ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
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stringlengths 108
11.1k
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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 NAA from body fluids.
Catalytic Activity: H2O + N-acyl-L-aspartate = a carboxylate + L-aspartate
Sequence Mass (Da): 35735
Sequence Length: 313
Subcellular Location: Cytoplasm
EC: 3.5.1.15
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O97157 | MDKRMITDAFEEIKWNGWGDTGVCIKYDEARQLPIHTNGKPMKHLLKFMKDDVLKVKGEFKIKPTPGLTKEEAIKRLPPPVVKQPFVDELRQVLSKDQIRLDAYARLTHIFGKNYRDLWRVRRGMIDRPPDAVILPNNHDDCVKIMELAQKHNVVVVPFGGGTNVTGGVEPNPFETRRMVISIDMRRMGRMLHIDTESGTAVFEVGVLGPDIDEQLSRYGFMMGHDPDSYAYSTLGGWIAARGSGAMSNKYGDIENMILAMRVVTPVGVVETPLTSRPCGVDLNAMFVGSEGAFGLVTEAVVKIERLPEVKRYEGWLFPSFEVAFTAFHTCTRKGIHPCTMRLYDEDDTRLSFAASTDSGLVSTFFSKCFKKYIATVKGWNLSKISLVVVGFEGTKAQTNCQRSELVGVFQAFGATCLGTKPGNTWQEKKYDLPYLRDFALAHNFWADVFETSVLYTDAIHCWRAVKKSFAEVMAENGKNAWIGCHTAHQYRFGCCLYFTFIGGQADENDLKIFLQVKKRAMEVMLQHRGNLTHHHGIGYEHVPWMKRYNGEGGLDAIMKFKKALDPKNICNPGKLLPSPPSEKETPKATQARQNREMMFDKMGIPGALQAHL | 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): 69068
Sequence Length: 613
Pathway: Glycerolipid metabolism; ether lipid biosynthesis.
Subcellular Location: Peroxisome
EC: 2.5.1.26
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Q54XP3 | MSWKLDKQFSDKICNFSHDFFNKKLIKKGKPISGEWTVLATLVLVVENTSSYEIKQVLSLGTGNRCLGKSSLSNQGDVLNDSHAEIICKRSFQKFCYNEILNLLQSKYYNSILFNIEYHDSNNNNKDNDNNGSLPTISIKKGHSLHFYVNQTPCGDCSIFPFKKETQPENFIEKEKLEKDGKDKIENHEKKEQKDIIKQVDKDKDEENYEDEESKRKLKKVKDDNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNINNNNNQYDDIQRTGAKTVFGEPEDKKLIGVDYHQIGVLRVKPGRGDPTVSMSCSDKIARWNVLGIQGSLLSHFIKEQIFLSSITIGDLFNHSSIYRGLIGRLLPNPTTTTTETSSSSSSSSSSSNTIPNFKLNSDLEIFSTNIQFQFSKLLLESDQQNNNKSTSSGLAISFCYPNQHEVTIAINGKKMGTNQKNFNAISQRSSICKFNLFKLFHQLVLIIKNKNSNEENEKNNQIVLIDSLFNYYECKHLSKKYYQEYEKLKEFKFKNWLTNSSDLENFVLDN | 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
|
Q9V3R6 | MCDNKKPTVKEIAELCLKKFESLPKTGKPTANQWTILAGIVEFNRNTEACQLVSLGCGTKCIGESKLCPNGLILNDSHAEVLARRGFLRFLYQELKQDRIFHWNSTLSTYDMDEHVEFHFLSTQTPCGDACILEEEQPAARAKRQRLDEDSEMVYTGAKLISDLSDDPMLQTPGALRTKPGRGERTLSMSCSDKIARWNVIGVQGALLDVLISKPIYFSSLNFCCDDAQLESLERAIFKRFDCRTFKHTRFQPQRPQINIDPGIRFEFSQRSDWQPSPNGLIWSQVPEELRPYEISVNGKRQGVTKKKMKTSQAALAISKYKLFLTFLELVKFNPKLSEMFDQQLSDPERIAYASCKDLARDYQFAWREIKEKYFLQWTKKPHELLDFNPMSNK | 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 | MWTADEIAQLCYEHYGIRLPKKGKPEPNHEWTLLAAVVKIQSPADKACDTPDKPVQVTKEVVSMGTGTKCIGQSKMRKNGDILNDSHAEVIARRSFQRYLLHQLQLAATLKEDSIFVPGTQKGVWKLRRDLIFVFFSSHTPCGDASIIPMLEFEDQPCCPVFRNWAHNSSVEASSNLEAPGNERKCEDPDSPVTKKMRLEPGTAAREVTNGAAHHQSFGKQKSGPISPGIHSCDLTVEGLATVTRIAPGSAKVIDVYRTGAKCVPGEAGDSGKPGAAFHQVGLLRVKPGRGDRTRSMSCSDKMARWNVLGCQGALLMHLLEEPIYLSAVVIGKCPYSQEAMQRALIGRCQNVSALPKGFGVQELKILQSDLLFEQSRSAVQAKRADSPGRLVPCGAAISWSAVPEQPLDVTANGFPQGTTKKTIGSLQARSQISKVELFRSFQKLLSRIARDKWPHSLRVQKLDTYQEYKEAASSYQEAWSTLRKQVFGSWIRNPPDYHQFK | 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
|
Q9JHI2 | MWTADEIAQLCYAHYNVRLPKQGKPEPNREWTLLAAVVKIQASANQACDIPEKEVQVTKEVVSMGTGTKCIGQSKMRESGDILNDSHAEIIARRSFQRYLLHQLHLAAVLKEDSIFVPGTQRGLWRLRPDLSFVFFSSHTPCGDASIIPMLEFEEQPCCPVIRSWANNSPVQETENLEDSKDKRNCEDPASPVAKKMRLGTPARSLSNCVAHHGTQESGPVKPDVSSSDLTKEEPDAANGIASGSFRVVDVYRTGAKCVPGETGDLREPGAAYHQVGLLRVKPGRGDRTCSMSCSDKMARWNVLGCQGALLMHFLEKPIYLSAVVIGKCPYSQEAMRRALTGRCEETLVLPRGFGVQELEIQQSGLLFEQSRCAVHRKRGDSPGRLVPCGAAISWSAVPQQPLDVTANGFPQGTTKKEIGSPRARSRISKVELFRSFQKLLSSIADDEQPDSIRVTKKLDTYQEYKDAASAYQEAWGALRRIQPFASWIRNPPDYHQFK | 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 | MQAKGLWSADEIAALSYGHYTTQLPKQGLPDPSREWTLMAAVIQIESVEDTKVIKKVVAMGTGTKCIGQAKLRKTGDVLQDSHAEIIAKRSFQRYLLHQLSLAVSDTKDCLFIPGTEKGKWMLRPEISFVFFTSHTPCGDASIIPVISHEDELGHPLPSEVTEKDHSSNNVCESVNTTYKRKVRSEEDIGFISKKMKHSIDEILTRPENYEEENRHDFPSTCQKALDVHRTGAKCVAGELQDSYSPGVNYHTVGVLRIKPGRGDRTMSMSCSDKMARWNVLGCQGALLMHFLQQPIYLSAVVVGKCPFSQDAMERALYNRCHKVLSLPCAFRLNRVQIIQSDLEFQHGRHALTKKDATRKLVPCGAAVSWSAVPHHPLDVTANGYRQGTTRKAIGSPQCRSRICKAEIFNTFRELVQRLSEKQRSESLSSQGLKTYWDYKAAAITYQEAWNCLRQQAFTSWIQTPRDFLMFS | 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 | MSHQHTTQTSGQGMLERVFKLREHGTTARTEVIAGFTTFLTMVYIVFVNPQILGVAGMDTSAVFVTTCLIAAFGSIMMGLFANLPVALAPAMGLNAFFAFVVVQAMGLPWQVGMGAIFWGAIGLLLLTIFRVRYWMIANIPVSLRVGITSGIGLFIGMMGLKNAGVIVANPETLVSIGNLTSHSVLLGILGFFIIAILASRNIHAAVLVSIVVTTLLGWMLGDVHYNGIVSAPPSVMTVVGHVDLAGSFNLGLAGVIFSFMLVNLFDSSGTLIGVTDKAGLADEKGKFPRMKQALYVDSISSVTGSFIGTSSVTAYIESSSGVSVGGRTGLTAVVVGLLFLLVIFLSPLAGMVPGYAAAGALIYVGVLMTSSLARVNWQDLTESVPAFITAVMMPFSFSITEGIALGFISYCVMKIGTGRLRDLSPCVIIVALLFILKIVFIDAH | 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 | MNQSELIRALPKAELHVHIEGTFEPELMFEIAQRNHIDIPYKSVEEIKKAYNFHNLQSFLDIYYAGANVLINEQDFYDLAWAYFKKCAEDRVVHTEMFFDPQTHTERGVSFEIVLNGLKRACKDAKEHLGISSHLIMCFLRHLSEEDAFKTLEQALPYKADIIAVGLDSSEVGHPPSKFARVFEKAREEGFLVVAHAGEEGPPEYVWEALDLLKVNRIDHGVRSEEDPALMQRLIQEKMPLTVCPLSNLKLCVVNDMKEHNIRRLLNQGVHVTVNSDDPSYFGGYMNDNFVAIQAALDLSNEELKKLAINSFEASFIDEEEKQNWIEEINQI | 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
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Q8UJ05 | MTSHLLKAEIHCHLEGAAPPALVVKQAEKYGIDTSGFLRDGQYVWSDFAEFIQCYDAVAQVFKSDEDYAVLTETYLTELAEANTIYSELIISPDHGDRIGLGADAYLAGVAEGIRIAKEKTGIETRIIVTGERHFGPERVIAAAEYAARIRHPLVTGFNMAGEERMGRVADYARAFDIARDAGLGLTIHAGEVCGPESVADALDLVKPSRIGHGVRAIEDAALISRLVETGTVLEVCPGSNIALSVYPDFASHPLKALSDAGVRVCISSDDPPFFFTSLAREYALAADAFGFNDAEINRMTRTALECAFVDEATRERLLARLGDA | 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
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P54202 | MAAPEIPKKQKAVIYDNPGTVSTKVVELDVPEPGDNEVLINLTHSGVCHSDFGIMTNTWKILPFPTQPGQVGGHEGVGKVVKLGAGAEASGLKIGDRVGVKWISSACGQCPPCQDGADGLCFNQKVSGYYTPGTFQQYVLGPAQYVTPIPDGLPSAEAAPLLCAGVTVYASLKRSKAQPGQWIVISGAGGGLGHLAVQIAAKGMGLRVIGVDHGSKEELVKASGAEHFVDITKFPTGDKFEAISSHVKSLTTKGLGAHAVIVCTASNIAYAQSLLFLRYNGTMVCVGIPENEPQAIASAYPGLFIQKHVHVTGSAVGNRNEAIETMEFAARGVIKAHFREEKMEALTEIFKEMEEGKLQGRVVLDLS | 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 | MSTQQTMTVDEHINQLVAKAQVALKEYLKPEYTQEKIDYIVKKASVAALDQHCALAAAAVEETGRGIFEDKATKNIFACEHVTHEMRHAKTVGIINVDPLYGITEIAEPVGVVCGVTPVTNPTSTAIFKSLISIKTRNPIVFSFHPSALKCSIMAAKIVRDAAISAGAPENCIQWIEFGGIEASNKLMNHPGVATILATGGNAMVKAAYSSGKPALGVGAGNVPTYIEKTCNIKQAANDVVMSKSFDNGMICASEQAAIIDKEIYDQVVEEMKTLGAYFINEEEKAKLEKFMFGVNAYSADVNNARLNPKCPGMSPQWFAEQVGIKVPEDCNIICAVCKEVGPNEPLTREKLSPVLAILKAENTQDGIDKAEAMVEFNGRGHSAAIHSNDKAVVEKYALTMKACRILHNTPSSQGGIGSIYNYIWPSFTLGCGSYGGNSVSANVTYHNLLNIKRLADRRNNLQWFRVPPKIFFEPHSIRYLAELKELSKIFIVSDRMMYKLGYVDRVMDVLKRRSNEVEIEIFIDVEPDPSIQTVQKGLAVMNTFGPDNIIAIGGGSAMDAAKIMWLLYEHPEADFFAMKQKFIDLRKRAFKFPTMGKKARLICIPTTSGTGSEVTPFAVISDHETGKKYPLADYSLTPSVAIVDPMFTMSLPKRAIADTGLDVLVHATEAYVSVMANEYTDGLAREAVKLVFENLLKSYNGDLEAREKMHNAATIAGMAFASAFLGMDHSMAHKVGAAFHLPHGRCVAVLLPHVIRYNGQKPRKLAMWPKYNFYKADQRYMELAQMVGLKCNTPAEGVEAFAKACEELMKATETITGFKQANIDEAAWMSKVPEMALLAFEDQCSPANPRVPMVKDMEKILKAAYYPIA | 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 | MKAAVVNEFKKALEIKEVERPKLEEGEVLVKIEACGVCHTDLHAAHGDWPIKPKLPLIPGHEGVGIVVEVAKGVKSIKVGDRVGIPWLYSACGECEYCLTGQETLCPHQLNGGYSVDGGYAEYCKAPADYVAKIPDNLDPVEVAPILCAGVTTYKALKVSGARPGEWVAIYGIGGLGHIALQYAKAMGLNVVAVDISDEKSKLAKDLGADIAINGLKEDPVKAIHDQVGGVHAAISVAVNKKAFEQAYQSVKRGGTLVVVGLPNADLPIPIFDTVLNGVSVKGSIVGTRKDMQEALDFAARGKVRPIVETAELEEINEVFERMEKGKINGRIVLKLKED | 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 | MQNFTFRNPTKLIFGRGQIEQLKEEVPKYGKKVLLVYGGGSIKRNGLYDEVMSLLTDIGAEVVELPGVEPNPRLSTVKKGVDICRREGIEFLLAVGGGSVIDCTKAIAAGAKFDGDPWEFITKKATVTEALPFGTVLTLAATGSEMNAGSVITNWETKEKYGWGSPVTFPQFSILDPTYTMTVPKDHTVYGIVDMMSHVFEQYFHHTPNTPLQDRMCEAVLKTVIEAAPKLVDDLENYELRETIMYSGTIALNGFLQMGVRGDWATHDIEHAVSAVYDIPHAGGLAILFPNWMKHVLDENVSRFAQLAVRVFDVDPTGKTERDVALEGIERLRAFWSSLGAPSRLADYGIGEENLELMADKAMAFGEFGRFKTLNRDDVLAILRASL | 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-chain primary fatty alcohol + H2O + 2 NAD(+) = a long-chain fatty acid + 3 H(+) + 2 NADH
Sequence Mass (Da): 42804
Sequence Length: 387
EC: 1.1.1.192
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Q9P4C2 | MSIPTTQKGVIFYENGGQLYYKDIPVPKPKSNELLINVKYSGVCHTDLHAWKGDWPLDTKLPLVGGHEGAGVVVAMGDNVKGWKIGDLAGIKWLNGSCMNCEECELSNESNCPDADLSGYTHDGSFQQYATADAVQAAHIPAGTDLAQVAPILCAGVTVYKALKTAEMKAGDWVAISGAAGGLGSLAVQYAKAMGFRVLGIDGGEGKEELFKSLGGEVFIDFTKSKDIVGEVIKATNGGAHGVINVSVSEKAIESSIEYCRSNGTVVLVGLPKDAKCKSDVFNQVVKSIHIVGSYVGNRADTREALDFFCRGLVNAPIKVVGLSTLPEIYEKMEQGKVLGRYVVDTSK | 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 | MSIPTTQKAVIFETNGGPLLYKDIPVPKPKPNELLINVKYSGVCHTDLHAWKGDWPLDTKLPLVGGHEGAGVVVALGENVTGWEIGDYAGIKWINGSCLQCEYCVTAHESNCPDADLSGYTHDGSFQQYATADAIQAARIPKGTDLALIAPILCAGITVYKALKTAQLQAGQWVAVSGAAGGLGSLAIQYAKAMGYRVVGIDGGADKGEFAKSLGAEVFVDFLSSKDVVADVLKATNGGAHGVINVSVSERAMQQSVDYVRPTGTVVLVGLPAGAKVSASVFSSVVRTIQIKGSYVGNRADSAEAIDFFTRGLIKCPIKIVGLSELASVYELMEQGKILGRYVVDTSK | 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 | MSTTVGQVIRCKAAVAWEAGKPLVMEEVDVAPPQKMEVRLKILYTSLCHTDVYFWEAKGQNPVFPRILGHEAAGIVESVGEGVTDLAPGDHVLPVFTGECKDCAHCKSEESNMCSLLRINTDRGVMLNDGKSRFSINGNPIYHFVGTSTFSEYTVVHVGCVAKINPLAPLDKVCVLSCGISTGLGASLNVAKPTKGSSVAIFGLGAVGLAAAEGARIAGASRIIGVDLNASRFEQAKKFGVTEFVNPKDYSKPVQEVIAEMTDGGVDRSVECTGHIDAMISAFECVHDGWGVAVLVGVPHKEAVFKTHPLNFLNERTLKGTFFGNYKPRSDIPCVVEKYMNKELELEKFITHTLPFAEINKAFDLMLKGEGLRCIITMAD | 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 | MSLNTPDVIICKAAVVRELGRSVMVEEIKVDPPKATEVRIKMLFASICHTDMLCFDGFPTPLFPRIPGHEGVGMVESVGEDIKTKLKPGDIVMPLFMGECGQCLNCKSKRTNLCHAYPLTLSGLLLDGTSRMSIAKTEETIYHHLSCSTWSEYMVIDINYVLKIDPKMHLPYASFLSCGFTTGFGAPWKETQITKGSIVAVFGLGAVGLGAIKGAQMQGASIIIGVDINENKAAKGKAFGMTHFINPKDHPNQLVSDMVRDITDGLGVDYCFECTGIASLLKEIIEASKIGFGTTILIGAAPDNVPISSLSLINGRTLKGTTFGGVRTRSDLPIILQKCMNEEIELDELMSHEIRLENIHEIFEILKKPDCVKILINFD | 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(+) + NADH
Sequence Mass (Da): 41397
Sequence Length: 379
Pathway: Isoprenoid biosynthesis.
