ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q8VXV4 | MPGHRSKSEKKDADKQLRRDPYEVLGVLRNSTDQEIKSAYRKLALKYHPDKTANDPVAADMFKEVTFSYNILSDPEKRRQFDSAGFEAVEAESQELELDLSSLGAVNTVFAALFSKLGVPIKTSVSATILEEALNGRVSVDPLVLGQAVSKKVEKQCAHFYAVTISEEEVSAGLVCRVESSSKSKFKLLYFDQEANSGLSLALQEDSKRTGKITSAGMYFLGFPVYRLDHTINSMAQAKDPETAFFKKLDGFQQCEVTELKAGTHVFAVYGDNFFKNVSYTIQVLCAAAFTQEKEDLRSVEAQILTKRAELAKFETEYRE... | 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 | MAIRWSELCIVLFALSYAICVLAGKSYYDVLQVPKGASDEQIKRAYRKLALKYHPDKNQGNEEATRKFAEINNAYEVLSDEEKREIYNKYGEEGLKQFSANGGRGGGGGGMNMQDIFSSFFGGGSMEEEEKVVKGDDVIVELEATLEDLYMGGSMKVWREKNVIKPAPGKRKCNCRNEVYHRQIGPGMFQQMTEQVCDKCPNVKYEREGYFVTVDIEKGMKDGEEVSFYEDGEPILDGDPGDLKFRIRTAPHARFRRDGNDLHMNVNITLVEALVGFEKSFKHLDDHEVDISSKGITKPKEVKKFKGEGMPLHYSTKKGN... | 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 i... |
Q17438 | MTADANKSESLLCMDKAREAIKSGDTDKARRMLLKAKKLDPGQNIEFLTKKIDDMTNNTSSSSQTSSSRASEERSYAHDDHYDDPNLRNRKARSPVKKNGKTEPEPKQRSASRTPKLGVDYTSEQKELVERIRHCKDYYEILKIDKKASDDDIRKEYRKLALKLHPDKCRAPHATEAFKALGNAYAVLSDTDKRRQYDQYGAEAANSHTPTTRRRGGGHGAFFEHDYAHGFEAEFTPEEIFNMFFGGGFPTEQVRRRARYAQQQQYHHYEQQQSPYGPLLQLLPLIAIMVIGLLAQLMVGEPAYSLHQTSKFTIKRLTAD... | 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... |
J9VKM5 | MKGFLLVALPVLFLSLSTQVFGEPSIPSAAQIVQNANRLLAEGSYSAAARAYGEAIELDPTGYANYYKRATAYLSMGRHNAALDDFEQILRINPGFVQAHYQRAKILAKEGDFAKAQYELKAYVRTKSDSEAEELSHLLTVGEAAEKSALQAFEKGKWQVCVEHSTKALEVGPNSEKLRRLRVNCATELGDINMVYGDLSRLASLDPSTTYLPLQLSNIAYFIRASSQAAAHIKQCLHFDPDSKPCKAVHKTIRSLEKDAARVRNFIESGTYRQAIKILDGDDGLLVRFEKALDDATKPKDGLPPYLAPQFHPKKNSQMR... | 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 mai... |
A0A0D2XVZ5 | MHLNLAGLAVAATAFLATASALSPQDIPADLPVSNLLTKAQTHLSRGETNEALVYYDAAIARDPTNYLSLFKRATAYLSLGRTSQATEDFNKVLSLKPGFEGAHLQLARLRAKAGDWDAAKAQYGLAGKAPKSAEFVELEEAKLAAHLADMASKGGKWEECVSHAGTAIVVASRSPHLRELRAHCRFELGDVELALSDLQHVLHMKPGDTSPHIVISATSFYALGDLENGIGQVKKCLQSDPDSKICKKLHKQEKKVEKAYKKIQGQLSRGQPTTAGRALVGTADDSGLVPDVRKQVEELKKNKSIPKTARIQLLENLIE... | 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 essent... |
A0A0D1E2P6 | MKATLLPSLLALSLTLCLALGLSSSGVLVRADAFASSQPPVVSDPVLASQHLTQANVALQSGRYQDALSAFDLALQADPSSWLTYYRRATAQLSLGRTSAALQDFQSLLKLNPKFDKAYLQQAKVYLKEGDCDKAKQALKTYDSIRAEKGAANSSPAEANSVRSKLTLVETSIKSLGQLVKELDKAQKADKKGKAKELDSTKVDHCIHLAGEVLKISPSHLETRLVRARCQTMKGRIEDAMADWTRAVHLTPSPFLLRRLSVLSYFVVSEPGSQSRDAGLQHLKACLHSDPDNKSCAKMHRKIKALEKSLKKARNFYNSQ... | 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... |
Q0WT48 | MAASEENSALFPIFILTIMAIPLVPYTMVKLSGALSKKQRTIHCQCLECDRSGKYKRSLFKKISNFSTWSNLTLVLLWVVMIFLIYYTKNMSREAQVFDPFSILGLEPGVTDSEIKKAYRRLSIQYHPDKNPDPEANKYFVEFISKAYQALTDSVSRENFEKYGHPDGRQGFQMGIALPQFLLDIDGASGGILLLWIVGVCILLPLVIAVIYLSRSSKYTGNYVMHQTLSAYYYLMKPSLAPSKVMEVFTKAAEYMEIPVRRTDDEPLQKLFMSVRSELNLDLKNMKQEQAKFWKQHPAIVKTELLIQAQLTRESGVLSP... | 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 | MAESEENSVLFPIFILTMMAIPLVPYTFVKLSRAFSKKQRSIHCQCLECDRSGKYKRSISQSISSFTSCSNLTVVLLWIVMIFLIYHTKNMSRESQLFEPFGILGLEPGASDSEIKKAYRRLSIQYHPDKNPDPEANKYFVESIAKAYQALTDPLSRENFEKYGHPDGRQGYTMGIALPQFILNMNGESGGILLLCTVGLCILLPLVIASIYLWRSSKYTGNHVKLQTRQAYFELLQPSLTPSKVMDIFIRAAEYAEISVRKSDDESLQKLFMSVKSELNLDPKKLKQEEAKFWKKHPATIKTELLIQKQLTRESSVLSP... | 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 | MQFAEFAARAAEIEAEPADLAVVSLLSDLFSDAGDDLPTVARFVQGRVFPAWDSTTLDIGPRLCHEAIARAAGPNVSADDVEDRLADRGEIGAVAASYDFGGQRGLAAFGSGEQDGLTVAEVDSELRALAAASGSGSEETKLKTLYGLFNRTDPDEARFLARLVLSEMRIGVGEGTVRDAVAEAFLVAPADAAAIRDDDADAETEAAARERRNEAIAAVARALQVSNDYGMVAGLARDEGEAGLDGVRLEVGRPVQAMLAQAGTAADALGEWGTAAVETKFDGARVQVHRDADGEVSLFSRNMEDVTDALPEVVEFVAGA... | 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... |
A2BJX6 | MSMPFSVLAETFEKLERVTARTQMLLYLVELFKKTPPEIIDKVVYFIQGKLWPDWKGLPELGIGEKMLIKAASIALHVSEKQIEQLVKKLGDTGKAIEMIKREKQQKQKAVGLLAFMQKPSGGESTLTVEKVYDTLARIALVQGEGSRDIKLKLLAGLLAEASPREAKYIARFVEGRLRLGVGDATIMEALAVVYGGSAAMRSVVERAYNLRADLGMVAKILATQGIDALKNIKPEVGVPIRPMLAERLNDPVEIIKKLGGRALVEYKYDGERAQIHKKGDKIWIFSRRLENITHMYPDVVEMAKKGIKAEEAIVEGEIV... | 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.
