ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P45381 | MTSCHIAEEHIQKVAIFGGTHGNELTGVFLVKHWLENGAEIQRTGLEVKPFITNPRAVKKCTRYIDCDLNRIFDLENLGKKMSEDLPYEVRRAQEINHLFGPKDSEDSYDIIFDLHNTTSNMGCTLILEDSRNNFLIQMFHYIKTSLAPLPCYVYLIEHPSLKYATTRSIAKYPVGIEVGPQPQGVLRADILDQMRKMIKHALDFIHHFNEGKEFPPCAIEVYKIIEKVDYPRDENGEIAAIIHPNLQDQDWKPLHPGDPMFLTLDGKTIPLGGDCTVYPVFVNEAAYYEKKEAFAKTTKLTLNAKSIRCCLH | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter. In other tissues it acts as a scavenger of... |
O97157 | MDKRMITDAFEEIKWNGWGDTGVCIKYDEARQLPIHTNGKPMKHLLKFMKDDVLKVKGEFKIKPTPGLTKEEAIKRLPPPVVKQPFVDELRQVLSKDQIRLDAYARLTHIFGKNYRDLWRVRRGMIDRPPDAVILPNNHDDCVKIMELAQKHNVVVVPFGGGTNVTGGVEPNPFETRRMVISIDMRRMGRMLHIDTESGTAVFEVGVLGPDIDEQLSRYGFMMGHDPDSYAYSTLGGWIAARGSGAMSNKYGDIENMILAMRVVTPVGVVETPLTSRPCGVDLNAMFVGSEGAFGLVTEAVVKIERLPEVKRYEGWLFPS... | Function: Catalyzes the exchange of an acyl for a long-chain alkyl group and the formation of the ether bond in the biosynthesis of ether phospholipids.
Catalytic Activity: a 1-acylglycerone 3-phosphate + a long chain fatty alcohol = 1-O-alkylglycerone 3-phosphate + a long-chain fatty acid + H(+)
Sequence Mass (Da): 69... |
Q54XP3 | MSWKLDKQFSDKICNFSHDFFNKKLIKKGKPISGEWTVLATLVLVVENTSSYEIKQVLSLGTGNRCLGKSSLSNQGDVLNDSHAEIICKRSFQKFCYNEILNLLQSKYYNSILFNIEYHDSNNNNKDNDNNGSLPTISIKKGHSLHFYVNQTPCGDCSIFPFKKETQPENFIEKEKLEKDGKDKIENHEKKEQKDIIKQVDKDKDEENYEDEESKRKLKKVKDDNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNINNNNNQYDDIQRTGAKTVFGEPEDKKLIGVDYHQIGVLRVKPGRGDPTVSMSCSDKIA... | Cofactor: Binds 1 myo-inositol hexakisphosphate (IP6) per subunit.
Function: Specifically deaminates adenosine-37 to inosine in tRNA-Ala.
Catalytic Activity: adenosine(37) in tRNA(Ala) + H(+) + H2O = inosine(37) in tRNA(Ala) + NH4(+)
Sequence Mass (Da): 62484
Sequence Length: 545
EC: 3.5.4.34
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Q9V3R6 | MCDNKKPTVKEIAELCLKKFESLPKTGKPTANQWTILAGIVEFNRNTEACQLVSLGCGTKCIGESKLCPNGLILNDSHAEVLARRGFLRFLYQELKQDRIFHWNSTLSTYDMDEHVEFHFLSTQTPCGDACILEEEQPAARAKRQRLDEDSEMVYTGAKLISDLSDDPMLQTPGALRTKPGRGERTLSMSCSDKIARWNVIGVQGALLDVLISKPIYFSSLNFCCDDAQLESLERAIFKRFDCRTFKHTRFQPQRPQINIDPGIRFEFSQRSDWQPSPNGLIWSQVPEELRPYEISVNGKRQGVTKKKMKTSQAALAISK... | Cofactor: Binds 1 myo-inositol hexakisphosphate (IP6) per subunit.
Function: Specifically deaminates adenosine-37 to inosine in tRNA-Ala.
Catalytic Activity: adenosine(37) in tRNA(Ala) + H(+) + H2O = inosine(37) in tRNA(Ala) + NH4(+)
Sequence Mass (Da): 45350
Sequence Length: 394
EC: 3.5.4.34
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Q9BUB4 | MWTADEIAQLCYEHYGIRLPKKGKPEPNHEWTLLAAVVKIQSPADKACDTPDKPVQVTKEVVSMGTGTKCIGQSKMRKNGDILNDSHAEVIARRSFQRYLLHQLQLAATLKEDSIFVPGTQKGVWKLRRDLIFVFFSSHTPCGDASIIPMLEFEDQPCCPVFRNWAHNSSVEASSNLEAPGNERKCEDPDSPVTKKMRLEPGTAAREVTNGAAHHQSFGKQKSGPISPGIHSCDLTVEGLATVTRIAPGSAKVIDVYRTGAKCVPGEAGDSGKPGAAFHQVGLLRVKPGRGDRTRSMSCSDKMARWNVLGCQGALLMHLL... | Cofactor: Binds 1 myo-inositol hexakisphosphate (IP6) per subunit.
Function: Specifically deaminates adenosine-37 to inosine in tRNA-Ala.
Catalytic Activity: adenosine(37) in tRNA(Ala) + H(+) + H2O = inosine(37) in tRNA(Ala) + NH4(+)
Sequence Mass (Da): 55392
Sequence Length: 502
EC: 3.5.4.34
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Q9JHI2 | MWTADEIAQLCYAHYNVRLPKQGKPEPNREWTLLAAVVKIQASANQACDIPEKEVQVTKEVVSMGTGTKCIGQSKMRESGDILNDSHAEIIARRSFQRYLLHQLHLAAVLKEDSIFVPGTQRGLWRLRPDLSFVFFSSHTPCGDASIIPMLEFEEQPCCPVIRSWANNSPVQETENLEDSKDKRNCEDPASPVAKKMRLGTPARSLSNCVAHHGTQESGPVKPDVSSSDLTKEEPDAANGIASGSFRVVDVYRTGAKCVPGETGDLREPGAAYHQVGLLRVKPGRGDRTCSMSCSDKMARWNVLGCQGALLMHFLEKPIY... | Cofactor: Binds 1 myo-inositol hexakisphosphate (IP6) per subunit.
Function: Specifically deaminates adenosine-37 to inosine in tRNA-Ala.
Catalytic Activity: adenosine(37) in tRNA(Ala) + H(+) + H2O = inosine(37) in tRNA(Ala) + NH4(+)
Sequence Mass (Da): 55355
Sequence Length: 499
EC: 3.5.4.34
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Q28FE8 | MQAKGLWSADEIAALSYGHYTTQLPKQGLPDPSREWTLMAAVIQIESVEDTKVIKKVVAMGTGTKCIGQAKLRKTGDVLQDSHAEIIAKRSFQRYLLHQLSLAVSDTKDCLFIPGTEKGKWMLRPEISFVFFTSHTPCGDASIIPVISHEDELGHPLPSEVTEKDHSSNNVCESVNTTYKRKVRSEEDIGFISKKMKHSIDEILTRPENYEEENRHDFPSTCQKALDVHRTGAKCVAGELQDSYSPGVNYHTVGVLRIKPGRGDRTMSMSCSDKMARWNVLGCQGALLMHFLQQPIYLSAVVVGKCPFSQDAMERALYNR... | Cofactor: Binds 1 myo-inositol hexakisphosphate (IP6) per subunit.
Function: Specifically deaminates adenosine-37 to inosine in tRNA-Ala.
Catalytic Activity: adenosine(37) in tRNA(Ala) + H(+) + H2O = inosine(37) in tRNA(Ala) + NH4(+)
Sequence Mass (Da): 53186
Sequence Length: 472
EC: 3.5.4.34
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Q5RIV4 | MQEVGVDPEKNDFLQPSDSEVQTWMAKAFDMAVEALENGEVPVGCLMVYNNEIIGKGRNEVNETKNATRHAEMVALDQVLDWCRLREKDCKEVCEQTVLYVTVEPCIMCAAALRLLRIPFVVYGCKNERFGGCGSVLDVSSDHLPHTGTSFKCIAGYRAEEAVEMLKTFYKQENPNAPKPKVRKDSINPQDGAAVIQVMRGPPDEETETIAHLS | Function: Probably participates in deamination of adenosine-34 to inosine in many tRNAs.
Catalytic Activity: adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+)
Sequence Mass (Da): 23839
Sequence Length: 214
EC: 3.5.4.33
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Q7Z6V5 | MEAKAAPKPAASGACSVSAEETEKWMEEAMHMAKEALENTEVPVGCLMVYNNEVVGKGRNEVNQTKNATRHAEMVAIDQVLDWCRQSGKSPSEVFEHTVLYVTVEPCIMCAAALRLMKIPLVVYGCQNERFGGCGSVLNIASADLPNTGRPFQCIPGYRAEEAVEMLKTFYKQENPNAPKSKVRKKECQKS | Function: Probably participates in deamination of adenosine-34 to inosine in many tRNAs.
Catalytic Activity: adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+)
Sequence Mass (Da): 21046
Sequence Length: 191
EC: 3.5.4.33
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Q6P6J0 | MEEKVESTTTPDGPCVVSVQETEKWMEEAMRMAKEALENIEVPVGCLMVYNNEVVGKGRNEVNQTKNATRHAEMVAIDQVLDWCHQHGQSPSTVFEHTVLYVTVEPCIMCAAALRLMKIPLVVYGCQNERFGGCGSVLNIASADLPNTGRPFQCIPGYRAEEAVELLKTFYKQENPNAPKSKVRKKDCQKS | Function: Probably participates in deamination of adenosine-34 to inosine in many tRNAs.
Catalytic Activity: adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+)
Sequence Mass (Da): 21308
Sequence Length: 191
EC: 3.5.4.33
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Q4V7V8 | MEPLQITEEIQNWMHKAFQMAQDALNNGEVPVGCLMVYGNQVVGKGRNEVNETKNATQHAEMVAIDQVLDWCEMNSKKSTDVFENIVLYVTVEPCIMCAGALRLLKIPLVVYGCRNERFGGCGSVLNVSGDDIPDTGTKFKCIGGYQAEKAIELLKTFYKQENPNAPKSKVRKKE | Function: Probably participates in deamination of adenosine-34 to inosine in many tRNAs.
Catalytic Activity: adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+)
Sequence Mass (Da): 19505
Sequence Length: 175
EC: 3.5.4.33
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Q0P4H0 | MTEEIQNWMHKAFQMAQDALNNGEVPVGCLMVYDNQVVGKGRNEVNETKNATRHAEMVAIDQVLDWCEKNSKKSRDVFENIVLYVTVEPCIMCAGALRLLKIPLVVYGCRNERFGGCGSVLNVAGDNIPDTGTEFKYIGGYQAEKAVELLKTFYKQENPNAPRSKVRKKE | Function: Probably participates in deamination of adenosine-34 to inosine in many tRNAs.
