ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q2U4D6 | MTTPQPSQVRVAVTQAEPVWLDLKATVDKTCSLIAEAASKGAQLVSFPECWIPGYPAWIWTRPVDQELHSRYIQNSLTVSSPEMTQICKSANENNVIVVLGFSENIHNSLYISQAIISNTGSILTTRKKIKATHMERTIFGDAFADCLDSVVETAVGRVGALSCWEHIQPLLKYHTCAQREAIHVAAWPPLFEWGGPEDESLFSMSRDGTIALARTYAIESSSFVLHTTAVISQEGVEKMRTATGAIMNMPGGGSSAIFGPDGRLLSKPLLPTEEGIIYADLEMHDIYKTKAFVDVLGHYSRPDLLWLGVGSCDRRHVKE... | Function: Nitrilase that hydrolyzes preferentially phenylacetonitrile, (R,S)-mandelonitrile, and 3-indolylacetonitrile.
Catalytic Activity: a nitrile + 2 H2O = a carboxylate + NH4(+)
Sequence Mass (Da): 36804
Sequence Length: 333
EC: 3.5.5.1
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Q19A54 | MSKSLKVAAIQAEPVWNDLQGGVNKSIGLIQEAAKEGANVIGYPEVFIPGYPWSIWANSPTENAPWINEYFKNSMEKESPEMDQIRAAVREAGVFVVLGYSERYRGTLYIAQSFIDETGTIVLHRRKIKPTHVERAIYGDGQGESLTNVADTKFGRVAGLNCWEHTQTLLRYYEYXQDVDIHVSSWPSIFPQNVPEWPYHITPECCKAFSHVVSMEGACFVLLASQIMTEENHKKANVDGYDYTKKSGGGFSMIFSPFGEELVKPLAPNEEGILYADINLEEKYKAKQNLDIVGHYSRPDQLSLRVNKHAAKPVFFANDL | Function: Nitrilase that hydrolyzes preferentially benzonitrile.
Catalytic Activity: a nitrile + 2 H2O = a carboxylate + NH4(+)
Sequence Mass (Da): 36030
Sequence Length: 320
EC: 3.5.5.1
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G9N4E3 | MPDRVVRVAVTQAEPVWLDLQATIEKTCRLITEAASNNAQLVAFPETWIPGYPCWIWSRLVDFDLNVAYIKNSLRVDSPEMERLQACAREAGIAVSLGFSENSNNSLYISNVLIGSDGEIKVHRRKMKPTHMERTVFGDASGHCLQSVAQLPFGRVGSLSCWEHIQPLLKYNTITQNEEIHVAAWPPLNSEVGDEIPWSMTAEGCKTLSRTYAIESGTFVLHCTAVISESGINSLGTLGGALMSTPGGGHSTIFGPDGRRITDHIEETSEGIVYANLDMDELVVNKMFADCTGHYSRPDLLWLGVSQEIKPVVRPQRAEV... | Function: Nitrilase that hydrolyzes preferentially phenylacetonitrile and heteroaromatic nitriles, but has significantly lower activity for (R,S)-mandelonitrile. Also acts on dinitriles like phenylenediacetonitriles (PDAs) 1,2-PDA, 1,3-PDA, and 1,4-PDA, and cyanophenyl acetonitriles (CPAs) 2-CPA and 4-CPA.
Catalytic Ac... |
V5IPE4 | MATTIKVAVTQAEPIWLDLQASIQKAVSLVHEAASNGAKIVAFSETWAPGYPGWCWARPVDPALNTKYAYNSLTANSPEMEQLQQAAKEDSIAVVIGFSERSSSGSLYIGQAIISPQGEVALQRRKLKPTHMERTIFGDGSGPDLNCVAELDFGSELGSIKVGTLNCWEHAQPLLKFHEIQQGVVIHIAMWPPIDPYPGVEFPGLWSMTADGCQNLSQTFAVESGAFVLHCTAVCNESGIEAMDTRNGMVFREPGGGHSCVIGPDGRRLTQPLADKPSAEGIVYADLDLTRVVTNKSFQDIVGHYSRPDLLWLSYDKEKK... | Function: Nitrilase that hydrolyzes preferentially phenylacetonitrile, but also (R,S)-mandelonitrile, and 2-phenylpropionitrile.
Catalytic Activity: a nitrile + 2 H2O = a carboxylate + NH4(+)
Sequence Mass (Da): 35582
Sequence Length: 327
EC: 3.5.5.1
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Q93NG1 | MNLMEVRELAPSRGQLDVAAVQVKFDSTELLEDRISRIQDLVSGVGKADLIVLPELWLHGGFSYDSWRKNAISLESEVFTFLSEVARDKKAWFHAGSFMVTEPSSAASDMWNTSVLFDPTGSLRATYKKIHRFGFSDGEPKLIAAGDEPRVVELQTERATAITGLSTCYDLRFPELYRHISAEGTALNVIPACWPLTRIQHWQTLGRARAIENQSFVVQCNMTGVDQEVELGGHSQIVDGNGDILAQADKEEAVLRATLNFDSLNELRSSFPVLNDRRADIWAAKGKTVIASHL | Function: Catalyzes the conversion of 2-oxoglutaramate to 2-oxoglutarate. Together with glutamate dehydrogenase, may form a physiologically relevant enzyme couple, leading to transformation of metabolically inert 2-oxoglutaramate derived from trihydroxypyridine into glutamate, a central compound of nitrogen metabolism.... |
A5DNJ4 | MGAKVKVAVVQAEPVWFNLQETVKRVNELIESAYNKGAELIAFPEVFVPGYPTWIWTNAADLDRNLMYTKNSLTYDSPEFISIIETVKKYPIHVVLGFSEKDQGSLYISQCIIDNTGEIVLKRRKFKPTHVERVIWGDTADSNMKSVVTLNFKEAGPVEVGCLSCWEHMQPLLYYNSAAQHEKIHIGSWPALNDKDLGVYCFTKAGFHGLARAYANQVQSFYLFTSILGQRIQEALPDVKLSPYFEKGAGCGAVFAPDGSQITEDHPDDFDGVIISELDMDKILLQKNLVDIVGHYARPDMVSLSHNRPNTEFVNRK | Function: Nitrilase that hydrolyzes preferentially 4-cyanopyridine. Is also able to hydrolyze some aliphatic nitriles, such as phenylacetonitrile.
Catalytic Activity: a nitrile + 2 H2O = a carboxylate + NH4(+)
Sequence Mass (Da): 35697
Sequence Length: 317
EC: 3.5.5.1
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B6Q5I3 | MSKIVRVGAVQSEPVWLDLEGSVDKTISLIEKAAADGVNVLGFPEVWIPGYPWSMWTSAVINNSHIIHDYMNNSMRKDSPQMKRIQAAVKEAGMVVVLGYSERDGASLYMAQSFIDPSGEIVHHRRKIKPTHIERTIWGEGQAESLTCVIDSPFGKVGGLNCWEHLQPLLRYYEYSQGVQIHIASWPAEFEMPDPKKIAWLYHETGEASYRASQFFAIEGQAFVLVASQILTEANVERNNLTGNPVTKTPGGGFSMIFGPDGKPLCEPVDAGAEAILTADIDLRDIDKPKAFIDVVGHYARPDLLSLLVNPTVDKHVTTM... | Function: Nitrilase that hydrolyzes preferentially 4-cyanopyridine.
Catalytic Activity: a nitrile + 2 H2O = a carboxylate + NH4(+)
Sequence Mass (Da): 35663
Sequence Length: 322
EC: 3.5.5.1
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P9WEU6 | MANTIKASVVQASTAAYSLPDTLDKLEKLTRLAKERDGAQLAVFPEAFIGGYPKMSTFGLVVGDRQPEGRDEFVRYAKAAIEIPSPAITRIEQISRETNVFIVVGVIERDAGTLYCTAVFVDPEKGYVDKHRKLVPTAMERVIWGQGDGSTLPVLDKSFESASAPGSTVNTKLSATICWENYMPLLRTYYYSQGTQIYCAPTVDARPAWQHTMTHIALEGRCFVLSACQFAQEKDYPPDHAVANASARDPNNVMIAGGSVIISPLGKVLAGPLLDAEGVISAELDLDDVLRGKFDLDVTGHYARNDVFEFKLREPPATSS | Function: Nitrilase that hydrolyzes preferentially fumaronitrile, while 3-phenylpropionitrile, beta-cyano-L-alanine and 4-cyanopyridine are transformed at much lower rates.
Catalytic Activity: a nitrile + 2 H2O = a carboxylate + NH4(+)
Sequence Mass (Da): 34911
Sequence Length: 320
EC: 3.5.5.1
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Q48262 | MKLWFPYFLAIVFLHALGLALLFMANNASFYAAASMAYMLGAKHAFDADHIACIDNTIRKLTQQGKNAYGVGFYFSMGHSSVVILMTIISAFAIAWAKEHTPMLEEIGGVVGTLVSGLFLLIIGLLNAIILLDLLKIFKKSHSNESLSQQQNEEIERLLTSRGLLNRFFKPLFNFVSKSWHIYPIGFLFGLGFDTASEIALLALSSSAIKVSMVGMLSLPILFAAGMSLFDTLDGAFMLKAYDWAFKTPLRKIYYNISITALSVFIALFIGLIELFQVVSEKLHLKFENRLLRALQSLEFTDLGYYLVGLFVIAFLGSFF... | Function: High-affinity nickel intake protein. Imports nickel ions in an energy-dependent fashion. Necessary for the expression of catalytically active urease.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37034
Sequence Length: 331
Subcellular Location: Cell inner membrane
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Q2LKV2 | MEESPPKQKSNTKVAQHEGQQDLNTTRHMNVELKHRPKLERHLKLGMIPVVYMKQREEILYPAQSLKEENLIQNFTSLPLLQKLCPKDPENMVRKSWASCIPEEGGHMINIQDLFGPNIGTQKEPQLVIIEGAAGIGKSTLARLVKRAWKEGQLYRDHFQHVFFFSCRELAQCKKLSLAELIAQGQEVPTAPINQILSHPEKLLFILDGIDEPAWVLADQNPELCLHWSQRQPVHTLLGSLLGKSILPEAFFLLTTRTTALQKFIPSLPMPCQVEVLGFSGIEWENYFYKYFANQRHAITAFMMVESNPVLLTLCEVPWV... | Function: Probable inactive allele of Nlrp1b, which lacks a CARD domain, suggesting that it is not able to form an inflammasome . Contrary to Nlrp1b allele 1, allele 4 is not activated by B.anthracis lethal toxin and no other activation signal is reported .
