ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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Q8VXV4 | MPGHRSKSEKKDADKQLRRDPYEVLGVLRNSTDQEIKSAYRKLALKYHPDKTANDPVAADMFKEVTFSYNILSDPEKRRQFDSAGFEAVEAESQELELDLSSLGAVNTVFAALFSKLGVPIKTSVSATILEEALNGRVSVDPLVLGQAVSKKVEKQCAHFYAVTISEEEVSAGLVCRVESSSKSKFKLLYFDQEANSGLSLALQEDSKRTGKITSAGMYFLGFPVYRLDHTINSMAQAKDPETAFFKKLDGFQQCEVTELKAGTHVFAVYGDNFFKNVSYTIQVLCAAAFTQEKEDLRSVEAQILTKRAELAKFETEYREVLVQFTDMTSRYAQEMQSIDELLKQRNEIHSAYTTIPLMKRSSSKNRMRKSSFKKAAAKAPAPTEQEEEEEEEEEEEEESSRQKNKKPSTCDKSETLKKKSKWFNLHLKLDKKKPC | Function: Plays a continuous role in plant development probably in the structural organization of compartments (By similarity). Seems to not be involved in gravitropism signaling pathway.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 49305
Sequence Length: 436
Subcellular Location: Membrane
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Q9LZK5 | MAIRWSELCIVLFALSYAICVLAGKSYYDVLQVPKGASDEQIKRAYRKLALKYHPDKNQGNEEATRKFAEINNAYEVLSDEEKREIYNKYGEEGLKQFSANGGRGGGGGGMNMQDIFSSFFGGGSMEEEEKVVKGDDVIVELEATLEDLYMGGSMKVWREKNVIKPAPGKRKCNCRNEVYHRQIGPGMFQQMTEQVCDKCPNVKYEREGYFVTVDIEKGMKDGEEVSFYEDGEPILDGDPGDLKFRIRTAPHARFRRDGNDLHMNVNITLVEALVGFEKSFKHLDDHEVDISSKGITKPKEVKKFKGEGMPLHYSTKKGNLFVTFEVLFPSSLTDDQKKKIKEVFA | Function: Regulates protein folding in the endoplasmic reticulum (ER) lumen. Forms a complex in the ER with SDF2 and MED37A/BIP1 which is required for the proper accumulation and function of the surface-exposed leucine-rich repeat receptor kinases EFR involved in pathogen-associated molecular pattern (PAMP) triggered immunity.
PTM: N-glycosylated.
Sequence Mass (Da): 39200
Sequence Length: 346
Subcellular Location: Endoplasmic reticulum lumen
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Q17438 | MTADANKSESLLCMDKAREAIKSGDTDKARRMLLKAKKLDPGQNIEFLTKKIDDMTNNTSSSSQTSSSRASEERSYAHDDHYDDPNLRNRKARSPVKKNGKTEPEPKQRSASRTPKLGVDYTSEQKELVERIRHCKDYYEILKIDKKASDDDIRKEYRKLALKLHPDKCRAPHATEAFKALGNAYAVLSDTDKRRQYDQYGAEAANSHTPTTRRRGGGHGAFFEHDYAHGFEAEFTPEEIFNMFFGGGFPTEQVRRRARYAQQQQYHHYEQQQSPYGPLLQLLPLIAIMVIGLLAQLMVGEPAYSLHQTSKFTIKRLTADLRVPYFVRTDFETSYRGRIRQVEQQVEDDYIQNLRMNCYKEQNLKETKLYRARWMRDEAMMRDAERTPLPSCIRLNEIYSH | Function: Acts as a co-chaperone with Hsp70 required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity). Acts by determining Hsp70's ATPase and polypeptide-binding activities (By similarity). Can also act as a chaperone that promotes maturation of potassium channel unc-103 by stabilizing nascent channel subunits and assembling them into tetramers .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 46582
Sequence Length: 401
Subcellular Location: Endoplasmic reticulum membrane
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J9VKM5 | MKGFLLVALPVLFLSLSTQVFGEPSIPSAAQIVQNANRLLAEGSYSAAARAYGEAIELDPTGYANYYKRATAYLSMGRHNAALDDFEQILRINPGFVQAHYQRAKILAKEGDFAKAQYELKAYVRTKSDSEAEELSHLLTVGEAAEKSALQAFEKGKWQVCVEHSTKALEVGPNSEKLRRLRVNCATELGDINMVYGDLSRLASLDPSTTYLPLQLSNIAYFIRASSQAAAHIKQCLHFDPDSKPCKAVHKTIRSLEKDAARVRNFIESGTYRQAIKILDGDDGLLVRFEKALDDATKPKDGLPPYLAPQFHPKKNSQMRLDLYALACKASVMANDFGEKGAHWCEETMSMNEENVDSWISRGERLLRVEKWEEAMRAVEKAFELSGRSQDILPRVQKAQRLLKQSKQKDYYKVLGVPRDADERAIKKAFRKAAKLAHPDVGGSEEKMAALNEAYEVLSNTELRQRYDNGDDPNDPTGGQQHNPFAHHGGGMPFQFFQQGGGFQGFHQGFPGGGQKMHFQWN | Function: Endoplasmic reticulum co-chaperone crucial for survival and virulence factor production at elevated temperatures representative of febrile patients during infection . Contributes to virulence in a mouse model of cryptococcosis . With chaperone CNE1, coordinately maintains ER homeostasis and contributes to maintenance of cell wall architecture .
Sequence Mass (Da): 58281
Sequence Length: 522
Domain: The TPR repeats mediate interaction with unfolded polypeptides and the J-domain is essential to stimulate the ATPase activity of the chaperone and to increase its substrate affinity during the folding cycle.
Subcellular Location: Endoplasmic reticulum lumen
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A0A0D2XVZ5 | MHLNLAGLAVAATAFLATASALSPQDIPADLPVSNLLTKAQTHLSRGETNEALVYYDAAIARDPTNYLSLFKRATAYLSLGRTSQATEDFNKVLSLKPGFEGAHLQLARLRAKAGDWDAAKAQYGLAGKAPKSAEFVELEEAKLAAHLADMASKGGKWEECVSHAGTAIVVASRSPHLRELRAHCRFELGDVELALSDLQHVLHMKPGDTSPHIVISATSFYALGDLENGIGQVKKCLQSDPDSKICKKLHKQEKKVEKAYKKIQGQLSRGQPTTAGRALVGTADDSGLVPDVRKQVEELKKNKSIPKTARIQLLENLIEMTCQAYTESSHKEAAKYCDESLQLNPDSFWGLLHKGKAQLKSELYDAAIATLEKAAEIRPDQKEKVNPILNKAHIALKRSKTKDYYKVLGVENDADERQIKSAYRKQSKIFHPDKAAKQGIPKEEAEKKMASINEAYEVLSDPELRARFDRGDDPNSQERPNPFQGQGNPFGGGHPFMFQQGGGGGGPNIKFQFGGQPFGF | Function: Endoplasmic reticulum co-chaperone required for the of virulence factors such as PG1, the major endopolygalacturonase produced during the infection of tomato plants.
Sequence Mass (Da): 56992
Sequence Length: 521
Domain: The TPR repeats mediate interaction with unfolded polypeptides and the J-domain is essential to stimulate the ATPase activity of the chaperone and to increase its substrate affinity during the folding cycle.
Subcellular Location: Endoplasmic reticulum lumen
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A0A0D1E2P6 | MKATLLPSLLALSLTLCLALGLSSSGVLVRADAFASSQPPVVSDPVLASQHLTQANVALQSGRYQDALSAFDLALQADPSSWLTYYRRATAQLSLGRTSAALQDFQSLLKLNPKFDKAYLQQAKVYLKEGDCDKAKQALKTYDSIRAEKGAANSSPAEANSVRSKLTLVETSIKSLGQLVKELDKAQKADKKGKAKELDSTKVDHCIHLAGEVLKISPSHLETRLVRARCQTMKGRIEDAMADWTRAVHLTPSPFLLRRLSVLSYFVVSEPGSQSRDAGLQHLKACLHSDPDNKSCAKMHRKIKALEKSLKKARNFYNSQSYRAVLSALKGGKVGRATVVDDIKEAIRSATEVQSGDEEPLIPSTYKGDPVQESGLLLELHTMYCKAYTELNDMDKAMPYCELVLAKDPDNVEATLARAELALQREDYDQAVRDLTKAFDASGRTDRAIHQKLQTAQKRLKLSQSKDYYKVLGVKRTDSLATIKKAYRKMARENHPDKGGSQEKMAQINEAWGVLGDEELRKKYDQGDDPNDPMGGQQGGYGNPFAQGGHPFDMFFQQQAGFGGFPGGGFPGGQQFHFKMG | Function: Endoplasmic reticulum (ER) protein that functions as a co-chaperone for BIP1 during ER stress . Might be specifically involved in the refolding of N-glycosylated proteins .
Sequence Mass (Da): 63837
Sequence Length: 581
Domain: The TPR repeats mediate interaction with unfolded polypeptides and the J-domain is essential to stimulate the ATPase activity of the chaperone and to increase its substrate affinity during the folding cycle.
Subcellular Location: Endoplasmic reticulum lumen
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Q0WT48 | MAASEENSALFPIFILTIMAIPLVPYTMVKLSGALSKKQRTIHCQCLECDRSGKYKRSLFKKISNFSTWSNLTLVLLWVVMIFLIYYTKNMSREAQVFDPFSILGLEPGVTDSEIKKAYRRLSIQYHPDKNPDPEANKYFVEFISKAYQALTDSVSRENFEKYGHPDGRQGFQMGIALPQFLLDIDGASGGILLLWIVGVCILLPLVIAVIYLSRSSKYTGNYVMHQTLSAYYYLMKPSLAPSKVMEVFTKAAEYMEIPVRRTDDEPLQKLFMSVRSELNLDLKNMKQEQAKFWKQHPAIVKTELLIQAQLTRESGVLSPALQGDFRRVLELAPRLLEELLKMAVIPRTAQGHGWLRPAVGVVELSQCIVQAVPLSARKSSGVSSEGISPFLQLPHFSDAVVKKIARKKVKSFQDLQEMRLEDRSELLTQVAGLSATDVEDIEKVLEMMPSITVDITCETEGEEGIQEGDIVTLQAWVTLKRPNGLVGALPHAPYFPFHKEENYWVLLADSVSNNVWFSQKVSFLDEGGAITAASKAISESMEGSGAGVKETNDAVREAIEKVKGGSRLVMGKLQAPAEGTYNLTCFCLCDTWIGCDKKQALKVKVLKRTRAGTRGLVSDEGAIAEEGMEEEDEIEEEDYDDDYESEYSEDEDEKKDMDEKRGSKKANGSVKQKKESSSEESGSEEE | Function: Required for integral membrane and secreted preprotein translocation across the endoplasmic reticulum membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76904
Sequence Length: 687
Subcellular Location: Endoplasmic reticulum membrane
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F4JIN3 | MAESEENSVLFPIFILTMMAIPLVPYTFVKLSRAFSKKQRSIHCQCLECDRSGKYKRSISQSISSFTSCSNLTVVLLWIVMIFLIYHTKNMSRESQLFEPFGILGLEPGASDSEIKKAYRRLSIQYHPDKNPDPEANKYFVESIAKAYQALTDPLSRENFEKYGHPDGRQGYTMGIALPQFILNMNGESGGILLLCTVGLCILLPLVIASIYLWRSSKYTGNHVKLQTRQAYFELLQPSLTPSKVMDIFIRAAEYAEISVRKSDDESLQKLFMSVKSELNLDPKKLKQEEAKFWKKHPATIKTELLIQKQLTRESSVLSPTLQRDFRHVLEFAPRLLEDLIKMAVIPRNEQGRGWLRPALGVMELSQCIVQAVPLSARKSSSEDIAPFLQLPHFNESIAKSIALQVKSFQKFQELSLAERSKLLREVVSLSETDVQDIEKVLEMIPSLKINVTCKTEGEEGIQEGDIMTVQAWITLKRPNGLIGAIPHSPYFPFHKEENFWVLLADSNHVWFFQKVKFMDEAGAIAAASNTITETMEPLGASVKETNDAVKEAVEKVKSGSRLVMGRLLAPGEGTYNLTCFCLSDTWIGCDQKTSLKVEVLKRTRDVEGENAEEGLEEEDDEIEEEDYESEYSEDEEDKKRGSKKKVNKESSSEESGSDEE | Function: Required for integral membrane and secreted preprotein translocation across the endoplasmic reticulum membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 74825
Sequence Length: 661
Subcellular Location: Endoplasmic reticulum membrane
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D4GYZ4 | MQFAEFAARAAEIEAEPADLAVVSLLSDLFSDAGDDLPTVARFVQGRVFPAWDSTTLDIGPRLCHEAIARAAGPNVSADDVEDRLADRGEIGAVAASYDFGGQRGLAAFGSGEQDGLTVAEVDSELRALAAASGSGSEETKLKTLYGLFNRTDPDEARFLARLVLSEMRIGVGEGTVRDAVAEAFLVAPADAAAIRDDDADAETEAAARERRNEAIAAVARALQVSNDYGMVAGLARDEGEAGLDGVRLEVGRPVQAMLAQAGTAADALGEWGTAAVETKFDGARVQVHRDADGEVSLFSRNMEDVTDALPEVVEFVAGAVDDPVILDGEVVAMDDGGEPLPFQEILRRFRRKHDVDRMREEVRVELRAFDCLHAAGDDLLADPLAARHDRLTALLGDDSPAVSDLLLSDDPDEIAAYEADALDAGHEGIMLKNPDAPYSPGDRGKNWLKRKPDVETLDLVVTGAEWGEGRRAEFLGTFLLSARVEAESGDDAFETIGKVATGITDEELAELTDLLEPEIEREAGKEVDIRPSVVFEVGYEEIQTSPTYSSGYALRFPRFVTVREDKTAETADSLDRVERLADSQ | Function: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
Sequence Mass (Da): 62738
Sequence Length: 585
EC: 6.5.1.1
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A2BJX6 | MSMPFSVLAETFEKLERVTARTQMLLYLVELFKKTPPEIIDKVVYFIQGKLWPDWKGLPELGIGEKMLIKAASIALHVSEKQIEQLVKKLGDTGKAIEMIKREKQQKQKAVGLLAFMQKPSGGESTLTVEKVYDTLARIALVQGEGSRDIKLKLLAGLLAEASPREAKYIARFVEGRLRLGVGDATIMEALAVVYGGSAAMRSVVERAYNLRADLGMVAKILATQGIDALKNIKPEVGVPIRPMLAERLNDPVEIIKKLGGRALVEYKYDGERAQIHKKGDKIWIFSRRLENITHMYPDVVEMAKKGIKAEEAIVEGEIVAIDPETGEFRPFQVLMHRRRKKDVHAVLSEIPVAVFLFDTLYVNGEDLTLKPLPARHEVLEKIIEQSDTWRIAEGIVTSDPQELESFFLKAIEDGAEGVMAKAIHDRSIYQAGARGWLWIKYKRDYKSEMSDTVDLVVIGAFYGKGRRGGKFGALLMAAYDPDTDTFKSVCKVGSGFTDEDLERLDDMLKPYISDKKPARVDSQMKPDVWVEPTLVAEIIGAELTLSPIHTCCYGWVKSGAGISIRFPRFIRWRPDKGPEDATTTKELYEMYKRQLRRIKEEEAPTGV | Function: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair. Can use ATP, ADP and GTP, but not CTP, TTP or NAD(+).
Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
Sequence Mass (Da): 68330
Sequence Length: 608
EC: 6.5.1.7
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A6WG40 | MLLADVVATSTAVAATRSRTAKVAAIAGLLRGLDPADAELTAVVAAYLGGSLRQRRTGLGGRSLSGLPAPAGEASLEVAEVDRRFEEVAALSGPGSAGRRAAAVADLFARATGEEQRWLRGVVAGELRQGALDALVQDAAAAVAGVPGPDVRRAAMLAGSTVQAVVAALRGGAAELAGFGLHVGRPLLPMLAASTTSVAEAVAGFAGPVAVDTKLDGIRIQVHRGPEGVRIATRTLEDITARLPEVVEVVRELPARAFVLDGEALVLDGSGRPKAFQDTASRTAQASGDAVVPYFFDVLHLDGADLLDVALRERLAALDGFVPPRWRTPRLVTADPAAAAEFAAQALAGGHEGVVVKDLDSPYAAGRRGGAWVKVKPVHTLDLVVLAVERGSGRRAGWLSNVHLGARDPATGGFVMLGKTFKGMTDETLAWQTARFRELQTGEDGYVVTVRPEQVVEVAFDGLQRSTRYPGGVALRFARVVRYREDKTAAEADTLETVLALAR | Function: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
Sequence Mass (Da): 52420
Sequence Length: 503
EC: 6.5.1.1
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Q1II25 | MQLLAQTCEAIAATSKKTEKIAIVATYLQSRTVPEAALSTLFLSGRTFAAHEERTLQVGGSILWRVVGELSGASEAKMTAAYKRHGDLGDATLGVLRGVAPEESTLTLKEVDYMFQQIAAVSGPAAKSRLIVTLLARATAPEAKYLVKFITGELRIGLKESQVEEAIAKAYGRELAEVRRANMLVGDIGETLVLAAHDKLATARMRLFHPMGFMLATPAESANEAFAEFEHAIVEDKYDGIRAQAHISRDKVRIFSRTLDDITDSFPELIPALKAIEHEVILDGEILAWRCGQALAFSELQKRLGRKNVSAAMQREVPVSYVTFDLLYAKGQLVIDRPLQERAAMLDGIFSEGAPRLVNVDPHGQASLMFAEVTPEQRVLRAPQARADSPEELDRLFAAAQERGNEGLMIKDIHSAYAVGRRGKSWLKLKRELAMLDVVVTAVELGHGKRAGILSDYTFAVRGGEELLNIGKAYSGLTDKEIAEMDEWFRAHTLVDHGFVREVEPKIVIEVAFNAVMKSDRHASGFALRFPRILRIRDDKGGEEIDTLERAEEIYRSQFHQRTRRIHRGDTKAQSS | Function: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
Sequence Mass (Da): 63771
Sequence Length: 576
EC: 6.5.1.1
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Q0W0X1 | MLFKELVSLYESLRSTSSRLEKTAMIAAFLQQAPVDELPVIVTFLTGRIFPEWDQRKIGIASQSMIKIISTITHNPEDAVVESYKKTGHLGVTAEEMFQKRRQVTFFEPEDITVKEVAETFYEIARSSGAGSSAKKQKILIGLLHRATTPKEAHYIVSLTIEYVLSGAKEGVMEDAIGQAFGATLDQVRRAHMLTSDLGETARIAKTEGAAGLEAITIRPMRPVRPMLAQNVSSIREALDTMGGVAEFEMKYDGARLQIHKVGKDVKLYSRRLEDLTDALPEIVGYVRESVKSDTAILDSECIAIDKDTGRPIPFQNILTRLRRIHKVEETQKQFPLILRPFDVLFNQGQSTIDLPLRERRKILEEIVIATDSVIQPARALVTDQEEKAQELFEESVKSGNEGLMGKDLNATYTPGVRGKKMVKIKSVLDTLDLAIVSAEWGHGRKAGWLTSFEVAALDEETGDYVILGRVASGFSDEQLIEMTEKLKPLITGEHGRIVDVRPEIIVEVKFEEIQKSPIYSSGYALRFPRLVRVRDDLSPEEVNSFTRVMNIYNVQQRYSISENGLRK | Function: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
Sequence Mass (Da): 63701
Sequence Length: 568
EC: 6.5.1.1
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Q2FTH4 | MIFLEFAELCSRLEKISGRLETISILAETISSLSDDDLPHFCRLILGKPFPEWSGKKLGVGPNLLYEAVAYVTGRKREEVIDRLSRVGDAGAAVEELLSQKSQTSFFTVELTLADIMAALIEISGMEGGRSQKEKVRVIQRILSSASPLEGHYITAILLEDFRIGVGEGNLRDAIAQAFSVDPNLVEYANQVRNDMGEVAVLARKGEEALRSVRLVPFHPVRMMLARQGTISGVLKEGDPVAVEFKYDGARFQFHKQNKTCRMYSRRLEEVTNAMPDVVALLDEALPDDIIVDGEVIAVQGGHPMPFQTVLRRFRRKHNVAEAADAITMIPNLFDILYYNQEMLIDLPFRERRNILTQVASRYVTPQLVSDDETEIEAYYHTALDAGHEGVMLKLQGSRYTPGVRGKDWVKIKPEADTLDLVVTGAEWGEGKRAHVFGSFLLSVRDDDRLVPISRVATGFSDEQLIWLFDTLQDDIIRKDGKMVYFEPRLVFEIGYSEIQKSPNYEGGYALRFPRFIEVREDKDLKEANTAEDVEERYIQTHSSLNT | Function: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
Sequence Mass (Da): 61698
Sequence Length: 547
EC: 6.5.1.1
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Q57635 | MLWRDVCEIFNKIEKTTKRLEKRDYFIKLIDMVKEKGKPEDLKKICYMAIGRVYPEYDERELGIGEKLLINAVTSIGIKKDELLEKIKETGDIGLAIEQLKSKIKQASLFFQPLTVDEVYETLKRVGEIEGEGSQKKKLRLISSLFLRASPIECRYLARLILEDMRIGMNVPTILDALSVYFNVPKEKLEKIYAITNDIGLLAEKLLMGDLESEELKLKLFRPIKPMLAQLTPSIEEALLEMGRAQFETKYDGARVQIHKDGNKVKIYSRRLEDVTNALPEIVEAVKNINVDKLIVEGECVAIDKQTGKPRPFQDILRRFRRKYDIGKMMKEINLRVYLFDILYKDGVSFIDEEFEKRRKVLEEIVGYENDWRTERKRIEKELKSDKIIDISYKLVTNDAKEAREFYNWSLSIGHEGVMIKNLKAPYTPGSRVRTMYKFKPTLESLDVVITKAKRGMGKRKDWYGSFEICVRDEEGNLYPIGHVGTGLTEADLEFLKEEIDKIIIRDLGEEVEVEPKIVIEVAYEEIQKSDKYPCGYALRFPRVVRFRFDKGVNEINTIEDVERIYEIQRGRK | Function: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
Sequence Mass (Da): 66790
Sequence Length: 573
EC: 6.5.1.1
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Q8TWN3 | MYYSSLAEAFERLERISSRKAKISLIAQFLRQCPEDVVDTVALFLANQVFPGWDPRDLGIGSKLMRKVIATATGSTDSEVTELFKRLGDLGLTAEELLKRRKTSTLLDSRPLMVGEVRETFEKIAEVEGEGAVKRKMRLMMGLLARAKPKEARYLVRQALSELRTGVRESTVEEAIAQAFGVSRKLVERAHMLSNDLGLVAKVAMTKGEEGLREIDLRPMRPIKPMLAQAARNVKEALAEVGGKGAVEIKLDGARVQVHSDGEEVRVYTRRIEDVTHALPDIVEAVKDCVDADEFILEGEAVAINPETGKPRPFQELLHRIKRKYDIEEVRKEIPVELHLFDCLYVDGESLVDTPFRERRRRLEEIVREREGEVMLVEQVITDDPKEAAEMFHRALEMGHEGVMVKDLDANYTPGVRGKKMLKVKPVLETLDCVVIGGIWGKGKRKGLIGSYLLAVWDENKENLLEVGKVGTGMDDETLERLTKMFEDLIVEESGREVRFKPEVVFEVEFEDIQKSPKYSSGFALRFPRLVRVRDDLGPEDADTIEKVRRIYEEVLQKH | Function: DNA ligase that seals nicks in double-stranded DNA during DNA replication, DNA recombination and DNA repair.
Catalytic Activity: ATP + (deoxyribonucleotide)n-3'-hydroxyl + 5'-phospho-(deoxyribonucleotide)m = (deoxyribonucleotide)n+m + AMP + diphosphate.
Sequence Mass (Da): 63337
Sequence Length: 559
EC: 6.5.1.1
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Q65MR2 | MEKEAAKRRVEQLHALINKYNYEYHTLDDPSVPDSEYDKLMKELIALEEEHPDLKTPDSPSQRVGGAVLDAFQKVQHKTPMLSLGNAFNEEDLRDFDRRVRQAVGDVEYNVEFKIDGLAVSLRYENGVFVRGATRGDGTTGEDITENLKTIRNIPLRMKRDLSIEVRGEAFMPKRSFELLNKARIERDEEPFANPRNAAAGSLRQLDPKIAAKRNLDIFVYSIAELDEMGVETQSQGLDFLDELGFKTNHERKKCSTIEEVIEIVEELKTKRADLPYEIDGIVIKVDSLDQQEELGFTAKSPRWAIAYKFPAEEVVTTLLDIELSVGRTGAVTPTAILEPVKVAGTTVQRASLHNEDLIKEKDIRLLDKVVVKKAGDIIPEVVNVLVEQRTGKEKEFNMPKECPECGSELVRIEGEVALRCINPECPAQIREGLIHFVSRNAMNIDGLGERVITQLFREDLVHNVADLYKLTREQLINLERMGEKSTDNLLNSIEKSKKNSLERLLFGLGIRFIGAKAAKTLAMHFETLDKLKKATKEELIEVDEIGDKMADALVTYFEKEEILKLLDELEELGVNTVYKGPKKAAAEASDSYFAGKTIVLTGKLSEMSRNDAKAEIEALGGKITGSVSKKTDLVIAGEAAGSKLAKAEDLNIEVWDEARLISELKK | 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): 74782
Sequence Length: 667
EC: 6.5.1.2
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O31498 | MDKETAKQRAEELRRTINKYSYEYYTLDEPSVPDAEYDRLMQELIAIEEEHPDLRTPDSPTQRVGGAVLEAFQKVTHGTPMLSLGNAFNADDLRDFDRRVRQSVGDDVAYNVELKIDGLAVSLRYEDGYFVRGATRGDGTTGEDITENLKTIRNIPLKMNRELSIEVRGEAYMPKRSFEALNEERIKNEEEPFANPRNAAAGSLRQLDPKIAAKRNLDIFVYSIAELDEMGVETQSQGLDFLDELGFKTNQERKKCGSIEEVITLIDELQAKRADLPYEIDGIVIKVDSLDQQEELGFTAKSPRWAIAYKFPAEEVVTKLLDIELNVGRTGVITPTAILEPVKVAGTTVSRASLHNEDLIKEKDIRILDKVVVKKAGDIIPEVVNVLVDQRTGEEKEFSMPTECPECGSELVRIEGEVALRCINPECPAQIREGLIHFVSRNAMNIDGLGERVITQLFEENLVRNVADLYKLTKERVIQLERMGEKSTENLISSIQKSKENSLERLLFGLGIRFIGSKAAKTLAMHFESLENLKKASKEELLAVDEIGEKMADAVITYFHKEEMLELLNELQELGVNTLYKGPKKVKAEDSDSYFAGKTIVLTGKLEELSRNEAKAQIEALGGKLTGSVSKNTDLVIAGEAAGSKLTKAQELNIEVWNEEQLMGELKK | 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): 74876
Sequence Length: 668
EC: 6.5.1.2
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Q8A9C1 | MDIKEKIEELRAELHRHNYNYYVLNAPEISDKEFDDKMRELQDLELAHPEYKDENSPTMRVGSDINKNFTQVAHKYPMLSLANTYSEGEVTDFYERVRKALNEDFEICCEMKYDGTSISLTYEDGKLVRAVTRGDGEKGDDVTDNVKTIRSIPLVLHGDNYPSSFEIRGEILMPWEVFEELNREKEAREEPLFANPRNAASGTLKLQNSSIVASRKLDAYLYYLLGDNLPCDGHYENLQEAAKWGFKISDLTRKCQTLEEVFEFINYWDVERKNLPVATDGIVLKVNSLRQQKNLGFTAKSPRWAIAYKFQAERALTRLNMVTYQVGRTGAVTPVANLDAVQLSGTVVKRASLHNADIIEGLDLHIGDMVYVEKGGEIIPKITGVDKDARSFMLGEKVRFITNCPECGSKLIRYEGEAAHYCPNETACPPQIKGKIEHFISRKAMNIDGLGPETVDMFYRLGLIHNTADLYELKADDIKGLDRMGEKSAENIITGIEQSKTVPFERVIFALGIRFVGETVAKKIAKSFGDIDELRQADLEKLISIDEIGEKIARSILLYFSNESNRELVGRLKEAGLQLYRTEEDMSGYTDKLAGQSIVISGVFTHHSRDEYKDLIEKNGGKNVGSISAKTSFILAGDNMGPAKLEKAKKLGVTILSEDEFLKLIS | 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): 75133
Sequence Length: 666
EC: 6.5.1.2
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Q6FZ81 | MNKDEIKNLTALEAESELEWLAKEIARHDVLYNRDDQPEISDAEYDALRRRNAEIEALFPELIRSDSPSHKIGAPVSEKFEKSVHAQAMLSLDNAFSSEDICEFIVRIRRFLRLPATQILEMTAEPKIDGLSLSLRYEKGRLVCAATRGDGYIGENVTANARTISDIPKVLRGEFPDIIEVRGEVYMRRENFQALNMSQQEKGKFVFANPRNAAAGSLRQLDPRITASRKLHFFAYACGEVSETFAASQMEMMKKLKEYGFFINPLTKSFKTLEEIISYYHDIEECRHSLSYDIDGIVYKVNDLKLQMRLGFVSRSPRWAVAHKFPAEKAMALLEGIDIQVGRTGALTPVARLAPITIGGVVVTNASLHNEDYIKGIGHKGESIREGRDIRVGDTVIVQRAGDVIPQIVDIIAEKRPKGASAFVFPHLCPACGSHAVREVGESVRRCTGGLICPAQAIERIRHFVSRNAFDIEGLGKKQVEFFFHIQDEALCIHTPADIFTLQRRQEKALVRLENMEGFGTVSVRKLYNAINMRRKVPLSRFLFALGIRHIGEVNARRLAHAYQNYTAFETVAMAATMPYDKVGEEGNEAWLELTNIEGIGPQVGEAIIDFYQEAHNREVLAALLREVTPLDEENVMTASSPIAGKTIVFTGTLARMSRDEAKALAERLGAKTSGSLSKKTDLLVAGSAVGSKLAKAQGLGVEVIDEEAWLQLIEGSYI | 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): 80128
Sequence Length: 719
EC: 6.5.1.2
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Q1LU20 | MKQIEQYIEQLRQQLRYWNFLYYAKDAPEVSDVEYDWLMMKLRELERQWPDLKTADSPTQHIGYKAQSKFRKVIHEVPMLSLDHIFNDTSFLAFDRRIRNRLQYGNNYLTYCCELKFDGIAVSLLYKHGKLIRAATRGDGHIGEDVTDNIRTICSIPLQLKDDGHIPRLIEIRGEVIMSEDAFRHLNETAKKNKSKRFANPRNAAAGSLRQVDPSITATRLLSFFCYGVGRIDSKKIPAAHLELLQQFKIWGLPVSNYRRYCVGHQEVLDFYSYVSKVRSKLGFNIDGIVIKVNALVQQQQLGFVARAPRWAIAYKLPANEQLTEIQNIDFQVGRTGIITPVARLKPVYISGAYISNASLHSFAEIKRLGLRIGDTVVIRLAGNIIPQIVNVVVSKRSIKTSPVLYPLYCPVCGSKVKQNNKEKTIICTAGMICSAQLKEALKHFVSRRAMNIYGMGGKIIDQLVDLKIIQNPVDLFRLNQDQLTCLKNMGQKKTKKLLDAIEYAKKTTFARFLYAIGIREIGETKAAYLADYYKHIDALMAADIESLTKIQDIGIIVATNVLNFFHNKHNIAIIEELCSPKIGIKFLSTLEKNNYFSGKNIVFTGTLAFLSREEAIDMLIALGARIRSSVSSKIDLLIAGKNTGFKLTKAKQLQIKIIEEAEFYQILGIR | 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): 76271
Sequence Length: 671
EC: 6.5.1.2
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Q6MRL9 | MPDAFCRDWTSEMGANYSMSKKRHEELKKIISEHDHNYHVLDKPTITDYEYDQLFAELLDIEKNPKGLDLSDSPSQRVGGTVLEGFTKAQHRLPMLSLANSYSPEDIFEFDERVRKFLNTEDPVEYLCELKFDGLSMELIYENGQLVRAITRGDGTVGEDVTHNIKTIKSIPLKLSHKNPPPLLEVRGEVLMFKEDFARLNETQQENGQQTFANPRNAAAGTVRQLDSRIAASRPLRFFGYALGAVEGETFNTQKNIQEYFNDHGIPTVLPYKEDLLVVAKGPEEVVKYYHHIEKVRPKLPFDIDGVVIKVNSLRLQEDLGLVARSPRWATAAKFKPEQAQTTVEDIVVQVGRTGALTPVAIMKPVKVGGVTVTNATLHNQDEITRKDIRIGDTVIIQRAGDVIPEVVEVVNPDKRPADRLPYSIPERCPACDSVAVKAEGEVVTRCVNPLCIAVVKESLKHFVARRAMNIDKVGDRLIETLVDNKLLTRFSDFYRLTKEQILSLERQGDKSADNIIKSIENSKNPTLARFIFALGIRFVGEQTGKHLADHFLTIDKFLEASEEELLQVPEIGAKVAKSIRDWTGNPKLVDEVKAMIELGVKIAGPVRAQEGSLSGMSFLITGTLPVKRDDAKDLIERNGGKILGSVSSKLNYLVVGDDPGSKVEKAQGLGVKIISWEELQAMI | 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): 76371
Sequence Length: 684
EC: 6.5.1.2
