTELHPRVAFWIIKLPRRRSHQDALEGGHWLSEKRHRLQAIRDGLRKGTHKDVLEEGTESSSHSRLSPRKTHLLYILRPSRQL | Function: Involved in fertilization by facilitating sperm penetration of the zona pellucida. May promote spermatocyte apoptosis, thereby limiting sperm production. In adults, may reduce testosterone synthesis in Leydig cells. Is not essential either for development or fertility.
PTM: N-glycosylated during spermatogenesis. Not N-glycosylated in mature sperm.
Sequence Mass (Da): 27007
Sequence Length: 242
Domain: Contains a N-terminal domain similar to that of the N-terminal section of DKK3.
Subcellular Location: Secreted
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Q9QZL9 | MCRLRVLLLLLPLAFVSSSALPIHDVDSQQNTSGFLGLQRLLQSFSRLFLKNDLLRDLDNFFSSPMDFRDLPRNFHQEENQEHRMGNHTLSSHLQIDKVTDNQTGEVLISEKVEASIEPERNPEGDWKVPKVEAKEPPVPVQKVTDSLHPEPRQVAFWIMKMPRRRTQPDVQDGGRWLIEKRHRMQAIRDGLRGGAREDSLEDGVHIPQHAKLPVRKTHFLYILRPSQQL | Function: Involved in fertilization by facilitating sperm penetration of the zona pellucida . May promote spermatocyte apoptosis, thereby limiting sperm production. In adults, may reduce testosterone synthesis in Leydig cells . Is not essential either for development or fertility .
PTM: N-glycosylated during spermatogenesis. Not N-glycosylated in mature sperm.
Sequence Mass (Da): 26639
Sequence Length: 230
Domain: Contains a N-terminal domain similar to that of the N-terminal section of DKK3.
Subcellular Location: Secreted
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P0CH43 | DCAKEGEVCSWGKKCCDLDNFYCPMEFIPHCKKYKPYVPVTTNCAKEGEVCGWGSKCCHGLDCPLAFIPYCEKYRGRND | Function: Selectively activates the heat-activated TRPV1 channel. It binds to TRPV1 in an open state-dependent manner, trapping it there to produce irreversible currents . It binds to the outer edge of the external pore of TRPV1 in a counterclockwise configuration, using a limited protein-protein interface and inserting hydrophobic residues into the bilayer . It also partitions naturally into membranes, with the two lobes exhibiting opposing energetics for membrane partitioning (K1) and channel activation (K2) . In addition, the toxin disrupts a cluster of hydrophobic residues behind the selectivity filter that are critical for channel activation .
Sequence Mass (Da): 8983
Sequence Length: 79
Domain: The presence of 'disulfide through disulfide knots' structurally defines this protein as a knottin. This toxin contains 2 'disulfide through disulfide knots' that are separated by a short linker. Bivalence accounts for irreversible toxin action.
Subcellular Location: Secreted
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A1ZAY1 | MAFLCPVRMRRDKKKATNASIERDLPAVGVLGMGRITGSSSIETLVRVGIEKEHGLSPDSKMVVLHDFTPCVDDELEVKRGQLVNILYRENDWVYVIGQDSRQEGFIPFSYCAPCNTQLADLAVKKKLPREQCPEQPIEENIPLLGTDNKLDVLCDETLNPGSANSIENTLLVEPECTPFVKEPSGRCIVLYTFIARDENDLSVERGEFVTVLNREDPDWFWIMRSDGQEGFVPASFIYPADSVRVLQQQKATLNAMETILQQGQQGQQSQQQQQPQLGLGTDDLRYHGTELVMLYDYKAQAPDDLYLSVRRGDWIYADLTNQTVDGWLWAYAPKTRKYGFIPKAYARPPAMTSL | Function: Required for the apical cell cortex localization, total cellular level and full activity of dachs.
PTM: Palmitoylated by app.
Sequence Mass (Da): 40131
Sequence Length: 355
Subcellular Location: Cytoplasm
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O01700 | MTSTTMVTTLDLVTPTSEEQPGPAPESSDFSTVVLSPDGSELVTQSAPNTPIQHREQANAEFGQKEGSPDPKNMVAATGNASKPSLNSFYADGLGQLRNGLFSCFQPVFGYFGTKTTVEIEKSEDELWEIPFDAISELEWLGSGSQGAVFRGQLENRTVAVKKVNQLKETEIKHLRHLRHQNIIEFLGVCSKSPCYCIVMEYCSKGQLCTVLKSRNTITRELFAQWVKEIADGMHYLHQNKVIHRDLKSPNILISAEDSIKICDFGTSHMQKKMDSTMMSFCGTVSWMAPEMIKKQPCNEKVDVYSFGVVLWEMLTRETPYANIAQMAIIFGVGTNILSLPMPEEAPKGLVLLIKQCLSQKGRNRPSFSHIRQHWEIFKPELFEMTEEEWQLAWDSYREFAKCIQYPSTVTRDHGGPKSAFAMEEEIQRKRHEQLNHIKDIRNMYEMKLKRTNKMYDKLQGCFTELKLKESELAEWEKDLTEREQWHNQNSPKAVAAPRAQLRGYPNEGYDDMSSDEDVQPCRGSPYRCSNTSSSSGVQSSPFSRQSSSRSSAGQQTRRSEGANPPKILRNDAIRHSGSYWETLGGARGSPARDSGFSQDSGMWSAGAGSCTAINGGGQQVCYSQTLYRNGDGRWSDGRIASRRRVSTSVNKSTAVPGQPVFFTRDSPSRVPHGVISCSSPRSSSKLNRSSYPSRNAPHQLEDGCCCAHARAPRAKSIAVPMTSSSRARSPTPYDNDFENAESFVDPESPKNLKNLEKIVNLPESTSYDEALCNSDVTMNPIYTSPITTYSNPCHVELVDEENANDVDLTSSMDSRRSRSDDADVESSEEDEGNGNNILNTSMESEDLRYRIDTSQSTMMSSLERSLEIGATRSDGLSDNEMRVQAVKMSIKTHRRTGSNPQALIHQCIDEYTTSATDDSDDAGAVRI | Function: Component of a MAP kinase pathway that functions presynaptically to regulate synaptic architecture and presynaptic differentiation . Phosphorylates and activates mkk-4 . Has a role in axonal regrowth following injury and synaptogenesis . Plays a role in modulating polymerization of neuronal microtubules . Also promotes tubulin post-translational modifications that protect microtubules . Plays a role in cilium length regulation, possibly by reducing rab-5 mediated endocytosis, and may also have a role in intraflagellar transport in cilia . Plays a role in the formation of muscle connections, also called muscle arm extensions, between the body wall and the motor axons in the dorsal and ventral cord .
PTM: Ubiquitinated by rpm-1. Negatively regulated by ubiquitination by fsn-1 bound rpm-1, followed by degradation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 103483
Sequence Length: 928
Domain: The C-terminal hexapeptide motif is required for homooligomerization and for its activation.
Subcellular Location: Synapse
EC: 2.7.11.25
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Q09163 | MIATGALLRVLLLLLAFGHSTYGAECDPPCDPQYGFCEADNVCRCHVGWEGPLCDKCVTAPGCVNGVCKEPWQCICKDGWDGKFCEIDVRACTSTPCANNGTCVDLEKGQYECSCTPGFSGKDCQHKAGPCVINGSPCQHGGACVDDEGQASHASCLCPPGFSGNFCEIVAATNSCTPNPCENDGVCTDIGGDFRCRCPAGFVDKTCSRPVSNCASGPCQNGGTCLQHTQVSFECLCKPPFMGPTCAKKRGASPVQVTHLPSGYGLTYRLTPGVHELPVQQPEQHILKVSMKELNKSTPLLTEGQAICFTILGVLTSLVVLGTVAIVFLNKCETWVSNLRYNHTFRKKKNLLLQYNSGEELAVNIIFPEKIDMTTFNKEAGDEEI | Function: May have a role in neuroendocrine differentiation. Inhibits adipocyte differentiation.
PTM: N- and O-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 41320
Sequence Length: 385
Subcellular Location: Membrane
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O70534 | MIATGALLRVLLLLLAFGHSTYGAECDPACDPQHGFCEADNVCRCEPGWEGPLCEKCVTSPGCVNGLCEEPWQCVCKEGWDGKFCEIDIRACTSTPCANNGTCVDLEKGQYECSCTPGFSGKDCQHKAGPCVINGSPCQHGGACVDDEGRASHASCLCPPGFSGNFCEIVTNSCTPNPCENDGVCTDIGGDFRCRCPAGFVDKTCSRPVSNCASGPCLNGGTCLQHTQVSFECLCKPPFMGPTCAKKRGTSPVQVTHLPSGYGLTYRLTPGVHELPVQQPEHHILKVSMKELNKSAPLLTEGQAICFTILGVLTSLVVLGTVAIVFLNKCEAWVSNLRYNHMLRKKKNLLLQYNSGEELAVNIIFPEKIDMTTFNKEAGDEDI | Function: May have a role in neuroendocrine differentiation. Inhibits adipocyte differentiation.