Sequence Mass (Da): 103119
Sequence Length: 906
Domain: Contra... |
Q9SRX9 | MKFCKKYEEYMQGQKEKKNLPGVGFKKLKKILKRCRRNHVPSRISFTDAINHNCSRECPVCDGTFFPELLKEMEDVVGWFNEHAQKLLELHLASGFTKCLTWLRGNSRKKDHHGLIQEGKDLVNYALINAVAIRKILKKYDKIHESRQGQAFKTQVQKMRIEILQSPWLCELMAFHINLKESKKESGATITSPPPPVHALFDGCALTFDDGKPLLSCELSDSVKVDIDLTCSICLDTVFDPISLTCGHIYCYMCACSAASVNVVDGLKTAEATEKCPLCREDGVYKGAVHLDELNILLKRSCRDYWEERRKTERAERLQQ... | Function: E3 ubiquitin-protein ligase that mediates E2-dependent protein ubiquitination . Plays a role in salicylic acid-mediated negative feedback regulation of salicylic acid (SA) accumulation . May be involved in the overall regulation of SA, benzoic acid and phenylpropanoid biosynthesis . Involved in defense respon... |
Q9FLX9 | MTMMDTDEGKTVMCLLTDPEGTHLGSAMYIPQKAGPLQLTQLVNRFLDNEEMLPYSFYVSDEELLVPVGTYLEKNKVSVEKVLTIVYQQQAVFRIRPVNRCSQTIAGHAEAVLCVSFSPDGKQLASGSGDTTVRLWDLYTETPLFTCKGHKNWVLTVAWSPDGKHLVSGSKSGEICCWNPKKGELEGSPLTGHKKWITGISWEPVHLSSPCRRFVTSSKDGDARIWDITLKKSIICLSGHTLAVTCVKWGGDGIIYTGSQDCTIKMWETTQGKLIRELKGHGHWINSLALSTEYVLRTGAFDHTGRQYPPNEEKQKALER... | Function: Required for female gametophyte development.
Sequence Mass (Da): 52897
Sequence Length: 473
Domain: The DWD box is required for interaction with DDB1A.
Subcellular Location: Nucleus
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Q9HAN9 | MENSEKTEVVLLACGSFNPITNMHLRLFELAKDYMNGTGRYTVVKGIISPVGDAYKKKGLIPAYHRVIMAELATKNSKWVEVDTWESLQKEWKETLKVLRHHQEKLEASDCDHQQNSPTLERPGRKRKWTETQDSSQKKSLEPKTKAVPKVKLLCGADLLESFAVPNLWKSEDITQIVANYGLICVTRAGNDAQKFIYESDVLWKHRSNIHVVNEWIANDISSTKIRRALRRGQSIRYLVPDLVQEYIEKHNLYSSESEDRNAGVILAPLQRNTAEAKT | Cofactor: Divalent metal cations. Zn(2+) confers higher activity as compared to Mg(2+).
Function: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP . Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency . Can use triazofurin monophos... |
Q9EPA7 | MDSSKKTEVVLLACGSFNPITNMHLRLFELAKDYMHATGKYSVIKGIISPVGDAYKKKGLIPAHHRIIMAELATKNSHWVEVDTWESLQKEWVETVKVLRYHQEKLATGSCSYPQSSPALEKPGRKRKWADQKQDSSPQKPQEPKPTGVPKVKLLCGADLLESFSVPNLWKMEDITQIVANFGLICITRAGSDAQKFIYESDVLWRHQSNIHLVNEWITNDISSTKIRRALRRGQSIRYLVPDLVQEYIEKHELYNTESEGRNAGVTLAPLQRNAAEAKHNHSTL | Cofactor: Divalent metal cations. Zn(2+) confers higher activity as compared to Mg(2+).
Function: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP . Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency (By similarity). Can use triaz... |
P91851 | MKRVALLAVGSFNPPTIAHLRMLEVARSHLETINTQVVEGIMSPVADSYNNKPTLIKSNFRIQMVRAATKSSDWIRADDWECTRTTWTRTIDVLRHHRELVQEKFGSDVGMMLVVGGDVVDSFTRILPDGSNLWNSSDIRTIITEFGLIVLSREGSNPLNTIQSMPAISEFCDRIIQVKDEVCPSGVSSTRLRAAIMNKKSIKYSTPDEVINFIRENNLYQKI | Function: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate.
Catalytic Activity: ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate + NAD(+)
Sequence Mass (Da): 25168
Sequence Length: 223
Pathw... |
Q9BZQ4 | MTETTKTHVILLACGSFNPITKGHIQMFERARDYLHKTGRFIVIGGIVSPVHDSYGKQGLVSSRHRLIMCQLAVQNSDWIRVDPWECYQDTWQTTCSVLEHHRDLMKRVTGCILSNVNTPSMTPVIGQPQNETPQPIYQNSNVATKPTAAKILGKVGESLSRICCVRPPVERFTFVDENANLGTVMRYEEIELRILLLCGSDLLESFCIPGLWNEADMEVIVGDFGIVVVPRDAADTDRIMNHSSILRKYKNNIMVVKDDINHPMSVVSSTKSRLALQHGDGHVVDYLSQPVIDYILKSQLYINASG | Cofactor: Divalent metal cations. Mg(2+) confers the highest activity.
Function: Nicotinamide/nicotinate-nucleotide adenylyltransferase that acts as an axon maintenance factor (By similarity). Axon survival factor required for the maintenance of healthy axons: acts by delaying Wallerian axon degeneration, an evolutiona... |
A4IH61 | MAETTKTHVILLACGSFNPITKGHIQMFERARDYLHKTGKFIVIGGIISPVHDSYGKQGLVSSRHRLNMCQLAVQNSDWIRVDPWECYQDTWQTTCSVLEHHRDLMKRVTGCILSNVNTPSVTPVIGQSLNQSTQPVYQNSNLSNKPTAVRILGKVGEGLSRMCCVRPNLQRVTFVDENANLGTVMRYEEIELRILLLCGSDLLESFCIPGLWNESDMEVIVGDFGIVVVPRDSVEPEQIINHSSLLRKYKNNILTVKDDSNHPMAVVSSTKSRLALQHGDGHVVDYLAQPVIDYVLKSQLYINTSG | Cofactor: Divalent metal cations. Mg(2+) confers the highest activity.
Function: Nicotinamide/nicotinate-nucleotide adenylyltransferase that acts as an axon maintenance factor. Axon survival factor required for the maintenance of healthy axons: acts by delaying Wallerian axon degeneration, an evolutionarily conserved p... |
Q96T66 | MKSRIPVVLLACGSFNPITNMHLRMFEVARDHLHQTGMYQVIQGIISPVNDTYGKKDLAASHHRVAMARLALQTSDWIRVDPWESEQAQWMETVKVLRHHHSKLLRSPPQMEGPDHGKALFSTPAAVPELKLLCGADVLKTFQTPNLWKDAHIQEIVEKFGLVCVGRVGHDPKGYIAESPILRMHQHNIHLAKEPVQNEISATYIRRALGQGQSVKYLIPDAVITYIKDHGLYTKGSTWKGKSTQSTEGKTS | Cofactor: Divalent metal cations. Mg(2+) confers the highest activity.
Function: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate with the same efficiency. Can use triazofurin monophosphate (TrMP) as sub... |
F4K687 | MDVPLPVEKLSYGSNTEDKTCVVLVATGSFNPPTFMHLRMFELARDELRSKGFHVLGGYMSPVNDAYKKKGLLSAEHRLEMCNVSCQSSDFVMVDPWEASQSNYQRTLTVLSRVKTFLTTNRHVPEESLKVMLLCGSDLLLSFCTPGVWIPEQLRTICKDYGIVCIRREGQDVENMISGDEILNENCANVKIVDNTVPNQISSSRLRQCISRGLSVKYLTEDGVIDYIRQHQLYTELT | Function: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate.
Catalytic Activity: ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate + NAD(+)
Sequence Mass (Da): 26923
Sequence Length: 238
Pathw... |
Q0DWH7 | MEELELPLPTEKLAVDPGREGGKRGVAVLVATGSFNPPTYMHLRMFELAKDELQQRGYSVLGGYMSPVNDAYKKKGLLSAAHRIRLCELACESSSFVMVDRWEAMQKGFQRTLTVLSRIRNALSKDGLADGGSPNVMLLCGSDLLESFSTPGVWIPDQVRIICKDFGVICIRREGKDVEKIISSSEILNECRDNIISVDEIVPNQISSSRVRECIKKCLSIKYLVCDEVIQYIGEHKLYKEADGSDTRK | Function: Catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Can also use the deamidated form; nicotinic acid mononucleotide (NaMN) as substrate.
Catalytic Activity: ATP + beta-nicotinamide D-ribonucleotide + H(+) = diphosphate + NAD(+)
Sequence Mass (Da): 27793
Sequence Length: 249
Pathw... |
O05413 | MNEFMKKFSLTKPIIQAPMAGGITKPRLASAVSNQGALGSLASGYLTPDLLEQQIKEIFELTDAPFQINVFVPLGLEMPPKDQIKKWKENIPLANQVNQFTSVQEEWDDFYQKIDLILKYKVKACSFTFDLPPEDAVKELKTAGCCLIGTASTVEEALLMEERGMDIVVLQGSEAGGHRGAFLPSKGESAVGLMALIPQAADALSVPVIAAGGMIDHRGVKAALTLGAQGVQIGSAFLICHESNAHPVHKQKILEANEADTKLTTLFSGKEARGIVNKWMEENEQFETQTLPYPYQNTLTKAMRQKASLQNNHDQMSLWA... | Cofactor: Binds 1 FMN per subunit.
Function: Nitronate monooxygenase that uses molecular oxygen to catalyze the oxidative denitrification of alkyl nitronates. Acts on propionate 3-nitronate (P3N), the presumed physiological substrate. Probably functions in the detoxification of P3N, a metabolic poison produced by plant... |
Q9HWH9 | MTDRFTRLLGIQQPIIQAPMLGVSTPALAAAVSNAGGLGSIAITGSAAEKGRALIREVRGLTDKPFNVNLFCHRPGQADPARERAWLDYLKPLFAEFGAEPPVRLKNIYLSFLEDPTLLPMLLEERPAAVSFHFGAPPRDQVRALQAVGIRVLVCATTPEEAALVEAAGADAVVAQGIEAGGHRGVFEPERGDAAIGTLALVRLLAARGSLPVVAAGGIMDGRGIRAALELGASAVQMGTAFVLCPESSANAAYREALKGPRAARTALTVTMSGRSARGLPNRMFFDAAAPGVPPLPDYPFVYDATKALQTAALARGNHD... | Cofactor: Binds 1 FMN per subunit.
Function: Nitronate monooxygenase that uses molecular oxygen to catalyze the oxidative denitrification of alkyl nitronates. The toxin propionate 3-nitronate (P3N) is the best substrate (and the presumed physiological substrate), but this enzyme is also active on other primary and seco... |
D0V3Y4 | MSNSLLSLLNIELPIIQSPMVGVSTPRLAAAVSNAGGLGSIGIGASNVEQARAMLRETAALTDRPFNVNLFCHVPARADAAREAQWLAFLAPLFAEFESPAPAALREIYTSFVEDFAMLEMLLEEKPAVVSFHFGLPPQSSIDALKDAGIVLLACVTNLAEAQQAEHAGVHALVAQGYEAGGHRGVFDPQQDSEMGTFALVRVLTDACQLPVIAAGGIMDGAGIKAVMQLGASAAQLGTAFILCPESSANPAYRDALQGPRAHQTRVTSAISGRPARGMVNRNYIDLETNAPALPDYPIAYDANKALNAAAANKANTDFA... | Cofactor: Binds 1 FMN per subunit.