Se... |
A6WG40 | MLLADVVATSTAVAATRSRTAKVAAIAGLLRGLDPADAELTAVVAAYLGGSLRQRRTGLGGRSLSGLPAPAGEASLEVAEVDRRFEEVAALSGPGSAGRRAAAVADLFARATGEEQRWLRGVVAGELRQGALDALVQDAAAAVAGVPGPDVRRAAMLAGSTVQAVVAALRGGAAELAGFGLHVGRPLLPMLAASTTSVAEAVAGFAGPVAVDTKLDGIRIQVHRGPEGVRIATRTLEDITARLPEVVEVVRELPARAFVLDGEALVLDGSGRPKAFQDTASRTAQASGDAVVPYFFDVLHLDGADLLDVALRERLAALDG... | 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... |
Q1II25 | MQLLAQTCEAIAATSKKTEKIAIVATYLQSRTVPEAALSTLFLSGRTFAAHEERTLQVGGSILWRVVGELSGASEAKMTAAYKRHGDLGDATLGVLRGVAPEESTLTLKEVDYMFQQIAAVSGPAAKSRLIVTLLARATAPEAKYLVKFITGELRIGLKESQVEEAIAKAYGRELAEVRRANMLVGDIGETLVLAAHDKLATARMRLFHPMGFMLATPAESANEAFAEFEHAIVEDKYDGIRAQAHISRDKVRIFSRTLDDITDSFPELIPALKAIEHEVILDGEILAWRCGQALAFSELQKRLGRKNVSAAMQREVPVS... | 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... |
Q0W0X1 | MLFKELVSLYESLRSTSSRLEKTAMIAAFLQQAPVDELPVIVTFLTGRIFPEWDQRKIGIASQSMIKIISTITHNPEDAVVESYKKTGHLGVTAEEMFQKRRQVTFFEPEDITVKEVAETFYEIARSSGAGSSAKKQKILIGLLHRATTPKEAHYIVSLTIEYVLSGAKEGVMEDAIGQAFGATLDQVRRAHMLTSDLGETARIAKTEGAAGLEAITIRPMRPVRPMLAQNVSSIREALDTMGGVAEFEMKYDGARLQIHKVGKDVKLYSRRLEDLTDALPEIVGYVRESVKSDTAILDSECIAIDKDTGRPIPFQNILT... | 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... |
Q2FTH4 | MIFLEFAELCSRLEKISGRLETISILAETISSLSDDDLPHFCRLILGKPFPEWSGKKLGVGPNLLYEAVAYVTGRKREEVIDRLSRVGDAGAAVEELLSQKSQTSFFTVELTLADIMAALIEISGMEGGRSQKEKVRVIQRILSSASPLEGHYITAILLEDFRIGVGEGNLRDAIAQAFSVDPNLVEYANQVRNDMGEVAVLARKGEEALRSVRLVPFHPVRMMLARQGTISGVLKEGDPVAVEFKYDGARFQFHKQNKTCRMYSRRLEEVTNAMPDVVALLDEALPDDIIVDGEVIAVQGGHPMPFQTVLRRFRRKHNV... | 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... |
Q57635 | MLWRDVCEIFNKIEKTTKRLEKRDYFIKLIDMVKEKGKPEDLKKICYMAIGRVYPEYDERELGIGEKLLINAVTSIGIKKDELLEKIKETGDIGLAIEQLKSKIKQASLFFQPLTVDEVYETLKRVGEIEGEGSQKKKLRLISSLFLRASPIECRYLARLILEDMRIGMNVPTILDALSVYFNVPKEKLEKIYAITNDIGLLAEKLLMGDLESEELKLKLFRPIKPMLAQLTPSIEEALLEMGRAQFETKYDGARVQIHKDGNKVKIYSRRLEDVTNALPEIVEAVKNINVDKLIVEGECVAIDKQTGKPRPFQDILRRF... | 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... |
Q8TWN3 | MYYSSLAEAFERLERISSRKAKISLIAQFLRQCPEDVVDTVALFLANQVFPGWDPRDLGIGSKLMRKVIATATGSTDSEVTELFKRLGDLGLTAEELLKRRKTSTLLDSRPLMVGEVRETFEKIAEVEGEGAVKRKMRLMMGLLARAKPKEARYLVRQALSELRTGVRESTVEEAIAQAFGVSRKLVERAHMLSNDLGLVAKVAMTKGEEGLREIDLRPMRPIKPMLAQAARNVKEALAEVGGKGAVEIKLDGARVQVHSDGEEVRVYTRRIEDVTHALPDIVEAVKDCVDADEFILEGEAVAINPETGKPRPFQELLHR... | 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... |
Q65MR2 | MEKEAAKRRVEQLHALINKYNYEYHTLDDPSVPDSEYDKLMKELIALEEEHPDLKTPDSPSQRVGGAVLDAFQKVQHKTPMLSLGNAFNEEDLRDFDRRVRQAVGDVEYNVEFKIDGLAVSLRYENGVFVRGATRGDGTTGEDITENLKTIRNIPLRMKRDLSIEVRGEAFMPKRSFELLNKARIERDEEPFANPRNAAAGSLRQLDPKIAAKRNLDIFVYSIAELDEMGVETQSQGLDFLDELGFKTNHERKKCSTIEEVIEIVEELKTKRADLPYEIDGIVIKVDSLDQQEELGFTAKSPRWAIAYKFPAEEVVTTLL... | 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(+) + (deoxyribonucleo... |
O31498 | MDKETAKQRAEELRRTINKYSYEYYTLDEPSVPDAEYDRLMQELIAIEEEHPDLRTPDSPTQRVGGAVLEAFQKVTHGTPMLSLGNAFNADDLRDFDRRVRQSVGDDVAYNVELKIDGLAVSLRYEDGYFVRGATRGDGTTGEDITENLKTIRNIPLKMNRELSIEVRGEAYMPKRSFEALNEERIKNEEEPFANPRNAAAGSLRQLDPKIAAKRNLDIFVYSIAELDEMGVETQSQGLDFLDELGFKTNQERKKCGSIEEVITLIDELQAKRADLPYEIDGIVIKVDSLDQQEELGFTAKSPRWAIAYKFPAEEVVTKL... | 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(+) + (deoxyribonucleo... |
Q8A9C1 | MDIKEKIEELRAELHRHNYNYYVLNAPEISDKEFDDKMRELQDLELAHPEYKDENSPTMRVGSDINKNFTQVAHKYPMLSLANTYSEGEVTDFYERVRKALNEDFEICCEMKYDGTSISLTYEDGKLVRAVTRGDGEKGDDVTDNVKTIRSIPLVLHGDNYPSSFEIRGEILMPWEVFEELNREKEAREEPLFANPRNAASGTLKLQNSSIVASRKLDAYLYYLLGDNLPCDGHYENLQEAAKWGFKISDLTRKCQTLEEVFEFINYWDVERKNLPVATDGIVLKVNSLRQQKNLGFTAKSPRWAIAYKFQAERALTRLN... | 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(+) + (deoxyribonucleo... |
