ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9WVS9 | MLFTVSCSKMSSIVDRDDSSIFDGLVEEDDKDKAKRVSRNKSEKKRRDQFNVLIKELGSMLPGNARKMDKSTVLQKSIDFLRKHKEITAQSDASEIRQDWKPTFLSNEEFTQLMLEALDGFFLAIMTDGSIIYVSETVTSLLEHLPSDLVDQSIFNFIPEGEHSEVYKILSTHLLESDSLTPEDLKSKNQLEFCCHMLRGTIDPKEPSTYEYVRFIGNFKSLNSVSTSTHNGFEGTIQRTHRPSYEDRVCFVATVRLATPQFIKEMCTVEEPNEEFTSRHSLEWKFLFLDHRAPPIIGYLPFEVLGTSGYDYYHVDDLES... | Function: Transcriptional activator which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism a... |
Q8GHB2 | MPALPIDQEFDCERFRADIRATAAAIGAPIAHRLTDTVLEAFRDNFAQGATLWKTTSQPGDQLSYRFFSRLKMDTVSRAIDAGLLDAAHPTLAVVDAWSSLYGGAPVQSGDFDAGRGMAKTWLYFGGLRPAEDILTVPALPASVQARLKDFLALGLAHVRFAAVDWRHHSANVYFRGKGPLDTVQFARIHALSGSTPPAAHVVEEVLAYMPEDYCVAITLDLHSGDIERVCFYALKVPKNALPRIPTRIARFLEVAPSHDVEECNVIGWSFGRSGDYVKAERSYTGNMAEILAGWNCFFHGEEGRDHDLRALHQHTESTM... | Function: Magnesium-independent aromatic prenyltransferase that catalyzes the irreversible transfer of a dimethylallyl group to 4-hydroxyphenylpyruvate to produce the ring A structure in the clorobiocin biosynthesis pathway. Clorobiocin is an aminocoumarin family antibiotic.
Catalytic Activity: 3-(4-hydroxyphenyl)pyruv... |
P56772 | MPIGVPKVPFRSPGEGDTSWVDIYNRLYRERLFFLGQEVDTEISNQLISLMIYLSIEKDTKDLYLFINSPGGWVISGMAIYDTMQFVRPDVQTICMGLAASIASFILVGGAITKRIAFPHARVMIHQPASSFYEAQTGEFILEAEELLKLRETITRVYVQRTGKPIWVISEDMERDVFMSATEAQAYGIVDLVAVQ | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q85FJ8 | MPIGVPKVPFRLPGEEDAVWVDVYNRLYRERLLFLGQQVDDEIANQLIGIMMYLNSEDQAKDMYLYVNSPGGAVLAGISVYDAMQFVVPDVHTICMGLAASMGSFILAGGEITRRIALPHARVMIHQPASSYYDGQAGECVMEAEEVLKLRDCITKVYAQRTGKPLWLISEDMERDVFLSAEEAQDYGVVDLVAVENVSR | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
A7M988 | MPIGVPRVRFQYRRDRSRVWIDIYNRLYRERCLFLAHVVESQIANQLVGLFIYLGVQDETKDIFLFINSPGGGIISGFAIYDTMQFVRPDIQTICVGLAASMGSFLLVGGAITKRLAFPHARVMIHQPMSAFFETQTVEAILEAEELLKLRESLAKVYVQRTGKPDWVIAEDMERDVFLSATEAQSYGIVDVVGVALASKG | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity).
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the ... |
Q3Z8J8 | MISPENVVPMVIESSARGERAFDIYSLLLKERIIFLGSQINDQVANLVIAQLLFLDREDPDKDISLYIHSPGGVISAGLAMYDTMQLIRPKVSTICVGVAASMATVLLCAGAKGKRYALPNATIHMHQAMGGAQGQASDIEIAAREIMRQQDILRNILVKHTGQPMEKIIHDSDRDYYLNAQQAVEYGLIDEILQKPENK | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q9RSZ7 | MEVMSVIPYVIEQTGRGERSYDIYSRLLKDRIIFVGTPVESQMANSIVAQLLLLDSQNPEQEIQMYINCPGGEVYAGLAIYDTMRYIKAPVSTICVGMAMSMGSVLLMAGDKGKRMALPNSRIMIHQGSAGFRGNTPDLEVQAKEVLKLRDTLVDIYHKHTDLPQEKLLRDMERDYFMSPEEALKYGLIDQVIDQTRENRGGEE | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
A4J7L9 | MSGLVPIVVEQTNRGERAYDIYSRLLKDRIIFIGGPIDDHIANLVIAQFLFLEAEDPEKDIHLYINSPGGVVTAGLAIYDTMQYIKPAVSTICLGQAASMGSFLLAAGAPGKRYALPMARIMIHQPLGGVQGQATDIDIHAKEILRMKDLLNDRLAHHTGQPLEQITRDTERDYFMSAEEAKKYGLIDEVMPYRK | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q72CE8 | MPVPIVIESTGRAERAYDIYSRLLKDRIVLLGTPIDDQVASLICAQLLFLESENPEKEIHMYINSPGGSVTAGMAIYDTMQYINSPVSTLCMGQAASMGALLLAAGAPGLRFSLPHSRIMIHQPSGGFQGQATDIDIQAREVLRLKQSLNAIMSQHTGKPLEQVALDTERDYFMGPEEAQAYGLIDRVLTSRSEATDTISK | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q06FP3 | MPVGVPKVPFLNPNPDPEPDSVEEELDSMEEKATWVDLYNRLYRQRWLFLGKDLEEEVANNIVGLMIHLNIEDPFWTQTLYINCLGGLIIPGLALYDTIGFVEPDVKTICLGIAASMASVVLVGGTVTERCAFPNARVMIHQPRAKEFDDRFSDLNLEGHLFLQLRNCVTQIYIHRTNKPAWVIIADLERDTFMSATEARTYGIIDGVYAFEEEYEEWS | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q3BAL3 | MPIGVPKVPFRNPGEEDAVWVDVYNRLHRERLLFLGQEVDSEISNQIVGLMVYLSIEDDTRDLYLFINSPGGWVIPGIAIYDTMQFVLPDVHTICMGLAASMGSFILVGGEITKRLAFPHARVMIHQPASSFYEAQARDFILEAEELLKLRETLTKVYVQRTGNPLWVISEDMERDVFMSATEAQAHGIVDLVAIENENTGNSI | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q6YXM7 | MPIGVPKVPFRLPGEEDAVWIDVYNNRLYRERLLFLGQHVDDEIANQLIGIMMYLNGEDENKDMYLYINSPGGAVLAGISVYDAMQFVVPDVHTICMGLAASMGSFILAGGEITKRIALPHARVMIHQPASSYYDGQAGECIMEAEEVLKLRDYITRVYVQRIGKPLWVISEDMERDVFMSAQEAKTYGIVDLVAIENT | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
P84723 | APTEADATWVDLYNRVMIHQPASSYYAAEMHNEAKTDNPEEVLDLDRDVFMSAAYGIVDTVWYVQAELVNGRGGAVVAGL | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins (By similarity).
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the ... |
A4GYT6 | MPIGVPKVPFRNPGEDSSNWIDVYNRLYRERLLFLGQDIDSEISNQLIGLMVYLSTESEIKDLYLFINSPGGWVIPGIAIYDTMQFVRPDVQTVCMGLAASMGSFILVGGKITKRLAFPHARVMIHQPFAAFYEAQIGEFVLEAEELLKLREILTRVYAQRTGKPLWVVSEDMERDVFMSAAEAQVHGIVDLVAVA | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
B5YI38 | MSIVPIVIEQTGRTERVYDIYSRLLKDRIIFIGTEINDHVANVVIAQLLFLQTEDPEKDIHIYINSPGGMVSSGLAIYDTMQYVKPDIATYCIGQASSMACVLLAAGTKGKRFALPHSRVMIHQPIGGFYGQATDVEIHAKEILKMKDLLNNILAKHTGQPIEKIQKDTERDFFMSAEEAKLYGIVDEVISSIKK | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
Q0ZIZ4 | MPIGVPKVPFRNPGEDDISWIDVYNRLYRERLLFLGQEVESEISNQLIGLMIYLSIEDENKDLYFFINSPGGWVLPGIAIYDTMQFVPPEVHTICLGLAASMGSFILVGGTITKRLAFPHARVMIHQPAAAFYEAQAGEFVMEAEELLKLREIITKVYVQRTGKPLWVVSEDLERDVFMSATEAQTHGIVDLVAVQ | Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Catalytic Activity: Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test subst... |
P45865 | MKVFIVIMIIVVIFFALILLDIFMGRAGYRKKAYEPVFSKKKSDIELIHCGADLVERMMNDIRQAASSVHMMFFIMKNDEVSHNMYTLLKTKAQAGVSVYLLLDWAGCRAIKKTALQTMKNAGVHVHVMNRPRFPFFFFHMQKRNHRKITVIDGKIGYIGGFNIAEEYLGKKAKFGNWEDYHLRMIGEGVHDLQTLFASDLKRNTGIELGSDVWPKLQQGTISHKIYATDGYSLENIYLANIAQAKNRLTVCTPYYIPSKPLQEALINARKNGVSVRIIVPMKSDHPLVREAAFTYYSELLDAGCLIYRYYQGFYHVKAL... | Function: Involved in the biosynthesis of cardiolipin.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 45842
Sequence Length: 398
Subcellular Location: Cell membrane
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P59715 | MKCSWREGNKIQLLENGEQYYPAVFKAIGEAQERIILETFIWFEDNVGKQLHAALLAAAQRGVKAEVLLDGYGSPDLSDEFVNELTAAGVVFRYYDPRPRLFGMRTNVFRRMHRKIVVIDARIAFIGGLNYSSEHMSSYGPEAKQDYAVRLEGPIVEDILQFELENLPGQSAARRWWRRHHKAEENRQPGEAQVLLVWRDNEEHRDDIERHYLKMLTQAQREVIIANAYFFPGYRFLHALRKAARRGVRIKLIIQGEPDMPIVRVGARLLYNYLVKGGVQVFEYRRRPLHGKVALMDDHWATVGSSNLDPLSLSLNLEAN... | Function: Catalyzes the phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Catalytic Activity: 2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol
Location Topology: Peripheral membrane protein
Sequence ... |
P75919 | MPRLASAVLPLCSQHPGQCGLFPLEKSLDAFAARYRLAEMAEHTLDVQYYIWQDDMSGRLLFSALLAAAKRGVRVRLLLDDNNTPGLDDILRLLDSHPRIEVRLFNPFSFRLLRPLGYITDFSRLNRRMHNKSFTVDGVVTLVGGRNIGDAYFGAGEEPLFSDLDVMAIGPVVEDVADDFARYWYCKSVSPLQQVLDVPEGEMADRIELPASWHNDAMTHRYLRKMESSPFINHLVDGTLPLIWAKTRLLSDDPAKGEGKAKRHSLLPQRLFDIMGSPSERIDIISSYFVPTRAGVAQLLRMVRKGVKIAILTNSLAAND... | Function: Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) from phosphatidylglycerol (PG) and phosphatidylethanolamine (PE).