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B2IGH4 | MTVQKPIESLSPAQAKREHRRLGEQITEHDRLYYQEDAPRVSDAEYDALRRRYEALETAFPELVSAESLTKKIGAAPAEKFAKIIHKVPMLSLANIFSDEEVGEFVARVRRFLGLGADAPLAISAEPKIDGLSCSLRYEGGYLVQAATRGDGYEGEDVTANVRTIQEIPHQLQGHAPEILEVRGEVYMTHADFAALNERQEAAGKTIFANPRNSAAGSLRQLDPKVTAGRPLHFFAYAWGEASEEPADTQMGMVTAFKAFGLPVNPLMQLCHSAEDLIAHYHDIEARRALLDYDIDGVVYKVNSIALQKRLGFVSRAPRWATAHKFPAEKAVTLLRDIEIQVGRTGALTPVARLEPITVGGVVVSNATLHNEDEIARKDIRIGDMVMIQRAGDVIPQILGPILDKRPQDAQPYEFPQVCPVCGSAAIREIDPKTGTADVVRRCTGGLVCAAQVVERLKHFASRNAFDIEGLGDKQIEQFYHDGLIHTPVDIFTLQERDARSLKKLKDREGYGETSVRNLFQAIEARRHIPVNRFIYALGIRHVGETNARRAARAFGTFDALRAVASRAEEGSEERSELTNVEGFGPVVAEAIFDFFHEQHNQDVLDGLLEQVTPEPMEAVAKESPVAGKTVVFTGALEHMTREEAKAQAERLGAKVAGSVSKKTDLVVAGPGAGSKLAKAAELNIETISEEDWLKLVGE | 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): 76839
Sequence Length: 699
EC: 6.5.1.2
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Q8G830 | MSTNEQLAWDFDDGDVAEVRPDTGIARFAPGSEQWIAALQPTDDDAIRLDRFDVNTMTAEAAARLWARVAAWVESDQIAYYIDDSPVSSDAAYDARMRCLERLEAAFPSLDNPQSPTHRVGGSFSNDFASVRHPSRMMSLDDVFSIEELKDWYDSVIRDLDWPESKPLPMSCEVKIDGLALNLIYRNGVLEQGLTRGDGVTGEDITLNVRTIGSIPANLGGPKEDVPDFVEIRGEVFMRWDDFHTLNNEQEDAGRAPFANPRNAAAGSLRQKDPRITATRRLSFYAHGLGQLTWGPDHPRGTHDVVADQSQAYDLYTKWGVPVSPHNRAVTSFQEILDMIEYYGEHRGDIEHALDGIVVKVDDLGLQRTLGATSRAPRWAIAYKYPPEEVNTELLNITVQVGRTGRVTPVAVLKPVYVAGSTVARTTLHNGFEVKRKGILIGDTVVVRKAGDVIPELVGPVLERRKGREDQLREFVMPEFCPSCGAKLSPAKEGDKDIRCPNVESCPAQLTERVISLASRKAFDIEHLGEQSAIALTNPEENRPDSVATYAPNITEVLVAPGEEPDPYEPVEGLELPAAQKPVLSNESGLFNLTAADLRDVRVWREAAIVEVHETVGANGKKKKVRKRVGGSGLWHQVPAFWTAPTPAKKLTAKQLAERAQGEAAIESAETQGDTASETTGAPTGAEAPLGTMPGFAAASYPEYDVPADAVIVRVDHKTTRTGVTDVPVIIRPGENTRKMFDEMDKARHADLWRVLVALSIRRLGPPTARLIASAMGSLAAIENATIEDLTAIDGVGPEIAESVVNWFAATREPGDWRGATLRAWQAAGVGVDEAETSSLPQTLAGKTVVVTGSLEGYSRDSAKEAIIERGGKAAGSVSKKTDYVVIGANAGSKAAKAEELGIPMLSETQFAQLLATGTI | 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): 99855
Sequence Length: 920
EC: 6.5.1.2
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Q7NMN8 | MSTTVPPEIEEHTRTLRALLHRWGYAYYVLDAPEVSDAIYDQHYRELVDLESRYPELVSPDSPTRRVGERPASAFVSVTHRVPMFSLENAFSQAELEKWGERLLRAIGPGLEFICELKIDGSATALSYEDGVLVRGATRGDGVEGEEITQNLRTIRAIPLKLLGGEVPAVLEVRGEAFIPRDEFERINQERQAAGEKLFANPRNACAGTLRQLDSRVVASRRLGFFAYTAHYGRAESQWEALAELESHGFRVNPHRSLCRDLAEVRTFCEHWENHRHELPYDTDGVVVKVNAFDHQREVGFTSKFPRWAIAFKYPAEEKSTVVEAIAVQVGRTGALTPVAELQPVAVAGTTVSRATLHNQDRIESLDVRVGDTVIIRKAGEIIPEVVRVIGELRPPEAVPYVFPQTCPECGTAVVRAPGEAAVRCPNPRCPALIRGKLGHWCAALEIDGIGDKLIARLVSLGLVHTVADLYELSAEQLAGLERLGARSAAKIVEQLDRSHRQPWSRVLYGLGLRHIGASVSVELARAFASADALARADLAAIASLYGFGEELARSVVEWFAQAENRALLERLKAHGLQLAGGGRAAQSSALAGLTFVITGTLPTLSREECTALIESHGGKVTSSVSSRTSYVVAGEKAGSKLARAQDLKVAVLDEEQLRALIETREMP | 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): 73224
Sequence Length: 668
EC: 6.5.1.2
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A9H0L6 | MDPSELTEPQAMVELERLAQQIRALDRAYYEDDAPTVTDAEYDALRQRNLAIEARFPDLRRADSPSLHVSGAPSAAFGRHRHLVPMLSLDNVFGREDFESFVTRAARFLGLNDDQARALRFVAEPKIDGLSISLTYEHGRFVRGTTRGDGTEGEDVTANLRTLRDVPLRLKGPAPALIEIRGEVFLSKPAFLSINAAQAEAGQKPFANPRNAAAGSLRQLDPNITARRPLSLFAYAQGFSSDRVADTHWDYLERLRQWGFTVNPLSCVVESAEAAEAFMDRIARERSGLEYDIDGVVYKVDDLALQDRLGFVGRAPRWAIAWKFPAEQAITRLTRIDIQVGRTGALTPVAILEPVNVGGVIVTRATLHNEDEIARKDVRVGDLVQIQRAGDVIPQILGVVPPGADAPPRGEAFIFPHTCPICGARAERPPGEVVWRCTGGLTCPAQVVERLIHFVSRDAFDIDGLGERTITEFHADGLLKTPADIFRLPDHEADIATREGWGTVSARNLTASVRARQTIPLARFIYALGIRRIGTSNARLLARHYGSYTHWREQMLRATTIGSDERLALGSITGIGGAIADELAAFFMEAHNLETLDDLTAMLTAIEDEDLPAQGHLSGKTVVFTGTLTTMTRPEAKAIAERLGARVTDSVSKKTDLVVLGADAGSKARKAAELGIDTLDEEGWRELAGIGPVGP | 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): 75946
Sequence Length: 695
EC: 6.5.1.2
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Q7VMX7 | MPLFSQFELSNNITPTQLEALRDQLREYEYHYHVLNNPLVPDAEYDRLINQLKNIEQQYPELITPDSPTQRVGAKPLAGFAQVAHEMPMLSLDNAFSETDLDNFLRRIENYLSLDANQLTFCCEPKLDGLAVSILYIDGVLQLAATRGDGTTGENITANVRTIRNIPLKLKMANPPHRLEIRGEIFMPLKGFNALNQRALAKGEKSFANPRNAAAGSLRQLDPQITRQRPLMLNAYGIGVYESNYQRLPTSHYARLEWLKSIGIPVNAEIRLARGYPQLLAFYADIQAKRADLGYDIDGTVLKVDDITIQETLGFISRSPRWAIAYKFPAQEEMTILKDVEFQVGRTGAITPVAKLEPTLVAGVTVSNATLHNGDEIERLGVAIGDTVIIRRAGDVIPQIIGIVADRRPANAKKIVFPTACPVCHSAVIRIAGEAVARCTGGLFCPAQRKEALKHFVSRKAMNIDGVGEKLIEQLMARELIHTPADLFKLDPLSLMRLERMGEKSAQNALNSIEKAKHTTLARFLFSLGIRDVGETTALNLANHFGSLENIRTANVEQLKEVQDVGEVVANRLVCFWQEQHNVAVVEELIAQGVHWDNIVQLEIADNPLKDKNVVLTGTLTQFSRDQARKLLQQLGCKVSSAVSTKTDFLIAGEKAGTKLTKAEQLGIRILDEHAFADLIKQLEYE | 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): 76289
Sequence Length: 686
EC: 6.5.1.2
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P43813 | MTNIQTQLDNLRKTLRQYEYEYHVLDNPSVPDSEYDRLFHQLKALELEHPEFLTSDSPTQRVGAKPLSGFSQIRHEIPMLSLDNAFSDAEFNAFVKRIEDRLILLPKPLTFCCEPKLDGLAVSILYVNGELTQAATRGDGTTGEDITANIRTIRNVPLQLLTDNPPARLEVRGEVFMPHAGFERLNKYALEHNEKTFANPRNAAAGSLRQLDPNITSKRPLVLNAYGIGIAEGVDLPTTHYARLQWLKSIGIPVNPEIRLCNGADEVLGFYRDIQNKRSSLGYDIDGTVLKINDIALQNELGFISKAPRWAIAYKFPAQEELTLLNDVEFQVGRTGAITPVAKLEPVFVAGVTVSNATLHNGDEIERLNIAIGDTVVIRRAGDVIPQIIGVLHERRPDNAKPIIFPTNCPVCDSQIIRIEGEAVARCTGGLFCAAQRKEALKHFVSRKAMDIDGVGGKLIEQLVDRELIHTPADLFKLDLTTLTRLERMGAKSAENALNSLENAKSTTLARFIFALGIREVGEATALNLANHFKTLDALKDANLEELQQVPDVGEVVANRIFIFWREAHNVAVVEDLIAQGVHWETVEVKEASENLFKDKTVVLTGTLTQMGRNEAKALLQQLGAKVSGSVSSKTDFVIAGDAAGSKLAKAQELNITVLTEEEFLAQITR | 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): 74043
Sequence Length: 670
EC: 6.5.1.2
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Q9KF37 | MERNDAERKIEKLRNQLEEYGYHYYVLDKPLVSDAEYDGLMNELIELEEAFPELKSDTSPSVRVGGPPLPHFEKVEHRTPMLSLGNAFSDQDLRDFDRRVRQVVGDEVTYSCELKIDGLAISLIYESGRFVRGATRGDGTTGEDITQNLRTIPSIPLRLKEAVSLEVRGEAFMPKRSFEALNEAKEAAGEERFANPRNAAAGSLRQLDPKLAAKRHLDAFIYAIGSVEGKELHSHHEGLNYLKTIGFKINPESAYCESIDEVIDYVNSWLERRADLPYEIDGIVIKVDNVNFQEQLGYTAKSPRWAIAYKFPAEEVITTLLDITLNVGRTGVVTPTAELKPVTVAGTTVKRASLHNEDLIREKDIRLGDSVVVKKAGDIIPEVVNVLTELRTGEERPFSMPTHCPECGSELVRLEGEVALRCINPQCPAQIREGLIHFVSRQAMNIDGLGEKVITQLFEHGLIHNVADLYKLNKDELLQLERMGEKSVNNLLASIETSKKSSLERLLFGLGIRFVGSKAAKTLAMHFPTMTELRRASYDELIAVNEIGEKMAASIVSYFEKPEVNELIDELASLGVNMTYNGPKPIGEEEIADSPFAGKTVVLTGKLQALTRGEAKEKIEALGGKVTGSVSKNTDLLVAGEDAGSKLTKAKELNIEIWDEEALVKAISH | 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): 74242
Sequence Length: 669
EC: 6.5.1.2
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B9LU22 | MTSSSPRHADPDENPYVEAPPTDFEPVGALSEDEATEQASLLRAAIREHDHRYYLEADPLIPDETYDRLFTRLQELENEFDLPTQNSPTRRVGGEPLDELATVEHVAPMRSIDNATEADAVREFDGRVRKGLDAEGFDSDAVEYVCEPKFDGLSVEVIYEDGEYVRAATRGDGTAGDDVTEQVRTIRSVPGKLRGDPPSRLAVRGEAYMPRDAFKAYNEALMERGEEPFANPRNAAAGTLRQLDPSVVAERPLDIFFFDVLGWENDAEGDSPNRPATHWEEFDTFDAFGLRRANRVERVDDIEGALDYRDRLMADREDLNFAIDGVVIAVDDRANREALGATARAPRWAFAYKFPPRTATTIVEGITVQVGRTGRLTPVAELDPIDVGGVTVSRATLHNPAEIEALGVNVGDCVRIYRAGDVIPYVPEVVEKRSEGTYVFPETCPICDAPVERDGPLAFCTGGLVCPAQLERAVEHWARRDALDIEGLGPERVQQLREAGLVESLPDLYDLAVDDLAALEGWGETSAENLIAELAATRDPPLDDFLAGLGIPDVGATTARALAAHFGDLDAILDADEDALRAVDDVGPEVAESIRTFLDNAENRVAIDGLRERGVDPESVDVETGDALDGLTFVFTGSLSTTRGEAQAHVEAHGADATSSVSGNTDYLVAGESPGRSKRDDADAEGVPVVDEEEFAGLLAERGVAWPPEE | 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): 77226
Sequence Length: 710
EC: 6.5.1.2
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B8D122 | MASKVEQEIRDLREKIRYHEYRYYVLDDPEISDAEFDELIQRLIDLEEKHPGLVTPDSPTQRVGGEPLDKFDKVEHRVPMLSLGNAFNEGDLTNFARRIYRLLDTGKIDFVVEHKIDGLSAILTYQGGRLIRGATRGNGVVGEDVTANIKTIPSVPLRLKKDVDIEVRGEVYIKKDDFSKLNERRLKKGEEPFANPRNAAAGSIRQLDPRLAAARPLSFIAYDVVAYEGEGLQTHVGALELLRELGFKVNWYRKCDDITEVVNICKDWVDKREELPFEIDGMVIKVNELGLREQLGATAKSPRWAIAYKFPAQQKTTVVKDIIISVGRTGALTPTAVLEPVEVDGSTVSRATLHNEDEIRRKDVRIGDHVLVQKAGDVIPEVVKVIKSKRDGSEQIFHMPETCPACGGEVVREEGEAVLRCVNVTGCPAQRREGILHFVSRNAMNIDGVGPALIDQLLEKGLIEDYADLYYLKKEDLIPLERMGEKSATNAIEAIRASKDRPLFRVIFALGIRHVGLGVARVLTEKYRSLSDLMRASGEELVAIDEIGPTIARSIIEFFKEPHNREVINKLKEAGVRLEEKENGKEEQNLYLSGKTFVFTGKLDGFTRSEARDKVIAAGGKVTSSVSRKTDYVVVGDSPGSKYDKARELGVTILDEDKFKEVLKAGDNNG | 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): 74872
Sequence Length: 670
EC: 6.5.1.2
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D4GY98 | MSDADVDAESNPYLRDPPTEFEPAESLSREAAEGQAALLREAVREHDHRYYVAADPLVSDAAYDALFSRLVALEDAFDLDTTNSPTNRVGGEPIDALETVEHVAPMLSIDQSTDADDLREFDERVRREVGAVDYVCEPKFDGLSVEVVYEDGEFVRAATRGDGRRGDDVSAQVKTIPTVPLSLRGDHPDRLAVRGEIYMPKSDFSDLNARRVEAGEDAFANPRNAAAGTLRNLDPSVVADRPLAVFFYDILDASARPDSQWAALDRLREWGLRVTDRIERAEDVAEAIDYRDRMQAARDDLDYEIDGTVIKVDSRDARERLGEKSRSVRWAFAYKFPARHEVTTVRDIVVQVGRTGRLTPVAILDPVDVGGVTVSRATLHNPDERAALGVAVGDRVRVKRAGDVIPQVVEVTEDGGGCYEFPDECPVCGSAVDRDGPLAFCSGGLSCPAQREASIGHFAVKGAMDIDGLGEERVAQLVDAGLVETVADLYDLTADDLAELEGWGETSAENLVAAVENAKHPSLDSFLVGLSIPEVGEATARGLAREFGSIEAFPIEADAEEDEFDAFEERLTTVPDVGETVARRVRDFFENADNRAVIRALLDRGVDPEPVESGGDELDGLTFVVTGTLAASRSDVTELVESHGGNVTGSVSGNTDYLVVGENPGRSKRDDAEANDVPTLAETEFEALLAERGVAYPPE | 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): 75811
Sequence Length: 699
EC: 6.5.1.2
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Q1D0P7 | MDDFQKAAARARELHRELAHHNYRYYVLDSPEVSDAQYDKLMRELQDLEAKHPSLQTPDSPTQRVGGAAAEEFGEVVHRAPMISLANIFEDQGLTEFDERIRKLVGLPGIAYVCEPKLDGLAIALRYEKGAFVQGATRGDGTTGEDVTSNLRTIRSLPMSLFPQDDVKVPDVLEVRGEVFIRKKDFQKLNEKREEEGEPLFANPRNAAAGSLRQLDPRMTAARPLSVFLYECVPGEGVPVFKTHIEKLEYLKTLGLPINQYRRAEGLEGVRQAYDASLKGRHELPFEVDGMVVKVDDEDQRKRLGQVSKSPRWAVAYKFPPEEESTEVMDIGIQVGRTGALTPVAHLKPVKVGGVTVARATLHNEDELRRKDVRKGDTVFVRRAGDVIPEIVSVVLSKRPADSAPFEFPKHCPVCDAVATKDEDGAIIRCTGASCPAQLVEKIRHFASRLAMDIEGLGDKLAAQLVSTGRVKAFADLYALTKEDLLTLERMGDKSADNLIASLERSKQTTQRRFLYSLGIRHVGDATAKALAEAFPRSEMLFEASLEDISRVKDVGPIMAQVIHTFFQEPQNQEAIRALLAAGVQPAAPQVATGGPFVGKSVVLTGAMTGMTREQAKEEVERRGGKVAGSVSRKTDFVVAGEDAGSKLKKAQELGVRILDEQAFLQMLQTNA | 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): 74045
Sequence Length: 672
EC: 6.5.1.2
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B2A5W5 | MSKDIQKKVEALREKIEYHNHRYYVLDAPEISDQEFDALMNELIELEQTYPEYQSPDSPSQRVGGEPLDKFPRVSHEIPMLSLENAESQKGLLDFHQRVSKNTQKTDPVYVAELKIDGLALSLRYEQGILVRGATRGDGTTGEDITPNVKTVRSIPLKLSKPLDIEIRGEAFMSKASFERLNQEKAERGEDPFANPRNAAAGSLRQLDPKIPAKRDLDFFPYSVPYIRGENLDSHYSAVKELKDLGFKINPYIRKFETMEEVISYCEEWQEKRTKLPYEIDGVVIKLNDYNLQQQLGATSKNPRWAIAYKFPAEQAESQVNNIFINVGRTGALTPVVELEPVRIAGSTVKRASLHNEDILRQKDVRIGDRVIIQKAGDIIPEVVKVKEEARTGHEQPFVYPESCPVCKSEAKRINDEAILRCINPGCPAQAKERIIHFSSRDAMDIEGLGEKVVEKLYSHGLIKDVADIYYLAKNELSNLEGFGDKSAENLLQAIEESKKNPFNKLLYGLGIRLVGKRAAQLLAFEFEHLDNLMKAQIEDLTKINDIGPRMATSIVSFFQLEHTHNLIRKLKKAGVNMKEPTEQNKSSDPSLTGKLVVITGTFDNYTRRELTDLIEAKGAKVTSNVSSNTDFVLVGANPGSKRDKAQDLGLTIIEESDLEDFL | 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): 74761