Function: Nitronate monooxygenase that uses molecular oxygen to catalyze the oxidative denitrification of alkyl nitronates. Acts on propionate 3-nitronate (P3N), the presumed physiological substrate. Is likely involved in the degradation of P3N, that allows Pseudomonas sp. JS189 to gr... |
Q4P219 | MSTSAAPGKLATTLGANVSSLASKVRSTSSTQQSLMQSVKRIIPPLSSAKHKGQAGRIGIVGGSRDYTGAPFFASMSSMRFGCDMSYTICTPEAGNVIKTYSPDLIVNRLLDASVEWSQVERSVDELFARFHAVVIGPGLGRDEFMQKCAKLCIGLARKHDMYLVVDADGLWLLQNEPDLIKGYKKAILTPNVAEFGRLCDTLGIDCKQEPDSAAKKLAQALEGPTVLEKGPVDRITNGKEVLYVDLQGGLKRCGGQGDVLAGCLGTLAGWAKIYQDENPTLPARSTTTDGDLIAEDRLLLLAGYAASVTARTCSRLAFA... | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
F6HDM2 | MLASSAVFRRQEFLIRCLGVGGQSQQFYRKSIPRTMALEADAENILRAITPTLDLARHKGQAGKIAVIGGCREYTGAPYFSAISALKIGADLSHVFCTKDAAPVIKSYSPELIVHPLLEESYSVREEDKKAISEKVLTEVVKWMERFDCLVVGPGLGRDPFLLGCVSEIMKHARQSNVPIVIDGDGLFLVTNSLDLVSGYPLAVLTPNVNEYKRLVQKVLNCEVGDQDAAEQLLSLAKGIGGVTILRKGKSDLISDGETVNSVGIYGSPRRCGGQGDILSGSVAVFLSWARQRIIAEGDLNISPKSPTVLGSIAGSALMR... | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
Q8PBP3 | MTGPRVRTVTAAALRAQPLPAPGGDKEQRGRVLIVGGSARVPGAVMLAGEAALRAGAGKLQLATAASVAPGMALAMPEALVLGLGENGQGEIVRGHRALDAAMSACDAAVIGPGMASTNTTAALVKRAIDQAVCTLVLDAGALSPRLRAPLGRPFVLTPHAGEMAALAGDDKAAVEAAPADYALAFAKKMRSVVIVKGADSFVAGPDGALWVHRGGVPGLGTSGSGDTLAGLIAGFAARGCDALTAALWGVFVHATAGKQLAKRIGTVGFLAREIPPEVPGILDRLPRG | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
P36059 | MLAELSHRELIKLAQKRCIPPLLPKFHKGQSGGRVCIIGGCEDYTGAPYFSANATALMGCDLTHVICEYNAGTVIKSYTPNLMVHPYLRMSNTKLDVDMDEQRKKINSLLDRIHVVVIGPGLGRDPLMLKSIKDIIRYILEKHEGKIPLVIDADGLFLVTQDSEVKEMLKSYPKGRVILTPNVVEFKRLCDAIGKKGDSHSEMGSLIAQELNCIVVEKGQSDKIFSPDSEKDMLTNSEEGSNKRVGGQGDTLTGAISCMLAFSRAMYDFKICEQEEKGESSNDKPLKNWVDYAMLSCYAGCTITRECSRLGFKAKGRAMQ... | Function: Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ATP, which is converted to ADP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or ... |
E3HVU4 | MPPSHSVAQIRDAERQTLATGRRLMPLAGAAAARHVAARIRPGAVVLALAGPGNNGGDALEAATGLRAMGHDVRVLLPSGAQGLPADAARAYAGWQAAGGETWSTLEPGFVPGLVIDGLFGIGLNRPLGADWQALVDTVNAWNVPVLALDVPSGIDADSGEALGRPIQARWTLSFIGRARGLERPGPGRDACGISEVDTLGVIMTPAN | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX... |
C7RGH4 | MLVVDSKTMKKIDQYAIDVLKVPSICLVERAALAVIKNINLEKRTSFAIVVGVGNNGADGLAIARNLLAMGKYVEIYIVGDLTKQSQDFKLNLDSCKRLTDKIFEPKSIEDLAIMERNLEEVSTIIDAIFGTGLNRTVGGMQSYMISLINRTMKYTISVDIPSGLDGDSGRNWGEVVDSDLIISMQIMKRGVYEKSHFKDKCIVEDIGIPQKAIRAIL | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX... |
E3XA68 | MKYLNQQEAISIDEELFNEYKFSVDQLMELAGLSCAHVIADAYAPESNKILICCGPGNNGGDGLVAARHLALMNYNPYVYYPKRTEKELFRNLQHQAESMGITVTTDCPDGASVEQEFGLIVDALFGFSFKPPVRDSFLPIMNVLQRSKLPIVSIDIPSGWNVEEGPQNECDIQPACLISLTAPKLCAKRLLNAQHYLGGRFVPKRLEEKYSLELPSYLGSNLFVKLN | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX... |
Q4WUG4 | MSLKAISAKDAASLDKDLMEMGGWSLDQLMELAGLSVSQAGMWSIYRLHPPSAGKNVLVVCGPGNNGGDGLVAARHLAQYGYTPSVYYPKEGKNELYQRLKTQLHNLSVPFVPDFTEALKSADFLVDAIFGFSFGGPLREPFPSIISQIESSSVPVLSVDAPSSWDIQSGPPKEGPGSKFMPKALISLTAPKPCVKYYRGRHFVGGRFLTKSIVEKYGLNCPDYPGIDQIVEVGVDAEGRL | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX... |
Q7WGX4 | MDIERVEQVRAVERLAHRRGLALMPRAGLAAADFVAARLPAGAQVLALAGPGNNGGDALVAATLLQARGYRVAVVMPAGPARLPDDARRAWQDWCAAGGQASADLPAHAPALVIDGLFGIGLARPLGGAWQGLIDQVNAWRVPVLALDVPSGLSAASGQPLGDPPGRPVRATWTLSFIGVPAALRAPGAAAWCGQQHLSLLGLTPAFLAEAVGPCGQATATAARRSGP | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX... |
Q6QRN6 | MSGLRALLGLGLLVAGSRLSRVRVQAGSCRAGATWWVPQRLISGGRGDSEVMASSAVKYLSQEEAQAVDQELFNEYQFSVDQLMELAGLSCATAIAKAYPPTSLSRSPPTVLVICGPGNNGGDGLVCARHLKLFGYQPTIYYPKRPNKPLFTALVTQCQKMDIPFLGEMPPEPMLIDELYELVVDAIFGFSFTGEVREPFRSILSVLNGLTVPIASIDIPSGWDVEKGSSGGIQPDLLISLTAPKKSATQFTGRYHYLGGRFVPPALEKKYQLNLPPYPDTECVYRLQ | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX... |
C3YDS7 | MESWKGKYASGLRFSFRKRYSTEKGGTVDEDCEVISIGHKIGDISYVSQEEAQQIDQELFNEYAYSVDQLMELAGHSCAVALAKSYPLTSLKKDATVLVCCGPGNNGGDGLVCARHLKMFGYNPSVFYPKRTDKPLYKNLTIQCEQLDIPFLSHLPKPQLLSDGFSYIVDALFGFSFKGEVRPPFGDVLKTLKEVTVPICSIDVPSGWDVEGGNPDGLQPEFLISLTAPKKCAEKFAGRYHYLGGRFVPPGIIQKYELNLPTYPGTEPCIRLH | Cofactor: Binds 1 potassium ion per subunit.
Function: Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX... |
P93328 | MASSSPILLMIIFSMWLLISHSESTDYLIGDSHNSWKVPLPSRRAFARWASAHEFTVGDTILFEYDNETESVHEVNEHDYIMCHTNGEHVEHHDGNTKVVLDKIGVYHFISGTKRHCKMGLKLAVVVQNKHDLVLPPLITMPMPPSPSPSPNSSGNKGGAAGLGFIMWLGVSLVMMMFLI | Function: May act as a carbohydrate transporter.
Location Topology: Lipid-anchor
Sequence Mass (Da): 20026
Sequence Length: 180
Subcellular Location: Symbiosome
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P93329 | MSSSSPILLMFIFSIWMLISYSESTDYLVGDSENSWKFPLPTRHALTRWASNYQFIVGDTITFQYNNKTESVHEVEEEDYDRCGIRGEHVDHYDGNTMVVLKKTGIHHFISGKKRHCRLGLKLAVVVMVAPVLSSPPPPPSPPTPRSSTPIPHPPRRSLPSPPSPSPSPSPSPSPSPSPRSTPIPHPRKRSPASPSPSPSLSKSPSPSESPSLAPSPSDSVASLAPSSSPSDESPSPAPSPSSSGSKGGGAGHGFLEVSIAMMMFLIF | Function: May act as a carbohydrate transporter.
Location Topology: Lipid-anchor
Sequence Mass (Da): 28668
Sequence Length: 268
Subcellular Location: Cell membrane
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P08995 | MADYSAGTESQEVVVNVTKNTSETIQRSDSLVSVPFLQKLVAEAVGTYFLIFAGCASLVVNENYYNMITFPGIAIVWGLVLTVLVYTVGHISGGHFNPAVTIAFASTRRFPLIQVPAYVVAQLLGSILASGTLRLLFMGNHDQFSGTVPNGTNLQAFVFEFIMTFFLMFVICGVATDNRAVGEFAGIAIGSTLLLNVIIGGPVTGASMNPARSLGPAFVHGEYEGIWIYLLAPVVGAIAGAWVYNIVRYTDKPLSETTKSASFLKGRAASK | Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes. This aquaporin may function in transporting small molecules across the peribacteroid membranes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28936
Sequence Length: 271
Domain: Aquaporins contain... |
F4IMH3 | MASILSKKQKKNEKYTLKELKSLGHDLLTSRSHINNLPLLLTFVSPESPPQFVVESLLSLQSFFTPLLSQLPPTSSSPSSTKTEDPEVVFKAWLRSKFDEFVKLLLDVLVSQQSEDSLRGIVLGTLMEFVKLLNAGRFHSSIYHRLLDAIIHSEVDIEIFLDILTSKYFKYIDVRYFTYISMEKFVKTLEASVSADRTVIENNEAESDSKESLELSVRKIYQVLSQIPPPEKQAEKSQHEMWSGSDESISEKPTDKKKKTEKGDSTLLSPATISKRMKLKFTKAWISFLRLPLPIDVYKEVLASIHLTVIPHLSNPTMLC... | Function: Essential protein required during embryogenesis . Involved in nucleolar processing of ribosomal RNA (rRNA) 40S and 90S ribosomal subunits and ribosome assembly; early in ribosome biogenesis, especially required during the maturation of 5.8S rRNA . Has a role in the nuclear export of 40S pre-ribosomal subunit ... |
Q5J1R2 | MGALPRVPLITAPTRLHPVDGLAPRRVLVKRDDENSPVFGGCKTRALEFVLGAARAAGATAVLTSGTAGSNHVAATALHAGRLGFRVTALVLPQEPGALVARNLRLAAGAGARLEPVPDGVSVHPDRERHRAAVAELRERGERVHVIPFGGADPVAGVAHALAGLELAEQARGLPGPLRVHLPAASTLTAAGIAAGLALSGLPFQVTAVDVVGSSSTLGPGLLGRAREVAALLGGPADAVRPEHVRHVGYAGAPYGVPDPEAGRCADLLREAADVRVDECYGAKAFHHLLGEVGDADGTHLFWHTGSTREAGEVFGPVPP... | Function: Involved in the biosynthesis of the beta-lactam antibiotic nocardicin A . Catalyzes the interconversion of the nocardicin homoseryl side chain in both nocardicin A with isonocardicin A, and nocardicin C with isonocardicin C .