Catalytic Activity: 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine = a cardiolipin + ethanolamine
Sequence Mass (Da): 53666
S... |
O66043 | MKNRLNVLAFFALLFAALYISRGFLQSWMVGTLSVVFTLSVIFIGIIIFFENRHPTKTLTWLLVLAAFPVVGFFFYLMFGQNHRKSKRFSKKAIEDERAFQKIEGQRQLNEEQLKKMGGHQQLLFRLAHKLGKNPISFSSETKVLTDGKETYAHILQALKMAEHHIHLEYYIVRHDDLGNQIKDILISKAKEGVHVRFLYDGVGSWKLSKSYVEELRDAGVEMVSFSPVKLPFLTHTINYRNHRKIIVIDGVVGFVGGLNIGDEYLGKDAYFGYWRDTHLYVRGEAVRTLQLIFLQDWHYQTGETILNQTYLSPSLSMTK... | Function: Catalyzes the reversible phosphatidyl group transfer from one phosphatidylglycerol molecule to another to form cardiolipin (CL) (diphosphatidylglycerol) and glycerol.
Catalytic Activity: 2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a cardiolipin + glycerol
Location Topology: Multi-pass membrane protei... |
Q93YW7 | MAIYRSLRKLVEINHRKTRPFFTAATASGGTVSLTPPQFSPLFPHFSHRLSPLSKWFVPLNGPLFLSSPPWKLLQSATPLHWRGNGSVLKKVEALNLRLDRIRSRTRFPRQLGLQSVVPNILTVDRNDSKEEDGGKLVKSFVNVPNMISMARLVSGPVLWWMISNEMYSSAFLGLAVSGASDWLDGYVARRMKINSVVGSYLDPLADKVLIGCVAVAMVQKDLLHPGLVGIVLLRDVALVGGAVYLRALNLDWKWKTWSDFFNLDGSSPQKVEPLFISKVNTVFQLTLVAGAILQPEFGNPDTQTWITYLSWLVASTTMA... | Function: Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). Cannot catalyze the phosphatidyl group transfer from one PG molecule to another to form CL. Possesses high activity with PG species carry... |
Q54MZ9 | MKGELIDITMKSGLKCDAYVSRPKDSQKELKPVIFVMDAFGLRDWLYEMADKIAEEGYFVVQPNFYYRIGKNIITNLEKLKSADTKDEVICQIRTQMAKINREETVSDVSEMFDFIDKQEGVRKSKEGVAIVGYCFGGGVAMRSAIAFPDIVKVVASFHAGRLAIPDDENSIHKHLKGVKAECYFGHADNDQSMPLDQIHLFEKSLTEAGIKYTSEIYNNPSCAHGWVMGDTLMYNPIGSDKHYDELFKLLKRAL | Function: Cysteine hydrolase.
Sequence Mass (Da): 28841
Sequence Length: 255
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q96DG6 | MANEAYPCPCDIGHRLEYGGLGREVQVEHIKAYVTKSPVDAGKAVIVIQDIFGWQLPNTRYIADMISGNGYTTIVPDFFVGQEPWDPSGDWSIFPEWLKTRNAQKIDREISAILKYLKQQCHAQKIGIVGFCWGGTAVHHLMMKYSEFRAGVSVYGIVKDSEDIYNLKNPTLFIFAENDVVIPLKDVSLLTQKLKEHCKVEYQIKTFSGQTHGFVHRKREDCSPADKPYIDEARRNLIEWLNKYM | Function: Cysteine hydrolase. Can convert the prodrug olmesartan medoxomil into its pharmacologically active metabolite olmerstatan, an angiotensin receptor blocker, in liver and intestine. May also activate beta-lactam antibiotics faropenem medoxomil and lenampicillin.
Sequence Mass (Da): 28048
Sequence Length: 245
Su... |
Q8R1G2 | MANEANPCPCDIGHKLEYGGMGHEVQVEHIKAYVTRSPVDAGKAVIVVQDIFGWQLPNTRYMADMIARNGYTTIVPDFFVGQEPWDPAGDWSTFPAWLKSRNARKVNREVDAVLRYLRQQCHAQKIGIVGFCWGGVVVHQVMTAYPDIRAGVSVYGIIRDSEDVYNLKNPTLFIFAENDTVIPLEQVSTLTQKLKEHCIVNYQVKTFSGQTHGFVHRKREDCSPADKPYIEEARRNLIEWLNKYV | Function: Cysteine hydrolase.
Sequence Mass (Da): 27902
Sequence Length: 245
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q6P7K0 | MANEACPCPCDIGDKIEYGAKGQEVQIEHIKAYVSKPHSSTDKAVIVVQDIFGWQLPNTRFMADLLTAHGYITICPDFFVGQEPWKPSNDRSTFTEWLQTRQATKVEKEINVVLKYLKEQCHVKKIGVIGFCWGGVVTHHLMLKYPELKAGVSFYGIIRDVEDRYNLLNPTLFIFAEMDHVIPLEQVSLLEEKLKVHSKVDFQVKVFPKQTHGFVHRKNEDINPEDKPFIEEARKNMLEWLHKYIN | Function: Cysteine hydrolase.
Sequence Mass (Da): 28471
Sequence Length: 246
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q21153 | MSFDHLLTSSKRRELLQNLGIGHGSDVFSTGLFRKAECNAETAISQRSIPRANPDHLRPIFDRFATKEIKGKKLMTPEDFIRGYLGLYTEENYNKETVRLLASAADTTKDGDISFEEFCAFEALLCSPDALYLTAFELFDRNASDTISCDEFEAVIRHTQPLHDQDFDFSSEFIKRYFGADKQRNVNYHSFCQLLHDFYEEQGIQAFKRYDKNGNGTISSLDFQQIMTTVKGHLLTDFVRHNLIAVSGGGASGHKFSDTRGGFVTFPYYAAFNSLLAKMELIKRVYVSTTRGNLDIEMTKEEFLHAIQSYTQVTPYEVEI... | Function: Mitochondrial and calcium-binding carrier that catalyzes the calcium-dependent exchange of cytoplasmic glutamate with mitochondrial aspartate across the mitochondrial inner membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 79595
Sequence Length: 716
Domain: Upon calcium binding, the... |
D6W196 | MLLKNCETDKQRDIRYACLFKELDVKGNGQVTLDNLISAFEKNDHPLKGNDEAIKMLFTAMDVNKDSVVDLSDFKKYASNAESQIWNGFQRIDLDHDGKIGINEINRYLSDLDNQSICNNELNHELSNEKVNKFSRFFEWAFPKRKANIALRGQASHKKNTDNDRSKKTTDSDLYVTYDQWRDFLLLVPRKQGSRLHTAYSYFYLFNEDVDLSSEGDVTLINDFIRGFGFFIAGGISGVISRTCTAPFDRLKVFLIARTDLSSILLNSKTDLLAKNPNADINKISSPLAKAVKSLYRQGGIKAFYVGNGLNVIKVFPESS... | Function: Calcium-dependent mitochondrial solute carrier.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55715
Sequence Length: 494
Subcellular Location: Mitochondrion inner membrane
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P0CI40 | MLLKNCETDKQRDIRYACLFKELDVKGNGQVTLDNLISAFEKNDHPLKGNDEAIKMLFTAMDVNKDSVVDLSDFKKYASNAESQIWNGFQRIDLDHDGKIGINEINRYLSDLDNQSICNNELNHELSNEKMNKFSRFFEWAFPKRKANIALRGQASHKKNTDNDRSKKTTDSDLYVTYDQWRDFLLLVPRKQGSRLHTAYSYFYLFNEDVDLSSEGDVTLINDFIRGFGFFIAGGISGVISRTCTAPFDRLKVFLIARTDLSSILLNSKTDLLAKNPNADINKISSPLAKAVKSLYRQGGIKAFYVGNGLNVIKVFPESS... | Function: Calcium-dependent mitochondrial solute carrier.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61270
Sequence Length: 545
Subcellular Location: Mitochondrion inner membrane
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Q20799 | MINKNEQTESTSGAAEQKEDDEEQYVQLSSLGEYKDEVTPLLSPKHVPLVLGKVTKEAAIATHSALHGGMSEEKERQIRDIYDRLDIDNDGTIDIRDLTLALKHETPHIPANLAPVIMSKMSPDDEGRVDFYSFSSYVLENEQKLAEMFADMDRNHDGLVDVVEMKNYCKDIGVPLDDHKAQHIVNKMDQTGSASVDLKEFQEFMMLYPSSDLKDIVDFWRHNLIIDIGEDSQIPEDFSQQEMQEGIWWRHLVAGGAAGAVSRTCTAPFDRIKVYLQVNSSKTNRLGVMSCLKLLHAEGGIKSFWRGNGINVIKIAPESA... | Function: Mitochondrial and calcium-binding carrier that catalyzes the calcium-dependent exchange of cytoplasmic glutamate with mitochondrial aspartate across the mitochondrial inner membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66337
Sequence Length: 588
Subcellular Location: Mitochondri... |
F2RB81 | MVELPDLLTDLFRRHRGRTALRTAGRTWTYEELDRVTSALARRIDAECPAGRRVLVAGEHTAEAVVWALAAMRSHAVHTPMNPGLPADRFEEFARVADAALLVCFEREALVRGEKAGLRALYAGDVGWPTDPAPAPADGTADEPARSRVAYSIFTSGSTGDPKLVDVGHGGLLNLCRSLRRLLDITPDDQVLHFASLSFDASVSEILGTLYAGATLVVPVRDQASWLGSVSRHLAAHGCDLAMLSPSVYARLDEAARSRIRKVEFCGEALGEGEYDKAARYSRVFNAYGPTEATVCFSLAELTSYTPSIGTPVDGFRAYV... | Cofactor: Binds 1 phosphopantetheine covalently.