Catalytic Activity: adenosine(34) in tRNA + H(+) + H2O = inosine(34) in tRNA + NH4(+)
Sequence Mass (Da): 19121
Sequence Length: 170
EC: 3.5.4.33
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P31466 | MSHQHTTQTSGQGMLERVFKLREHGTTARTEVIAGFTTFLTMVYIVFVNPQILGVAGMDTSAVFVTTCLIAAFGSIMMGLFANLPVALAPAMGLNAFFAFVVVQAMGLPWQVGMGAIFWGAIGLLLLTIFRVRYWMIANIPVSLRVGITSGIGLFIGMMGLKNAGVIVANPETLVSIGNLTSHSVLLGILGFFIIAILASRNIHAAVLVSIVVTTLLGWMLGDVHYNGIVSAPPSVMTVVGHVDLAGSFNLGLAGVIFSFMLVNLFDSSGTLIGVTDKAGLADEKGKFPRMKQALYVDSISSVTGSFIGTSSVTAYIESS... | Function: High-affinity transporter for adenine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46866
Sequence Length: 445
Subcellular Location: Cell inner membrane
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Q6FCU0 | MNQSELIRALPKAELHVHIEGTFEPELMFEIAQRNHIDIPYKSVEEIKKAYNFHNLQSFLDIYYAGANVLINEQDFYDLAWAYFKKCAEDRVVHTEMFFDPQTHTERGVSFEIVLNGLKRACKDAKEHLGISSHLIMCFLRHLSEEDAFKTLEQALPYKADIIAVGLDSSEVGHPPSKFARVFEKAREEGFLVVAHAGEEGPPEYVWEALDLLKVNRIDHGVRSEEDPALMQRLIQEKMPLTVCPLSNLKLCVVNDMKEHNIRRLLNQGVHVTVNSDDPSYFGGYMNDNFVAIQAALDLSNEELKKLAINSFEASFIDEE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism.
Catalytic Activity: adenine + H(+) + H2O = hypoxanthine + NH4(+)
Sequence Mass (Da): 38108
Sequence Length: 332
EC: 3.5.4.2... |
Q8UJ05 | MTSHLLKAEIHCHLEGAAPPALVVKQAEKYGIDTSGFLRDGQYVWSDFAEFIQCYDAVAQVFKSDEDYAVLTETYLTELAEANTIYSELIISPDHGDRIGLGADAYLAGVAEGIRIAKEKTGIETRIIVTGERHFGPERVIAAAEYAARIRHPLVTGFNMAGEERMGRVADYARAFDIARDAGLGLTIHAGEVCGPESVADALDLVKPSRIGHGVRAIEDAALISRLVETGTVLEVCPGSNIALSVYPDFASHPLKALSDAGVRVCISSDDPPFFFTSLAREYALAADAFGFNDAEINRMTRTALECAFVDEATRERLLA... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the hydrolytic deamination of adenine to hypoxanthine. Plays an important role in the purine salvage pathway and in nitrogen catabolism.
Catalytic Activity: adenine + H(+) + H2O = hypoxanthine + NH4(+)
Sequence Mass (Da): 35127
Sequence Length: 325
EC: 3.5.4.2... |
P54202 | MAAPEIPKKQKAVIYDNPGTVSTKVVELDVPEPGDNEVLINLTHSGVCHSDFGIMTNTWKILPFPTQPGQVGGHEGVGKVVKLGAGAEASGLKIGDRVGVKWISSACGQCPPCQDGADGLCFNQKVSGYYTPGTFQQYVLGPAQYVTPIPDGLPSAEAAPLLCAGVTVYASLKRSKAQPGQWIVISGAGGGLGHLAVQIAAKGMGLRVIGVDHGSKEELVKASGAEHFVDITKFPTGDKFEAISSHVKSLTTKGLGAHAVIVCTASNIAYAQSLLFLRYNGTMVCVGIPENEPQAIASAYPGLFIQKHVHVTGSAVGNRN... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH
Sequence Mass (Da): 38690
Sequence Length: 367
Subcellular Location: Cytoplasm
EC: 1.1.1.1
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Q24803 | MSTQQTMTVDEHINQLVAKAQVALKEYLKPEYTQEKIDYIVKKASVAALDQHCALAAAAVEETGRGIFEDKATKNIFACEHVTHEMRHAKTVGIINVDPLYGITEIAEPVGVVCGVTPVTNPTSTAIFKSLISIKTRNPIVFSFHPSALKCSIMAAKIVRDAAISAGAPENCIQWIEFGGIEASNKLMNHPGVATILATGGNAMVKAAYSSGKPALGVGAGNVPTYIEKTCNIKQAANDVVMSKSFDNGMICASEQAAIIDKEIYDQVVEEMKTLGAYFINEEEKAKLEKFMFGVNAYSADVNNARLNPKCPGMSPQWFA... | Cofactor: Zinc or iron.
Function: This enzyme has two NAD(+)-dependent activities: ADH and ACDH. May be a critical enzyme in the fermentative pathway.
Catalytic Activity: a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH
Sequence Mass (Da): 95590
Sequence Length: 870
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P42327 | MKAAVVNEFKKALEIKEVERPKLEEGEVLVKIEACGVCHTDLHAAHGDWPIKPKLPLIPGHEGVGIVVEVAKGVKSIKVGDRVGIPWLYSACGECEYCLTGQETLCPHQLNGGYSVDGGYAEYCKAPADYVAKIPDNLDPVEVAPILCAGVTTYKALKVSGARPGEWVAIYGIGGLGHIALQYAKAMGLNVVAVDISDEKSKLAKDLGADIAINGLKEDPVKAIHDQVGGVHAAISVAVNKKAFEQAYQSVKRGGTLVVVGLPNADLPIPIFDTVLNGVSVKGSIVGTRKDMQEALDFAARGKVRPIVETAELEEINEVF... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Active with primary alcohols, including methanol.
Catalytic Activity: a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH
Sequence Mass (Da): 36205
Sequence Length: 339
EC: 1.1.1.1
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A4ISB9 | MQNFTFRNPTKLIFGRGQIEQLKEEVPKYGKKVLLVYGGGSIKRNGLYDEVMSLLTDIGAEVVELPGVEPNPRLSTVKKGVDICRREGIEFLLAVGGGSVIDCTKAIAAGAKFDGDPWEFITKKATVTEALPFGTVLTLAATGSEMNAGSVITNWETKEKYGWGSPVTFPQFSILDPTYTMTVPKDHTVYGIVDMMSHVFEQYFHHTPNTPLQDRMCEAVLKTVIEAAPKLVDDLENYELRETIMYSGTIALNGFLQMGVRGDWATHDIEHAVSAVYDIPHAGGLAILFPNWMKHVLDENVSRFAQLAVRVFDVDPTGKT... | Function: Long-chain alkyl alcohol dehydrogenase that can oxidize a broad range of alkyl alcohols from methanol to 1-triacontanol (C1 to C30) as well as 1,3-propanediol and acetaldehyde. Oxidizes isopropyl alcohol, isoamylol, acetone, octanal and decanal. The best substrate is 1-octanol.
Catalytic Activity: a long-chai... |
Q9P4C2 | MSIPTTQKGVIFYENGGQLYYKDIPVPKPKSNELLINVKYSGVCHTDLHAWKGDWPLDTKLPLVGGHEGAGVVVAMGDNVKGWKIGDLAGIKWLNGSCMNCEECELSNESNCPDADLSGYTHDGSFQQYATADAVQAAHIPAGTDLAQVAPILCAGVTVYKALKTAEMKAGDWVAISGAAGGLGSLAVQYAKAMGFRVLGIDGGEGKEELFKSLGGEVFIDFTKSKDIVGEVIKATNGGAHGVINVSVSEKAIESSIEYCRSNGTVVLVGLPKDAKCKSDVFNQVVKSIHIVGSYVGNRADTREALDFFCRGLVNAPIKV... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH
Sequence Mass (Da): 36968
Sequence Length: 348
Subcellular Location: Cytoplasm
EC: 1.1.1.1
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O13309 | MSIPTTQKAVIFETNGGPLLYKDIPVPKPKPNELLINVKYSGVCHTDLHAWKGDWPLDTKLPLVGGHEGAGVVVALGENVTGWEIGDYAGIKWINGSCLQCEYCVTAHESNCPDADLSGYTHDGSFQQYATADAIQAARIPKGTDLALIAPILCAGITVYKALKTAQLQAGQWVAVSGAAGGLGSLAIQYAKAMGYRVVGIDGGADKGEFAKSLGAEVFVDFLSSKDVVADVLKATNGGAHGVINVSVSERAMQQSVDYVRPTGTVVLVGLPAGAKVSASVFSSVVRTIQIKGSYVGNRADSAEAIDFFTRGLIKCPIKI... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Converts ethanol to acetaldehyde.
Catalytic Activity: a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH
Sequence Mass (Da): 36565
Sequence Length: 348
Subcellular Location: Cytoplasm
EC: 1.1.1.1
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P28032 | MSTTVGQVIRCKAAVAWEAGKPLVMEEVDVAPPQKMEVRLKILYTSLCHTDVYFWEAKGQNPVFPRILGHEAAGIVESVGEGVTDLAPGDHVLPVFTGECKDCAHCKSEESNMCSLLRINTDRGVMLNDGKSRFSINGNPIYHFVGTSTFSEYTVVHVGCVAKINPLAPLDKVCVLSCGISTGLGASLNVAKPTKGSSVAIFGLGAVGLAAAEGARIAGASRIIGVDLNASRFEQAKKFGVTEFVNPKDYSKPVQEVIAEMTDGGVDRSVECTGHIDAMISAFECVHDGWGVAVLVGVPHKEAVFKTHPLNFLNERTLKG... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH
Sequence Mass (Da): 41040
Sequence Length: 380
Subcellular Location: Cytoplasm
EC: 1.1.1.1
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A0A2I7G3B3 | MSLNTPDVIICKAAVVRELGRSVMVEEIKVDPPKATEVRIKMLFASICHTDMLCFDGFPTPLFPRIPGHEGVGMVESVGEDIKTKLKPGDIVMPLFMGECGQCLNCKSKRTNLCHAYPLTLSGLLLDGTSRMSIAKTEETIYHHLSCSTWSEYMVIDINYVLKIDPKMHLPYASFLSCGFTTGFGAPWKETQITKGSIVAVFGLGAVGLGAIKGAQMQGASIIIGVDINENKAAKGKAFGMTHFINPKDHPNQLVSDMVRDITDGLGVDYCFECTGIASLLKEIIEASKIGFGTTILIGAAPDNVPISSLSLINGRTLKG... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Component of the monoterpenoid pyrethrins biosynthesis; pyrethrins are widely used plant-derived pesticide . Mediates the conversion of trans-chrysanthemol into trans-chrysanthemal .
Catalytic Activity: (R,R)-chrysanthemol + NAD(+) = (1R,3R)-chrysanthemal + H(+) + NA... |
Q8GIX7 | MKAAVLHEFGQSLQIEEVDIPTPGAGEIVVKMQASGVCHTDLHAVEGDWPVKPSPPFIPGHEGVGLITAVGEGVTHVKEGDRVGVAWLYSACGHCTHCLGGWETLCESQQNSGYSVNGSFAEYVLANANYVGIIPESVDSIEIAPVLCAGVTVYKGLKMTDTKPGDWVVISGIGGLGHMAVQYAIAMGLNVAAVDIDDDKLAFAKKLGAKVTVNAKNTDPAEYLQKEIGGAHGALVTAVSAKAFDQALSMLRRGGTLVCNGLPPGDFPVSIFDTVLNGITIRGSIVGTRLDLQESLDMAAAGKVKATVTAEPLENINDIF... | Cofactor: Binds 2 Zn(2+) ions per subunit. One metal ion is located at the active-site region and has been termed catalytic, while the second metal ion has been termed structural.
