ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q7VRD3 | MINNRSVIIGIVVGENSGDILGVGLIRSLKKCFKKVQFFGIGGFRMRSENMECWYDISELSIMGITGVIFRLPKLLNMRRELIKRFLKLKLNIFIGIDFPDFNISLEKRLKKYGITTIHYVSPSIWAWRSNRVFALKEATHNVLLLFPFEKSIYARCGIPNQFIGHPLADEIPLYPNKIALRQKFDIPSNRCCLAILPGSRPKEIQILTKIFMHCAKLLQDTIPNLEILIPLHDTDLINQFVTLTSFISVKFRVLHTLTAWEVMAAADAALLTSGTATLECMLAKCPMVVAYRMNPVIFMLIRHLIKVKWISLPNLLAGK... | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosam... |
Q493B9 | MSSIVPSMHNNRTIIIGIVAGEASGDILGAGLIRTLKKYLKKVRFFGIGGPCMQSEDMKSWYNIEELSVMGFAEIVMKLPRLLYIRRNLARRFINLKPDVFIGIDSPDFNISLENRLKKRGIRTIHYVSPSVWAWRKKRIFALKKATDNILVILPFEKKIYDHFNIPCQFIGHSLADQIPLNPNKVSARQKLGIPHDVYCLAVLPGSRIREIKMLAHDFLVCAKLLKNNFPNLEILVPLTNQTSIKKFISVASTSVKYRVLSNQSAWEIMMAADASLVTAGTATLECMLVKCPMVVAYRMHPLTFMLAKHFINIPWISLP... | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosam... |
Q7WJ81 | MSLRIGMVAGEPSGDLLAGRIIAGLQARAPGVHCAGIGGPQMAARGFEAWHPMHALTVFGYIDAFKRIPSLLSTYGDVKRRLLAEPPSVFVGIDAPDFNLRLEHQLRQAGTPTVHFVGPSIWAWRYERINKIRAAVSHMLVLFPFEEALYRKEGIPVTYVGHPLAGVIPMQPDRAAARARLGIDADARVLAILPGSRSSEIRLLAPRFLQAAAELVRRDPRLQCVVPMVNPQRRAEFEAIAAQHPVPGLRCVTAAEGQGETPVAWSVMEASNAVLVASGTATLETALYKRPMVISYVLSPWMRRIMAWKSGQQRPYLPWV... | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D... |
Q89KQ7 | MMQGRDPKRKIFLIATEESGDRLGSALMKVLRQRLGDGVQFEGVGGRTMAREGLETLFPIEELSIVGFAAVVQQLPKILRLIRETADAVLEAVPDALVIIDSPDFTHRVARRVRARNPAIPIVDYVSPQLWAWRPGRARTMLGYVDHVLGLLPFEPEEYRKLGGPPCSYVGHPLIEQLGSLRPNAEEQKRRNSELPVLLVLPGSRRSEIRHHIEVFGAALGRLQAEGRAFELMLPTMPHLEATVREGIASWPVKPQIVIGEAEKRAAFRIAHAALAKSGTVTLELALSGIPMVTAYRVGAIEAFILRRAIRVSSVILANL... | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D... |
Q02AZ6 | MPKILVSAGEASGDLYASLVVQELRRIMPDAEFFGCTGPRLRAAGVRTIVDSADLAVVGLIEVVAHIPRIYGEFRKLLRAAREERPLLAILTDSPDFHLRVARKLHRQEVPVVYLVAPQAWAWRRGRVREMRRTIRRLLCIFPFEEEFFRRYGVPATYIGHPLAGLVHPALSREEFFKKHRLAAERPLVSVLPGSRRGEAARHIPALLDAVDRIYREQAVNVVLPASATTGVAFFQERMGNSPIRVIEGESWDAMAHSDLALAASGTVTVEAALLGTPMVTFYKVTGVSWLAGKFLVDIPFYSMVNLIAGRAVVPELMQS... | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D... |
Q2LVL8 | MNSKLVLIVAGEASGDLHGASLVGAMVKREPGIRFYGIGGVNLKTAGVDLWADAADMAVVGLTEVASKLRGILTVMHRLKKSMQLLKPDLVILIDYPDFNLPLARSAKKNGIPVFYYISPQVWAWRKGRLRTISGLVDRMAVILPFEEPLYRQAGVDVSFVGHPLLDVVQATSSRDETLRMFGLREDVTTVALLPGSRKGEVTRLLPVMLKAARILTENICPVQFLLPMANTLDETWMKDQIAKADPPGVRLIRGATYDAVAAADAAVVVSGTATLETALLGTPLIVIYKVSALSYLIGRMLISVDHIGLVNIVAGKTVA... | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D... |
Q3A550 | MHEVKQPRRIMVVTGEASGDLHGAHLIEAAGKVDPGLSFFGVGGACMAKAGCEILIPGEDLAVMGLVEVLGHFPTIWRAFRKLKKILHGPQRPDALVLIDFAEFNLLLAAQAKKAGVPVLYYVSPQVWAWRRGRVRRIASVVDRLAAIFPFEPELYQGLDIDVEYVGHPLLDEFAITCERDAFLRRLGLDPARQVIGLFPGSRKNELKYIAETILQSAVKLREKHPDAQFLLPVASSFRRQDIEALVAPYGLPVTVVDEPIYDVINACDAVISVSGTVTLQVALVGTPMAIVYKMAPLSFAIGKRLIRVPHIGLANIVAG... | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D... |
Q57310 | MRIFISTGEVSGDLQGSLLVGALRQQAEEQNLELELVGLGGEKMAAAGLTLLANTAAIGSVGLTESLRFIIPTWQIQQRVKRYLKTNPIDLLVLIDYMGPNLTIANYLRKTYPNLPILYYIAPQAWVWSPTKRETAQIMAVTDRLLAIFPGEAEFFQKQGLDVTWVGHPLLDRITKEAPSRGSAREKLGIDHNETVITLLPASRIQELRYLLPSICGAAQQLQSQLPNVKLLLPVSLKDYQPQIEQTLKEFNLTVQLLEGKETLTAIAAADLAITKSGTVNLEIALLNVPQVILYRVSPLTMAIARRIFKFNLPFVSPTN... | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D... |
Q3SKM8 | MVAGEASGDLLGAHFFDALKKNRPGLTAAGIAGPRMVEAGVKAIYPSEKLAVNGYVEVLRHLPELLWIRARITRHFLRERPRVFVGIDAPDFNFTLEAALKRAGVPTIHFVSPSIWAWRPERIERIKQAVSHMLVVFPFEEAIYRDAGIPVSYVGHPLADVIPLQAPTGAARATLGLGDGPIVALLPGSRLSEVDRHARLMLEAAMQVRAKEMDVRFVLPAASEAARERIARAAQGLDLPLTVLAGRSHQALAACDVAVVASGTATLEAALFKKPMVITYRVPALTARLMRKKALLPWIGLPNILARDFVVPERVQEAAT... | Function: Condensation of UDP-2,3-diacylglucosamine and 2,3-diacylglucosamine-1-phosphate to form lipid A disaccharide, a precursor of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a lipid X + a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D... |
Q12EK9 | MLAQRTLKSLTKAVGVGLHSGQRVELTLRPAPPDTGIVFRRVDLPQPVDIVISAQAVTDTRLASTISAGGAKVHTVEHLMSACAGLGIDNLYIDITAEEVPILDGSASSFVFLLQSAGIELQSAPKRFIRVLKPVEVREGEGATAKWARLSPYEGYKLSFEIDFDHPAVDSTGQRVEFDLSSGSYSRDIARARTFGFTKDVEMMRANGLALGGGLDNAIVMDDYKVLNSEGLRYNDEFVKHKILDAMGDLYLLGKPLLAAYSAFRSGHAMNNKLLRELLAHQDAYEVVTFADEKRAPQGFATLARAW | Function: Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis.