Function: Involved in chloramphenicol biosynthesis . Activates 4-amino-L-phenylalanine by adenylation and loads it onto its peptidyl carrier domain, via a thioester linkage to the phosphopanthetheine moiety . Can also adenylate tyrosine and phenylalanine at low rates, bu... |
B2K217 | MNIDKIFENPSNLRSFEFNNDVCKVFDDMVSRSVPGYHNIQDIISLTYDEFSQNRVFIDVGCSTGTTIAKILSENQVNYCYGIDISESMLAIAQEKCGEHESLVTFKNCNLLNGTDNVINSEKVPDFIILNLVLQFIRPPERKKFITNIKSLCSSSTLMLVFEKIIFNDAEINMKYIDSYLKWKGKNGYSESEVSNKRKALENKLIPYLHEENIELFKSSGFNSVEICFSFLNFRGYLCRC | Function: Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
Catalytic Activity: prephenate + S-adenosyl-L-methionine = 3-phenylpyruvate + carboxy-S-adenosyl-L-methionine + H2O
Sequence Mass (Da): 27715
Sequence Length: 241
EC: 2.1.3.-
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A8EVV4 | MIDKVFNKSITKQFEFDEEVASVFDDMLNRSVPFYKEMQRLSINFACNFLSENDKVYDLGCSTASTLIELSKHCKHNLKLIGIDNSDAMLKRASNKAKAFGVEIELINADLHDVTYNDAKLILSNYTLQFIRPLQREKLVKKIYDSLDEKGIFIFSEKVISTNSNLNKQCIDEYYEFKKTQGYSEFEISQKREALENVLIPYTEDENKKMIKDAGFSHCETIFKWVNFATFIAIK | Function: Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
Catalytic Activity: prephenate + S-adenosyl-L-methionine = 3-phenylpyruvate + carboxy-S-adenosyl-L-methionine + H2O
Sequence Mass (Da): 27291
Sequence Length: 235
EC: 2.1.3.-
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Q4FQB1 | MSHPMSQSQPATVKHDTLFTTPLDKAARFSFDEQVVACFPDMIRRSVPGYGQVLAMLPIFARRHCKYRQQGDNGQRVSRIYDLGCSLGAASMTLAGEFESQDLQIKAIDISPAMTTEATTLLSDNYPEHDIEVITADIRDIEFEPCDMVILNLTLQFLPAADRVAVLEKIYAALSEGGILVLTEKTHAFDEQYDAWLVERYYDFKRANGYTEMEISGKRNALENVLITDTLDEHHTRLAQVGFQRHLTWFQFLNFVSIVAFK | Function: Catalyzes the conversion of S-adenosyl-L-methionine (SAM) to carboxy-S-adenosyl-L-methionine (Cx-SAM).
Catalytic Activity: prephenate + S-adenosyl-L-methionine = 3-phenylpyruvate + carboxy-S-adenosyl-L-methionine + H2O
Sequence Mass (Da): 29723
Sequence Length: 262
EC: 2.1.3.-
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A5WC55 | MTNHTITTAERELYLALIQRAQYRPIATQWLANLPQWLSDVKDKRRYAHAPAYLSAVENLPQIKVKNVDLNSDILTIDADLTDGQSKQITALMKQLMPWRKGPFQIGSGDNKVFIDTEWHSDWKWNRIKPHLGTLQGRYVLDVGGGSGYHGWRMAGAGAKQVVIIDPSCLFYHQFMAIRHFVAGFDTDMDSDRTGVGYRTHYIPVGLEQLPSSSDQGNQLFDTVFCMGVLYHRQSPFEHLIQLKNQLINGGQLVLETLVIEGDANTVLVPHNRYAKMNNVYFIPSVAALTGWLEKVGFSEVKCVDIDITSIKEQRATDWM... | Function: Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs.
Catalytic Activity: 5-hydroxyuridine(34) in tRNA + carboxy-S-adenosyl-L-methionine = 5-carboxymethoxyuridine(34) in tRNA + H(+) + S-adenosy... |
A1AVT4 | MLSDFYKYATSTQLDLICTQLINLSTHVFNTNNGNIPKWEQAIKQIKTQNTGSLDFITPYLNISAHHINNFTLEKSLKQLIPWRKGPYQIGDLQLDSEWRGDMKWHRLIPHIKPLKDKVVLDVGSGNGYFTYLMAISGAKIALGIEPFLLFNYQFQAIRTLINNLPNVFVLPLSLDKIPKKPLFDTVFSMGVLYHQKDYELHLNQLKDVMKPSGELILETLIIDLEKVKKIIPKGRYAKMRNVYCLPSKNTLRTWLEDAEFKNIKLLDVTKTTSKEQRATHWIGNNTQSLKNFLDPNNRDLTIEGFPAPKRAIFICQK | Function: Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs.
Catalytic Activity: 5-hydroxyuridine(34) in tRNA + carboxy-S-adenosyl-L-methionine = 5-carboxymethoxyuridine(34) in tRNA + H(+) + S-adenosy... |
Q21JL7 | MIDYTSFLEQEKEGPLARWVEILPDQISEGLSTKRYGDLEQWLTAMQNLPQVDNVQVSYQSAVTLKSTAPLAQETHTLIEQQFRALIPWRKGPYNIFDIEIDTEWHSDWKWDRVLPHLAPLKHRKILDVGCGNGYHCWRMYGEGASQVIGIDPSPRFVVQFYMLKHFIGSNAPVDLLPVPMEAVPANLQAFDTTFSMGVLYHRRSPMDHLRELKATLRPGGQLVLETLVIEGKLGEVLVPEGRYAMMNNVWFLPSVPTLISWLTKCGFKNARCVDVNQTSTDEQRSTEWMTFQSLSDFLDPNDPTLTAEGHPAPLRAVIL... | Function: Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs.
Catalytic Activity: 5-hydroxyuridine(34) in tRNA + carboxy-S-adenosyl-L-methionine = 5-carboxymethoxyuridine(34) in tRNA + H(+) + S-adenosy... |
Q8ZNV1 | MIEFGNFYQLIAKNHLSHWLETLPAQIASWQREQQHGLFKQWSNAVEFLPEMTPWRLDLLHSVTAESETPLSEGQLKRIDTLLRNLMPWRKGPFSLYGVDIDTEWRSDWKWDRVLPHLSDLTGRTILDVGCGSGYHLWRMIGAGAHLAVGIDPTQLFLCQFEAVRKLLGNDQRAHLLPLGIEQLPALKAFDTVFSMGVLYHRRSPLEHLWQLKDQLVNEGELVLETLVIDGDENTVLVPGDRYAQMRNVYFIPSAPALKKWLEKCGFIDVRIADVCVTTTEEQRRTEWMVTESLADFLDPNDRSKTVEGYPAPQRAVLIA... | Function: Catalyzes carboxymethyl transfer from carboxy-S-adenosyl-L-methionine (Cx-SAM) to 5-hydroxyuridine (ho5U) to form 5-carboxymethoxyuridine (cmo5U) at position 34 in tRNAs.