Catalytic Activity: isonocardicin C = nocardicin C
Sequence Mass (Da): 33559
Sequenc... |
Q5J1R4 | MTRTDTRSYPFGDPVALDLHPGYAPLRAEQPALRVRLPYGEDCWLVTRHEDVKAVLSDSRFSRARAAGREETPRVTPEAAPAGSMLSMDPPEHSRLRKLIARAFTSRRVREFRPRTQEIVDGLLDQVEQAGAPADLVAGLALPLPVSVISQMLGVPTEDHYRFRDFSATVLSTTAHTREEIVAARAALEEYLGELADQRRREPGEDLMSALVAAHDDDRLTDRELTQTGITLLVGGHESTASQFACSVYLLLERPERWALLRDNPELVPTAVEELLRFIPLGSGGAFARIATEDVEVGGVLVRAGEAVVASTNSANRDDR... | Function: Involved in the biosynthesis of the beta-lactam antibiotic nocardicin A . Catalyzes the conversion of nocardicin C to nocardicin A . Cannot use nocardicin G .
Sequence Mass (Da): 43696
Sequence Length: 398
Pathway: Antibiotic biosynthesis.
EC: 1.14.15.-
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P35113 | MDIQLIIESFPKLLAAVPTTLTLAFISLLIGFVVSVPVALMRLSKNRIVSSLAYGYVYIIRSTPLLVQMFLIYYGSAQFRGVLSEVGLWSSFREPWFCAILALALNTAAYTSEIIRGGIQSVSLGQIEAARAVGMSTFLQFRRIVFPIAIRQALPAYGNEVMLIIKSTSLASTITIVEVTGLAKQIISATYSPVEVFIVAGAIYLFITFVVSRLVMLAEWWLNPHMRARVGGTAPKAAETH | Function: Component of the nopaline active transport system probably consisting of four subunits: Q, M, P and T. This system is also capable of transporting octopine provided that catabolic functions are induced with nopaline.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26424
Sequence Length: 241... |
P35118 | MDLTLLQWGDAGWGDELARGAMMTVVVAACSYFFGIIFGSLFAAAKLSRFWSLRLLGDVYTTVVRGVPELLIIFLVFFGGGTLLRTIANGLFGYEGYIEPPIFVIGVLCISVSAGAYATEVIRAAVLAVPPGQIEAAKSIGMGPWLRLRRVLIPQAARFALPGLGNVWQFTLKDTSLISVVGLVEIMRTAAMGAGSTKQPFTFYITAFVIFLLLSSVSNRGFLKAEKWANRGVRSQ | Function: Component of the nopaline active transport system probably consisting of four subunits: Q, M, P and T. This system is also capable of transporting octopine provided that catabolic functions are induced with nopaline.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 25524
Sequence Length: 236... |
P28603 | MPTLPNDLRLLEAESIAILRETAASFTKPVLLYSIGKDSGVLLHLARKAFHPSPVPFPLLHVDTGWKFREMIAFRDATVRRLGLTLIVHRNEEGHARGIDPIRSGSALHTRVMKTEALRQALDRHGFDAAIGGARRDEEKSRAKERVFSIRNAAHAWDPRDQRPELWRLWNPRIQPGESVRVFPLSNWTELDVWRYVAAQSIPVVPLYFAAERPVVHRSGALIMVDDGRLPLNPGETPEMRRVRFRTLGCYPLSGAIDSDAATVEDIIVEMRASRTSERQGRLIDGDEPASMERKKREGYF | Function: Proposed to provide activated sulfate for transfer to nod factor.
Catalytic Activity: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
Sequence Mass (Da): 34137
Sequence Length: 301
EC: 2.7.7.4
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P13441 | MSLPHLRRLEAEAIHVIREVVATFSNPVVLYSIGKDSSVLLHLAMKAFYPAKPPFPFLHVDTKWKFREMIEFRDRMARELGFDLLVHVNQDGVEQGIGPFTHGSNVHTHVMKTMGLRQALEKYGFDAALAGARRDEEKSRAKERIFSIRSAQHGWDPQRQRPEMWKTYNTRVGQGETMRVFPLSNWTEFDIWQYILREEIPIVPLYFAARRPVVKREGMLIMVDDDRMPIQPEEEVTEQLVRFRTLGCYPLTGAVESDAVTVPEILREMLTVRTSERQSRLIDTDEVGAMEKKKREGYF | Function: Proposed to provide activated sulfate for transfer to nod factor.
Catalytic Activity: ATP + H(+) + sulfate = adenosine 5'-phosphosulfate + diphosphate
Sequence Mass (Da): 34763
Sequence Length: 299
EC: 2.7.7.4
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Q8VYP6 | MSEAENKLPFIPEEWSNAASSVSCSSLQPVIALVCGPKNSGKSTFSRNLVEVLLQRYKRVAYLDTDVGQPEFTAPGFLSLTIVDKSILESDWTVPCVKTPERCFFYGDVSSKRDPKAYLRYVYTLFDYYQLHFCKSSENKTELPLVINTPGWVKGIGYELLVDVLRYVSPSHVVKINISAYNKNLPAGLFWLDGNDDETAHLIEIQSAYQDRYNQSILIHKDARLMRDMRIIAYFRQCFKGKEVNTIKELTHELASHIPYEVPISSLTINHLHCQIPSSEVYYSLNASIVGLGISTEVFEDLPSCVGLGIVRGIDTERGI... | Function: Polynucleotide 5'-kinase involved in rRNA processing.
Sequence Mass (Da): 41481
Sequence Length: 368
Subcellular Location: Nucleus
EC: 2.7.1.-
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Q9U3B6 | MEEVVRFECRDSNLEIYVVQPGERLSIFGSCSFLCLAGNASINDYNLPAVSCESSNFMKISAPQRMDVPAILQVFKSGPSYKHARLKFRLKEVAPKNYEKIMEMIGTTEPSVFIFSKILDFAEETVSGVVSNFLIHSSIQKQIILPPHFFISRDDFIIYPQQQEAQLKSQMNRLNKLRNDGQRTTILPIGHKGAGKSNLMRSLVNRCLSNGYEHVYVLDCDIGQSEFTPCGCLSLTKVTSPILGKPHGHQRASFENSFFYGDITVRDINLYMDIFERLFNKFKVISEPGSVCIINSMGWVTDEGAEILDGITRVTDPELF... | Function: Polynucleotide 5'-kinase involved in rRNA processing.
Sequence Mass (Da): 61990
Sequence Length: 549
Subcellular Location: Nucleus
EC: 2.7.1.-
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Q54Z27 | MEINKNDNNNNINNNNINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNQNNNQKNNYRNYKPIKTGTLIQHQILQQTLSNFQTKNKVFQLGSDKLILIFKENETIYFHGTIQARSIIGSVEVYGYTITPQSTTYYPIYSPFCSPTLSITSNNSNNKLYTLKEIIENQLIKIPELVKNKLKENEKQIEIDEPTLAISSIIVLKILDDHCENPKMFTKKKIEIIDSFKLLKGFYPLYQPDFNTQLLTIPNEWLNLINTQFLYNDHCNNNGLSILTCGERNVGKSTFNRILINKLLKKYTHIIFIETDTGQTEFTPSGIMS... | Function: Polynucleotide 5'-kinase involved in rRNA processing.
Sequence Mass (Da): 78065
Sequence Length: 683
Subcellular Location: Nucleus
EC: 2.7.1.-
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A1ZA92 | MLDEHILKEMKLSFQLTEQRELASGRRKPEKPQHPPAVPKKKVISKVASNPAKISETMIQKAQMESPKKSKKNKTAGAKRPLSNNVSNPDSSPSQKRLKKDNTLPKKNPVNKSSNVAAKKSAATSKSAKLPIPKVHSINELAPKKTKVKTPNKTKEASLSKKHKVNGNKSSMKVVQNGKVVEIIGTAAETSDIEMNSLDDWSEEDDYLIESDSENDVVEEIDETFLKDPKIFKVKCKGPEYKLSDILPPFEHDEYQPLLLDGDGSGTVRKIKVFKSAQEETDSDEDDIDYEPEDSDDFGSEEFDSEESDSEDTSSADYDS... | Function: Polynucleotide 5'-kinase involved in rRNA processing.
Sequence Mass (Da): 111208
Sequence Length: 995
Subcellular Location: Nucleus
EC: 2.7.1.-
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Q5SY16 | MADSGLLLKRGSCRSTWLRVRKARPQLILSRRPRRRLGSLRWCGRRRLRWRLLQAQASGVDWREGARQVSRAAAARRPNTATPSPIPSPTPASEPESEPELESASSCHRPLLIPPVRPVGPGRALLLLPVEQGFTFSGICRVTCLYGQVQVFGFTISQGQPAQDIFSVYTHSCLSIHALHYSQPEKSKKELKREARNLLKSHLNLDDRRWSMQNFSPQCSIVLLEHLKTATVNFITSYPGSSYIFVQESPTPQIKPEYLALRSVGIRREKKRKGLQLTESTLSALEELVNVSCEEVDGCPVILVCGSQDVGKSTFNRYLI... | Function: Polynucleotide 5'-kinase involved in rRNA processing. The kinase activity is required for the processing of the 32S precursor into 5.8S and 28S rRNAs, more specifically for the generation of the major 5.8S(S) form. In vitro, has both DNA and RNA 5'-kinase activities. Probably binds RNA.
Sequence Mass (Da): 79... |
Q8NWQ5 | MEKPSREAFEGNNKLLIGIVLSVITFWLFAQSLVNVVPILEDSFNTDIGTVNIAVSITALFSGMFVVGAGGLADKYGRIKLTNIGIILNILGSLLIIISNIPLLLIIGRLIQGLSAACIMPATLSIIKSYYIGKDRQRALSYWSIGSWGGSGVCSFFGGAVATLLGWRWIFILSIIISLIALFLIKGTPETKSKSISLNKFDIKGLVLLVIMLLSLNILITKGSELGVSSLLFITLLAIAIGSFSLFIVLEKRATNPLIDFKLFKNKAYTGATASNFLLNGVAGTLIVANTFVQRGLGYSSLQAGSLSITYLVMVLIMIR... | Function: Multidrug efflux pump that acts independently of NorA and is one of the factors that confers resistance against diverse quinolones and chemical compounds (By similarity). Can facilitate bacterial survival in vivo when overexpressed in an abscess and may contribute to the relative resistance of staphylococcal ... |
P98008 | MSSFNPHLKFQSQAVAKPYFVFALILFVGQVLFGLIMGLQYVVGDFLFPLLPFNVARMVHTNLLIVWLLFGFMGAAYYLIPEESDCELHSPKLAIILFWVFAAAGVLTILGYLFVPYAALAEMTRNDLLPTMGREFLEQPTITKIGIVVVALGFLYNIGMTMLKGRKTVVSTVMMTGLIGLAVFFLFAFYNPENLSRDKFYWWFVVHLWVEGVWELIMGAMLAFVLIKVTGVDREVIEKWLYVIIAMALITGIIGTGHHFFWIGAPTVWLWVGSIFSALEPLPFFAMVLFALNMVNRRRREHPNKAASLWAIGTTVTAFL... | Function: Component of the anaerobic respiratory chain that transforms nitrate to dinitrogen (denitrification). NorB is the catalytic subunit of the enzyme complex. Shows proton pump activity across the membrane in denitrifying bacterial cells. The mononitrogen reduction is probably coupled to electron transport phosph... |
Q51662 | MSEIMTKNMARNVFYGGSIFFILIFGALTVHSHIYARTKAVDESQLTPSVVEGKHIWERNACIDCHTLLGEGAYFAPELGNVMKRWGVQDDPDSAFETLKGWMESMPTGIEGRRQMPRFDLTDEEFRALSDFLLWTGTINTQNWPPNDAG | Function: Component of the anaerobic respiratory chain that transforms nitrate to dinitrogen (denitrification).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16992
Sequence Length: 150
Subcellular Location: Cell membrane
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Q59646 | MSETFTKGMARNIYFGGSVFFILLFLALTYHTEKTLPERTNEAAMSAAVVRGKLVWEQNNCVGCHTLLGEGAYFAPELGNVVGRRGGEEGFNTFLQAWMNIQPLNVPGRRAMPQFHLSEGQVDDLAEFLKWSSKIDTNQWPPNKEG | Function: Component of the anaerobic respiratory chain that transforms nitrate to dinitrogen (denitrification).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 16344
Sequence Length: 146
Subcellular Location: Cell membrane
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B1XCN7 | MSIVVKNNIHWVGQRDWEVRDFHGTEYKTLRGSSYNSYLIREEKNVLIDTVDHKFSREFVQNLRNEIDLADIDYIVINHAEEDHAGALTELMAQIPDTPIYCTANAIDSINGHHHHPEWNFNVVKTGDTLDIGNGKQLIFVETPMLHWPDSMMTYLTGDAVLFSNDAFGQHYCDEHLFNDEVDQTELFEQCQRYYANILTPFSRLVTPKITEILGFNLPVDMIATSHGVVWRDNPTQIVELYLKWAADYQEDRITIFYDTMSNNTRMMADAIAQGIAETDPRVAVKIFNVARSDKNEILTNVFRSKGVLVGTSTMNNVMM... | Cofactor: Binds 3 Fe cations per monomer.