Catalytic Activity: a UDP-3-O-[(3R)-3-hydroxyacyl]-N-acetyl-alpha-D-glucosamine + H2O = a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + acetate
S... |
P21645 | MPSIRLADLAQQLDAELHGDGDIVITGVASMQSAQTGHITFMVNPKYREHLGLCQASAVVMTQDDLPFAKSAALVVKNPYLTYARMAQILDTTPQPAQNIAPSAVIDATAKLGNNVSIGANAVIESGVELGDNVIIGAGCFVGKNSKIGAGSRLWANVTIYHEIQIGQNCLIQSGTVVGADGFGYANDRGNWVKIPQIGRVIIGDRVEIGACTTIDRGALDDTIIGNGVIIDNQCQIAHNVVIGDNTAVAGGVIMAGSLKIGRYCMIGGASVINGHMEICDKVTVTGMGMVMRPITEPGVYSSGIPLQPNKVWRKTAALV... | Function: Catalyzes the N-acylation of UDP-3-O-(hydroxytetradecanoyl)glucosamine using 3-hydroxytetradecanoyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell. Prefers (3R)-3-hydroxytetradecanoyl-ACP over... |
B2KAU6 | MQISLEELVKITGGELRGNKDFQITAPCSIDNPKEDAVCYFSDGSKAESISSIKAGCFILPSKIKETFKTDKNVIFADNPEWAFTLFLRHYDSSKPKFDRGVHPTAVIGKNVVLGNNITVGAYSVIEDDVTLGDNTVIYPHVYIGRRTFVGKDCILYPNVVVREECIIKDRVIIEAGATIGTDGFGFVLVNYKHEKIPQVGNVIIESDSEIGANTTIDRAKIDSTVIGVNVKVDNLTQLAHNVKVGQGSIIISQVGVAGSTEIGRGVVLAGQVGVAGHIKIGDGVQVGAQSGIMQDIPAGKKMFGTPVRDYMETLKLYAA... | Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydrox... |
Q8R6D9 | MEYRVTDIITLLNAEYKGEVVEKVSKLSPFFHSDEKSLTFAADEKFLKNLSQTKAKVIIVPDIDLPLIEGKGYIVVKDSPRVIMPKLLHFFSRNLKKIEKMREDSAKIGENVDIAPNVYIGHDVVIGNNVKIFPNVTIGEGSIIGDGTVIYSNVSIREFVEIGKNCVIQPGAVIGSDGFGFVKVNGNNTKIDQIGTVIVEDEVEIGANTTIDRGAIGDTIIKKYTKIDNLVQIAHNDIIGENCLIISQVGIAGSTTIGNNVTLAGQVGVAGHLEIGDNTMIGAQSGVPGNVEANKILSGHPLVDHREDMKIRVAMKKLPE... | Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydrox... |
Q74AT5 | MAVSKTLQELADYLGGTLVGDGSRQIVGVASLDDATDSQITFLANPRYAPKVASTRAGAVILPPGAERHNHNAIMVPNPYLAFARLLTLFYVAPRAARGVMDGAHVGRNVKLGSEITIHPGAVVGDNVTIGDRVTLHPGVVLYEGVTVGDDVTLHANVTVYQGCRIGNRVTIHGGTIIGSDGFGYAPDGDGWYKIPQLGNVVIEDDVEIGANAAIDRAALASTVIGKGTKVDNLVMIAHNCVIGENCMIVSQVGISGSTKLGRRVTLGGQVGVAGHLEIGDNAMIGAKSGVPGNVPSGTIMSGIPAFDHREWLRASAVVP... | Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydrox... |
Q0BTL2 | MSVQEVVGDPRFFARSGPYDVAAVAEAVGASIPADCTLSLTGVAPLQIAGPSEVSFLDNRRYADALEQTRAGAVIIKADMVDRVPAGVIALVVPEPYLAWARVAALFYPLPPVQPGIHPSAVVDETACIDPSAQIGPLAVIEAGVEIGPDCRIAAHAVIGAGVKMGRSCRIGSHASLSHAILGDRVYVYPGVRIGQDGFGFAPSSEGFVTVPQLGRVVLENDVEVGANSTIDRGSMHDTVIGAGSRLDNLVMIAHNVRMGRACVIVSQVGISGSTTLGDHVVLAGQAGLIGHLKIGSGARIGAQAGVMADVPAGAEIVGS... | Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydrox... |
Q7VM24 | MAVFRLSELAEQIGATLKGNADLAITSIAALNNAEPTHITFISNAKYRSQLSQSKAGAIIVTAEDVEFCQATQNLLIVKDPYLAYALLAQYMDDLPKSANEISESAVISATAKLGKNVSIGANVVIESGVELADDITIGAGCFIGKNTKIGARSHLWANISVYHNVEIGSDCLIQSSAVIGSDGFGYANDKGRWIKIPQTGGVIIGNRVEIGACTCIDRGALDPTIIEDNVIIDNLCQIAHNVHIGFGTAIAGGVILAGSLKIGRFCQIGGASVINGHMEICDGAIITGMSMIMKPITEKGVYSSGIPAQTNKEWRKTAA... | Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydrox... |
Q2SBQ8 | MGKTDLSYTLADIAFRIGAELRGDGSVEVKGLATLQKAQAGQISFLANKNYLKHLKDTCASAVIIPSSFADQCSTNVLVMENSYFGYALCSQLFSPQWWSMSGISPSAAISESAKLGAGVTIGANVVIEEDAEIGEGAVIGPGCYIGAGSIIGAKTQLRPNVTVYHGVNIGARALIHSGAVIGSDGFGFAPNKGDWAKIAQLGGVVIGDDVEIGANTTIDRGALDDTVIETGAKLDNQIQIAHNVKVGAYTVIAACVGVSGSSSIGKHCMIGGGVGIAGHLEITDQVQITGMTLVTHNIKEPGVYSSGTAVEPNASWRKN... | Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydrox... |
A1WT71 | MTSAMTVQELAARLGARLAGDGERPVCRAATLLGAGGDAVSFCTSKRHLPELRRSGAAAVLVRAEHEGDCPGTALVVEDPYLAFIEVVELLHPEPSAPPGIHPGAVVASDVVLGDGVSVGANAVIEAGVELGAGSTVAPGAFIGPGARLGTGSWLGPNAVLAGGCRTGERVRIHAGAVIGADGFGYAPLPDGQGWRKVPQIGGVDIGDDVEIGANATVDRGALEDTVIEAGVKLDDHVHIAHNCRVGARTVIAGGTLVAGSTTIGRDCLIGGLVAITDHIRIADGVSLMGMTGVTGSIRESGAYASPLPAQPVRQWRRNT... | Function: Catalyzes the N-acylation of UDP-3-O-acylglucosamine using 3-hydroxyacyl-ACP as the acyl donor. Is involved in the biosynthesis of lipid A, a phosphorylated glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydrox... |
Q1QVV3 | MTTLLISDLHLHTGQPDITRGFLDYLERDARHADTLYLLGDIFEAWIGDDYLGDLERQVIEALRRLSDAGTQLYFMHGNRDFLVGEDFAAAAGATLLDDPCLATLGRQTVLLMHGDSLCTGDEEYMKFRAMARDPEWQAQILALPIEQRLELAKSLRMQSSDANTQKADAIMDVTPAEVEAIMREHGVSTLIHGHTHRPAVHEFTLDGQPAQRIVLGDWRPGRGWEVRVEDDAPPRLREFAFQARA | Cofactor: Binds 2 Mn(2+) ions per subunit in a binuclear metal center.
Function: Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated gl... |
Q7NT75 | MAIHFISDLHLADDTPALNQLFLDTLAAWRGRIAALYILGDLFEYWVGDDDDSPYLAAPLAAMRDFAAQTPLYVMRGNRDFLLGAGFEARSGARLLDDPTLIEAHGQRILLSHGDALCTDDAAYQQFRAMSRNPQWQQAMLAKPLAERHAIARHARAQSEMNKQQTGLTDISDVTENAVRELLAAHGWPTLIHGHTHRPAHHLHDASSRWVIQDWHGGRGGYLLLDDGGIRSLPLGN | Cofactor: Binds 2 Mn(2+) ions per subunit in a binuclear metal center.
Function: Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated gl... |
A9KBJ4 | MRHTLFISDLHLEEETPSITAHFLYFLKHQAPKADAIYILGDFFEAWIGDDNQTPFNRKIIESLQTLARTKPTYFMRGNRDFLIGQRFAAMTGVSLLEDPSVIQLYNKPVLLMHGDSLCTLDHKHQAYRRKIMKPWVQKLMLSLPLSLRRKLAKKFREQSRRHNRTLSYGIKDVTPEEVNRVMKEQNVELLIHGHTHRPAIHDLTINGNPTKRIVLGAWHHGGSVLRYAQDGSFELQAFKIDL | Cofactor: Binds 2 Mn(2+) ions per subunit in a binuclear metal center.