Catalytic Activity: 5-hydroxyuridine(34) in tRNA + carboxy-S-adenosyl-L-methionine = 5-carboxymethoxyuridine(34) in tRNA + H(+) + S-adenosy... |
G7IBJ4 | MASVISRAVRFHDDLEKEKLQEGEESHMEMRAYEMSSEYKHGKDAINKPSSNGRGLSRVFSEDYDAGEILVFDPRGPRINLWNKIFLAACLISLFVDPLFFYLPVAKKEKCIDMSIGLEVSLTIIRTFVDAFYIIHIYIRFQTAYIAPSSRVSGRGELIIDSSKIASNYMKKELWSDLVAALPLPQVLIWAVIPNIKGSEMIASRHVVRLVSIFQYLLRLYLIYPLSSKITKASGVMMEKAWAGAAYYLTLYMLASHVLGSTWYLLSIERQDECWKKACTLQYPHCQYHYLDCQSLSDPNRNAWLKSSNLSGLCDQNSHF... | Function: Cyclic nucleotide-gated channel involved in the establishment of both rhizobial and mycorrhizal associations . Required for full activation of nuclear-localized Ca(2+) oscillations by Nod and Myc factors . Simultaneous activation of the K(+)-permeable channel DMI1 and the Ca(2+) channel CNGC15 can give rise t... |
G7JND3 | MVTPKFMSDLFEGDHLELAKLTSPNGDNGIKFNEKHVAPRVLSRVFSEDYKRVKRRRRIFDPRGQTIHQWNKIFLVACLISLFVDPLFFYLPIVQDEVCIDIGIAVEVFLIIIRSIADVFYVIHIFMRFHTAYVAPSSRVFGRGELVIDSSKIASRYLHKGFFLDFIAALPLPQVLIWIVIPNLGGSTIANTKNVLRFIIIIQYLPRLFLIFPLSSQIVKATGVVTETAWAGAAYNLMLYMLASHVLGACWYLLSIERQEACWKSVCKLEESSCQFDFFDCNMVKDSLRVSWFVTSNVTNLCSPNSLFYQFGIYGDAVTS... | Function: Cyclic nucleotide-gated channel involved in the establishment of both rhizobial and mycorrhizal associations . Required for full activation of nuclear-localized Ca(2+) oscillations by Nod and Myc factors . Simultaneous activation of the K(+)-permeable channel DMI1 and the Ca(2+) channel CNGC15 can give rise t... |
Q00195 | MMTEKSNGVKSSPANNHNHHPPPSIKANGKDDHRAGSRPQSVAADDDTSPELQRLAEMDTPRRGRGGFQRIVRLVGVIRDWANKNFREEEPRPDSFLERFRGPELQTVTTHQGDDKGGKDGEGKGTKKKFELFVLDPAGDWYYRWLFVIAMPVLYNWCLLVARACFSDLQRNYFVVWLVLDYFSDTVYIADLIIRLRTGFLEQGLLVKDPKKLRDNYIHTLQFKLDVASIIPTDLIYFAVGIHSPEVRFNRLLHFARMFEFFDRTETRTSYPNIFRISNLVLYILVIIHWNACIYYVISKSIGFGVDTWVYPNITDPEYG... | Function: Odorant signal transduction is probably mediated by a G-protein coupled cascade using cAMP as second messenger. The olfactory channel can be shown to be activated by cyclic nucleotides which leads to a depolarization of olfactory sensory neurons.
Location Topology: Multi-pass membrane protein
Sequence Mass (D... |
Q16281 | MAKINTQYSHPSRTHLKVKTSDRDLNRAENGLSRAHSSSEETSSVLQPGIAMETRGLADSGQGSFTGQGIARLSRLIFLLRRWAARHVHHQDQGPDSFPDRFRGAELKEVSSQESNAQANVGSQEPADRGRSAWPLAKCNTNTSNNTEEEKKTKKKDAIVVDPSSNLYYRWLTAIALPVFYNWYLLICRACFDELQSEYLMLWLVLDYSADVLYVLDVLVRARTGFLEQGLMVSDTNRLWQHYKTTTQFKLDVLSLVPTDLAYLKVGTNYPEVRFNRLLKFSRLFEFFDRTETRTNYPNMFRIGNLVLYILIIIHWNACI... | Function: Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cyclic GMP which leads to an opening of the cation channel and thereby causing a depolarization of cone photoreceptors. Induced a flickering channel gating, weakened the outwa... |
Q9JJZ8 | MAKVNTQCSQPSPTQLSIKNADRDLDHVENGLGRVSRLIISIRAWASRHLHDEDQTPDSFLDRFHGSELKEVSTRESNAQPNPGEQKPPDGGEGRKEEPIVVDPSSNIYYRWLTAIALPVFYNWCLLVCRACFDELQSEHLTLWLVLDYSADVLYVLDMLVRARTGFLEQGLMVRDTKRLWKHYTKTLHFKLDILSLIPTDLAYLKLGVNYPELRFNRLLKFSRLFEFFDRTETRTNYPNVFRIGNLVLYTLIIIHWNACIYFAISKFIGFGTDSWVYPNTSKPEYARLSRKYIYSLYWSTLTLTTIGETPPPVKDEEYL... | Function: Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cyclic GMP which leads to an opening of the cation channel and thereby causing a depolarization of cone photoreceptors. Essential for the generation of light-evoked electrical... |
Q3UW12 | MSQDSKVKTTESTPPAPTKARKWLPVLDPSGDYYYWWLNTMVFPIMYNLIIVVCRACFPDLQHSYLVAWFVLDYTSDLLYLLDIGVRFHTGFLEQGILVVDKSMIASRYVRTWSFLLDLASLVPTDAAYVQLGPHIPTLRLNRFLRVPRLFEAFDRTETRTAYPNAFRIAKLMIYIFVVIHWNSCLYFALSRYLGFGRDAWVYPDPAQPGFERLRRQYLYSFYFSTLILTTVGDTPLPAREEEYLFMVGDFLLAVMGFATIMGSMSSVIYNMNTADAAFYPDHALVKKYMKLQHVNRRLERRVIDWYQHLQINKKMTNEV... | Function: Second messenger, cAMP, causes the opening of cation-selective cyclic nucleotide-gated (CNG) channels and depolarization of the neuron (olfactory sensory neurons, OSNs). CNGA4 is the modulatory subunit of this channel which is known to play a central role in the transduction of odorant signals and subsequent ... |
Q64359 | MSQDGKVKTTESTPPAPTKARKWLPVLDPSGDYYYWWLNTMVFPIMYNLIIVVCRACFPDLQHSYLVAWFVLDYTSDLLYLLDIGVRFHTGFLEQGILVVDKGMIASRYVRTWSFLLDLASLVPTDAAYVQLGPHIPTLRLNRFLRVPRLFEAFDRTETRTAYPNAFRIAKLMLYIFVVIHWNSCLYFALSRYLGFGRDAWVYPDPAQPGFERLRRQYLYSFYFSTLILTTVGDTPLPDREEEYLFMVGDFLLAVMGFATIMGSMSSVIYNMNTADAAFYPDHALVKKYMKLQHVNKRLERRVIDWYQHLQINKKMTNEV... | Function: Second messenger, cAMP, causes the opening of cation-selective cyclic nucleotide-gated (CNG) channels and depolarization of the neuron (olfactory sensory neurons, OSNs). CNGA4 is the modulatory subunit of this channel which is known to play a central role in the transduction of odorant signals and subsequent ... |
Q24278 | MRHFKVKAMVQSLDISAITGQQTDAEPSKRSKPSALRRTLQALRQRLTKRNRPKPPDWFLEKFSNTTNTDKIGKGCPAMEDAALSSEIRGSSVLCNRLSVDPTLQSHYRWLAIVSLAVLYNIIFVVGRAVFWEINKSAPAFWYTLDYLCDFIYLLDTLVHMHEGFLDQGLLVRDAFRLRRHYFHTKGWYLDVLSMLPTDLAYIWWPPETCSSLYLPCPVIVRLNRLLRINRLWEWFDRTETATGYPNAFRICKVVLAILVLIHWNACMYFAISYEIGFSSDSWVYNLNGTRNNTLQRQYIYSFYWSTLTLTTIGETPTPE... | Function: Approximately 50-fold more sensitive to cGMP than to cAMP. May be involved in transduction cascades of both invertebrate photoreceptors and olfactory sensillae.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75823
Sequence Length: 665
Subcellular Location: Membrane
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Q9NQW8 | MFKSLTKVNKVKPIGENNENEQSSRRNEEGSHPSNQSQQTTAQEENKGEEKSLKTKSTPVTSEEPHTNIQDKLSKKNSSGDLTTNPDPQNAAEPTGTVPEQKEMDPGKEGPNSPQNKPPAAPVINEYADAQLHNLVKRMRQRTALYKKKLVEGDLSSPEASPQTAKPTAVPPVKESDDKPTEHYYRLLWFKVKKMPLTEYLKRIKLPNSIDSYTDRLYLLWLLLVTLAYNWNCCFIPLRLVFPYQTADNIHYWLIADIICDIIYLYDMLFIQPRLQFVRGGDIIVDSNELRKHYRTSTKFQLDVASIIPFDICYLFFGFN... | Function: Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cGMP which leads to an opening of the cation channel and thereby causing a depolarization of rod photoreceptors. Induced a flickering channel gating, weakened the outward rect... |
O65717 | MNFRQEKFVRFQDWKSDKTSSDVEYSGKNEIQTGIFQRTISSISDKFYRSFESSSARIKLFKRSYKSYSFKEAVSKGIGSTHKILDPQGPFLQRWNKIFVLACIIAVSLDPLFFYVPIIDDAKKCLGIDKKMEITASVLRSFTDVFYVLHIIFQFRTGFIAPSSRVFGRGVLVEDKREIAKRYLSSHFIIDILAVLPLPQMVILIIIPHMRGSSSLNTKNMLKFIVFFQYIPRFIRIYPLYKEVTRTSGILTETAWAGAAFNLFLYMLASHVFGAFWYLFSIERETVCWKQACERNNPPCISKLLYCDPETAGGNAFLNE... | Function: Acts as cyclic nucleotide-gated ion channel. Can be activated by cyclic AMP which leads to an opening of the cation channel. May be responsible for cAMP-induced calcium entry in cells and thus should be involved in the calcium signal transduction. Could transport K(+), Na(+) and Pb(2+).