Function: Psychrophilic alcohol dehydrogenase that exhibits a wide range of substrate specificity, oxidizing mainly primary and secondary al... |
P75214 | MKAYAMLKIGATGWIEKPRPVCGPNDAIIRPLAVAPCTSDVHTVWEGGIGERHNMVLGHEGCGVVDEVGSEVKSFKVGDRVLVAAITPEWNSVNAQAGYPMHSGGMLGGWKFSNVKDGMFAEYFHVNDAEGNLALMPEGMDLADACMLSDMIPTGFHANELADIQYGVALSFFCAGPVGLMAIAGAALKGAGRIIVVDSRPDIVEIAKAYGATDYIDFKKVSVVDEILKWTNNEGVEKVLISGGGSTILETAIKVLRPGGKIGNVNYFGAGEFLTIPRVEWGVGMAHKAIHGGLMLGGRLRLEKLARLIMTKKLDPSKMI... | Cofactor: Binds 1 zinc ion per subunit.
Function: Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary ... |
P9WQC2 | MSDGAVVRALVLEAPRRLVVRQYRLPRIGDDDALVRVEACGLCGTDHEQYTGELAGGFAFVPGHETVGTIAAIGPRAEQRWGVSAGDRVAVEVFQSCRQCANCRGGEYRRCVRHGLADMYGFIPVDREPGLWGGYAEYQYLAPDSMVLRVAGDLSPEVATLFNPLGAGIRWGVTIPETKPGDVVAVLGPGIRGLCAAAAAKGAGAGFVMVTGLGPRDADRLALAAQFGADLAVDVAIDDPVAALTEQTGGLADVVVDVTAKAPAAFAQAIALARPAGTVVVAGTRGVGSGAPGFSPDVVVFKELRVLGALGVDATAYRAA... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH
Sequence Mass (Da): 37997
Sequence Length: 367
EC: 1.1.1.1
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P39462 | MRAVRLVEIGKPLSLQEIGVPKPKGPQVLIKVEAAGVCHSDVHMRQGRFGNLRIVEDLGVKLPVTLGHEIAGKIEEVGDEVVGYSKGDLVAVNPWQGEGNCYYCRIGEEHLCDSPRWLGINFDGAYAEYVIVPHYKYMYKLRRLNAVEAAPLTCSGITTYRAVRKASLDPTKTLLVVGAGGGLGTMAVQIAKAVSGATIIGVDVREEAVEAAKRAGADYVINASMQDPLAEIRRITESKGVDAVIDLNNSEKTLSVYPKALAKQGKYVMVGLFGADLHYHAPLITLSEIQFVGSLVGNQSDFLGIMRLAEAGKVKPMITK... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH
Sequence Mass (Da): 37569
Sequence Length: 347
EC: 1.1.1.1
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P00332 | MTIPDKQLAAVFHTHGGPENVKFEEVPVAEPGQDEVLVNIKYTGVCHTDLHALQGDWPLPAKMPLIGGHEGAGVVVKVGAGVTRLKIGDRVGVKWMNSSCGNCEYCMKAEETICPHIQLSGYTVDGTFQHYCIANATHATIIPESVPLEVAAPIMCAGITCYRALKESKVGPGEWICIPGAGGGLGHLAVQYAKAMAMRVVAIDTGDDKAELVKSFGAEVFLDFKKEADMIEAVKAATNGGAHGTLVLSTSPKSYEQAAGFARPGSTMVTVSMPAGAKLGADIFWLTVKMLKICGSHVGNRIDSIEALEYVSRGLVKPYY... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH
Sequence Mass (Da): 37396
Sequence Length: 350
Subcellular Location: Cytoplasm
EC: 1.1.1.1
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P07700 | MGDGWLPPDCGPHNRSGGGGATAAPTGSRQVSAELLSQQWEAGMSLLMALVVLLIVAGNVLVIAAIGRTQRLQTLTNLFITSLACADLVMGLLVVPFGATLVVRGTWLWGSFLCECWTSLDVLCVTASIETLCVIAIDRYLAITSPFRYQSLMTRARAKVIICTVWAISALVSFLPIMMHWWRDEDPQALKCYQDPGCCDFVTNRAYAIASSIISFYIPLLIMIFVYLRVYREAKEQIRKIDRCEGRFYGSQEQPQPPPLPQHQPILGNGRASKRKTSRVMAMREHKALKTLGIIMGVFTLCWLPFFLVNIVNVFNRDLV... | Function: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity . In dorsal pons neurons, involved in the regulation of sleep/wake behaviors (By similarity).
PTM: ... |
P18090 | MGAGALALGASEPCNLSSAAPLPDGAATAARLLVLASPPASLLPPASEGSAPLSQQWTAGMGLLLALIVLLIVVGNVLVIVAIAKTPRLQTLTNLFIMSLASADLVMGLLVVPFGATIVVWGRWEYGSFFCELWTSVDVLCVTASIETLCVIALDRYLAITLPFRYQSLLTRARARALVCTVWAISALVSFLPILMHWWRAESDEARRCYNDPKCCDFVTNRAYAIASSVVSFYVPLCIMAFVYLRVFREAQKQVKKIDSCERRFLTGPPRPPSPAPSPSPGPPRPADSLANGRSSKRRPSRLVALREQKALKTLGIIMG... | Function: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity. Mediates Ras activation through G(s)-alpha- and cAMP-mediated signaling (By similarity). Involved ... |
P07550 | MGQPGNGSAFLLAPNGSHAPDHDVTQERDEVWVVGMGIVMSLIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVPFGAAHILMKMWTFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYFAITSPFKYQSLLTKNKARVIILMVWIVSGLTSFLPIQMHWYRATHQEAINCYANETCCDFFTNQAYAIASSIVSFYVPLVIMVFVYSRVFQEAKRQLQKIDKSEGRFHVQNLSQVEQDGRTGHGLRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQDNLIRKEVYILLNWIGYVNSG... | Function: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine.
PTM: Palmitoylated . Mainly palmitoylated at Cys-341 . Palm... |
O70431 | LACAGLVMGLAVVPFGASHILMNMWNFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYIAITAPFKYQSLLTKNKARVVILMVWIVSGLTSFLPIQMHWYRATNKEAITCYTNETCCDFFTNQAYAIASSIVSFYVPLVVMVFVYSRVFQVAKRQLQKIDKSEGRFHAQNLSQVEQDGRSGHGLRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNVVHAIKENLIPKEVYILLNWLGYVNSAFNPLI | Function: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine (By similarity).
PTM: Phosphorylated by PKA and BARK upon ag... |
Q28997 | MGQPGNRSVFLLAPNGSHAPDQDVPQERDEAWVVGMAIVMSLIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVPFGASHILMKMWTFGSFWCEFWISIDVLCVTASIETLCVIAVDRYLAITSPFKYQCLLTKNKARVVILMVWVVSGLISFLPIKMHWYQATHREALNCYAEEACCDFFTNQPYAIASSIVSFYLPLVVMVFVYSRVFQVARRQLQKIDKSEGRFHAQNLSQAEQDGRSGPGHRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHGIHDNLIPKEVYILLNWVGYVNSA... | Function: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine (By similarity).
PTM: Palmitoylated; may reduce accessibilit... |
P0DQS0 | MLVNARAIRQSIGIVVAQCRRDLESNRTLDYRTRMRTSLILVAMVMVSVLLPYTYGSSCDSFCTEQANKCLTGCEGFVGCMECTNFAGHCREQCRKRSVKRRKEIRARFTKEPTEES | PTM: The mature peptide may be cleaved at a dibasic residue site and be shorter than the sequence shown (possibly residues 1-94).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 13369
Sequence Length: 117
Subcellular Location: Membrane
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P09167 | MQKIKLTGLSLIISGLLMAQAQAAEPVYPDQLRLFSLGQGVCGDKYRPVNREEAQSVKSNIVGMMGQWQISGLANGWVIMGPGYNGEIKPGTASNTWCYPTNPVTGEIPTLSALDIPDGDEVDVQWRLVHDSANFIKPTSYLAHYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTAIKVSNFAYNLDPDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSGYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETELSIEIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIEL... | Function: Secreted, cytolytic toxin that forms pores in host membranes after proteolytic removal of a C-terminal propeptide, leading to destruction of the membrane permeability barrier and host cell death. The pores are formed by transmembrane beta-strands and are approximately 3 nm in diameter.
PTM: Proteolytic cleava... |
A0A073CEA3 | MLKFSMEFCYPQPDVKTLIVGTLGPKETSSEQTLNYLITQWQAEQISVTSHLFDTFTELKEALLQDRVDLALVPHAYERVNDFYMEPSLKLGFVFTYPTPIYGLAKRKNEELVWENCTLVTHPAPFPLLPYLLPGYPHQKNIKVEFVNSTSAAAIQVKQGLADLAITNENALKENDLEFIAEYGKIEMSWSIFHKKGTVHRE | Function: In vivo, involved in the biosynthesis of 2-carboxy-6-hydroxyoctahydroindole (Choi) present in the nonribosomal glycopeptides aeruginoside 126A and B. AerD is an unusual prephenate decarboxylase that avoids the typical aromatization of the cyclohexadienol ring of prephenate. AerD catalyzes the protonation at C... |
Q39172 | MTATNKQVILKDYVSGFPTESDFDFTTTTVELRVPEGTNSVLVKNLYLSCDPYMRIRMGKPDPSTAALAQAYTPGQPIQGYGVSRIIESGHPDYKKGDLLWGIVAWEEYSVITPMTHAHFKIQHTDVPLSYYTGLLGMPGMTAYAGFYEVCSPKEGETVYVSAASGAVGQLVGQLAKMMGCYVVGSAGSKEKVDLLKTKFGFDDAFNYKEESDLTAALKRCFPNGIDIYFENVGGKMLDAVLVNMNMHGRIAVCGMISQYNLENQEGVHNLSNIIYKRIRIQGFVVSDFYDKYSKFLEFVLPHIREGKITYVEDVADGLE... | Function: Involved in the detoxification of reactive carbonyls . Acts on lipid peroxide-derived reactive aldehydes . Specific to a double bond activated by an adjacent carbonyl group . Can use both quinones and diamide as substrates, but not menadione, ferricyanide or phylloquinone . Can use 4-hydroxy-(2E)-nonenal (HNE... |
P50466 | MSSHPYVTQQNTPLADDTTLMSTTDLQSYITHANDTFVQVSGYTLQELQGQPHNMVRHPDMPKAAFADMWFTLKKGEPWSGIVKNRRKNGDHYWVRANAVPMVREGKISGYMSIRTRATDEEIAAVEPLYKALNAGRTSKRIHKGLVVRKGWLGKLPSLPLRWRARGVMTLMFILLAAMLWFVAAPVVTYILCALVVLLASACFEWQIVRPIENVAHQALKVATGERNSVEHLNRSDELGLTLRAVGQLGLMCRWLINDVSSQVSSVRNGSETLAKGTDELNEHTQQTVDNVQQTVATMNQMAASVKQNSATASAADKLS... | Function: Signal transducer for aerotaxis. The aerotactic response is the accumulation of cells around air bubbles. The nature of the sensory stimulus detected by this protein is the proton motive force or cellular redox state. It uses a FAD prosthetic group as a redox sensor to monitor oxygen levels.