PTM: Glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 41149
Sequence Length: 383
Subcellular Location: Membrane
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A4FV93 | MPSGCRCLHLVCLLCILGAPVKPARGNDCSSLCDLAHGCCAPDGSCRCDPGWEGLHCERCVRMPGCQHGTCHQPWQCICHTGWAGKFCDKDEHICTTQSPCRNGGQCVYDGGGDYHCVCPPGFHGRDCERKAGPCEQAGSPCRNGGQCQDDQGFALNFTCRCLAGFMGARCEVNVDDCLMRPCANGATCLDGINRFSCLCPEGFTGRFCTINLDDCASRPCQRGARCRDRVHDFDCLCPSGYGGKTCELVLPVPGPAATADSPPGPTLAVLVPATGPIPHSAGAGLLRISVKEVVRRQEAGLGEPSLVAVVVFGAVTAALVLSTVLLTLRAWRRGFCPPGPCCYPAPHYAPARQDQECQVSMLPTGLPLPPDLPPEPGKTTAL | Function: Regulates adipogenesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 40507
Sequence Length: 383
Subcellular Location: Membrane
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Q8K1E3 | MPSGCRCLNLVCLLCILGATSQPARADDCSSHCDLAHGCCAPDGSCRCDPGWEGLHCERCVRMPGCQHGTCHQPWQCICHSGWAGKFCDKDEHICTSQSPCQNGGQCVYDGGGEYHCVCLPGFHGRGCERKAGPCEQAGFPCRNGGQCQDNQGFALNFTCRCLAGFMGAHCEVNVDDCLMRPCANGATCIDGINRFSCLCPEGFAGRFCTINLDDCASRPCQRGARCRDRVHDFDCLCPSGYGGKTCELVLPAPEPASVGTPQMPTSAVVVPATGPAPHSAGAGLLRISVKEVVRRQESGLGESSLVALVVFGSLTAALVLATVLLTLRAWRRGICPTGPCCYPAPHYAPARQDQECQVSMLPAGFPLSPDLPPEPGKTTAL | Function: Regulates adipogenesis.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 40404
Sequence Length: 382
Subcellular Location: Membrane
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Q61483 | MGRRSALALAVVSALLCQVWSSGVFELKLQEFVNKKGLLGNRNCCRGGSGPPCACRTFFRVCLKHYQASVSPEPPCTYGSAVTPVLGVDSFSLPDGAGIDPAFSNPIRFPFGFTWPGTFSLIIEALHTDSPDDLATENPERLISRLTTQRHLTVGEEWSQDLHSSGRTDLRYSYRFVCDEHYYGEGCSVFCRPRDDAFGHFTCGDRGEKMCDPGWKGQYCTDPICLPGCDDQHGYCDKPGECKCRVGWQGRYCDECIRYPGCLHGTCQQPWQCNCQEGWGGLFCNQDLNYCTHHKPCRNGATCTNTGQGSYTCSCRPGYTGANCELEVDECAPSPCKNGASCTDLEDSFSCTCPPGFYGKVCELSAMTCADGPCFNGGRCSDNPDGGYTCHCPLGFSGFNCEKKMDLCGSSPCSNGAKCVDLGNSYLCRCQAGFSGRYCEDNVDDCASSPCANGGTCRDSVNDFSCTCPPGYTGKNCSAPVSRCEHAPCHNGATCHQRGQRYMCECAQGYGGPNCQFLLPEPPPGPMVVDLSERHMESQGGPFPWVAVCAGVVLVLLLLLGCAAVVVCVRLKLQKHQPPPEPCGGETETMNNLANCQREKDVSVSIIGATQIKNTNKKADFHGDHGAEKSSFKVRYPTVDYNLVRDLKGDEATVRDTHSKRDTKCQSQSSAGEEKIAPTLRGGEIPDRKRPESVYSTSKDTKYQSVYVLSAEKDECVIATEV | Function: Transmembrane ligand protein of NOTCH1, NOTCH2 and NOTCH3 receptors that binds the extracellular domain (ECD) of Notch receptor in a cis and trans fashion manner . Following transinteraction, ligand cells produce mechanical force that depends of a clathrin-mediated endocytosis, requiring ligand ubiquitination, EPN1 interaction, and actin polymerisation; these events promote Notch receptor extracellular domain (NECD) transendocytosis and triggers Notch signaling through induction of cleavage, hyperphosphorylation, and nuclear accumulation of the intracellular domain of Notch receptors (NICD) . Is required for embryonic development and maintenance of adult stem cells in many different tissues and immune systeme; the DLL1-induced Notch signaling is mediated through an intercellular communication that regulates cell lineage, cell specification, cell patterning and morphogenesis through effects on differentiation and proliferation . Plays a role in brain development at different level, namely by regulating neuronal differentiation of neural precursor cells via cell-cell interaction, most likely through the lateral inhibitory system in an endogenous level dependent-manner . During neocortex development, Dll1-Notch signaling transmission is mediated by dynamic interactions between intermediate neurogenic progenitors and radial glia; the cell-cell interactions are mediated via dynamic and transient elongation processes, likely to reactivate/maintain Notch activity in neighboring progenitors, and coordinate progenitor cell division and differentiation across radial and zonal boundaries . During cerebellar development, regulates Bergmann glial monolayer formation and its morphological maturation through a Notch signaling pathway . At the retina and spinal cord level, regulates neurogenesis by preventing the premature differentiation of neural progenitors and also by maintaining progenitors in spinal cord through Notch signaling pathway . Also controls neurogenesis of the neural tube in a progenitor domain-specific fashion along the dorsoventral axis . Maintains quiescence of neural stem cells and plays a role as a fate determinant that segregates asymmetrically to one daughter cell during neural stem cells mitosis, resulting in neuronal differentiation in Dll1-inheriting cell . Plays a role in immune systeme development, namely the development of all T-cells and marginal zone (MZ) B cells . Blocks the differentiation of progenitor cells into the B-cell lineage while promoting the emergence of a population of cells with the characteristics of a T-cell/NK-cell precursor (By similarity). Upon MMP14 cleavage, negatively regulates Notch signaling in haematopoietic progenitor cells to specifically maintain normal B-cell development in bone marrow . Also plays a role during muscle development. During early development, inhibits myoblasts differentiation from the medial dermomyotomal lip and later regulates progenitor cell differentiation . Directly modulates cell adhesion and basal lamina formation in satellite cells through Notch signaling. Maintains myogenic progenitors pool by suppressing differentiation through down-regulation of MYOD1 and is required for satellite cell homing and PAX7 expression . During craniofacial and trunk myogenesis suppresses differentiation of cranial mesoderm-derived and somite-derived muscle via MYOD1 regulation but in cranial mesoderm-derived progenitors, is neither required for satellite cell homing nor for PAX7 expression . Also plays a role during pancreatic cell development. During type B pancreatic cell development, may be involved in the initiation of proximodistal patterning in the early pancreatic epithelium . Stimulates multipotent pancreatic progenitor cells proliferation and pancreatic growth by maintaining HES1 expression and PTF1A protein levels . During fetal stages of development, is required to maintain arterial identity and the responsiveness of arterial endothelial cells for VEGFA through regulation of KDR activation and NRP1 expression . Controls sprouting angiogenesis and subsequent vertical branch formation through regulation on tip cell differentiation . Negatively regulates goblet cell differentiation in intestine and controls secretory fat commitment through lateral inhibition in small intestine . Plays a role during inner ear development; negatively regulates auditory hair cell differentiation . Plays a role during nephron development through Notch signaling pathway . Regulates growth, blood pressure and energy homeostasis .
PTM: Ubiquitinated by MIB (MIB1 or MIB2), leading to its endocytosis and subsequent degradation. Ubiquitinated; promotes recycling back to the plasma membrane and confers a strong affinity for NOTCH1 . Multi-ubiquitination of Lys-613 by MIB1 promotes both cis and trans-interaction with NOTCH1, as well as activation of Notch signaling . Ubiquitinated by NEURL1B .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 78449
Sequence Length: 722
Subcellular Location: Apical cell membrane
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Q9NYJ7 | MVSPRMSGLLSQTVILALIFLPQTRPAGVFELQIHSFGPGPGPGAPRSPCSARLPCRLFFRVCLKPGLSEEAAESPCALGAALSARGPVYTEQPGAPAPDLPLPDGLLQVPFRDAWPGTFSFIIETWREELGDQIGGPAWSLLARVAGRRRLAAGGPWARDIQRAGAWELRFSYRARCEPPAVGTACTRLCRPRSAPSRCGPGLRPCAPLEDECEAPLVCRAGCSPEHGFCEQPGECRCLEGWTGPLCTVPVSTSSCLSPRGPSSATTGCLVPGPGPCDGNPCANGGSCSETPRSFECTCPRGFYGLRCEVSGVTCADGPCFNGGLCVGGADPDSAYICHCPPGFQGSNCEKRVDRCSLQPCRNGGLCLDLGHALRCRCRAGFAGPRCEHDLDDCAGRACANGGTCVEGGGAHRCSCALGFGGRDCRERADPCAARPCAHGGRCYAHFSGLVCACAPGYMGARCEFPVHPDGASALPAAPPGLRPGDPQRYLLPPALGLLVAAGVAGAALLLVHVRRRGHSQDAGSRLLAGTPEPSVHALPDALNNLRTQEGSGDGPSSSVDWNRPEDVDPQGIYVISAPSIYAREVATPLFPPLHTGRAGQRQHLLFPYPSSILSVK | Function: Inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm (By similarity).