Location Topology: Mul... |
O65718 | MPSHPNFIFRWIGLFSDKFRRQTTGIDENSNLQINGGDSSSSGSDETPVLSSVECYACTQVGVPAFHSTSCDQAHAPEWRASAGSSLVPIQEGSVPNPARTRFRRLKGPFGEVLDPRSKRVQRWNRALLLARGMALAVDPLFFYALSIGRTTGPACLYMDGAFAAVVTVLRTCLDAVHLWHVWLQFRLAYVSRESLVVGCGKLVWDPRAIASHYARSLTGFWFDVIVILPVPQAVFWLVVPKLIREEKVKLIMTILLLIFLFQFLPKIYHCICLMRRMQKVTGYIFGTIWWGFALNLIAYFIASHVAGGCWYVLAIQRVA... | Function: Acts as cyclic nucleotide-gated ion channel. Permeable to potassium and calcium in a cyclic nucleotide-dependent fashion (cAMP or cGMP). Could also transport lithium, cesium and rubium and displays a strong selectivity against sodium. Seems to directly participate in pathogen-induced calcium influx. May funct... |
Q9SKD7 | MMNPQRNKFVRFNGNDDEFSTKTTRPSVSSVMKTVRRSFEKGSEKIRTFKRPLSVHSNKNKENNKKKKILRVMNPNDSYLQSWNKIFLLLSVVALAFDPLFFYIPYVKPERFCLNLDKKLQTIACVFRTFIDAFYVVHMLFQFHTGFITPSSSGFGRGELNEKHKDIALRYLGSYFLIDLLSILPIPQVVVLAIVPRMRRPASLVAKELLKWVIFCQYVPRIARIYPLFKEVTRTSGLVTETAWAGAALNLFLYMLASHVFGSFWYLISIERKDRCWREACAKIQNCTHAYLYCSPTGEDNRLFLNGSCPLIDPEEITNS... | Function: Probable cyclic nucleotide-gated ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81669
Sequence Length: 706
Domain: The binding of calmodulin to the C-terminus might interfere with cyclic nucleotide binding and thus channel activation.
Subcellular Location: Cell membrane
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Q94AS9 | MATEQEFTRASRFSRDSSSVGYYSEEDNTEEEDEEEEEMEEIEEEEEEEEEEDPRIGLTCGGRRNGSSNNNKWMMLGRILDPRSKWVREWNKVFLLVCATGLFVDPLFLYTLSVSDTCMCLLVDGWLALTVTALRSMTDLLHLWNIWIQFKIARRWPYPGGDSDGDTNKGGGTRGSTRVAPPYVKKNGFFFDLFVILPLPQVVLWVVIPSLLKRGSVTLVVSVLLVTFLFQYLPKIYHSIRHLRRNATLSGYIFGTVWWGIALNMIAYFVAAHAAGACWYLLGVQRSAKCLKEQCENTIGCDLRMLSCKEPVYYGTTVMV... | Function: Acts as cyclic nucleotide-gated ion channel. Permeable to potassium and sodium in a cyclic nucleotide-dependent fashion (cAMP or cGMP). Might constitute a common downstream component of the signaling pathways leading to hypersensitive response (HR).
Location Topology: Multi-pass membrane protein
Sequence Mass... |
Q8RWS9 | MAGKRENFVRVDDLDSRLPSSSVAFQQNYASNFSGQLHPIHASNETSRSFKKGIQKGSKGLKSIGRSLGFGVYRAVFPEDLKVSEKKIFDPQDKFLLYCNKLFVASCILSVFVDPFFFYLPVINAESKCLGIDRKLAITASTLRTFIDVFYLAHMALQLRTAYIAPSSRVFGRGELVIDPAQIAKRYLQRWFIIDFLSVLPLPQIVVWRFLQSSNGSDVLATKQALLFIVLVQYIPRFLRVLPLTSELKRTAGVFAETAWAGAAYYLLLYMLASHIVGAFWYLLALERNDACWQEACIDAGNCSTDFLYCGNQNMDGYAV... | Function: Probable cyclic nucleotide-gated ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81969
Sequence Length: 717
Domain: The binding of calmodulin to the C-terminus might interfere with cyclic nucleotide binding and thus channel activation.
Subcellular Location: Cell membrane
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O82226 | MFDTCGPKGVKSQVISGQRENFVRLDSMDSRYSQSSETGLNKCTLNIQGGPKRFAQGSKASSGSFKKGFRKGSEGLWSIGRSIGLGVSRAVFPEDLEVSEKKIFDPQDKFLLLCNKLFVASCILAVSVDPLFLYLPFINDKAKCVGIDRKLAIIVTTIRTVIDSFYLFHMALRFRTAYVAPSSRVFGRGELVIDPAQIAKRYLQQYFIIDLLSVLPVPQIIVWRFLYTSRGANVLATKQALRYIVLVQYIPRFLRMYPLSSELKRTAGVFAETAWAGAAYYLLLYMLASHIVGALWYLLALERNNDCWSKACHNNQNCTR... | Function: Probable cyclic nucleotide-gated ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 85441
Sequence Length: 747
Domain: The binding of calmodulin to the C-terminus might interfere with cyclic nucleotide binding and thus channel activation.
Subcellular Location: Cell membrane
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Q9S9N5 | MYKSQYISGQREKFVRLDDIDSSSSPATGMMMQRNCFGFNLKNRGGEKKKASKSFREGVKKIRSEGLITIGKSVTRAVFPEDLRITEKKIFDPQDKTLLVWNRLFVISCILAVSVDPLFFYLPIVDNSGSSCIGIDTKLAVTTTTLRTIVDVFYLTRMALQFRTAYIAPSSRVFGRGELVIDPAKIAERYLTRYFVVDFLAVLPLPQIAVWKFLHGSKGSDVLPTKTALLNIVIVQYIPRFVRFIPLTSELKKTAGAFAEGAWAGAAYYLLWYMLASHITGAFWYMLSVERNDTCWRFACKVQPDPRLCVQILYCGTKFV... | Function: Putative cyclic nucleotide-gated ion channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 84634
Sequence Length: 738
Domain: The binding of calmodulin to the C-terminus might interfere with cyclic nucleotide binding and thus channel activation.
Subcellular Location: Cell membrane
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A9ZSY0 | MNLQDELDELKIYMTIDKTTIQELNRCMAEKREEQLFRHHEDAGVKKSTPEKNEKAISEQTLEKVIELENRLKSFEKNSRKLKEESKKLKKENDFLKSHLQHYQEDSESRGKELEKLLRVSSSVEQDKSELQTKVTALEREVTTLRRQVAKAKALRDENEEVVNPEEKEHCPTDKAKSEMATTDVRAQHCDCKTTTTKVKFKAAKKKCSVGRHHTVLNHSIKVMSHVENLSKDGWEDMSEGSSDSETQTFQNLGTVIVETSQNIRPIENDGNQKETDQTEDSRAQQEVQTYSCEDLKAPQNTKKMTFQNKSGSLQKNLHS... | Function: Required for centrosome cohesion and recruitment of CEP68 to centrosomes.
PTM: Phosphorylated directly or indirectly by NEK2.
Sequence Mass (Da): 82721
Sequence Length: 721
Subcellular Location: Cytoplasm
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Q12860 | MKMWLLVSHLVIISITTCLAEFTWYRRYGHGVSEEDKGFGPIFEEQPINTIYPEESLEGKVSLNCRARASPFPVYKWRMNNGDVDLTSDRYSMVGGNLVINNPDKQKDAGIYYCLASNNYGMVRSTEATLSFGYLDPFPPEERPEVRVKEGKGMVLLCDPPYHFPDDLSYRWLLNEFPVFITMDKRRFVSQTNGNLYIANVEASDKGNYSCFVSSPSITKSVFSKFIPLIPIPERTTKPYPADIVVQFKDVYALMGQNVTLECFALGNPVPDIRWRKVLEPMPSTAEISTSGAVLKIFNIQLEDEGIYECEAENIRGKDK... | Function: Contactins mediate cell surface interactions during nervous system development. Involved in the formation of paranodal axo-glial junctions in myelinated peripheral nerves and in the signaling between axons and myelinating glial cells via its association with CNTNAP1. Participates in oligodendrocytes generatio... |
P0DM15 | RDCQEKWEYCIVPILGFVYCCPGLICGPFVCV | Function: MuO-conotoxins are gating-modifier toxins that inhibit sodium current by trapping the domain II voltage sensor in the closed position to prevent opening of the sodium channel. This toxin shows high activity on Nav1.4/SCN4A (IC(50)=81 nM) and Nav1.8/SCN10A (IC(50)=96-529 nM). It also shows low activity on othe... |
P13671 | MARRSVLYFILLNALINKGQACFCDHYAWTQWTSCSKTCNSGTQSRHRQIVVDKYYQENFCEQICSKQETRECNWQRCPINCLLGDFGPWSDCDPCIEKQSKVRSVLRPSQFGGQPCTAPLVAFQPCIPSKLCKIEEADCKNKFRCDSGRCIARKLECNGENDCGDNSDERDCGRTKAVCTRKYNPIPSVQLMGNGFHFLAGEPRGEVLDNSFTGGICKTVKSSRTSNPYRVPANLENVGFEVQTAEDDLKTDFYKDLTSLGHNENQQGSFSSQGGSSFSVPIFYSSKRSENINHNSAFKQAIQASHKKDSSFIRIHKVM... | Function: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells.