EC: 1.1.1.144
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Q8GIX7 | MKAAVLHEFGQSLQIEEVDIPTPGAGEIVVKMQASGVCHTDLHAVEGDWPVKPSPPFIPGHEGVGLITAVGEGVTHVKEGDRVGVAWLYSACGHCTHCLGGWETLCESQQNSGYSVNGSFAEYVLANANYVGIIPESVDSIEIAPVLCAGVTVYKGLKMTDTKPGDWVVISGIGGLGHMAVQYAIAMGLNVAAVDIDDDKLAFAKKLGAKVTVNAKNTDPAEYLQKEIGGAHGALVTAVSAKAFDQALSMLRRGGTLVCNGLPPGDFPVSIFDTVLNGITIRGSIVGTRLDLQESLDMAAAGKVKATVTAEPLENINDIFERMRQGKIEGRIVIDYTM | 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 aliphatic alcohols, utilizing NAD(+) as a cosubstrate. In vitro, shows highest reaction rates for ethanol as a substrate and gradually decreases its reaction rates as the length and branching of the carbon chain of the alcohol substrates increase. To a lesser extent, is also able to reduce aldehydes and ketones. Do not catalyze the further oxidation of aldehydes to carboxylic acids. Cannot use NADP(+) instead of NAD(+).
Catalytic Activity: a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH
Sequence Mass (Da): 35587
Sequence Length: 338
Domain: Each subunit comprises two distinct structural domains: the catalytic domain (residues 1-150 and 288-340/345) and the nucleotide-binding domain (residues 151-287).
EC: 1.1.1.1
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P75214 | MKAYAMLKIGATGWIEKPRPVCGPNDAIIRPLAVAPCTSDVHTVWEGGIGERHNMVLGHEGCGVVDEVGSEVKSFKVGDRVLVAAITPEWNSVNAQAGYPMHSGGMLGGWKFSNVKDGMFAEYFHVNDAEGNLALMPEGMDLADACMLSDMIPTGFHANELADIQYGVALSFFCAGPVGLMAIAGAALKGAGRIIVVDSRPDIVEIAKAYGATDYIDFKKVSVVDEILKWTNNEGVEKVLISGGGSTILETAIKVLRPGGKIGNVNYFGAGEFLTIPRVEWGVGMAHKAIHGGLMLGGRLRLEKLARLIMTKKLDPSKMITHRFKGFEHIEEALFLMKDKPKDLIKSVVIF | 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 alcohols. Is also active with acetaldehyde and propionaldehyde (By similarity).
Catalytic Activity: NADP(+) + propan-2-ol = acetone + H(+) + NADPH
Sequence Mass (Da): 37812
Sequence Length: 351
EC: 1.1.1.80
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P9WQC2 | MSDGAVVRALVLEAPRRLVVRQYRLPRIGDDDALVRVEACGLCGTDHEQYTGELAGGFAFVPGHETVGTIAAIGPRAEQRWGVSAGDRVAVEVFQSCRQCANCRGGEYRRCVRHGLADMYGFIPVDREPGLWGGYAEYQYLAPDSMVLRVAGDLSPEVATLFNPLGAGIRWGVTIPETKPGDVVAVLGPGIRGLCAAAAAKGAGAGFVMVTGLGPRDADRLALAAQFGADLAVDVAIDDPVAALTEQTGGLADVVVDVTAKAPAAFAQAIALARPAGTVVVAGTRGVGSGAPGFSPDVVVFKELRVLGALGVDATAYRAALDLLVSGRYPFASLPRRCVRLEGAEDLLATMAGERDGVPPIHGVLTP | 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 | MRAVRLVEIGKPLSLQEIGVPKPKGPQVLIKVEAAGVCHSDVHMRQGRFGNLRIVEDLGVKLPVTLGHEIAGKIEEVGDEVVGYSKGDLVAVNPWQGEGNCYYCRIGEEHLCDSPRWLGINFDGAYAEYVIVPHYKYMYKLRRLNAVEAAPLTCSGITTYRAVRKASLDPTKTLLVVGAGGGLGTMAVQIAKAVSGATIIGVDVREEAVEAAKRAGADYVINASMQDPLAEIRRITESKGVDAVIDLNNSEKTLSVYPKALAKQGKYVMVGLFGADLHYHAPLITLSEIQFVGSLVGNQSDFLGIMRLAEAGKVKPMITKTMKLEEANEAIDNLENFKAIGRQVLIP | 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 | MTIPDKQLAAVFHTHGGPENVKFEEVPVAEPGQDEVLVNIKYTGVCHTDLHALQGDWPLPAKMPLIGGHEGAGVVVKVGAGVTRLKIGDRVGVKWMNSSCGNCEYCMKAEETICPHIQLSGYTVDGTFQHYCIANATHATIIPESVPLEVAAPIMCAGITCYRALKESKVGPGEWICIPGAGGGLGHLAVQYAKAMAMRVVAIDTGDDKAELVKSFGAEVFLDFKKEADMIEAVKAATNGGAHGTLVLSTSPKSYEQAAGFARPGSTMVTVSMPAGAKLGADIFWLTVKMLKICGSHVGNRIDSIEALEYVSRGLVKPYYKVQPFSTLPDVYRLMHENKIAGRIVLDLSK | 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 | MGDGWLPPDCGPHNRSGGGGATAAPTGSRQVSAELLSQQWEAGMSLLMALVVLLIVAGNVLVIAAIGRTQRLQTLTNLFITSLACADLVMGLLVVPFGATLVVRGTWLWGSFLCECWTSLDVLCVTASIETLCVIAIDRYLAITSPFRYQSLMTRARAKVIICTVWAISALVSFLPIMMHWWRDEDPQALKCYQDPGCCDFVTNRAYAIASSIISFYIPLLIMIFVYLRVYREAKEQIRKIDRCEGRFYGSQEQPQPPPLPQHQPILGNGRASKRKTSRVMAMREHKALKTLGIIMGVFTLCWLPFFLVNIVNVFNRDLVPDWLFVFFNWLGYANSAFNPIIYCRSPDFRKAFKRLLCFPRKADRRLHAGGQPAPLPGGFISTLGSPEHSPGGTWSDCNGGTRGGSESSLEERHSKTSRSESKMEREKNILATTRFYCTFLGNGDKAVFCTVLRIVKLFEDATCTCPHTHKLKMKWRFKQHQA | 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: Homologous desensitization of the receptor is mediated by its phosphorylation by beta-adrenergic receptor kinase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54078
Sequence Length: 483
Subcellular Location: Cell membrane
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P18090 | MGAGALALGASEPCNLSSAAPLPDGAATAARLLVLASPPASLLPPASEGSAPLSQQWTAGMGLLLALIVLLIVVGNVLVIVAIAKTPRLQTLTNLFIMSLASADLVMGLLVVPFGATIVVWGRWEYGSFFCELWTSVDVLCVTASIETLCVIALDRYLAITLPFRYQSLLTRARARALVCTVWAISALVSFLPILMHWWRAESDEARRCYNDPKCCDFVTNRAYAIASSVVSFYVPLCIMAFVYLRVFREAQKQVKKIDSCERRFLTGPPRPPSPAPSPSPGPPRPADSLANGRSSKRRPSRLVALREQKALKTLGIIMGVFTLCWLPFFLANVVKAFHRDLVPDRLFVFFNWLGYANSAFNPIIYCRSPDFRKAFQRLLCCARRAACRRRAAHGDRPRASGCLARAGPPPSPGAPSDDDDDDAGATPPARLLEPWAGCNGGTTTVDSDSSLDEPGRQGFSSESKV | 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 in the regulation of sleep/wake behaviors (By similarity).
PTM: Homologous desensitization of the receptor is mediated by its phosphorylation by beta-adrenergic receptor kinase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50472
Sequence Length: 466
Domain: The PDZ domain-binding motif mediates competitive interactions with GOPC, MAGI3 and DLG4 and plays a role in subcellular location of the receptor.
Subcellular Location: Cell membrane
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P07550 | MGQPGNGSAFLLAPNGSHAPDHDVTQERDEVWVVGMGIVMSLIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVPFGAAHILMKMWTFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYFAITSPFKYQSLLTKNKARVIILMVWIVSGLTSFLPIQMHWYRATHQEAINCYANETCCDFFTNQAYAIASSIVSFYVPLVIMVFVYSRVFQEAKRQLQKIDKSEGRFHVQNLSQVEQDGRTGHGLRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQDNLIRKEVYILLNWIGYVNSGFNPLIYCRSPDFRIAFQELLCLRRSSLKAYGNGYSSNGNTGEQSGYHVEQEKENKLLCEDLPGTEDFVGHQGTVPSDNIDSQGRNCSTNDSLL | 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 . Palmitoylation may reduce accessibility of phosphorylation sites by anchoring the receptor to the plasma membrane. Agonist stimulation promotes depalmitoylation and further allows Ser-345 and Ser-346 phosphorylation . Also undergoes transient, ligand-induced palmitoylation at Cys-265 probably by ZDHHC9, ZDHHC14 and ZDHHC18 within the Golgi . Palmitoylation at Cys-265 requires phosphorylation by PKA and receptor internalization and stabilizes the receptor . Could be depalmitoylated by LYPLA1 at the plasma membrane .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46459
Sequence Length: 413
Subcellular Location: Cell membrane
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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 agonist stimulation, which mediates homologous desensitization of the receptor. PKA-mediated phosphorylation seems to facilitate phosphorylation by BARK.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28502
Sequence Length: 251
Subcellular Location: Cell membrane
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Q28997 | MGQPGNRSVFLLAPNGSHAPDQDVPQERDEAWVVGMAIVMSLIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVPFGASHILMKMWTFGSFWCEFWISIDVLCVTASIETLCVIAVDRYLAITSPFKYQCLLTKNKARVVILMVWVVSGLISFLPIKMHWYQATHREALNCYAEEACCDFFTNQPYAIASSIVSFYLPLVVMVFVYSRVFQVARRQLQKIDKSEGRFHAQNLSQAEQDGRSGPGHRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHGIHDNLIPKEVYILLNWVGYVNSAFNPLIYCRSPDFRMAFQELLCLHRSSLKAYGNGCSSNSNGRTDYTGEQSGCYLGEEKDSERLCEDAPGPEGCAHRQGTVPDDSTDSQGRNCSTNDSML | 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 accessibility of Ser-345 and Ser-346 by anchoring Cys-341 to the plasma membrane. Agonist stimulation promotes depalmitoylation and further allows Ser-345 and Ser-346 phosphorylation (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46760
Sequence Length: 418
Subcellular Location: Cell membrane
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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 | MQKIKLTGLSLIISGLLMAQAQAAEPVYPDQLRLFSLGQGVCGDKYRPVNREEAQSVKSNIVGMMGQWQISGLANGWVIMGPGYNGEIKPGTASNTWCYPTNPVTGEIPTLSALDIPDGDEVDVQWRLVHDSANFIKPTSYLAHYLGYAWVGGNHSQYVGEDMDVTRDGDGWVIRGNNDGGCDGYRCGDKTAIKVSNFAYNLDPDSFKHGDVTQSDRQLVKTVVGWAVNDSDTPQSGYDVTLRYDTATNWSKTNTYGLSEKVTTKNKFKWPLVGETELSIEIAANQSWASQNGGSTTTSLSQSVRPTVPARSKIPVKIELYKADISYPYEFKADVSYDLTLSGFLRWGGNAWYTHPDNRPNWNHTFVIGPYKDKASSIRYQWDKRYIPGEVKWWDWNWTIQQNGLSTMQNNLARVLRPVRAGITGDFSAESQFAGNIEIGAPVPLAADSKVRRARSVDGAGQGLRLEIPLDAQELSGLGFNNVSLSVTPAANQ | 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 cleavage and subsequent release of the propeptide trigger a major conformation change, leading to the formation of a heptameric pre-pore that then inserts into the host membrane.