Function: Hydrolyzes the pyrophosphate bond of UDP-2,3-diacylglucosamine to yield 2,3-diacylglucosamine 1-phosphate (lipid X) and UMP by catalyzing the attack of water at the alpha-P atom. Involved in the biosynthesis of lipid A, a phosphorylated gl... |
Q2T0K1 | MSARPGLLARAEARLTREWQRRGALAWALTPFACAFGAIAALRRAAYARGWKARVDCGVPVVVVGNVTVGGTGKTPTVIALVDALRAAGFTPGVVSRGYGAKIVAPTAVTPASAPQQAGDEPLLIARRTLAPVWVCPDRVAAVRALKAAHPEVDVVVSDDGLQHYRLARAVEIVVFDHRLGGNGFLLPAGPLREPLSRRRDATLVNDPYSRALPPWPDTFALSLAPGDAWHLARPSRRKPLAQFAGERVLAAAGIGAPERFFATLRAAGVTPATRALPDHYAFATNPFVDDHFDAILITEKDAVKLGTSWRDARIWVVPV... | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 36555
Sequence Length: 342
P... |
A8Z6M1 | MFKKFNILLHSWANDYFFRPNFFQILLAFLLLPLSLIYTLVVVCKKFSAQKKDFGIKIISVGNLTLGGSGKTPLCVAIAKNYGGAFIILRGYKRKSKGMQVVARNGEILLDVAASGDEAMIYATSIKNANVIVSEDRKIAINYAKKHGAKYILLDDGFSKFDIAKFDILVRPNPEPKLRLCLPSGAYRYPFSFYKFGNFIACEGQTHFRKSEILNKTEKMVLVTAIANPARLEAFFSECVGQVFFPDHYDFSKEELSEILQSYGATSLLMTQKDYVKVKDFGLRVSLITLEVTLSEEFKKVLAKQI | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 34519
Sequence Length: 306
P... |
Q4FS43 | MNIETTITRAWQRQAAWLWLLLPVSWLYSLLMILRRQAYKAGIFSSYRAPIPVMVIGNITVGGSGKTPLIIALVRHLQQQGIKVGVISRGYGGDSSQMPALVNTESVPNIVGDEPCLIVNMTGVAMAVCPNRQQAMTTLLASYPDLQLIIADDGLQHYALQRDIEWIVVDAARGFGNKQLLPTGFLREPMSRLKGANVVYHQKADSLSSTDDKYDDTCPPTKRLRMHLQPDNLERLWSFDTQSDGLATVKAMAPEKGSRVHAVSGIGYPQRFFDTLDTLGFQVSPHPYPDHHDFSLTELLRYTEHPIIVTSKDAVKIRAL... | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 43039
Sequence Length: 385
P... |
A1STC8 | MPFWYRPVTWAWLLLPLALLFKMISFCRRLAYQKGFFKRYKSKLPVIIVGNISVGGNGKTPFVIWLCEMLITVGYKPAVISRGYGGKSNHYPLLVGDHIKGHEAGDEPVLIHKRLGIPVVVDPNRKNAVKYIEQHFLADIIISDDGLQHYALQRDIEIVIVDGKRRFGNQHLMPIGPLRENLSRLNSVDFVVNNGGQQVNEITMLLKAQNCQRVDGETAQLSSGVQVNACAAIGYPQRFFDTLNQQQFEILKAVGFNDHHAFSKDDFTQFEASIPLLMTEKDAVKCTDFAQPNWWYLPVSAEFSAGFEQQLLNRIKEIKC | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 36309
Sequence Length: 320
P... |
P58185 | MASEAPPFWWEEPDWKVLALSPLSAVYALVAGRVMRRARREKIEAPVLCVGNFTVGGTGKTPVAIALAQQAKRMQLKPGFLSRGHGGSFAEPHVVDAHHDAAKHVGDEPLLLAEHAPVAVTPNRAAGARLLMAKHGCDFLIMDDGFQSARIHIDYALIVVDARYGIGNGRVIPGGPLRAKIVDQLVFTSGLLKMGEGTAADAVVRQAARAGRPIFEARAEPISKAGLAGKRFLAFAGIGHPDKFFDTVREAGGEVVLSKPFPDHHFYAEDELAELAAVARAEGLGLITTAKDAARLRHGASQDFLNRLEVLEIDTVFELD... | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 36941
Sequence Length: 341
P... |
Q7UNW7 | MSWDYRPLLSGQSRDPFSSMARGALWCASGFYNVAARHRRRQYDSGNREICNAGVPVISVGNLTTGGTGKTPVVADLCRRLRAMDFRVTIISRGYGASDGRMNDEAMELQERLPDVPHVQHPDRVEAARIAVEELAAEVLVMDDGFQHRRLQRDLDIVVIDATCPFGYGHVLPRGTLREPLDSVTRADWVLITRVDQVDPEEVLAIRSTIAQHAPDCPVLETEHRPSTIQSSVGDWEAIEVLIDQPVALVSAIGNPDAFEQTVLDCGAIVVDHLRLPDHDSYERATREKLRSWVTKLKGGPQPPQRLLCTHKDAVKLATD... | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 40432
Sequence Length: 365
P... |
B6IXD8 | MKAPAFWYAPPGTARPLLSALLTPAALAWTAATRRRLSGTRPWHAPVPVICVGNLVAGGAGKTPVVLDLLSRLRRGGLDAHALSRGHGGRLPGPLRVDPARHTAAEVGDEPLLLAAAAPAWIARDRAAGARAAADAGAGVLVLDDGFQNPGIAKDLSLLVVDGDAGFGNGRVIPAGPLREPVADGLARAQAVLLLGEDRRGTADLCRGRLPVLRGRLVPDPQAAADLEGRRVLAFAGIGRPEKLFRTLEALGADVVARLPFPDHHPFTAAELRALLDRAAALDALPVTTQKDLVRLPAELRGQVRALPVSIAWEEPDTLD... | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 35254
Sequence Length: 337
P... |
Q2RWV9 | MRAPEFWHKDGFAARLLEPVGLVYAALTRHRVARPPGVRLGIPVVCVGNLTAGGAGKTPVALAVMDALRRRGVVGHFLSRGYGGKMEGPVAVDPVGHGPEDVGDEPLLLANSAPCWVSRNRASGGLVAEGAGAQAVVMDDGHQNPSLAKDLSLVVVDGGYGFGNGRYIPAGPLRESIEAGLARAGAVILIGSDSENLAARIPPHLKAGVPLLTARLEPGPEAARLVGRKVVAFAGIGRPEKFFATLTALGARVVARHPFADHYPYAEADIQPILDEAYGLGAVPVTTSKDAVRLPPDQRPQVDVVGVRVVFDEPLAFEAL... | Function: Transfers the gamma-phosphate of ATP to the 4'-position of a tetraacyldisaccharide 1-phosphate intermediate (termed DS-1-P) to form tetraacyldisaccharide 1,4'-bis-phosphate (lipid IVA).
Catalytic Activity: a lipid A disaccharide + ATP = a lipid IVA + ADP + H(+)
Sequence Mass (Da): 34631
Sequence Length: 331
P... |
Q5VT99 | MRPRAPACAAAALGLCSLLLLLAPGHACPAGCACTDPHTVDCRDRGLPSVPDPFPLDVRKLLVAGNRIQRIPEDFFIFYGDLVYLDFRNNSLRSLEEGTFSGSAKLVFLDLSYNNLTQLGAGAFRSAGRLVKLSLANNNLVGVHEDAFETLESLQVLELNDNNLRSLSVAALAALPALRSLRLDGNPWLCDCDFAHLFSWIQENASKLPKGLDEIQCSLPMESRRISLRELSEASFSECRFSLSLTDLCIIIFSGVAVSIAAIISSFFLATVVQCLQRCAPNKDAEDEDEDKDD | Function: Auxiliary protein of the large-conductance, voltage and calcium-activated potassium channel (BK alpha). Modulates gating properties by producing a marked shift in the BK channel's voltage dependence of activation in the hyperpolarizing direction, and in the absence of calcium.
Location Topology: Single-pass t... |
Q8CN54 | MVILEQTHLVKNKAVDNKKSMKYSIFQQALTIAVILLISKIIESFMPIPMPASVIGLVLLFIALCTGIVKLGQVETVGTALTNNIGFLFVPAGISVINSLPILKQSPILIILLIIISTLLLLICTGFSSQLLVTKSLFPSKEKNEETSHIGG | Function: Inhibits the expression or activity of extracellular murein hydrolases by interacting, possibly with LrgB, with the holin-like proteins CidA and/or CidB. The LrgAB and CidAB proteins may affect the proton motive force of the membrane. May be involved in programmed cell death (PCD), possibly triggering PCD in ... |
P65264 | MSSSVSSKTRYWVLALAAIVLDQWSKWAVLSSFQYRERVNVIPSFFDLTLVYNPGAAFSFLADQGGWQKYFFLVLAVAVSAYLVRAILRDEFATLGKTGAAMIIGGALGNVIDRLIHGHVVDFLLFYWQNWFYPAFNIADSFICVGAVLAVLDNIVHRKTQEEKY | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
Q1QIP9 | MTPLRSGIVAAVAALIADQASKLWLLFVFDIGHRGAVRVTPFFDLVLAWNTGISYGWFQTDSPVGATILLAIKAGAVVLLAIWMARSQTRLATIGLGLIIGGAIGNAIDRFAYGAVVDFVLFHVPLAGKTYSWYVFNLADVAIVAGVIALLYDSFLRTPAAKAP | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
B3CS08 | MLLEQVIYIMCNLEVSKNSSRNKLWSLIFGIQLLIIDQLVKSFFINFLKKTPEIAISIFKYFKISYVWNYGISFGIFNYYYDISNNFFLIVNTIIVLCICYLITKAKKLLQFNAYMLIIIGGTSNIIDRMLYGAVFDFIDIYLIIFNLADLYIFVGTILLVIYYSYYE | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
Q7U7A6 | MTGSILRRAPLLGVAGLVVLVDQATKLLAASQLADGRIVQLLPGLINGQLVHNTGAAFSLFRGSVQWLGLLSLAVTTGLLIWVVRHRTPPFWQGMAVAFLLGGTLGNGIDRWRLGHVIDFLALVPINFPIFNPADIAINLAVLCFLVDLWSSRTSSRHG | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
B2JDY8 | MSRTLSKPAGGSLAPWLGVAVIVILFDQLTKIAVAKVFAYGSSHAIAPFFNLVLVYNRGAAFSFLAMAGGWQRWAFTALGVAAAVLICYLLKRHGTQKMFCTALALIMGGAIGNVIDRLLYGHVIDFLDFHVGAWHWPAFNLADSAITIGAALLVFDELRRVRGAR | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
A5D178 | MFLFIIIAVVLLVDQATKAAVQMLMCQGESIPVVPPAFYLTYIMNPGAAFGLLPHKKMLFVTVTVIIIAGVLVGYFKIRPRKPVLDYGLGLVAGGALGNLADRLRYGLVVDFLDFRIWPVFNLADTAIVTGAFLLAWALLNDSDKSSKKERK | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
Q4FPB0 | MNKINLKNFYLNLVIILVVFIFDRTTKLYILKLAEVETSVDIYITPFLNLFLIWNKGIAFGLFSIDGSVIYNSITILIGLIIIAIIFMMLKNDNIQRYFFALIAGGAFGNFYDRIVYTAVPDFIDLHFYGFHWFVFNVADIFITIGVFCLILVELFFNNKKTNEKN | Function: This protein specifically catalyzes the removal of signal peptides from prolipoproteins.