Location Topology... |
Q9I3F6 | MRNNQPITQHERVYPAEQRLITTTNLKGIITYCNEAFIDISGFSREELMSAPHNLIRHPDVPPAVFAHMWTTLKAGRPWMGIVKNRCKNGDHYWVSAYVTPIYDQGAVVGYESVRVKPTAEQIQRAEALYRRLGAGKPAIPRRDRWLPVLLDWLPFILISQIGFLIGIWLNSWWGFILAGLLAVPLGLAGLRWQKRGLKRLMRLAEQTTSDPLIAQMYTDSRGDQARLEMAILSQDARLKTCLTRLQDTAEYLTEQARQADTLAHHSSAGLEQQRAETEQVATAVNEMAATTQEVANNVQLTADATQKANELTSRGRDIA... | Function: Chemotactic transducer for aerotaxis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57180
Sequence Length: 521
Subcellular Location: Cell inner membrane
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A7J2C6 | MRSILVIPSFVAVLNAFSLFPKPHDDFKYLITFGDSYTDNGRLGYYGSHQAHGPPPGVMPPEANVTASGGLQWPQYVEASTGATLYDYAIAGATCDNNNVERWAAFMNANYPSIITDEIPSFKADRKTKLYRGVTSANTVYALWIGTNDLSYTGILSDSQVKGTNITTYIDCLWNVFDAIHAAGGRRFVILNNNALQLTGLYRPLSDGGAGDNQFWQNKTLYNQTEYAQKMLEYTTSSNTMIDYGVPFHLLVKNRWPGSKVAVYDIHSLIMDIYNQPSRYLEPPHNVVGYYKHCDVNGTNCLYGPGRLDSYLWYDELHPS... | Function: Acetylesterase that acts as an exo-deacetylase . Shows activity towards naphtyl acetate, triacetin, as well as towards glucose- and xylose acetates . Liberates acetic acid from xylo-oligomers .
PTM: N-glycosylated.
Catalytic Activity: an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+)
Sequence Mass... |
T2FKR1 | MGRFLTTTALALLATGGAATARPIRACDVSTKYLITFGDSYSQTGFDVTGTKPSASNPLGNPLLPGWTASGGLNWVGFLVSEFNTSTTLSYNFAYGGATTNATIVPPYQPTVLSFIDQVAQFSGSIARKPDYAPWNADNALFGVWIGVNDVGNVWWDPNYDSLLEQIMESYFGQLQILYDAGARNFVLLSVPPIQRTPAVLLNNSPENQKAEALAVDKYNEALAANLEAFTDKNGGITAKIVDTGVPFNTALDNPTDYGAPDATCYNSDGKSCLWFNDYHPGIEINRLVAQAVADAWKGSFF | Function: Acetyl esterase that acts as an exo-deacetylase . Liberates acetic acid from xylo-oligomers .
Catalytic Activity: an acetyl ester + H2O = acetate + an aliphatic alcohol + H(+)
Sequence Mass (Da): 32473
Sequence Length: 302
Subcellular Location: Secreted
EC: 3.1.1.6
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P52957 | MEPPAISQQSTPTAPGGTQGTRKLRESCISCSRSKVKCNKEKPTCSRCVRRGLPCEYMVSRRTGRTRVIGVEQPKTAPSPTTPTNTTAATTATKAGPPVTTDSAVHTPVITTAPSPKPVQIQSPPAEPDLWGAILSPNTSTSTDLSSLLSVNTNFSQLFASLSPSLLEGMDGMDAEMHAPELGALSVADPSSSMMQGLEAPNAAQPPSSNTTSHSYCLSICLDTLMRLFPNAGANCERPGHESNPGKLFTIESVIEDNKQILDTAQTILACRCAEDEYVVTLVSLIVFKVLGWYVAAARDRSSDPGREEDFNWSTAQDSR... | Function: Transcription factor; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins . Binds to the palindromic sequence 5'-TCG(N5)CGA-3'found in the promoter regions of... |
Q6UEH3 | MLIDEAAEASSHISGMKLYLIVLSLLLAVFCVALDNTILSVAIPRITDEFHRLNDIGWYASAYLLTTCAFQLLYGKLYALFSTKWVFLVALCIFEVGSLICGVAPSSVVLIVGRAIAGVGSSGIFTGALVTIAHIVPLAKRPVYMGLLGGMYGIASVAGPLLGGAFTNEVTWRWCFYINLPVGGVTAVVILFLLRIPKSADLRTHGAWEMLKGLDPLGTIVFTPSIICVLLALQWGGVDYAWSNGRIIALFVLFGVLLITFIIIQVLMKDKATVPIKVASQRSVACASVFVFFIGASMFVMIYYVPIWFQAIRNQSPVQA... | Function: Efflux pump; part of the gene cluster that mediates the biosynthesis of aflatoxins .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55021
Sequence Length: 514
Subcellular Location: Cell membrane
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Q6UEH4 | MASNTVYTSLIGLLVALTVRSIYRVYFHPLRKIPGPKIAAITHLYQHYYDAVKGGKYIWKLDELHRKYGPIVRFNPNEVHIQDSHYYHHIYAGGAKKQDKDPGFPAVPLFPGVTVTTIKHNHHRLRRGIIKSFFSKQYVTGLEHVIQSKVNLLASRFTEAYRHGTVLDLKYVFAALTSDLTTHYVYGTNLNHLAEPDFKNDFLAGMDSVGPWIPVLLVFGRLLKLARYLPACLVPAGEFLHLWTLSERRVGEILDSQDNGTMGDQKTLLQAMATADVSEEEKTATRLQMETLNIIAGGTETTARALAVGVFHLAHKPSLL... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins . The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), a... |
Q6UEF2 | MRRYAILGATGNTGQALLNVLLQSPDNQIHAYCRSASKLNRLRPEISQHRQVKVWEGSLEDVSLLSECIRGTRAVFMVVAIPDNMPHCTIAQDCTNAVLNTLKKLQAEGCQSLPKLIVLSSASLEDSLCADVPPLIHRVLNIAAGNLYSDLAKAEKILRAEKHWVSTTFVKPGGLVHDVQRGHTLSTKTAKTPVSFLDVAAGMVEIADMDDKTYDMMNVSVNAIGDGTAFPWKGVYYVLTGLLFHFFPWTYKYFGDSPMPKPRKDL | Function: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins . The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AF... |
Q6UEF1 | MGSHAPAVAGKPDPKKGPYQATPWNIQLSATDTPGFTHVGNLERRSADRASDLVMNNHSKFHTFHDEIVGFHNHISHHVLTLWALGATPDEMQAAYDFNKPFQLLTYYNDPSVNIKLRDPEFFRQGLGNFELYGDYVRFFQAEVAAKGTQTVLHDYLFKGDTLTEDLLARLFSGFLHPLINLGFALEFQQPFLAAECLASTCMHPPYPAEFLTATEQHVECNGRPRSLPILSIAEGMRLDPVVATAVGPEDGNNRIADALLKRALKELIPHLSYFQVEPTEHDLARKTAEILQASAYICGAAQHPRKVEALDFVMLHSLT... | Function: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of aflatoxins, a group of polyketide-derived furanocoumarins, and part of the most toxic and carcinogenic compounds among the known mycotoxins . The four major aflatoxins produced by A.parasiticus are aflatoxin B1 (AFB1), aflatoxin B2 (AF... |
Q5BEJ9 | MAETDSSHTRGPVDSIQKNDASSDDAEAETKIQYPSGWRVTMILTSVTLAYFLFFLDLAVLSTATPAITSQFDSLVDVGWYGGAYQLGSAAFQPLTGKIYSQFSIKQWTFLVFFIVFELGSVLCAAARNSPMFIVGRVIAGVGSAGMSNGAVTTISAVLPTQKQALFMGLNMGMGQLGLATGPIIGGAFTTNVSWREDAPADDDAGFYINLPLGAVVGGFLLFNTIPEPKPKAPPLQILGTAIRSLDLPGFMLICPAVVMFLLGLQFGGNEHPWDSSVVIGLIVGGGATFGVFLVHQWWRGDEAMVPFALLKHKVIWSAA... | Function: Efflux pump; part of the gene cluster that mediates the biosynthesis of asperfuranone, a probable antitumor agent .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56843
Sequence Length: 538
Subcellular Location: Membrane
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Q5BEJ7 | MADHEQEQEPLSIAIIGGGIIGLMTALGLLHRNIGKVTIYERASAWPDIGAAFAFTGIARECMQRLDPAILSALSKVAQRNPHDKVRYWDGFHPKSKEEAQDPEKSVLFEIEEKNMAYWACLRGVFHAEMARLLPERVVRFGKRLVAYEDGGDQKVVLRFEDGEVEEADIVIACDGVHSTARRVLLGAEHPAANARYSRKAVYRALVPMPAAIDALGTEKAHVQIAHCGPDAHIVSFPVNNAQIYNVFLFTHDSNEWTHGHTMTVPSSKEEILSAVENWGPHIKELASLFPEQLSKYAIFDQADHPLPYYAAGRVALAGD... | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of asperfuranone, a probable antitumor agent . The polyketide synthase afoG is responsible for producing the 3,5-dimethyloctadienone moiety from acetyl-CoA, three malonyl-CoA, and two S-adenosyl methionines (SAM) . The 3,5-di... |
Q9FT97 | MSRRAMVIKMPILMILISSMVMTMVESSRSVNNGHDDSEILRRHLLTNGLGVTPPMGWNSWNHFSCNIDEKMIKETADALVTTGLSKLGYNYVNIDDCWAEISRDSKGSLVPKKSTFPSGIKAVADYVHSKGLKLGIYSDAGYFTCSKTMPGSLGYEEHDAKTFAEWGIDYLKYDNCNSDGSKPTVRYPVMTRALMKSGRPIFHSLCEWGDMHPALWGSPVGNSWRTTNDIKDTWLSMISIADMNEVYAEHARPGGWNDPDMLEVGNGGMTKDEYIVHFSIWAISKAPLLLGCDIRNMTKETMEIVANKEVIAINQDPHG... | Function: May regulate leaf (and possibly other organ) development by functioning in cell wall loosening and cell wall expansion.
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.
Sequence ... |
Q8RX86 | MVLLSFSLRFIAFTLTITLTQIADGFQSRMLMNNGLALSPQMGWNSWNHFQCNINETLIKQTADAMVSSGLSAIGYKYINIDDCWGELKRDSQGSLVAKASTFPSGIKALSDYVHSKGLKLGIYSDAGTLTCSQTMPGSLGHEEQDAKTFASWGIDYLKYDNCENTGTSPRERYPKMSKALLNSGRSIFFSLCEWGQEDPATWAGDIGNSWRTTGDIQDNWKSMTLIADQNDRWASYARPGSWNDPDMLEVGNGGMTKEEYMSHFSIWALAKAPLLIGCDLRSMDKVTFELLSNKEVIAVNQDKLGIQGKKVKKEGDLEV... | Function: May regulate leaf (and possibly other organ) development by functioning in cell wall loosening and cell wall expansion.