Sequence Mass (Da): 54342
Sequence Length: 493
Domain: The C-terminal propeptide is required for normal protein folding and secretion; it maintains the aerolysin precursor in its soluble form and prevents premature heptamerization and pore formation.
Subcellular Location: Secreted
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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 C8 followed by decarboxylation to produce the dihydro-4-hydroxyphenylpyruvate regioisomer A258 (H2HPP A258)(3-(4-hydroxycyclohexa- 1,5-dienyl)-2-oxopropanoic acid), which is able to undergo a nonenzymatic isomerization to produce dihydro-4-hydroxyphenylpyruvate regioisomer A295 (H2HPP A295)(3-(4-hydroxycyclohex-2-enylidene)-2-oxopropanoic acid).
Catalytic Activity: H(+) + prephenate = 3-[(4R)-4-hydroxycyclohexa-1,5-dien-1-yl]-2-oxopropanoate + CO2
Sequence Mass (Da): 23114
Sequence Length: 202
EC: 4.1.1.100
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Q39172 | MTATNKQVILKDYVSGFPTESDFDFTTTTVELRVPEGTNSVLVKNLYLSCDPYMRIRMGKPDPSTAALAQAYTPGQPIQGYGVSRIIESGHPDYKKGDLLWGIVAWEEYSVITPMTHAHFKIQHTDVPLSYYTGLLGMPGMTAYAGFYEVCSPKEGETVYVSAASGAVGQLVGQLAKMMGCYVVGSAGSKEKVDLLKTKFGFDDAFNYKEESDLTAALKRCFPNGIDIYFENVGGKMLDAVLVNMNMHGRIAVCGMISQYNLENQEGVHNLSNIIYKRIRIQGFVVSDFYDKYSKFLEFVLPHIREGKITYVEDVADGLEKAPEALVGLFHGKNVGKQVVVVARE | 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), 4-hydroxy-(2E)-hexenal (HHE), (2E)-nonenal, (2E)-hexenal, (2E)-pentenal, propenal (acrolein), 3-buten-2-one and 3-penten-2-one, but not (R)-(-)-carvone, n-nonanal, n-hexanal, (3Z)-hexanal, cyclohex-2-en-1-one or 12-oxo phytodienoic acid (OPDA) as electron acceptors . Catalyzes the reduction of the alpha,beta-unsaturated bond of 2-alkenals, of lipid peroxide-derived oxenes 9-oxo-10(E),12(Z)-octadecadienoic acid (9-KODE) and 13-oxo-9(Z),11(E)-octadecadienoic acid (13-KODE), as well as 4-oxo-(2E)-nonenal and 4-hydroxynonenal . Can use 12-oxo-10(E) dodecanoate (traumatin), trans-1,3 diphenyl-2-propenone, trans-1,4-diphenyl-2-butene-1,4-dione, 9-oxo-12,13-epoxy-(10E)-octadecenoic acid (trans-EKODE-1b) and 9,13-dihydroxy-10-oxo-11-octadecenoic acid as substrates . Catalyzes the reduction of the 7-8 double bond of phenylpropanal substrates, such as p-coumaryl aldehyde and coniferyl aldehyde (in vitro) . Has activity towards toxic substrates, such as 4-hydroxy-(2E)-nonenal (in vitro) . May play a distinct role in plant antioxidant defense and is possibly involved in NAD(P)/NAD(P)H homeostasis .
Catalytic Activity: an n-alkanal + NAD(+) = an alk-2-enal + H(+) + NADH
Sequence Mass (Da): 38134
Sequence Length: 345
Subcellular Location: Cytoplasm
EC: 1.3.1.-
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P50466 | MSSHPYVTQQNTPLADDTTLMSTTDLQSYITHANDTFVQVSGYTLQELQGQPHNMVRHPDMPKAAFADMWFTLKKGEPWSGIVKNRRKNGDHYWVRANAVPMVREGKISGYMSIRTRATDEEIAAVEPLYKALNAGRTSKRIHKGLVVRKGWLGKLPSLPLRWRARGVMTLMFILLAAMLWFVAAPVVTYILCALVVLLASACFEWQIVRPIENVAHQALKVATGERNSVEHLNRSDELGLTLRAVGQLGLMCRWLINDVSSQVSSVRNGSETLAKGTDELNEHTQQTVDNVQQTVATMNQMAASVKQNSATASAADKLSITASNAAVQGGEAMTTVIKTMDDIADSTQRIGTITSLINDIAFQTNILALNAAVEAARAGEQGKGFAVVAGEVRHLASRSANAANDIRKLIDASADKVQSGSQQVHAAGRTMEDIVAQVKNVTQLIAQISHSTLEQADGLSSLTRAVDELNLITQKNAELVEESAQVSAMVKHRASRLEDAVTVLH | 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: Multi-pass membrane protein
Sequence Mass (Da): 55066
Sequence Length: 506
Subcellular Location: Cell inner membrane
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Q9I3F6 | MRNNQPITQHERVYPAEQRLITTTNLKGIITYCNEAFIDISGFSREELMSAPHNLIRHPDVPPAVFAHMWTTLKAGRPWMGIVKNRCKNGDHYWVSAYVTPIYDQGAVVGYESVRVKPTAEQIQRAEALYRRLGAGKPAIPRRDRWLPVLLDWLPFILISQIGFLIGIWLNSWWGFILAGLLAVPLGLAGLRWQKRGLKRLMRLAEQTTSDPLIAQMYTDSRGDQARLEMAILSQDARLKTCLTRLQDTAEYLTEQARQADTLAHHSSAGLEQQRAETEQVATAVNEMAATTQEVANNVQLTADATQKANELTSRGRDIAAETRNAIQRLSESVGETGAAVSRLAQDSNEIGGVVDVIKGIADQTNLLALNAAIEAARAGDQGRGFAVVADEVRSLAQRTAASTEQIHHLIAKLQNTANDAVHTMESGLQQAEAGVQRVLEADSALVGISEAVSNITEMTTQIAAAAEEQSAVAEEINRNISTIAALAEQTSDEALRTAKLSEELTTTAQSQYSLVERFNR | 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 | MRSILVIPSFVAVLNAFSLFPKPHDDFKYLITFGDSYTDNGRLGYYGSHQAHGPPPGVMPPEANVTASGGLQWPQYVEASTGATLYDYAIAGATCDNNNVERWAAFMNANYPSIITDEIPSFKADRKTKLYRGVTSANTVYALWIGTNDLSYTGILSDSQVKGTNITTYIDCLWNVFDAIHAAGGRRFVILNNNALQLTGLYRPLSDGGAGDNQFWQNKTLYNQTEYAQKMLEYTTSSNTMIDYGVPFHLLVKNRWPGSKVAVYDIHSLIMDIYNQPSRYLEPPHNVVGYYKHCDVNGTNCLYGPGRLDSYLWYDELHPSNIIASYIAREFLNVVSGRSKYGTYWEHW | 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 (Da): 39158
Sequence Length: 348
Subcellular Location: Secreted
EC: 3.1.1.6
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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 | MEPPAISQQSTPTAPGGTQGTRKLRESCISCSRSKVKCNKEKPTCSRCVRRGLPCEYMVSRRTGRTRVIGVEQPKTAPSPTTPTNTTAATTATKAGPPVTTDSAVHTPVITTAPSPKPVQIQSPPAEPDLWGAILSPNTSTSTDLSSLLSVNTNFSQLFASLSPSLLEGMDGMDAEMHAPELGALSVADPSSSMMQGLEAPNAAQPPSSNTTSHSYCLSICLDTLMRLFPNAGANCERPGHESNPGKLFTIESVIEDNKQILDTAQTILACRCAEDEYVVTLVSLIVFKVLGWYVAAARDRSSDPGREEDFNWSTAQDSRRGSVSSFEEQVLHLPTVVGSYCIDGHHQSRMAAQLVLSELYRVQRLVTQVSRRLESIRRRSSSSSSSASSNTTDSDGGMSTPLSSTTLVHLEDDLRKRLRAVSSETISILRHA | 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 several sterigmatocystin cluster genes to induce their expression .
Sequence Mass (Da): 46566
Sequence Length: 433
Pathway: Mycotoxin biosynthesis; sterigmatocystin biosynthesis [regulation].
Subcellular Location: Nucleus
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Q6UEH3 | MLIDEAAEASSHISGMKLYLIVLSLLLAVFCVALDNTILSVAIPRITDEFHRLNDIGWYASAYLLTTCAFQLLYGKLYALFSTKWVFLVALCIFEVGSLICGVAPSSVVLIVGRAIAGVGSSGIFTGALVTIAHIVPLAKRPVYMGLLGGMYGIASVAGPLLGGAFTNEVTWRWCFYINLPVGGVTAVVILFLLRIPKSADLRTHGAWEMLKGLDPLGTIVFTPSIICVLLALQWGGVDYAWSNGRIIALFVLFGVLLITFIIIQVLMKDKATVPIKVASQRSVACASVFVFFIGASMFVMIYYVPIWFQAIRNQSPVQAGIDSIALILANTAGAIISGAVTNKTGHYAPWFIVSSVIMSIGAGCLTLFTVDIAQSKWIGFLFLYGIGVGFGFQQGAVAVQAVLPMAQVPIGTALIWFVQMLGGALFTSVAQNIFSTHLAENLANLQLPGLDPEAIVGAGATGFRQLVQPEYMDQVLVAYNAALLDVFQVALICSCLSILGAVGIEWRSVKQNR | 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 | MASNTVYTSLIGLLVALTVRSIYRVYFHPLRKIPGPKIAAITHLYQHYYDAVKGGKYIWKLDELHRKYGPIVRFNPNEVHIQDSHYYHHIYAGGAKKQDKDPGFPAVPLFPGVTVTTIKHNHHRLRRGIIKSFFSKQYVTGLEHVIQSKVNLLASRFTEAYRHGTVLDLKYVFAALTSDLTTHYVYGTNLNHLAEPDFKNDFLAGMDSVGPWIPVLLVFGRLLKLARYLPACLVPAGEFLHLWTLSERRVGEILDSQDNGTMGDQKTLLQAMATADVSEEEKTATRLQMETLNIIAGGTETTARALAVGVFHLAHKPSLLLQLRDELRTVMPFPDSSASWTQLEQLPYLAGVVNESLRLSFGFIIRSARVYPNDPLVYEDLVIPPGTPISQSAYFVCMDPSIFPQPEDFNPDRWVQAAREGNNLHRYLIVFSKGSRHCLGINFALAEIYLAIATIARRFDLVPYQTTVEQLQMKRDLGFAAPEKGPFTVRAKVTGLAD | 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), aflatoxin B2 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2) . Within the aflatoxin pathway, the cytochrome P450 monooxygenase aflU is involved in the last steps in which OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2 . The biosynthesis of aflatoxins begins with the norsolorinic acid synthase aflC that combines a hexanoyl starter unit produced by the fatty acid synthase aflA/aflB and 7 malonyl-CoA extender units to synthesize the precursor NOR. The second step is the conversion of NOR to averantin and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN. The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway. The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen. Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2. Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring-opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring. The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O-methylsterigmatocystin (DHOMST), respectively. Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 56064
Sequence Length: 498
Pathway: Mycotoxin biosynthesis; aflatoxin biosynthesis.
Subcellular Location: Membrane
EC: 1.-.-.-
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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 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2) . Within the aflatoxin pathway, the oxidoreductase aflX seems to be involved in the conversion of versicolorin A (VERA) to demethylsterigmatocystin (DMST), through probable epoxide ring-opening step following versicolorin A oxidation required for the formation of the xanthone ring . The biosynthesis of aflatoxins begins with the norsolorinic acid synthase aflC that combines a hexanoyl starter unit produced by the fatty acid synthase aflA/aflB and 7 malonyl-CoA extender units to synthesize the precursor NOR. The second step is the conversion of NOR to averantin and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN. The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway. The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen. Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2. Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring-opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring. The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O-methylsterigmatocystin (DHOMST), respectively. Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 .
Sequence Mass (Da): 29374
Sequence Length: 266
Pathway: Mycotoxin biosynthesis; aflatoxin biosynthesis.