Catalytic Activity: Release of signal peptides from bacterial membrane prolipoproteins. Hydrolyzes -Xaa-Yaa-Zaa-|-(S,diacylglyceryl)Cys-, in which Xaa is hydrophobic (preferably Leu), and Yaa (Ala or Ser) and Zaa (Gly or ... |
Q1C138 | MPHTVATPPPLLQVRGISKQFSGVVVLKSIDFTLQPGQVHALLGGNGAGKSTLMKIIAGILPPDTGVIEMNGQPCFNLTPAKAHQLGIYLVPQEPMLFANLSVQENILFRLPKHQADKKKMAQLLKNLGCHLDLSVSAGSLEVADQQLVEIMRGLIRDSHILILDEPTASLTPAETHRLFSQIRMLLQQGVGVVFISHKLPEIRQLADWVSVMRDGGIALSGATADFSTEDMIQAMTPEAQKGALTDSQKLWLELPGNRRAQSHAQSQQPVIHVHDLSGEGFAHISFHVQAGEILGLAGVVGAGRTELAETLYGLRPAST... | Function: Part of the ABC transporter complex LsrABCD involved in autoinducer 2 (AI-2) import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + (2R,4S)-2-methyl-2,3,3,4-tetrahydroxytetrahydrofuran-[AI-2-binding protein]Side 1 = ADP + phosphate + (2R,4S)-2-methyl-2,3,3,4-tetrahydr... |
Q9HCC9 | MMNRFRKWLYKPKRSDPQLLARFYYADEELNQVAAELDSLDGRKDPQRCTLLVSQFRSCQDNVLNIINQIMDECIPQDRAPRDFCVKFPEEIRHDNLAGQLWFGAECLAAGSIIMNRELESMAMRPLAKELTRSLEDVRGALRDQALRDLNTYTEKMREALRHFDVLFAEFELSYVSAMVPVKSPREYYVQQEVIVLFCETVERALDFGYLTQDMIDDYEPALMFSIPRLAIVCGLVVYADGPLNLDRKVEDMSELFRPFHTLLRKIRDLLQTLTEEELHTLERNLCISQDVEFPIRADVQGPAALAPALSAPLPPEGPL... | Function: Negative regulator of epidermal growth factor receptor (EGFR) signaling. Acts by promoting EGFR degradation in endosomes when not monoubiquitinated.
PTM: Monoubiquitination at Lys-87 prevents binding to phosphatidylinositol 3-phosphate (PI3P) and localization to early endosome membranes.
Sequence Mass (Da): 9... |
Q6ZPK7 | MMNRFRKWLYKPKRSDPQLLAQFYYADEELNQVAAELDSLDGRKEPQRCTLLVSQFRSCQDNVLNIINQIMEECIPQDRAPRDFCVKFPEEIRHDNLAGQLWFGAECLAAGSIIMNRELESMAMRPLAKELTRSLEDVRGTLRDQALRDLNTYTEKMREALRRFDVLFAEFELSYVSAMVPVKSPREYYVQQEVIVLFCETVERALDFGYLTQDMIDDYEPALMFTIPRLAIVCGLVVYADGPLNLDRKVEDMSELFRPFHTLLRKIRDLLQALTEEELHTLERSLCVSQDVELPIRADTQAPSALAPTFSASLPPEETL... | Function: Negative regulator of epidermal growth factor receptor (EGFR) signaling. Acts by promoting EGFR degradation in endosomes when not monoubiquitinated (By similarity).
PTM: Monoubiquitination at Lys-87 prevents binding to phosphatidylinositol 3-phosphate (PI3P) and localization to early endosome membranes.
Seque... |
Q0P4S0 | MMNRFRKWLYKPKRSDPQLLAQFYYADEELNQVAAELDSLDGRKDPQRCTLLVNQFRSCQDNVLNIINQIMEECIAHERANRDFCVKFPEEIRHDNLAGQLWFGAECLAAGSIIMNREIESMAMRPLAKDLTRSLEEVRNLIRDQALRDLNIYTEKMKESLRHFDVLFAEFELSYVSAMVPVKSPKEYYVQQEVIVLFCETVERALKLGYLTQDMIDDYEPALMFTIPRLAIVCGLVVYAEGPLNLERKPEDMSELFRPFHTLLRKIRDLLQTLTEDELHTLERNLCISQDVEFPANADPEVPSAISPVLVTALPTEEPP... | Function: Negative regulator of epidermal growth factor receptor (EGFR) signaling. Acts by promoting EGFR degradation in endosomes when not monoubiquitinated (By similarity).
PTM: Monoubiquitination at Lys-87 prevents binding to phosphatidylinositol 3-phosphate (PI3P) and localization to early endosome membranes.
Seque... |
Q8I4E2 | MAQVKAEYDFQSQPNTGELSISAGEVLTVIRENIDGGWIEGRNVRGSVGLFPESYVTPYQASRPPPVLPPPLPPTSSGPPAASSRPFDDWGGASEVAAPPSYGAQHHHQPTPSVPEVTRSSYPSQNDDFDDEWTDEDDEQEPTRPNVQSSIGSNSRRDLSRSHSEHGGPDRGSNKVNKNINRFSNFVKSGVEAYVIGESKTTSQISERHEVVMNNGIIQWKPIQQYYTCIVDKPKKESKLKGLKSFIAYSITSSLTNIQRQVSRRYKHFDWLHEQLSAKYVLIPIPPLPEKQVAGRYEEDLIDHRKHILQLWVNKICRHP... | Function: Involved in the signaling of vulval development by acting as a negative regulator of epidermal growth factor receptor (EGFR) signaling. Aids in phagosomal membrane tubule formation which is required for phagosomal fusion with endosomes and lysosomes. Also recruits rab-7 to phagosomes by an interaction with dy... |
Q6CZ26 | MKKTSDYAVAVIGLGSMGFGAAASCINAGLTTYGVDINPQALEKLRQAGAAQADTRIDAFADKLDAVVLLVVNATQVNGILFGEPQVAAKLKPGTVVMVSSTISAQDAKNIEQRLAEHQLVMLDAPVSGGAAKAAAGDMTVMASGSDLAFEKLKPVLDAVAGKVYRIGEEIGLGATVKIIHQLLAGVHIAAGAEAMALAARADIPLDIMYDVVTNAAGNSWMFENRMRHVVDGDYTPKSAVDIFVKDLGLVTDTAKSLHFPLPLASTAFNMFTAASNAGFGKEDDSAVIKIFNGITLPEKKEAP | Function: Catalyzes oxidation of L-threonate to 2-oxo-tetronate. Can use either NAD(+) or NADP(+) as cosubstrate, with a preference for NAD(+).
Catalytic Activity: L-threonate + NAD(+) = 2-dehydro-L-erythronate + H(+) + NADH
Sequence Mass (Da): 31629
Sequence Length: 304
EC: 1.1.1.411
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Q8L540 | MMARFVSVSSCQFHFGFREVSPPSVTSYPRRFEVSDRRFPAIPIKCSSSEPENGEDSAPSLSSSSSSSTSEVSTSNSSTYNWYTGIGGIGMLDTAYLTYLKVTGSDAFCPIGGGTCGDVLNSDYAVVFGVPLPVIGFVMYGVVTALSAELGEGNLPFGISKSNGRFALFGITTAMASASAYFLYILSTKLSGSSCLYCLVSAFLSFSLFFLSVKDVKLQEIQQVVGLQICLAIIVVASLTASYSTAQPIPSRSGDIELPYFRTEISSSSSPYAIALAKHLNSIGAKMYGAFWCSHCLEQKEMFGREAAKELNYVECFPDG... | Function: Thiol-disulfide oxidoreductase catalyzing disulfide bond formation of chloroplast proteins and involved in redox regulation and photosynthetic electron transport. Required for the assembly of photosystem II (PSII) through the formation of disulfide bond in PSBO, a subunit of the PSII oxygen-evolving complex i... |
Q6IAA8 | MGCCYSSENEDSDQDREERKLLLDPSSPPTKALNGAEPNYHSLPSARTDEQALLSSILAKTASNIIDVSAADSQGMEQHEYMDRARQYSTRLAVLSSSLTHWKKLPPLPSLTSQPHQVLASEPIPFSDLQQVSRIAAYAYSALSQIRVDAKEELVVQFGIP | Function: Key component of the Ragulator complex, a multiprotein complex involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids . Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the R... |
Q6P2W7 | MGCCYSGETDTGKGDQGEREHLLPQSQSLPNKAPNESEQNSTNNPSARTDEQAMLSRILAKTAQNIIDVSAVESQGMEQHECMDRARQYSTRLAKLSSNLMDWKKVPPLPSLTSQPHQILASDPVPFADIQQVSKIAAYAFSALSQIRVDAKEDLVVQFGIP | Function: Key component of the Ragulator complex, a multiprotein complex involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ra... |
Q9Y2Q5 | MLRPKALTQVLSQANTGGVQSTLLLNNEGSLLAYSGYGDTDARVTAAIASNIWAAYDRNGNQAFNEDNLKFILMDCMEGRVAITRVANLLLCMYAKETVGFGMLKAKAQALVQYLEEPLTQVAAS | Function: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids . Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator plays a dual ro... |
Q9JHS3 | MLRPKALTQVLSQANTGGVQSTLLLNNEGSLLAYSGYGDTDARVTAAIASNIWAAYDRNGNQAFNEDSLKFILMDCMEGRVAITRVANLLLCMYAKETVGFGMLKAKAQALVQYLEEPLTQVAAS | Function: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids (By similarity). Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator ... |
D4A8G3 | MEGTAESQTPDLRDVEGKVGRKTPEGLLRGLRGECDLGTSGDVLLPGASSTGHGLGDKIMALRMELAYLRAIDVKILQQLVTLNEGIEAVRWLLEERGTLTSHCSSLTSSQYSLTGGSPERSRRGSWDSLPDTSSTDRLDSVSIGSFLDTVAPRELDEQGHPGPSCPEIDWAKVIPSEDRARTEVDMTSTKLGSLTATWKLPGDGLQCGPPEPSEDDSAKQGFEAHWYWGQCQDDVTFL | Function: Acts as an activator of the canonical NF-kappa-B pathway and drive the production of pro-inflammatory cytokines. Promotes the antigen (Ag)-presenting and priming function of dendritic cells via the canonical NF-kappa-B pathway (By similarity). In concert with MYO18A and CDC42BPA/CDC42BPB, is involved in modul... |
Q6TBX7 | MESSLFSPSSSSYSSLFTAKPTRLLSPKPKFTFSIRSSIEKPKPKLETNSSKSQSWVSPDWLTTLTRTLSSGKNDESGIPIANAKLDDVADLLGGALFLPLYKWMNEYGPIYRLAAGPRNFVIVSDPAIAKHVLRNYPKYAKGLVAEVSEFLFGSGFAIAEGPLWTARRRAVVPSLHRRYLSVIVERVFCKCAERLVEKLQPYAEDGSAVNMEAKFSQMTLDVIGLSLFNYNFDSLTTDSPVIEAVYTALKEAELRSTDLLPYWKIDALCKIVPRQVKAEKAVTLIRETVEDLIAKCKEIVEREGERINDEEYVNDADPS... | Function: Heme-containing cytochrome P450 involved in the biosynthesis of xanthophylls. Specific for epsilon- and beta-ring hydroxylation of alpha-carotene. Has only a low activity toward the beta-rings of beta-carotene. The preferred substrate in planta is not alpha-carotene but the epsilon-ring of zeinoxanthin . Poss... |
Q93VK5 | MAMAFPLSYTPTITVKPVTYSRRSNFVVFSSSSNGRDPLEENSVPNGVKSLEKLQEEKRRAELSARIASGAFTVRKSSFPSTVKNGLSKIGIPSNVLDFMFDWTGSDQDYPKVPEAKGSIQAVRNEAFFIPLYELFLTYGGIFRLTFGPKSFLIVSDPSIAKHILKDNAKAYSKGILAEILDFVMGKGLIPADGEIWRRRRRAIVPALHQKYVAAMISLFGEASDRLCQKLDAAALKGEEVEMESLFSRLTLDIIGKAVFNYDFDSLTNDTGVIEAVYTVLREAEDRSVSPIPVWDIPIWKDISPRQRKVATSLKLINDT... | Function: Heme-containing cytochrome P450 involved in the biosynthesis of xanthophylls. Specific for beta-ring hydroxylation of alpha- and beta-carotene. Has also a low activity toward the epsilon-rings of alpha-carotene. The beta-ring of alpha-carotene is the preferred substrate in planta.