PTM: Ubiquitinated by MIB (MIB1 or MIB2), leading to its endocytosis and subsequent degradation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 64618
Sequence Length: 618
Domain: The DSL domain is required for binding to the Notch receptor.
Subcellular Location: Membrane
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O88516 | MVSLQVSPLSQTLILAFLLPQALPAGVFELQIHSFGPGPGLGTPRSPCNARGPCRLFFRVCLKPGVSQEATESLCALGAALSTSVPVYTEHPGESAAALPLPDGLVRVPFRDAWPGTFSLVIETWREQLGEHAGGPAWNLLARVVGRRRLAAGGPWARDVQRTGTWELHFSYRARCEPPAVGAACARLCRSRSAPSRCGPGLRPCTPFPDECEAPSVCRPGCSPEHGYCEEPDECRCLEGWTGPLCTVPVSTSSCLNSRVPGPASTGCLLPGPGPCDGNPCANGGSCSETSGSFECACPRGFYGLRCEVSGVTCADGPCFNGGLCVGGEDPDSAYVCHCPPGFQGSNCEKRVDRCSLQPCQNGGLCLDLGHALRCRCRAGFAGPRCEHDLDDCAGRACANGGTCVEGGGSRRCSCALGFGGRDCRERADPCASRPCAHGGRCYAHFSGLVCACAPGYMGVRCEFAVRPDGADAVPAAPRGLRQADPQRFLLPPALGLLVAAGLAGAALLVIHVRRRGPGQDTGTRLLSGTREPSVHTLPDALNNLRLQDGAGDGPSSSADWNHPEDGDSRSIYVIPAPSIYAREDWLIQVLF | Function: Inhibits primary neurogenesis. May be required to divert neurons along a specific differentiation pathway. Plays a role in the formation of somite boundaries during segmentation of the paraxial mesoderm.
PTM: Ubiquitinated by MIB (MIB1 or MIB2), leading to its endocytosis and subsequent degradation.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 62069
Sequence Length: 592
Domain: The DSL domain is required for binding to the Notch receptor.
Subcellular Location: Membrane
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Q4FP21 | MKNFSIAKSRRLRSTPYTSRIEKQGVTAYTIYNHMLLPAAFGSIEDSYKHLKEHVQIWDVAAERQVEISGKDSAELVQLMTCRDLSKSKIGRCYYCPIIDENGNLVNDPVVLKLDENKWWISIADSDVIFFAKGLASGHKFDVKIVEPVVDIMAIQGPKSFALMEKVFGKKITELKFFGFDYFDFEGTKHLIARSGWSKQGGYEVYVENTQSGQKLYDHLFEVGKEFNVGPGCPNLIERIESALLSYGNDFDNNDNPFECGFDQYVSLDSDINFLGKEKLKEIKLKGPQKKLRGVKIDIKEISLTGSKNIYDENNNVIGELRSACYSPHFQKVIGIAMIKKSHWEASQGFKIQINDNTINGNVCDLPFI | Function: Major contributor to the demethylation of dimethylsulfonioproprionate (DMSP). Demethylates DMSP to methyl-mercaptopropionate (MMPA).
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + S,S-dimethyl-beta-propiothetin = (6S)-5-methyl-5,6,7,8-tetrahydrofolate + 3-(methylsulfanyl)propanoate + H(+)
Sequence Mass (Da): 41832
Sequence Length: 369
EC: 2.1.1.269
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Q5LS57 | MASIFPSRRVRRTPFSAGVEAAGVKGYTVYNHMLLPTVFDSLQADCAHLKEHVQVWDVACERQVSIQGPDALRLMKLISPRDMDRMADDQCYYVPTVDHRGGMLNDPVAVKLAADHYWLSLADGDLLQFGLGIAIARGFDVEIVEPDVSPLAVQGPRADDLMARVFGEAVRDIRFFRYKRLAFQGVELVVARSGWSKQGGFEIYVEGSELGMPLWNALFAAGADLNVRAGCPNNIERVESGLLSYGNDMTRENTPYECGLGKFCNSPEDYIGKAALAEQAKNGPARQIRALVIGGEIPPCQDAWPLLADGRQVGQVGSAIHSPEFGVNVAIGMVDRSHWAPGTGMEVETPDGMRPVTVREGFWR | Function: Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton, by mediating demethylation of dimethylsulfonioproprionate (DMSP) to methyl-mercaptopropionate (MMPA). The intracellular concentration of DMSP is estimated to be 70 mM.
Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + S,S-dimethyl-beta-propiothetin = (6S)-5-methyl-5,6,7,8-tetrahydrofolate + 3-(methylsulfanyl)propanoate + H(+)
Sequence Mass (Da): 39895
Sequence Length: 364
EC: 2.1.1.269
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Q0QLE1 | MKAKGSVFRYGDNVDTDVIIPARFLNTSDPLELAAHCMEDIDADFSSKVNAGDIIVADDNFGCGSSREHAPISIKASGVSCVIANSFARIFYRNAINIGLPILECPEAVAVIEAGDEVEVDFDSGVITDVTKGQSFQGQAFPEFMQTLIAAGGLVNYINATEK | Catalytic Activity: (2R,3S)-2,3-dimethylmalate = dimethylmaleate + H2O
Sequence Mass (Da): 17369
Sequence Length: 163
Pathway: Cofactor degradation; nicotinate degradation; propanoate and pyruvate from 6-hydroxynicotinate: step 7/8.
EC: 4.2.1.85
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Q5LRT0 | MLGQMMYQPLLISSLIDHAARYHGEAQIWSVSTEGGVEETNWAGIADNARRLGSVLTDAGLAPQSRVATLAWNNRRHLEIYYGVSGAGFVLHTINPRLFPEQLVYILNHAEDRILFFDATFLPLVEGIRPHLTTVERLVLMGPRDEAAAARIEGLEFYDEFVATGDAGFDWPDLDERTASSLCYTSGTTGNPKGVLYSHRSTVLHSFGSNTRDCIGFSARDVVMPVVPMFHVNAWGTPYACAMSGSCMVLPGPDLHGEALVGLIDRYRVTIALGVPTIWQGLLATARAKGSTLESLTRTVIGGAACPPSMIAEFRDRYGVDTVHAWGMSEMSPLGTTNQPLAKHGALPIEAQHKLRENQGRPPYGVELKIVDDDGNTLPNDGQTQGDLMVRGHWVLDSYFQLQDQPILSDGWFATGDVATLDRDGYMTIRDRSKDIIKSGGEWISSVELENIAVAHPKLATAAVIGVPHPKWDERPLLVAVKAEGETPDEAELLAFFDGKIAKWQVPDRVVFVEALPLNATGKVLKRTLREQFRDVLTG | Function: Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton. Catalyzes the ATP-dependent ligation of methylmercaptopropionate (MMPA) and CoA to yield methylmercaptopropionate-CoA (MMPA-CoA) . It is also active with short-chain-fatty-acid (carboxylic acids up to six carbons in length) .
Catalytic Activity: 3-(methylsulfanyl)propanoate + ATP + CoA = 3-(methylsulfanyl)propanoyl-CoA + AMP + diphosphate
Sequence Mass (Da): 59066
Sequence Length: 539
Pathway: Lipid metabolism; fatty acid metabolism.
EC: 6.2.1.44
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Q5LLW7 | MTYQAPVRDIMFAIEHLSQWPQVEALQTYSEIELDDARAALEEFGRFCGEMIAPLSTIGDTEGARLENGRVVLPEGYKTAYDQFVDMGWQSLSHPAEHGGMGLPKVVGAAATEIVNSADMSFGLCPLLTNGAIDALSITGSDAQKAFYLDKLITGRWSGTMNLTEPQAGSDLSRVRCTAVPQDDGTYAISGTKIFITFGEHDLSENIVHLVLARTPDAPEGVRGLSLFVVPKLLAGEGGETSQRNTLGCVSLEHKLGVRASPTAVMEYDNATGYLVGEENSGLRYMFIMMTSARYAVGVQGVAIAERAYQHALSYARDRIQSRPVDGSAQDAVPIIQHPDVRRMLLRMRALTEGGRALAIATGGWLDLAEHGPEEARAEAQSMAEFLVPLVKGFCTERAVEVASLGVQIHGGMGFIEETGVAQFYRDARILPIYEGTTAIQANDLLGRKVLRDGGRTARRFAEMIAATEGELSKGGAAAQRIAQRLAEARAAFAAGLDHLLATAGQDPNRAYAGSVPFLMLTGNLATGWQLGLSALAAEAELAKGGDAEFLQAKIATADIFAQQVLVECSAEHSRITDTGDSLLTASL | Function: Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton, by mediating the conversion of 3-(methylthio)propanoyl-CoA (MMPA-CoA) to 3-(methylthio)acryloyl-CoA (MTA-CoA).