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.
Sequence ... |
P43469 | MPVEYDPKTGLINLHNDQISYVIQILAHRYPVHRYFGRYFSKQPYFEPMPSGSHAFANDPTERFPYSVTSLPLEYSTIGSGDYRQPAYVIKDANNQLLPILEYTGFSVNDQPINSRQLPPTVSKHTPVTTLVIHLTDAVTKLQMDLNYTIFENQPLILRSTTLRHHGTTNLQVTALSSAQLDLPTDQYTALTLSGTHAHEANPSFNRLHPGLQTVRSLRGTSGPQHQPFMALAEPNTTELAGTVIGCALAWSGNFDSTVEVDQYQHSRLTIGLEPDTFEWQLKPNSSFQTPEAVLTWTNTGFNGMSQVFHDFSYQLMPSQ... | Function: Alpha-galactosidase associated with the sucrase operon.
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.
Sequence Mass (Da): 81368
Sequence Length: 719
EC: 3.2.1.22
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Q8VXZ7 | MVIMKKMKDSVLFLVVGLFSLSVLVSQSIAGRVKAPLLQSNTGGLVFSKSFNSIYDTSMYGRLQLNNGLARTPQMGWNSWNFFACNINETVIKETADALVSSGLADLGYIHVNIDDCWSNLLRDSEGQLVPHPETFPSGIKLLADYVHSKGLKLGIYSDAGVFTCEVHPGSLFHEVDDADIFASWGVDYLKYDNCFNLGIKPIERYPPMRDALNATGRSIFYSLCEWGVDDPALWAKEVGNSWRTTDDINDTWASMTTIADLNNKWAAYAGPGGWNDPDMLEIGNGGMTYEEYRGHFSIWALMKAPLLIGCDVRNMTAET... | Function: May regulate leaf (and possibly other organ) development by functioning in cell wall loosening and cell wall expansion.
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.
Sequence ... |
Q92451 | MSPSAAVLIPLAAAVLLRPVVGQTQCGGNLYTPGTLNFTLECYNAFQDCVAQFEANASQVDCNDGKGNLFMQQQANLGASPGSQNNDAIIAFQDIRDLCLLSGSTTATWGYSDNQWYWAAAEDACYTNDPTRTDVVKTHPAPFCIQNRDSSLPECYPQPDATPPGGPLKVIKTAKTRNGFKSSARGWNTYGVQALVNGSQVVPSFAGQSGLFYTQKFVETQCGVLARPEFKKAGYDLCSLDSGWQATTAVDQHGRIIYNTTRFNLPELASWLHKRDLKLGVYITPGVPCLAHNQTILGTNIKIKDVLNGNNDQINCDFDF... | Function: Alpha-galactosidase involved in the degradation of simple oligosaccharides like melibiose, raffinose and stachyose, and of polymeric galacto(gluco)mannans.
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galacto... |
C8VJZ7 | MELEKFKPWRDSHSEHIPVPLTSRQNIIIILLILFSHYHHWYWRCRRPTDRWSLLAVCHKHHQRAPNSLPTSKSLHSFLHSARGWNSWGIQATPNTIPSYPKEELGRVLNQKFIISQCTMLTDPATQDAGYDLCSLDGGWYSSITDKFGCITYNASLFDISALSRYLHGKGLRMGLYSQPGTPCKARHGTNVTVGSAFIDHVDKNNNCYFDYENPNTQLYRELITLWVSWGVDMIKLDYVTPGSTFQDTCMPGNLNASAIAYHCAIEKSGRKFQLDVSSDVCRSQPYWGTWNSNADSIRVDTDINPYDSDDFFFFYMQHC... | Function: Putative alpha-galactosidase involved in the degradation of simple oligosaccharides like melibiose, raffinose and stachyose, and of polymeric galacto(gluco)mannans.
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides... |
Q4WVZ3 | MDTTKSLLSTLIAIMIPLSLGSVSSPNLLPTPPMGFNNWARFMCDLNETLFLETASAMISTGLLEAGYNRVNLDDCWMAYDRAADSSLQWNTTKFPHGIPWLARHLKAQGFHVGIYEDAGNLTCGGYPGSFGHEALDAQTFAAWGIDYLKLDGCNVFPEHSRTLEEEYKARYAHWHSILKQMHHPLIFSESAPAYFADPANLTSWYEVMDWVPAFGELARHSTDILVYVGEGSAWDSIMVNYRYNTLLARYQRPGYINDPDFLIPDHPGLTLEEKRSQFALWASFSAPLIVSAYIPGLSSEELAILRNEELIRVDQDVLG... | Function: Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides.
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids... |
P28351 | MIQGLESIMNQGTKRILLAATLAATPWQVYGSIEQPSLLPTPPMGFNNWARFMCDLNETLFTETADTMAANGLRDAGYNRINLDDCWMAYQRSDNGSLQWNTTKFPHGLPWLAKYVKAKGFHFGIYEDSGNMTCGGYPGSYNHEEQDANTFASWGIDYLKLDGCNVYATQGRTLEEEYKQRYGHWHQVLSKMQHPLIFSESAPAYFAGTDNNTDWYTVMDWVPIYGELARHSTDILVYSGAGSAWDSIMNNYNYNTLLARYQRPGYFNDPDFLIPDHPGLTADEKRSHFALWASFSAPLIISAYIPALSKDEIAFLTNEA... | Function: Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides.
PTM: A C-terminal Ser/Thr-rich region may provide possible sites for O-glycosylation.
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-... |
Q2UT06 | MRLITRWIPLANALASTMPVQVVASIENPSLLPTPPMGFNNWARFMCDLNETLFVETTDAMASNGLLEAGYNRINLDDCWMNYDRAENGSLEWNVTKFPRGLPWLGQYVKSKGFNFGIYEDSGNLTCGGYPGSEGYEEIDAEIFAAWGIDYLKLDGCNVYPKEGRTLQEEYKYLYGNWHEILSKMQQPLIFSESAPAYFSMTDNLTDWHTVMDWVPEYGELARHSVDILVYSGEGSAWDSIMTNYKFNTLVARYQRPGYYNDPDFLIADHPGLSLDEKRSQFALWASFSAPLIISAHIPDLSSEDLEYLTNQALIAVDQD... | Function: Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides.
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids... |
A1C5D3 | MSRFHLPLAAAVVLVSCLWSANALVRPDGVGKLPALGWNSWNAFGCDIDDAKIMTAAKEIVNLGLKDLGYEYINIDDCWSVKSGRDKTTKRIVPDPAKFPDGIAGVADRIHDLGLKVGIYSSAGLTTCAGYPASLGYEEIDAQTFAEWGIDYLKYDNCGVPSNWTDAYTFCVPDPGSASTNGTCPDNENPAPQGYDWSTSLTAQRHQRMRDALLGVEHTIFYSLCEWGQADVSAWGNATGNSWRMSGDITPSWDRIAAIANENSFLLNHVDFWGHSDPDMLEVGNGDLTLAENRAHFALWAAMKSPLIIGTALDGIDPAH... | Function: Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides.
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids... |
Q4WE86 | MTTFFSLTTAAAVLTLARGSNALVRPGNVGKLPALGWNTWNAFGCDIDATKIMTAANEVVNLGLKDLGYEYINIDDCWSVKSGRDASTQRIIPDPDKFPDGISGVADQIHDLGLKIGIYSSAGLTTCAGYPASLGYEDIDAQTFAEWGIDYLKYDNCGVPSNWTDTYTYCVPDPGSKATNGTCPDNKNPAPAGYDWRTSLTAERYRRMRDALVSVDRTILYSLCEWGQANVNDWGNETGNSWRTTGDITPSWPRIAAIANENSFLMNHVDFWGYPDPDMLEVGNGNLTLAENRAHFALWAAMKSPLIIGTALDSISQDHL... | Function: Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides.
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-galactose residues in alpha-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids... |
D4GU68 | MDLARSSIKLFIANIFGAGLQFLGITFFARELGASQMGVFFLFQALLGIVAIPADFGLRGAVEKRISEGIQPGEYLSSAIILKLIPISLIILSIVVFEQRINGYLGGDFAVYLALAIILQETAQLAVSVLKGELRVGETAELNIIRRITWVGGGFLLVSSGLDAEALIYSLLAGMVVTLAWGLSKISTSLKKPSFKNARSLFNYSKYSVVSSIGGYFYSWMDVAIIGIFLTQSHVGAYETAWRVTAITMLFSQAVASTIFPQVSQWSSKNEQQQIESVISNSITPSMLLVIPAFFGILVFSDEIMGIVFGSEFTIASYVL... | Function: Flippase involved in N-glycan biosynthetic pathway that takes place under low-salt conditions (1.75 M instead of 3.4 M). Participates in the formation of the tetrasaccharide present at 'Asn-532' of S-layer glycoprotein Csg, consisting of a sulfated hexose, 2 hexoses and rhamnose. Probably moves the tetrasacch... |
Q4JAK2 | MYKVWMLTPLFLPVRGGTEVHVFNLSRELVKMSIDVEVHTTRDTYTEREKLIPFEIMDGIKVVRHKRTWIYRDSPSVLHFHNLGRKFSTWNLYTFLFFSLPSVEAPLVMTPHHIFVSDQGRVINWLKRNIGKRVDKLIAVSEWEKEEMINLGYDGSKIVVIPNGVDDMAFNYPKSEGFEDYLLYIGRISPEKNQLFAIECIKNLNVKLILIGQVRDKDYLEKIMTRVSELGLEDKVRYLGVVTEEEKYSLMDKSLAVILTSDIEAEGIVIKEAMVRGVPVIVGNKAKVLSTIVKDGVNGFVISSCQDLKDAVEKLRDPKV... | Function: Glycosyltransferase catalyzing the last biosynthesis step of the N-glycan biosynthesis.
Sequence Mass (Da): 40625
Sequence Length: 352
Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
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O82794 | MAREKIRIKKIDNITARQVTFSKRRRGIFKKADELSVLCDADVALIIFSATGKLFEFSSSRMRDILGRYSLHASNINKLMDPPSTHLRLENCNLSRLSKEVEDKTKQLRKLRGEDLDGLNLEELQRLEKLLESGLSRVSEKKGECVMSQIFSLEKRGSELVDENKRLRDKLETLERAKLTTLKEALETESVTTNVSSYDSGTPLEDDSDTSLKLGLPSWE | Function: Transcription activator that mediates floral transition in response to vernalization. Promotes inflorescence fate in apical meristems. Acts in a dosage-dependent manner. Probably involved in the transduction of RLK-mediated signaling (e.g. IMK3 pathway). Together with AP1 and SVP, controls the identity of the... |
Q4JBJ3 | MRILVLGIDGHLGWPLALRLAKRGHEVIGIDNLSTRRFSEEVGSDSAFPLPQPQERVSEAKKHLGVDITFYVGDITNYGFFKDIVQRYKPDAIVHFAEQRSAPYSMIDMDHAVYTVINNEVSTLRVIQAVLEVDPTIHILKMGTMGEYGTPAFDIPESIYVEAIVNGKKDKIIVPRKAGSVYHWTKVHDTDFLLHFQELYGLTVTDIMQGPVYGTRTEEIVEETLRTRFDFDEVWGTVVNRYCVEAILGLPLTVYGKGGQTRGFISLEDSIQALTLLLENPPKQGEYRVANQFAEIYSVKKIAEFVKKAGEELGLNVEIG... | Function: Catalyzes the biosynthesis of UDP-sulfoquinovose by the transfer of sulfite to UDP-glucose . Important for the assembly of the S-layer N-glycans . The reaction probably occurs through an NAD(+)-dependent oxidation/dehydration/enolization/sulfite addition process . In vitro, in the absence of sulfite, UDP-D-gl... |
Q9YE60 | MAQRVRWERVERVAEAFSRLSIGEVLGFEEQVDPQYKLVSRLAGEIGAGKAALSALLVGLASYRLAMRGEEWWLCFYRHMRSSLPRAEGLRGVLRAVEGFLTSCSGAAIGREAKLRRVRRAASAAEVLGEVLDNPLVLVERPSEVLEALRVALGEKGFRKTTVFSVKIAYYAVRPLAGRKPLTLDVPIPVDVRVACASISSEMVEAPSYREVVARPEAAQRAWGRVARSSGIPVLHIDSILWVTGWAPRELPPGEAREAVAGILSRALDRGKAVLLASELVRRPCPGG | Function: DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates.