EC: 1.-.-.-
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Q6UEF1 | MGSHAPAVAGKPDPKKGPYQATPWNIQLSATDTPGFTHVGNLERRSADRASDLVMNNHSKFHTFHDEIVGFHNHISHHVLTLWALGATPDEMQAAYDFNKPFQLLTYYNDPSVNIKLRDPEFFRQGLGNFELYGDYVRFFQAEVAAKGTQTVLHDYLFKGDTLTEDLLARLFSGFLHPLINLGFALEFQQPFLAAECLASTCMHPPYPAEFLTATEQHVECNGRPRSLPILSIAEGMRLDPVVATAVGPEDGNNRIADALLKRALKELIPHLSYFQVEPTEHDLARKTAEILQASAYICGAAQHPRKVEALDFVMLHSLTAAVFFPTIIKQEWISIETRARLLEWKGRSDLITYAALGCPKLYPDRITGYQPKQAATGWSDVVQRARVYQDDGHACKVIRALMCAENVCQPFEGEEGFPLKKADFLTVAHMTMDSVERMSDPNWVRQTEKVKQMSAQGRGQHSQVSAIMLRWVRWCGTEGAWDDFPDLEELSPSA | 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 (AFB2), aflatoxin G1 (AFG1) and aflatoxin G2 (AFG2) . Within the aflatoxin pathway, the oxidoreductase aflY seems to be involved in the conversion of versicolorin A (VERA) to demethylsterigmatocystin (DMST), through probable Baeyer-Villiger oxidation required for the formation of the xanthone ring . The biosynthesis of aflatoxins begins with the norsolorinic acid synthase aflC that combines a hexanoyl starter unit produced by the fatty acid synthase aflA/aflB and 7 malonyl-CoA extender units to synthesize the precursor NOR. The second step is the conversion of NOR to averantin and requires the norsolorinic acid ketoreductase aflD, which catalyzes the dehydration of norsolorinic acid to form (1'S)-averantin. The norsolorinic acid reductases aflE and aflF may also play a role in the conversion of NOR to AVN. The cytochrome P450 monooxygenase aflG then catalyzes the hydroxylation of AVN to 5'hydroxyaverantin (HAVN). The next step is performed by the 5'-hydroxyaverantin dehydrogenase aflH that transforms HAVN to 5'-oxoaverantin (OAVN) which is further converted to averufin (AVF) by aflK that plays a dual role in the pathway, as a 5'-oxoaverantin cyclase that mediates conversion of 5'-oxoaverantin, as well as a versicolorin B synthase in a later step in the pathway. The averufin oxidase aflI catalyzes the conversion of AVF to versiconal hemiacetal acetate (VHA). VHA is then the substrate for the versiconal hemiacetal acetate esterase aflJ to yield versiconal (VAL). Versicolorin B synthase aflK then converts VAL to versicolorin B (VERB) by closing the bisfuran ring of aflatoxin which is required for DNA-binding, thus giving to aflatoxin its activity as a mutagen. Then, the activity of the versicolorin B desaturase aflL leads to versicolorin A (VERA). A branch point starts from VERB since it can also be converted to dihydrodemethylsterigmatocystin (DMDHST), probably also by aflL, VERA being a precursor for aflatoxins B1 and G1, and DMDHST for aflatoxins B2 and G2. Next, the versicolorin reductase aflM and the cytochrome P450 monooxygenase aflN are involved in conversion of VERA to demethylsterigmatocystin (DMST). AflX and aflY seem also involved in this step, through probable aflX-mediated epoxide ring-opening step following versicolorin A oxidation and aflY-mediated Baeyer-Villiger oxidation required for the formation of the xanthone ring. The methyltransferase aflO then leads to the modification of DMST to sterigmatocystin (ST), and of DMDHST to dihydrosterigmatocystin (DHST). Both ST and DHST are then substrates of the O-methyltransferase aflP to yield O-methylsterigmatocystin (OMST) and dihydro-O-methylsterigmatocystin (DHOMST), respectively. Finally OMST is converted to aflatoxins B1 and G1, and DHOMST to aflatoxins B2 and G2, via the action of several enzymes including O-methylsterigmatocystin oxidoreductase aflQ, the cytochrome P450 monooxygenase aflU, but also the NADH-dependent flavin oxidoreductase nadA which is specifically required for the synthesis of AFG1 .
Sequence Mass (Da): 55555
Sequence Length: 495
Pathway: Mycotoxin biosynthesis; aflatoxin biosynthesis.
EC: 1.-.-.-
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Q5BEJ9 | MAETDSSHTRGPVDSIQKNDASSDDAEAETKIQYPSGWRVTMILTSVTLAYFLFFLDLAVLSTATPAITSQFDSLVDVGWYGGAYQLGSAAFQPLTGKIYSQFSIKQWTFLVFFIVFELGSVLCAAARNSPMFIVGRVIAGVGSAGMSNGAVTTISAVLPTQKQALFMGLNMGMGQLGLATGPIIGGAFTTNVSWREDAPADDDAGFYINLPLGAVVGGFLLFNTIPEPKPKAPPLQILGTAIRSLDLPGFMLICPAVVMFLLGLQFGGNEHPWDSSVVIGLIVGGGATFGVFLVHQWWRGDEAMVPFALLKHKVIWSAAMTMFFSLSSVLVADFYIAIYFQAIRDDSPLMSGGAISAVGYGLLSTLSPTTSVAKWVGYQILYGVASGCTTAAPYVAIQNLVPAPQIPQAMAIIIFWQNIGAAISLIAANAIFSNSLRDQLAQRASQITVSPGAIVAAGVRSIRDLVSGSALAAVLEAYAEAIDRVMYLGIAVSVMVIVFSPGLGWKDIRKTKDLQALTSDGAQGEATEKETVPVALG | 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 | MADHEQEQEPLSIAIIGGGIIGLMTALGLLHRNIGKVTIYERASAWPDIGAAFAFTGIARECMQRLDPAILSALSKVAQRNPHDKVRYWDGFHPKSKEEAQDPEKSVLFEIEEKNMAYWACLRGVFHAEMARLLPERVVRFGKRLVAYEDGGDQKVVLRFEDGEVEEADIVIACDGVHSTARRVLLGAEHPAANARYSRKAVYRALVPMPAAIDALGTEKAHVQIAHCGPDAHIVSFPVNNAQIYNVFLFTHDSNEWTHGHTMTVPSSKEEILSAVENWGPHIKELASLFPEQLSKYAIFDQADHPLPYYAAGRVALAGDAAHASSPFHGAGACMGVEDALVLAELLEKVQNGSAFKEKKSNIELALKTYSDVRIERSQWLVKSSREMGDLYEWRYEDIGGDGVKCKAEWERRSRVIWDFDVQGMVDQAREAYERAVVKV | 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-dimethyloctadienone moiety is then loaded onto the SAT domain of afoE and extended with four malonyl-CoA and one SAM, which leads to the formation of 2,4-dihydroxy-6-(5,7-dimethyl-2-oxo-trans-3-trans-5-nonadienyl)-3-methylbenzaldehyde (compound 2) after reductive release and aldol condensation . AfoD is the next enzyme in the biosynthesis sequence and hydroxylates the side chain at the benzylic position of compound 2 . After benzylic hydroxylation, a furan ring is formed after five-member ring hemiacetal formation and water elimination . AfoF and afoC are proposed to oxidize the R-diketone proton and to reduce the unconjugated carbonyl group, respectively, to generate asperfuranone . Since no intermediates could be isolated from afoF and afoC deletants, the sequence of these two enzymes is not fully understood . Moreover, since afoC deletant still produces a small amount of asperfuranone, other endogenous oxidoreductases might catalyze the same reaction with much less efficiency .
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 49022
Sequence Length: 440
Subcellular Location: Membrane
EC: 1.-.-.-
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Q9FT97 | MSRRAMVIKMPILMILISSMVMTMVESSRSVNNGHDDSEILRRHLLTNGLGVTPPMGWNSWNHFSCNIDEKMIKETADALVTTGLSKLGYNYVNIDDCWAEISRDSKGSLVPKKSTFPSGIKAVADYVHSKGLKLGIYSDAGYFTCSKTMPGSLGYEEHDAKTFAEWGIDYLKYDNCNSDGSKPTVRYPVMTRALMKSGRPIFHSLCEWGDMHPALWGSPVGNSWRTTNDIKDTWLSMISIADMNEVYAEHARPGGWNDPDMLEVGNGGMTKDEYIVHFSIWAISKAPLLLGCDIRNMTKETMEIVANKEVIAINQDPHGVQAKKVRMEGDLEVWAGPLSGYRVALLLLNRGPSRTSITALWEDIEIPANSIVEARDLWEHQTLKQKFVGNLTATVDSHACKLYVLKPVA | 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 Mass (Da): 45709
Sequence Length: 410
Subcellular Location: Secreted
EC: 3.2.1.22
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Q8RX86 | MVLLSFSLRFIAFTLTITLTQIADGFQSRMLMNNGLALSPQMGWNSWNHFQCNINETLIKQTADAMVSSGLSAIGYKYINIDDCWGELKRDSQGSLVAKASTFPSGIKALSDYVHSKGLKLGIYSDAGTLTCSQTMPGSLGHEEQDAKTFASWGIDYLKYDNCENTGTSPRERYPKMSKALLNSGRSIFFSLCEWGQEDPATWAGDIGNSWRTTGDIQDNWKSMTLIADQNDRWASYARPGSWNDPDMLEVGNGGMTKEEYMSHFSIWALAKAPLLIGCDLRSMDKVTFELLSNKEVIAVNQDKLGIQGKKVKKEGDLEVWAGPLSKKRVAVILWNRGSASANITARWAEIGLNSSDIVNARDLWEHSTYSCVKKQLSALVEPHACKMYTLTRRKA | 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 Mass (Da): 44037
Sequence Length: 396
Subcellular Location: Secreted
EC: 3.2.1.22
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P43469 | MPVEYDPKTGLINLHNDQISYVIQILAHRYPVHRYFGRYFSKQPYFEPMPSGSHAFANDPTERFPYSVTSLPLEYSTIGSGDYRQPAYVIKDANNQLLPILEYTGFSVNDQPINSRQLPPTVSKHTPVTTLVIHLTDAVTKLQMDLNYTIFENQPLILRSTTLRHHGTTNLQVTALSSAQLDLPTDQYTALTLSGTHAHEANPSFNRLHPGLQTVRSLRGTSGPQHQPFMALAEPNTTELAGTVIGCALAWSGNFDSTVEVDQYQHSRLTIGLEPDTFEWQLKPNSSFQTPEAVLTWTNTGFNGMSQVFHDFSYQLMPSQTNIPSVLNTWETLTFAVSESKVQHLIEHAHQLGLQMLVLDDGWFVNRNGENGQLGDWFVDPIKFPNGLNPLAQQAHHHRMKFGLWVEPEMITTNSQLYQQHPDWVLQYVDRTPITARHQLVLDLSQAAVRDHLITTLTNLVQNNQLDYLKWDMNRHLTQVGSTHLPAAQQGELYHRYVCGLYDILTRLKRACPKLIIENCSAGGGRFDFGMLPYTNQTWISDLTDPVDRATIENGFSYLFPPRIFSNHITASPNAQNGRITPFETRLQLACIGQLGLELNPKQLAPSEQQLLRGALIKYQQLKSTFIKAHFYRLPTTRHVVAWLIVTADKKQAICCYLNGLNSRVKTQHPLPLHYLDAELAYSDSSGNRYTGHQLNTMGIPLKPTNADFTSQLIYLCQN | 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 | MVIMKKMKDSVLFLVVGLFSLSVLVSQSIAGRVKAPLLQSNTGGLVFSKSFNSIYDTSMYGRLQLNNGLARTPQMGWNSWNFFACNINETVIKETADALVSSGLADLGYIHVNIDDCWSNLLRDSEGQLVPHPETFPSGIKLLADYVHSKGLKLGIYSDAGVFTCEVHPGSLFHEVDDADIFASWGVDYLKYDNCFNLGIKPIERYPPMRDALNATGRSIFYSLCEWGVDDPALWAKEVGNSWRTTDDINDTWASMTTIADLNNKWAAYAGPGGWNDPDMLEIGNGGMTYEEYRGHFSIWALMKAPLLIGCDVRNMTAETLEILSNKEIIAVNQDPLGVQGRKIQANGENDCQQVWSGPLSGDRMVVALWNRCSEPATITASWDMIGLESTISVSVRDLWQHKDVTENTSGSFEAQVDAHDCHMYVLTPQTVSHSDV | 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 Mass (Da): 48363
Sequence Length: 437
Subcellular Location: Secreted
EC: 3.2.1.22
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Q92451 | MSPSAAVLIPLAAAVLLRPVVGQTQCGGNLYTPGTLNFTLECYNAFQDCVAQFEANASQVDCNDGKGNLFMQQQANLGASPGSQNNDAIIAFQDIRDLCLLSGSTTATWGYSDNQWYWAAAEDACYTNDPTRTDVVKTHPAPFCIQNRDSSLPECYPQPDATPPGGPLKVIKTAKTRNGFKSSARGWNTYGVQALVNGSQVVPSFAGQSGLFYTQKFVETQCGVLARPEFKKAGYDLCSLDSGWQATTAVDQHGRIIYNTTRFNLPELASWLHKRDLKLGVYITPGVPCLAHNQTILGTNIKIKDVLNGNNDQINCDFDFRKDGVQQWHDSVVAQWASWGVDMLKLDFLTPGSPSNGANLACDSSDAVRAYQKAIKKSGRKIRLDISWKLCRNETWLPIWSDLAESMRTDQDLDNYGTNTLMAWQVGQRAIENYRQYIGLQAQRNVPLTIYPDMDALFTVNPEHLAGVNDTIRYTVQNHWLGAGANLIIGGDMEQVDALGLKLTTSKQSIDAADFFAKYPMQPRNPGTGSNAAKQLQAWIGGPSDDHEAYVLIVNYGPDLGNGGFSTKLYGKQKVTVSLKDLGISGSAWTFTDIWSGKSSRVTGSYSAWLTEGESQLLRLKRTH | 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, galactomannans and galactolipids.
Sequence Mass (Da): 68455
Sequence Length: 624
Subcellular Location: Secreted
EC: 3.2.1.22
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C8VJZ7 | MELEKFKPWRDSHSEHIPVPLTSRQNIIIILLILFSHYHHWYWRCRRPTDRWSLLAVCHKHHQRAPNSLPTSKSLHSFLHSARGWNSWGIQATPNTIPSYPKEELGRVLNQKFIISQCTMLTDPATQDAGYDLCSLDGGWYSSITDKFGCITYNASLFDISALSRYLHGKGLRMGLYSQPGTPCKARHGTNVTVGSAFIDHVDKNNNCYFDYENPNTQLYRELITLWVSWGVDMIKLDYVTPGSTFQDTCMPGNLNASAIAYHCAIEKSGRKFQLDVSSDVCRSQPYWGTWNSNADSIRVDTDINPYDSDDFFFFYMQHCTVEDYRQFVNLQVVDAQNDKPVTLRGNLDNLFVGNPAKVKGVTDKQRNTLMRIWIGASSNLFLGSDMRILDDLGRWLITSPSSIAAADFCAMYPMQPRNPGTGSNQAVQLQACITGPSEHGEAYVLLTNLGPNLGDGGYVTVGGGEQKMSVTLADMGPSRSSANRLDLSPRPIHVLILL | 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, galactomannans and galactolipids.
Sequence Mass (Da): 56049
Sequence Length: 499
Subcellular Location: Secreted
EC: 3.2.1.22
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Q4WVZ3 | MDTTKSLLSTLIAIMIPLSLGSVSSPNLLPTPPMGFNNWARFMCDLNETLFLETASAMISTGLLEAGYNRVNLDDCWMAYDRAADSSLQWNTTKFPHGIPWLARHLKAQGFHVGIYEDAGNLTCGGYPGSFGHEALDAQTFAAWGIDYLKLDGCNVFPEHSRTLEEEYKARYAHWHSILKQMHHPLIFSESAPAYFADPANLTSWYEVMDWVPAFGELARHSTDILVYVGEGSAWDSIMVNYRYNTLLARYQRPGYINDPDFLIPDHPGLTLEEKRSQFALWASFSAPLIVSAYIPGLSSEELAILRNEELIRVDQDVLGLQATLASRGLEVDVLTRSLEGGDRLLTVLNRGDGVAVVSVPVEWMGLQRGCPYVVKNLWDGEVQVLEEEIVIRLNSHATQVYRIALPDECSTVIPTGIVFNTASGNCLTDENGERVGFEACRGSETQIWQVSELGYLRPLSRTSHCLTGGSQASVQLCTEQKNQQWAYAITGILKNEHTEMCLTEGTGISQCGFERDSQVFGLPSGVDIKPS | 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.