Catalytic Activity: 3-(methylsulfanyl)propanoyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = 3-(methylsulfanyl)acryloyl-CoA + reduced [electron-transfer flavoprotein]
Sequence Mass (Da): 62854
Sequence Length: 588
EC: 1.3.8.-
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Q5LLW6 | MTQDVTSGYSNLDLDLRDNGVCVVTLNRPDKRNALDVATIEELVTFFSTAHRKGVRAVVLTGAGDHFCAGLDLVEHWKADRSADDFMHVCLRWHEAFNKMEYGGVPIIAALRGAVVGGGLELASAAHLRVMDQSTYFALPEGQRGIFTGGGATIRVSDMIGKYRMIDMILTGRVYQGQEAADLGLAQYITEGSSFDKAMELADKIASNLPLTNFAICSAISHMQNMSGLDAAYAEAFVGGIVNTQPAARERLEAFANKTAARVRPNS | Function: Involved in the assimilation of dimethylsulphoniopropionate (DMSP), an important compound in the fixation of carbon in marine phytoplankton, by catalyzing both the hydration and the hydrolysis of 3-(methylthio)acryloyl-CoA (MTA-CoA) to acetaldehyde, CO2, MeSH, and CoA .
Catalytic Activity: 3-(methylsulfanyl)acryloyl-CoA + 2 H2O = acetaldehyde + CO2 + CoA + methanethiol
Sequence Mass (Da): 28836
Sequence Length: 267
EC: 4.2.1.155
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Q97UL5 | MLKSVTVSAPSNIAVVKYWGKRGDERLNLPLNNSLSITLDDQLSVITKVTLNDKNIVIVNDRILSEDEMKEYAGRVLDTFKKIVGKEFHVKVESKSKFPINAGLASSAAGIAALAFSLNELLELNLKSEELSKIARLGSGSACRSMFGGFVVWNKGEREDGEDSYCYQIFRHDYWSELVDIIPILSEKEKKISSRKGMIRSAETSELMECRLKYIEKTFNEVIEAIRNRDEKKFYYLMMRHSNSMHAVILDSWPSFFYLNDTSIRIMEWIHDYGKAGYTFDAGPNPHIFTTERNIGDILEFLKSLEIKRIIVSKVGDGPKVLSRE | Function: Catalyzes the decarboxylation of mevalonate 5-diphosphate (MVAPP) to isopentenyl diphosphate (IPP). Functions in the mevalonate (MVA) pathway leading to IPP, a key precursor for the biosynthesis of isoprenoid compounds such as archaeal membrane lipids.
Catalytic Activity: (R)-5-diphosphomevalonate + ATP = ADP + CO2 + isopentenyl diphosphate + phosphate
Sequence Mass (Da): 37028
Sequence Length: 325
Pathway: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 3/3.
EC: 4.1.1.33
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Q9LCC1 | MTEASESCVRDPSNYRDRSADWYAFYDERRRKEIIDIIDEHPEIVEEHAANPFGYRKHPSPYLQRVHNYFRMQPTFGKYYIYSEREWDAYRIATIREFGELPELGDERFKTEEEAMHAVFLRRIEDVRAELA | Function: Hydrolyzes N,N-dimethylformamide, and to a lesser extent N,N-dimethylacetamide and N,N-diethylacetamide. Has no activity against the substituted amides N-methylformamide, N-ethylformamide, N-ethylformamide and N-methylacetamide or the unsubstituted amides formamide, nicotinamide, acetoamide, benzamide, acetamide and acrylamide.
Catalytic Activity: H2O + N,N-dimethylformamide = dimethylamine + formate
Sequence Mass (Da): 16031
Sequence Length: 132
EC: 3.5.1.56
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Q3INE3 | MQDTAKYLVHADITADGVVERSDVVGAVFGQTEGLLGDELDLRELQDASKVGRIDVEIDSENGQSFGRITIATSLDRVETAILGGALETIDRVGPCRSAIEVRKIEDVRSAKRREVVERAKSLLDGAFDESMRSSRDLVEEVRESVRVEDITDYEGLPAGPAVADSDAIVVVEGRADVLTLLQYGIKNAVAVEGTNVPEAVASLTETRTVTAFLDNDRGGELIRKELGQVGDIDYVATPPDGKCVEDLARHEVMSALREKVPYGRFKQAASDDADPEAAEQRTGEAAGATAADSEPAATDGIGGVTTDAEGKPVSSPESPAESPAADETAAVSAGTTPADAEEAAVDGATKTSTAGEEPNTPDDELTATSEAAEPGSAETKGESTAAEAPESSADGPAAAGASTDEQPKTLRGHVSDVIEAETGTFRLLDAEFAPLAAGDAGDVFEAVADAETVPAAVVVDGEASQRLLDIAAQRGIDHVVAASTGEFVKRPTSVRVRTATQLLNPEKA | Cofactor: Binds two Mg(2+) per subunit.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 52822
Sequence Length: 509
EC: 2.7.7.101
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P57029 | MIPSDFIDELLAKTDIVDIIDEQVPLKKGGANYMACCPFHKEKTPSFSVSPTKQFYHCFSCGAHGSAIGFVMEHQGLSFPEAVQFLADRVGMVVPKVHGQNDNPEVRAERKKKQQTLEETTAAAADFYAQQLKFNPAAKAYLDKRGLSAEVIAHYGLGYAPDGWQPLTQVFQPYPNTALVDTGMVIDNEGRHYDRFRHRIMFPIRNPRGQVIGFGGRVLDDSKPKYLNSPDTPLFDKGKNLYGLYEGRAAVKEAGRILVVEGYMDVVALAQFGVGYGVAALGTATTAEHVKILMRQADSIYFCFDGDSAGRKAAWRALENALPQLKDDKSLHFLFLPEEHDPDSYIRAYGKAQFEDALLNQSKPLSEYFWEHLSDGIHLNTQEGKAELVKTSSPLLAQITAPALAYLLKQRLSELVGIDPDNLAQLLGQEAPKRHVKQKNYKLPPISVKQPVMLTLVQRQIRSLLINPDWAAYIDLPDYLALDGDFACLANLAESIKNHAAVPETAQVLEYMRGSPYEETITRIFHSTHQSEEMNSSSEEDCENFQIGMKKLLNELKYSQIETLKQKSLQSGLNESEKKLLLSLLTAKQN | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 65915
Sequence Length: 590
Domain: Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
EC: 2.7.7.101
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Q6L1F0 | MNVDPNITKYMIKAKIVTDGVVEKPDVVGAIFGQTEGLLGDELDLRDLQKSGKIGRIEVEIDTKKGRTEGYVLIPSGLDQVESSILAAALETIDRIGPCKAKVEIESIEDVRINKRDRVIKRAEELYRKMGENGKSLSESIVQTVREEVEKKEIISYGEEHLPAGPAIADSDSIIVVEGRNDVLNLLRYGIKNTIAVQGTSVPKTVKELSKSRTVTLFVDGDHGGDLIIKEMLQVADVDFIARAPPGTEVEELTYKQIIKALKYKTPVEQYLETHGMIEELKEWSSRNTKELEERQGNELKNERPEKINENEESEKNVELKEGSVQKLETVPEFDPSSPESIKFKLKQLYESRELELFDGQSSVGKFPVSDAIEKIESMHGDLLITGGIISQRLLDIAYNIGVKAIYGFKIGNITKKPDDIKVVAWDHI | Cofactor: Binds two Mg(2+) per subunit.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 47945
Sequence Length: 429
EC: 2.7.7.101
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Q9I5W0 | MAGLIPQSFIDDLLNRTDIVEVVSSRIQLKKTGKNYSACCPFHKEKTPSFTVSPDKQFYYCFGCGAGGNALGFVMDHDQLEFPQAVEELAKRAGMDVPREERGGRGHTPRQPTDSPLYPLLSAAAEFYKQALKSHPARKAAVNYLKGRGLTGEIARDFGLGFAPPGWDNLLKHLGGDNLQLKAMLDAGLLVENSDTGKRYDRFRDRVMFPIRDSRGRIIAFGGRVLGDDKPKYLNSPETPVFHKGQELYGLYEARQKNRDLDEIMVVEGYMDVIALAQQGIRNAVATLGTATSEEHIKRLFRLVPSILFCFDGDQAGRKAAWRALESVLPNLQDGKRVRFLFLPEGEDPDSLVRAEGEDAFRARITQQAQPLAEYFFQQLMLEADPATLEGKAHLATLAAPLLEKIPGNNLRLLMRQRLSEITGLSGENIGQLAHHSPPPSSMDHGASGVLDGDDYFAASAYYENEPSHAPFDAAPGYVEAQPRKSWNKDKKPWDGKKWDGKKKWDKGGRGDFKAPQRTPVSVESTTLNALRTLLHHPQLALKVDDAGTLAREQDTYAQLLVSLLEALQKNPRQSSMQLIARWHGTPQGRLLQALGEKEWLIVQENLEKQFFDTITKLSESQRFGEREERLRSVMQKSYSELTDEEKALLREHYSVAASSPSQS | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 74176
Sequence Length: 664
Domain: Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
EC: 2.7.7.101
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Q8ZVU9 | MGALTIVAKYMIVAQIEVNGSVDKSDIIGALFSQTEGLLGKDMDLRELQMMGRIGRIEVDIFEKNGKTKAKIHIPSNLDRYETALVAALIESIERVGPYPAAVKVVEIRDLREEKRKKIIEKAKELVKLIEEEILPDTKEIIEKLKEDVAKAEIIEYGPERLPAGPDVDKSDSIIIVEGRADVVNLVKHGYRNVIALEGISRGVPQTIIELSKKKNVTVFIDGDKGGELVLRELLKVAHVDYIARAPPGKEVEQLTAKEIAKALRNKITLEEWLAQQKAAGEKAETPQQPPPQQPVPQQEVREEAQKPAFPFDITKKIDEMLGTLEAEIYDENWTLVKRLPVRELPDFLTTSGDSIYAIILDGITTQRIVDLAAKKGVKIIVTARTGPLTKVPENMQILTFDQLKKVE | Cofactor: Binds two Mg(2+) per subunit.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication. Also part of the exosome, which is a complex involved in RNA degradation. Acts as a poly(A)-binding protein that enhances the interaction between heteromeric, adenine-rich transcripts and the exosome.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 45496
Sequence Length: 408
EC: 2.7.7.101
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P30103 | MRVTQEFYEFLRNRINISDVVRQKLALTRKSSNYVGLCPFHQEKTPSFTVSDSKRFFYCFGCKASGDVIKFTSNISGLSYNESAIKLANDYGIEIPKLTVKQKEFYEESDNILNILELANKFFRTQLTPEILNYLYKRNITETTIKEFSIGFAPRNNKFEKFFLDKKIDITKLGQAGLIGKCKNGKIYNLFSNRITIPIRNIYNKIVGFGGRVLGNELPKYLNSFETIVFQKSDILYGEHKAISSSYKKNRSILVEGYFDVIALHQAGFNEVVASLGTSVTESHLHKLWRAGDEIILCLDGDNAGIKASIRTINLALPLVNSEKKISFIRLPSGLDPDDAVNKNGADFFAKLIDKRISLSEMIWHIEYSGKNFRTAEEKANLEKNLKDYCNKISDSNLKASYYRFFKDQIWQNLVTKQKKIITPSSNSVLIASSHCYSELEMLEHAFCALLIKFPIMFAEKDIRDFILNLNFNNKSLEEFRNWYLNEIIDNKVKENEITAIVEKTSFFDIFLLLSKADNLFLDISFNKNNIRLDLLWQWLYKKYYLINLQQEYAISINSNHDFEKVLLYKKEIIKIVNELQVLNESFINQTIT | Cofactor: Binds 1 zinc ion per monomer.