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucl... |
Q8TXW8 | MTVPTFLRKVTLREICVIEEYVDVQYRAIEALMDTLPSTDLVRLTVANALVSYQLSSSGEDWWREFSSYFRERRPRDIVREYARFLPRSRGNRRLIRQKLRRLHRAKAFLEELSWQDAKSYYRDMNRLRLDLARVLNADPESKTIVFTVKMFGYALRAITGRFRPYPFEIPIPVDARIERITRRITNDDPQLYWDSIARRTGIPPLHLDSILWVGTSRDPEVKRLLAKVLPKLIGELEMLGN | Function: DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates.
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucl... |
Q6M0G7 | MRNLEKINELLEIFGHFDVNFAKTMEEKIDTQYFVLENLKNSMNNDEMFIKLVILNSIVSYQLCTTGELWWEEFSKYWSKHDANNENLGESYVNFLENSKGNKRLLNVKIKRIERITPFLENLNLLDFKTYYSDMEKLLENLSKYLNSKKNSKTVVFAVKMFGYASRIVFNEFFPYPMNIEIPKDSRIEKYTLKFTDENPIKFWNEVSKTAKIPPLHIDSIIWPVLGRNFDFKSCENKLDENFRYLLKLTEL | Function: DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates.
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucl... |
Q74MX2 | MEDPLIKILKQFSIEDAKYVEYNLDRQFLALKENPKPVGLVIANALISYQLTMPGERYWELFAKKVNSFNDLYDFVKKYNPRFLSNKLKRLERFKPYIDIIEQNREHYYENMVALNKFLAKIMNQNIYDKTIVFSIKMFAYAMRALGYKFKPFPFEIAIPLDYRLKKINPDLNYWFYVSKQTNIPPLHIDSLIWPIFRIKNLPKKFALLKEYLSNL | Function: DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates.
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucl... |
Q9UZY0 | MIARIIGEIGIEGARFIEENIDEQFKALRYLSKGIDSETFVKLVIANSLVSYQLTGKGEQWWWEFAKYFYGRDVKSIYLAYKEFLPNSRFNRRLIPQKLSRIRRVETFLSTLTEERIEEYYGDMSSLWGSIARALGVDKESKTVVFSVKMFGYAARIVLSTFNPYPMEIPIPEDSRIVKLTKKLTNEKPRKFWMKIARESGVPPLHIDSILWPLLGGASIDSAPPELRDKLAELIKIIR | Function: DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates.
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucl... |
Q8ZVK6 | MAAESQLKRVIETLRRLGIEEVLKLERRDPQYRAVCNVVKRHGETVGSRLAMLNALISYRLTGKGEEHWEYFGKYFSQLEVIDLCRDFLKYIETSPFLKIGVEARKKRALKACDYVPNLEDLGLTLRQLSHIVGARREQKTLVFTIKILNYAYMCSRGVNRVLPFDIPIPVDYRVARLTWCAGLIDFPPEEALRRYEAVQKIWDAVARETGIPPLHLDTLLWLAGRAVLYGENLHGVPKEVIALFQWRGGCRPPSE | Function: DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates.
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucl... |
Q8U2D5 | MRELVEIIKGIGIEGAKEVEEKVDRQFYALQYLFRHQDPEMFIKLVIANSLVSYQLTGRGEDWWWEFARYFSGREVDSIWKAYGEFLPKSKNNRRLIEAKLNRIRKVEGFLSTLTLKDLEGYYKNMKMLWKALIKIMGSREDSKTIVFTVKMFGYASRIAFSRFIPYPMEIPIPEDLRIKSVTSKLTQEKPTKFWMKIGQESGVPPLHIDSLIWPLLGNADLTPLDIELRNKLMKLTELLGL | Function: DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates.
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucl... |
O58954 | MIAELIREIGIEGARFIEENIDEQFKALSYLSEGMDRVNFVRLVIANALVSYQLTGKGEMWWWEFAKYFKGKEVKTIYSAYKEFLPNSKFNRRLIQQKLLRIKKIEPFLSTLTEESIERYYEDMTLLWKAIAKVLKVDRESKTVVFSVKMFGYAARIVLSKFNPYPMEIPIPEDVRIIKLTRKLTNERPRDFWMKIAKESNVPPLHIDSILWPLLGGARVEEAPPELKEKLEKLIRVIR | Function: DNA repair enzyme that is part of the base excision repair (BER) pathway; protects from oxidative damage by removing the major product of DNA oxidation, 8-oxoguanine (GO), from single- and double-stranded DNA substrates.
Catalytic Activity: 2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucl... |
O67434 | MGKEALLNLYRIEYRPKDTTFTVFKPTHEIQKEKLNKVRWRVFLQTGLPTFRREDEFWCAGKVEKDTLYLTLSNGEIVELKRVGEEEFRGFQNERECQELFRDFLTKTKVKDKFISDFYKKFRDKITVQGKNRKIALIPEVNEKVLKSEEGYFLLHLDLKFRIQPFETLQTLLERNDFNPKRIRVKPIGIDFVGRVQDVFKAKEKGEEFFRLCMERSTHKSSKKAWEELLKNRELREKAFLVVLEKGYTYPATILKPVLTYENLEDEERNEVADIVRMEPGKRLNLIRYILRRYVKALRDYGWYISPEEERAKGKLNFKD... | Cofactor: Mg(2+) is the preferred cation for DNA-guided cleavage while Mn(2+) supports both DNA- and RNA-guided cleavage of an RNA target. Ca(2+), which is found in the structure, does not support cleavage . Cleavage probaby requires 2 divalent metal cations (By similarity).
Function: A DNA-guided RNA endonuclease. Use... |
A4WYU7 | MAPVQAADEMYDSNPHPDRRQLVSNGFEVNLPDQVEVIVRDLPDPSKVKEERTRLMGYWFVHWFDGKLFHLRIKAGGPNVDGEHRAIRTAEHPWLLRARLDDALEEALPKYAAVKKRPFTFLAQKDELIDAAATAAGLSHRLLNSFKVIPRFALSPKIYEPVDGTTRVGVFVTIGMRYDIEASLRDLLEAGIDLRGMYVVRRKRQPGERGLLGRVRAISDDMVQLFEETDLASVNVNDAKLEGSKENFTRCLSALLGHNYKKLLNALDDQEAGYRTGPRFDDAVRRMGEFLAKKPIRLADNINAQVGDRIVFSNEGQARN... | Cofactor: Mg(2+) contributes to binding the 5'-end of the gRNA.
Function: A catalytically inactive argonaute protein. Binds 5'-phosphorylated RNA as the guide (gRNA) and short DNA as target DNA (tDNA); does not bind other nucleic acid combinations, does not bind tDNA alone . Has highest affinity for gRNA that begins wi... |
C6LTG5 | MTTDIVTSRINFYPYTVLPSAKPVYQYDLSIQVSTQGYNLDNADSYRALEKFCEQQDTALGNDPARSLFYSLIVDFPSSDSRPISSFYSQTDLGSRPVTHTVEFLSTQKPKRRGGRAGGMRGNRGGPSTTSVQALVKVTRVRQMDPLDLMSMKTLLNILLRRTFESSLGMLNIRSGFYDLNRTSTHNIQVDGRGFDICWIPGFRLTTATLYGKLGLQVLPETTKVRSKSMCELLNENRGSLHPNALAAITVMAMHNGRVFRIHSIVRGQSVVSPLAEGSDTDYFTYYSAKYKDKIDSAALSLLKQDDYCNSVLQRDKFIL... | Function: Plays an essential role in growth and, with Dicer, also involved in microRNA (miRNA)-mediated translational repression. The RNA interference pathway is implicated in antigenic variation having a role in regulation of variant-specific surface protein (VSP)-coding gene expression. Several VSP genes are transcri... |
A0A1M5A5Z8 | MYLNLYEIKIPYRVKRLYYFNKENDPKEFARNLSRVNNIRFNDSKDLVWLEIPDIDFKITPQQAEKYKIEKNEIIGEKEDSDLFVKTIYRYIKKKFIDNNFYYKRGNNYISINDKFPLDSNTNVNAHLTYKIKLYKINERYYISVLPKFTFLSDKPALESPIKSTYLFNIKSGKTFPYISGLNGVLKIDLGENGIKEVLFPENYYFNFTSKEAEKFGFSKEIHNIYKEKIFSGYKKIKQSLYFLEDIININNYNLTMDKKIYVNIEYEFKKGISRNIKDVFKYSFYKNDQKIKIAFFFSSKKQIYEIQRSLKMLFQNKNS... | Cofactor: Mn(2+) supports cleavage of all guide:target combinations, Mg(2+) only supports gRNA-directed cleavage . Cleavage probaby requires 2 divalent metal cations (By similarity).
Function: A highly versatile argonaute that uses 5'-phospho- and 5'-OH- guide RNA (gRNA) or DNA (gDNA) to cleave target RNA or ssDNA (tDN... |
H2J4R4 | MYLNLYKIDIPKKIKRLYFYNPDMEPKLFARNLSRVNNFKFQDSNDLVWIEIPDIDFQITPKNVFQYKVEKEEIIKEEEDKKLFVKTLYKYIKKLFLDNDFYFKKGNNFISNSEVFSLDSNENVNAHLTYKIKIHNISNEYYLSILPKFTFLSKEPALESAIKSGYLYNIKSGKSFPYISGLDGILKIDIGNNQIVEVAYPENYLFNFTTRDAEKYGFSKEVHEIYKNKVFEGFKKIPKTLGFLNKITNLNENYQLKDGYKIFINVIYKFKNGESRYAKDVFKYSFYKNEQPLKAIFFFSSKKQFFEVQKSLKELFHNKH... | Cofactor: tDNA cleavage prefers Mn(2+) over Mg(2+) . Cleavage probaby requires 2 divalent metal cations (By similarity).