Q6FZ81 | MNKDEIKNLTALEAESELEWLAKEIARHDVLYNRDDQPEISDAEYDALRRRNAEIEALFPELIRSDSPSHKIGAPVSEKFEKSVHAQAMLSLDNAFSSEDICEFIVRIRRFLRLPATQILEMTAEPKIDGLSLSLRYEKGRLVCAATRGDGYIGENVTANARTISDIPKVLRGEFPDIIEVRGEVYMRRENFQALNMSQQEKGKFVFANPRNAAAGSLRQLDPRITASRKLHFFAYACGEVSETFAASQMEMMKKLKEYGFFINPLTKSFKTLEEIISYYHDIEECRHSLSYDIDGIVYKVNDLKLQMRLGFVSRSPRWA... | 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(+) + (deoxyribonucleo... |
Q1LU20 | MKQIEQYIEQLRQQLRYWNFLYYAKDAPEVSDVEYDWLMMKLRELERQWPDLKTADSPTQHIGYKAQSKFRKVIHEVPMLSLDHIFNDTSFLAFDRRIRNRLQYGNNYLTYCCELKFDGIAVSLLYKHGKLIRAATRGDGHIGEDVTDNIRTICSIPLQLKDDGHIPRLIEIRGEVIMSEDAFRHLNETAKKNKSKRFANPRNAAAGSLRQVDPSITATRLLSFFCYGVGRIDSKKIPAAHLELLQQFKIWGLPVSNYRRYCVGHQEVLDFYSYVSKVRSKLGFNIDGIVIKVNALVQQQQLGFVARAPRWAIAYKLPAN... | 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(+) + (deoxyribonucleo... |
Q6MRL9 | MPDAFCRDWTSEMGANYSMSKKRHEELKKIISEHDHNYHVLDKPTITDYEYDQLFAELLDIEKNPKGLDLSDSPSQRVGGTVLEGFTKAQHRLPMLSLANSYSPEDIFEFDERVRKFLNTEDPVEYLCELKFDGLSMELIYENGQLVRAITRGDGTVGEDVTHNIKTIKSIPLKLSHKNPPPLLEVRGEVLMFKEDFARLNETQQENGQQTFANPRNAAAGTVRQLDSRIAASRPLRFFGYALGAVEGETFNTQKNIQEYFNDHGIPTVLPYKEDLLVVAKGPEEVVKYYHHIEKVRPKLPFDIDGVVIKVNSLRLQEDL... | 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(+) + (deoxyribonucleo... |
B2IGH4 | MTVQKPIESLSPAQAKREHRRLGEQITEHDRLYYQEDAPRVSDAEYDALRRRYEALETAFPELVSAESLTKKIGAAPAEKFAKIIHKVPMLSLANIFSDEEVGEFVARVRRFLGLGADAPLAISAEPKIDGLSCSLRYEGGYLVQAATRGDGYEGEDVTANVRTIQEIPHQLQGHAPEILEVRGEVYMTHADFAALNERQEAAGKTIFANPRNSAAGSLRQLDPKVTAGRPLHFFAYAWGEASEEPADTQMGMVTAFKAFGLPVNPLMQLCHSAEDLIAHYHDIEARRALLDYDIDGVVYKVNSIALQKRLGFVSRAPRW... | 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(+) + (deoxyribonucleo... |
Q8G830 | MSTNEQLAWDFDDGDVAEVRPDTGIARFAPGSEQWIAALQPTDDDAIRLDRFDVNTMTAEAAARLWARVAAWVESDQIAYYIDDSPVSSDAAYDARMRCLERLEAAFPSLDNPQSPTHRVGGSFSNDFASVRHPSRMMSLDDVFSIEELKDWYDSVIRDLDWPESKPLPMSCEVKIDGLALNLIYRNGVLEQGLTRGDGVTGEDITLNVRTIGSIPANLGGPKEDVPDFVEIRGEVFMRWDDFHTLNNEQEDAGRAPFANPRNAAAGSLRQKDPRITATRRLSFYAHGLGQLTWGPDHPRGTHDVVADQSQAYDLYTKWG... | 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(+) + (deoxyribonucleo... |
Q7NMN8 | MSTTVPPEIEEHTRTLRALLHRWGYAYYVLDAPEVSDAIYDQHYRELVDLESRYPELVSPDSPTRRVGERPASAFVSVTHRVPMFSLENAFSQAELEKWGERLLRAIGPGLEFICELKIDGSATALSYEDGVLVRGATRGDGVEGEEITQNLRTIRAIPLKLLGGEVPAVLEVRGEAFIPRDEFERINQERQAAGEKLFANPRNACAGTLRQLDSRVVASRRLGFFAYTAHYGRAESQWEALAELESHGFRVNPHRSLCRDLAEVRTFCEHWENHRHELPYDTDGVVVKVNAFDHQREVGFTSKFPRWAIAFKYPAEEKS... | 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(+) + (deoxyribonucleo... |
A9H0L6 | MDPSELTEPQAMVELERLAQQIRALDRAYYEDDAPTVTDAEYDALRQRNLAIEARFPDLRRADSPSLHVSGAPSAAFGRHRHLVPMLSLDNVFGREDFESFVTRAARFLGLNDDQARALRFVAEPKIDGLSISLTYEHGRFVRGTTRGDGTEGEDVTANLRTLRDVPLRLKGPAPALIEIRGEVFLSKPAFLSINAAQAEAGQKPFANPRNAAAGSLRQLDPNITARRPLSLFAYAQGFSSDRVADTHWDYLERLRQWGFTVNPLSCVVESAEAAEAFMDRIARERSGLEYDIDGVVYKVDDLALQDRLGFVGRAPRWAI... | 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(+) + (deoxyribonucleo... |
Q7VMX7 | MPLFSQFELSNNITPTQLEALRDQLREYEYHYHVLNNPLVPDAEYDRLINQLKNIEQQYPELITPDSPTQRVGAKPLAGFAQVAHEMPMLSLDNAFSETDLDNFLRRIENYLSLDANQLTFCCEPKLDGLAVSILYIDGVLQLAATRGDGTTGENITANVRTIRNIPLKLKMANPPHRLEIRGEIFMPLKGFNALNQRALAKGEKSFANPRNAAAGSLRQLDPQITRQRPLMLNAYGIGVYESNYQRLPTSHYARLEWLKSIGIPVNAEIRLARGYPQLLAFYADIQAKRADLGYDIDGTVLKVDDITIQETLGFISRSP... | 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(+) + (deoxyribonucleo... |
P43813 | MTNIQTQLDNLRKTLRQYEYEYHVLDNPSVPDSEYDRLFHQLKALELEHPEFLTSDSPTQRVGAKPLSGFSQIRHEIPMLSLDNAFSDAEFNAFVKRIEDRLILLPKPLTFCCEPKLDGLAVSILYVNGELTQAATRGDGTTGEDITANIRTIRNVPLQLLTDNPPARLEVRGEVFMPHAGFERLNKYALEHNEKTFANPRNAAAGSLRQLDPNITSKRPLVLNAYGIGIAEGVDLPTTHYARLQWLKSIGIPVNPEIRLCNGADEVLGFYRDIQNKRSSLGYDIDGTVLKINDIALQNELGFISKAPRWAIAYKFPAQE... | 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(+) + (deoxyribonucleo... |