Sequence Mass (Da): 66846
Se... |
Q97F13 | MEKIASFTVNHLTLQPGVYVSRKDKFGDVVITTFDIRMTSPNEEPVMNTAEVHTIEHLGATFLRNHGTYAEKTVYFGPMGCRTGFYLILQGDYTSNDIVPLLREMYKFIADFKGEVPGAAARDCGNYLDMNLPMANYWGKKFSALLDNISEDRLNYPE | Cofactor: Binds 1 Fe cation per subunit.
Function: Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum se... |
B2UWX8 | MEKVESFELDHRKVKAPYIRKCCLLDGKCGDKVTKFDIRFLQPNKEEFGTAAMHGLEHLLAHELRAKLEGIIDLSPMGCRTGFYLSIWGDREASEIKEALEYSLEKVLEAKEIPAANDIQCGNYRDLSLFGAKEYAKEALERGFSLNIYGE | Cofactor: Binds 1 Fe cation per subunit.
Function: Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum se... |
Q181K1 | MEKVESFKLDHTKVKAPFVRKCSVLDGVKGDKVTKFDLRFLQPNVESFGTAAMHGLEHLLATYLRDTLDGVIDLSPMGCRTGFYLILWGDVDAKTVKIGLEEALKKVLESDKMPAATAIECGNYRDLSLFGAKEYAKDVLDKGFSLNIYGE | Cofactor: Binds 1 Fe cation per subunit.
Function: Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum se... |
Q9XDU6 | MVKVESFELDHTKVKAPYVRKAGIKIGPKGDIVSKFDLRFVQPNKELLSDKGMHTLEHFLAGFMREKLDDVIDISPMGCKTGFYLTSFGDIDVKDIIEALEYSLSKVLEQEEIPAANELQCGSAKLHSLELAKSHAKQVLENGISDKFYVE | Cofactor: Binds 1 Fe cation per subunit.
Function: Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum se... |
Q6AAL4 | MAHKMNVESFNLDHTKVAAPFVRVADVKHLPAGDTLTKYDVRFCQPNKEHLDMPAVHSLEHSFAECVRNHSDAVIDFGPMGCQTGFYLIMIGEPDVSGTCELVETTLRDILKLNTTPAANEVQCGWGANHSIKAAQEAAHTMLNHRDEWEQVMA | Cofactor: Binds 1 Fe cation per subunit.
Function: Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum se... |
Q1IW42 | MANVESFDLDHTKVQAPYVRLAGVKTTPRGDQISKYDLRLLQPNRGAIEPAALHTLEHLLAGYLRDHLQNVVDVSPMGCRTGLYLAVIGEPDEEGVLQAFEAALRDTATHDRPIPGVSELECGNYRDHDLQAARQYARDALTQGLKVQKTILLQR | Cofactor: Binds 1 Fe cation per subunit.
Function: Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum se... |
Q9RRU8 | MPDMANVESFDLDHTKVKAPYVRLAGVKTTPKGDQISKYDLRFLQPNQGAIDPAAIHTLEHLLAGYMRDHLEGVVDVSPMGCRTGMYMAVIGEPDEQGVMKAFEAALKDTAGHDQPIPGVSELECGNYRDHDLAAARQHARDVLDQGLKVQETILLER | Cofactor: Binds 1 Fe cation per subunit.
Function: Involved in the synthesis of autoinducer 2 (AI-2) which is secreted by bacteria and is used to communicate both the cell density and the metabolic potential of the environment. The regulation of gene expression in response to changes in cell density is called quorum se... |
A0A3G9JYH7 | MRINISLSSLFERLSKLSSRSIAITCGVVLASAIAFPIIRRDYQTFLEVGPSYAPQNFRGYIIVCVLSLFRQEQKGLAIYDRLPEKRRWLADLPFREGTRPSITSHIIQRQRTQLVDQEFATRELIDKVIPRVQARHTDKTFLSTSKFEFHAKAIFLLPSIPINDPLNIPSHDTVRRTKREIAHMHDYHDCTLHLALAAQDGKEVLKKGWGQRHPLAGPGVPGPPTEWTFLYAPRNEEEARVVEMIVEASIGYMTNDPAGKIVENAK | Function: Luciferase; part of the gene cluster that mediates the fungal bioluminescence cycle . Uses the fungal luciferin 3-hydroxyhispidin as a substrate to produce an endoperoxide as a high-energy intermediate with decomposition that yields oxyluciferin (also known as caffeoylpyruvate) and light emission . The fungal... |
Q7Z3F1 | MNSNLPAENLTIAVNMTKTLPTAVTHGFNSTNDPPSMSITRLFPALLECFGIVLCGYIAGRANVITSTQAKGLGNFVSRFALPALLFKNMVVLNFSNVDWSFLYSILIAKASVFFIVCVLTLLVASPDSRFSKAGLFPIFATQSNDFALGYPIVEALYQTTYPEYLQYIYLVAPISLMMLNPIGFIFCEIQKWKDTQNASQNKIKIVGLGLLRVLQNPIVFMVFIGIAFNFILDRKVPVYVENFLDGLGNSFSGSALFYLGLTMVGKIKRLKKSAFVVLILLITAKLLVLPLLCREMVELLDKGDSVVNHTSLSNYAFLY... | Function: Cholesterol-binding protein that acts as a regulator of mTORC1 signaling pathway . Acts as a sensor of cholesterol to signal cholesterol sufficiency to mTORC1: in presence of cholesterol, binds cholesterol, leading to disrupt interaction between the GATOR1 and KICSTOR complexes and promote mTORC1 signaling . ... |
M0L7V9 | MPELPTDRLTAVIPPEETLLGYLLRLSRPRFWLYLGGPVIVGVSYAADGPGELFSPLAIALFLYFTIPGNVFLYGVNDIFDADIDEHNPKKDDGREVSYRGDSAVTAIVVASGALALLFALVLPTLGIVALLAWMALSVEYSAPPLRFKTTPFLDSISNGLYILPGVIGYAAIEGVAPPATAVVGAWLWAMGMHTFSAIPDIEPDREAGIQTTATFLGESNTYYYCVMCWLMAAFVFNFTHWVFGVLLLVYPGLVFGILGVGVDIDEAYWWYPAINTVVGMVFTLIALWVMLYG | Function: Involved in the biosynthesis of the acyclic C50 carotenoid bacterioruberin (BR) . Acts as a bifunctional elongase/hydratase that catalyzes the elongation of lycopene by attaching a C(5) isoprene unit at C-2, as well as the hydroxylation of the previous end of the molecule . The enzyme acts at both ends of the... |
Q9HPD9 | MFRYLFVLSRPRFWLYLAGPVLVGVSYGATTVGELFSAPAVVLFSYFLLPANIYLYGINDVFDRDVDETNPKKDGRESRYRGGAAVAVIVAVCGVFLGFVAAPLPAEAWPYLAAWFVLATEYSAPPLRFKTTPVLDSLSNGLYVLPAAAAYAGVSGTHPPLLAVAGGWLWAMGMHTFSAIPDIEPDRAAGIQTTATALGADRALAYCAGIWLLSAAVFALVDVRFGLLLLAYPVLVFGIRRLQVAVGRAYWWYPAVNTLVGMVFTLGGLWGVVHG | Function: Involved in the biosynthesis of the acyclic C50 carotenoid bacterioruberin (BR) . Acts as a bifunctional elongase/hydratase that catalyzes the elongation of lycopene by attaching a C(5) isoprene unit at C-2, as well as the hydroxylation of the previous end of the molecule . The enzyme acts at both ends of the... |
Q86SG7 | MLSSVVFWGLIALIGTSRGSYPFSHSMKPHLHPRLYHGCYGDIMTMKTSGATCDANSVMNCGIRGSEMFAEMDLRAIKPYQTLIKEVGQRHCVDPAVIAAIISRESHGGSVLQDGWDHRGLKFGLMQLDKQTYHPVGAWDSKEHLSQATGILTERIKAIQKKFPTWSVAQHLKGGLSAFKSGIEAIATPSDIDNDFVNDIIARAKFYKRQSF | Function: May act as a potent antibacterial protein that may play a role in the innate immunity.