Function: An RNA-guided ssDNA endonuclease that may play a role in defense against invading mobile genetic elements. Uses short 5'-OH-ssRNA sequences as guides (gRNA) to bind complementary target DNA... |
Q58717 | MVLNKVTYKINAYKIKEEFIPKEVHFYRIKSFVNEAFNFYRFVNFYGGMIINKKDKSFVLPYKVDNKVLKYKDGNNEIPIDIEYIKSLKLEYVKPEIAEKLVRGYLKSVHKIEPELSRIIKNIRKHKVVENIKVESYCEYEVKKHDGDYYLILNFRHTASITKHLWDFVNRDKALLEEYVGKKIIFKPNPKVRYTISLVDAPNPQKIEEIMSHIIKYYKWSEDMVKSTFGEIDYNQPIMYCEEILEPFAPQFCNLVFYMDELDSYILKELQSYWRLSNENKGKIINEIAKKLRFIDNTPKELEFMKFNNTPLLVKDVNKN... | Cofactor: Also liganded by DNA . Cleavage probaby requires 2 divalent metal cations (By similarity).
Function: A DNA-guided ssDNA endonuclease that may play a role in defense against invading genetic elements. Uses short ssDNA sequences as guides (gDNA) to bind complementary target strands, resulting in slicing of the ... |
B9DML4 | MQKVLERKIDAWAQALQKRNNLDRIAYLKIKLGLEVFFNNLFKTIVVYGLALLFHVFLYTLTVHLSYFAIRHYAHGAHAKSTFACYIESIILFVILPWILIKVDIPQIFMIVLAAVAFILICLYSPAITRKQPIPNHMRKKKKITAIFVAGILLIISFFIKQPFNELVQLGIVLIGAAQLPIFFPKQTKEG | Function: Essential for the production of a quorum sensing system signal molecule, the autoinducing peptide (AIP). This quorum sensing system is responsible for the regulation of the expression of virulence factor genes. Involved in the proteolytic processing of AgrD, the precursor of AIP.
Location Topology: Multi-pass... |
P61649 | MLLIDNGIEKMALKLQQRQNLSHIEFLKVRLGMQVVVINTFKAIVTYGLALLLNIFLYTLIVHLTFLTLRTYSHGAHAKTSMLCHVQNIVAFVMLPWLIVQYDISFQFLLILSLLSALIVIKYAPAATKKRPIAPKKVKGLKIKSIIVFVLLMTIACIVPPPYNRFVVYGVLLQSFTLLPIFSIKEEV | Function: Essential for the production of a quorum sensing system signal molecule, the autoinducing peptide (AIP). This quorum sensing system is responsible for the regulation of the expression of virulence factor genes. Involved in the proteolytic processing of AgrD, the precursor of AIP.
Location Topology: Multi-pass... |
Q54337 | MKAIDKKIERFARYLQRQNNLDHIQFLKIRLGLQVALGNFFKTIVTYGVALLFHTFLYTLITHLTYFFVRRFAHGAHARSSLLCHIQNLVLFVALPWSIVHFQVSWTFMIFVAFIAFIIIICYAPSATKKQPILPHLRKKKKRNAILISICFLVLMLFVSEPYMQLIALGMCIEAITLLPIFFSKEET | Function: Essential for the production of a quorum sensing system signal molecule, the autoinducing peptide (AIP). This quorum sensing system is responsible for the regulation of the expression of virulence factor genes. Involved in the proteolytic processing of AgrD, the precursor of AIP.
Location Topology: Multi-pass... |
A6QLU6 | MKKLLPLCCWHSWLLLFYCDFQVRGAHTRSHVHPGFEVLASASHYWPLENVDGIHELQETTGASRTHNLTVLPSHNSTFVYTNDSAYSNFSATVDIVEGKVNKGIYLKEGKGVTFLYYRKNKTSCISNPAQCGPEGVSFSFFWKTQGEQSTSIPSAYGGQVISNGFKVCSRGGKGSVELYTHNKSVTWEASFSPPGHYWTHVLFTWKSEEGLKVYVNGTLRTSDPSGKASPAYGESNDNLVLDLTKSYENRAFDEFIIWERALTPDEIAMYFTAAIGEQLSLSSTPPSFSVTPTVNTMAPTNAYHPIITNLTEERKNFRR... | Function: Orphan receptor. Signals via G(s)-alpha family of G-proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 99812
Sequence Length: 902
Domain: A short peptide sequence (termed the Stachel sequence) in the C-terminal part of the extra-cellular domain (ECD) functions as a tethered agonist. ... |
Q6QNK2 | MEKLLRLCCWYSWLLLFYYNFQVRGVYSRSQDHPGFQVLASASHYWPLENVDGIHELQDTTGDIVEGKVNKGIYLKEEKGVTLLYYGRYNSSCISKPEQCGPEGVTFSFFWKTQGEQSRPIPSAYGGQVISNGFKVCSSGGRGSVELYTRDNSMTWEASFSPPGPYWTHVLFTWKSKEGLKVYVNGTLSTSDPSGKVSRDYGESNVNLVIGSEQDQAKCYENGAFDEFIIWERALTPDEIAMYFTAAIGKHALLSSTLPSLFMTSTASPVMPTDAYHPIITNLTEERKTFQSPGVILSYLQNVSLSLPSKSLSEQTALNL... | Function: Orphan receptor. Signals via G(s)-alpha family of G-proteins . Has protumorigenic function especially in glioblastoma .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 96530
Sequence Length: 874
Domain: A short peptide sequence (termed the Stachel sequence) in the C-terminal part of the ext... |
Q80T32 | MKDLPAFPCSWVWLLWSFCSVQVCSTQPRAQEHPGFAVLASASHYWPLENVDGILELQDTTGALRTLNLTVPLSHNATFVFTNDSAYSNLSATVDIMEGKVNKGIYLKEEKGVTFLYYGTYKSSCISNPAQCGPEGVTFSFFWKTQGDQTRPAPYAYGGQVVSDGFKVCSSGGKGSVELYTRDNSMTWKATFNPPGPYWTHVLFTWKSKEGLKVYVNGTLSTSDPSGKVSHTYGDPHVNLVIGSEQDQTKRYENGAFDEFIIWERALTPDEIKMYFTAAIGKHALLSSTPPAMPTAHTVIPTDAYHPIITNLTEERKRFQ... | Function: Orphan receptor. Signals via G(s)-alpha family of G-proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 99277
Sequence Length: 903
Domain: A short peptide sequence (termed the Stachel sequence) in the C-terminal part of the extra-cellular domain (ECD) functions as a tethered agonist. ... |
Q7Z7M1 | MDAPWGAGERWLHGAAVDRSGVSLGPPPTPQVNQGTLGPQVAPVAAGEVVKTAGGVCKFSGQRLSWWQAQESCEQQFGHLALQPPDGVLASRLRDPVWVGQREAPLRRPPQRRARTTAVLVFDERTADRAARLRSPLPELAALTACTHVQWDCASPDPAALFSVAAPALPNALQLRAFAEPGGVVRAALVVRGQHAPFLAAFRADGRWHHVCATWEQRGGRWALFSDGRRRAGARGLGAGHPVPSGGILVLGQDQDSLGGGFSVRHALSGNLTDFHLWARALSPAQLHRARACAPPSEGLLFRWDPGALDVTPSLLPTVW... | Function: Orphan receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 104087
Sequence Length: 963
Subcellular Location: Membrane
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Q14246 | MRGFNLLLFWGCCVMHSWEGHIRPTRKPNTKGNNCRDSTLCPAYATCTNTVDSYYCACKQGFLSSNGQNHFKDPGVRCKDIDECSQSPQPCGPNSSCKNLSGRYKCSCLDGFSSPTGNDWVPGKPGNFSCTDINECLTSSVCPEHSDCVNSMGSYSCSCQVGFISRNSTCEDVDECADPRACPEHATCNNTVGNYSCFCNPGFESSSGHLSFQGLKASCEDIDECTEMCPINSTCTNTPGSYFCTCHPGFAPSNGQLNFTDQGVECRDIDECRQDPSTCGPNSICTNALGSYSCGCIAGFHPNPEGSQKDGNFSCQRVLF... | Function: Orphan receptor involved in cell adhesion and probably in cell-cell interactions specifically involving cells of the immune system. May play a role in regulatory T-cells (Treg) development.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 97683
Sequence Length: 886
Subcellular Location: Cell... |
Q61549 | MWGFWLLLFWGFSGMYRWGMTTLPTLGQTLGGVNECQDTTTCPAYATCTDTTDSYYCTCKRGFLSSNGQTNFQGPGVECQDVNECLQSDSPCGPNSVCTNILGRAKCSCLRGFSSSTGKDWILGSLDNFLCADVDECLTIGICPKYSNCSNSVGSYSCTCQPGFVLNGSICEDEDECVTRDVCPEHATCHNTLGSYYCTCNSGLESSGGGPMFQGLDESCEDVDECSRNSTLCGPTFICINTLGSYSCSCPAGFSLPTFQILGHPADGNCTDIDECDDTCPLNSSCTNTIGSYFCTCHPGFASSNGQLNFKDLEVTCEDI... | Function: Orphan receptor involved in cell adhesion and probably in cell-cell interactions specifically involving cells of the immune system. May play a role in regulatory T-cells (Treg) development.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 102130
Sequence Length: 931
Subcellular Location: Cel... |
Q5Y4N8 | MWGFWLLLFWGFSGTHRWGMTTLAILGQRLNGVNECQDTTTCPAYATCTDTTESYYCTCKQGFLPSNGQTNFQGPGVECQDVNECLRSDSPCGSNSVCTNIPGRARCSCLSGFSSSAGGSWILGSPGHFLCTDVDECLTIGICPKNSNCSNSVGSYSCTCQSGFVSNGSTCEDEDECVTRNACPEHATCHNTLGSYYCTCNEGLEFSGGGPMFQGLEESCEDVDECSRNSTLCGPSFICINTLGSYSCSCPAGFSLSTFQIPGHPADGNCTDIDECDDICPSNSSCTNTLGSYFCTCHPGFASSNGQLNFTDQEVTCEDI... | Function: Orphan receptor involved in cell adhesion and probably in cell-cell interactions involved specifically cells of the immune system. May play a role in regulatory T-cells (Treg) development.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 102308
Sequence Length: 932
Subcellular Location: Cell... |
Q2Q421 | MRHGHPRLLPGLLMLLLLPLGAAAQKTSGCARWCPPKSTCVNATTCRCSPGFSSLSGEIFSSPLESCDDIDECGPPPLVSCGRLADCQNTEGSYHCMCSPGYALASGATTFMNESENTCRDVDECQLKPRVCKSRGICTNTKGSYTCKCPPGFELNLGDLNLCTDVNECTSGQNPCHNSTHCLNNIGGYECRCRPGWKPVPGSPNGPKSTVCEDVDECSSGKHTCHYSTVCINTVGSYKCRCRRGWKPKPRFQDRQLNTTCEVPAEMSFPTWTPPPGIKSQRLSNFFERVQELHRDFKPALAQETIQDLIQEVDELLEIP... | Function: Cell surface receptor that binds to the chondroitin sulfate moiety of glycosaminoglycan chains and promotes cell attachment. Promotes granulocyte chemotaxis, degranulation and adhesion. In macrophages, promotes the release of inflammatory cytokines, including IL8 and TNF. Signals probably through G-proteins.