Sequence Length: 663
EC: 6.5.1.2
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Q5F9Z9 | MNLYESMNPTAQRIHELTDLLNRYAYEYYTLDAPSIPDAEYDRLFRELEALERNHPELKLPDSPTQRVGGEPLAGFAEVRHEVPMLSLTNAFSPQDENGVFDHAEMYAFDQRVRDGLDGGNPEYVIEPKFDGLAISLLYRDGVLVQAATRGDGTTGEDVTRNVKTVSNIPLRLHGENVPELIEVRGEVLMLKADFAALNQRQTENGQKPFANPRNAAAGSLRQLDSRITAQRKLHFFPYSVARQQGGLIAEEHIQELAYFQALGFSLPNGNFGCFKNIGEVLAFYEHMQQKRPELPYEIDGTVVKVNSLAQQHELGFISRAPRWAVAHKFPAEEALTIVEAIDVQIGRTGAVTPVARLQPVFVGGVTVTNATLHNQDEVSRKDVRVGDTVVVRRAGDVIPEVVRVIFERRPMQETAVAVSDGIGHQQDDLFAETPSAKQTESVPLHKPYRLPARCPICRSEIEREEGEAVARCSGGMLCQAQRAQGLIHFASRKAMDIDGLGEKQIEQLVAQDLVRHFADLYRIDIPTLQKMKETADKGSSENENGDAETVSGDLSKYNTQNGKKQPTKWAQNILAGIESGKTPELARFLFALGIRHVGERTAKTLAQAFGTLERVRRAPEPVLACLPDIGTVVARSIAHFFAQAEQQAMIDELLAAGVAPQAQAVSLPAAQYAGPQRWITRLPGFKISENKAQALWELAGQSIEGLQNDKALPADWQAWRSKAQNTALLENLKTFFAQMPSEDEAAQGSDGINKAVAGKTFVLTGTLPTFKRDQAQALIEAAGGKVSGSVSKKTDYVVAGETAGSKLEKANALGVSVLSEAELLTLLC | 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): 90942
Sequence Length: 829
EC: 6.5.1.2
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Q2GDR2 | MEAKKEIQELYEKLLRHNKKYYQDDSPEITDAEYDSIKDRYLKLLEANPSLGFPVVVGYPASEKFQKVKHLSPMLSLRNIFSEEELVEYIEKTKRFLNLKSALEFLCEPKIDGVSFSARYVNGKLVSCATRGDGKIGENIIDNMKVINGFPIEIMDVPDLLEVRGEVFLDHDTFQTLEGFSNPRNAAAGSLRQLNPEITNERNLQYFAYSASKIDGIEHQEDVLHFLSGRGFMTNPLRLASSKVPEIMSFYDSVYRRRSQIKYDIDGLVYKVNDLKLHARLGTLSDAPRWAIAHKFPSHRAKTILEKIKLSVGRTGIITPVAHLKPITIGGVVISRASLYNEDELERKDIREGDLVIVERAGDVIPKVLEVDISYRTNQERFIFPDKCPSCSSTLIRKNNEAATRCNNSKKCPEQVIQQIKHLVSAQAFDIDGIGTSHISFFIEKGFISEPADIFRLDKHRDEIKKYDGWGEKSVENILKNIKNSRKISLEKFIFSLGIKNIGEKTAYMLAQQFKSFANWFDKMSMLKDDTQTEDEIRNLDGMGSCICESLLDFFSDSDNCNMVKSLSNHVMITDHTVNIGGSLSGKKFVFTGTLLSITREEAKEIIKKAGGIVVNSISKQIDYVVAGEKAGSKLAKANELGIAIIEEKTLIEFTNGNNTPALKKETSSN | 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): 75576
Sequence Length: 670
EC: 6.5.1.2
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Q0AHH6 | MESEKIIEERLKALRSTIALHDFHYYVQDAPIIPDADYDKLFRTLQQLEQQYPHLITPDSPTQRVGAPPLKVFARLTHQTPMLSLTNAFTEDEAIAFDKRIREALNVDQVNYAVEPKFDGLAVSLVYTNGILTNGATRGDGYTGEDITLNLRTIPSIPLRLQTATVTDQFEVRGEVVMLKADFEHLNEQQRNKGEKLFANPRNAAAGSLRQLDSNITAARKLTFFAYDAVLSHKDQPFFSKHSEILDYLKSQQFLVAQQNGTTTGVAGLLTYYHEMGALRLSLPYEIDGVVYKVDNLTQQETLGYVSRAPRFAIAHKFPAQEASTELLTIEIQVGRTGALTPVARLAPVFVGGVTVTNATLHNEDEVQRKQIMIGDTVIVRRAGDVIPEVVAVIPEQRPAHAQPFIMPDHCPVCGSKAARLPGEAVTRCTGGLYCPAQRKQAIWHFASRRALDIDGLGEKLIDQLIDRELVHTPADLYKLNIDTLASLERMAEKSARNLVTAIEHSKKTTLPRFIYALGIRHVGEATAKALANQASHLDQLMTLDIEQLQQIPDVGPIVAQSIIDFFSEAHNREVIRQLLDSGLQWEIPNHGVQQSEQTNSAVSGKTFVLTGTLPTMTRDQAKIKIEQQGGKVTGSVSSATSYVVAGSDPGSKYAKAIGLGISVLDEDQLLSLLQNISTGAQQ | 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): 75297
Sequence Length: 683
EC: 6.5.1.2
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Q1QNT2 | MAAKPKTPPPVDSLTRAQAKIEHKRLALEIETHNERYYQKDAPTVSDAAYDALRQRLEAIEARFPDLITANSPTQTVGAAPARGFAKVQHAVPMLSLGNAFSDEEVAEFVERIQRFLKLGPDDIPAIVAEPKIDGLSLSLRYENGELVRAATRGDGFTGEDVTANVRTIKDVPHNLRGRNIPTACELRGEVYMLKTDFLALNKKQEDAGDTVFANPRNSAAGSLRQKDVAITASRPLKFFAYAWGEMTDRPADTQHDMLEWLKDVGFKVNPLIELCNSVEKVLKFYRKIGEQRASLGYDIDGVVYKVDRLDWQERLGFVSRSPRWAIAHKFAAEQATTILKGIDIQVGRTGAMTPVARLEPVTIGGVVVQNATLHNEDYIKGIGNDGQPIRDGVDLRVGDTVVVQRAGDVIPQVVSVVIDKRPNSAQPYAFPHTCPICGSHAVREEGEAVRRCTGALICPAQAVERLKHFVSRLAFDIDGLGEKQIQEFHERGWIKEPADIFTLRERNPKIKLEELEGFGEVSVRNLFAAIDARRTIELNRLIFALGIRHVGEGNAKLLARHYGGIDAFRAAMSEAAAAQTDDGNASEAYADLNNISGIGDIVADAVVEFFAETRNVKALNDLLEEIEVLPVAQARNDSAVAGKTVVFTGSLEKFTRDEAKASAERMGAKVSGSVSKKTDLVVAGPGAGSKLKDAEKHGVQVISEDEWLKLIEG | 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): 78181
Sequence Length: 714
EC: 6.5.1.2
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A6Q433 | MIKNYQEYKEAVEKLKRWAYAYYVLDNPEVPDEVYDKLYREVEEYEKAHPDQIDPTSPTQRIGAEPAKEFKKIKHLSKMWSMEDVFNQREMHEWLERVYKNAGRKDLQFYIEPKFDGASLNLIYENGLLKSAATRGDGEVGEDVTANAKTIPSIPLGIDYKGLIEIRGEVVIRKDDFEKLNHERALKGESTFANPRNAAAGSLRQLDPKVTAQRKLYFYPWDIGYNTLNFKYQHEKMDFVYQQGFIKPFKRAICENEEEIQQLYEEFSKERDKLPVMLDGMVVKVDEIALHEILGYTVKYPRWMVAYKFPAVEKMTRIIDIVPQVGRTGVITPVAILEPVEIEGVVVERATLHNYAEIERKDIRIGDMVIVIRSGDVIPEVTKVLTQYRTGKEKKVERPKVCPVCGQPVLDEGILIKCQNLSCPARVVNSIIYFASKQCLDISGLGEATVKLLYEKGLVKDVVDLFKLKKEDLLRLPGFAEKKAQNLIDATQSVKGVECWRFVNALGIEHIGEVASKKLCEKFGLDWYKAPKEKLYEIEGFGPEMVRSIEEFVEVNKEKIEKLIELLQPTEPKKEEEVENSPLAHKTVVLTGEMKLPRSKIKELLERAGAHVTNSVSHHTDYVFYGENPGSKFQKAQQLGVPLLPEEKMWELLKEAGIEA | 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): 75770
Sequence Length: 660
EC: 6.5.1.2
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Q80VJ3 | MAASGELVPCSVYFCGSIRGGREDQALYSRIVSRLRRYGKVLTEHVADAELEPRGEEAAGGDQFIHERDLAWLRQADVVVAEVTQPSLGVGYELGRAVALGKPILCLFRPQSGRVLSAMIRGAADGSRFQVWDYAEEEVETMLHRYFEAYLPQGTASSSNPSACLNPTVLEKI | Function: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'-monophosphates containing purine bases are preferred to those containing pyrimidine bases.
Catalytic Activity: a pyrimidine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-D-ribose 5-phosphate + a pyrimidine nucleobase
Sequence Mass (Da): 18977
Sequence Length: 173
Subcellular Location: Cytoplasm
EC: 3.2.2.-
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O35820 | MAASGEQAPCSVYFCGSIRGGREDQALYARIVSRLRRYGKVLTEHVADAELEPLGEEAAGGDQFIHEQDLNWLQQADVVVAEVTQPSLGVGYELGRAVALGKPILCLFRPQSGRVLSAMIRGAADGSRFQVWDYAEGEVETMLDRYFEAYLPQKTASSSHPSA | Function: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'-monophosphates containing purine bases are preferred to those containing pyrimidine bases.
Catalytic Activity: a pyrimidine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-D-ribose 5-phosphate + a pyrimidine nucleobase
Sequence Mass (Da): 17781
Sequence Length: 163
Subcellular Location: Cytoplasm
EC: 3.2.2.-
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Q3A6G9 | MKIFFSGSIRGGNKYRRQYGQILAFLQAFGETISEHSDRPEAFDDGGLKGDAAIYARDTHWIREADLLVAEVSQPSIGVGYEIAYAEARNIPILALYHVGAESPMSAMVFGNPKITSIRYDSLSELWPVLKDTLAETHLPPK | Function: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base.
Catalytic Activity: a pyrimidine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-D-ribose 5-phosphate + a pyrimidine nucleobase
Sequence Mass (Da): 15745
Sequence Length: 142
EC: 3.2.2.-
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Q4S2L4 | MKVYFCGSIRGGRDDAELYHRMVAKLQSFATVLTEHVGRRELGDTGEHVTQGDRFIHDRDVDWLRQSDVVVAEVTQPSLGVGYELGRAVDMKKKVLCLFRPSSGRRLSAMIRGADNGDSFVVRDYCQDEIEQVLEDFFSNQK | Function: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base. Deoxyribonucleoside 5'-monophosphates containing purine bases are preferred to those containing pyrimidine bases.
Catalytic Activity: a pyrimidine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-D-ribose 5-phosphate + a pyrimidine nucleobase
Sequence Mass (Da): 16130
Sequence Length: 142
Subcellular Location: Cytoplasm
EC: 3.2.2.-
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Q24FH8 | MSQKKLTIYFCGSMRGVNANHQNYQTIVQELSKYGEVLTTHVAYPEMSNKLEHKMNDKQIYERDYSWFTESQVMVAEVTAPSHGVGMELGWASLRQNYKTLCLSQKEKEFKTSGLIAGCPTFEYKEYQNQEDIVAIIAEFMKQLQ | Function: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base.
Catalytic Activity: a pyrimidine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-D-ribose 5-phosphate + a pyrimidine nucleobase
Sequence Mass (Da): 16780
Sequence Length: 145
Subcellular Location: Cytoplasm
EC: 3.2.2.-
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A1RW47 | MKVYLAAPMRGDRSALANVKKLLQALEERGYVVLTKHVADDVLDVEKGMTPREVFERDIRLLEEADVLVAEVSYPSLGVGFEIAYFLLRGKPVIALALRERLESVSAMIRGITWENFRLVAYSDVDEAIEKLDSMLPGSVDMQ | Function: Catalyzes the cleavage of the N-glycosidic bond of deoxyribonucleoside 5'-monophosphates to yield deoxyribose 5-phosphate and a purine or pyrimidine base.
Catalytic Activity: a pyrimidine 2'-deoxyribonucleoside 5'-phosphate + H2O = 2-deoxy-D-ribose 5-phosphate + a pyrimidine nucleobase
Sequence Mass (Da): 16043
Sequence Length: 143
EC: 3.2.2.-
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Q54818 | MQDSSYKEQVTQAFDQSSSTYDRLGVEFFTPMGRPLVEISEPVTGERVLDIGCGRGACLFPAAEKVGPQGRVHGIDIAPGMIEEARKEAAERGLRNIALDVMDAETPELPARSFDLVMGSYSVIFLPDAVGALARYAGILDHGGRIAFTSPVFRAGTFPFLPPEFTPLIPQALLEHLPEQWRPEALVRRFNSWLERAEDLLRTLERCGYTSVAVTDEPVRMTALSSEAWVDWSHTQGMRLLWQNLPQAQRTELRARLVEGLDKLSDATGALAIDVPVRFVTARVAH | Function: Involved in the biosynthesis of aklavinone which is an important precursor common to the formation of the clinically significant anthracyclines such as carminomycin, daunorubicin (daunomycin), rhodomycin, aclacinomycin T (aklavin) and aclacinomycin A (aclarubicin). These compounds are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the methyl esterification of aklanonic acid to yield aklanonic acid methyl ester.
Catalytic Activity: aklanonate + S-adenosyl-L-methionine = methyl aklanonate + S-adenosyl-L-homocysteine
Sequence Mass (Da): 31676
Sequence Length: 286
Pathway: Antibiotic biosynthesis; daunorubicin biosynthesis.
EC: 2.1.1.288
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Q55214 | MQDSSYKKQVTQAFDQSSSTYDRLGVEFFTPMGRRLVDISEPVTGERVLDIGCGRGACLFPAAEKVGSQGCVHGIDIAPGMIEEARKEATERGLRNISLMVMDAETPGFPARSFDLVMGSYSVIFLPDAVGALARYADILDHGGRIAFTSPVFRAGTFPFLPPEFTPLIPQALLEHLPEQWRPEALVRRFNSWLERAEDLVRTLEGCGYARLRQSTSRCG | Function: Involved in the biosynthesis of aklavinone which is an important precursor common to the formation of the clinically significant anthracyclines such as carminomycin, daunorubicin (daunomycin), rhodomycin, aclacinomycin T (aklavin) and aclacinomycin A (aclarubicin). These compounds are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the methyl esterification of aklanonic acid to yield aklanonic acid methyl ester.