Sequence Mass (Da): 23498
Sequence Length: 212
Subcellular Location: Secreted
EC: 3.2.1.-
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Q90X99 | MGYGNIMNVETTGASWQTAQQDKLGYSGVRASHTMANTDSGRMERYRSKINSVGAKYGIDPALIAAIISEESRAGNVLHDGWGDYDSNRGAYNAWGLMQVDVNPNGGGHTARGAWDSEEHLSQGAEILVYFIGRIRNKFPGWNTEQQLKGGIAAYNMGDGNVHSYDNVDGRTTGGDYSNDVVARAQWYKTQKGF | Function: Has lytic activity against M.lysodeikticus, V.alginolyticus from Epinephelus fario, V.vulnificus from culture water, A.hydrophila from soft-shell turtle, A.hydrophila from goldfish and V.parahaemolyticus, P.fluorescens and V.fluvialis from culture water.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages ... |
Q90VZ3 | MSYGQIRLVETSGASGATSQQDNLGYSGVKASHKMAEIDSGRMSKYKSKINKVGQSYGIEPALIAAIISRESRAGNQLKDGWGDWNPQRQAYNAWGLMQVDVNPNGGGHTAVGGWDSEDHLRQATGILVTFIERIRTKFPGWSKEKQLKGGIAAYNMGDKNVHSYEGVDENTTGRDYSNDVTARAQWYRDNGYSG | Function: Possesses lytic activity against M.lysodeikticus and several fish pathogenic bacteria.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 21... |
Q86UE4 | MAARSWQDELAQQAEEGSARLREMLSVGLGFLRTELGLDLGLEPKRYPGWVILVGTGALGLLLLFLLGYGWAAACAGARKKRRSPPRKREEAAAVPAAAPDDLALLKNLRSEEQKKKNRKKLSEKPKPNGRTVEVAEGEAVRTPQSVTAKQPPEIDKKNEKSKKNKKKSKSDAKAVQNSSRHDGKEVDEGAWETKISHREKRQQRKRDKVLTDSGSLDSTIPGIENTITVTTEQLTTASFPVGSKKNKGDSHLNVQVSNFKSGKGDSTLQVSSGLNENLTVNGGGWNEKSVKLSSQISAGEEKWNSVSPASAGKRKTEPS... | Function: Down-regulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also... |
Q9Z1W6 | MAARSWQDELAQQAEEGSARLRELLSVGLGFLRTELGLDLGLEPKRYPSWVILVGTGALGLLLLFLLGYGWAAACAGARKKRRSPPRKREEVTPPTPAPEDPAQLKNLRSEEQKKKNRKKLPEKPKPNGRTVEIPEDEVVRTPRSITAKQPPETDKKNEKSKKNKKKSKSDAKAVQNSSRHDGKEVDEGAWETKISHREKRQQRKRDKVLTDSGSLDSTIPGIENTITVTTEQLTTASFPVGSKKNKGDSHLNVQVSNFKSGKGDSTLQVSSGLNENITVNGGGWSEKSVKLSSQLSAGEEKWNSVPPASAGKRKTEQSA... | Function: Down-regulates SLC1A2/EAAT2 promoter activity when expressed ectopically. Activates the nuclear factor kappa-B (NF-kappa-B) transcription factor. Promotes anchorage-independent growth of immortalized melanocytes and astrocytes which is a key component in tumor cell expansion. Promotes lung metastasis and also... |
P04421 | MKALVILGFLFLSVAVQGKVFERCELARTLKKLGLDGYKGVSLANWLCLTKWESSYNTKATNYNPSSESTDYGIFQINSKWWCNDGKTPNAVDGCHVSCRELMENDIAKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYVEGCTL | Function: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidog... |
P00698 | MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQAWIRGCRL | Function: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and ... |
P00708 | KDIPRCELVKILRRHGFEGFVGKTVANWVCLVKHESGYRTTAFNNNGPNSRDYGIFQINSKYWCNDGKTRGSKNACNINCSKLRDDNIADDIQCAKKIAREARGLTPWVAWKKYCQGKDLSSYVRGC | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-a... |
Q4L8V4 | MKTLIVDDEPLARNELHYLLNEISGFNVIDEAENIEETLEKLLSETYDLVFLDINLMDESGIDLAQKIKKMKQPPHIIFATAHDTFAVKAFELDAIDYILKPFELERIEQAVNKVKHQISNSNEIDHITSEPSTLSMQQDDRQENEDQTVLPIEMNERIYVIRKDDITAVSVNNGITTINTTHRTYQTNEPLNYYEKKLSNNTFIKIHRATIINKTHIDSVEHWFNYTYQVTMTSGDKFQVSRSFMKAFKHEIGLA | Function: Member of the two-component regulatory system LytR/LytS that probably regulates genes involved in cell wall metabolism.
PTM: Phosphorylated by LytS.
Sequence Mass (Da): 29725
Sequence Length: 256
Subcellular Location: Cytoplasm
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Q8DVB7 | MNILILDDEMLARQELTFLIQQSKELDHPDIFEAEDISSAEKILFRQQIDLIFLDISLSEENGFTLANQLEQLAHPPLVVFATAYDHYAVKAFESNAADYILKPFEQGRVDKALAKVKKIQHLSTIDETATTEKKGMELLTLTLADRSIVLKMPDIVAASIEDGELTVSTKNTSYTIKKTLNWFKTRAKTNYFLQIHRNTVVNLEMIQEIQPWFNHTLLLVMVNGEKFPVGRSYMKELNAHLTL | Function: Member of the two-component regulatory system LytR/LytS that probably regulates genes involved in cell wall metabolism.
PTM: Phosphorylated by LytS.
Sequence Mass (Da): 27913
Sequence Length: 244
Subcellular Location: Cytoplasm
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P94513 | MIHLMIMMLERVGIIVILGFILAHTKLFRQALQNQDGYKGKAILISIFSLFSIISNYTGIEIQRNMIVNNDWVFTIDPSGSIANTRILGVEIGGLLGGPFVGAGIGILAGLHRFSLGGSTALSCAVSSILAGVLAGLIGRYFTKRYRMPTPRIAALVGIGMESLQMIIILLMAKPFSDAWELVSMIGIPMILINGTGSFIFLSIIQAIIRKEEQARALETHRVLTIADQTLPFFRQGLNENSCKSVAAIIHKLTGTDAVSLTDKEKILAHVGAGMDHHIPSKSLITGLSKKVIKTGHIMKAISQEEIECTHAECPLHAAI... | Function: Member of the two-component regulatory system LytS/LytT that probably regulates genes involved in cell wall metabolism.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64855
Sequence Length: 593
Subcellular... |
Q8EQQ2 | MIELTIVLFQRIGLLLLMAFILTRIPRFRSLLDKDITLKTVIYHSLIFGLISIIGAHVGVVMIGNELIMQAWIINVAENEVLIGFSIVVVMIAGLLGGPFLGLGTGMVAGLYIIFLGGGGWVANSLINPLAGLLTGWAGQFFSDDRVMSPNKALFIGIFPPVLHMGLLLIMLPDQQIGVQIVNTIGIPLVVTNSIALTIFTMMIRLALNETEQEAALETNRALTIAEKALPLLSEEPGTMNARKMAKLLFKELDIAAISITNRTTVLSHVGLGDDHHQPGEPLKMRLSKKAVKDGRIQIAYHQSDIQCGVENCKLKTAIM... | Function: Member of the two-component regulatory system LytS/LytT that probably regulates genes involved in cell wall metabolism.
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64669
Sequence Length: 585
Subcellular... |
Q2FK10 | MLSLTMLLLERVGLIIILAYVLMNIPYFKNLMNRRRTWKARWQLCIIFSLFALMSNLTGIVIDHQHSLSGSVYFRLDDDVSLANTRVLTIGVAGLVGGPFVGLFVGVISGIFRVYMGGADAQVYLISSIFIGIIAGYFGLQAQRRKRYPSIAKSAMIGIVMEMIQMLSILTFSHDKAYAVDLISLIALPMIIVNSVGTAIFMSIIISTLKQEEQMKAVQTHDVLQLMNQTLPYFKEGLNRESAQQIAMIIKNLMKVSAVAITSKNEILSHVGAGSDHHIPTNEILTSLSKDVLKSGKLKEVHTKEEIGCSHPNCPLRAAI... | Function: Member of the two-component regulatory system LytR/LytS that regulates genes involved in autolysis, programmed cell death, biofilm formation and cell wall metabolism. Participates also in sensing and responding to host defense cationic antimicrobial peptides (HDPs). Functions as a sensor protein kinase which ... |
Q6WB97 | MSRKAPCKYEVRGKCNRGSECKFNHNYWSWPDRYLLIRSNYLLNQLLRNTDRADGLSIISGAGREDRTQDFVLGSTNVVQGYIDDNQSITKAAACYSLHNIIKQLQEVEVRQARDSKLSDSKHVALHNLILSYMEMSKTPASLINNLKRLPREKLKKLAKLIIDLSAGADNDSSYALQDSESINQVQ | Function: Essential for viral replication in vivo . Plays a role in the association of the matrix protein with the nucleocapsid, which initiates assembly and budding (By similarity).