PTM: All cysteine residues are assumed to be cross-linked to one another. Individual modules containing an even number of conserved cystein... |
P10643 | MKVISLFILVGFIGEFQSFSSASSPVNCQWDFYAPWSECNGCTKTQTRRRSVAVYGQYGGQPCVGNAFETQSCEPTRGCPTEEGCGERFRCFSGQCISKSLVCNGDSDCDEDSADEDRCEDSERRPSCDIDKPPPNIELTGNGYNELTGQFRNRVINTKSFGGQCRKVFSGDGKDFYRLSGNVLSYTFQVKINNDFNYEFYNSTWSYVKHTSTEHTSSSRKRSFFRSSSSSSRSYTSHTNEIHKGKSYQLLVVENTVEVAQFINNNPEFLQLAEPFWKELSHLPSLYDYSAYRRLIDQYGTHYLQSGSLGGEYRVLFYVD... | Function: Constituent of the membrane attack complex (MAC) that plays a key role in the innate and adaptive immune response by forming pores in the plasma membrane of target cells. C7 serves as a membrane anchor.
PTM: C7 has 28 disulfide bridges.
Sequence Mass (Da): 93518
Sequence Length: 843
Subcellular Location: Secr... |
P27658 | MAVLPGPLQLLGVLLTISLSSIRLIQAGAYYGIKPLPPQIPPQMPPQIPQYQPLGQQVPHMPLAKDGLAMGKEMPHLQYGKEYPHLPQYMKEIQPAPRMGKEAVPKKGKEIPLASLRGEQGPRGEPGPRGPPGPPGLPGHGIPGIKGKPGPQGYPGVGKPGMPGMPGKPGAMGMPGAKGEIGQKGEIGPMGIPGPQGPPGPHGLPGIGKPGGPGLPGQPGPKGDRGPKGLPGPQGLRGPKGDKGFGMPGAPGVKGPPGMHGPPGPVGLPGVGKPGVTGFPGPQGPLGKPGAPGEPGPQGPIGVPGVQGPPGIPGIGKPGQ... | Function: Macromolecular component of the subendothelium. Major component of the Descemet's membrane (basement membrane) of corneal endothelial cells. Also a component of the endothelia of blood vessels. Necessary for migration and proliferation of vascular smooth muscle cells and thus, has a potential role in the main... |
Q83PC5 | MSIKEQTLMTPYLQFDRNQWAALRDSVPMTLSEDEIARLKGINEDLSLEEVAEIYLPLSRLLNFYISSNLRRQAVLEQFLGTNGQRIPYIISIAGSVAVGKSTTARVLQALLSRWPEHRRVELITTDGFLHPNQVLKERGLMKKKGFPESYDMHRLVKFVSDLKSGVPNVTAPVYSHLIYDVIPDGDKTVVQPDILILEGLNVLQSGMDYPHDPHHVFVSDFVDFSIYVDAPEDLLQTWYINRFLKFREGAFTDPDSYFHNYAKLTKEEAIKTAMTLWKEINWLNLKQNILPTRERASLILTKSANHVVEEVRLRK | Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 36388
Sequence Length: 316
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 1/5.
Subcellular Location: Cytoplasm
EC: 2.7.1.33
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Q38WQ7 | MTERIALFPGSFDPFTKGHLDTVERASRLFDRVIIAVMTNAAKKPLFDGPTKVALIETVIADLDNVSVVAQPKTLTANFAQAVGARYLIRGIRNANDFEYERDIAALNQTQDAQLETVLLLAKQEFSFISSSMVKEIAAFGGQVDQLVPPAVAVALQEKLKHGRD | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 18059
Sequence Length: 165
Pathway: Cofactor biosynthesis; coenzyme A bios... |
Q5ZY26 | MQMVINEMKQKAIYPGTFDPVTNGHIDIITRASTIFPELIVAVASNKNKRPYLSWESRISLLEESVGHLTGVRVVGFDNLLIDFVLEQNAGIILRGLRAVSDFEYEFQLAGMNRKLSKKVETLFLTPAEHLMYISSTLVREIAALNGDISQFVPPNVVRELKKRQNERSL | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 19231
Sequence Length: 170
Pathway: Cofactor biosynthesis; coenzyme A bios... |
B1MXS2 | MSIALFPGSFDPLTNGHLDIIERASLMFDKVVVGVGYNTGKKALFTPEEKLALISEVVSDLPNVEVAIMHGLTVQFMAEIGARFIVRGLRNSKDFEYERDIAGVNSALADVETILLLAKPENQNISSSMVKEIGSMGADNMAKFVPKVVVDALKERLN | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 17211
Sequence Length: 158
Pathway: Cofactor biosynthesis; coenzyme A bios... |
Q8ZL48 | MQKRAIYPGTFDPITNGHLDIVTRATQMFDHVILAIAASPSKKPMFTLDERVALAQKATAHLGNVEVVGFSDLMANFARDRQANILIRGLRAVADFEYEMQLAHMNRHLMPQLESVFLMPSKEWSFISSSLVKEVARHQGDVTHFLPDNVHQALMDKLK | Function: Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate.
Catalytic Activity: (R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate
Sequence Mass (Da): 17956
Sequence Length: 159
Pathway: Cofactor biosynthesis; coenzyme A bios... |
O34932 | MTLVIGLTGGIASGKSTVANMLIEKGITVIDADIIAKQAVEKGMPAYRQIIDEFGEDILLSNGDIDRKKLGALVFTNEQKRLALNAIVHPAVRQEMLNRRDEAVANREAFVVLDIPLLFESKLESLVDKIIVVSVTKELQLERLMKRNQLTEEEAVSRIRSQMPLEEKTARADQVIDNSGTLEETKRQLDEIMNSWA | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22013
Sequence Length: 197
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q89YY6 | MAIKIGITGGIGSGKSVVSRLLEIMGIPVYISDIEAKRITHTNDVIRRELCALVGQDVFLNGELNRPLLASYIFGSPEHAKKVNAVIHPQVKEDFRRWVKGKGDIAMVGMESAILLEAGFKQEVDFVVMVYAPLEVRVERAIRRDYSSRELIMKRIEAQMSDEVKRNHADFVIVNDDETPLIPQVLKFISLLSKNNHYLCSAKK | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22948
Sequence Length: 204
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q6G1B3 | MKIIGLTGSIAMGKSTAADFFKQAGISVFSADETVHQLYKSKPILSLIEHTFPGVVENGKVNRLKLSKILINDSEKLQTLEEIIHPLVQEKEKEFIDTARQQGKKIVVLDIPLLFEKKGEKRVDSIIVVSAPLAIQKERTMTRPDMNEKKFSFINAKQMPDEKKRERADFIINTGKDLENTHQQVFSIIENLLKN | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22131
Sequence Length: 195
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q6MIK8 | MKWIGLTGGIACGKSTVSRMLRTHDIPVVDADEIAKEVVKPGSAGLKSVIQEFGPEFLTADGALDRRKLGQKVFGHPELLHKLEAITHPLIREETRRRRRLYEDMGHKLAIYDIPLLFETRAKDQFDGVIVVACTKEQQKERLRRQNWSEDEIEMRIASQIPIQFKEQQADFVLHNNRDEQHLLREVDRVLKWLEELKNQN | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 23343
Sequence Length: 201
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q8G5L8 | MGTMMRIGLTGGIAAGKSTVAARLKQLGALHIDYDALAHQIVEPGGVALPQIVAEFGPDALLADGTMNRPWIADHVFGANAAPGARERLDAIEHPLIYAEAARLEHEHPEAAIIIHDIPLLAEVIDDIPFAFDHIVTVEAPVCMRLDRMVEERGMSLEQAEARIRHQSSEEERRAIADIVIDSTHPLPEMLAQVGEIYAGWCAGR | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22256
Sequence Length: 205
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q493P4 | MSYIVALTGGICSGKSVVAKKFSNLSKKVSVIDADVISKNITQPGSIALRMITKHFGPHILFSNGSLNRSMLKKIIFFNPKDKEWLEQLLHPLIRKETQKTINILSNRSSYILWVVPLLIENNLQKYADHILMIDVHVDIQLNRIISRDKIHKQYAENILLSQVSRQHRLNYADNVIENNKSIDGMTQHIHNLHRDYLKAEKTTTKKTIFSK | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 24382
Sequence Length: 212