Catalytic Activity: aklanonate + S-adenosyl-L-methionine = methyl aklanonate + S-adenosyl-L-homocysteine
Sequence Mass (Da): 24320
Sequence Length: 220
Pathway: Antibiotic biosynthesis; daunorubicin biosynthesis.
EC: 2.1.1.288
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O52646 | MSEQIAAVRRMVEAYNTGKTDDVADYIHPEYMNPGTLEFTSLRGPELFAINVAWVKKTFSEEARLEEVGIEERADWVRARLVLYGRHVGEMVGMAPTGRLFSGEQIHLLHFVDGKIHHHRDWPDYQGTYRQLGEPWPETEHRRP | Function: Involved in the biosynthesis of aklavinone which is an important precursor common to the formation of the clinically significant anthracyclines such as carminomycin, daunorubicin (daunomycin), rhodomycin, aclacinomycin T (aklavin) and aclacinomycin A (aclarubicin). These compounds are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the cyclization of aklanonic acid methyl ester to yield aklaviketone. It is also able to use nogalonic acid methyl ester as substrate, but produces exclusively auraviketone with C9-R stereochemistry.
Catalytic Activity: methyl aklanonate = aklaviketone
Sequence Mass (Da): 16731
Sequence Length: 144
Pathway: Antibiotic biosynthesis; daunorubicin biosynthesis.
EC: 5.5.1.23
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Q54808 | MSTQIDLVRRMVEAYNTGKTDDVAEFIHLEYLNPGALEHNPELRGPEAFAAAVTWLKYAFSEEAHLEEIEYEENGPWVRAKLALYGRHVGNLVGMPATGRRFSGEQIHLIRIVDGKIRDHRDWPDYLGTYRQLGEPWPTPEGWRP | Function: Involved in the biosynthesis of aklavinone which is an important precursor common to the formation of the clinically significant anthracyclines such as carminomycin, daunorubicin (daunomycin), rhodomycin, aclacinomycin T (aklavin) and aclacinomycin A (aclarubicin). These compounds are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the cyclization of aklanonic acid methyl ester to yield aklaviketone presumably via an intramolecular aldol condensation mechanism, although water is not eliminated.
Catalytic Activity: methyl aklanonate = aklaviketone
Sequence Mass (Da): 16701
Sequence Length: 145
Pathway: Antibiotic biosynthesis; daunorubicin biosynthesis.
EC: 5.5.1.23
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Q53882 | MENTQRSVIVTGGGSGIGRAVARAFAARGDRVLVVGRTAGPLAETVDGHKEAHTLAVDITDPAAPQAVVREVRERLGGVVDVLVNNAATAVFGHLGELDRTAVEAQVATNLVAPVLLTQALLDPLETASGLVVNIGSAGALGRRAWPGNAVYGAAKAGLDLLTRSWAVELGPRGIRVIGVAPGVIETGAGVRAGMSQEAYDGFLEAMGQRVPLGRVGRPEDVAWWVVRLADPEAAYASGAVLAVDGGLSVT | Function: Involved in the biosynthesis of aklavinone which is an important precursor common to the formation of the clinically significant anthracyclines such as carminomycin, daunorubicin (daunomycin), rhodomycin, aclacinomycin T (aklavin) and aclacinomycin A (aclarubicin). These compounds are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the NADPH-specific conversion of aklaviketone to yield aklavinone. It can also convert maggiemycin and 7-oxodaunomycinone to epsilon-rhodomycinone and daunomycinone, respectively.
Catalytic Activity: aklavinone + NADP(+) = aklaviketone + 2 H(+) + NADPH
Sequence Mass (Da): 25632
Sequence Length: 251
Pathway: Antibiotic biosynthesis; daunorubicin biosynthesis.
EC: 1.1.1.362
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Q54530 | MNDHEVDVLVVGAGLGGLSTAMFLARQGVRVLVVERRPGLSPYPRAAGQNPRTMELLRIGGVADEVVRADDIRGTQGDFVIRLAESVRGEILRTVSESFDDMVAATEPCTPAGWAMLSQDKLEPILLAQARKHGGAIRFGTRLLSFRQHDDDAGAGVTARLAGPDGEYDLRAGYLVGADGNRSLVRESLGIGRYGHGTLTHMVGVIFDADLSGIMEPGTTGWYYLHHPEFKGTFGPTDRPDRHTLFVEYDPDEGERPEDFTPQRCVELIGLALDAPEVKPELVDIQGWEMAARIAERWREGRVFLAGDAAKVTPPTGGMSGNAAVADGFDLAWKLAAVLQGQAGAGLLDTYEDERKVAAELVVAEALAIYAQRMAPHMAEVWDKSVGYPETLLGFRYRSSAVLATDDDPARVENPLTPSGRPGFRGPHVLVSRHGERLSTVDLFGDGWTLLAGELGADWVAAAEAVSAELGVPVRAYRVGAGLTDPESAVSERYGIGKAGASLVRPDGIVAWRTDEAAADAAQTLEGVLRRVLDR | Function: Involved in the biosynthesis of the anthracyclines carminomycin, rhodomycin and daunorubicin (daunomycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. Catalyzes the incorporation of a hydroxyl group at position C-11 of aklavinone, resulting in epsilon-rhodomycinone. It cannot accept substrates glycosylated at position C-7 and is specific for the C-9R configuration of anthracyclines. It can use both NAD or NADP but it is slowly inactivated in the presence of NADH.
Catalytic Activity: aklavinone + H(+) + NADPH + O2 = epsilon-rhodomycinone + H2O + NADP(+)
Sequence Mass (Da): 57437
Sequence Length: 535
Pathway: Antibiotic biosynthesis; daunorubicin biosynthesis.
EC: 1.14.13.180
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A0SVK0 | MGSSSKNIEQAQDSYLEWMSLQSQRIPELKQLLAQRRSHGDEDNDNKLRKLTGKIIGDFKNYAAKRADLAHRCSSNYYAPTWNSPLENALIWMGGCRPSSFFRLVYALCGSQTEIRVTQFLRNIDGYESSGGGGGASLSDLSAEQLAKINVLHVKIIDEEEKMTKKVSSLQEDAADIPIATVAYEMENVGEPNVVVDQALDKQEEAMARLLVEADNLRVDTLAKILGILSPVQGADFLLAGKKLHLSMHEWGTMRDRRRRDCMVDTEVIFDACTTVNSGPRPTETTNNERN | Function: Required for the induction of seed dormancy . The level of DOG1 protein in freshly harvested seeds determines the level of seed dormancy . Determines the temperature window for germination by regulating the expression of micropylar endosperm-weakening genes through temperature control of the gibberellins metabolism . Regulates seed dormancy and flowering time through an influence on levels of microRNAs miR156 and miR172 . Regulator of seed maturation interfering with abscisic acid signaling components and activating ABI5 . In cv. Cvi-1, enhances glucose induction of ABI4 .
PTM: A shift in isoelectric focusing of the protein occurs during after-ripening, probably leading to its loss of function.
Sequence Mass (Da): 32470
Sequence Length: 291
Subcellular Location: Nucleus
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P38773 | MPQFSVDLCLFDLDGTIVSTTTAAESAWKKLCRQHGVDPVELFKHSHGARSQEMMKKFFPKLDNTDNKGVLALEKDMADNYLDTVSLIPGAENLLLSLDVDTETQKKLPERKWAIVTSGSPYLAFSWFETILKNVGKPKVFITGFDVKNGKPDPEGYSRARDLLRQDLQLTGKQDLKYVVFEDAPVGIKAGKAMGAITVGITSSYDKSVLFDAGADYVVCDLTQVSVVKNNENGIVIQVNNPLTRD | Function: Phosphatase that is active on 2-deoxy-D-glucose 6-phosphate (2-DOG-6P), but not very active on fructose-1-P.
Catalytic Activity: 2-deoxy-D-glucose 6-phosphate + H2O = 2-deoxy-D-glucose + phosphate
Sequence Mass (Da): 27165
Sequence Length: 246
EC: 3.1.3.68
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A0QZ49 | MQRIIGTEVEYGISSPSDPTANPILTSTQAVLAYAAAAGIQRAKRTRWDYEVESPLRDARGFDLSRSSGPPPIVDADEVGAANMILTNGARLYVDHAHPEYSAPECTDPMDAVIWDKAGERVMEAAARHVASVPGAAKLQLYKNNVDGKGASYGSHENYLMSRQTPFSAVIAGLTPFMVSRQVVTGSGRVGIGPSGDEPGFQLSQRADYIEVEVGLETTLKRGIINTRDEPHADADKYRRLHVIIGDANLAETSTYLKLGTTSLVLDLIEEGVDLSDLALARPVHAVHVISRDPSLRATVALADGRELTALALQRIYLDRVAKLVDSRDPDPRASHVIETWANVLDLLERDPMECAEILDWPAKLRLLEGFRQRENLTWQAPRLHLVDLQYSDVRLDKGLYNRLVARGSMKRLVTEQQVLDAVENPPTDTRAYFRGECLRRFGADIAAASWDSVIFDLGGDSLVRIPTLEPLRGSKAHVGALLDSVDSAVELVEQLTN | Cofactor: ATP is required for the deamidation reaction but is not hydrolyzed during this reaction.
Function: Specifically catalyzes the deamidation of the C-terminal glutamine of the prokaryotic ubiquitin-like protein Pup to glutamate, thereby rendering Pup competent for conjugation. Probably also displays depupylase (DPUP) activity, removing conjugated Pup from target proteins; thus may be involved in the recycling of Pup and may function similarly to deubiquitinases (DUBs) in eukaryotes to prevent or promote proteasomal degradation of certain proteins.
Catalytic Activity: [prokaryotic ubiquitin-like protein]-C-terminal-L-glutamine + H2O = [prokaryotic ubiquitin-like protein]-C-terminal-L-glutamate + NH4(+)
Sequence Mass (Da): 54574
Sequence Length: 498
Pathway: Protein degradation; proteasomal Pup-dependent pathway.
EC: 3.4.-.-
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P0C1B7 | ADVPGNYPLDKDGNTYTCLKLGENKDCQKVCKLHGVQYGYCYAFECWCKEYLDDKDSV | Function: Binds to sodium channels (Nav) and affects the channel activation process (By similarity). In mice, causes hyperactivity that persists until death.
Sequence Mass (Da): 6648
Sequence Length: 58
Domain: Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Subcellular Location: Secreted
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Q5BPS3 | MKSRRQNVSVARQTILGRDENFEPIPIDLVIEIFSRSPVKSIARCRCVSKLWASILRLPYFTELYLTKSCARPRLLFACQKHRELFFFSTPQPHNPNESSSPLAASFHMKIPFDGRFNIISPIGGLVFVRYEQILKGRKTPEFVSAICNPSTGQSLTLPKPKTRKRIWGTSHFGYDPIEKQFKVLSMNIGDGVYKEHYVLTLGTENLSWRRIECSIPHVHGSKGICINGVLYYRAKADMFSGTLMIVCFDVRFEKFSYIKILKPTTTLISYNGKLASLVWEGPSYICGKRFEMWVLGDPEKHEWLKHTYELRPRWQNVLGEDLLIFAGMTGTNEIVLSPKYPSHPFYVFYYNLERNTIRRVEIQGMGAFKVNEDYIFLDHVEDVKLI | Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Negative regulator of guard cell abscisic acid (ABA) signaling, especially during drought stress.
Sequence Mass (Da): 44770
Sequence Length: 387
Domain: The F-box is necessary for the interaction with ASK proteins.
Pathway: Protein modification; protein ubiquitination.
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Q320T0 | MEMYFKRMKDEWTGLVEQADPLIRAKAAEIAVAHAHYLSIEFYRIVRIDPHAEEFLSNEQVERQLKSAMERWIINVLSAQVDDVERLIQIQHTVAEVHARIGIPVEIVEMGFRVLKKILYPVIFSSDYSAAEKLQVYHFSINSIDIAMEVMTRAFTFSDSSASKEDENYRIFSLLENAEEEKERQIASILSWEIDIIYKILLDSDLGSSLPLSQADFGLWFNHKGRHYFSGIAEVGHISRLIQDFDGIFNQTMRNTRNLNNRSLRVKFLLQIRNTVSQIITLLRELFEEVSRHEVGMDVLTKLLNRRFLPTIFKREIAHANRTGTPLSVLIIDVDKFKEINDTWGHNTGDEILRKVSQAFYDNVRSSDYVFRYGGDEFIIVLTEASENETLRTAERIRSRVEKTKLKAANGEDIALSLSIGAAMFNGHPDYERLIQIADEALYIAKRRGRNRVELWKASL | Cofactor: Binds 1 heme group per subunit.
Function: Globin-coupled heme-based oxygen sensor protein displaying diguanylate cyclase (DGC) activity in response to oxygen availability. Thus, catalyzes the synthesis of cyclic diguanylate (c-di-GMP) via the condensation of 2 GTP molecules. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria (By similarity).
Catalytic Activity: 2 GTP = 3',3'-c-di-GMP + 2 diphosphate
Sequence Mass (Da): 53194
Sequence Length: 460
Domain: Is composed of an N-terminal sensory globin-fold domain that binds heme and oxygen, and a C-terminal GGDEF diguanylate cyclase domain.
Pathway: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
EC: 2.7.7.65
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Q83KV7 | MEMYFKRMKDEWTGLVEQADPLIRAKAAEIALAHAHYLSIEFYRIVRIDPHAEEFLSNEQVERQLKSAMERWIINVLSAQVDDVERLIQIQHTVAEVHARIGIPVEIVEMGFRVLKKILYPVIFSSDYSAAEKLQVYHFSINSIDIAMEVMTRAFTFSDSSASKEDENYRIFSLLENAEEEKERQIASILSWEIDIIYKVLLDSDLGSSLPLSQADFGLWFNHKGRHYFSGIAEVGHISRLIQDFDGIFNQTMRNTRILNNRSLRVKFLLQIRNTVSQIITLLRELFEEVSRHEVGMDVLTKLLNRRFLPTIFKREIAHANRTGTPLSVLIIDVDKFKEINDTWGHNTGDEILRKVSFLSQKRLVKSKILGAGSSRKLAVS | Cofactor: Binds 1 heme group per subunit.
Function: Globin-coupled heme-based oxygen sensor protein displaying diguanylate cyclase (DGC) activity in response to oxygen availability. Thus, catalyzes the synthesis of cyclic diguanylate (c-di-GMP) via the condensation of 2 GTP molecules. Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria (By similarity).
Catalytic Activity: 2 GTP = 3',3'-c-di-GMP + 2 diphosphate
Sequence Mass (Da): 43997
Sequence Length: 381
Domain: Is composed of an N-terminal sensory globin-fold domain that binds heme and oxygen, and a C-terminal GGDEF diguanylate cyclase domain.
Pathway: Purine metabolism; 3',5'-cyclic di-GMP biosynthesis.
EC: 2.7.7.65
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P76129 | MKLTDADNAADGIFFPALEQNMMGAVLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGGKARVEGMSRELQLEKKDGSKIWTRFALSKVSAEGKVYYLALVRDASVEMAQKEQTRQLIIAVDHLDRPVIVLDPERHIVQCNRAFTEMFGYCISEASGMQPDTLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIRQLEGNILAAMCSSPPFHEMGEIICRNIESVLNESHVSLFALRNGMPIHWASSSHGAEIQNAQSWSATIRQRDGAPAGILQIKTSSGAETSAFIERVADISQHMAALALEQEKSRQHIEQLIQFDPMTGLPNRNNLHNYLDDLVDKAVSPVVYLIGVDHIQDVIDSLGYAWADQALLEVVNRFREKLKPDQYLCRIEGTQFVLVSLENDVSNITQIADELRNVVSKPIMIDDKPFPLTLSIGISYDLGKNRDYLLSTAHNAMDYIRKNGGNGWQFFSPAMNEMVKERLVLGAALKEAISNNQLKLVYQPQIFAETGELYGIEALARWHDPLHGHVPPSRFIPLAEEIGEIENIGRWVIAEACRQLAEWRSQNIHIPALSVNLSALHFRSNQLPNQVSDAMHAWGIDGHQLTVEITESMMMEHDTEIFKRIQILRDMGVGLSVDDFGTGFSGLSRLVSLPVTEIKIDKSFVDRCLTEKRILALLEAITSIGQSLNLTVVAEGVETKEQFEMLRKIHCRVIQGYFFSRPLPAEEIPGWMSSVLPLKI | Function: Heme-based oxygen sensor protein displaying phosphodiesterase (PDE) activity toward c-di-GMP in response to oxygen availability. Involved in the modulation of intracellular c-di-GMP levels, in association with DosC which catalyzes the biosynthesis of c-di-GMP (diguanylate cyclase activity). Cyclic-di-GMP is a second messenger which controls cell surface-associated traits in bacteria. Has very poor PDE activity on cAMP but is not active with cGMP, bis(p-nitrophenyl) phosphate or p-nitrophenyl phosphate . Via its PDE activity on c-di-GMP, DosP regulates biofilm formation through the repression of transcription of the csgBAC operon, which encodes curli structural subunits.