Function: RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Catalytic Activity: ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.
Sequence Mass (Da): 68684
Sequence Length: 593
Domain: Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
EC: 2.7.7.101
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Q057X7 | MTKQDYYTTLNISNTASQLDIKRAYKKLAIKYHPDRNQGNKTAEEKFKKIKQAYEILSDTKKRNLYDQYGHSAFEQNNNSNNEFHSSFTTSTSDFNDIFGDVFGDIFGSNKKNRKEKGSDLQYNIILTLEEAVKGIKKEIRIPKLDKCQSCYGYGSAYGSKPSTCTSCNGHGQIHMRKGFFSVQQTCSTCRGTGTMIKNPCKICFGQGRIKKSKKLSITIPAGIDTNDQIRLNNEGEAGKYGAKSGDLYIQIKVKKHPIFKRDENNLHCKIPINFVIAGGSIILYSSFRGEITVPTLEGKINLKIPSETQSGKIFRIRGKGVKSVRKGFQGDLFCKIIVETPVNLNSFQKKILYQLGESFKNYKGENNSPKSKRFFNSVKKFFNNFTK | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Sequence Mass (Da): 43906
Sequence Length: 388
Domain: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Subcellular Location: Cytoplasm
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Q6AEC0 | MADHYEVLGVERNATPDEIKKAYRRLARELHPDVNPSTEAQERFKLVTHAYDVLSDPQQRQQYDRGGASGFGGGGGADFSGFGDIFETFFGGGGASRGPRSRRERGQDALLRVEVDLDEVVFGAHRDLEVDTAIVCETCDGSCCQPGTAPVPCDICHGTGSIQRSVRSLLGNVMTSSPCGSCRGYGTVIATPCVTCQGQGRVRARRTVPVDIPAGVDTGLRLQMPGSGEAGPAGGPNGDLYLEIKVKHHDVFSRDGDDLLCTLEVSMADAILGAAATIKALDGDIRLELKPGTQSADIVSVKDRGITHLRCSGRGDLRVGIQVVTPTKLDHREKELIKKFAESHKASEPSLARFQQGLFAKLRDRFLNV | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Sequence Mass (Da): 39646
Sequence Length: 369
Domain: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Subcellular Location: Cytoplasm
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P61440 | MSERSYYDILGVSKSANDEEIKSAYRKLAIKYHPDKNKGNKESEEKFKEATEAYEILRDPKKRQAYDQFGKAGVSGGAGGFGQGAYTDFSDIFGDFGDIFGDFFGGGRSSGFGGGRRSGPQRGSDLRYNLEVSLEDAALGREYKIEIPRLESCVDCNGSGASKGSSPATCPDCGGSGQIRRTQGFFSVATTCPTCRGKGTIISNPCRSCGGQGLQEKRRTINIKIPPGVETGSRLKVSGEGEAGPNGGPHGDLYVVTHIKKHELFERQGNDLILVRKISLAQAILGAEIEVPTIDGKKAKMKIPEGTESGQVFRLKGHGMPYLGAYGKGDQHVIVKIEIPKKITRRQRELIEEFARESGENIPGSKGKIFTK | Cofactor: Binds 2 Zn(2+) ions per monomer.
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding. Also involved, together with DnaK and GrpE, in the DNA replication of plasmids through activation of initiation proteins.
Sequence Mass (Da): 40258
Sequence Length: 372
Domain: The J domain is necessary and sufficient to stimulate DnaK ATPase activity. Zinc center 1 plays an important role in the autonomous, DnaK-independent chaperone activity of DnaJ. Zinc center 2 is essential for interaction with DnaK and for DnaJ activity.
Subcellular Location: Cytoplasm
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O60884 | MANVADTKLYDILGVPPGASENELKKAYRKLAKEYHPDKNPNAGDKFKEISFAYEVLSNPEKRELYDRYGEQGLREGSGGGGGMDDIFSHIFGGGLFGFMGNQSRSRNGRRRGEDMMHPLKVSLEDLYNGKTTKLQLSKNVLCSACSGQGGKSGAVQKCSACRGRGVRIMIRQLAPGMVQQMQSVCSDCNGEGEVINEKDRCKKCEGKKVIKEVKILEVHVDKGMKHGQRITFTGEADQAPGVEPGDIVLLLQEKEHEVFQRDGNDLHMTYKIGLVEALCGFQFTFKHLDGRQIVVKYPPGKVIEPGCVRVVRGEGMPQYRNPFEKGDLYIKFDVQFPENNWINPDKLSELEDLLPSRPEVPNIIGETEEVELQEFDSTRGSGGGQRREAYNDSSDEESSSHHGPGVQCAHQ | Function: Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro) .
Location Topology: Lipid-anchor
Sequence Mass (Da): 45746
Sequence Length: 412
Subcellular Location: Membrane
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O35824 | MANVADTKLYDILGVPPGASENELKKAYRKLAKEYHPDKNPNAGDKFKEISFAYEVLSNPEKRELYDRYGEQGLREGSGGGGGMDDIFSHIFGGGLFGFMGNQSRSRNGRRRGEDMMHPLKVSLEDLYNGKTTKLQLSKNVLCSACSGQGGKSGAVQKCSACRGRGVRIMIRQLAPGMVQQMQSVCSDCNGEGEVINEKDRCKKCEGKKVIKEVKILEVHVDKGMKHGQRITFTGEADQAPGVEPGDIVLFVQEKEHEVFQRDGNDLHMTYKIGLVEALCGFQFTFKHLDARQIVVKYPPGKVIEPGCVRVVRGEGMPQYRNPFEKGDLYIKFDVQFPENNWINPDKLSELEDLLPSRPEVPNVIGETEEVELQEFDSTRGSGGGQRREAYNDSSDEESSSHHGPGVQCAHQ | Function: Co-chaperone of Hsc70. Stimulates ATP hydrolysis and the folding of unfolded proteins mediated by HSPA1A/B (in vitro).
Location Topology: Lipid-anchor
Sequence Mass (Da): 45766
Sequence Length: 412
Subcellular Location: Membrane
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Q96EY1 | MAARCSTRWLLVVVGTPRLPAISGRGARPPREGVVGAWLSRKLSVPAFASSLTSCGPRALLTLRPGVSLTGTKHNPFICTASFHTSAPLAKEDYYQILGVPRNASQKEIKKAYYQLAKKYHPDTNKDDPKAKEKFSQLAEAYEVLSDEVKRKQYDAYGSAGFDPGASGSQHSYWKGGPTVDPEELFRKIFGEFSSSSFGDFQTVFDQPQEYFMELTFNQAAKGVNKEFTVNIMDTCERCNGKGNEPGTKVQHCHYCGGSGMETINTGPFVMRSTCRRCGGRGSIIISPCVVCRGAGQAKQKKRVMIPVPAGVEDGQTVRMPVGKREIFITFRVQKSPVFRRDGADIHSDLFISIAQALLGGTARAQGLYETINVTIPPGTQTDQKIRMGGKGIPRINSYGYGDHYIHIKIRVPKRLTSRQQSLILSYAEDETDVEGTVNGVTLTSSGGSTMDSSAGSKARREAGEDEEGFLSKLKKMFTS | Function: Modulates apoptotic signal transduction or effector structures within the mitochondrial matrix. Affect cytochrome C release from the mitochondria and caspase 3 activation, but not caspase 8 activation. Isoform 1 increases apoptosis triggered by both TNF and the DNA-damaging agent mytomycin C; in sharp contrast, isoform 2 suppresses apoptosis. Can modulate IFN-gamma-mediated transcriptional activity. Isoform 2 may play a role in neuromuscular junction development as an effector of the MUSK signaling pathway.