Sequence Mass (Da): 58991
Sequence Length: 532
Subcellular Location: Secreted
EC: 3.2.1.22
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P28351 | MIQGLESIMNQGTKRILLAATLAATPWQVYGSIEQPSLLPTPPMGFNNWARFMCDLNETLFTETADTMAANGLRDAGYNRINLDDCWMAYQRSDNGSLQWNTTKFPHGLPWLAKYVKAKGFHFGIYEDSGNMTCGGYPGSYNHEEQDANTFASWGIDYLKLDGCNVYATQGRTLEEEYKQRYGHWHQVLSKMQHPLIFSESAPAYFAGTDNNTDWYTVMDWVPIYGELARHSTDILVYSGAGSAWDSIMNNYNYNTLLARYQRPGYFNDPDFLIPDHPGLTADEKRSHFALWASFSAPLIISAYIPALSKDEIAFLTNEALIAVNQDPLAQQATLASRDDTLDILTRSLANGDRLLTVLNKGNTTVTRDIPVQWLGLTETDCTYTAEDLWDGKTQKISDHIKIELASHATAVFRLSLPQGCSSVVPTGLVFNTASGNCLTAASNSSVAFQSCNGETSQIWQVTPSGVIRPVSQTTQCLAADGNLVKLQACDSTDSDGQKWTYPVTGNLKNAKTDGCLTEGSVQMKSCLYERDGQVFGLPSGVQLA | 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-D-galactosides, including galactose oligosaccharides, galactomannans and galactolipids.
Sequence Mass (Da): 60148
Sequence Length: 545
Subcellular Location: Secreted
EC: 3.2.1.22
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Q2UT06 | MRLITRWIPLANALASTMPVQVVASIENPSLLPTPPMGFNNWARFMCDLNETLFVETTDAMASNGLLEAGYNRINLDDCWMNYDRAENGSLEWNVTKFPRGLPWLGQYVKSKGFNFGIYEDSGNLTCGGYPGSEGYEEIDAEIFAAWGIDYLKLDGCNVYPKEGRTLQEEYKYLYGNWHEILSKMQQPLIFSESAPAYFSMTDNLTDWHTVMDWVPEYGELARHSVDILVYSGEGSAWDSIMTNYKFNTLVARYQRPGYYNDPDFLIADHPGLSLDEKRSQFALWASFSAPLIISAHIPDLSSEDLEYLTNQALIAVDQDPLAQQATLASRDGSLDVLTRNLADGSRLVTILNHGSESIETDISLDILGLSTDCTYKAQDLWGGSTQTIKDAIRIKLNTHATAVYKIDTDEKCSQVIPTGLIFNTASGKCLTGTSSSVGSESCNGSKSQIWQIDASGVIRTLSEQSKCLTADGKAISLQECSENNGQKWSYAITGNLKNADTGYCLTNGGGVSACGFETNSQVFGLPAGVHVAL | 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.
Sequence Mass (Da): 58739
Sequence Length: 534
Subcellular Location: Secreted
EC: 3.2.1.22
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A1C5D3 | MSRFHLPLAAAVVLVSCLWSANALVRPDGVGKLPALGWNSWNAFGCDIDDAKIMTAAKEIVNLGLKDLGYEYINIDDCWSVKSGRDKTTKRIVPDPAKFPDGIAGVADRIHDLGLKVGIYSSAGLTTCAGYPASLGYEEIDAQTFAEWGIDYLKYDNCGVPSNWTDAYTFCVPDPGSASTNGTCPDNENPAPQGYDWSTSLTAQRHQRMRDALLGVEHTIFYSLCEWGQADVSAWGNATGNSWRMSGDITPSWDRIAAIANENSFLLNHVDFWGHSDPDMLEVGNGDLTLAENRAHFALWAAMKSPLIIGTALDGIDPAHLEILLNKYLIAFHQDPVIGRPAYPYKWGYSPDWTFDPAHPAEYWSGPSSTLDGTLVLMLNSEGSRQTRTAVWKEIPELKDALGRKGRRQTGFRVTDVWTGKDLGCVRDHYTVTLESHDVAALLVGKGC | 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.
Sequence Mass (Da): 49135
Sequence Length: 448
Subcellular Location: Secreted
EC: 3.2.1.22
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Q4WE86 | MTTFFSLTTAAAVLTLARGSNALVRPGNVGKLPALGWNTWNAFGCDIDATKIMTAANEVVNLGLKDLGYEYINIDDCWSVKSGRDASTQRIIPDPDKFPDGISGVADQIHDLGLKIGIYSSAGLTTCAGYPASLGYEDIDAQTFAEWGIDYLKYDNCGVPSNWTDTYTYCVPDPGSKATNGTCPDNKNPAPAGYDWRTSLTAERYRRMRDALVSVDRTILYSLCEWGQANVNDWGNETGNSWRTTGDITPSWPRIAAIANENSFLMNHVDFWGYPDPDMLEVGNGNLTLAENRAHFALWAAMKSPLIIGTALDSISQDHLAILSNKILLKFHQDPVIGRPAQPYKWGYNPDWTFDPAHPAEYWSGASSVLGGTLVLMLNSEDTTQRRTAVWKEVPELKDVLGRQGKRRIGFRVTDVWTGKDLGCVRDHYSVELESHDVAALVVGRAC | 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.
Sequence Mass (Da): 49202
Sequence Length: 447
Subcellular Location: Secreted
EC: 3.2.1.22
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D4GU68 | MDLARSSIKLFIANIFGAGLQFLGITFFARELGASQMGVFFLFQALLGIVAIPADFGLRGAVEKRISEGIQPGEYLSSAIILKLIPISLIILSIVVFEQRINGYLGGDFAVYLALAIILQETAQLAVSVLKGELRVGETAELNIIRRITWVGGGFLLVSSGLDAEALIYSLLAGMVVTLAWGLSKISTSLKKPSFKNARSLFNYSKYSVVSSIGGYFYSWMDVAIIGIFLTQSHVGAYETAWRVTAITMLFSQAVASTIFPQVSQWSSKNEQQQIESVISNSITPSMLLVIPAFFGILVFSDEIMGIVFGSEFTIASYVLIILAGEKILQSVHVIIGRSLQALNQPGLAARATVISVVLNLILNVILILSFGIVGAAVATALSFAVNTVLHAHYLSSFVSIKFQYSQIGWCTVSSLIMAGVLFGFKTLVGVNSLIQLFIGIFFGMLVYTTITLLYQPIRETAFKNLIRLVPI | 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 tetrasaccharide from the cytosolic to the extracytosolic side of the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51165
Sequence Length: 472
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Cell membrane
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Q4JAK2 | MYKVWMLTPLFLPVRGGTEVHVFNLSRELVKMSIDVEVHTTRDTYTEREKLIPFEIMDGIKVVRHKRTWIYRDSPSVLHFHNLGRKFSTWNLYTFLFFSLPSVEAPLVMTPHHIFVSDQGRVINWLKRNIGKRVDKLIAVSEWEKEEMINLGYDGSKIVVIPNGVDDMAFNYPKSEGFEDYLLYIGRISPEKNQLFAIECIKNLNVKLILIGQVRDKDYLEKIMTRVSELGLEDKVRYLGVVTEEEKYSLMDKSLAVILTSDIEAEGIVIKEAMVRGVPVIVGNKAKVLSTIVKDGVNGFVISSCQDLKDAVEKLRDPKVRKEIGENNISISREWRWRNVSLKVLELYKSLS | 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 floral meristem and regulates expression of class B, C and E genes. When associated with SOC1, mediates effect of gibberellins on flowering under short-day conditions, and regulates the expression of LEAFY (LFY), which links floral induction and floral development. Confers inflorescence characteristics to floral primordia and early flowering.
PTM: Phosphorylated by IMK3. Induced by vernalization.
Sequence Mass (Da): 25064
Sequence Length: 220
Subcellular Location: Nucleus
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Q4JBJ3 | MRILVLGIDGHLGWPLALRLAKRGHEVIGIDNLSTRRFSEEVGSDSAFPLPQPQERVSEAKKHLGVDITFYVGDITNYGFFKDIVQRYKPDAIVHFAEQRSAPYSMIDMDHAVYTVINNEVSTLRVIQAVLEVDPTIHILKMGTMGEYGTPAFDIPESIYVEAIVNGKKDKIIVPRKAGSVYHWTKVHDTDFLLHFQELYGLTVTDIMQGPVYGTRTEEIVEETLRTRFDFDEVWGTVVNRYCVEAILGLPLTVYGKGGQTRGFISLEDSIQALTLLLENPPKQGEYRVANQFAEIYSVKKIAEFVKKAGEELGLNVEIGSYENPRVEAEEHYYNPERKVLPSLGFYPKKRLPEDVKIMIKDLLPYKTRLERFKHVILPKTKWRKPQYVKRVR | 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-glucose is converted via UDP-4-keto-D-glucose to UDP-D-glucose-5,6-ene .
Catalytic Activity: H(+) + sulfite + UDP-alpha-D-glucose = H2O + UDP-alpha-D-6-sulfoquinovose
Sequence Mass (Da): 45016
Sequence Length: 393
EC: 3.13.1.1
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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'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Mass (Da): 31443
Sequence Length: 288
Domain: Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif).
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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'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Mass (Da): 28614
Sequence Length: 242
Domain: Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif).
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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'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Mass (Da): 30106
Sequence Length: 252
Domain: Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif).
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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'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Mass (Da): 26005
Sequence Length: 216
Domain: Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif).
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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'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Mass (Da): 27662
Sequence Length: 239
Domain: Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif).
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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'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Mass (Da): 29467
Sequence Length: 256
Domain: Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif).
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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'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Mass (Da): 28345
Sequence Length: 242
Domain: Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif).
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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'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2,3-dehydro-2,3-deoxyribose 5'-phosphate)-DNA + a 5'-end 5'-monophospho-2'-deoxyribonucleoside-DNA + H(+)
Sequence Mass (Da): 28191
Sequence Length: 239
Domain: Contains two alpha-helical subdomains, with the 8-oxoguanine binding site located in a cleft at their interface. Contains a helix-hairpin-helix (HhH) structural motif and a Gly/Pro-rich sequence followed by a conserved Asp (HhH-GPD motif).
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O67434 | MGKEALLNLYRIEYRPKDTTFTVFKPTHEIQKEKLNKVRWRVFLQTGLPTFRREDEFWCAGKVEKDTLYLTLSNGEIVELKRVGEEEFRGFQNERECQELFRDFLTKTKVKDKFISDFYKKFRDKITVQGKNRKIALIPEVNEKVLKSEEGYFLLHLDLKFRIQPFETLQTLLERNDFNPKRIRVKPIGIDFVGRVQDVFKAKEKGEEFFRLCMERSTHKSSKKAWEELLKNRELREKAFLVVLEKGYTYPATILKPVLTYENLEDEERNEVADIVRMEPGKRLNLIRYILRRYVKALRDYGWYISPEEERAKGKLNFKDTVLDAKGKNTKVITNLRKFLELCRPFVKKDVLSVEIISVSVYKKLEWRKEEFLKELINFLKNKGIKLKIKGKSLILAQTREEAKEKLIPVINKIKDVDLVIVFLEEYPKVDPYKSFLLYDFVKRELLKKMIPSQVILNRTLKNENLKFVLLNVAEQVLAKTGNIPYKLKEIEGKVDAFVGIDISRITRDGKTVNAVAFTKIFNSKGELVRYYLTSYPAFGEKLTEKAIGDVFSLLEKLGFKKGSKIVVHRDGRLYRDEVAAFKKYGELYGYSLELLEIIKRNNPRFFSNEKFIKGYFYKLSEDSVILATYNQVYEGTHQPIKVRKVYGELPVEVLCSQILSLTLMNYSSFQPIKLPATVHYSDKITKLMLRGIEPIKKEGDIMYWL | 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. Uses short ssDNA sequences as guides (gDNA) to bind complementary target strands, resulting in cleavage of the target RNA. The cleavage site is 10 nucleotides downstream of the residue base paired with the 5'-end of the gDNA . Binds ssDNA better than ssRNA, binds dsDNA and DNA-RNA hybrids but does not bind dsRNA . A 2 nucleotide 3'-overhang (possibly on the guide strand) may help load nucleic acids into the complex (Probable).
Sequence Mass (Da): 83122
Sequence Length: 706
Domain: Has 4 domains; N-terminal, PAZ, Mid and PIWI. The N-terminal and PAZ domain are joined by linker 1, the PAZ and Mid domain are joined by linker 2. The domains assemble in 2 lobes; the PAZ lobe consists of the N-terminal, L1, PAZ and L2 domains, while the PIWI lobe has the Mid and PIWI domains. The PIWI box is exposed on the surface of the protein. The PIWI domain assumes an RNase H fold and has the catalytic residues . The N-terminal and PAZ domains are relatively mobile and move further apart when in complex with RNA .
EC: 3.1.26.-
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A4WYU7 | MAPVQAADEMYDSNPHPDRRQLVSNGFEVNLPDQVEVIVRDLPDPSKVKEERTRLMGYWFVHWFDGKLFHLRIKAGGPNVDGEHRAIRTAEHPWLLRARLDDALEEALPKYAAVKKRPFTFLAQKDELIDAAATAAGLSHRLLNSFKVIPRFALSPKIYEPVDGTTRVGVFVTIGMRYDIEASLRDLLEAGIDLRGMYVVRRKRQPGERGLLGRVRAISDDMVQLFEETDLASVNVNDAKLEGSKENFTRCLSALLGHNYKKLLNALDDQEAGYRTGPRFDDAVRRMGEFLAKKPIRLADNINAQVGDRIVFSNEGQARNVRLAPKVEYVFDRTGAKSAEYAWRGLSQFGPFDRPSFANRSPRILVVYPSSTQGKVENFLSAFRDGMGSNYSGFSKGFVDLMGLTKVEFVMCPVEVSSADRNGAHTKYNSAIEDKLAGAGEVHAGIVVLFEDHARLPDDRNPYIHTKSLLLTLGVPTQQVRMPTVLLEPKSLQYTLQNFSIATYAKLNGTPWTVNHDKAINDELVVGMGLAELSGSRTEKRQRFVGITTVFAGDGSYLLGNVSKECEYEGYSDAIRESMTGILRELKKRNNWRPGDTVRVVFHAHRPLKRVDVASIVFECTREIGSDQNIQMAFVTVSHDHPFVLIDRSERGLEAYKGSTARKGVFAPPRGAISRVGRLTRLLAVNSPQLIKRANTPLPTPLLVSLHPDSTFKDVDYLAEQALKFTSLSWRSTLPAATPVTIFYSERIAELLGRLKSIPNWSSANLNIKLKWSRWFL | 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 with 5'-phospho-U and poor affinity for gRNA with 5'-OH . Upon expression in E.coli, plasmid sequences are found in RsAgo, its induction leads to plasmid degradation and suppression of genes encoded on foreign plasmids, suggesting it may also interfere with transcription . Does not interact with preformed gRNA:tDNA duplexes. Mismatches and nt bulges are tolerated in the ternary complex, however, they significantly reduce the affinity of RsAgo:gRNA for tDNA. Mismatched tDNA can cause dissociation of gRNA from RsAgo . In situ binds 2 populations of RNA (15-19 and 45 nucleotides, nt) and a population of ssDNA 22-24 nt in length. The small sense RNA is probably derived from mRNA degradation and strongly enriched for U in the first and U/C in the second positions. The small DNA is enriched for sequences complementary to the RNA, with 3 nt overhangs on both ends; another nuclease may trim the ends. The sequences are largely derived from exogenous plasmids or genome-encoded foreign elements such as prophages and transposons . Forms a ternary complex with gRNA and double-stranded tDNA only when the tDNA is open .