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q2KUM5 | MLRIGLTGGIGSGKTRVADKLGEWGAAVIDTDAIAHALTQADGLAMPAIIQAFGPEAVRADGAMDRAWVRNRVFREPQARACLEAILHPLIGQETQAAAERAVGSYLVFVVPLLVESGRWRGQLDRICVVDCDPETQIKRVQNRSGLTESDIRRIMDAQAARATRLKAADDVIVNDGSTTAEVLLARARSLHQSYLALADKHDRHGSTEAGPP | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22923
Sequence Length: 213
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q7WF46 | MYKIGLTGGIGSGKSRVADMLAEWGASVIDADEISHALTAPGGAAMPAIAREFGPQAVAADGALDRAWMRDLVFREPAARGRLEALLHPLIGLHTEQAAAQARGLYLVFVVPLLVESGRWRGRVDRICVVDCDPATQIARVQKRSGLTEPAIRRIMAAQAARATRLEAADDVIVNDGATSPDTLRARARTLHDRWLALAGAASQPGGKAAGTPE | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22588
Sequence Length: 214
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
O51497 | MGRNPLIIGVTGRIASGKDTVSKIISNKYGFYEINADKLGHSVLHEKKEEIVKIFGQKILNTKNEIDKLLLRNLVFNDNKELKKLESVSHPVILSKIKKILIQNQSTKIIINAALLFKMNLEKLCDYIIVLKAKNSIIKNRLSYSIPNIDSNMINKILKIQKDIFFEKNIINLKIINIINNKNYAYLEKEIEKKMQGIINYERFE | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 23729
Sequence Length: 205
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
P57299 | MTYIVALTGGISSGKTTISNGFKKIGINVIDTDIIAKNIIEKNLQVSFSIKRKFGKKILNIDNSINRLLLRQYVFNNHHHRLWLENLLHPKIYQESKHQIKMTQSNWCLWVVPLLVEKKLEKKAHRILLIDTPVKEQIKRTVRRDKISFLEAKKIIALQSSRKTRISLSDDIIFNKKNFKKINLYIYYFNLLYSHLSRIYNKNKTINIKKNFLTKFY | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 25718
Sequence Length: 217
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q9X1A7 | MVIGVTGKIGTGKSTVCEILKNKYGAHVVNVDRIGHEVLEEVKEKLVELFGGSVLEDGKVNRKKLAGIVFESRENLKKLELLVHPLMKKRVQEIINKTSGLIVIEAALLKRMGLDQLCDHVITVVASRETILKRNREADRRLKFQEDIVPQGIVVANNSTLEDLEKKVEEVMKLVWEKRE | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 20331
Sequence Length: 180
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q72K90 | MGHEAKHPIIIGITGNIGSGKSTVAALLRSWGYPVLDLDALAARARENKEEELKRLFPEAVVGGRLDRRALARLVFSDPERLKALEAVVHPEVRRLLMEELSRLEAPLVFLEIPLLFEKGWEGRLHGTLLVAAPLEERVRRVMARSGLSREEVLARERAQMPEEEKRKRATWVLENTGSLEDLERALKAVLAELTGGAKGGRG | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22590
Sequence Length: 203
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q8DKG1 | MSRLLRLGITGGIACGKSVVAGYLQRQYGVPIVDADVLARQVVAVGTPIYQAIVDRYGDGICRRDGTLDRSRLGEIVFAQPQERQWLEAQIHPAVVAEMEQAMATCDQPLMALVIPLLFEAHLEGLVDHIWVVATPPEQQLARLQQRDRLSAHAAGQRLASQLPLEEKIRRADTVLWNTGSLEELYRQVDQAFSLLGRGGKGG | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22346
Sequence Length: 203
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q3SGD0 | MFTIGLTGGIGSGKSAAAERFAELGVPVIDTDVIAHELTRPGSRALDVIRASFGEAVIAADGSLDRPVLRRRVFVDPAARRQLEAILHPLILHEVKARLASLSGPYAVAVIPLLVETGAYDAPVDRIAVVDCPEELQIARTIARSGLTPDEVGAILAAQAARPARLAVADDVIVNTGSLAALRDQVDALHQRYLTLAANRLP | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 21303
Sequence Length: 202
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q73M71 | MDSVLNGRQSRQSLDAPSEPILIGLSGPSCSGKNTASTILQDYGFYCIDADAVSRKVFTEHEKEILNLFQAEAEKRGINLKNENGIDKKAFALLVFSDEELLKKHEAFILPIIEEKIWEEIKRAFTEKPERPILLNAPTLHKTSFIKKCLFILYIDAPFILRLIRAKKRDRLPLKNIWLRFSKQKKFFSQYFFLNADTIVVKNFWSSASLKRKLLQEVKKRGF | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 25840
Sequence Length: 223
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
O83319 | MREFCPLIGVIGRSGAGKNVVSRLLAERGCYCIDADARTRELLESYGDSIVERFQVAAAARGLSLRRKDGGLHSAHLGVLLFSEPKLLQQHEEFLLPKVTRLLCEDIARAQAARPKAIVLNAPTLHKTELLQACSFVLYIWAPSILRMWRCKKRERVSFTHLLRRFSAQKGFYAQSIAQNADTYTVANCGRVASLARKVDCILTRRGVLGE | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 23584
Sequence Length: 211
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q9KPE3 | MSFVVALTGGIASGKTTVANLFHDQFGIDLVDADVIARDVVKPETEGLKAIAAHFGQAILHPDGSLNRAALRERIFAAPNEKAWLNQLLHPMIRQGMRNALTQTTSPYALLIVPLLVENQLQTMADRVLVVDVDEKIQIERTMARDKVSREQAEAILAAQASRAQRLAIADDVLKNDAENQKLLPQITLLHQKYLAMSRQNL | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22307
Sequence Length: 202
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q8D308 | MLINSPYIVAMTGGIGSGKSTIAKIFSELKVPIIESDIISKKIMFSEKSILNSIKNKLGINFSLNNNKYSKLVLRECIFESKSSVLFINKILHPVVKKKIKKIISNVNFPYIIWVTSLLIEENLYKYVNRILVIDVDPEIQIKRSILRDNVSKNQILNIINFQISREKRLTFAHDIINNYDYSCIRRKVFELHKYYLFKSKKYFKYDM | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 24396
Sequence Length: 208
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q7M7Q5 | MESLHYAIALSGGIGTGKSTVASLLRLYGFEVIDADSIAHRLLKEKQKEVVDLFGEGILKEGEIDRKSLGARVFGDPKERARLEALLHPPIRQEILQKAQKLEAKAFPYFIDIPLFFEKRDDYPMVNQTLLIYAPRKLQVERIKKRDSLSMEEIEARLGAQMDIKEKVPMAHYILSNEGNLNDLTQEVERLIETIKKDFHV | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22989
Sequence Length: 201
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q5GT26 | MIIGLTGGIGVGKSFIANCFKEFGAAVFDADFIVHQLYRVDKNIISYAEKNFPGAIANGEIDKTVLSKYFLDYDENWKQFQSLVHSAVQNELEIFIAQDKEINRKLLVLDVPLLLETRFHLYCDFIIFIYADSAAQAQRLSERNIDKEKLDLISSIQLPVKEKRQMSDFTIDTSTSKEHVLSQVKDIVDSLSLSS | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 22132
Sequence Length: 195
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q8PHK7 | MSDFIVGLTGGIASGKSALAAEFEKLGVPVIDADVIARQVAEPGPILDAIAAYFGDSVLLPDGTLNRQALRYRVFADTAQRQALEAITHPAIRRELQRAALAAQGPYAIVAIPLLAEAGGRATYPWLDRILVVDVPVALQHERLMQRDGATAELADRMITAQATREKRLAIADEVVCNHGVLKQLSQAARRLDADYRARANP | Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A.
Catalytic Activity: 3'-dephospho-CoA + ATP = ADP + CoA + H(+)
Sequence Mass (Da): 21757
Sequence Length: 202
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5.