PTM: Tyrosine phosphorylated.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 52489
Sequence Length: 480
Domain: Modulation of apoptosis, i.e. proapoptotic activity of isoform 1 and antiapoptotic activity of isoform 2, is J domain-dependent.
Subcellular Location: Mitochondrion matrix
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P25686 | MASYYEILDVPRSASADDIKKAYRRKALQWHPDKNPDNKEFAEKKFKEVAEAYEVLSDKHKREIYDRYGREGLTGTGTGPSRAEAGSGGPGFTFTFRSPEEVFREFFGSGDPFAELFDDLGPFSELQNRGSRHSGPFFTFSSSFPGHSDFSSSSFSFSPGAGAFRSVSTSTTFVQGRRITTRRIMENGQERVEVEEDGQLKSVTINGVPDDLALGLELSRREQQPSVTSRSGGTQVQQTPASCPLDSDLSEDEDLQLAMAYSLSEMEAAGKKPAGGREAQHRRQGRPKAQHQDPGLGGTQEGARGEATKRSPSPEEKASRCLIL | Function: Functions as a co-chaperone, regulating the substrate binding and activating the ATPase activity of chaperones of the HSP70/heat shock protein 70 family . In parallel, also contributes to the ubiquitin-dependent proteasomal degradation of misfolded proteins . Thereby, may regulate the aggregation and promote the functional recovery of misfolded proteins like HTT, MC4R, PRKN, RHO and SOD1 and be crucial for many biological processes . Isoform 1 which is localized to the endoplasmic reticulum membranes may specifically function in ER-associated protein degradation of misfolded proteins .
PTM: Ubiquitinated by STUB1; does not lead to proteasomal degradation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 35580
Sequence Length: 324
Domain: The J domain is sufficient to interact with HSP70 (HSPA1A or HSPA1B) and activate its ATPase activity . The J domain is also required for the HSP70-mediated and ubiquitin-dependent proteasomal degradation of proteins like ATXN3 . The J domain is required to reduce PRKN cytoplasmic aggregation .
Subcellular Location: Cytoplasm
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Q8RC42 | MDREEARKRIEELREKINYHNYRYYVLDQPEISDYEYDMLMRELIELEEKYPEFKTPDSPSQRVGGEPLDEFEPFTHIVPMLSLANAFTAEEIKEFDRRVKEAVGEVEYVVEPKIDGLSVELVYENGMFTVGSTRGDGIVGENVTPNLKTIKSIPLRLKDSVNLVVRGEVFMPKASFAKLNEERAERGESLFANPRNAAAGSVRQLDPKVTAKRDLDIFIFNLQRIEGRDFKTHVEALEFLKEQGFKVIPLIKKCTTIEEVIKAIEELGEMKDSLPYDIDGAVIKVNELDKREILGQTAKDYRWAIAFKYPAEMKKTKIVDIVVQVGRTGALTPTAVLEPVVISGSVVSRATLHNEDYIKEKDIRIGDTVLVHKAGGIIPEVVEVVKEERTGDEKAFVMPDKCPECGALAVRLPGEAVRRCTGLNCPAQIARRIIHFASKDAMDIEGLGPAIISQLLSKGLIQNVADLYYLKYRDLITLERMGDKSARNLLEAIEKSKKRDLDRLLFGLGINLIGSKAAQVIAEHFKSMDNIMKAKYEDFLELPDIGPKMARSIVTFFSEEQNRRVVERLKEAGVNMEKLSTGKVSNIFEGKIFVLTGALKNYTRDEAARLIVERGGKVTNSVSKKTDYLIVGADPGSKLKKAQELGVKIINEEQFEAMLKGDIQP | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Catalytic Activity: NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.
Sequence Mass (Da): 74963
Sequence Length: 666
EC: 6.5.1.2
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B2GL64 | MSTVNAKGAKPATDANGQSLNPEEPSEALREEYAQLSDRVREARAAYYVHDQPVISDAEYDQLYRSLEEFEALHPELKANDSPTQEVGGEVGAAFSPVKHLEKMYSLEDVFSTDELVAWLERAQKQVAELPGAPEVAWLSEVKIDGLAVNLLYRDGVLVRAATRGDGTTGEDITHNVATIKTIPQRLSGENLPEEVEVRGEVFISSKDFRTLNEAMVEEGRAPFANPRNAAAGSLRQKDPQVTARRPLSMFVHGIGYVRGVDLETQSEAYEILRGWGLPVSPYSRVLSTVAEVLEFIAEFGDKRHALLHEIDGIVVKVDDRRTQFRLGYTSRVPRWAVAYKYPPEEVNTTLVDILVNVGRTGRVTPFGLMDPVRVAGSTVEMATLHNQDMVRAKGVLIGDTVVLRKAGDVIPEIVGPVVALRDGSEREFVMPAECPSCGTPLRPAKEGDVDIRCPNAETCPSQLKERVNHAAGRGAFDIEALGEEAARALTQPVPLDAPDGTELSVPPLRNEAGLFDLTPEDLRDVMVWRDARRTVTDEETGEKVQRVTPELVPYFWTKPTKARPSVPSKTTEQMFAQLEQAKDTELWRVLVALSIRHVGPTAARSLATSLRSMDAIRQADPETLAGTDGVGPVIAQAVQEFFAEPWRRRVVEQWAAAGVRMEEEVDESTPRTLEGVTVVVTGSLEGYSRDSAKEAILKRGGKASGSVSKKTHFLVAGDNAGTKLDKAESLGVPVLDEAGFEQLLAQGPEAFGDRADAADQPAAGE | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Catalytic Activity: NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.
Sequence Mass (Da): 83591
Sequence Length: 766
EC: 6.5.1.2
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Q1GBF7 | MAESLEEAKQEVRQLRAQLDQWAKAYYEQDAPVVEDHVYDEKYARLLELEAAYPELKSADSITQRVGGEVNSDLPKVEHPVPMLSMGDVFSKEELAEFDQRVQKAIGHPVAYNVELKIDGLSLSLEYEEGCLKRASTRGNGQVGEDVTKNVKYIKDVPQKLPKAITTEVRGECYMSKEAFAKLNQERDEAGESIFANPRNAAAGSLRQLDPKVTKKRQLSTFIYTWINPPAGIDSQHQAICEMAKLGFHTNENGRRLENLADVYDYIDEFTKKRDSLPYVIDGIVLKVDDLALQADLGNTVKVPRWEIAYKFPPEEEETVVREIEWTVGRTGVVTPTAVMDPVRLAGSTVARASLHNPDLLAKLDVRLGDTVKLHKAGDIIPEISEVVLSKRPEDSVPYEVPTKCPSCGEDLVHLDEEVALRCINPSCPAQVEEGITHFASRQAMNIAGLGPKIVKQLIAKDLVHNVADLYYLTADDLSQLDHFKEKSINNLLVAIDQSRKNSVELVLFGLGIDNVGGKAAQLIARKFKNMSKIASASVQELTAIDTIGMTIAESLTAYFQQEEAKKLLARLEEAGVNMDYLGEDGEAADNFFKGKTVVLTGKLAHYSRAEFTKKLQALGAKVTGSVSKKTNCLVYGEDAGSKLAKAEALDIPRLTEAEAISKIEEKDTEK | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Catalytic Activity: NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.
Sequence Mass (Da): 74205
Sequence Length: 671
EC: 6.5.1.2
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A9KPL0 | MQGKKQRITQLTELLDEAARVYEQEDREIMSNFEYDKLYDELKKLEEETGIVLAGSPTRKVGYEILSELPKERHESAMLSLDKTKEVPALIDWLGNKEGILSWKMDGLTIVLTYRNGELVKAVTRGNGEVGEVVTNNAKVFKNLPLTIPYEGELIIRGEAVIRYSDFEMINAQIPDADAKYKNPRNLCSGSVRQLNNAITAKRNVNFFAFALIRMDEMNRFKTMMEQFNWLKELGFDVVEEKLVTAENMAETMEYFESHIITNDFPSDGLVLFFNDIAYGESLGRTSKFPRNGIAFKWRDEIKETTLQEIEWSASRTGLINPVAIFEPVELEGTTVSRASLHNISIMEGLELGLGDKVTVYKANMIIPQIADNLTRSGHLPIPKTCPVCGGDTMIKQDSDVKSLYCMNPECLAKKIKSFTHFVSRDAMNIEGLSEATIEKLIAKGLIKELADIFHVKDFKEEITTMEGFGEKSFRNLVDSVEKARTPILAKFIYSLGIANVGLANAKLICKEFGYDFNKVSNATVDELTQIPQIGYVIAEAFVSYFQKPENKLIIEDLLKEITFEKEEAAGGSEKLKGLTFVITGSVEHFTNRNEVKDVIEQHGGKVTGSVTAKTNYLINNDNTSSSSKNKKARELGIPVITEEEFIQLLNEA | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Catalytic Activity: NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.