Sequence Mass (Da): 87090
Sequence Length: 777
Domain: Has 4 domains (N-terminal, PAZ, Mid and PIWI). The N-terminal and PAZ domains are joined by linker L1, the PAZ and Mid domains are joined by linker L2. The domains assemble in 2 lobes; the PAZ lobe consists of the N-terminal, L1, PAZ and L2 domains, while the PIWI lobe has the Mid and PIWI domains. The PIWI domain assumes an RNase H fold but in this bacteria does not have catalytic activities. The gRNA:tDNA duplex lies between the 2 lobes. The 5'-phosphate and first base of the gRNA bind in the Mid domain, the middle of the gRNA binds to the PAZ domain, while the 3'-region of the gRNA strand base-pairs with the 5'-region of the tDNA strand but not to the PAZ domain. The 5'-region of the tDNA strand binds to RsAgo N-terminal domain in the heteroduplex.
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C6LTG5 | MTTDIVTSRINFYPYTVLPSAKPVYQYDLSIQVSTQGYNLDNADSYRALEKFCEQQDTALGNDPARSLFYSLIVDFPSSDSRPISSFYSQTDLGSRPVTHTVEFLSTQKPKRRGGRAGGMRGNRGGPSTTSVQALVKVTRVRQMDPLDLMSMKTLLNILLRRTFESSLGMLNIRSGFYDLNRTSTHNIQVDGRGFDICWIPGFRLTTATLYGKLGLQVLPETTKVRSKSMCELLNENRGSLHPNALAAITVMAMHNGRVFRIHSIVRGQSVVSPLAEGSDTDYFTYYSAKYKDKIDSAALSLLKQDDYCNSVLQRDKFILKLTPLKKTHNGKVVRSCNVPSSLCIIISDNEIAPYGVSKLSTNKTAVALSTMSPDALLEKATEFANQLIDNAELQSVLGDYGFRFTSQPLELDTFVCKPPKLMMDTLSRELTVEDDSGGVFRSLIQSPGVSSIYYANNGQPAVGMPHWALMVPRYLKNDYARRLKQELTQRIRSLAGATASTVEEPLLIAVDVNEQRRDMYRIEPYKDAFESLLVKLNTQYPDTKNSELISRIQLVVVVIPGPKQYSGGLYKEVKRFYTDKGIVTQCLLTPRLSRDGPEWYDQAILNGLCQQIYAKAGGAVWAPALPKDNAYSTSTMLCALDVSRPKKTVGRPTEVPASTAGFISTYEGSFEYIYSQKKNLMPNRLNQGGEVQQQTLMKTFIKNSCEVYSAFNSSLPDRIVIFRDGVSDGQISTVLETEINSLYEYLCQRYREANRPMCDLKVIVAQKTCAMRLAAVSNTDLRPGFYILNHSPDNKQKGSEFIMASQAIVHGTTPKPIRYKLIFDSTEASMDNSSFKQLIELTNTMAYGYVNWPQAISLPHILHMAHLLSKFCGEILGNGRDLLESQAIFGLQYRPFFI | 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 transcribed but only transcripts encoding the VSP to be expressed accumulate. Antisense RNAs corresponding to the silenced VSP genes are detected (By similarity).
Sequence Mass (Da): 100571
Sequence Length: 899
Domain: PAZ domain is absent, but Ago is capable of binding small RNAs in the same way as the other Argonaute proteins.
Subcellular Location: Cytoplasm
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A0A1M5A5Z8 | MYLNLYEIKIPYRVKRLYYFNKENDPKEFARNLSRVNNIRFNDSKDLVWLEIPDIDFKITPQQAEKYKIEKNEIIGEKEDSDLFVKTIYRYIKKKFIDNNFYYKRGNNYISINDKFPLDSNTNVNAHLTYKIKLYKINERYYISVLPKFTFLSDKPALESPIKSTYLFNIKSGKTFPYISGLNGVLKIDLGENGIKEVLFPENYYFNFTSKEAEKFGFSKEIHNIYKEKIFSGYKKIKQSLYFLEDIININNYNLTMDKKIYVNIEYEFKKGISRNIKDVFKYSFYKNDQKIKIAFFFSSKKQIYEIQRSLKMLFQNKNSIFYQTIYEMGFSKVIFLREPKTNSSAFMYNPETFEISNKDFFENLEGNIMAIIILDKFLGNIDSLIQKFPENLILQPILKEKLEKIQPYIIKSYVYKMGNFIPECQPYVIRNLKDKNKTLYIGIDLSHDNYLKKSNLAISAVNNFGDIIYLNKYKNLELNEKMNLDIVEKEYIQILNEYYERNKNYPENIIVLRDGRYLEDIEIIKNILNIENIKYSLIEVNKSVNINSCEDLKEWIIKLSDNNFIYYPKTYFNQKGVEIKIIENNTDYNNEKILEQVYSLTRVVHPTPYVNYRLPYPLQVVNKVALTELEWKLYIPYMK | 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 (tDNA) in all possible combinations; has no detectable activity in the absence of guide. Uses short guide sequences (18-21 nucleotides (nt) on average) to bind complementary target nucleic acids resulting in target cleavage in a site-specific manner. Using 5'-phospho-gRNA or 5'-OH-gRNA the cleavage site is 10 nt downstream of the target residue base-paired with the 5'-end of the gRNA, using 5'-phospho-gDNA the cleavage site is 11 nucleotides (nt) downstream, while with 5'-OH-gDNA the cleavage site is 9 nt downstream.
Sequence Mass (Da): 76715
Sequence Length: 640
Domain: Has 4 domains (N-terminal, PAZ, Mid and PIWI). The N-terminal and PAZ domains are joined by linker L1, the PAZ and Mid domains are joined by linker L2. The domains assemble in 2 lobes; the PAZ lobe consists of the N-terminal, L1, PAZ and L2 domains, while the PIWI lobe has the Mid and PIWI domains. The PIWI domain assumes an RNase H fold and has the catalytic residues. gDNA lies between the 2 lobes, with its unpaired 5'-end anchored in the Mid lobe.
EC: 3.1.24.-
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H2J4R4 | MYLNLYKIDIPKKIKRLYFYNPDMEPKLFARNLSRVNNFKFQDSNDLVWIEIPDIDFQITPKNVFQYKVEKEEIIKEEEDKKLFVKTLYKYIKKLFLDNDFYFKKGNNFISNSEVFSLDSNENVNAHLTYKIKIHNISNEYYLSILPKFTFLSKEPALESAIKSGYLYNIKSGKSFPYISGLDGILKIDIGNNQIVEVAYPENYLFNFTTRDAEKYGFSKEVHEIYKNKVFEGFKKIPKTLGFLNKITNLNENYQLKDGYKIFINVIYKFKNGESRYAKDVFKYSFYKNEQPLKAIFFFSSKKQFFEVQKSLKELFHNKHSVFYRAAAELGFSKVEFLRDSKTKSSAFLYNPEEFTVKNTEFINQIEDNVMAIVLLDKYIGNIDPLVRNFPDNLILQPILKEKLEDIKPFIIKSYVYKMGNFIPECKPFILKKMEDKEKNLYIGIDLSHDTYARKTNLCIAAVDNTGDILYIGKHKNLELNEKMNLDILEKEYIKAFEKYIEKFNVSPENVFILRDGRFIEDIEIIKNFISYNDTKYTLVEVNKNTNINSYDDLKEWIIKLDENTYIYYPKTFLNQKGVEVKILENNTDYTIEEIIEQIYLLTRVAHSTPYTNYKLPYPLHIANKVALTDYEWKLYIPY | 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 (tDNA) or target RNA resulting in target cleavage. The cleavage site is 10 nucleotides (nt) downstream of the target residue base-paired with the 5'-end of the gRNA. Reaction rates are fastest on 5'-OH-gRNA:tDNA followed by 5'-OH-gRNA:target RNA. gRNA between 17-21 nt supports equivalent rates of cleavage, has no preferred 5'-nt. Has weak activity on tDNA with 5'-phospho-gRNA, yielding products 1-2 nt longer . Unlike other characterized prokaryotic Ago proteins symmetric mismatches centered around the cleavage site reduce cleavage efficiency .
Sequence Mass (Da): 75906
Sequence Length: 639
Domain: Has 4 domains (N-terminal, PAZ, Mid and PIWI). The N-terminal and PAZ domains are joined by linker L1, the PAZ and Mid domains are joined by linker L2. The domains assemble in 2 lobes; the PAZ lobe consists of the N-terminal, L1, PAZ and L2 domains, while the PIWI lobe has the Mid and PIWI domains. The PIWI domain assumes an RNase H fold and has the catalytic residues. Compared to orthologs, the N-terminal domain has a different secondary structure and position. The 5'-end of the gRNA is anchored between the MID and PIWI domains while the 3'-end is in the PAZ domain . In the gRNA:tDNA complex the 5'-end of gRNA remains anchored in the Mid domain and is unpaired with tDNA, while the 3'-end of the gRNA is released from the PAZ domain. Upon release of the 3'-end of the gRNA from the PAZ domain during nucleic acid duplex formation, conformational changes allow Glu-482 to move to complete the active site. An N-lobe rearrangement allows a unique, straight orientation of the hybrid helix not seen in other Ago ternary complexes .
Subcellular Location: Cytoplasm
EC: 3.1.24.-
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Q58717 | MVLNKVTYKINAYKIKEEFIPKEVHFYRIKSFVNEAFNFYRFVNFYGGMIINKKDKSFVLPYKVDNKVLKYKDGNNEIPIDIEYIKSLKLEYVKPEIAEKLVRGYLKSVHKIEPELSRIIKNIRKHKVVENIKVESYCEYEVKKHDGDYYLILNFRHTASITKHLWDFVNRDKALLEEYVGKKIIFKPNPKVRYTISLVDAPNPQKIEEIMSHIIKYYKWSEDMVKSTFGEIDYNQPIMYCEEILEPFAPQFCNLVFYMDELDSYILKELQSYWRLSNENKGKIINEIAKKLRFIDNTPKELEFMKFNNTPLLVKDVNKNPTKIYSTNTLFTWIYNQNAKIYLPYDVPEIIRNKNLLTYILIDEEIKDELKAIKDKVNKMFRNYNKIANKTELPKFNYANRWKYFSTDDIRGIIKEIKSEFNDEICFALIIGKEKYKDNDYYEILKKQLFDLKIISQNILWENWRKDDKGYMTNNLLIQIMGKLGIKYFILDSKTPYDYIMGLDTGLGIFGNHRVGGCTVVYDSEGKIRRIQPIETPAPGERLHLPYVIEYLENKANIDMENKNILFLRDGFIQNSERNDLKEISKELNSNIEVISIRKNNKYKVFTSDYRIGSVFGNDGIFLPHKTPFGSNPVKLSTWLRFNCGNEEGLKINESIMQLLYDLTKMNYSALYGEGRYLRIPAPIHYADKFVKALGKNWKIDEELLKHGFLYFI | 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 target DNA (tDNA) . Endonucleolytically cleaves tDNA (the gDNA indicates where to cleave); two major and two minor products are seen which correspond to cleavage sites between nucleotides 9/10, 10/11, 13/14, and 14/15 downstream of the target residue base-paired with the 5'-end of the gDNA . Efficient guide-dependent tDNA cleavage requires a minimal length of 15 bp and is maximal at 19 bp . Prefers gDNA with 5'-phosphorylated purines and 3'-pyrimidines; changing these bases alters the cleavage activity and patterns . Also has guide-independent activity on tDNA called 'chopping' . Probably a first round of guide-independent activity on an invading plasmid or virus would generate guide DNAs for subsequent, more efficient, guide-dependent degradation of invading nucleic acids . Has no activity on substrate with a mismatch at positions 10 and 11, on ssDNA or RNA, nor on DNA:RNA hybrids . Digests longer (750 bp) dsDNA as well as circular plasmid and naked genomic DNA, but not chromatin, in a guide DNA-independent manner . Addition of endogenous histone A3 protects DNA from cleavage, while cleavage is insensitive to methylation . When plasmid encoding active or mutated protein (Ala-541) is transformed into Sulfolobus acidocaldarius about 25-fold fewer transformants are found with active protein; reduced levels of plasmid are found in wild-type transformed cells. While S.acidocaldarius grows at a similar temperature to M.jannaschii (70 to 80 degrees Celsius) it has very different histone-like proteins, which presumably do not protect against MjAgo . Binds ssDNA, dsDNA and DNA-RNA hybrids; binding is most efficient with dsDNA .
Sequence Mass (Da): 84583
Sequence Length: 713
Domain: Has 4 structurally distinct domains; N-terminal, PAZ (binds the 3'-end of gDNA), Mid (binds the phosphorylated 5'-end of gDNA) and PIWI (binds near the 5'-end of gDNA) arranged in a bilobal manner . Upon binding of gDNA the PAZ and Mid domains separate, opening a channel probably for tDNA-binding; a smaller channel also opens between the N-terminal and PIWI domains . The N-terminal and PAZ domains undergo further major rearrangement when the binary Ago-guide DNA complex binds tDNA; the PAZ domain binds the 3'-end of gDNA in the absence of target, upon ternary complex formation it is probably the N-terminal domain that binds that end of the dsDNA . The PIWI domain assumes an RNase H fold and has the catalytic residues .