Function: Anaerobic nitric oxide reductase; uses NADH to detoxify nitric oxide (NO), protecting several 4Fe-4S NO-sensitive enzymes. Has at least 2 reductase partners, only one of which (NorW, flavorubredoxin reductase) has been identified. NO probably binds to the di-iron cent... |
E7F0Z8 | MNIFCHALFLLLLGVVSCQNNNRNVKPGGKPAKKPNNPAIEATQHGPEADPNSGLAGAGDSSKETNPGGRGSSQQSASVNKPADDMKLHFLKNTAVTCNDGTAAGFYLKEFKGSKRWLIFLEGGWCCYSKETCDSRYKTIPRLMGSTDWPQTRRGSGLLSAQVDENPHWYNANIVFVPYCSSDVWSGNKAASKPKQGKETEYAFMGSQIIREVIKDLVPKGLKQAKVVMLAGTSAGGTGVLLNIDKVSSLLEQQGAEAQVRGLVDSGWFLESKQQKVPDCPDSASCTPADAIKKGLRLWNGVVPEKCKQQYKRGEDWHCF... | Function: Carboxylesterase that mediates deacylation of target proteins (By similarity). Acts as a regulator of growth cone migration. Does not act as an inhibitor of Wnt signaling .
Sequence Mass (Da): 54411
Sequence Length: 495
Subcellular Location: Secreted
EC: 3.1.1.-
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A0A0D3QS97 | MRILEIFAILLILKEVRPQTKRSHKVNMKTPFQKRKNHHLNTDSRATLMSPADLHSVEHSIVQIRDPTLIPHYDQKSQEDMKLHFLKNTLVTCNDGTTAGYYLRETKGSKRWIIFLEGGWCCYSKETCGVRYDNVKRLMSSSNWPQTRKGTGILSPRQDENPYWWNVNAVFVPYCSSDVWSGNVSKTQDGYAFMGSVIIQEVIRDLVPRGMKQAKSVILAGSSAGGTGVLINIDRVAALVEETTSESVQVRGLVDSGWFLDSRHSKQSDCLDISKCALTEAIKKGLKLWNGILPENCKQQFKKGDEWRCFYGPRLFTSMK... | Function: Carboxylesterase that acts as a key negative regulator of the Wnt signaling pathway by specifically mediating depalmitoleoylation of WNT proteins. Serine palmitoleoylation of WNT proteins is required for efficient binding to frizzled receptors.
Catalytic Activity: [Wnt protein]-O-(9Z)-hexadecenoyl-L-serine + ... |
Q9VUX3 | MAVEQIDKMAAKAGEATNKWIKPQQPLLTLLLLLATFSQLPAVCSSSILDAASLQEKDPLRDTSMNMIQRNYMVMHSASGSGDHSRSLKRANLANTSITCNDGSHAGFYLRKHPSSKKWIVLLEGGWHCFDVRSCRSRWMRLRHLMTSSQWPETRDVGGILSPHPEENPYWHNANHVLIPYCSSDSWSGTRTEPDTSDRENSWRFMGALILRQVIAELIPVGLGRVPGGELMLVGSSAGGMGVMLNLDRIRDFLVNEKKLQITVRGVSDSGWFLDREPYTPAAVASNEAVRQGWKLWQGLLPEECTKSYPTEPWRCYYGY... | Function: Carboxylesterase that acts as a key negative regulator of the Wnt signaling pathway by specifically mediating depalmitoleoylation of WNT proteins. Serine palmitoleoylation of WNT proteins is required for efficient binding to frizzled receptors . Also acts as a regulator of long-range activity of Hedgehog (hh)... |
Q6P988 | MGRGVRVLLLLSLLHCAGGSEGRKTWRRRGQQPPPPPRTEAAPAAGQPVESFPLDFTAVEGNMDSFMAQVKSLAQSLYPCSAQQLNEDLRLHLLLNTSVTCNDGSPAGYYLKESRGSRRWLLFLEGGWYCFNRENCDSRYDTMRRLMSSRDWPRTRTGTGILSSQPEENPYWWNANMVFIPYCSSDVWSGASSKSEKNEYAFMGALIIQEVVRELLGRGLSGAKVLLLAGSSAGGTGVLLNVDRVAEQLEKLGYPAIQVRGLADSGWFLDNKQYRHTDCVDTITCAPTEAIRRGIRYWNGVVPERCRRQFQEGEEWNCFF... | Function: Carboxylesterase that acts as a key negative regulator of the Wnt signaling pathway by specifically mediating depalmitoleoylation of WNT proteins. Serine palmitoleoylation of WNT proteins is required for efficient binding to frizzled receptors .
Catalytic Activity: [Wnt protein]-O-(9Z)-hexadecenoyl-L-serine +... |
Q8R116 | MGGEVRVLLLLGLLHWVGGSEGRKTWRRRGQQPPQPPPPPPLPQRAEVEPGAGQPVESFPLDFTAVEGNMDSFMAQVKSLAQSLYPCSAQQLNEDLRLHLLLNTSVTCNDGSPAGYYLKESKGSRRWLLFLEGGWYCFNRENCDSRYSTMRRLMSSKDWPHTRTGTGILSSQPEENPHWWNANMVFIPYCSSDVWSGASPKSDKNEYAFMGSLIIQEVVRELLGKGLSGAKVLLLAGSSAGGTGVLLNVDRVAELLEELGYPSIQVRGLADSGWFLDNKQYRRSDCIDTINCAPTDAIRRGIRYWSGMVPERCQRQFKEG... | Function: Carboxylesterase that acts as a key negative regulator of the Wnt signaling pathway by specifically mediating depalmitoleoylation of WNT proteins. Serine palmitoleoylation of WNT proteins is required for efficient binding to frizzled receptors.
Catalytic Activity: [Wnt protein]-O-(9Z)-hexadecenoyl-L-serine + ... |
F8U830 | MKSYLILNTLLLSLLKINGFSKSSWFSSKTSLIFDRINKLNDPQSSNSIHSRKYQYFQLKKFPNSTNVRCNDGSIPGYYTRPSTTNCSKKWLIFLEGGWYCFNNNTCESRRRTHYDLFSSEFWSSERQLGGILSNNERINPNFHDYNSVYIPYCSSDLWSGKQLEKTNGLYFHGSRILDTVVDDLTQNQHFKKVHEVAFVGSSAGGIGVLLNIDRLKRRLKKKLKRKVFIHGIVDSAWFLDYPAYRQSNCTHIYECPPENALRNGMKLWNPRIPRRCKKFQGRGREWKCFMGPVIYRHLKNPTFIIQSLFDDAQLQMSKV... | Function: Carboxylesterase that acts as a key negative regulator of the Wnt signaling pathway . Acts by specifically mediating depalmitoleoylation of WNT proteins. Serine palmitoleoylation of WNT proteins is required for efficient binding to frizzled receptors (By similarity). Promotes head regeneration following amput... |
Q9VVR1 | MSETGCRHYQSYVKEHSYDTFRVIDAYFAACVNRDARERKAIHCNCFECGSYGIQLYACLHCIYFGCRGAHITSHLRSKKHNVALELSHGTLYCYACRDFIYDARSREYALINRKLEAKDLQKSIGWVPWVPTTKETNLLLANARRRLVRPNQTIGLRGLLNLGATCFMNCIVQALVHTPLLSDYFMSDRHDCGSKSSHKCLVCEVSRLFQEFYSGSRSPLSLHRLLHLIWNHAKHLAGYEQQDAHEFFIATLDVLHRHCVKAKAEHESKSNSSGSGSGTNSSNSSSSHCYGQCNCIIDQIFTGMLQSDVVCQACNGVST... | Function: Histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. Catalyzes the deubiquitination of histone H2B, thereby acting as a coactivator in a large subset of genes. Required to counteract heterochromatin silencing. Controls the development of neuronal connectiv... |
Q9JKN6 | MMAAAPIQQNGTHTGVPIDLDPPDSRKRPLEAPPEAGSTKRTNTGEDGQYFLKVLIPSYAAGSIIGKGGQTIVQLQKETGATIKLSKSKDFYPGTTERVCLIQGTIEALNAVHGFIAEKIREMPQNVAKTEPVSILQPQTTVNPDRIKQTLPSSPTTTKSSPSDPMTTSRANQVKIIVPNSTAGLIIGKGGATVKAIMEQSGAWVQLSQKPDGINLQERVVTVSGEPEQNRKAVELIIQKIQEDPQSGSCLNISYANVTGPVANSNPTGSPYANTAEVLPTAAAAAGLLGHANLAGVAAFPAVLSGFTGNDLVAITSALN... | Function: Functions to regulate alternative splicing in neurons by binding pre-mRNA in a sequence-specific manner to activate exon inclusion or exclusion . It binds specifically to the sequences 5'-YCAY-3' and regulates splicing in only a subset of regulated exons . Binding to an exonic 5'-YCAY-3' cluster changes the p... |
Q80WA4 | MAAAPIQQNGTHTGVPIDLDPPDSRKRPLEAPPEAGSTKRTNTGEDGQYFLKVLIPSYAAGSIIGKGGQTIVQLQKETGATIKLSKSKDFYPGTTERVCLIQGTIEALNAVHGFIAEKIREMPQNVAKTEPVSILQPQTTVNPDRIKQVKIIVPNSTAGLIIGKGGATVKAIMEQSGAWVQLSQKPDGINLQERVVTVSGEPEQNRKAVELIIQKIQEDPQSGSCLNISYANVTGPVANSNPTGFPYANTAEVLPTAAAAAGLLGHANLAGVAAFPAVLSGFTGNDLVAITSALNTLASYGYNLNTLGLGLSQAAATGAL... | Function: Functions to regulate alternative splicing in neurons by binding pre-mRNA in a sequence-specific manner to activate exon inclusion or exclusion. It binds specifically to the sequences 5'-YCAY-3' and regulates splicing in only a subset of regulated exons. Binding to an exonic 5'-YCAY-3' cluster changes the pro... |
Q9UNW9 | MEPEAPDSRKRPLETPPEVVCTKRSNTGEEGEYFLKVLIPSYAAGSIIGKGGQTIVQLQKETGATIKLSKSKDFYPGTTERVCLVQGTAEALNAVHSFIAEKVREIPQAMTKPEVVNILQPQTTMNPDRAKQAKLIVPNSTAGLIIGKGGATVKAVMEQSGAWVQLSQKPEGINLQERVVTVSGEPEQVHKAVSAIVQKVQEDPQSSSCLNISYANVAGPVANSNPTGSPYASPADVLPAAAAASAAAASGLLGPAGLAGVGAFPAALPAFSGTDLLAISTALNTLASYGYNTNSLGLGLNSAAASGVLAAVAAGANPAA... | Function: Functions to regulate alternative splicing in neurons by binding pre-mRNA in a sequence-specific manner to activate exon inclusion or exclusion . It binds specifically to the sequences 5'-YCAY-3' and regulates splicing in only a subset of regulated exons . Binding to an exonic 5'-YCAY-3' cluster changes the p... |
A0A1W2P872 | MEPEAPDSRKRPLETPPEVVCTKRSNTGEEGEYFLKVLIPSYAAGSIIGKGGQTIVQLQKETGATIKLSKSKDFYPGTTERVCLVQGTAEALNAVHSFIAEKVREIPQAMTKPEVVNILQPQTTMNPDRAKQAKLIVPNSTAGLIIGKGGATVKAVMEQSGAWVQLSQKPEGINLQERVVTVSGEPEQVHKAVSAIVQKVQEDPQSSSCLNISYANVAGPVANSNPTGSPYASPADVLPAAAAASAAAASGLLGPAGLAGVGAFPAALPAFSGTDLLAISTALNTLASYGYNTNSLSLGLNSAAASGVLAAVAAGANPAA... | Function: Functions to regulate alternative splicing in neurons by binding pre-mRNA in a sequence-specific manner to activate exon inclusion or exclusion. It binds specifically to the sequences 5'-YCAY-3' and regulates splicing in only a subset of regulated exons . Binding to an exonic 5'-YCAY-3' cluster changes the pr... |
Q9SRQ6 | MVEETSSGGGSSASPIKTIVVLVQENRSFDHMLGWFKELNPEIDGVSESEPRSNPLSTSDPNSAQIFFGKESQNIDPDPGHSFQAIYEQVFGKPFSDESPYPDPKMNGFVQNAEAITKGMSEKVVMQGFPPEKLPVFKELVQEFAVCDRWFSSLPSSTQPNRLYVHAATSNGAFSNDTNTLVRGFPQRTVFESLEESGFTFGIYYQSFPNCLFYRNMRKLKYVDNFHQYHLSFKRHCKEGKLPNYVVIEPRYFKILSAPANDDHPKNDVVEGQNLVKEIYEALRASPQWNEILFVVVYDEHGGYYDHVPTPVIGVPNPDG... | Function: Possesses specific phosphatase activity toward lysophosphatidic acid (LPA) in vitro. Does not show phospholipase C activity. May play a role in signal transduction and storage lipid synthesis. May be involved in brassinolide-mediated signaling in root development.