Q9KF37 | MERNDAERKIEKLRNQLEEYGYHYYVLDKPLVSDAEYDGLMNELIELEEAFPELKSDTSPSVRVGGPPLPHFEKVEHRTPMLSLGNAFSDQDLRDFDRRVRQVVGDEVTYSCELKIDGLAISLIYESGRFVRGATRGDGTTGEDITQNLRTIPSIPLRLKEAVSLEVRGEAFMPKRSFEALNEAKEAAGEERFANPRNAAAGSLRQLDPKLAAKRHLDAFIYAIGSVEGKELHSHHEGLNYLKTIGFKINPESAYCESIDEVIDYVNSWLERRADLPYEIDGIVIKVDNVNFQEQLGYTAKSPRWAIAYKFPAEEVITTL... | 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(+) + (deoxyribonucleo... |
B9LU22 | MTSSSPRHADPDENPYVEAPPTDFEPVGALSEDEATEQASLLRAAIREHDHRYYLEADPLIPDETYDRLFTRLQELENEFDLPTQNSPTRRVGGEPLDELATVEHVAPMRSIDNATEADAVREFDGRVRKGLDAEGFDSDAVEYVCEPKFDGLSVEVIYEDGEYVRAATRGDGTAGDDVTEQVRTIRSVPGKLRGDPPSRLAVRGEAYMPRDAFKAYNEALMERGEEPFANPRNAAAGTLRQLDPSVVAERPLDIFFFDVLGWENDAEGDSPNRPATHWEEFDTFDAFGLRRANRVERVDDIEGALDYRDRLMADREDLN... | 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(+) + (deoxyribonucleo... |
B8D122 | MASKVEQEIRDLREKIRYHEYRYYVLDDPEISDAEFDELIQRLIDLEEKHPGLVTPDSPTQRVGGEPLDKFDKVEHRVPMLSLGNAFNEGDLTNFARRIYRLLDTGKIDFVVEHKIDGLSAILTYQGGRLIRGATRGNGVVGEDVTANIKTIPSVPLRLKKDVDIEVRGEVYIKKDDFSKLNERRLKKGEEPFANPRNAAAGSIRQLDPRLAAARPLSFIAYDVVAYEGEGLQTHVGALELLRELGFKVNWYRKCDDITEVVNICKDWVDKREELPFEIDGMVIKVNELGLREQLGATAKSPRWAIAYKFPAQQKTTVVK... | 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(+) + (deoxyribonucleo... |
D4GY98 | MSDADVDAESNPYLRDPPTEFEPAESLSREAAEGQAALLREAVREHDHRYYVAADPLVSDAAYDALFSRLVALEDAFDLDTTNSPTNRVGGEPIDALETVEHVAPMLSIDQSTDADDLREFDERVRREVGAVDYVCEPKFDGLSVEVVYEDGEFVRAATRGDGRRGDDVSAQVKTIPTVPLSLRGDHPDRLAVRGEIYMPKSDFSDLNARRVEAGEDAFANPRNAAAGTLRNLDPSVVADRPLAVFFYDILDASARPDSQWAALDRLREWGLRVTDRIERAEDVAEAIDYRDRMQAARDDLDYEIDGTVIKVDSRDARER... | 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(+) + (deoxyribonucleo... |
Q1D0P7 | MDDFQKAAARARELHRELAHHNYRYYVLDSPEVSDAQYDKLMRELQDLEAKHPSLQTPDSPTQRVGGAAAEEFGEVVHRAPMISLANIFEDQGLTEFDERIRKLVGLPGIAYVCEPKLDGLAIALRYEKGAFVQGATRGDGTTGEDVTSNLRTIRSLPMSLFPQDDVKVPDVLEVRGEVFIRKKDFQKLNEKREEEGEPLFANPRNAAAGSLRQLDPRMTAARPLSVFLYECVPGEGVPVFKTHIEKLEYLKTLGLPINQYRRAEGLEGVRQAYDASLKGRHELPFEVDGMVVKVDDEDQRKRLGQVSKSPRWAVAYKFP... | 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(+) + (deoxyribonucleo... |
B2A5W5 | MSKDIQKKVEALREKIEYHNHRYYVLDAPEISDQEFDALMNELIELEQTYPEYQSPDSPSQRVGGEPLDKFPRVSHEIPMLSLENAESQKGLLDFHQRVSKNTQKTDPVYVAELKIDGLALSLRYEQGILVRGATRGDGTTGEDITPNVKTVRSIPLKLSKPLDIEIRGEAFMSKASFERLNQEKAERGEDPFANPRNAAAGSLRQLDPKIPAKRDLDFFPYSVPYIRGENLDSHYSAVKELKDLGFKINPYIRKFETMEEVISYCEEWQEKRTKLPYEIDGVVIKLNDYNLQQQLGATSKNPRWAIAYKFPAEQAESQV... | 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(+) + (deoxyribonucleo... |
Q5F9Z9 | MNLYESMNPTAQRIHELTDLLNRYAYEYYTLDAPSIPDAEYDRLFRELEALERNHPELKLPDSPTQRVGGEPLAGFAEVRHEVPMLSLTNAFSPQDENGVFDHAEMYAFDQRVRDGLDGGNPEYVIEPKFDGLAISLLYRDGVLVQAATRGDGTTGEDVTRNVKTVSNIPLRLHGENVPELIEVRGEVLMLKADFAALNQRQTENGQKPFANPRNAAAGSLRQLDSRITAQRKLHFFPYSVARQQGGLIAEEHIQELAYFQALGFSLPNGNFGCFKNIGEVLAFYEHMQQKRPELPYEIDGTVVKVNSLAQQHELGFISR... | 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(+) + (deoxyribonucleo... |
Q2GDR2 | MEAKKEIQELYEKLLRHNKKYYQDDSPEITDAEYDSIKDRYLKLLEANPSLGFPVVVGYPASEKFQKVKHLSPMLSLRNIFSEEELVEYIEKTKRFLNLKSALEFLCEPKIDGVSFSARYVNGKLVSCATRGDGKIGENIIDNMKVINGFPIEIMDVPDLLEVRGEVFLDHDTFQTLEGFSNPRNAAAGSLRQLNPEITNERNLQYFAYSASKIDGIEHQEDVLHFLSGRGFMTNPLRLASSKVPEIMSFYDSVYRRRSQIKYDIDGLVYKVNDLKLHARLGTLSDAPRWAIAHKFPSHRAKTILEKIKLSVGRTGIITP... | 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(+) + (deoxyribonucleo... |
Q0AHH6 | MESEKIIEERLKALRSTIALHDFHYYVQDAPIIPDADYDKLFRTLQQLEQQYPHLITPDSPTQRVGAPPLKVFARLTHQTPMLSLTNAFTEDEAIAFDKRIREALNVDQVNYAVEPKFDGLAVSLVYTNGILTNGATRGDGYTGEDITLNLRTIPSIPLRLQTATVTDQFEVRGEVVMLKADFEHLNEQQRNKGEKLFANPRNAAAGSLRQLDSNITAARKLTFFAYDAVLSHKDQPFFSKHSEILDYLKSQQFLVAQQNGTTTGVAGLLTYYHEMGALRLSLPYEIDGVVYKVDNLTQQETLGYVSRAPRFAIAHKFPA... | 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(+) + (deoxyribonucleo... |