PTM: The heme distal ligand is coordinated by Met-87 in the active Fe(2+) (ferrous) form, by O(2) in the O(2)-bound form and by H(2)O in the inactive Fe(3+) (ferric) form.
Catalytic Activity: 3',3'-c-di-GMP + H2O = 5'-phosphoguanylyl(3'->5')guanosine + H(+)
Sequence Mass (Da): 90260
Sequence Length: 799
Domain: The EAL domain (residues 532 to 799) is a cyclic dinucleotide di-GMP (c-di-GMP) PDE hydrolyzing c-di-GMP to 5'pGpG; it has no activity on cAMP.
EC: 3.1.4.52
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P9WGK0 | MTHPDRANVNPGSPPLRETLSQLRLRELLLEVQDRIEQIVEGRDRLDGLIDAILAITSGLKLDATLRAIVHTAAELVDARYGALGVRGYDHRLVEFVYEGIDEETRHLIGSLPEGRGVLGALIEEPKPIRLDDISRHPASVGFPLHHPPMRTFLGVPVRIRDEVFGNLYLTEKADGQPFSDDDEVLVQALAAAAGIAVDNARLFEESRTREAWIEATRDIGTQMLAGADPAMVFRLIAEEALTLMAGAATLVAVPLDDEAPACEVDDLVIVEVAGEISPAVKQMTVAVSGTSIGGVFHDRTPRRFDRLDLAVDGPVEPGPALVLPLRAADTVAGVLVALRSADEQPFSDKQLDMMAAFADQAALAWRLATAQRQMREVEILTDRDRIARDLHDHVIQRLFAVGLTLQGAAPRARVPAVRESIYSSIDDLQEIIQEIRSAIFDLHAGPSRATGLRHRLDKVIDQLAIPALHTTVQYTGPLSVVDTVLANHAEAVLREAVSNAVRHANATSLAINVSVEDDVRVEVVDDGVGISGDITESGLRNLRQRADDAGGEFTVENMPTGGTLLRWSAPLR | Cofactor: Binds 1 heme group per monomer.
Function: Interacts with the two-component regulatory system DevR/DevS (DosR/DosS) involved in onset of the dormancy response. Required for full induction of the DevR (DosR) regulon; required during early adaptation to anaerobiosis, to start induction of the DevR regulon (By similarity). May act as a direct hypoxia/oxygen sensor (By similarity). May be the secondary sensor for CO (By similarity). Donates a phosphate group to DevR (DosR) (By similarity).
Sequence Mass (Da): 62169
Sequence Length: 573
Subcellular Location: Cytoplasm
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Q9VZZ9 | MDRTFYEGWLIKSPPTKRIWRARWRRRYFTLKQGEIPEQFCLEYYTDHNCRKLKGVIDLDQCEQVDCGLRLENRKQKFQYMFDIKTPKRTYYLAAETEADMRDWVNCICQVCHLHDTKQSNELPLGAVGADENRTQHTSSSGGLSNSTQNTTTTSLHSSAGTTAPQASVPNAGGSAQLRRPAVIEEQPMPSNAGNNNSDSVYVNTEYSNRETMLCDANFDQQELLSAAQQQPPPSPATALYLNHSALIQAQAAAAAAEQLQQQQQQAARLAVSANGVVRKLPEHLVLTQQTLAEAAAQQHSSVQASPALSTASGPYIPISECFSGSPRFLPGVPLPGADLAIPNNPTTPLNNLDPKFYDTPRSHNNIGLNLTNDQSYSPKITNLSLQQLANNNASKQRSDSDSESVFTDDDEWAHPLPLRENVDRSTRPSDSSIENESFVLTYSQRFSKMPEEGGAIVPPAEKSSKLAGAASLPEAGDQGTLDKLAKVLKNKNNLILDFKENEKIPRDLPQLSDTENTSPAIVARRNAHSAFIEESYDIPRSHQQPYYNVNQLLGERPVTSPHNSNPIAASTPNLMAADLGAVAAISAAANPGLMGEAQAVASSPTSARTLPRHCYTNAAPTKMEGNVFRYDFMEQADCPPVNRKLKPKVAGGLPVVEDKPPEEFPAKPPVGVDQLTNKLGAAQLQQPIGPPSVDRKCKPNAYKLGNSATMSPATRRSSGAPLSMVLPHETDVHSPAAANAFFHETRTLPRQQHRHHPNSPGSMSVQHQRTASAAAAMMSLTAAAAPKQQAAAQTEHKLQYFDLDVTNKPPLLNRSSMSVGNLYSQGGNGASGMRFAGVEAGGARAPVPSSVVYRSVDFVKTEAFKRIREERESSGNK | Function: Essential component for signaling from various receptor tyrosine kinases such as Sevenless, TORSO and DER. Required for photoreceptor cell and wing development.
PTM: Phosphorylated on Tyr-801 and Tyr-854 in response to sevenless activation, which initiates the recruitment of the phosphatase CSW.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 95536
Sequence Length: 878
Subcellular Location: Cytoplasm
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Q6AW06 | MSEADAGARDESPSRTAEEPAAAMRIKEERRSSSVDVVDVGNGELLVLHSIFYQGKTLRLPGNRAHMYPVVFQMIKGVCSLVKQLVVAFPKGWDQNTPSISEIAALTKSFNRVAKPFASNWSGSYNTDTLKEWGEPNCSAEVAKAITTYAYECAVPRPADLNQHYKSFTSETYGETNPEQLISIIDELNIGPQDVFVDLGSGIGQLVCLTAAYAKCKKSVGIELSQVPSNFAQDLAGYFKKFMSHFGKNHGKFEHIQGDFLNPKFKQLICEEATVIFINNFAFDAALMLRINTELLQDLKHGTRIVTTKELGTNKKEITFRSTSDINAISHTTELKTTESAVSWTSSHVKFWLTTIDHTKLIKYYEDQRRRQEVKSSREGSEISDGRDMGLKKRKSQRESSVHPDKLQKTEQAAASSHQSPKWNEPDTDYTPPAKKPKKEKLLREQQDATPASSHHHGASSSSGKDREKEKEKKKNKIYEEKKVKTPKPPKSSSSRYSSETPTSHHHHHRSNSISHSSDVIRPSQPKATAPPPPLVPAPARATASTPPPAPPAARAQSPKREEPLEPPTDLIHHGGGQLDAKTMNALHTIREAATTSAQAAAIQDAINSVLSQPTEASPSAFGPPLAHLPAPVAIYPTPPPPPAPAPAAPQQASAAPAAPNVMPVCTEIAAEQRHTFMIPPTDPFYNMIVSYYFAMKQFCNQSKTADPEFVGRLRLDIEAEEARRAELKESITLTSTQIDELLATGVNTLKSRLDELGMPSVTDVTELLAGSKQIVTQHKGLTNTVAQMENSVAVEEQKLRLIGGPDAVRYFDEAMSHPNVDIAKLTDLVITTRPPNFVAQILLPDDSPTASIDSKVSPSSSSSRRPRQPKPRANNTAAGAGGGGKRGTSGGRKSDGGGGGGATEDVELEIRQFVQHALKVDNAVKEKERKARGNFMAAAADRIPR | Function: Histone methyltransferase, which in complex with zfp-1, methylates 'Lys-79' of histone H3 to activate transcription (Probable). During stress, the zfp-1-dot-1.1 complex also plays a role in the deubiquitination of histone H2B sites, which negatively modulates the RNA polymerase II-induced transcription of highly expressed genes . Involved in controlling tissue-specific gene expression, particularly in the epidermis .
Catalytic Activity: L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(79)-[histone H3] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 103206
Sequence Length: 946
Subcellular Location: Nucleus
EC: 2.1.1.360
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H1VM35 | MSEPHFKVIIVGGSITGLTLAHSLHKIGVDFTILEKRATVTPQEGASVGILPNGARVLDQLGLYGLVEEATAPLGATHIHFPDGFHFCSLYPKSMLDNFGYPVAFLERRRLLEVLYNALPDKSKVLVNKTVSDIEQCEDGKSAGVKVRTADGDVYEGDIVVGADGVHSRTRSELWRMSSSAGQSEDVRMEKARMSAEYSCVFGISRGPSGLKAGEQIMRMYDGRTLVVIPSKDDVVFWFLSRKLGKKYKYSEAPRFTLEDAAAECAELADAPLGNDVRFGDVWKIRQTFNMVVLEENLLRTWSFGRVLCIGDSIHKMTVNLGQGANCAIEDVAILTNLLSQCLGSKREAKPSGQELDALLRRFNDVHLSRVSHIYDTSWLIARVHARDGFVRKIIGRYVMPYFGHKFESRPFNMIANAAALEFLPLPRSSFPGWEKYKSKEDKSGSWAVVSRSVLLLVGLAILSTWWRRA | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the diterpenoid pyrones higginsianins A and B . The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpchA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpchD through the action of the prenyltransferase dpchC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpchE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpchB (Probable). The short chain dehydrogenase/reductase dpchG then oxidizes the 8S hydroxy group to a ketone and the short chain dehydrogenase/reductase dpchH reduces the ketone to the 8R hydroxy group to yield higginsianin B . Finally, the FAD-dependent oxidoreductase dpchF converts higginsianin B into higginsianin A .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 52266
Sequence Length: 470
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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H1VQW0 | MKLSFIASPVWALALAQFAAATQVKIDVDVAIFGGGSAGIHAAIQLRDAGATVAVIEKKSQIGGHAETYTDPQGKSTNVGVVVFDNIEVASNYFARLNVSIVRGSPLGTAGPTYTYDFTSGAQIPAVNTSAEAQQQLTAALQSYSTNVLSKYPWIDEGFLVPDPVPEELTIPFGELAQKYNFTALMPTIAMYNYFTGDLSTIPSLYGIKGLGQGALKNLFGSFILPASGKTRDLYDAAAIELGNSVLLNADVVKVQRDVRINSTTTGVTVLIQQPGQPPKLIRARKLLVAAPPTLENVGAFDLTAEERGLISKFSSLGCWASVANVPGLNVTLKNYGVHMPYNQPSIPGPYGFVAYGSPNNFLVTVGLPDAANTAAKGEAVVRQSLATLSAVGAVPADALEKLTFPFSAVHSPYSLRVSAEEIKAGFYSKFLALEGARNTYWTGAVWAGHNSALIWNFNMGTVLPGLKKDLGL | Function: FAD-dependent oxidoreductase; part of the gene cluster that mediates the biosynthesis of the diterpenoid pyrones higginsianins A and B . The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpchA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpchD through the action of the prenyltransferase dpchC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpchE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpchB (Probable). The short chain dehydrogenase/reductase dpchG then oxidizes the 8S hydroxy group to a ketone and the short chain dehydrogenase/reductase dpchH reduces the ketone to the 8R hydroxy group to yield higginsianin B . Finally, the FAD-dependent oxidoreductase dpchF converts higginsianin B into higginsianin A .
Sequence Mass (Da): 50041
Sequence Length: 473
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 1.21.-.-
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Q9YFJ2 | MSVALSIPLLSLPEDMREALAAAAGPVYSGDRFRRQLLQTPCSGVACIGDYVSQACIATLSTAWTGPLILVVDGKTRRESWRDMVVPQGFRVHRVRSPPGSLSLEAYTTICKLMEEYGRHVVFVEGEEDLIALAALDCGIDWTVVYGLPGVGGVVVHRCLRKPGLENSSVLAFKPGTGVHHQSSP | Function: Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
Catalytic Activity: 3'-dephospho-CoA + GTP = CoA + GDP + H(+)
Sequence Mass (Da): 19932
Sequence Length: 185
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
EC: 2.7.1.237
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O29150 | MKGLRLPESMREELAKPHGKLYRGKGEKLLLEVEEISEAKPFCTVGDLVTASAIKVGLTPDLAVADGKTLREENVEFEQEAFDEVIETTNPPAHISCELISALLKALKLCEDGKKVLVFVDGEEDLAVVPLVKLLPLGALILYGQPGEGVVALKVDEEKKVLILNLLNKMEIIGECDELKYLLGGD | Function: Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
Catalytic Activity: 3'-dephospho-CoA + GTP = CoA + GDP + H(+)
Sequence Mass (Da): 20278
Sequence Length: 186
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
EC: 2.7.1.237
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A8MBP6 | MSETNHPRLILRSKRARALMALPFAISIPRDPPDSIMIARELFNDFKLSIIATVGDVVSLNVATYWRRPDLRVIDLNTRRGTVIQHSDMDGVVYRVRNERSTLSYESFNIMRSAYANVLSGNRVTIIVDGEEDLLAIPAVLEAPGNTGILYGLYTGYLVLIPAVNEYKILMLKLLTLLDRDECETLRNCNSVNNYGWKNS | Function: Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
Catalytic Activity: 3'-dephospho-CoA + GTP = CoA + GDP + H(+)
Sequence Mass (Da): 22605
Sequence Length: 200
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
EC: 2.7.1.237
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A0RW81 | MGTLILDSMVNKEAVLREAPPGTILVTVGDVTSERISGFGMTPLLQIIDGKTRRAAHEPAGPPPDVEIIRCENPAGGISPECIETIRRALGSSSPLRLVVSGEEDLLVIPACIYAPDGAVIMYGQPGRGLVAIHVDAGIRYKAKGLLDSVS | Function: Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
Catalytic Activity: 3'-dephospho-CoA + GTP = CoA + GDP + H(+)
Sequence Mass (Da): 15839
Sequence Length: 151
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
EC: 2.7.1.237
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B8D6D8 | MNKAIPVLKLPVDFRLSLSIPQGDLYVSPDRGLVYGLRADAAVGDIVSKNHMVEMRITDAKTKRHTVDVGPGECDVLVVNPQGTISINSFTSSLIGGARSICVVGEEDLLVIPFTLVRGFKIIYGQPDVGVVISSPSRERVLKILKGLKPDIVIMNL | Function: Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
Catalytic Activity: 3'-dephospho-CoA + GTP = CoA + GDP + H(+)
Sequence Mass (Da): 16965
Sequence Length: 157
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
EC: 2.7.1.237
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Q5UYR8 | MSDVVLELPSDLRHELKEPLGRIYTDTAALLADAGDPIIAVGDMVTYHLIEAGRTPDLALVDERTERSAVDADVAAAIDGFDRTLSVDNPAATLTADLLAALRDGLDSDETTLLDVDGEEDLATLPAVLAAPAGASVVYGQPDEGMVLADCDDTARDRVRSLLERMDGDAERAIALVSN | Function: Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
Catalytic Activity: 3'-dephospho-CoA + GTP = CoA + GDP + H(+)
Sequence Mass (Da): 18872
Sequence Length: 179
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
EC: 2.7.1.237
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B0R6Y3 | MSETDAAATLPADARDAFKSPIGPVYTDAAALLADATPPIIAVGDVVTYHLVDAGQTPAVAVVDGRTERDAVRPAVRDAIPEPDLTVASEPGTVSVSLVRALVDAIADADATVVSVDGEEDLAVVPAVLAAPADATVVYGQPGEGMVRVPVTDAGRAEMRERADRLETTAAFWRLVD | Function: Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
Catalytic Activity: 3'-dephospho-CoA + GTP = CoA + GDP + H(+)
Sequence Mass (Da): 18213
Sequence Length: 177
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
EC: 2.7.1.237
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Q18KI2 | MDRLPLELPSSLRQEFKSPFGPVYTDVTQFLTDAGRPIIAVGDIVTYHLQTVDYTPAVAVIDGQTKRESVDETVKAALSKHNKRIDVENQPGTISIALLEALQTAVETPESVMIVVDGEEDLATLPAVLVARPGGTVVYGQPDQGMVRIAVTPETKITMSRLLKRMDGDAAAAFDRLGVDRSGDKK | Function: Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
Catalytic Activity: 3'-dephospho-CoA + GTP = CoA + GDP + H(+)
Sequence Mass (Da): 20117
Sequence Length: 186
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
EC: 2.7.1.237
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A2BJZ2 | MYHLFHSRLCLPQGLRSLLAQRMPAAKLLPNDSAVAAYARHRRVVAVGDRVSETLIRHGVKPWVMVFDCVEARRDKTCPSIPEGYAILRTRNERSTVEPGAVEVIRKALRQGHTVVRVDGEEDLLALPALLYGDVGSVVLYGLPGKGVVAAAVNREAKLLAMRVLEFFEPC | Function: Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
Catalytic Activity: 3'-dephospho-CoA + GTP = CoA + GDP + H(+)
Sequence Mass (Da): 18896
Sequence Length: 171
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
EC: 2.7.1.237
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A8A8L4 | MRTLLASPRGALVKDDRLLPFLLRGKTLVTVGDVTTKRCLELGLVPRTAIFDGKTRRSQWVELRAPNGVLKAFNPPGQICLDAAKVVKKAILTSTWVKVEGEEDLLAIPALLSSENGWALLYGQPKAGVVLVEINKYTKLHFLEIIKMFDGDVEEFLREFDYDPNQPLLGELDERLYDLLFPEL | Function: Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
Catalytic Activity: 3'-dephospho-CoA + GTP = CoA + GDP + H(+)
Sequence Mass (Da): 20678
Sequence Length: 184
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
EC: 2.7.1.237
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B1L6M9 | MLFDLKLLEDKRGKVSEIKGSIIKSLDILENKRIISVGDRVTRELLGSGRRPEVAIIDLKERREMNCSTIFYLDDYLILVARNPAGTLMREAWLKVRKAIEISLSGKNAAVIVDGEEDLLGFPAIILPPEGWVMVYGQPGVGMVSVNIDRKAREEAMNLLQEAFLPI | Function: Catalyzes the GTP-dependent phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (CoA).