... |
Q9UHX3 | MGGRVFLVFLAFCVWLTLPGAETQDSRGCARWCPQDSSCVNATACRCNPGFSSFSEIITTPMETCDDINECATLSKVSCGKFSDCWNTEGSYDCVCSPGYEPVSGAKTFKNESENTCQDVDECQQNPRLCKSYGTCVNTLGSYTCQCLPGFKLKPEDPKLCTDVNECTSGQNPCHSSTHCLNNVGSYQCRCRPGWQPIPGSPNGPNNTVCEDVDECSSGQHQCDSSTVCFNTVGSYSCRCRPGWKPRHGIPNNQKDTVCEDMTFSTWTPPPGVHSQTLSRFFDKVQDLGRDYKPGLANNTIQSILQALDELLEAPGDLET... | Function: Cell surface receptor that binds to the chondroitin sulfate moiety of glycosaminoglycan chains and promotes cell attachment. Promotes granulocyte chemotaxis, degranulation and adhesion. In macrophages, promotes the release of inflammatory cytokines, including IL8 and TNF. Signals probably through G-proteins. ... |
Q2Q426 | MGGRVFLAFCVWLTLLGAETQDSRDCARWCPENSSCVNATACRCNPGFSSSSEIFTSPTEICDDINECVPPSKVSCGKSSDCRNTEGSYDCVCNPGYELVSGAKTFKNESENTCQDVDECQQNPRLCKSYGTCVNTLGSFTCQCLPGFKFKPEDPKLCTDVNECTSGQNPCHSSTHCLNNVGSYQCRCRPGWQPIPGSPNGPNNTICEDVDECSSGLHQCDNSTVCFNTVGSYTCRCRPGWEPKHGIPNNQKDTVCKDMNFPTWTLPPGVHSQTLSQFFNKVQDLDRDFKTSSAKVTIQSILKELDELLEAPGDLETLPR... | Function: Cell surface receptor that binds to the chondroitin sulfate moiety of glycosaminoglycan chains and promotes cell attachment. Promotes granulocyte chemotaxis, degranulation and adhesion. In macrophages, promotes the release of inflammatory cytokines, including IL8 and TNF. Signals probably through G-proteins.
... |
Q9SB31 | MEEREGTNINNNITSSFGLKQQHEAAASDGGYSMDPPPRPENPNPFLVPPTTVPAAATVAAAVTENAATPFSLTMPTENTSAEQLKKKRGRPRKYNPDGTLVVTLSPMPISSSVPLTSEFPPRKRGRGRGKSNRWLKKSQMFQFDRSPVDTNLAGVGTADFVGANFTPHVLIVNAGEDVTMKIMTFSQQGSRAICILSANGPISNVTLRQSMTSGGTLTYEGRFEILSLTGSFMQNDSGGTRSRAGGMSVCLAGPDGRVFGGGLAGLFLAAGPVQVMVGTFIAGQEQSQLELAKERRLRFGAQPSSISFNISAEERKARF... | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs) (By similarity). Acts redundantly with AHL4 to regulate the formation of tissue boundary between the xylem and procambium in the root meristem .
Sequence Mass (Da): 43014
Sequence Length:... |
Q9LVB0 | MEEKGEISPSGVVTVKGDEALVPRTEFQQNPSFLQFVSPTTVVTPLPPPPAPSSAPVPTTVTPGSATASTGSDPTKKKRGRPRKYAPDGSLNPRFLRPTLSPTPISSSIPLSGDYQWKRGKAQQQHQPLEFVKKSHKFEYGSPAPTPPLPGLSCYVGANFTTHQFTVNGGEDVTMKVMPYSQQGSRAICILSATGSISNVTLGQPTNAGGTLTYEGRFEILSLSGSFMPTENGGTKGRAGGMSISLAGPNGNIFGGGLAGMLIAAGPVQVVMGSFIVMHQAEQNQKKKPRVMEAFAPPQPQAPPQLQQQQPPTFTITTVN... | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Sequence Mass (Da): 42804
Sequence Length: 404
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
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Q4V3E0 | METSDRISPGGGIGAEVPSAYHMAPRPSDSPANQFMGLSLPPMEAPMPSSGEASGKKRRGRPRKYEANGAPLPSSSVPLVKKRVRGKLNGFDMKKMHKTIGFHSSGERFGVGGGVGGGVGSNFTPHVITVNTGEDITMRIISFSQQGPRAICILSANGVISNVTLRQPDSCGGTLTYEGRFEILSLSGSFMETENQGSKGRSGGMSVSLAGPDGRVVGGGVAGLLIAATPIQVVVGSFITSDQQDHQKPRKQRVEHAPAAVMSVPPPPSPPPPAASVFSPTNPDREQPPSSFGISSWTNGQDMPRNSATDINISLPVD | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Sequence Mass (Da): 33151
Sequence Length: 318
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
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O80834 | MDRRDAMGLSGSGSYYIHRGLSGSGPPTFHGSPQQQQGLRHLPNQNSPFGSGSTGFGSPSLHGDPSLATAAGGAGALPHHIGVNMIAPPPPPSETPMKRKRGRPRKYGQDGSVSLALSSSSVSTITPNNSNKRGRGRPPGSGKKQRMASVGELMPSSSGMSFTPHVIAVSIGEDIASKVIAFSQQGPRAICVLSASGAVSTATLIQPSASPGAIKYEGRFEILALSTSYIVATDGSFRNRTGNLSVSLASPDGRVIGGAIGGPLIAASPVQVIVGSFIWAAPKIKSKKREEEASEVVQETDDHHVLDNNNNTISPVPQQQ... | Function: Transcription factor that specifically binds AT-rich DNA sequences related to the nuclear matrix attachment regions (MARs).
Sequence Mass (Da): 36335
Sequence Length: 348
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
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P0CJ63 | MTVKKLYFIPAGRCMLDHSSVNSALTPGKLLNLPVWCYLLETEEGPILVDTGMPESAVNNEGLFNGTFVEGQILPKMTEEDRIVNILKRVGYEPDDLLYIISSHLHFDHAGGNGAFTNTPIIVQRTEYEAALHREEYMKECILPHLNYKIIEGDYEVVPGVQLLYTPGHSPGHQSLFIETEQSGSVLLTIDASYTKENFEDEVPFAGFDPELALSSIKRLKEVVKKEKPIIFFGHDIEQEKSCRVFPEYI | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes hydrolysis of N-hexanoyl-(S)-homoserine lactone, but not the R-enantiomer. Hydrolyzes short- and long-chain N-acyl homoserine lactones with or without 3-oxo substitution at C3, has maximum activity on C10-AHL.
Catalytic Activity: an N-acyl-L-homoserine lact... |
A9CKY2 | MGNKLFVLDLGEIRVDENFIIANSTFVTPQKPTVSSRLIDIPVSAYLIQCTDATVLYDTGCHPECMGTNGRWPAQSQLNAPYIGASECNLPERLRQLGLSPDDISTVVLSHLHNDHAGCVEYFGKSRLIAHEDEFATAVRYFATGDHSSPYIVKDIEAWLATPRNWDLVGRDERERELAPGVNLLNFGTGHASGMLGLAVRLEKQPGFLLVSDACYTATNYGPPARRAGVLHDTIGYDRTVSHIRQYAESRSLTVLFGHDREQFASLIKSTDGFYE | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine + H(+)
Sequence Mass (Da): 30562
Sequence Length: 276
EC: 3.1.1.81
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Q7D3U0 | MTDIRLYMLQSGTLKCKVHNIKMNQGNGADYEIPVPFFLITHPAGHTVIDGGNAIEVATDPRGHWGGICDVYWPVLDKDQGCVDQIKALGFDPADVKYVVQSHLHLDHTGAIGRFPNATHIVQRSEYEYAFTPDWFAGGGYIRKDFDKPGLKWQFLNGAQDDYYDVYGDGTLTTIFTPGHAPGHQSFLVRLPNSKPLLLTIDAAYTLDHWEEKALPGFLASTVDTVRSVQKLRTYAEKHDATVVTGHDPDAWANFKKAPEFYA | Cofactor: Binds 2 Zn(2+) ions per subunit.
Catalytic Activity: an N-acyl-L-homoserine lactone + H2O = an N-acyl-L-homoserine + H(+)
Sequence Mass (Da): 29353
Sequence Length: 263
EC: 3.1.1.81
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Q7X3T2 | MEKDQLKVRVLETGVMEADMAWLLLKPGRIIADRNNKERQREWGEIPTHAVLIEHPEGRILWDTGVPRDWSSRWQESGMDNYFPVKTESSSESGFLDSSLAQVGLEPADIDLLILSHLHLDHAGNARLFDNGKTKIVANRKELEGVQEIMGSHLGGHLKADFEGLKIDAIEGDTEIVPGVSVIDTPGHTWGTMSLQVDLPDDGTKIFTSDAVYLRDSFGPPAIGAAVVWNNLLWLESVEKLRRIQERTNAEMIFGHESEQTSQIRWAHQGHYQ | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Hydrolyzes the acyl homoserine lactones N-hexanoyl-L-homoserine lactone, N-3-oxohexanoyl-L-homoserine lactone, N-octonoyl-L-homoserine lactone, N-decanoyl-L-homoserine lactone and N-3-oxododecanoyl-L-homoserine lactone.
Catalytic Activity: an N-acyl-L-homoserine lact... |
P27250 | MSMIKSYAAKEAGGELEVYEYDPGELRPQDVEVQVDYCGICHSDLSMIDNEWGFSQYPLVAGHEVIGRVVALGSAAQDKGLQVGQRVGIGWTARSCGHCDACISGNQINCEQGAVPTIMNRGGFAEKLRADWQWVIPLPENIDIESAGPLLCGGITVFKPLLMHHITATSRVGVIGIGGLGHIAIKLLHAMGCEVTAFSSNPAKEQEVLAMGADKVVNSRDPQALKALAGQFDLIINTVNVSLDWQPYFEALTYGGNFHTVGAVLTPLSVPAFTLIAGDRSVSGSATGTPYELRKLMRFAARSKVAPTTELFPMSKINDA... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Catalyzes the reduction of a wide range of aldehydes including aliphatic fatty aldehydes (C4-C16), into their corresponding alcohols. Has a strong preference for NADPH over NADH as the electron donor. Cannot use glyceraldehyde or a ketone as substrate. Is a relevant ... |
P30561 | MSSGANITYASRKRRKPVQKTVKPIPAEGIKSNPSKRHRDRLNTELDRLASLLPFPQDVINKLDKLSVLRLSVSYLRAKSFFDVALKSTPADRNGGQDQCRAQIRDWQDLQEGEFLLQALNGFVLVVTADALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWALNPDSAQGVDEAHGPPQAAVYYTPDQLPPENASFMERCFRCRLRCLLDNSSGFLAMNFQGRLKYLHGQNKKGKDGALLPPQLALFAIATPLQPPSILEIRTKNFIFRTKHKLDFTPIGCDAKGQLILGYTEVELCTRGSGYQFIH... | Function: Ligand-activated transcription factor that enables cells to adapt to changing conditions by sensing compounds from the environment, diet, microbiome and cellular metabolism, and which plays important roles in development, immunity and cancer . Upon ligand binding, translocates into the nucleus, where it heter... |
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