PTM: Phosphorylated by host in infected cells . Phosphorylation is not essential for zinc binding activity and oligomerization, but zinc ... |
P04545 | MSRRNPCKFEIRGHCLNGKRCHFSHNYFEWPPHALLVRQNFMLNRILKSMDKSIDTLSEISGAAELDRTEEYALGVVGVLESYIGSINNITKQSACVAMSKLLTELNSDDIKKLRDNEELNSPKIRVYNTVISYIESNRKNNKQTIHLLKRLPADVLKKTIKNTLDIHKSITINNPKESTVSDTNDHAKNNDTT | Function: Acts as a tetrameric transcription processivity factor that binds in a competitive manner to RNA and the phosphoprotein (P) to prevent premature termination during transcription . Transcription anti-terminator that enhances readthrough of intergenic junctions during viral transcription . Preferentially binds ... |
Q5MKM1 | MSVRPCKFEVQGFCSRGRNCKYSHKYWEWPLKTLMLRQNYMLNRIYRFLDTNTDAMSDVSGFDAPQRTAEYALGTIGVLKSYLEKTNNITKSIACGSLITVLQNLDVGLVIQARDSNTEDTNYLRSCNTILSYIDKIHKKRQIIHILKRLPVGVLCNLIQSVISIEEKINSSMKTE | Function: Acts as a tetrameric transcription processivity factor that binds in a competitive manner to RNA and the phosphoprotein (P) to prevent premature termination during transcription. Transcription anti-terminator that enhances readthrough of intergenic junctions during viral transcription. Preferentially binds to... |
C0HKZ3 | ECCRYVDCRRGCTPCC | Function: Has a sleep-inducing effect in mice when injected intraperitoneally.
Sequence Mass (Da): 1867
Sequence Length: 16
Domain: The cysteine framework is III (CC-C-C-CC). Classified in the M-2 branch, since 2 residues stand between the fourth and the fifth cysteine residues.
Subcellular Location: Secreted
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Q02779 | MEEEEGAVAKEWGTTPAGPVWTAVFDYEAAGDEELTLRRGDRVQVLSQDCAVSGDEGWWTGQLPSGRVGVFPSNYVAPGAPAAPAGLQLPQEIPFHELQLEEIIGVGGFGKVYRALWRGEEVAVKAARLDPEKDPAVTAEQVCQEARLFGALQHPNIIALRGACLNPPHLCLVMEYARGGALSRVLAGRRVPPHVLVNWAVQVARGMNYLHNDAPVPIIHRDLKSINILILEAIENHNLADTVLKITDFGLAREWHKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKL... | Function: Activates the JUN N-terminal pathway.
PTM: Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 103694
Sequence Length: 954
EC: 2.7.11.25
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Q66L42 | MEEEEGAAAREWGATPAGPVWTAVFDYEAVGDEELTLRRGDRVQVLSQDCAVSGDEGWWTGQLPSGRVGVFPSNYVAPAAPAAPSDLQLPQEIPFHELQLEEIIGVGGFGKVYRAVWRGEEVAVKAARLDPERDPAVTAEQVRQEARLFGALQHPNIIALRGACLSPPNLCLVMEYARGGALSRVLAGRRVPPHVLVNWAVQVARGMNYLHNDAPVPIIHRDLKSINILILEAIENHNLADTVLKITDFGLAREWHKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKL... | Function: Activates the JUN N-terminal pathway.
PTM: Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 103187
Sequence Length: 940
EC: 2.7.11.25
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Q7T2V3 | MDGLPKDEAFLWQSSKDNKENGVWSDVQSYGVSNPLWMAVFDYEPTAEEELTLRRGDLVEILSKDSTVSGDEGWWTGKIKDKVGIFPSNYVVSDDKYTTLTGAPKQCPLPLEIEFDELNLDEIIGVGGFGKVYKGLWRDEEVAVKAVRHDPDEDINVTAENVRQEAKIFCMLCHPNIIALTGVCLKPPHLCLVMEYARGGPLHRALAGKKVPAHVLVNWAVQIAKGMTYLHNEAIVPIIHRDLGSSNILILEKAENDDLFNKTLNITDFGLAREWQKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGE... | Function: Activates the JUN N-terminal pathway. Essential for pronephros and cement gland development.
PTM: Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence M... |
Q16584 | MEPLKSLFLKSPLGSWNGSGSGGGGGGGGGRPEGSPKAAGYANPVWTALFDYEPSGQDELALRKGDRVEVLSRDAAISGDEGWWAGQVGGQVGIFPSNYVSRGGGPPPCEVASFQELRLEEVIGIGGFGKVYRGSWRGELVAVKAARQDPDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEALVPVIHRDLKSNNILLLQPIESDDMEHKTLKITDFGLAREWHKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEV... | Function: Activates the JUN N-terminal pathway. Required for serum-stimulated cell proliferation and for mitogen and cytokine activation of MAPK14 (p38), MAPK3 (ERK) and MAPK8 (JNK1) through phosphorylation and activation of MAP2K4/MKK4 and MAP2K7/MKK7. Plays a role in mitogen-stimulated phosphorylation and activation ... |
Q66HA1 | MEPLKNLFLKSPLGSWNGSGSGGGGGSGGVRPEGSPKATAAYANPVWTALFDYEPNGQDELALRKGDRVEVLSRDAAISGDEGWWAGQVGGQVGIFPSNYVSRGGGPPPCEVASFQELRLEEVIGIGGFGKVYRGSWRGELVAVKAARQDPDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEALVPVIHRDLKSNNILLLQPIEGDDMEHKTLKITDFGLAREWHKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGE... | Function: Activates the JUN N-terminal pathway. Required for serum-stimulated cell proliferation and for mitogen and cytokine activation of MAPK14 (p38), MAPK3 (ERK) and MAPK8 (JNK1) through phosphorylation and activation of MAP2K4/MKK4 and MAP2K7/MKK7. Plays a role in mitogen-stimulated phosphorylation and activation ... |
Q12852 | MACLHETRTPSPSFGGFVSTLSEASMRKLDPDTSDCTPEKDLTPTHVLQLHEQDAGGPGGAAGSPESRASRVRADEVRLQCQSGSGFLEGLFGCLRPVWTMIGKAYSTEHKQQQEDLWEVPFEEILDLQWVGSGAQGAVFLGRFHGEEVAVKKVRDLKETDIKHLRKLKHPNIITFKGVCTQAPCYCILMEFCAQGQLYEVLRAGRPVTPSLLVDWSMGIAGGMNYLHLHKIIHRDLKSPNMLITYDDVVKISDFGTSKELSDKSTKMSFAGTVAWMAPEVIRNEPVSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIW... | Function: Part of a non-canonical MAPK signaling pathway . Activated by APOE, enhances the AP-1-mediated transcription of APP, via a MAP kinase signal transduction pathway composed of MAP2K7 and MAPK1/ERK2 and MAPK3/ERK1 . May be an activator of the JNK/SAPK pathway.
PTM: Autophosphorylated on Ser/Thr. Phosphorylated i... |
O60476 | MTTPALLPLSGRRIPPLNLGPPSFPHHRATLRLSEKFILLLILSAFITLCFGAFFFLPDSSKHKRFDLGLEDVLIPHVDAGKGAKNPGVFLIHGPDEHRHREEEERLRNKIRADHEKALEEAKEKLRKSREEIRAEIQTEKNKVVQEMKIKENKPLPPVPIPNLVGIRGGDPEDNDIREKREKIKEMMKHAWDNYRTYGWGHNELRPIARKGHSPNIFGSSQMGATIVDALDTLYIMGLHDEFLDGQRWIEDNLDFSVNSEVSVFEVNIRFIGGLLAAYYLSGEEIFKIKAVQLAEKLLPAFNTPTGIPWAMVNLKSGVG... | Function: Involved in the maturation of Asn-linked oligosaccharides. Progressively trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(5)GlcNAc(2).