Catalytic Activity: a 1-acyl-sn-glycero-3-pho... |
Q9SRQ7 | MIETTKGGSGSYPIKTIVVLVQENRSFDHTLGWFKELNREIDGVTKSDPKSNTVSSSDTNSLRVVFGDQSQYVNPDPGHSIQDIYEQVFGKPWDSGKPDPNPGHPNMSGFAQNAERNKKGMSSAVMNGFKPNALPVYKELVQNFAICDRWFASVPASTQPNRLYVHSATSHGATSNDKKLLLEGFPQKTIFESLDEAGFSFGIYYQFPPSTLFYRNLRKLKYLTHFHQYGIQFKKDCKEGKLPNYVVVEQRWFDLLSTPANDDHPSHDVSEGQKLVKEVYEALRSSPQWNEILFIITYDEHGGFYDHVPTPVDGVPNPDG... | Function: Non-specific phospholipase C (PLC) which assumes major PLC activity during inorganic phosphate starvation. Substrate preference is phosphatidylcholine (PC), but can also hydrolyze phosphatidylethanolamine (PE) with lower efficiency. Has no activity toward phosphatidic acid (PA). Plays an important role in the... |
Q9S816 | MAETKKGSESYPIKTIVVLVQENRSFDHTLGWFKELNREIDGVMKSDQKFNPGFSSDLNSHNVVFGDQSQYVDPNPGHSIRDIYEQVFGKPWDSGHPDPNPGPATMSGFAQNAERKMKGMSSAVMNGFKPDALPVYKELVQNFAICDRWFASVPGATQPNRLFIHSATSHGTTNNERKLLIEGFPQKTIFESLDEAGFTFGIYYQCFPTTLFYRNLRKLKYLTRFHDYGLQFKKDCKEGNLPNYVVVEQRWYDLLLNPANDDHPSHDVSEGQKLVKEVYEALRSSPQWNEILFIITYDEHGGFYDHVPTPLDGVPNPDGI... | Function: Non-specific phospholipase C (PLC) which assumes minor PLC activity during inorganic phosphate starvation. Can hydrolyze both phosphatidylcholine (PC) and phosphatidylethanolamine (PE). Required for normal accumulation of digalactosyldiacylglycerol (DGDG) during phosphate limitation and may contribute to the ... |
Q6F4M8 | MRTGQQYLESLRDGRQVYVGGELIDDVTTHPKTSGYAKAIAEYYDLHLDPEHQDVLTFVDDDGVRKSMHWFLPRSKADAARRRAYHEFWFRHFQGGIFTRPPAGMHVVMYAQIDDPEPWGDNAVVAGGRTISFADNIRSQWQRVTTDDVALSPMFVDVQFDRGRDDALVETPMLSIVEQNDQGIVVRGWKAMGTSLPFVNELLVGNLWRPGQTSDQTVYAIVPVNTPGLSLVCRQSNATPDADPYDHPLSTIGDELDGMAYFDDVFIPWENVQHIGNPDHAKWYPQRQFDWVHIETQIRHAVHAELIVGLALLLTNALGT... | Function: Involved in the degradation of para-nitrophenol (4-NP). Catalyzes both the initial hydroxylation of 4-NP to produce 4-nitrocatechol (4-NCA) and the subsequent oxidative release of the nitro group from 4-NCA to produce 2-hydroxy-1,4-benzoquinone. It can also use 4-nitroresorcinol as substrate with a rate of ni... |
Q6F4M9 | MLEDPMKQNVLQPLDKAEFRNVVGHFASGVTIVTAAHDGVPYGATISAVTSLCDTPPMVLVCLNQKLGTHAAIRKARHFTINILGEDQASLAHTFATPGADKFADVAVHHRQHGPRLAEALAYLTCRVVDDLEGGTHRIFVAEVVEAQAGTGNPLSYYRGRFGHFVPYRNAMWRTTQADNAVSPH | Function: Involved in the degradation of para-nitrophenol (4-NP). Catalyzes both the initial hydroxylation of 4-NP to produce 4-nitrocatechol (4-NCA) and the subsequent oxidative release of the nitro group from 4-NCA to produce 2-hydroxy-1,4-benzoquinone. It can also use 4-nitroresorcinol as substrate with a rate of ni... |
O28597 | MDEKLLKTIAESKYLVALTGAGVSAESGIPTFRGKDGLWNRYRPEELANPQAFAKDPEKVWKWYAWRMEKVFNAQPNKAHQAFAELERLGVLKCLITQNVDDLHERAGSRNVIHLHGSLRVVRCTSCNNSFEVESAPKIPPLPKCDKCGSLLRPGVVWFGEMLPPDVLDRAMREVERADVIIVAGTSAVVQPAASLPLIVKQRGGAIIEINPDETPLTPIADYSLRGKAGEVMDELVRHVRKALS | Cofactor: Binds 1 zinc ion per subunit.
Function: NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form. Deacetylates the N-terminal lysine residue of Alba, the ma... |
Q89LY4 | MRLIASDLRSGVERLGDMIAEAKTIVPFTGAGISTECGIPDFRSPGGIWTRNRPIPFDGFVASQEARDESWRRRFAMEETFAAARPGRGHRALASLYRAGKVPAVITQNIDNLHQASGFAHEHVIELHGNTTYARCVGCGQTYQLDWVKRRFDQDGAPNCTVCDEPVKTATISFGQMMPEEEMQRATALSRACDLFIAIGSSLVVWPAAGFPMMAKRAGARLVIINREPTEQDDIADLVIRHDIGETLGPFVGN | Cofactor: Binds 1 zinc ion per subunit.
Function: NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form.
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
Sequence Mass... |
Q8R9N6 | MDFKILKEKLPQSNLTVVLTGAGISKESGIPTFRGEDGLWKKYNPEELATPWAFQRNPALVWEWYDYRRRIISKAKPNKCHLLIAEFEERFKNVRVITQNVDGLHEAAGSTNVIELHGNIWKVKCTKCDFRGINREVPLSKIPPECPKCGSIVRPDVVWFGEPLPSDKLTEAMELSQRADLFIVIGTSLMVQPAASLPFLALERGAFVVEVSPEETPLSRKAHLFFQMGAVEFAMKFEEKEG | Cofactor: Binds 1 zinc ion per subunit.
Function: NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form.
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[protein] + ... |
Q8FUC8 | MEEGAALEGVVKLLEAGSVLAVTGAGVSTDSGIPDYRSPRGSLNQGRPMTYQEFRFDPVASHRYWARSFVGWRVMADAQPNRTHYALVELERAGLLSGIVTQNVDGLHRRAGSENLVALHGDLATIVCLQCGHREARELLDARLDHLNPGYFDSIALDPSAVNPDGDVTLDDHHVQRFTMAGCARCGSVLLKPDVVYFGEPVPSIRKTRVAQLLDGADAVVVAGSSLAVMSGYRIVIEAQRAGKPVAVINGGPGRADHRVDILWRTRVGPAFDQILDALDL | Cofactor: Binds 1 zinc ion per subunit.
Function: NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form.
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
Sequence Mass... |
A0QDH4 | MTVGRAESPELVAVLAGRRIAVLTGAGISTDSGIPDYRGPESPPSNPMTIRQFTGDPAFRQRYWARNHVGWRHMDDTLPNAGHRALAALEDAAVVTGVITQNVDLLHTKAGSRNVIDLHGSYARVICLGCGDTTSRAALAERLEALNPGFIERTEAIGGLAVAPDADAVVAETASFRYVDCARCAGMLKPDIVYFGESVPKDVVAAAYRLIDESDTLLVAGSSLTVFSGYRFVRHAAARGIPIAIVNRGDTRGDHLATVKVDGGCSELLALLADELSPLPTH | Cofactor: Binds 1 zinc ion per subunit.
Function: NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form.
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
Sequence Mass... |
Q9I4L0 | MRAVVELLAGARRLVIFTGAGVSAESGIPTFRDALGGLWARYDPAALATPAAFADDPALVWGWYEWRRLKVLGVQPNPAHRAIAALSGRIANTRLVTQNVDDLHERAGSRDVLHLHGSLHAPRCATCAAAYRDALPDSVEPEEGRRIEPPRCPACGGQVRPGVVWFGEALPEAALREAFAAACECDLLLSVGTSGVVQPAARIPGLALEHGASVVHVNPQPVRTRHPREHCLVGPAGEVLPELLRRAFPG | Cofactor: Binds 1 zinc ion per subunit.
Function: NAD-dependent lysine deacetylase and desuccinylase that specifically removes acetyl and succinyl groups on target proteins. Modulates the activities of several proteins which are inactive in their acylated form.