Q1QNT2 | MAAKPKTPPPVDSLTRAQAKIEHKRLALEIETHNERYYQKDAPTVSDAAYDALRQRLEAIEARFPDLITANSPTQTVGAAPARGFAKVQHAVPMLSLGNAFSDEEVAEFVERIQRFLKLGPDDIPAIVAEPKIDGLSLSLRYENGELVRAATRGDGFTGEDVTANVRTIKDVPHNLRGRNIPTACELRGEVYMLKTDFLALNKKQEDAGDTVFANPRNSAAGSLRQKDVAITASRPLKFFAYAWGEMTDRPADTQHDMLEWLKDVGFKVNPLIELCNSVEKVLKFYRKIGEQRASLGYDIDGVVYKVDRLDWQERLGFVS... | 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(+) + (deoxyribonucleo... |
A6Q433 | MIKNYQEYKEAVEKLKRWAYAYYVLDNPEVPDEVYDKLYREVEEYEKAHPDQIDPTSPTQRIGAEPAKEFKKIKHLSKMWSMEDVFNQREMHEWLERVYKNAGRKDLQFYIEPKFDGASLNLIYENGLLKSAATRGDGEVGEDVTANAKTIPSIPLGIDYKGLIEIRGEVVIRKDDFEKLNHERALKGESTFANPRNAAAGSLRQLDPKVTAQRKLYFYPWDIGYNTLNFKYQHEKMDFVYQQGFIKPFKRAICENEEEIQQLYEEFSKERDKLPVMLDGMVVKVDEIALHEILGYTVKYPRWMVAYKFPAVEKMTRIID... | 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(+) + (deoxyribonucleo... |
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'-deoxy... |
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'-deoxy... |
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): 157... |
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'-deoxy... |
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): 167... |
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): 160... |
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 anti... |
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 anti... |
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 anti... |
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 anti... |
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 anti... |
Q54530 | MNDHEVDVLVVGAGLGGLSTAMFLARQGVRVLVVERRPGLSPYPRAAGQNPRTMELLRIGGVADEVVRADDIRGTQGDFVIRLAESVRGEILRTVSESFDDMVAATEPCTPAGWAMLSQDKLEPILLAQARKHGGAIRFGTRLLSFRQHDDDAGAGVTARLAGPDGEYDLRAGYLVGADGNRSLVRESLGIGRYGHGTLTHMVGVIFDADLSGIMEPGTTGWYYLHHPEFKGTFGPTDRPDRHTLFVEYDPDEGERPEDFTPQRCVELIGLALDAPEVKPELVDIQGWEMAARIAERWREGRVFLAGDAAKVTPPTGGMS... | 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-1... |
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 meta... |
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
|
A0QZ49 | MQRIIGTEVEYGISSPSDPTANPILTSTQAVLAYAAAAGIQRAKRTRWDYEVESPLRDARGFDLSRSSGPPPIVDADEVGAANMILTNGARLYVDHAHPEYSAPECTDPMDAVIWDKAGERVMEAAARHVASVPGAAKLQLYKNNVDGKGASYGSHENYLMSRQTPFSAVIAGLTPFMVSRQVVTGSGRVGIGPSGDEPGFQLSQRADYIEVEVGLETTLKRGIINTRDEPHADADKYRRLHVIIGDANLAETSTYLKLGTTSLVLDLIEEGVDLSDLALARPVHAVHVISRDPSLRATVALADGRELTALALQRIYLDR... | 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 (... |
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... |
Q5BPS3 | MKSRRQNVSVARQTILGRDENFEPIPIDLVIEIFSRSPVKSIARCRCVSKLWASILRLPYFTELYLTKSCARPRLLFACQKHRELFFFSTPQPHNPNESSSPLAASFHMKIPFDGRFNIISPIGGLVFVRYEQILKGRKTPEFVSAICNPSTGQSLTLPKPKTRKRIWGTSHFGYDPIEKQFKVLSMNIGDGVYKEHYVLTLGTENLSWRRIECSIPHVHGSKGICINGVLYYRAKADMFSGTLMIVCFDVRFEKFSYIKILKPTTTLISYNGKLASLVWEGPSYICGKRFEMWVLGDPEKHEWLKHTYELRPRWQNVLG... | 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... |
Q320T0 | MEMYFKRMKDEWTGLVEQADPLIRAKAAEIAVAHAHYLSIEFYRIVRIDPHAEEFLSNEQVERQLKSAMERWIINVLSAQVDDVERLIQIQHTVAEVHARIGIPVEIVEMGFRVLKKILYPVIFSSDYSAAEKLQVYHFSINSIDIAMEVMTRAFTFSDSSASKEDENYRIFSLLENAEEEKERQIASILSWEIDIIYKILLDSDLGSSLPLSQADFGLWFNHKGRHYFSGIAEVGHISRLIQDFDGIFNQTMRNTRNLNNRSLRVKFLLQIRNTVSQIITLLRELFEEVSRHEVGMDVLTKLLNRRFLPTIFKREIAHA... | 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 messenge... |
Q83KV7 | MEMYFKRMKDEWTGLVEQADPLIRAKAAEIALAHAHYLSIEFYRIVRIDPHAEEFLSNEQVERQLKSAMERWIINVLSAQVDDVERLIQIQHTVAEVHARIGIPVEIVEMGFRVLKKILYPVIFSSDYSAAEKLQVYHFSINSIDIAMEVMTRAFTFSDSSASKEDENYRIFSLLENAEEEKERQIASILSWEIDIIYKVLLDSDLGSSLPLSQADFGLWFNHKGRHYFSGIAEVGHISRLIQDFDGIFNQTMRNTRILNNRSLRVKFLLQIRNTVSQIITLLRELFEEVSRHEVGMDVLTKLLNRRFLPTIFKREIAHA... | 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 messenge... |