Catalytic Activity: 4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)... |
Q9UKM7 | MAACEGRRSGALGSSQSDFLTPPVGGAPWAVATTVVMYPPPPPPPHRDFISVTLSFGENYDNSKSWRRRSCWRKWKQLSRLQRNMILFLLAFLLFCGLLFYINLADHWKALAFRLEEEQKMRPEIAGLKPANPPVLPAPQKADTDPENLPEISSQKTQRHIQRGPPHLQIRPPSQDLKDGTQEEATKRQEAPVDPRPEGDPQRTVISWRGAVIEPEQGTELPSRRAEVPTKPPLPPARTQGTPVHLNYRQKGVIDVFLHAWKGYRKFAWGHDELKPVSRSFSEWFGLGLTLIDALDTMWILGLRKEFEEARKWVSKKLHF... | Function: Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trim... |
A2AJ15 | MYPPPAPPPAPHRDFISVTLSLGESYDNSKSRRRRSCWRKWKQLSRLQRNVILFVLGFLILCGFLYSLHTADQWKALSGRPAEVEKMKQEVLPVLPAPQKESAEQEGFADILSQKRQRHFRRGPPHLQIRPPNTVSKDGMQDDAKEREAALGKAQQEENTQRTVISWRGAVIEPEQATELPYKRAEASIKPLVLASKIWKEPAPPNERQKGVIEAFLHAWKGYQKFAWGHDELKPVSKTFSEWFGLGLTLIDALDTMWILGLKQEFKQARKWVSENLDFQKNVDVNLFESTIRILGGLLSTYHLSGDSLFLTKAEDFGKR... | Function: Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trim... |
Q9NR34 | MLMRKVPGFVPASPWGLRLPQKFLFLLFLSGLVTLCFGALFLLPHSSRLKRLFLAPRTQQPGLEVVAEIAGHAPAREQEPPPNPAPAAPAPGEDDPSSWASPRRRKGGLRRTRPTGPREEATAARGNSIPASRPGDEGVPFRFDFNAFRSRLRHPVLGTRADESQEPQSQVRAQREKIKEMMQFAWQSYKRYAMGKNELRPLTKDGYEGNMFGGLSGATVIDSLDTLYLMELKEEFQEAKAWVGESFHLNVSGEASLFEVNIRYIGGLLSAFYLTGEEVFRIKAIRLGEKLLPAFNTPTGIPKGVVSFKSGNWGWATAGS... | Function: Involved in the maturation of Asn-linked oligosaccharides. Trim alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce first Man(8)GlcNAc(2) then Man(6)GlcNAc and a small amount of Man(5)GlcNAc.
Catalytic Activity: 4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-... |
P0CAY9 | YQRXSRYYYYXGPPDDIDDRY | Function: May be specifically involved in the formation of the nacreous layer.
PTM: According to PubMed:11250534, amino acids 4 and 11 may be sulfated or phosphorylated. By similarity with the N14 matrix protein, amino-acid 4 may be a cysteine involved in a disulfide bond.
Sequence Mass (Da): 2728
Sequence Length: 21
S... |
A2R6F5 | MFAKLSLLSLLFSSAALGASNQTLSYGNIDKSATPEARALLKYIQLQYGSHYISGQQDIDSWNWVEKNIGVAPAILGSDFTYYSPSAVAHGGKSHAVEDVIQHAGRNGINALVWHWYAPTCLLDTAKEPWYKGFYTEATCFNVSEAVNDHGNGTNYKLLLRDIDAIAAQIKRLDQAKVPILFRPLHEPEGGWFWWGAQGPAPFKKLWDILYDRITRYHNLHNMVWVCNTADPAWYPGNDKCDIATIDHYPAVGDHGVAADQYKKLQTVTNNERVLAMAEVGPIPDPDKQARENVNWAYWMVWSGDFIEDGKQNPNQFLHK... | Function: Endo-1,4-mannanase, a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans.
Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 37700
Sequence Length: 335
Subcellular Location: Secreted
E... |
G2Q4H7 | MARTLRYLLCGILALAAGSNAVPAARGSTRAAPAAEPSTSATTYEAEDAILSGTTVDTAQEGYTGSGYVTGFDEASDKITFEVESEATKLYDLSIRIAAIYGDKHTTVVLNGGASSDVSFPAGDTWVDVPAGQVLLNEGANTIEIVSNWGWYLVDSITLTPSAPRPEHQINRSLNNPSADASARALYDYLRSIYGKKILAGQQDLTWADYVTQQTGKTPALVSVDLMDYSPSRVERGTKGTSVEEAITHAERGGIVSALWHWNAPAGLYDTDEHPWWSGFYTDATDFDVAAALSSTDNANYTLLLRDIDAIAVQLKRLRD... | Function: Mannan endo-1,4-beta-mannosidase that exhibits high activity against konjac glucomannan and carob galactomannan, as well as a lower activity toward beta-mannan . Shows no activity against barley beta-glucan, birchwood xylan, and low viscosity carboxymethyl cellulose (CMC) . Has the ability to hydrolyze manno-... |
Q8VHC8 | MGASVLPLGLGAGDCQSSSGRRMSACLPRTALSFLLSLLLATPGARAAGYETCPMVQPGMLNVHLVAHTHDDVGWLKTVDQYYWGIHNDLQQAGVQYILDSVISALLAEPTRRFVYVEMAFFSRWWHQQTNETQEVVRRLVRQGRLEFANGGWVMNDEAATHYGAIVDQMTLGLRFLEDTFGSDGRPRVAWHIDPFGHSREQASLFAQMGFDGVFFGRIDYQDKLVRKKRREMELVWRASASLKAPAADLFTGVLPNNYGPPEGLCWDVLCADPPVVDDPRSPEYNAKKLVSYFLQLATAQGRYYRTNHTVMTMGSDFQY... | Cofactor: Binds 1 zinc ion per subunit.
Function: Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover.
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.
Sequence Mass (Da): 113184
Sequence Length: 1007
Subcellular Location: ... |
O00754 | MGAYARASGVCARGCLDSAGPWTMSRALRPPLPPLCFFLLLLAAAGARAGGYETCPTVQPNMLNVHLLPHTHDDVGWLKTVDQYFYGIKNDIQHAGVQYILDSVISALLADPTRRFIYVEIAFFSRWWHQQTNATQEVVRDLVRQGRLEFANGGWVMNDEAATHYGAIVDQMTLGLRFLEDTFGNDGRPRVAWHIDPFGHSREQASLFAQMGFDGFFFGRLDYQDKWVRMQKLEMEQVWRASTSLKPPTADLFTGVLPNGYNPPRNLCWDVLCVDQPLVEDPRSPEYNAKELVDYFLNVATAQGRYYRTNHTVMTMGSDF... | Cofactor: Binds 1 zinc ion per subunit.
Function: Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. Cleaves all known types of alpha-mannosidic linkages.
PTM: First processed into 3 peptides of 70 kDa, 42 kDa (D) and 13/15 kDa (E). The 70 kDa peptide is further processed into... |
Q96GV9 | MEVDINGESRSTLTTLPFPGAEANSPGKAEAEKPRCSSTPCSPMRRTVSGYQILHMDSNYLVGFTTGEELLKLAQKCTGGEESKAEAMPSLRSKQLDAGLARSSRLYKTRSRYYQPYEIPAVNGRRRRRMPSSGDKCTKSLPYEPYKALHGPLPLCLLKGKRAHSKSLDYLNLDKMIKEPADTEVLQYQLQHLTLRGDRVFARNNT | Function: Regulates the macrophage function, by enhancing the resolution of inflammation and wound repair functions mediated by M2 macrophages . The regulation of macrophage function is, due at least in part, to its ability to inhibit glycolysis . May also play a role in trafficking of proteins via its interaction with... |
A0A2P1DP74 | MCFFALEEWAAANRDYENTPAPYWHVKSVPDGFTAISGILWSISYILMAKKAFKDRSYAMPLHCLCLNITWEAVYGFVYGPGLLNQVVFAQWMIVDVVLFYAILRSAPYAWKQSPLVAQHLAGIIVVGCVICLWLHLAIAATFIPSIGRQVVFMTAWPMQVLINFSSIAQLLSRGNTLGHSWGIWWTRMLGTIAAACCFFWRIHYWPERFGYAWTPYGKFLLLGSIGSDMVYAAVYVYVQRIEKQLDSLVNTKAQKAR | Function: Terpene cyclase; part of the gene cluster that mediates the biosynthesis of macrophorins, isoprenoid epoxycyclohexenones containing cyclized drimane moieties . The first step of the pathway is the synthesis of 6-methylsalicylic acid (6-MSA) by the polyketide synthase macA . 6-MSA is then converted to m-cresol... |
P91193 | MMQQQKPGKPKKINRIDKIKRLQINRSRRPDINQTVPSPLFYVRIVVTWLGMVSLDAMTGFRFELLWPTWLMIRAAAESIQMRNQHCVTTIANPTAARFSVLFICVTATSDLICYLFIPIRMLIFLATTYVWISLYYHTQGGFLRSLATVYGGERLQSWPIVFITCFIVIFELFLRIRSHPILISFFPNVAEYAGVSPVWPRSLNAFFGAHSIGYPVILITVSMHYYFNEWKLRRKQCDVSNRNEQLFRILVEGLPAEYEGPKDYTSQQCLEDDLYYLDPPVQTLQPMQAIQAASATPPTSSKKNGIHKRNGDVTSSTTT... | Function: Plays a role in the regulation of neuronal activity. In AWA and AWC neurons, plays a role in regulating olfactory adaptation by controlling the forgetting sensory responses to odorants such as diacetyl and isoamyl alcohol . May play a role in regulating daf-7 expression in ASI neurons in response to bacterial... |
Q2TLY2 | MKRRNADCSKLRRPLKRNRITEGIHSSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFFVCVAFTSDIICLLFIPKQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKHFHVDLCRPFAAHCIGYPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQRQERETEEATSKGMSEADSVLVAQNGTAINKKLPISLPELEYKEKGKDSAKDKKQQQHSIGINNNILQTVDAKLQDIEYMENHLNAKRLNNELGGSAENLFLKEEVGAGGG... | Function: May play a role in the regulation of neuronal activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76082
Sequence Length: 664
Subcellular Location: Nucleus membrane
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Q2TLY1 | MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFFVCVAFTSDIICLLFIPVQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKHFHVDLCRPFAAHCIGYPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQLIQRQEREAEEAAAAAAAAASKSIHDVDSPAVAQNGSAGGKKPSSNTLPELEYREKERGKNESKKQHNHNQNHHSSTSSSILPSVDNKAQEMEYMENHVNSKRLSSSDLLGSTE... | Function: May play a role in the regulation of neuronal activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 78344
Sequence Length: 699
Subcellular Location: Nucleus membrane
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