Catalytic Activity: 3'-dephospho-CoA + GTP = CoA + GDP + H(+)
Sequence Mass (Da): 18707
Sequence Length: 167
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis.
EC: 2.7.1.237
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Q9BZG8 | MAALVVSGAAEQGGRDGPGRGRAPRGRVANQIPPEILKNPQLQAAIRVLPSNYNFEIPKTIWRIQQAQAKKVALQMPEGLLLFACTIVDILERFTEAEVMVMGDVTYGACCVDDFTARALGADFLVHYGHSCLIPMDTSAQDFRVLYVFVDIRIDTTHLLDSLRLTFPPATALALVSTIQFVSTLQAAAQELKAEYRVSVPQCKPLSPGEILGCTSPRLSKEVEAVVYLGDGRFHLESVMIANPNVPAYRYDPYSKVLSREHYDHQRMQAARQEAIATARSAKSWGLILGTLGRQGSPKILEHLESRLRALGLSFVRLLLSEIFPSKLSLLPEVDVWVQVACPRLSIDWGTAFPKPLLTPYEAAVALRDISWQQPYPMDFYAGSSLGPWTVNHGQDRRPHAPGRPARGKVQEGSARPPSAVACEDCSCRDEKVAPLAP | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 . DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase (By similarity). Acts as a tumor suppressor .
Catalytic Activity: L-histidyl-[translation elongation factor 2] + S-adenosyl-L-methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 48134
Sequence Length: 438
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Nucleus
EC: 2.5.1.108
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Q5NCQ5 | MAALVVSETAEPGSRVGPGRGRISRGRLANQIPPEVLNNPQLQAAVQVLPSNYNFEIPKTIWRIQQAQAKKVALQMPEGLLLFACTIVDILERFTEAEVMVMGDVTYGACCVDDFTARALGVDFLVHYGHSCLVPMDTSVQDFRVLYVFVDIRIDTAHLLDSVRLTFTPGSSLALVSTIQFVSTLQAAAQELKADYHISVPQCKPLSPGEILGCTSPRLSKEVEAVVYLGDGRFHLESVMIANPNIPAYRYDPYGKVLSREYYDHQRMQATRQEAIAAARSAKSWGLILGTLGRQGSPKILEHLESQLRNLGLPFVRLLLSEIFPSKLSLLPEVDVWVQVACPRLSIDWGSAFPKPLLTPYEAAVALKDISWQQPYPMDFYSGSSLGPWTVNYGRDRAPRGLCQPASDKVQQGSRGGSPAPACESCNCADQKATSPAP | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 . DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase (By similarity). Acts as a tumor suppressor .
Catalytic Activity: L-histidyl-[translation elongation factor 2] + S-adenosyl-L-methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 48004
Sequence Length: 438
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Nucleus
EC: 2.5.1.108
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A7SLX5 | MADSVEQSSVTTKRISAKGARKRFVGTKSASGKHSQGVDRVGSAAHRPVNQIPEEILKDTKLQEALPENYNFEIHKTIWRIQQVKAKRVALQFPEGLLLFACTIADILESFTGCETVIMGDVTYGACCVDDYSARALGCDLLVHYGHSCLVPIDATAGIKMLYVFVDIKIDTAHFVESVRFNLGAGSCLALVSTIQFVAALQAASNELSKDYQVEIPQCKPLSPGEILGCTAPMLKDKDAVIYLGDGRFHLEAVMIANPAIQAYRYDPYDKTFSKEYYDIDKMHEARQTAIKQASLASKYGLILGTLGRQGSPKVLQTLEKQLQSLNMDYIIVLLSEVFPDKLKLFKDVDAWVQVACPRLSIDWGTAFPKPLLSPYEASVALQSVAWQQSYPMDFYAYSSLGGWTPNNESNRPTPANRRKKNLHTEVIIDNVSDSKPVIKESECGSGETCCGKCTKETDKHSSTP | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 (By similarity). Dph1 and dph2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising dph3 and a NADH-dependent reductase (By similarity).
Catalytic Activity: L-histidyl-[translation elongation factor 2] + S-adenosyl-L-methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 51299
Sequence Length: 465
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
EC: 2.5.1.108
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Q3T7C9 | MNMEEDTQSKEIVVAPKKEKKVFRPARSVIKGVPAEIEKDPKLQKAIEVLPSNYNFEIPKTIWRVKQANAKHVALQFPEGLLLFATSIADIIETWTEAETTIMGDVTYGACCVDDFTARAVGADFMVHYGHSCLVPIDQTGSIPCLYVFVDIQFDTVHLIDTIKSVFPSTVPLALVSIIQFVSSLQKMAQDLKSCGYTVCVPQCRPLSPGEVLGCTSPPVPEGHTIVCLGDGRFHLESIMISNPEVPTYLYNPYSKVLSREYYDQPLMKKIRKEIIDKASTAKKWGLILGTLGRQGNTKVMENLKNQLEAAGKDFVIVLLSEIFPAKLEAMSDVEAWVQVACPRLSIDWGASFPRPLLNPYEATVALKHAEWHAQRYPMDFYANESLGEWTPNHKPPCPCGQTRNTGCKGLRCPSSKQGSNKD | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 (By similarity). DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase (By similarity).
PTM: Polyubiquitinated by white spot syndrome virus E3 ubiquitin-protein ligase WSSV222. This targets the protein for rapid degradation via the ubiquitin system.
Catalytic Activity: L-histidyl-[translation elongation factor 2] + S-adenosyl-L-methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 47024
Sequence Length: 423
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
EC: 2.5.1.108
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O59713 | MAEVKKSIPKRRFVGKKNRKENNLDGSNRDVENAALVTINSKRSAGRVATQIPEDILNDKAINEAIKLLPQNYNFEIHKTIWHIRLRKAKRVALQLPEGLLMFGCILSDIFEQFCQVETIVMGDVTYGACCIDDFTARALDCDFLVHYGHSCLIPVDQTPIKVLYVFVDIKIDLQHVVSSLKHNLPSNSRLALVGTIQFVGSLNSIKDALQIQDEDGKGGFYVVIPQAKPLSPGEALGCTSPYIEKGSVDALIYIGDGRFHLESVMIANPDLPAYRYDPYSHKLSIESYAHEEMKSIRYSAVEKARTAKKFGLIQGTLGRQGSPKVLENLKNTLRKNNKDFVCVLMSEIFPSRLGQFSDIDAWIQVACPRLSIDWGYAFPAPLLTPYEASAAFNVVPWKEVYPMDFYATNSLGNWTPNNPENRPLPNRKKTGPVSS | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. Dph1 and dph2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising dph3 and a NADH-dependent reductase, predominantly cbr1.
Catalytic Activity: L-histidyl-[translation elongation factor 2] + S-adenosyl-L-methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 48795
Sequence Length: 436
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.108
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Q4PA25 | MQSNAENPRKRFTATSPNGNRQNVSVDTSSNVAGPSRPRIANAVPAEILDDPALNQAIKSILPSNYNFEIHKTIHHIRKASASCVALQMPEGLTLWATGIADIVERFTDATTVIMGDVTYGACCVDDYTAMALGCDMLVHYGHSCLVPVDQTAIKTLYVFVEISIDPAHLAATIRANFPNDRHDFRAKILGGSQSAAGKRSEVDESAGRAQIQIGEQASVASGAPPSTLTHLALVGTVQFINAINGLREALRQQQHRLADGQIVSTESPVDRLMLTAGTASSAPVQHITQAAKWKAWSSGEYKVTVPQVKPLSPGEVLGCTSPKLDKDEIDAIVYIGDGRFHLESIMIANPRIPAFRYDPYTKRFVRELYDHAEMRRMRGEAVRLAQDSVGGLDLDPETSIVKKNKAVVVDAEKDRVTASGWGVLLGTLGRQGSLRVLESLSASLSEHVPPIPHVPILLSELSPQKLGLFGEHLAAFIQSSCPRLSIDWGSAFAKPLLSPYEAAVSVKKVKGWQEDVQGLGMSRTPAKQQQDGNGNGSDAVPAEDKHLPLDGDYPMDFYSDTSLGPWTPRHGMAPAKKPVGAKSNLALLRSLRSKRAKASSTPTSAATA | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase, predominantly CBR1.
Catalytic Activity: L-histidyl-[translation elongation factor 2] + S-adenosyl-L-methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 65549
Sequence Length: 609
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.108
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Q6GPQ5 | MEPERNESGTPSVAVTPAAPINAGRAPVRRVANQIPDEIAHNPLLLEAMKVLPENYNFEIPKTIWRIQQASAKRVALQMPEGLLMFACAIADIIERFTSAETVVMGDVTYGACCVDDYTAQALGADFMVHYGHSCLIPIDATHGVRMLYVFVDIKIDTSHFVDTIRFNFQAGASLALVSTVQFVSALQAARQALQTDYNVTVPQCKPLSPGEILGCTSPRLNKSVDAVVYLGDGRFHLESVMISNPDTKAYRYDPYSKVFSREYYDHSTMLRHRGEAISVATNAKTWGLILGTLGRQGSPKIMEHLESRLQALGCRYVRLLLSEIFPNKLKLFAEVEVWVQVACPRLSIDWGTAFSKPLLTPYEASVALKEAEWQLTYPMDFYANESLGPWTVNHESHRPTRATVRRTQKPEQRKLQCTDVGATVEECPCQEKVETKTE | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 (By similarity). Dph1 and dph2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising dph3 and a NADH-dependent reductase (By similarity).
Catalytic Activity: L-histidyl-[translation elongation factor 2] + S-adenosyl-L-methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 49004
Sequence Length: 439
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Nucleus
EC: 2.5.1.108
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P40487 | MSGSTESKKQPRRRFIGRKSGNSNNDKLTTVAENGNEIIHKQKSRIALGRSVNHVPEDILNDKELNEAIKLLPSNYNFEIHKTVWNIRKYNAKRIALQMPEGLLIYSLIISDILEQFCGVETLVMGDVSYGACCIDDFTARALDCDFIVHYAHSCLVPIDVTKIKVLYVFVTINIQEDHIIKTLQKNFPKGSRIATFGTIQFNPAVHSVRDKLLNDEEHMLYIIPPQIKPLSRGEVLGCTSERLDKEQYDAMVFIGDGRFHLESAMIHNPEIPAFKYDPYNRKFTREGYDQKQLVEVRAEAIEVARKGKVFGLILGALGRQGNLNTVKNLEKNLIAAGKTVVKIILSEVFPQKLAMFDQIDVFVQVACPRLSIDWGYAFNKPLLTPYEASVLLKKDVMFSEKYYPMDYYEAKGYGRGETPKHAIE | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 . In association with DPH2, transfers a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising KTI11/DPH3 and a NADH-dependent reductase, predominantly CBR1 .
Catalytic Activity: L-histidyl-[translation elongation factor 2] + S-adenosyl-L-methionine = 2-[(3S)-amino-3-carboxypropyl]-L-histidyl-[translation elongation factor 2] + H(+) + S-methyl-5'-thioadenosine
Sequence Mass (Da): 48311
Sequence Length: 425
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Cytoplasm
EC: 2.5.1.108
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Q757B6 | MSEAALVPPALSTNQTEETFNFQQYELLRQDRAAHLGPGITDLASLKERIRSYYAIESLADHLNSHAEYRSITLQFPDDLLFDSALVAEELQALLPDLQCARTDAPAQADTTCSCGTQKTCADSKDSADGRKIWILADTAYSPCCVDEVAAEHVQADVVVHFGDTCLNPVETLPVVYIFGEPYLDRAKVISLFTERYDKDAKVCLMANAPYSRHLESLSGELSQLGYSNLVFTDVALPDTPNAAATILGVSDSHPISHKLYASGDRVYYGAKEQLLCEEQLQSFELFHIGLPPDPRLLFLSTKFQGVTAYDTQKRQIAKGPFPAMMRRYRFMHVARTASTIGILVNTLSLKSTRSLISSLVELIRSCGKKHYMFVVGKPNVAKLANFEPVDVWCVLGCGHGGIVLDHANEFYKPIVTPYELTLALAPELSWTGAWVVDFNTVIDGISADLGLQAGAIPAENVPEFDAVTGKYVGNSRPLRELNHLEIESPQESITTGSTELVKKFSGALTIGSTVSTSAQFLQARQWTGLGSDFNAEDSYEEEGATVEEGLSGVARGYQYDVSNAEHTDADVPKTSGRVMNT | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the DPH1 subunit.
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase, predominantly CBR1 (By similarity). Facilitates the reduction of the catalytic iron-sulfur cluster found in the DPH1 subunit (By similarity).
Sequence Mass (Da): 63662
Sequence Length: 582
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Cytoplasm
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Q4WN99 | MATEMQAAPVLSTPDSLILEATEPVARQNATRTLSDEELSITYDIERTLQEIRQARYKRIALQFPDDMLPDAPRVFQLLSRGLACRDVDKITVEKNGNGTGGVESEKLAQDVSQLSVDDKPEPEPKLYILADTSYGTCCVDEVAAEHVNADVVVHYGRSCLSPTARLPVIYVFTHKELPIEPVIQAFKATYPDQATKIILAADVTYCDHIPAVYARLMEEGYTNLYATELIHCPSSAIPNRTVPDSVRENPDTLSEWQLFHISDPPTALLLTLASRVAAIHIYPTTDAPSDNVKPLPVSTSAALGRRYAILTRLSTVPIFGILINTLSVKNYLHIVEHVKQKIADAGKKSYMFVVGKLNAAKVANFSEIGGWVVIGCWESSLVDSKDFWKPVITPFELELALKGDHERVWTGAWQSDFQSILDQPAEEAQTADHEESPNDDDDMSEPESAPPEFDLRTGRYVSHTRPMRNPAPRVSAQSDDAVSAASGPAAARALARRAKGELAMIGGTVSPGAEYLRSQRTWKGLGSDFDIQYDDEDPSDSTLVVEGRKGIARGYTVGDSIEKH | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the dph1 subunit.
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. Dph1 and dph2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising dph3 and a NADH-dependent reductase, predominantly cbr1 (By similarity). Facilitates the reduction of the catalytic iron-sulfur cluster found in the dph1 subunit (By similarity).
Sequence Mass (Da): 62076
Sequence Length: 565
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
Subcellular Location: Cytoplasm
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Q09454 | MTESAPSAFFTTSTPADHVHEEESSNTGYFENLPENDIHSFFEIDATSEWIKQGNHQRIALQFPDSLLPYSEKVTKLIESRFRSESAKKTFVLADTSYRSCCVDEVAAAHADCTALVHFGEACHSAPTDKIDVKYVLGSMPIFIDQFRMEFQNVADQLTAEHIVLLMDSCFSHEQEKVAAVIKEVLPGNRHVECSLLPSEDVLKQNRQNIYLGREIPSCLRNNQPTDLIFCGFPNSPLLPIWLLSYPSCSTVSHFNPINKTIQHESTRSSRLLRKRLFLVEKLKDADTVGLVVGSVGVDKHREAVKRMREMCKKAGKKIYVISVGKINVPKLSNFSTDIDVFVLLSCPFGVVLDSSDYFRPVVSYFEAEIALNPAKTWAADFGWSAEFAAFLEDKIETEVPDDKAAGDFSLISGKVRVQKTEEEKNGDGPSSVAIYNPGYCNDRTWKGLNDGVSTAEDSTKMGEGRSGIAQGYSGK | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the dph-1 subunit.
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 (By similarity). Dph-1 and dph-2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising dph-3 and a NADH-dependent reductase (By similarity). Facilitates the reduction of the catalytic iron-sulfur cluster found in the dph-1 subunit (By similarity).
Sequence Mass (Da): 52955
Sequence Length: 476
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
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Q5ZKI2 | MAAAFSSDGEAVLRRTLDPAAAAPRGDKDEFYEVDRAAAFVRDGGFRKVALQFPDALLADAAAVAARMEEVTGAEMYVLGDTTYGSCCVDEVAAEHVSAGAVVHYGPACLSPCRKLPVLHVFGRQPLDVGRCAEVFRELYPERQSRVVVLSDVVYAHAMGELEKQLCHEYPNIIFSEVVCGDAPSPTLPGEVRQFGRRFHMEAAEELQDCSMFYVGAEGLALTSFMLTWNRFPFSSFDPATGHGRRETLNVNRALMRRLYLVERARDAHVVGILVGTLGVAGYLDVLEHLHQLVRRAGKRSYTLSVGKPNPAKLANFLEVDIFVLVACAQNSLLDSSEFYRPIVTPYELELACNPAREWTGNYLTDFRDLLPGACAHIELPPAVPAAEAIPDVSLITGEMRATHLCDPLAPQPPSSTTLACRDQTRALAEMSPAATFLESRSWRGLEQQLGKTAVSKAVQGRRGIAIAYEDEGREQS | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. The cluster facilitates the reduction of the catalytic iron-sulfur cluster in the DPH1 subunit.