P76129 | MKLTDADNAADGIFFPALEQNMMGAVLINENDEVMFFNPAAEKLWGYKREEVIGNNIDMLIPRDLRPAHPEYIRHNREGGKARVEGMSRELQLEKKDGSKIWTRFALSKVSAEGKVYYLALVRDASVEMAQKEQTRQLIIAVDHLDRPVIVLDPERHIVQCNRAFTEMFGYCISEASGMQPDTLLNIPEFPADNRIRLQQLLWKTARDQDEFLLLTRTGEKIWIKASISPVYDVLAHLQNLVMTFSDITEERQIRQLEGNILAAMCSSPPFHEMGEIICRNIESVLNESHVSLFALRNGMPIHWASSSHGAEIQNAQSWS... | 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... |
P9WGK0 | MTHPDRANVNPGSPPLRETLSQLRLRELLLEVQDRIEQIVEGRDRLDGLIDAILAITSGLKLDATLRAIVHTAAELVDARYGALGVRGYDHRLVEFVYEGIDEETRHLIGSLPEGRGVLGALIEEPKPIRLDDISRHPASVGFPLHHPPMRTFLGVPVRIRDEVFGNLYLTEKADGQPFSDDDEVLVQALAAAAGIAVDNARLFEESRTREAWIEATRDIGTQMLAGADPAMVFRLIAEEALTLMAGAATLVAVPLDDEAPACEVDDLVIVEVAGEISPAVKQMTVAVSGTSIGGVFHDRTPRRFDRLDLAVDGPVEPGP... | 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 si... |
Q9VZZ9 | MDRTFYEGWLIKSPPTKRIWRARWRRRYFTLKQGEIPEQFCLEYYTDHNCRKLKGVIDLDQCEQVDCGLRLENRKQKFQYMFDIKTPKRTYYLAAETEADMRDWVNCICQVCHLHDTKQSNELPLGAVGADENRTQHTSSSGGLSNSTQNTTTTSLHSSAGTTAPQASVPNAGGSAQLRRPAVIEEQPMPSNAGNNNSDSVYVNTEYSNRETMLCDANFDQQELLSAAQQQPPPSPATALYLNHSALIQAQAAAAAAEQLQQQQQQAARLAVSANGVVRKLPEHLVLTQQTLAEAAAQQHSSVQASPALSTASGPYIPIS... | 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 Topo... |
Q6AW06 | MSEADAGARDESPSRTAEEPAAAMRIKEERRSSSVDVVDVGNGELLVLHSIFYQGKTLRLPGNRAHMYPVVFQMIKGVCSLVKQLVVAFPKGWDQNTPSISEIAALTKSFNRVAKPFASNWSGSYNTDTLKEWGEPNCSAEVAKAITTYAYECAVPRPADLNQHYKSFTSETYGETNPEQLISIIDELNIGPQDVFVDLGSGIGQLVCLTAAYAKCKKSVGIELSQVPSNFAQDLAGYFKKFMSHFGKNHGKFEHIQGDFLNPKFKQLICEEATVIFINNFAFDAALMLRINTELLQDLKHGTRIVTTKELGTNKKEITF... | 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 hig... |
H1VM35 | MSEPHFKVIIVGGSITGLTLAHSLHKIGVDFTILEKRATVTPQEGASVGILPNGARVLDQLGLYGLVEEATAPLGATHIHFPDGFHFCSLYPKSMLDNFGYPVAFLERRRLLEVLYNALPDKSKVLVNKTVSDIEQCEDGKSAGVKVRTADGDVYEGDIVVGADGVHSRTRSELWRMSSSAGQSEDVRMEKARMSAEYSCVFGISRGPSGLKAGEQIMRMYDGRTLVVIPSKDDVVFWFLSRKLGKKYKYSEAPRFTLEDAAAECAELADAPLGNDVRFGDVWKIRQTFNMVVLEENLLRTWSFGRVLCIGDSIHKMTVN... | 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 ... |
H1VQW0 | MKLSFIASPVWALALAQFAAATQVKIDVDVAIFGGGSAGIHAAIQLRDAGATVAVIEKKSQIGGHAETYTDPQGKSTNVGVVVFDNIEVASNYFARLNVSIVRGSPLGTAGPTYTYDFTSGAQIPAVNTSAEAQQQLTAALQSYSTNVLSKYPWIDEGFLVPDPVPEELTIPFGELAQKYNFTALMPTIAMYNYFTGDLSTIPSLYGIKGLGQGALKNLFGSFILPASGKTRDLYDAAAIELGNSVLLNADVVKVQRDVRINSTTTGVTVLIQQPGQPPKLIRARKLLVAAPPTLENVGAFDLTAEERGLISKFSSLGCW... | 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... |
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 | MAALVVSGAAEQGGRDGPGRGRAPRGRVANQIPPEILKNPQLQAAIRVLPSNYNFEIPKTIWRIQQAQAKKVALQMPEGLLLFACTIVDILERFTEAEVMVMGDVTYGACCVDDFTARALGADFLVHYGHSCLIPMDTSAQDFRVLYVFVDIRIDTTHLLDSLRLTFPPATALALVSTIQFVSTLQAAAQELKAEYRVSVPQCKPLSPGEILGCTSPRLSKEVEAVVYLGDGRFHLESVMIANPNVPAYRYDPYSKVLSREHYDHQRMQAARQEAIATARSAKSWGLILGTLGRQGSPKILEHLESRLRALGLSFVRLLL... | 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... |
Q5NCQ5 | MAALVVSETAEPGSRVGPGRGRISRGRLANQIPPEVLNNPQLQAAVQVLPSNYNFEIPKTIWRIQQAQAKKVALQMPEGLLLFACTIVDILERFTEAEVMVMGDVTYGACCVDDFTARALGVDFLVHYGHSCLVPMDTSVQDFRVLYVFVDIRIDTAHLLDSVRLTFTPGSSLALVSTIQFVSTLQAAAQELKADYHISVPQCKPLSPGEILGCTSPRLSKEVEAVVYLGDGRFHLESVMIANPNIPAYRYDPYGKVLSREYYDHQRMQATRQEAIAAARSAKSWGLILGTLGRQGSPKILEHLESQLRNLGLPFVRLLL... | 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... |
A7SLX5 | MADSVEQSSVTTKRISAKGARKRFVGTKSASGKHSQGVDRVGSAAHRPVNQIPEEILKDTKLQEALPENYNFEIHKTIWRIQQVKAKRVALQFPEGLLLFACTIADILESFTGCETVIMGDVTYGACCVDDYSARALGCDLLVHYGHSCLVPIDATAGIKMLYVFVDIKIDTAHFVESVRFNLGAGSCLALVSTIQFVAALQAASNELSKDYQVEIPQCKPLSPGEILGCTAPMLKDKDAVIYLGDGRFHLEAVMIANPAIQAYRYDPYDKTFSKEYYDIDKMHEARQTAIKQASLASKYGLILGTLGRQGSPKVLQTLE... | 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 trans... |