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[protein] + ... |
Q8ZU41 | MAVDFTTDELDEVASLIARSSCNVALTGAGVSTASGIPDFRGPQGVWRRVDPEKFEISYFYNNPDEVWDLFVKYLLPAFNVKPNPAHYALAEMERLGKLCAVITQNVDRLHQAAGSKNVIELHGALEYAVCTNCGSKYALAEALKWRKSGAPRCPKCGGVIKPDVVFFGEPLPQDALREAFMLAEMAEVFMAIGTSLAVYPANQLPLVAKKRGAKLVIINADETYYDFFADYIIRGRAEEVLPKLLDRLRGMLF | Cofactor: Binds 1 zinc ion per subunit.
Function: NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form. Deacetylates the N-terminal lysine residue of Alba, the major archaeal chromatin protein and that, in turn, increases Alba's DNA binding affi... |
Q9RL35 | MRMRPTLSWTPGADLPPGTTDLAPVADALRAGGVLVLSGAGISTESGIPDYRGEGGSLSRHTPMTYQDFTAHPEARRRYWARSHLGWRTFGRARPNAGHRSVAAFGRHGLLTGVITQNVDGLHQAAGSEGVVELHGSLDRVVCLSCGVLSPRRELARRLEEANAGFSPVAAGINPDGDADLTDEQVGDFRVVPCAVCGGVLKPDVVFFGENVPPRRVEHCRELVRGASSLLVLGSSLTVMSGLRFVRQAAEAGKPVLIVNRDATRGDRLAVTRVALPLGPALTTVADRLGLRVGDAATA | Cofactor: Binds 1 zinc ion per subunit.
Function: NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form.
Catalytic Activity: H2O + N(6)-acetyl-L-lysyl-[protein] + NAD(+) = 2''-O-acetyl-ADP-D-ribose + L-lysyl-[protein] + nicotinamide
Sequence Mass... |
B0YEV0 | MKITALASAILAVAQGALALPARAPALDITLSQVNNTRIKAVVKNSGTEKITFVHLNFFNDPSPVKKVSLYRNATEVEFTGIKQRLRSDGLSNDALTTLAPGATYEDEFDIASTANLTQGGPVTVRTQGFVPIAMNNKIAGYIPYSSNELELEVDAEKAVAVPASIKPLDRRTKITSSCTGNRATVLNTALRNAASIASKAADAASSGSSALFTEYFKSTSGNIRSAVAARLKAVASEASMNGGGSTTYYCSDPYGYCDSNVLAYTLPSTNEVVNCELFYTLQEVTNDCHGQDQATTIIHEFTHAPGVYPPGTEDLGYGY... | Cofactor: Binds 1 zinc ion per subunit.
Function: Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine. May be involved in virulence (By similarity).
Catalytic Activity: Preferential cleavage of bonds with hydrop... |
E3QWD3 | MKFSIGVSLLATLAGAVNVDMAKRDTSPLNVKLEALGNSGVKAVLTNTGDSDIKLFKTGTFLDKSPVEKVEVFAAGSKIDFDGVRLQISTTGLTEEAFQIVAAGETFEVEFDAAELHDLSKGGAVDIVTQGSFLYADVDSTEIAGTIPFSSNSVHTEINGDEAASVRAAFLAKRTIVQSDCTGTRRTATVNAISRCRALAAAASQAAASGPVARMTEYFKSSTTATRNSVATVFRNIVSECGSTTSGVSRQYCTDVYGACSNGVIAYTVPAQNYMVNCPYFFNNMAAASSTCHAQDQQTTILHEMTHLRQIKGTSDYGGY... | Cofactor: Binds 1 zinc ion per subunit.
Function: Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine (By similarity).
Catalytic Activity: Preferential cleavage of bonds with hydrophobic residues in P1'. Also 3-... |
C1G1N6 | MRRVSGILAVAAFTISAFAGVIQPVAKDARDSAELDVKLTQVDGTVIKAVVTNNGDKDLNILNLNFFRDTAPVKKVSIYSQGVEVPFGGIRVRHKTSDLSSDVITYLAPGESFEDEFDVAITSDLSQGGPVVLQTQGYVPTTDTGGKTLSGVVRYKSNKLEIDVDGTTAAKSFAAMNQFVKIAKLSSCEGSQGDDTRRALRDCASLSTLAAAQAWAGGPKMLEYFKANDDATRKLVADRFTAVALESSNLTGGSTTYYCRDPYNICTNNIIAYTIPAENLISNCPIYYTEFDNVNRKCHGQDRVTTSLHEFTHASSVFSP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine (By similarity).
Catalytic Activity: Preferential cleavage of bonds with hydrophobic residues in P1'. Also 3-... |
Q0UCJ2 | MKVSSQLAVAALASFATAASVDVHKRETPLSVKLAASGNSEVKVTLTNNGEKTLNLLSKGTFLDEQLPVEKVQMYAAGGSDKVAFEGMKVRLLTSGLKADDFVTLAAGETKEITVETAALHSLHEGGDFDVFAKGALPFAEGASTELAGALDYESNKLSMTIDGAQAASVAKALNKRTAIGSSCTGTKLSTVRTALSNCARLANAAASAATSGTKLTTYFKTTSSASTVAARLRAVASDCGSTSSRTTTNCNDPYSGCSSNVLAYTVPSANFITYCPIFFSALPALASTCHGQDQATTALHEETHAPGVYSPGTQDNGYG... | Cofactor: Binds 1 zinc ion per subunit.
Function: Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine (By similarity).
Catalytic Activity: Preferential cleavage of bonds with hydrophobic residues in P1'. Also 3-... |
A7F811 | MSILRAKTSGAQQHEEFRMAFKLSYITGRQDNNVLEVTLAAGQNAVVHATVKNTGTEALNLLKYGTLFDSAPVQKVDVYEGENAVPFKGILRSIQRTDLAPEVFHTLAAGETFETTFNAAEVHDLSSTNYTFIAEGTIPVAPVGSTKISDTIFFKSNTLTIPVDGAAAQSMAKAIPASIDRRTILQSGCSTTQKTQTTQALSYCAQLARAASTAASSGSATKFSEYFKTTAAATRSVVAARLSAVASQCSSLTSGSTTYYCTDIYNYCSSNVLAYTIPSTNEIVNCPLYYSALPTLSGTCHAQDRATTSLHEFTHAPATY... | Cofactor: Binds 1 zinc ion per subunit.
Function: Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine (By similarity).
Catalytic Activity: Preferential cleavage of bonds with hydrophobic residues in P1'. Also 3-... |
C0IPP1 | MQFTALLAALGAPLALAASIPAAAHNHTMIDVQLAATGNSMIKATITNTGDRTLNLLKFNTIMDEHPTRKVMVYQDGAEVQFTGMLPRYKMSDLTPEYFVNLGPKASVEHSFDLAATHDLSRGGKITVKAHGMVPTAEENATTITGHTLYESNELTMDVDGKQAAAVEQAMGGDDSTGVIDKRSNIVTSSCRGSQLRVLQTALSNASRLSRAAASAAQRNPSKMREYFKTADKPHRPEGASRFLSVARESSSGSTGRTTYYCNDNRGGCHPGVLAYTLPSRNQVFNCPSYYQLPALNNRCHGQDQATTTLHELTHNPAVV... | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable secreted metalloprotease that shows high activities on basic nuclear substrates such as histone and protamine (By similarity). May be involved in virulence.
Catalytic Activity: Preferential cleavage of bonds with hydrophobic residues in P1'. Also 3-Asn-|-Gln-4 ... |
Q9P780 | MILRFRSKRGMARAEFQPTDTLAMLSAKILSDILKNDYSPENVSLCQNESDQGVIFSNLNDQTLQDAGLTHGQMLYLRLGTPNSDIASSNNEPALTVTGAPKQVSTPDVSEKKPSMPVIQDPIDDSLEKEDGLIRRSMTSLCRHGPKGMCDYCSPLEPYDESYRQENKIKHLSFHAYLRKINSNVNKYASSQSFIPPLEEPSFTVKEKCPSGHPPWPAGICTKCQPSTVMLNLQPFRVIDHIEFASPGIVDSFLNKWRQSGFQRIGYTYGHFEQYNNVPLGIKGVIEAIYEPPQVSEADGVTLEEWADEALVEQVATACG... | Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 63619
Sequence Length: 572
Su... |
A7EGK5 | MLLRFRGPDGTVRIAVEANETFGQLGDKLLKLLPENLDPRTLTLSNAPSGGEVKLLMEIARAKVSQIGLKNGDMVFINYKLLDNLPNGNSTTSTSTTHSSHLTSSTNRLNGSAVLPESIPVNVPAQAVTSPSEKIKNPWEVVQQSDLDNRLDKKDGKIPRKRDTKMCRHGEKGMCDYCMPLEPFNAQYLAEKKIKNLSFHSYLRKINSATNKPELGSSFMPPLTEPYYRVKKNCPSGHPQWPEGICTKCQPSAITLQPQEFRMVDHVEFAQASLVENLLVFWRSTGAQRFGYLYGRYEEYTEVPLGVKAVVEAIYEPPQV... | Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 67728
Sequence Length: 611
Su... |
A7TTC4 | MLLRFRSKIGMNRVSCEATDLFGDVVENWVKEVGLNVDPGTVVVGNDPGSAKEPVSNIAGRSVEEMGLKHGDIVYIEYSDSSGSNEGQSVPVNAVGAGSAVISELPVDVLLEKEDGLIKRTRSSLCKHGDKGMCEYCSPLPPWDKEYHAENKLKHISFHSYLKKLNEATNKKSSGSSYIPPLSQPDYKINKRCNNGHEPWPRGICSKCQPSAITLQQQEFRMVDHVEIQQSDLINQFIESWRATGMQRFGYLYGSYEKYDSTPLGVKAVVHAIYEPPQHDEQDGLTMDLEQVEEEMQKVDQIAMSMGLLRVGLIFSDLTD... | Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 63620
Sequence Length: 568
Su... |
Q6C619 | MILRFRSKKGTLRAEAQPTDLFDVAFKKLTEDLPDIDPATITLATSPTGKQEPASRLLGKTVQKLGLNHGDMLFVSYTDSAPRAAVEAVTAETAPQMTAAHIRDATKQLPVDDYLEKQDGKIKRQLSALQQRKFGSRGMGEDTLPVDPWDEEYLKEQKIKHMSYHAYVKKLNSQANKKNGGGYIAPLNVSDFGVSKSCTGAHAPWPEGICSRCQPSAITLQSQPFRMVDHVEFAESGMINSFIEPWRQSGTQRIGWMYGHYEPYELVPLGIKAVVEAIYEPAQSGEYDGITITEITQADGQPQPPHIATAEACGLVPLGV... | Function: Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) RNA out of the nucleus. Has a role in the endoplasmic reticulum-associated degradation (ERAD) pathway (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 61600
Sequence Length: 563
Su... |
P33755 | MLIRFRSKNGTHRVSCQENDLFGTVIEKLVGNLDPNADVDTFTVCEKPGQGIHAVSELADRTVMDLGLKHGDMLILNYSDKPANEKDGVNVEIGSVGIDSKGIRQHRYGPLRIKELAVDEELEKEDGLIPRQKSKLCKHGDRGMCEYCSPLPPWDKEYHEKNKIKHISFHSYLKKLNENANKKENGSSYISPLSEPDFRINKRCHNGHEPWPRGICSKCQPSAITLQQQEFRMVDHVEFQKSEIINEFIQAWRYTGMQRFGYMYGSYSKYDNTPLGIKAVVEAIYEPPQHDEQDGLTMDVEQVKNEMLQIDRQAQEMGLS... | Function: Substrate-recruiting cofactor of the CDC48-NPL4-UFD1 segregase . Assists CDC48 in the dislocation of misfolded, polyubiquitinated ERAD substrates that are subsequently delivered to the proteasome for degradation . Involved in the import of nuclear-targeted proteins into the nucleus and the export of poly(A) R... |
Q5XGL8 | MAFTGKRLKGLIAATFTPMTPNSDINLLVIEQYVDYLVQKQHIRNIFVNGTTGEGMSLSICERKRLTEEWVKHARGKMDNVIVHVGCLGLSDSKDLAAHAASCGADAISAVCPSFLKPANLDALVLYLKDVASAAPSLPFYYYHIPKLTGITYQIYELLGKVKENIPSFRGVKFSDVNLMDFSLCVSEYKEFDCLYGVDEQLLGALAFGAHGAVGSTYNYLGNKNGDMLEAFEAGNLQKARKIQCSLQEFLYFVFDMAHFSGSKAN | Function: Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate. It prevents sialic acids from being recycled and returning to the cell surface. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway (By similarity).