EC: 3.1.24.-
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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 membrane protein
Sequence Mass (Da): 21899
Sequence Length: 191
Subcellular Location: Cell membrane
EC: 3.4.-.-
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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 membrane protein
Sequence Mass (Da): 21324
Sequence Length: 188
Subcellular Location: Cell membrane
EC: 3.4.-.-
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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 membrane protein
Sequence Mass (Da): 21911
Sequence Length: 188
Subcellular Location: Cell membrane
EC: 3.4.-.-
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A6QLU6 | MKKLLPLCCWHSWLLLFYCDFQVRGAHTRSHVHPGFEVLASASHYWPLENVDGIHELQETTGASRTHNLTVLPSHNSTFVYTNDSAYSNFSATVDIVEGKVNKGIYLKEGKGVTFLYYRKNKTSCISNPAQCGPEGVSFSFFWKTQGEQSTSIPSAYGGQVISNGFKVCSRGGKGSVELYTHNKSVTWEASFSPPGHYWTHVLFTWKSEEGLKVYVNGTLRTSDPSGKASPAYGESNDNLVLDLTKSYENRAFDEFIIWERALTPDEIAMYFTAAIGEQLSLSSTPPSFSVTPTVNTMAPTNAYHPIITNLTEERKNFRRPGVVLSYLQNMSLSLPNKSLSEETAFNLTKTFLNTVGEVLRLPSWTAVSEDSAVVPGLIDTIDTVMSHITYNLQASKPQVAIVGSSSMADFSVAKVLPKTMNSSHYRFPARGQNYIEIPHEAFHSQAWTTIVGLLYHSVHYYLSNIQPASTKIAEAANYKNCLLSATSYLISLEVSPTPKLSQNLSGSPLITVHLRHHLTQRQYTEATNESNRIFLYCAFLDFSSGEGIWSNQGCALTEGNLSYSICRCTHLTNFAILMQVVPLELTRGHQVALSSISYIGCSLSVLCLAITLVTFAVLSSVSTIRNQRYHIHANLSCAVLVAQVLLLISFRFEPGTAPCQVLAMLLHYFFLSAFAWMLVEGLHLYSMVIKVFGSEDSKHRYYYGIGWGFPLLICIISIVFAMDSYGTSKNCWLSLGNGAIWAFVAPALFIIVVNIGILIAVTRVISQISAENYKIHGDPSAFKLTAKAVAVLLPILGTSWVFGVLAVNNQAMVFQYMFAILNSLQGFFIFLFHCLLNSEVRAAFKHKTKVWSLTSSSSRQANVKPFSSDIMNGTRPATGSTRLSPWDKSSHSGHRVDLSAV | 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. Upon structural changes within the ECD, e.g. due to extracellular ligand binding or mechanical movements, this intramolecular agonist is exposed to the 7TM domain, triggering G-protein activation.
Subcellular Location: Cell membrane
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Q6QNK2 | MEKLLRLCCWYSWLLLFYYNFQVRGVYSRSQDHPGFQVLASASHYWPLENVDGIHELQDTTGDIVEGKVNKGIYLKEEKGVTLLYYGRYNSSCISKPEQCGPEGVTFSFFWKTQGEQSRPIPSAYGGQVISNGFKVCSSGGRGSVELYTRDNSMTWEASFSPPGPYWTHVLFTWKSKEGLKVYVNGTLSTSDPSGKVSRDYGESNVNLVIGSEQDQAKCYENGAFDEFIIWERALTPDEIAMYFTAAIGKHALLSSTLPSLFMTSTASPVMPTDAYHPIITNLTEERKTFQSPGVILSYLQNVSLSLPSKSLSEQTALNLTKTFLKAVGEILLLPGWIALSEDSAVVLSLIDTIDTVMGHVSSNLHGSTPQVTVEGSSAMAEFSVAKILPKTVNSSHYRFPAHGQSFIQIPHEAFHRHAWSTVVGLLYHSMHYYLNNIWPAHTKIAEAMHHQDCLLFATSHLISLEVSPPPTLSQNLSGSPLITVHLKHRLTRKQHSEATNSSNRVFVYCAFLDFSSGEGVWSNHGCALTRGNLTYSVCRCTHLTNFAILMQVVPLELARGHQVALSSISYVGCSLSVLCLVATLVTFAVLSSVSTIRNQRYHIHANLSFAVLVAQVLLLISFRLEPGTTPCQVMAVLLHYFFLSAFAWMLVEGLHLYSMVIKVFGSEDSKHRYYYGMGWGFPLLICIISLSFAMDSYGTSNNCWLSLASGAIWAFVAPALFVIVVNIGILIAVTRVISQISADNYKIHGDPSAFKLTAKAVAVLLPILGTSWVFGVLAVNGCAVVFQYMFATLNSLQGLFIFLFHCLLNSEVRAAFKHKTKVWSLTSSSARTSNAKPFHSDLMNGTRPGMASTKLSPWDKSSHSAHRVDLSAV | 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 extracellular domain (ECD) functions as a tethered agonist. Upon structural changes within the ECD, e.g. due to extracellular ligand binding or mechanical movements, this intramolecular agonist is exposed to the 7 transmembrane region, triggering G-protein activation.
Subcellular Location: Cell membrane
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Q80T32 | MKDLPAFPCSWVWLLWSFCSVQVCSTQPRAQEHPGFAVLASASHYWPLENVDGILELQDTTGALRTLNLTVPLSHNATFVFTNDSAYSNLSATVDIMEGKVNKGIYLKEEKGVTFLYYGTYKSSCISNPAQCGPEGVTFSFFWKTQGDQTRPAPYAYGGQVVSDGFKVCSSGGKGSVELYTRDNSMTWKATFNPPGPYWTHVLFTWKSKEGLKVYVNGTLSTSDPSGKVSHTYGDPHVNLVIGSEQDQTKRYENGAFDEFIIWERALTPDEIKMYFTAAIGKHALLSSTPPAMPTAHTVIPTDAYHPIITNLTEERKRFQRPGTVLRYLQNVSLRLPNKSLSEETALNLTETFLRTVGEVLLLPSWTHESEDNAMTLGLVDTIDTVMGHISSNLQSREPHVTLTGSSSTAEFTVAKVLPPALSAPHYRFPAHGHSYIEIPREALHSQAWTTIVGLLYHTMHYYLKNIHPTSTEIPEAVNCRDCLLSVASHLISLEVSPPPTLSQNLSGSPLITVHLRHKLTQKQYSDATNESNRLFLYCAFLNFSSGEGVWSSQGCALTEGNLTYSVCHCTHLTNFAILMQVVPLKLTHGHQVALSSISYVGCSLSVLCLAATLVTFAVLSSVSTIRNQRYHIHANLSFAVLVAQVLLLISFSMEPGTVPCQVLAVLLHYFFLTAFAWMLVEGLHLYSMVIKVFGSEDSKHLYYYGIGWGCPLLICIISISSSMDSYGTSDSCWLALGSGAIWAFVGPALLVIVVNIVILVAVTRVISHISTDSYKIHGDPSAFKLTAKAVAVLLPILGTSWVFGVLAVSDRALVFQYMFAILNSLQGLFIFLFHCLLNSEVRAAFKHKTKVWSLTSSSARTANTKPFSSDTVNGTRPGTASTKLSPWDKSSHSAHRVDLSAV | 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. Upon structural changes within the ECD, e.g. due to extracellular ligand binding or mechanical movements, this intramolecular agonist is exposed to the 7TM domain, triggering G-protein activation.
Subcellular Location: Cell membrane
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Q7Z7M1 | MDAPWGAGERWLHGAAVDRSGVSLGPPPTPQVNQGTLGPQVAPVAAGEVVKTAGGVCKFSGQRLSWWQAQESCEQQFGHLALQPPDGVLASRLRDPVWVGQREAPLRRPPQRRARTTAVLVFDERTADRAARLRSPLPELAALTACTHVQWDCASPDPAALFSVAAPALPNALQLRAFAEPGGVVRAALVVRGQHAPFLAAFRADGRWHHVCATWEQRGGRWALFSDGRRRAGARGLGAGHPVPSGGILVLGQDQDSLGGGFSVRHALSGNLTDFHLWARALSPAQLHRARACAPPSEGLLFRWDPGALDVTPSLLPTVWVRLLCPVPSEECPTWNPGPRSEGSELCLEPQPFLCCYRTEPYRRLQDAQSWPGQDVISRVNALANDIVLLPDPLSEVHGALSPAEASSFLGLLEHVLAMEMAPLGPAALLAVVRFLKRVVALGAGDPELLLTGPWEQLSQGVVSVASLVLEEQVADTWLSLREVIGGPMALVASVQRLAPLLSTSMTSERPRMRIQHRHAGLSGVTVIHSWFTSRVFQHTLEGPDLEPQAPASSEEANRVQRFLSTQVGSAIISSEVWDVTGEVNVAMTFHLQHRAQSPLFPPHPPSPYTGGAWATTGCSVAALYLDSTACFCNHSTSFAILLQIYEVQRGPEEESLLRTLSFVGCGVSFCALTTTFLLFLVAGVPKSERTTVHKNLTFSLASAEGFLMTSEWAKANEVACVAVTVAMHFLFLVAFSWMLVEGLLLWRKVVAVSMHPGPGMRLYHATGWGVPVGIVAVTLAMLPHDYVAPGHCWLNVHTNAIWAFVGPVLFVLTANTCILARVVMITVSSARRRARMLSPQPCLQQQIWTQIWATVKPVLVLLPVLGLTWLAGILVHLSPAWAYAAVGLNSIQGLYIFLVYAACNEEVRSALQRMAEKKVAEVLRALGVWGGAAKEHSLPFSVLPLFLPPKPSTPRHPLKAPA | Function: Orphan receptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 104087
Sequence Length: 963
Subcellular Location: Membrane
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Q14246 | MRGFNLLLFWGCCVMHSWEGHIRPTRKPNTKGNNCRDSTLCPAYATCTNTVDSYYCACKQGFLSSNGQNHFKDPGVRCKDIDECSQSPQPCGPNSSCKNLSGRYKCSCLDGFSSPTGNDWVPGKPGNFSCTDINECLTSSVCPEHSDCVNSMGSYSCSCQVGFISRNSTCEDVDECADPRACPEHATCNNTVGNYSCFCNPGFESSSGHLSFQGLKASCEDIDECTEMCPINSTCTNTPGSYFCTCHPGFAPSNGQLNFTDQGVECRDIDECRQDPSTCGPNSICTNALGSYSCGCIAGFHPNPEGSQKDGNFSCQRVLFKCKEDVIPDNKQIQQCQEGTAVKPAYVSFCAQINNIFSVLDKVCENKTTVVSLKNTTESFVPVLKQISTWTKFTKEETSSLATVFLESVESMTLASFWKPSANITPAVRTEYLDIESKVINKECSEENVTLDLVAKGDKMKIGCSTIEESESTETTGVAFVSFVGMESVLNERFFKDHQAPLTTSEIKLKMNSRVVGGIMTGEKKDGFSDPIIYTLENIQPKQKFERPICVSWSTDVKGGRWTSFGCVILEASETYTICSCNQMANLAVIMASGELTMDFSLYIISHVGIIISLVCLVLAIATFLLCRSIRNHNTYLHLHLCVCLLLAKTLFLAGIHKTDNKMGCAIIAGFLHYLFLACFFWMLVEAVILFLMVRNLKVVNYFSSRNIKMLHICAFGYGLPMLVVVISASVQPQGYGMHNRCWLNTETGFIWSFLGPVCTVIVINSLLLTWTLWILRQRLSSVNAEVSTLKDTRLLTFKAFAQLFILGCSWVLGIFQIGPVAGVMAYLFTIINSLQGAFIFLIHCLLNGQVREEYKRWITGKTKPSSQSQTSRILLSSMPSASKTG | 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 membrane
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Q61549 | MWGFWLLLFWGFSGMYRWGMTTLPTLGQTLGGVNECQDTTTCPAYATCTDTTDSYYCTCKRGFLSSNGQTNFQGPGVECQDVNECLQSDSPCGPNSVCTNILGRAKCSCLRGFSSSTGKDWILGSLDNFLCADVDECLTIGICPKYSNCSNSVGSYSCTCQPGFVLNGSICEDEDECVTRDVCPEHATCHNTLGSYYCTCNSGLESSGGGPMFQGLDESCEDVDECSRNSTLCGPTFICINTLGSYSCSCPAGFSLPTFQILGHPADGNCTDIDECDDTCPLNSSCTNTIGSYFCTCHPGFASSNGQLNFKDLEVTCEDIDECTQDPLQCGLNSVCTNVPGSYICGCLPDFQMDPEGSQGYGNFNCKRILFKCKEDLILQSEQIQQCQAVQGRDLGYASFCTLVNATFTILDNTCENKSAPVSLQSAATSVSLVLEQATTWFELSKEETSTLGTILLETVESTMLAALLIPSGNASQMIQTEYLDIESKVINEECKENESINLAARGDKMNVGCFIIKESVSTGAPGVAFVSFAHMESVLNERFFEDGQSFRKLRMNSRVVGGTVTGEKKEDFSKPIIYTLQHIQPKQKSERPICVSWNTDVEDGRWTPSGCEIVEASETHTVCSCNRMANLAIIMASGELTMEFSLYIISHVGTVISLVCLALAIATFLLCRAVQNHNTYMHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLACFFWMLVEAVMLFLMVRNLKVVNYFSSRNIKMLHLCAFGYGLPVLVVIISASVQPRGYGMHNRCWLNTETGFIWSFLGPVCMIITINSVLLAWTLWVLRQKLCSVSSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGPLASIMAYLFTIINSLQGAFIFLIHCLLNRQVRDEYKKLLTRKTDLSSHSQTSGILLSSMPSTSKMG | 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: Cell membrane
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Q5Y4N8 | MWGFWLLLFWGFSGTHRWGMTTLAILGQRLNGVNECQDTTTCPAYATCTDTTESYYCTCKQGFLPSNGQTNFQGPGVECQDVNECLRSDSPCGSNSVCTNIPGRARCSCLSGFSSSAGGSWILGSPGHFLCTDVDECLTIGICPKNSNCSNSVGSYSCTCQSGFVSNGSTCEDEDECVTRNACPEHATCHNTLGSYYCTCNEGLEFSGGGPMFQGLEESCEDVDECSRNSTLCGPSFICINTLGSYSCSCPAGFSLSTFQIPGHPADGNCTDIDECDDICPSNSSCTNTLGSYFCTCHPGFASSNGQLNFTDQEVTCEDIDECTQDPFRCGRNSSCTNVPGSYNCSCLPDFRMDPGGSQAHGNFTCKRIPFKCKEDLIPKSEQIEQCQAGQGRNLDYTSFCTFVNATFTILDNTCENKSAPVSLQSAATSVSLMLEQASTWFEFSREETSTLGTILLETVESTMLAALLTPSGNASQTIRTEYLEIESKVINEECNEENVSINLKARGDKMDVGCFIIKESESTGTPGVAFVSFAHMDSVLDERFFEDGQASWKLRMNSHVVGGTVTGERKEDFSKPIVYTLQHIQPKQKSERSICVSWNTDVEDGRWTPSGCETVEASETHTVCSCNRMTNLAIIMASGELTMEFSLYIISYVGTVISLVCLALAIATFLLFRAVQNHNTYLHLHLCVCLFLAKILFLTGIDKTDNQTACAIIAGFLHYLFLACFFWMLVEAVMLFLMVRNLKVVNYFSSRNIKMLHLCAFGYGLPVVVVIISATVHPWGYGMHNRCWLNTETGFIWSFLGPVCMIITINSALLAWTLWVLRQKLCSVNSEVSKLKDTRLLTFKAIAQIFILGCSWVLGIFQIGPLASIMAYLFTTINSLQGAFIFLIHCLLNRQVRDEYRKLLTRKTDLSSHSQTSGILLSSMPSTSKTG | 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 membrane
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Q2Q421 | MRHGHPRLLPGLLMLLLLPLGAAAQKTSGCARWCPPKSTCVNATTCRCSPGFSSLSGEIFSSPLESCDDIDECGPPPLVSCGRLADCQNTEGSYHCMCSPGYALASGATTFMNESENTCRDVDECQLKPRVCKSRGICTNTKGSYTCKCPPGFELNLGDLNLCTDVNECTSGQNPCHNSTHCLNNIGGYECRCRPGWKPVPGSPNGPKSTVCEDVDECSSGKHTCHYSTVCINTVGSYKCRCRRGWKPKPRFQDRQLNTTCEVPAEMSFPTWTPPPGIKSQRLSNFFERVQELHRDFKPALAQETIQDLIQEVDELLEIPGDLEALPHSEQHCVATNLLVGLEGVLRNVSQAMPNGPWTFNASAGTDLSLEVQEEGYRNVTLSQNLAKMMLKWDVVHKSGDSGPSVVGLLSTPGMGKLLAEAPLVLEPEKQAVLHGAPKGLLQGVSSVLLSDVISVFMSNKVTQKLSSPVTFIFSHHSATHEPKLKVFCVFWEHSQDECGHWSTRGCTVVDSGDTSTTCQCTHLSSFAVLMAHYDVQEEDLVLPVITYVGLGLSLLCLLLAALTFLLCKAIQNTSTSLHLQLLICLFLAHLLFLMAIDRTEIKVLCSIIAGALHYLYLASFTWMLLEGLHLFLTARNLMVVNYSSVSMLMKKLMYPVGYGVPTLIVAISAASRSHLYGTRTRCWLNPEERFIWSFLGPVCTIFSVNLGFFLMTLWILKSKLSSLNSDVSTLQNTRMLTFKAIAQLFILGCTWCLGILQVGPAAHVMAYLFTIINSLQGVFIFLVYCLLSQQVREEYGKWFKGIRKTRAESEKYTLSSRAMSDVNKPMMVN | 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.