Q3T7C9 | MNMEEDTQSKEIVVAPKKEKKVFRPARSVIKGVPAEIEKDPKLQKAIEVLPSNYNFEIPKTIWRVKQANAKHVALQFPEGLLLFATSIADIIETWTEAETTIMGDVTYGACCVDDFTARAVGADFMVHYGHSCLVPIDQTGSIPCLYVFVDIQFDTVHLIDTIKSVFPSTVPLALVSIIQFVSSLQKMAQDLKSCGYTVCVPQCRPLSPGEVLGCTSPPVPEGHTIVCLGDGRFHLESIMISNPEVPTYLYNPYSKVLSREYYDQPLMKKIRKEIIDKASTAKKWGLILGTLGRQGNTKVMENLKNQLEAAGKDFVIVLL... | 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 trans... |
O59713 | MAEVKKSIPKRRFVGKKNRKENNLDGSNRDVENAALVTINSKRSAGRVATQIPEDILNDKAINEAIKLLPQNYNFEIHKTIWHIRLRKAKRVALQLPEGLLMFGCILSDIFEQFCQVETIVMGDVTYGACCIDDFTARALDCDFLVHYGHSCLIPVDQTPIKVLYVFVDIKIDLQHVVSSLKHNLPSNSRLALVGTIQFVGSLNSIKDALQIQDEDGKGGFYVVIPQAKPLSPGEALGCTSPYIEKGSVDALIYIGDGRFHLESVMIANPDLPAYRYDPYSHKLSIESYAHEEMKSIRYSAVEKARTAKKFGLIQGTLGR... | 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-... |
Q4PA25 | MQSNAENPRKRFTATSPNGNRQNVSVDTSSNVAGPSRPRIANAVPAEILDDPALNQAIKSILPSNYNFEIHKTIHHIRKASASCVALQMPEGLTLWATGIADIVERFTDATTVIMGDVTYGACCVDDYTAMALGCDMLVHYGHSCLVPVDQTAIKTLYVFVEISIDPAHLAATIRANFPNDRHDFRAKILGGSQSAAGKRSEVDESAGRAQIQIGEQASVASGAPPSTLTHLALVGTVQFINAINGLREALRQQQHRLADGQIVSTESPVDRLMLTAGTASSAPVQHITQAAKWKAWSSGEYKVTVPQVKPLSPGEVLGC... | 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-... |
Q6GPQ5 | MEPERNESGTPSVAVTPAAPINAGRAPVRRVANQIPDEIAHNPLLLEAMKVLPENYNFEIPKTIWRIQQASAKRVALQMPEGLLMFACAIADIIERFTSAETVVMGDVTYGACCVDDYTAQALGADFMVHYGHSCLIPIDATHGVRMLYVFVDIKIDTSHFVDTIRFNFQAGASLALVSTVQFVSALQAARQALQTDYNVTVPQCKPLSPGEILGCTSPRLNKSVDAVVYLGDGRFHLESVMISNPDTKAYRYDPYSKVFSREYYDHSTMLRHRGEAISVATNAKTWGLILGTLGRQGSPKIMEHLESRLQALGCRYVRL... | 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 trans... |
P40487 | MSGSTESKKQPRRRFIGRKSGNSNNDKLTTVAENGNEIIHKQKSRIALGRSVNHVPEDILNDKELNEAIKLLPSNYNFEIHKTVWNIRKYNAKRIALQMPEGLLIYSLIISDILEQFCGVETLVMGDVSYGACCIDDFTARALDCDFIVHYAHSCLVPIDVTKIKVLYVFVTINIQEDHIIKTLQKNFPKGSRIATFGTIQFNPAVHSVRDKLLNDEEHMLYIIPPQIKPLSRGEVLGCTSERLDKEQYDAMVFIGDGRFHLESAMIHNPEIPAFKYDPYNRKFTREGYDQKQLVEVRAEAIEVARKGKVFGLILGALGR... | 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, transfer... |
Q757B6 | MSEAALVPPALSTNQTEETFNFQQYELLRQDRAAHLGPGITDLASLKERIRSYYAIESLADHLNSHAEYRSITLQFPDDLLFDSALVAEELQALLPDLQCARTDAPAQADTTCSCGTQKTCADSKDSADGRKIWILADTAYSPCCVDEVAAEHVQADVVVHFGDTCLNPVETLPVVYIFGEPYLDRAKVISLFTERYDKDAKVCLMANAPYSRHLESLSGELSQLGYSNLVFTDVALPDTPNAAATILGVSDSHPISHKLYASGDRVYYGAKEQLLCEEQLQSFELFHIGLPPDPRLLFLSTKFQGVTAYDTQKRQIAKG... | 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 ... |
Q4WN99 | MATEMQAAPVLSTPDSLILEATEPVARQNATRTLSDEELSITYDIERTLQEIRQARYKRIALQFPDDMLPDAPRVFQLLSRGLACRDVDKITVEKNGNGTGGVESEKLAQDVSQLSVDDKPEPEPKLYILADTSYGTCCVDEVAAEHVNADVVVHYGRSCLSPTARLPVIYVFTHKELPIEPVIQAFKATYPDQATKIILAADVTYCDHIPAVYARLMEEGYTNLYATELIHCPSSAIPNRTVPDSVRENPDTLSEWQLFHISDPPTALLLTLASRVAAIHIYPTTDAPSDNVKPLPVSTSAALGRRYAILTRLSTVPIF... | 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 ... |
Q09454 | MTESAPSAFFTTSTPADHVHEEESSNTGYFENLPENDIHSFFEIDATSEWIKQGNHQRIALQFPDSLLPYSEKVTKLIESRFRSESAKKTFVLADTSYRSCCVDEVAAAHADCTALVHFGEACHSAPTDKIDVKYVLGSMPIFIDQFRMEFQNVADQLTAEHIVLLMDSCFSHEQEKVAAVIKEVLPGNRHVECSLLPSEDVLKQNRQNIYLGREIPSCLRNNQPTDLIFCGFPNSPLLPIWLLSYPSCSTVSHFNPINKTIQHESTRSSRLLRKRLFLVEKLKDADTVGLVVGSVGVDKHREAVKRMREMCKKAGKKIY... | 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 an... |
Q5ZKI2 | MAAAFSSDGEAVLRRTLDPAAAAPRGDKDEFYEVDRAAAFVRDGGFRKVALQFPDALLADAAAVAARMEEVTGAEMYVLGDTTYGSCCVDEVAAEHVSAGAVVHYGPACLSPCRKLPVLHVFGRQPLDVGRCAEVFRELYPERQSRVVVLSDVVYAHAMGELEKQLCHEYPNIIFSEVVCGDAPSPTLPGEVRQFGRRFHMEAAEELQDCSMFYVGAEGLALTSFMLTWNRFPFSSFDPATGHGRRETLNVNRALMRRLYLVERARDAHVVGILVGTLGVAGYLDVLEHLHQLVRRAGKRSYTLSVGKPNPAKLANFLEV... | 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 ... |