Catal... |
O00476 | MATKTELSPTARESKNAQDMQVDETLIPRKVPSLCSARYGIALVLHFCNFTTIAQNVIMNITMVAMVNSTSPQSQLNDSSEVLPVDSFGGLSKAPKSLPAKSSILGGQFAIWEKWGPPQERSRLCSIALSGMLLGCFTAILIGGFISETLGWPFVFYIFGGVGCVCCLLWFVVIYDDPVSYPWISTSEKEYIISSLKQQVGSSKQPLPIKAMLRSLPIWSICLGCFSHQWLVSTMVVYIPTYISSVYHVNIRDNGLLSALPFIVAWVIGMVGGYLADFLLTKKFRLITVRKIATILGSLPSSALIVSLPYLNSGYITATA... | Function: Transports organic anions in a voltage-driven, multispecific, manner, on the apical side of renal proximal tubule . In particular, participates in the secretion of urate from the cell into the lumen . Urate is the end product of purine metabolism . May have roles in the metabolism and secretion of estrone sul... |
C8VEJ5 | MVATPDDPRAQTIVDLFNGQGSAPAPFDVLTSALSFPTRDQEQWWRKTGPMFGQMLASSGYTLDQQYRHLTFYYNQLVPRLGPHPATFHSSLTVSGLPMEFSINYQQKGAHPMVRIGAEPIDSFSGTERDPFNQIPPAEMVNHFSRAGVKGFDPELYAYFEPKHSLTREQQARLPKEVPGGDKLKTQYAFGFDFKGDEVSLKGYSYPGLKATMAGQEVAKLVGDGVKDLKNQGKLDCTEAWAAVEAYMTELNGWGYHNLWAWDYVSPAKSRLKFYSFVMDVVDKTKLEELWTLNGRATSPAHQEGLRHLKELWDIIDLKN... | Function: Nonribosomal peptide synthase involved in the synthesis of nidulanin A and derived compounds . Nidulanin A is a tetracyclopeptide with the sequence L-Phe-L-Kyn-L-Val-D-Val and an isoprene unit N-linked to the amino group of L-kynurenine . The NRPS nlsA is responsible of the synthesis of the cyclopeptide and t... |
Q9Y639 | MSGSSLPSALALSLLLVSGSLLPGPGAAQNAGFVKSPMSETKLTGDAFELYCDVVGSPTPEIQWWYAEVNRAESFRQLWDGARKRRVTVNTAYGSNGVSVLRITRLTLEDSGTYECRASNDPKRNDLRQNPSITWIRAQATISVLQKPRIVTSEEVIIRDSPVLPVTLQCNLTSSSHTLTYSYWTKNGVELSATRKNASNMEYRINKPRAEDSGEYHCVYHFVSAPKANATIEVKAAPDITGHKRSENKNEGQDATMYCKSVGYPHPDWIWRKKENGMPMDIVNTSGRFFIINKENYTELNIVNLQITEDPGEYECNATN... | Function: Probable homophilic and heterophilic cell adhesion molecule involved in long term potentiation at hippocampal excitatory synapses through activation of p38MAPK. May also regulate neurite outgrowth by activating the FGFR1 signaling pathway. May play a role in synaptic plasticity (By similarity). Also acts as a... |
P97300 | MSGSSLPGALALSLLLVSGSLLPGPGAAQNAGFVKSPMSETKLTGDAFELYCDVVGSPTPEIQWWYAEVNRAESFRQLWDGARKRRVTVNTAYGSNGVSVLRITRLTLEDSGTYECRASNDPKRNDLRQNPSITWIRAQATISVLQKPRIVTSEEVIIRESLLPVTLQCNLTSSSHTLMYSYWTRNGVELTATRKNASNMEYRINKPRAEDSGEYHCVYHFVSAPKANATIEVKAAPDITGHKRSENKNEGQDAMMYCKSVGYPHPEWIWRKKENGVFEEISNSSGRFFITNKENYTELSIVNLQITEDPGEYECNATNS... | Function: Probable homophilic and heterophilic cell adhesion molecule involved in long term potentiation at hippocampal excitatory synapses through activation of p38MAPK. May also regulate neurite outgrowth by activating the FGFR1 signaling pathway. May play a role in synaptic plasticity (By similarity). Also acts as a... |
P97546 | MSGSSLPGALALSLLLVSGSLLPGPGAAQNAGFVKSPMSETKLTGDAFELYCDVVGSPTPEIQWWYAEVNRAESFRQLWDGARKRRVTVNTAYGSNGVSVLRITRLTLEDSGTYECRASNDPKRNDLRQNPSITWIRAQATISVLQKPRIVTSEEVIIRDSLLPVTLQCNLTSSSHTLMYSYWTKNGVELTATRKNASNMEYRINKPRAEDSGEYHCVYHFVSAPKANATIEVKAAPDITGHKRSENKNEGQDAMMYCKSVGYPHPEWMWRKKENGVFEEISNSSGRFFIINKENYTELNIVNLQITEDPGEYECNATNS... | Function: Probable homophilic and heterophilic cell adhesion molecule involved in long term potentiation at hippocampal excitatory synapses through activation of p38MAPK . May also regulate neurite outgrowth by activating the FGFR1 signaling pathway . May play a role in synaptic plasticity . Also acts as a chaperone fo... |
Q62443 | MLAGRAARTCALLALCLLGSGAQDFGPTRFICTSVPVDADMCAASVAAGGAEELRSNVLQLRETVLQQKETILSQKETIRELTTKLGRCESQSTLDSGPGEARSGGGRKQPGSGKNTMGDLSRTPAAETLSQLGQTLQSLKTRLENLEQYSRLNSSSQTNSLKDLLQSKIDDLERQVLSRVNTLEEGKGGPKNDTEERAKIESALTSLHQRISELEKGQKDNRPGDKFQLTFPLRTNYMYAKVKKSLPEMYAFTVCMWLKSSAAPGVGTPFSYAVPGQANELVLIEWGNNPMEILINDKVAKLPFVINDGKWHHICVTWT... | Cofactor: Binds 2 calcium ions per subunit.
Function: May be involved in mediating uptake of synaptic material during synapse remodeling or in mediating the synaptic clustering of AMPA glutamate receptors at a subset of excitatory synapses.
Sequence Mass (Da): 47117
Sequence Length: 432
Subcellular Location: Secreted
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P47971 | MLAGRAARTCALLALCLLGSRAQDFGPTRFICTSVPVDADMCAASVAAGGAEELRSNVLQLRETVLQQKETILSQKETIRELTTKLGRCESQSTLDAGPGEARSGGGRKQPGSGKNTMGDLSRTPASETLSQLGQTLQSLKTRLENLEQYSRLNSSSQTNSLKDLLQSKIDDLERQVLSRVNTLEEGKGGPKNDTEERAKIESALTSLHQRISELEKGQKDNRPGDKFQLTFPLRTNYMYAKVKKSLPEMYAFTVCMWLKSSAAPGVGTPFSYAVPGQANELVLIEWGNNPMEILINDKVAKLPFVINDGKWHHICVTWT... | Cofactor: Binds 2 calcium ions per subunit.
Function: May be involved in mediating uptake of synaptic material during synapse remodeling or in mediating the synaptic clustering of AMPA glutamate receptors at a subset of excitatory synapses.
PTM: Glycosylated.
Sequence Mass (Da): 47216
Sequence Length: 432
Subcellular L... |
P47972 | MLALLAASVALAVAAGAQDSPAPGSRFVCTALPPEAVHAGCPLPAMPMQGGAQSPEEELRAAVLQLRETVVQQKETLGAQREAIRELTGKLARCEGLAGGKARGAGATGKDTMGDLPRDPGHVVEQLSRSLQTLKDRLESLEHQLRANVSNAGLPGDFREVLQQRLGELERQLLRKVAELEDEKSLLHNETSAHRQKTESTLNALLQRVTELERGNSAFKSPDAFKVSLPLRTNYLYGKIKKTLPELYAFTICLWLRSSASPGIGTPFSYAVPGQANEIVLIEWGNNPIELLINDKVAQLPLFVSDGKWHHICVTWTTRD... | Cofactor: Binds 2 calcium ions per subunit.
Function: Likely to play role in the modification of cellular properties that underlie long-term plasticity. Binds to agar matrix in a calcium-dependent manner (By similarity).
Sequence Mass (Da): 47042
Sequence Length: 431
Subcellular Location: Secreted
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P97738 | MLALLTAGVALAVAAGQAQDNPIPGSRFVCTALPPEAARAGCPLPAMPMQGGALSPEEELRAAVLHWRETVVQQKETLGAQREAIRELTSKLARCEGLAGGKARGTGATGKDTMGDLPRDPGHVVEQLSRSLQTLKDRLESLELQLHTNASNAGLPSDFREVLQRRLGELERQLLRKVAELEDEKSLLHNETSAHRQKTENTLNALLQRVTELERGNSAFKSPDAFKVSLPLRTNYLYGKIKKTLPELYAFTICLWLRSSASPGIGTPFSYAVPGQANEIVLIEWGNNPIELLINDKVAQLPLFVSDGKWHHICITWTTR... | Cofactor: Binds 2 calcium ions per subunit.
Function: Likely to play role in the modification of cellular properties that underlie long-term plasticity. Binds to agar matrix in a calcium-dependent manner.
Sequence Mass (Da): 47429
Sequence Length: 432
Subcellular Location: Secreted
|
O95502 | MKFLAVLLAAGMLAFLGAVICIIASVPLAASPARALPGGADNASVASGAAASPGPQRSLSALHGAGGSAGPPALPGAPAASAHPLPPGPLFSRFLCTPLAAACPSGAQQGDAAGAAPGEREELLLLQSTAEQLRQTALQQEARIRADQDTIRELTGKLGRCESGLPRGLQGAGPRRDTMADGPWDSPALILELEDAVRALRDRIDRLEQELPARVNLSAAPAPVSAVPTGLHSKMDQLEGQLLAQVLALEKERVALSHSSRRQRQEVEKELDVLQGRVAELEHGSSAYSPPDAFKISIPIRNNYMYARVRKALPELYAFT... | Cofactor: Binds 2 calcium ions per subunit.
Function: May be involved in mediating uptake of synaptic material during synapse remodeling or in mediating the synaptic clustering of AMPA glutamate receptors at a subset of excitatory synapses.
PTM: Ubiquitinated by a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-prot... |
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