PTM: Autoproteolytically cleaved into 2 subunits, an extracellular alpha subunit and a seven-transmembrane beta subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 91452
Sequence Length: 830
Domain: The GPS domain is necessary, but not sufficient for receptor cleavage, which require the entire extracellular stalk.
Subcellular Location: Cell membrane
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Q9UHX3 | MGGRVFLVFLAFCVWLTLPGAETQDSRGCARWCPQDSSCVNATACRCNPGFSSFSEIITTPMETCDDINECATLSKVSCGKFSDCWNTEGSYDCVCSPGYEPVSGAKTFKNESENTCQDVDECQQNPRLCKSYGTCVNTLGSYTCQCLPGFKLKPEDPKLCTDVNECTSGQNPCHSSTHCLNNVGSYQCRCRPGWQPIPGSPNGPNNTVCEDVDECSSGQHQCDSSTVCFNTVGSYSCRCRPGWKPRHGIPNNQKDTVCEDMTFSTWTPPPGVHSQTLSRFFDKVQDLGRDYKPGLANNTIQSILQALDELLEAPGDLETLPRLQQHCVASHLLDGLEDVLRGLSKNLSNGLLNFSYPAGTELSLEVQKQVDRSVTLRQNQAVMQLDWNQAQKSGDPGPSVVGLVSIPGMGKLLAEAPLVLEPEKQMLLHETHQGLLQDGSPILLSDVISAFLSNNDTQNLSSPVTFTFSHRSVIPRQKVLCVFWEHGQNGCGHWATTGCSTIGTRDTSTICRCTHLSSFAVLMAHYDVQEEDPVLTVITYMGLSVSLLCLLLAALTFLLCKAIQNTSTSLHLQLSLCLFLAHLLFLVAIDQTGHKVLCSIIAGTLHYLYLATLTWMLLEALYLFLTARNLTVVNYSSINRFMKKLMFPVGYGVPAVTVAISAASRPHLYGTPSRCWLQPEKGFIWGFLGPVCAIFSVNLVLFLVTLWILKNRLSSLNSEVSTLRNTRMLAFKATAQLFILGCTWCLGILQVGPAARVMAYLFTIINSLQGVFIFLVYCLLSQQVREQYGKWSKGIRKLKTESEMHTLSSSAKADTSKPSTVN | 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. Is a regulator of mast cell degranulation .
PTM: Autoproteolytically cleaved into 2 subunits, an extracellular alpha subunit and a seven-transmembrane beta subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90472
Sequence Length: 823
Domain: The GPS domain is necessary, but not sufficient for receptor cleavage, which require the entire extracellular stalk.
Subcellular Location: Cell membrane
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Q2Q426 | MGGRVFLAFCVWLTLLGAETQDSRDCARWCPENSSCVNATACRCNPGFSSSSEIFTSPTEICDDINECVPPSKVSCGKSSDCRNTEGSYDCVCNPGYELVSGAKTFKNESENTCQDVDECQQNPRLCKSYGTCVNTLGSFTCQCLPGFKFKPEDPKLCTDVNECTSGQNPCHSSTHCLNNVGSYQCRCRPGWQPIPGSPNGPNNTICEDVDECSSGLHQCDNSTVCFNTVGSYTCRCRPGWEPKHGIPNNQKDTVCKDMNFPTWTLPPGVHSQTLSQFFNKVQDLDRDFKTSSAKVTIQSILKELDELLEAPGDLETLPRFQQHCVATHLLDGLEDVLRGLSKNPSIGLLNFSYPAGTEFSLEVQKQVDRNVTLRQNQATMQLHWNLAQKSGDPGPSVVGLVSVPGMGKLLAEAPLVSEPENQVVRNETHQGLLPILLSDVISAFLSNNDTQNLSSPVTFIFSHRSVIPRRKVLCVFWEHGQNGCGHWATTGCSTMDTRDTSTICRCTHLSSFAVLMAPYDVQEEDPVLTVITYMGLSLSLLCLLLAALTFLLCKAIQNISTSLHLQLSLCLLLAHLLFLVAIDRTEHEVLCAIIASALHYLYLAAFTWMLLEALYLFLTARNLMVVNYSSINRFTKKLMFPVAYGVPAVTVAISAASRPHLYGTPSRCWLQPEKGFIWGFLGPVCAIFSVNLALLLVTLWILKNRLSSLNNEVSTLQNTRMLAFKATAQLFILGCTWCLGILQVGPAARVMAYLFTIINSLQGVFIFLVYCLLSQQVREQYRKWSKGFRKLRTESEMHTLSSSAKRDTPKPSTPGLLGLQS | 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.
PTM: Autoproteolytically cleaved into 2 subunits, an extracellular alpha subunit and a seven-transmembrane beta subunit.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90787
Sequence Length: 822
Domain: The GPS domain is necessary, but not sufficient for receptor cleavage, which require the entire extracellular stalk.
Subcellular Location: Cell membrane
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Q9SB31 | MEEREGTNINNNITSSFGLKQQHEAAASDGGYSMDPPPRPENPNPFLVPPTTVPAAATVAAAVTENAATPFSLTMPTENTSAEQLKKKRGRPRKYNPDGTLVVTLSPMPISSSVPLTSEFPPRKRGRGRGKSNRWLKKSQMFQFDRSPVDTNLAGVGTADFVGANFTPHVLIVNAGEDVTMKIMTFSQQGSRAICILSANGPISNVTLRQSMTSGGTLTYEGRFEILSLTGSFMQNDSGGTRSRAGGMSVCLAGPDGRVFGGGLAGLFLAAGPVQVMVGTFIAGQEQSQLELAKERRLRFGAQPSSISFNISAEERKARFERLNKSVAIPAPTTSYTHVNTTNAVHSYYTNSVNHVKDPFSSIPVGGGGGGEVGEEEGEEDDDELEGEDEEFGGDSQSDNEIPS | 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: 404
Domain: The PPC domain mediates interactions between AHL proteins.
Subcellular Location: Nucleus
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Q9LVB0 | MEEKGEISPSGVVTVKGDEALVPRTEFQQNPSFLQFVSPTTVVTPLPPPPAPSSAPVPTTVTPGSATASTGSDPTKKKRGRPRKYAPDGSLNPRFLRPTLSPTPISSSIPLSGDYQWKRGKAQQQHQPLEFVKKSHKFEYGSPAPTPPLPGLSCYVGANFTTHQFTVNGGEDVTMKVMPYSQQGSRAICILSATGSISNVTLGQPTNAGGTLTYEGRFEILSLSGSFMPTENGGTKGRAGGMSISLAGPNGNIFGGGLAGMLIAAGPVQVVMGSFIVMHQAEQNQKKKPRVMEAFAPPQPQAPPQLQQQQPPTFTITTVNSTSPSVNTVEEQKPQAYGGGIVRPMAQMPSSFQNDNSTMNNFTPAYHGYGNMNTGTTHKEEHEDEDGGDDDDDSGDTRSQSHSG | 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 | MDRRDAMGLSGSGSYYIHRGLSGSGPPTFHGSPQQQQGLRHLPNQNSPFGSGSTGFGSPSLHGDPSLATAAGGAGALPHHIGVNMIAPPPPPSETPMKRKRGRPRKYGQDGSVSLALSSSSVSTITPNNSNKRGRGRPPGSGKKQRMASVGELMPSSSGMSFTPHVIAVSIGEDIASKVIAFSQQGPRAICVLSASGAVSTATLIQPSASPGAIKYEGRFEILALSTSYIVATDGSFRNRTGNLSVSLASPDGRVIGGAIGGPLIAASPVQVIVGSFIWAAPKIKSKKREEEASEVVQETDDHHVLDNNNNTISPVPQQQPNQNLIWSTGSRQMDMRHAHADIDLMRG | 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 lactone + H2O = an N-acyl-L-homoserine + H(+)
Sequence Mass (Da): 28220
Sequence Length: 250
EC: 3.1.1.81
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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 lactone + H2O = an N-acyl-L-homoserine + H(+)
Sequence Mass (Da): 30663
Sequence Length: 273
EC: 3.1.1.81
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P27250 | MSMIKSYAAKEAGGELEVYEYDPGELRPQDVEVQVDYCGICHSDLSMIDNEWGFSQYPLVAGHEVIGRVVALGSAAQDKGLQVGQRVGIGWTARSCGHCDACISGNQINCEQGAVPTIMNRGGFAEKLRADWQWVIPLPENIDIESAGPLLCGGITVFKPLLMHHITATSRVGVIGIGGLGHIAIKLLHAMGCEVTAFSSNPAKEQEVLAMGADKVVNSRDPQALKALAGQFDLIINTVNVSLDWQPYFEALTYGGNFHTVGAVLTPLSVPAFTLIAGDRSVSGSATGTPYELRKLMRFAARSKVAPTTELFPMSKINDAIQHVRDGKARYRVVLKADF | 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 source of NADPH-dependent aldehyde reductase activity in E.coli. The in vivo functions of Ahr has yet to be determined.
Catalytic Activity: a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH
Sequence Mass (Da): 36502
Sequence Length: 339
EC: 1.1.1.2
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P30561 | MSSGANITYASRKRRKPVQKTVKPIPAEGIKSNPSKRHRDRLNTELDRLASLLPFPQDVINKLDKLSVLRLSVSYLRAKSFFDVALKSTPADRNGGQDQCRAQIRDWQDLQEGEFLLQALNGFVLVVTADALVFYASSTIQDYLGFQQSDVIHQSVYELIHTEDRAEFQRQLHWALNPDSAQGVDEAHGPPQAAVYYTPDQLPPENASFMERCFRCRLRCLLDNSSGFLAMNFQGRLKYLHGQNKKGKDGALLPPQLALFAIATPLQPPSILEIRTKNFIFRTKHKLDFTPIGCDAKGQLILGYTEVELCTRGSGYQFIHAADMLHCAESHIRMIKTGESGMTVFRLFAKHSRWRWVQSNARLIYRNGRPDYIIATQRPLTDEEGREHLQKRSTSLPFMFATGEAVLYEISSPFSPIMDPLPIRTKSNTSRKDWAPQSTPSKDSFHPSSLMSALIQQDESIYLCPPSSPAPLDSHFLMGSVSKCGSWQDSFAAAGSEAALKHEQIGHAQDVNLALSGGPSELFPDNKNNDLYNIMRNLGIDFEDIRSMQNEEFFRTDSTAAGEVDFKDIDITDEILTYVQDSLNNSTLMNSACQQQPVTQHLSCMLQERLQLEQQQQLQQPPPQALEPQQQLCQMVCPQQDLGPKHTQINGTFASWNPTPPVSFNCPQQELKHYQLFSSLQGTAQEFPYKPEVDSVPYTQNFAPCNQPLLPEHSKSVQLDFPGRDFEPSLHPTTSNLDFVSCLQVPENQSHGINSQSTMVSPQAYYAGAMSMYQCQPGPQRTPVDQTQYSSEIPGSQAFLSKVQSRGIFNETYSSDLSSIGHAAQTTGHLHHLAEARPLPDITPGGFL | 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 heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE) (By similarity). Regulates a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation . Xenobiotics can act as ligands: upon xenobiotic-binding, activates the expression of multiple phase I and II xenobiotic chemical metabolizing enzyme genes (such as the CYP1A1 gene) . Mediates biochemical and toxic effects of halogenated aromatic hydrocarbons (By similarity). Next to xenobiotics, natural ligands derived from plants, microbiota, and endogenous metabolism are potent AHR agonists (By similarity). Tryptophan (Trp) derivatives constitute an important class of endogenous AHR ligands (By similarity). Acts as a negative regulator of anti-tumor immunity: indoles and kynurenic acid generated by Trp catabolism act as ligand and activate AHR, thereby promoting AHR-driven cancer cell motility and suppressing adaptive immunity (By similarity). Regulates the circadian clock by inhibiting the basal and circadian expression of the core circadian component PER1 (By similarity). Inhibits PER1 by repressing the CLOCK-BMAL1 heterodimer mediated transcriptional activation of PER1 . The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription .
PTM: Mono-ADP-ribosylated, leading to inhibit transcription activator activity of AHR.
Sequence Mass (Da): 95017
Sequence Length: 848
Domain: The PAS 1 domain is essential for dimerization and also required for AHR:ARNT heterodimerization.
Subcellular Location: Cytoplasm
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