Sequence Mass (Da): 73434
Sequence Length: 653
EC: 6.5.1.2
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C1D4R5 | MTDLNPTARAAGLRALLHRYNHEYYVLDAPSVPDAEYDRLFRELEALEAAHPELASADSPTRRVGGAPLAAFASVTHRLPMLSLNNVFSDMQDSDPAGRHAELAAFDQRVRDGLGLDEVEYAVEPKFDGLAVSLVYEHGVLVQGATRGDGETGENVTENLRTVRSIPLRLENAPGDDLFAPAVVPARLEVRGEVLMLKRDFERLNSEQDAAGLKRFANPRNAAAGSLRQLDSRITASRRLTFFAYAVAEADGVSLPATHSATMDWLAGLGLPVSRQRSVVRGLAGLTGAYEAMLAQRAGLPFDIDGVVYKVNRLSEQARLGFVSRAPRFAVAHKFPAEEALTVVEDITVQVGRTGAITPVARLQPVFVGGVTVTNATLHNEDEVRRKDVHVGDTVIVRRAGDVIPEVVSVLAERRPPQARAFEMPLVCPVCGSHIVREADEAVARCSGGLYCSAQHKQALQHFASRKALDVEGLGEKLVDQLVDAGLVHTPADLFALDQPALARLERMGDKSAENLVRALDACRHTTLARFVYALGIRNVGEATARDLARHFGTLDALMAADQDMLMTAPDVGPIVARSIVDFFAEAHNREVVDALLAAGVSWPVVETVTSAGVAGVSGKTFVLTGTLPTLGRDDAKARIEAAGGKVTGSVSKKTHYVVAGEAAGSKLDKAHELGITVLDEAALLALLAGNA | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Catalytic Activity: NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.
Sequence Mass (Da): 73986
Sequence Length: 692
EC: 6.5.1.2
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Q4UN15 | MQNIDLISEEEAKKLLEELADKIAAYNHAYYIEDNPLVSDSEYDQLFNTNLKLEQKFPHLVLENSPSKKIGAKITNKFAKITHQIPMLSLSNAFDEQDVRDFVDRIKNFLRLDEFAPIFCEPKIDGLSFSAIYKNGLLTTGATRGDGYVGEDITANIKTIKNFPHKIDNAPEFLEVRGEIYIEKQDFLNLNKEQEEQGRDKFANPRNAAAGSLRQLDASITAQRSLKYFVYSGGVTEQNLASSQEQLLIKLKEFGFSVNEISKLTNSEEEIFTFYEYLKTNRENLPYEIDGVVYKLNDFALQNRMGFIARSPRFATAHKFPAIIGRTKLLSITVQVGRTGTLTPVAELEPIEIGGVTVSRATLHNFQEIMRKDVRIDDYVFLQRAGDVIPKITGVDIGKRPNDTIAFDTPLFCPSCNSKLHYAPEDIIIRCDNGLNCPAQNYERIRHFVSKNAMDIEGLGRKQVEFLIDKGLISNPLDIFFLKEKNDSSLTKLENMDGWGKKSVENLFKNIEQSKNVSLPRFIYALGIRHIGEQNAKLLAREFGSYANFIAQMELLSKNDLDIYQKLNDLEGIGDKILVDIIDFFDVKENTTLIKKLGEVLNIEDYKETREQSSLTGKIIVFTGSLPTISRAEAKATAEKLGAKVAASVSSNTDLVVAGVDAGSKLKKAKELNIKIIGEEEWLTLIKNV | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Catalytic Activity: NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.
Sequence Mass (Da): 77634
Sequence Length: 689
EC: 6.5.1.2
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A5V1U3 | MNNDHLTRRVEALREQIRYHNYRYYVLDEPVISDAEYDALMRELRALEAAHPELVTPDSPTQRVGAPPGEQFAKVQHVVPMLSLANASDEAEVRAWYDRVVRLLGNDARVAFVVEPKIDGLAVTLIYRNGILVRGATRGDGETGEDVTANLRTIPGIPLRLGAFASNPEGQTNGAPVQAVIPPLIEVRGEVYMRIADFLRLNEQLAASGEKVAANPRNAAAGSLRQKDPAITARRPLRFFAYGIGQIEGVQVQTQWETLNLLRTLGFPVNRDARRFERLDDALAYCREWMTRRDELEYEVDGVVIKIDSLAQQAQLGVVGRDPRWAIAFKFPAREAVSRLIDIVVNVGRTGVITPNAVIEPVNIGGVTVRNASLHNADYIAERDIRIGDYVIVKRAGDVIPYIVGPIVARRDGSERPWQMPATCPACGTPLERAEGEVAYRCPNFGICPAQITRRIEHFVSRGAMDIAGIGEKQVQLFVERGWVQDVADLYTLTPDHFANVEGYGPKRVANLLSAIAGSKNRPLHRLIVGLGIRYVGEVVAQILADHFGSLDALAAASADEIDALEGIGPAIAASVAAYFARPESKALIAKLKRAGVRTEAQETARASRGNALAGKTFVITGTLPSMSREEASALITAHGGKVSGSVSKKTDYLVIGAEPGGTKFAKAQELGIPMIDEAGLLALIGSGRTADDQATPASDRRAATASVPPSDDAPGSPRQLDFDLT | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Catalytic Activity: NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.
Sequence Mass (Da): 78636
Sequence Length: 726
EC: 6.5.1.2
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Q1AZ75 | MGAPTLPRIIPPVAEKLAEARQRVEELREQIRYHNRKYYVEDAPEISDAEYDALYRELEELESRFPELVTPDSPTQRVGGEPLEEFEEVRHAVPMLSLQNARRVEELREWDARVRRLLGPEEEGRLRYVTELKIDGLAVSLRYENGRLVRGATRGNGFVGEDVTRQLRTIRSVPDRLDDDPPGVLEPRGEVYIKLKDFEEFNRRRQERGERPFANPRNLAAGSVRQLDPRVTARRPLTIYLYGVGEGYENFESHSEALAALRRYGLRVNPHTVHGDIDSVIEECGRWAKKREALDFQVDGVVVKVDSREQQERLGAVQKAPRWAIAYKFEPLAGRTRLRDIVVTVGRTGALTPQAVLEPVNVGGVTISRATLHNEDYIKEKGILIGDTVIVERAGDVIPQVVRPVPEERDGDEEEFRMPERCPVCGERVSRPEGEAITRCANVRCPAQALEHIIHWASRGAMDIEGLGEKLARKLFDLGLIRDVADLYELRAEQLAPLEGLGEKSAQNLIRAIERSKERPFDRVLFGLGIRHVGSATAELIAERFSGEELLRGVGVEELTQIEGVGEIVARAVVEYFSLEENRKLVRRLMEHGLNFGPVRGKPEEGPLSGRRLVITGTLSRPRSEISDLIEGAGGTVTSSVSRNTDYLVAGENPGSKLERARELGVPVLDEEGLRRLLSGEERPG | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Catalytic Activity: NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.
Sequence Mass (Da): 76996
Sequence Length: 685
EC: 6.5.1.2
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B8I3I1 | MADKIQLMKDKIEILDRAAKAYYQENTEIMSNIEYDKLYDELLELEKETGVVLSNSPSIHVGYELLSNLPKERHEKPMLSLDKTKDVGTLKEWLGTQKGILSWKLDGLTIVLTYQDGHLVKAVTRGTGEEGEVITNNARVFRNLPVTIAYKGTLILRGEAIIRYSDFIKINNEIADVGVKYKNPRNLCSGSVRQLNNKVTSERNVYFFGFSLVKADNVELDNSRASQMNWLKNQGFDIVDFKEVTSSNIEETVQWFSQNIEANDFPSDGLVLTFEDIAYGESLGSTAKFPRDSIAFKWRDEIKETTLLNIEWSPSRTGLINPIAIFEPVELEGTTVSRASIHNISIMEGLELGIGDTIGVYKANMIIPQISENLTRSGMAPIPEECPVCKGKTEIKQENGVKTLYCVNNECLAKQIKSFTHFVGRDAMNMEGLSEATLEKLIAKGLIKELADLFHIEKYKNEILELEGLGEKSFNKLITSINKARKTTAVRLLYSLGIPNVGLSNAKLICRYFKYDWNKIENAEFSELIQIGGIGDIMAESFIRFFSDEKKKVIVQDVLNELELEEVQLSQSEQIFENLNFVITGSVEQFKNRDELKDVIEEKGGKVTGAVTSKTNYLINNDNMSNSSKNKKAKELNISIITEAQFLEWLNNGVRPE | Function: DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Catalytic Activity: NAD(+) + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + beta-nicotinamide D-nucleotide.