Function: Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2 (By similarity). DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase (By similarity). Facilitates the reduction of the catalytic iron-sulfur cluster found in the DPH1 subunit (By similarity).
Sequence Mass (Da): 52163
Sequence Length: 477
Pathway: Protein modification; peptidyl-diphthamide biosynthesis.
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K2QVI4 | MESSSSKGGFKVLIIGGSVTGLTLAHSLDKMGVDYRLLEKRKEIAPQEGASIGILPNGARILDQLGLYNAIEQSAIALGTSDVYFPDGFHFTSSYPKRMHDRRSFAYPIAFMERRKLLEILYDLLPDKSRVEVDKAVSRIEEHPEHHGVLRAYTHDGDVYEGNLVVGADGVHSRTRREMWRLSGSSPTGDVPVSERNSTSVEYACIFGISDGIAELTPGRQVMRFGNGWTLAVIPSRQGQVFWFIVQKLDREYQYGSAPRFAPEDAAEQCSKLARLPIHGDVRFDDLWQRRKAVNMAALEENVFQTWSCGRLVCIGDSIHKMTVNLGQGANCAIEDVAVLCNILHHALNEKANSELSDQDVEALLRRFHKEHFPRVSRVYDMSWSVTRVHARDGSMRKFVGRYVAPYFGERLQGRLFNLMADAAKIDFLPLPRASRSGWEEYRSSERNALLWASSLALLIVLIALFTGRSYW | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of diterpenoid pyrones . The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpmpA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpmpD through the action of the prenyltransferase dpmpC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpmpE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpmpB (Probable). The short chain dehydrogenase/reductase dpmpG then oxidizes the 8S hydroxy group to a ketone and the short chain dehydrogenase/reductase dpmpH reduces the ketone to the 8R hydroxy group to yield higginsianin B . Higginsianin B is further methylated by the methyltransferase dpmpI to produce the intermediate named FDDP B . The cytochrome P450 monooxygenase dpmpJ then oxidizes the C-26 methyl to primary alcohol, producing the final diterpenoid pyrone with a C-26 primary alcohol on the gamma-pyrone moiety named FDDP C .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 53143
Sequence Length: 472
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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K2RLM6 | MSASSTEATNLAGKTCLITGGAGGLGRALAAAFLRAGANVAICDLNEERLKQASAELSGTGAGSLLAANADVADPAAAQQLFDRITAKFRTVDVLVNNAAIMDRFDPVADLDHELWDRVISVNLAGPFIFSKLALRVMLQQPKPDGCILNIASGAAKGGWLAGRCDLGLARICRG | Function: Short chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of diterpenoid pyrones . The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpmpA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpmpD through the action of the prenyltransferase dpmpC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpmpE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpmpB (Probable). The short chain dehydrogenase/reductase dpmpG then oxidizes the 8S hydroxy group to a ketone and the short chain dehydrogenase/reductase dpmpH reduces the ketone to the 8R hydroxy group to yield higginsianin B . Higginsianin B is further methylated by the methyltransferase dpmpI to produce the intermediate named FDDP B . The cytochrome P450 monooxygenase dpmpJ then oxidizes the C-26 methyl to primary alcohol, producing the final diterpenoid pyrone with a C-26 primary alcohol on the gamma-pyrone moiety named FDDP C .
Sequence Mass (Da): 18066
Sequence Length: 175
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 1.1.1.-
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K2RU68 | MSAIGHSPTACSRCSRPRLRRKDLTSVLSPRLPCFKVSSSGEAFATDKADFITPKDLDDPCASPGWEASSLAQAKRYGKSKMANVLFAAELQRRMDAEGVDIISISLNPGPVKTQGAADVLPFMVRPMVWLFFKDPAEGAQTTLFAAAAAEIREEKERWKGGYLDGPGKLKSPSPRARDPQVAYNLWHTTESAVRAIGVLDKS | Function: Short chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of diterpenoid pyrones . The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpmpA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpmpD through the action of the prenyltransferase dpmpC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpmpE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpmpB (Probable). The short chain dehydrogenase/reductase dpmpG then oxidizes the 8S hydroxy group to a ketone and the short chain dehydrogenase/reductase dpmpH reduces the ketone to the 8R hydroxy group to yield higginsianin B . Higginsianin B is further methylated by the methyltransferase dpmpI to produce the intermediate named FDDP B . The cytochrome P450 monooxygenase dpmpJ then oxidizes the C-26 methyl to primary alcohol, producing the final diterpenoid pyrone with a C-26 primary alcohol on the gamma-pyrone moiety named FDDP C .
Sequence Mass (Da): 22081
Sequence Length: 203
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 1.1.1.-
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K2RGJ8 | MVAETGTGLFSAHKITEELASTSLDSGVHLLFDIHDRTFQALPDFLAEHRYQEVNDIRNTVFQKAFDTNLSIYEYLVHHPQLQAHMQDAMKLHQPEGDWLSVFPADEIVGNQQTAPDPARVLFVDIGGGMGQQCIRFRERYPDLAGRVILQDIPQTINRVPKPMPNGIEAVPHSFEDPQPIKSKSPRLDNLARERL | Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of diterpenoid pyrones . The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpmpA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpmpD through the action of the prenyltransferase dpmpC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpmpE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpmpB (Probable). The short chain dehydrogenase/reductase dpmpG then oxidizes the 8S hydroxy group to a ketone and the short chain dehydrogenase/reductase dpmpH reduces the ketone to the 8R hydroxy group to yield higginsianin B . Higginsianin B is further methylated by the methyltransferase dpmpI to produce the intermediate named FDDP B . The cytochrome P450 monooxygenase dpmpJ then oxidizes the C-26 methyl to primary alcohol, producing the final diterpenoid pyrone with a C-26 primary alcohol on the gamma-pyrone moiety named FDDP C .
Sequence Mass (Da): 22191
Sequence Length: 196
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 2.1.1.-
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K2RLM2 | MLQLILHHPYASLAAGILLYFFCLATYRLYLSPVAGFPGPRLAALTRFYEYYYDGVKGGQFVWKVKDLHQKYGRLSCSTVVGQELKLEQGPIVRIGPCELHVNDPTFVSTLYPATGQRRNKDPFWTDQFGPKTAFGTVDHDHHRLRRGPFNRFFSKANVTRLEPMLRQQANKLCEKLEKYAGTGRVIDLSDPFGCMATDIISTYALGYSFNFLDAEDFQPNLLQGLNGFTPLAPTVKQFPWLLKLLRALPDSWALKINPKIAPFLDFQRTMKKVITDVEAEVQSEAGRPKADQATTIFHEVLRGDIPPEEKETARLWQEGEAIIGAGTFLQTPQEAV | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of diterpenoid pyrones . The first step of the pathway is the synthesis of the alpha-pyrone moiety by the polyketide synthase dpmpA via condensation of one acetyl-CoA starter unit with 3 malonyl-CoA units and 2 methylations (Probable). The alpha-pyrone is then combined with geranylgeranyl pyrophosphate (GGPP) formed by the GGPP synthase dpmpD through the action of the prenyltransferase dpmpC to yield a linear alpha-pyrone diterpenoid (Probable). Subsequent steps in the diterpenoid pyrone biosynthetic pathway involve the decalin core formation, which is initiated by the epoxidation of the C10-C11 olefin by the FAD-dependent oxidoreductase dpmpE, and is followed by a cyclization cascade catalyzed by the terpene cyclase dpmpB (Probable). The short chain dehydrogenase/reductase dpmpG then oxidizes the 8S hydroxy group to a ketone and the short chain dehydrogenase/reductase dpmpH reduces the ketone to the 8R hydroxy group to yield higginsianin B . Higginsianin B is further methylated by the methyltransferase dpmpI to produce the intermediate named FDDP B . The cytochrome P450 monooxygenase dpmpJ then oxidizes the C-26 methyl to primary alcohol, producing the final diterpenoid pyrone with a C-26 primary alcohol on the gamma-pyrone moiety named FDDP C .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 38103
Sequence Length: 337
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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Q42546 | MAYEKELDAAKKAASLAARLCQKVQKALLQSDVQSKSDKSPVTVADYGSQAVVSLVLEKELSSEPFSLVAEEDSGDLRKDGSQDTLERITKLVNDTLATEESFNGSTLSTDDLLRAIDCGTSEGGPNGRHWVLDPIDGTKGFLRGDQYAVALGLLEEGKVVLGVLACPNLPLASIAGNNKNKSSSDEIGCLFFATIGSGTYMQLLDSKSSPVKVQVSSVENPEEASFFESFEGAHSLHDLSSSIANKLGVKAPPVRIDSQAKYGALSRGDGAIYLRFPHKGYREKIWDHVAGAIVVTEAGGIVTDAAGKPLDFSKGKYLDLDTGIIVANEKLMPLLLKAVRDSIAEQEKASAL | Function: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. May regulate the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS. May play a role in the biosynthesis of sulfate conjugates and RNA processing. Is also able to hydrolyze inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate. Could be considered as a negative regulator of abscisic acid (ABA)- and stress-responsive genes, through modulating the inositol 1,4,5-trisphosphate (IP3) turnover. Is also involved in salt tolerance. Acts as a suppressor of virus- and transgene-induced silencing.
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
Sequence Mass (Da): 37564
Sequence Length: 353
Pathway: Signal transduction; phosphatidylinositol signaling pathway.
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O49623 | MSYEKELAAAKKAVTLAARLSQEVQKTLLQSQVWKKSDRSPVTAADYGSQAVVSLVLERELQPDKLSLVAEEETGDLRKNGSEAFLEDIAKLVKDTLASEESYTSSPLSTDDVLNAIDCGKSEGGCKGSHWVLDPIDGTRGFVRGEQYAVGLALLVEGKVVLGVMACPNLPLASAVCATDNSSQEDVGCLFFATTGSGTYVQSLKGNSLPQKVQVSSNENLDEAKFLESYHKPIPIHGTIAKKLGIKALPVRIDSQAKYAALSRGDAEIYLRFTLNGYRECIWDHAPGSIITTEAGGVVCDATGKSLDFSKGKYLAHKTGIIVTTKKLKPWILKAVRESIEEENLYF | Function: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. May regulate the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS (By similarity). Prevents both the toxicity of PAP on RNA processing enzymes as well as the product inhibition by PAP of sulfate conjugation. Is also able to hydrolyze inositol 1,4-bisphosphate .
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
Sequence Mass (Da): 37509
Sequence Length: 347
Pathway: Signal transduction; phosphatidylinositol signaling pathway.
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Q8GY63 | MSYDEMLSAAKKAVSLAARLSNEVRKSLLVTDVWNKSDDSPVTVADYGSQAVVSLVLERELQNEPVSLVAEEDSGELRKIAAETVLARITELVKDTLASDESYAIASPLTSDDVLNAIDRGKSEGGPKGRHWILDPIGGTRGFIRGEQYAIGLALLVEGKVVLGVMACPKLPLASTAGNALKSLPEKVGCLFYGSVGNGTYVQSLSVDSLPAKVEVSSIDDPAKASFFESYHTPVPIHNTIATKLGIKESPIKINSQTKYAALSRGDGEVYLRFTRKARPESIWNHAAGSIIVSEAGGKVTDAAGNPLDFSKGKYLDYKRGIVVTTQKLLPRLLTAVRESIKEEEEEEEKAASLKLH | Function: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Is also able to hydrolyze inositol 1,4-bisphosphate.
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
Sequence Mass (Da): 38385
Sequence Length: 357
Pathway: Signal transduction; phosphatidylinositol signaling pathway.
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Q84VY5 | MPYEKELAAAKKAVSLAARLSQEVQKSLLQSDVRSKSDKSPVTAADYGSQAVISHVLERELHPEPLYLVAEENAEDLHKNGAEEFLESITKLVNNALASDDSYANSSLSMDDVRKAIDHGRSQGGSSGRHWILDPVDGTRGFVKGEEYAVALALLVEGKVVLGVMACPKLENHKSSSSGCLFFATVGEGAYVQSLEGDSHPPQKVQVSNIENPEEATFVESSHKPIPIHSSIANKLGIKAPPLRIHSQVKYAALARGDAEIYLRFTLKGYREFIWNHAAGAIITTEAGGVVCDADGNPLDFSRGNHLEHKTGIVVSTKNLMPRLLKAIRESIEEEMLLSETQLKL | Function: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Is also able to hydrolyze inositol 1,4-bisphosphate.
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
Sequence Mass (Da): 37489
Sequence Length: 345
Pathway: Signal transduction; phosphatidylinositol signaling pathway.
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Q9M0Y6 | MYILDTGARFSAVRFSPVFNPPPTSLRRRYFIVRANLPFPKHQAKYHKELEVAIDAVDRACRLCVDVKRSLFSSKEKIVEKNDQTPVTIADFGVQALVSLELSKLFPSIPLVAEEDSHFVRANNLVSSVVSEVKSKASIGDNHLSDADVLEAIDRGGKDAYTFCNKPATYWVLDPIDGTRGFLKGDEALYVVGLALVVDNEIVLGVMGCPNWPGDSSDGSTGTLMLSHIGCGTWTKKLQNVSGNVAGDWIRCFVDACVLMNKARFCIQESQTWESLPLSGFFDASTVSEDLKHKEILLLPTCCGSLCKYLMVASGRASVFLLRAKTQRTIKSWDHAVGIICVHEAGGKVTDWEGDEINLEEDQSERRLIFPAGGVVVSNGSLHNQILEMISSASPTL | Function: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP.
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
Sequence Mass (Da): 43531
Sequence Length: 397
Subcellular Location: Mitochondrion
EC: 3.1.3.7
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Q55F34 | MSLCNLAKIRSVAIKAVEKACIACLDIQKQLISEDTINKKDQSPVTVGDYTVQALVINELLKGLDEEYPIIAEEDSKTLSSQKDVESKVLSFFNRYSNESFVESQLSSLLDKGNKKKDLNSSNRWWTLDPIDGTLGFLRKDQYAVALALMEDNKPILGILGCPNLPVSKGSTEKGCIFVGLKNKGSFMIKLSNLDQEEPIKVSNQSDPTKAIFTESFVSRGFGHELNQKISNSMGVTAEPLKIDSQCKYAMVARGDSDCYLRLTQLDYKECIWDHAAGHIIVEEAGGIVTDFKKQQLDYSKGFKLENNVGIVCSNKLLNDSLFDSIKKSIQF | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Regulates the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS. Is also able to hydrolyze inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate (By similarity).
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
Sequence Mass (Da): 36888
Sequence Length: 332
EC: 3.1.3.7
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Q5BCG1 | MSYERERYIAELAVQRATILTQKVFNEKAKGTVSKDDKSPVTIGDFGAQALIIQAIRKNFPNDEIVAEEEASTLREDKALSAEIWRLVKDIKLEDAESNELLGGSLPSEEAMLDIIDEGKSAGGPKGRIWALDPIDGTKGFLRGGQYAVCLGLLEDGDVKVGAIGCPNLPVDDAATISSSIGVDQNSGAGNGVLFSAIKGAGSVSRPLTSGARAESKSISMRPVPDIAQAVFCEGVEAGHSAQGDNAAVAQLLGITSPSVRLDSQAKYCSIARGAGDIYLRLPVKKDYQEKIWDHAAGDLIVREAGGQVTDIYGQTLDFSKGRTLAANKGVVAAPKAIQDEVISAVKKVLKL | Function: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Regulates the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS (By similarity). Involved in osmoadaptation.
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
Sequence Mass (Da): 37167
Sequence Length: 352
EC: 3.1.3.7
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C4M4T9 | MSFDKELALALEIVQVSCKITTSVAEHTLTDQTQIKNDKSPVTVGDYSVQAYVNKKIHETFPEDQIVAEEDTKTIPEDIFAKVCKHVQIYSDMKDDEIRKSIDLGNSTGGKGRHWVLDPIDGTLGFLRREQYAVCLAFMIDGDIKVGVLGCPNFEGGLIVAAQKGCGAKMFSVNDIKNGKDIHVSTTPKTSDMCFCESVEVSHTDQSRSKTITERLQVTKPPVRMDSQCKYMAIASGRADVYLRLPRNLSYQEKIWDHAAGYLIVKEAGGKVTDIYGNDLDFSLGRTLCNNHGIVASNGILHEETVNVVKDVLSDLK | Cofactor: Binds 3 Mg(2+) ions per subunit . Active also with Mn(2+) or Co(2+) .
Function: Converts 3'(2')-phosphoadenosine 5'-phosphate (PAP) to AMP . Is also able to hydrolyze inositol 1,4-bisphosphate but with less efficiency .
Catalytic Activity: adenosine 3',5'-bisphosphate + H2O = AMP + phosphate
Sequence Mass (Da): 35038
Sequence Length: 317
Subcellular Location: Cytoplasm
EC: 3.1.3.7
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