K2QVI4 | MESSSSKGGFKVLIIGGSVTGLTLAHSLDKMGVDYRLLEKRKEIAPQEGASIGILPNGARILDQLGLYNAIEQSAIALGTSDVYFPDGFHFTSSYPKRMHDRRSFAYPIAFMERRKLLEILYDLLPDKSRVEVDKAVSRIEEHPEHHGVLRAYTHDGDVYEGNLVVGADGVHSRTRREMWRLSGSSPTGDVPVSERNSTSVEYACIFGISDGIAELTPGRQVMRFGNGWTLAVIPSRQGQVFWFIVQKLDREYQYGSAPRFAPEDAAEQCSKLARLPIHGDVRFDDLWQRRKAVNMAALEENVFQTWSCGRLVCIGDSIH... | 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 (... |
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 methyl... |
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 methyl... |
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... |
K2RLM2 | MLQLILHHPYASLAAGILLYFFCLATYRLYLSPVAGFPGPRLAALTRFYEYYYDGVKGGQFVWKVKDLHQKYGRLSCSTVVGQELKLEQGPIVRIGPCELHVNDPTFVSTLYPATGQRRNKDPFWTDQFGPKTAFGTVDHDHHRLRRGPFNRFFSKANVTRLEPMLRQQANKLCEKLEKYAGTGRVIDLSDPFGCMATDIISTYALGYSFNFLDAEDFQPNLLQGLNGFTPLAPTVKQFPWLLKLLRALPDSWALKINPKIAPFLDFQRTMKKVITDVEAEVQSEAGRPKADQATTIFHEVLRGDIPPEEKETARLWQEG... | 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... |
Q42546 | MAYEKELDAAKKAASLAARLCQKVQKALLQSDVQSKSDKSPVTVADYGSQAVVSLVLEKELSSEPFSLVAEEDSGDLRKDGSQDTLERITKLVNDTLATEESFNGSTLSTDDLLRAIDCGTSEGGPNGRHWVLDPIDGTKGFLRGDQYAVALGLLEEGKVVLGVLACPNLPLASIAGNNKNKSSSDEIGCLFFATIGSGTYMQLLDSKSSPVKVQVSSVENPEEASFFESFEGAHSLHDLSSSIANKLGVKAPPVRIDSQAKYGALSRGDGAIYLRFPHKGYREKIWDHVAGAIVVTEAGGIVTDAAGKPLDFSKGKYLD... | 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 pr... |
O49623 | MSYEKELAAAKKAVTLAARLSQEVQKTLLQSQVWKKSDRSPVTAADYGSQAVVSLVLERELQPDKLSLVAEEETGDLRKNGSEAFLEDIAKLVKDTLASEESYTSSPLSTDDVLNAIDCGKSEGGCKGSHWVLDPIDGTRGFVRGEQYAVGLALLVEGKVVLGVMACPNLPLASAVCATDNSSQEDVGCLFFATTGSGTYVQSLKGNSLPQKVQVSSNENLDEAKFLESYHKPIPIHGTIAKKLGIKALPVRIDSQAKYAALSRGDAEIYLRFTLNGYRECIWDHAPGSIITTEAGGVVCDATGKSLDFSKGKYLAHKTG... | 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... |
Q8GY63 | MSYDEMLSAAKKAVSLAARLSNEVRKSLLVTDVWNKSDDSPVTVADYGSQAVVSLVLERELQNEPVSLVAEEDSGELRKIAAETVLARITELVKDTLASDESYAIASPLTSDDVLNAIDRGKSEGGPKGRHWILDPIGGTRGFIRGEQYAIGLALLVEGKVVLGVMACPKLPLASTAGNALKSLPEKVGCLFYGSVGNGTYVQSLSVDSLPAKVEVSSIDDPAKASFFESYHTPVPIHNTIATKLGIKESPIKINSQTKYAALSRGDGEVYLRFTRKARPESIWNHAAGSIIVSEAGGKVTDAAGNPLDFSKGKYLDYKR... | 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... |
Q84VY5 | MPYEKELAAAKKAVSLAARLSQEVQKSLLQSDVRSKSDKSPVTAADYGSQAVISHVLERELHPEPLYLVAEENAEDLHKNGAEEFLESITKLVNNALASDDSYANSSLSMDDVRKAIDHGRSQGGSSGRHWILDPVDGTRGFVKGEEYAVALALLVEGKVVLGVMACPKLENHKSSSSGCLFFATVGEGAYVQSLEGDSHPPQKVQVSNIENPEEATFVESSHKPIPIHSSIANKLGIKAPPLRIHSQVKYAALARGDAEIYLRFTLKGYREFIWNHAAGAIITTEAGGVVCDADGNPLDFSRGNHLEHKTGIVVSTKNL... | 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... |
Q9M0Y6 | MYILDTGARFSAVRFSPVFNPPPTSLRRRYFIVRANLPFPKHQAKYHKELEVAIDAVDRACRLCVDVKRSLFSSKEKIVEKNDQTPVTIADFGVQALVSLELSKLFPSIPLVAEEDSHFVRANNLVSSVVSEVKSKASIGDNHLSDADVLEAIDRGGKDAYTFCNKPATYWVLDPIDGTRGFLKGDEALYVVGLALVVDNEIVLGVMGCPNWPGDSSDGSTGTLMLSHIGCGTWTKKLQNVSGNVAGDWIRCFVDACVLMNKARFCIQESQTWESLPLSGFFDASTVSEDLKHKEILLLPTCCGSLCKYLMVASGRASVF... | 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: ... |
Q55F34 | MSLCNLAKIRSVAIKAVEKACIACLDIQKQLISEDTINKKDQSPVTVGDYTVQALVINELLKGLDEEYPIIAEEDSKTLSSQKDVESKVLSFFNRYSNESFVESQLSSLLDKGNKKKDLNSSNRWWTLDPIDGTLGFLRKDQYAVALALMEDNKPILGILGCPNLPVSKGSTEKGCIFVGLKNKGSFMIKLSNLDQEEPIKVSNQSDPTKAIFTESFVSRGFGHELNQKISNSMGVTAEPLKIDSQCKYAMVARGDSDCYLRLTQLDYKECIWDHAAGHIIVEEAGGIVTDFKKQQLDYSKGFKLENNVGIVCSNKLLND... | 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 in... |
Q5BCG1 | MSYERERYIAELAVQRATILTQKVFNEKAKGTVSKDDKSPVTIGDFGAQALIIQAIRKNFPNDEIVAEEEASTLREDKALSAEIWRLVKDIKLEDAESNELLGGSLPSEEAMLDIIDEGKSAGGPKGRIWALDPIDGTKGFLRGGQYAVCLGLLEDGDVKVGAIGCPNLPVDDAATISSSIGVDQNSGAGNGVLFSAIKGAGSVSRPLTSGARAESKSISMRPVPDIAQAVFCEGVEAGHSAQGDNAAVAQLLGITSPSVRLDSQAKYCSIARGAGDIYLRLPVKKDYQEKIWDHAAGDLIVREAGGQVTDIYGQTLDFS... | 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: adenosi... |
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... |
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