Subcellul... |
Q7P0S9 | MKLLIDAGNSRVKWALYQGEDCVRQGAAEHGELAGLAAVWRDLPLTGAWMSSVARREVADALAAAVPCPLHRVHAERRFGDVRNHYRNTAEQGADRWLAVLAARELCRGDVIVACAGTALTVEALTAEGDYLGGLILPGHGLMLQSLAQGTANLNRPAGEVVDFPQGTQDALASGAIAALAGAIAEQRRRLAERTGRAPATVILTGGDAARIAPWLAAPMQIVDNLVLMGLLKVANT | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 24952
Sequence Length: 237
Pathway: Cofactor biosynthesis; coe... |
Q97EB4 | MILVLDVGNTNIVLGIYNDTKLTAEWRLSTDVLRSADEYGIQVMNLFQQDKLDPTLVEGVIISSVVPNIMYSLEHMIRKYFKINPLVVGPGIKTGINIKYDNPKEVGADRIVNAVAAHEIYKRSLIIIDFGTATTFCAVRENGDYLGGAICPGIKVSSEALFEKAAKLPRVELIKPAYAICKNTISSIQSGIVYGYIGQVRYIVERMKEELQEEGEKEPLVVATGGLAKLISEEAKNVDVINPFLTLEGLRIIYEKNRVKVI | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 29049
Sequence Length: 262
Pathway: Cofactor biosynthesis; coe... |
Q181F7 | MLLVFDVGNTNMVLGIYKGDKLVNYWRIKTDREKTSDEYGILISNLFDYDNVNISDIDDVIISSVVPNVMHSLENFCIKYCKKQPLIVGPGIKTGLNIKYDNPKQVGADRIVNAVAGIEKYGAPSILVDFGTATTFCAISEKGEYLGGTIAPGIKISSEALFQSASKLPRVELAKPGMTICKSTVSAMQSGIIYGYVGLVDKIISIMKKELNCDDVKVIATGGLAKLIASETKSIDYVDGFLTLEGLRIIYEKNQE | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27939
Sequence Length: 256
Pathway: Cofactor biosynthesis; coe... |
C5BPP8 | MKLLVDAGNSRIKWWVPECQAHGVVDRLALDDLAGEIAAVIDISKLSSVRVSCVAGKSIETQLRGELGFARDLDVKFARVSSPLPILTVAYREIHRLGVDRWLAMLAVREKFPDRFCAVLDAGSAVTVDFVTEAGVHEGGMIVPGVQTMARALWSNTSDVAVERLELVPRWCPGVDTYDCVRQGVSALYTGLVNEVHSYIDGSAERHLSPAIVVTGGDRHWFTQAFSSPVVVDPHLVLKGLLVLDELEK | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27199
Sequence Length: 249
Pathway: Cofactor biosynthesis; coe... |
Q9WZY5 | MYLLVDVGNTHSVFSITEDGKTFRRWRLSTGVFQTEDELFSHLHPLLGDAMREIKGIGVASVVPTQNTVIERFSQKYFHISPIWVKAKNGCVKWNVKNPSEVGADRVANVVAFVKEYGKNGIIIDMGTATTVDLVVNGSYEGGAILPGFFMMVHSLFRGTAKLPLVEVKPADFVVGKDTEENIRLGVVNGSVYALEGIIGRIKEVYGDLPVVLTGGQSKIVKDMIKHEIFDEDLTIKGVYHFCFGD | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27154
Sequence Length: 246
Pathway: Cofactor biosynthesis; coe... |
B9L0J2 | MLMVIDIGNTNVVVGLFAGHELRARWRLATARDRMPDEWWVQLNVLSQSAGFSLGEVVGIAISSVVPSLTATFQELAQRYLLVEPLIVNGAQDYGLPVRVEHPAEVGADRICNAIAAVERYGAPVIVVDFGTGTTFDVIDADGAYIGGAIAPGITIAFEALTQRAARLYTVALQAPPRAIGRNTRESLQSGTVLGYAELVRGLIRRIRSELGHEAPAIATGGLATLIAPLVPEFSAVEADLTLYGLRSAYERMHRSLGA | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27691
Sequence Length: 259
Pathway: Cofactor biosynthesis; coe... |
Q5SIJ5 | MLLAVDIGNTSTALGLFSGEELIAHFRIHTDRMRMESEYRVILKNLFALEDLPPPKAALLASVVPPVEREMKRAIERLFGVEARVVEAADTGLEVLIDNPREAGADRLVNAVGALAYPSPTGRYIVVDFGTATTFDLVEAPNRYLGGAIAIGPQTAADALAQRTAKLPRIDLTPPKAAVGKNTLEALRSGLVLGYAALVEGMVRRFKEEAGEALVIATGGFAETLRPLCPCFDVVDEDLTLKGLLRIHLGRG | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27055
Sequence Length: 252
Pathway: Cofactor biosynthesis; coe... |
Q8DJS3 | MVPPETNQWFALMIGNTRQHWALFRGEHLSRTWHLTPEELACNPAQDYPNLPCWGASVGSVPLHQVYPRAIALTLEDIPLPQMYPTLGLDRALALWGALQVYGAPVCVVDAGTALTLTLANDRREFAGGVILPGVGLMARALADYTAALPYVPLPTEPPRRWGTTTTTAIASGLYYGTAAILQAYLDAFLQEFPQGTVIVTGGDRPFVSELLRTFLDSDRWCEDDHLVFWGIRALRNPAAKIEMHPMERIDEFH | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 28166
Sequence Length: 254
Pathway: Cofactor biosynthesis; coe... |
Q3SLJ6 | MSGCRILLDAGNSSLKWAVVEDGTWLARGRSDYSDLSAVEAELDAGSECFIASVASRVYEEKLAALLTAAGCSAVWLKSEAAFDDVTNDYRDPTQLGVDRWMGLVAARARRRAPTLVVSAGTAMTVDALSGDGSFLGGLIVPGVALMQRSLQQGTAGGAAAGGAWQAFPRCTADAAYSGIIAALCGAVEGQHVRLAAHEGISPACLITGGGAETLLPHLGVDAEHVPTLVLEGIERVARAGGRG | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 25010
Sequence Length: 244
Pathway: Cofactor biosynthesis; coe... |
O83446 | MLLIDVGNSHVVFGIQGENGGRVCVRELFRLAPDARKTQDEYSLLIHALCERAGVGRASLRDAFISSVVPVLTKTIADAVAQISGVQPVVFGPWAYEHLPVRIPEPVRAEIGTDLVANAVAAYVHFRSACVVVDCGTALTFTAVDGTGLIQGVAIAPGLRTAVQSLHTGTAQLPLVPLALPDSVLGKDTTHAVQAGVVRGTLFVIRAMIAQCQKELGCRCAAVITGGLSRLFSSEVDFPPIDAQLTLSGLAHIARLVPTSLLPPATVSGSSGN | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 28472
Sequence Length: 273
Pathway: Cofactor biosynthesis; coe... |
Q3MC63 | MISQQFPKHVENQWLALEIGNSRLHWALFMGESLKFTWDTEYLPESVIQQLGNGETNWELGTGEKGISSSTFPPLPPAPCPSGSQSLMGETPKTELSHPLPLFIASVVPKQTALWQSYPNVRVITLDQIPLNNTYPTLGIDRALALWGAGMSWGFPMLVIDAGTALTFTAADGERNLVGGAILPGVGLQFASLGQKTEQLPQVEMAEIKSLPPHFALNTAEAIQSGVIYTLIAGIRDFTEEWLSLFPDGKVAIKGGDRILLLNYLQALYPELAGRLIVEPNMIFWGMQTIVAGVA | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 32142
Sequence Length: 295
Pathway: Cofactor biosynthesis; coe... |
A1WJV9 | MTFLAIDVGNTRLKWALYDAPRAGAALRAHGVEFLDHIDRLAEGSWARLPPPGHMLGCVVAGDAVKRRVQEQMEIWDVTPSWVVASAQEAGLSNGYDHPSRLGADRWVAMIGARQHVLARGPARPLVLVMVGTAVTVECVDAQGRFIGGLILPGHGIMLRALESGTAGLHVPTGEVRLFPTNTSDALTSGGTYAIAGAVERMVQHVIAHCGTEPICLMTGGAGWKVAPSMTRPFELLENLIFDGLLEIAMRRLAAA | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 27312
Sequence Length: 256
Pathway: Cofactor biosynthesis; coe... |
Q7MS38 | MLLCDIGNTYLHFYQEGKVWKELPRRLKAGMEVQEVYYISVNPPSARRLLEVYPHAIDLAPHMVLDTAYKGLGVDRMAACKGIEDGVVVDAGSAITVDVMQNQVHLGGFIMPGIASFSSMLKSISPALEKELNLSVELSALPQNTRDALSYGAIKAIVMMIQNSCKNKRLFFTGGDGKYLARFFENAIHDNSIVFKGMLKTLEEMKEGKR | Cofactor: A monovalent cation. Ammonium or potassium.
Function: Catalyzes the phosphorylation of pantothenate (Pan), the first step in CoA biosynthesis.
Catalytic Activity: (R)-pantothenate + ATP = (R)-4'-phosphopantothenate + ADP + H(+)
Sequence Mass (Da): 23319
Sequence Length: 210
Pathway: Cofactor biosynthesis; coe... |
O68098 | MTRLLVLGGTTEASRLAKTLADQGFEAVFSYAGRTGAPVAQPLPTRIGGFGGVAGLVDYLTREGVSHVIDATHPFAAQMSANAVAACAQTGVALCAFERAPWTAQAGDRWTHVPDLAAAVAALPQAPARVFLAIGKQHLRDFSAAPQHHYLLRLVDPPEGPLPLPDARAVIARGPFTVQGDTELLRSETITHVVAKNAGGAGAEAKLIAARSLGLPVILIDRPAVPARDICATLEGVMGWLADHGATPRGV | Function: Catalyzes the reduction of the macrocycle of precorrin-6X into precorrin-6Y.
Catalytic Activity: NADP(+) + precorrin-6B = 2 H(+) + NADPH + precorrin-6A
Sequence Mass (Da): 26048
Sequence Length: 251
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from precorrin-2 (ae... |
Q53139 | MTRILILGGTGEARALAAALADVPGVEAVSSLAGRVRDPRLPVGDVRIGGFGGADGLAECVRAHPVDAIVDATHPFAAQITRNAADAAHRRGIPLVVLRRPEWSPRPGEHWHGAADLADAAELLPDLGTRIFLTIGRQGVDAFADLQALWFLIRAIDPPDVAMPPHSTLLLARGPFAVADETALMREHRIDVLVTKNSGGGQTDAKLDAARALGIPVLMIRRPPLPPATETVDDVAGAIAWVGTLTRR | Function: Catalyzes the reduction of the macrocycle of precorrin-6X into precorrin-6Y.
Catalytic Activity: NADP(+) + precorrin-6B = 2 H(+) + NADPH + precorrin-6A
Sequence Mass (Da): 26142
Sequence Length: 248
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from precorrin-2 (ae... |
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