Sequence Mass (Da): 74138
Sequence Length: 657
EC: 6.5.1.2
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O31504 | MALIDLEDKIAEIVNREDHSDFLYELLGVYDVPRATITRLKKGNQNLTKRVGEVHLKNKVWFKEAKKGKLFDALIDIEQQVEYLSAKPRYLLVTDYDGVLAKDTKTLEALDVKFEELPQYFDFFLAWKGIEKVEFEKENPADIKAAERFARIYDVLRKENNIIETNRGLDLFLIRLLFCFFAEDTDIFKRNSFTNLIKTLTEEDGSNLNKLFADLFIVLDKNERDDVPSYLKEFPYVNGQLFTEPHTELEFSAKSRKLIIECGELLNWAKINPDIFGSMIQAVASEESRSYLGMHYTSVPNIMKVIKPLFLDKLNQSFLDAYDDYTKLENLLTRIGKIKFFDPACGSGNFLIITYKELRRMEINIIKRLQELLGEYLYVPSVTLSQFYGIEIEDFAHDVAKLSLWIAEHQMNEELKNEVHNAVRPTLPLHTAGDIRCANAIRVEWTEVCPAQGSEEVYVFGNPPYLGSKKQNKEHKSDMLSIFGKVKNGKMLDYISAWFYFGAKYASTTNAKVAFVSTNSVTQGEQVSILWNELFKFGIQINFAYKSFKWANNAKNNAAVIVVIVGFGPLDTKVNKYLFVDETKKLVSNISPYLTDGENILVSSRTKPISDLPKLHFGNMPNDGGGLLFTITEYTDAINKYPELVPYFKKFIGSVEFINGGLRYCLWLNEAKYEKIKSNPLIQERISISKNHREKSTDKGTNKLALTPWKFRDTHETTNYSIVVPSVSSENRFYIPMGLAGADTILSNLIYVIYDAEIYLLGILMSRMHMTWVKAVAGRLKTDYRYSAGLCYNTFPIPELSTRRKNEIEEAILEILDLREEQGGTLAELYNPSTMPIELKVAHEKLDGIVERAYRQKQFESDEERLEVLLKLYQEMTER | Function: Recognizes the double-stranded sequence 5'-GACGAG-3' and methylates A-5, yielding m6A. m6A methylation functions as a transcriptional modifier, promoting transcription of a number of genes (at least scpA, hbs, rnhC, yumC and zapA). One studied mechanism is via transcriptional repressor ScoC (also called hpr) which binds to non-methylated scpA promoter; when the m6A target is methylated ScoC no longer binds and scpA transcription is up-regulated. Other mechanisms for gene expression regulation probably exist. Binds DNA with and without the target sequence. Although it resembles a restriction-modification system, it does not have detectable endonuclease activity under tested conditions . A gamma subtype methylase .
Catalytic Activity: a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 101158
Sequence Length: 879
EC: 2.1.1.72
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P04531 | MKLIFLSGVKRSGKDTTADFIMSNYSAVKYQLAGPIKDALAYAWGVFAANTDYPCLTRKEFEGIDYDRETNLNLTKLEVITIMEQAFCYLNGKSPIKGVFVFDDEGKESVNFVAFNKITDVINNIEDQWSVRRLMQALGTDLIVNNFDRMYWVKLFALDYLDKFNSGYDYYIVPDTRQDHEMDAARAMGATVIHVVRPGQKSNDTHITEAGLPIRDGDLVITNDGSLEELFSKIKNTLKVL | Function: Phosphorylates dGMP, dTMP and 5-hydroxymethyl-dCMP while excluding dCMP and dAMP. The phosphorylation of 5-hydroxymethyl-dCMP represents the first step in the replacement of cytosine by hydroxymethylcytosine in new viral DNA genomes.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-phosphate + ATP = a 2'-deoxyribonucleoside 5'-diphosphate + ADP
Sequence Mass (Da): 27329
Sequence Length: 241
EC: 2.7.4.13
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Q6QGP4 | MSVLVGLHGEAGSGKDTVAKLIIDWCNDTYPTCLSRRYSFAKPVYELASVILGVTPEFLGERRGKEIDQWFTVTQSQLERARDVWFKYGIDKFEDFSYVWPIFEEKYLNPQQLISENKEDGLYSLFISPRKMLQLVGTELGRQLVHERIWLIILEQSIAKDDPDVAVITDVRFPNEGELLRETNHLDMDSLLVNVVPAEQKFTIKSDHPSESGIPAKYITHELVNKFDGINNLKLEVYNFCDLELEPLVG | Function: Allows the synthesis of deoxyribonucleoside triphosphates necessary for the rapid viral DNA replication . Phosphorylates all four dNMPs .
Catalytic Activity: a 2'-deoxyribonucleoside 5'-phosphate + ATP = a 2'-deoxyribonucleoside 5'-diphosphate + ADP
Sequence Mass (Da): 28701
Sequence Length: 250
EC: 2.7.4.13
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Q9UPQ8 | MTRECPSPAPGPGAPLSGSVLAEAAVVFAVVLSIHATVWDRYSWCAVALAVQAFYVQYKWDRLLQQGSAVFQFRMSANSGLLPASMVMPLLGLVMKERCQTAGNPFFERFGIVVAATGMAVALFSSVLALGITRPVPTNTCVILGLAGGVIIYIMKHSLSVGEVIEVLEVLLIFVYLNMILLYLLPRCFTPGEALLVLGGISFVLNQLIKRSLTLVESQGDPVDFFLLVVVVGMVLMGIFFSTLFVFMDSGTWASSIFFHLMTCVLSLGVVLPWLHRLIRRNPLLWLLQFLFQTDTRIYLLAYWSLLATLACLVVLYQNAKRSSSESKKHQAPTIARKYFHLIVVATYIPGIIFDRPLLYVAATVCLAVFIFLEYVRYFRIKPLGHTLRSFLSLFLDERDSGPLILTHIYLLLGMSLPIWLIPRPCTQKGSLGGARALVPYAGVLAVGVGDTVASIFGSTMGEIRWPGTKKTFEGTMTSIFAQIISVALILIFDSGVDLNYSYAWILGSISTVSLLEAYTTQIDNLLLPLYLLILLMA | Function: Catalyzes CTP-mediated phosphorylation of dolichol, the terminal step in de novo dolichyl monophosphate (Dol-P) biosynthesis . Dol-P is a lipid carrier essential for the synthesis of N-linked and O-linked oligosaccharides and for GPI anchors .
Catalytic Activity: CTP + di-trans,poly-cis-dolichol = a dolichyl phosphate + CDP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59268
Sequence Length: 538
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.7.1.108
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P64598 | MKALSPIAVLISALLLQGCVAAAVVGTAAVGTKAATDPRSVGTQVDDGTLEVRVNSALSKDEQIKKEARINVTAYQGKVLLVGQSPNAELSARAKQIAMGVDGANEVYNEIRQGQPIGLGEASNDTWITTKVRSQLLTSDLVKSSNVKVTTENGEVFLMGLVTEREAKAAADIASRVSGVKRVTTAFTFIK | Function: Plays an important role in maintaining outer membrane integrity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 20028
Sequence Length: 191
Subcellular Location: Cell outer membrane
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P45301 | MTLSPLKKLAILLGATIFLQGCVAAVIGGGAVAAKVATDPRTTGTQIDDETLEFKVENAVEKDAQIKAEGRVNAVSYNGRVLLIGQVPNSDVKDTATALAKGVEGVNEVYNELTVSPKISFAQISKDSWLTTQVKSKMFVDGRVKATDVKVISENGEVFLLGNVTQSQANAAADIASKISGVKKVIKVFKYLD | Function: Plays an important role in maintaining outer membrane integrity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 20414
Sequence Length: 193
Subcellular Location: Cell outer membrane
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Q7CPQ6 | MKAFSPLAVLISALLLQGCVAAAVVGTAAVGTKAATDPRSVGTQVDDGTLELRVSSALSKDEQIKKETRINVTAYQGKVLLVGQSPNSELSARAKQIAMGVEGTTEVYNEIRQGQPIGLGTASNDTWITTKVRSQLLTSDQVKSSNVKVTTENGEVFLLGLVTEREGKAAADIASRVSGVKRVTTAFTYIK | Function: Plays an important role in maintaining outer membrane integrity . Contributes to virulence .
Location Topology: Lipid-anchor
Sequence Mass (Da): 20097
Sequence Length: 191
Subcellular Location: Cell outer membrane
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A0A0N9HTA1 | MDTRADAEIKAMELIGIGVLPLAMKAIIELNVLEILSKAGPDTQLTAAQIVTDIPTTNPNAGFQLDRILRLLASHSVLSSSITKSGERVYGLTPMCKYFLPDQDGVSLAPMVVTIHDKVLLQSWHYLKDSVLKQGSLPFTEAFGMSPFEYSVSDTRFNKVFNAGMFDHSTLCMRDVLQRYKGFQGLGELVDVGGGTGGSLKMILSQYPNLKGINFDLPHVVADAPSFPGVKHIGGDMFESVPSGDAIFMKWILHDWDDGRCLTLLKNCWNALPEHGKVIIVEWILPSDAATDPTSRRVFTADLMMLAFSEGGKERTLGDYGALAKEAGFTTVKDFPCANGISVIEFHKK | Function: O-methyltransferase involved in the biosynthesis of etoposide, a chemotherapeutic compound of the topoisomerase inhibitor family . Catalyzes the methylation of (-)-5'-demethylyatein to produce (-)-yatein .
Catalytic Activity: (-)-5'-demethylyatein + S-adenosyl-L-methionine = (-)-yatein + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 38175
Sequence Length: 349
Pathway: Aromatic compound metabolism; phenylpropanoid biosynthesis.
EC: 2.1.1.330
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