ids
stringlengths 6
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Q7VRD3 | MINNRSVIIGIVVGENSGDILGVGLIRSLKKCFKKVQFFGIGGFRMRSENMECWYDISELSIMGITGVIFRLPKLLNMRRELIKRFLKLKLNIFIGIDFPDFNISLEKRLKKYGITTIHYVSPSIWAWRSNRVFALKEATHNVLLLFPFEKSIYARCGIPNQFIGHPLADEIPLYPNKIALRQKFDIPSNRCCLAILPGSRPKEIQILTKIFMHCAKLLQDTIPNLEILIPLHDTDLINQFVTLTSFISVKFRVLHTLTAWEVMAAADAALLTSGTATLECMLAKCPMVVAYRMNPVIFMLIRHLIKVKWISLPNLLAGKPIVQEFIQKKCDPQRLASSLFYLLNYNQEQRTTLQQEFYHLHRSIKLHANDQATRLILKYINLL | 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-glucosaminyl 1-phosphate + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine = H(+) + lipid A disaccharide (E. coli) + UDP
Sequence Mass (Da): 44187
Sequence Length: 384
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 5/6.
EC: 2.4.1.182
|
Q493B9 | MSSIVPSMHNNRTIIIGIVAGEASGDILGAGLIRTLKKYLKKVRFFGIGGPCMQSEDMKSWYNIEELSVMGFAEIVMKLPRLLYIRRNLARRFINLKPDVFIGIDSPDFNISLENRLKKRGIRTIHYVSPSVWAWRKKRIFALKKATDNILVILPFEKKIYDHFNIPCQFIGHSLADQIPLNPNKVSARQKLGIPHDVYCLAVLPGSRIREIKMLAHDFLVCAKLLKNNFPNLEILVPLTNQTSIKKFISVASTSVKYRVLSNQSAWEIMMAADASLVTAGTATLECMLVKCPMVVAYRMHPLTFMLAKHFINIPWISLPNLLAGHELVKEFIQNNCRPENLAQTLINLLNNNNQHIVLKKKFRQLHHSIRCNADEQAAYAVLRLIK | 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-glucosaminyl 1-phosphate + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine = H(+) + lipid A disaccharide (E. coli) + UDP
Sequence Mass (Da): 44034
Sequence Length: 387
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 5/6.
EC: 2.4.1.182
|
Q7WJ81 | MSLRIGMVAGEPSGDLLAGRIIAGLQARAPGVHCAGIGGPQMAARGFEAWHPMHALTVFGYIDAFKRIPSLLSTYGDVKRRLLAEPPSVFVGIDAPDFNLRLEHQLRQAGTPTVHFVGPSIWAWRYERINKIRAAVSHMLVLFPFEEALYRKEGIPVTYVGHPLAGVIPMQPDRAAARARLGIDADARVLAILPGSRSSEIRLLAPRFLQAAAELVRRDPRLQCVVPMVNPQRRAEFEAIAAQHPVPGLRCVTAAEGQGETPVAWSVMEASNAVLVASGTATLETALYKRPMVISYVLSPWMRRIMAWKSGQQRPYLPWVGLPNVLLRDFAVPELLQDEATPAALAEATWQALTDEAGAARIEARFTALHQDLLRDTPALAAQAILEVADGAA | 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-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Mass (Da): 42748
Sequence Length: 393
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.4.1.182
|
Q89KQ7 | MMQGRDPKRKIFLIATEESGDRLGSALMKVLRQRLGDGVQFEGVGGRTMAREGLETLFPIEELSIVGFAAVVQQLPKILRLIRETADAVLEAVPDALVIIDSPDFTHRVARRVRARNPAIPIVDYVSPQLWAWRPGRARTMLGYVDHVLGLLPFEPEEYRKLGGPPCSYVGHPLIEQLGSLRPNAEEQKRRNSELPVLLVLPGSRRSEIRHHIEVFGAALGRLQAEGRAFELMLPTMPHLEATVREGIASWPVKPQIVIGEAEKRAAFRIAHAALAKSGTVTLELALSGIPMVTAYRVGAIEAFILRRAIRVSSVILANLVIGEDVIPEFLQEDCTPEKLAPALSEVLTDSDMRRRQVEAFARLDTIMSTGNKAPSVLAADIVLATMRKGRR | 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-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Mass (Da): 43262
Sequence Length: 392
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.4.1.182
|
Q02AZ6 | MPKILVSAGEASGDLYASLVVQELRRIMPDAEFFGCTGPRLRAAGVRTIVDSADLAVVGLIEVVAHIPRIYGEFRKLLRAAREERPLLAILTDSPDFHLRVARKLHRQEVPVVYLVAPQAWAWRRGRVREMRRTIRRLLCIFPFEEEFFRRYGVPATYIGHPLAGLVHPALSREEFFKKHRLAAERPLVSVLPGSRRGEAARHIPALLDAVDRIYREQAVNVVLPASATTGVAFFQERMGNSPIRVIEGESWDAMAHSDLALAASGTVTVEAALLGTPMVTFYKVTGVSWLAGKFLVDIPFYSMVNLIAGRAVVPELMQSQMTGENLAREALRLLQGGRDREEMKAGLAQVKEKLAGRTGAPGRAALAIQEILEGQVTHVS | 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-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Mass (Da): 42109
Sequence Length: 381
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.4.1.182
|
Q2LVL8 | MNSKLVLIVAGEASGDLHGASLVGAMVKREPGIRFYGIGGVNLKTAGVDLWADAADMAVVGLTEVASKLRGILTVMHRLKKSMQLLKPDLVILIDYPDFNLPLARSAKKNGIPVFYYISPQVWAWRKGRLRTISGLVDRMAVILPFEEPLYRQAGVDVSFVGHPLLDVVQATSSRDETLRMFGLREDVTTVALLPGSRKGEVTRLLPVMLKAARILTENICPVQFLLPMANTLDETWMKDQIAKADPPGVRLIRGATYDAVAAADAAVVVSGTATLETALLGTPLIVIYKVSALSYLIGRMLISVDHIGLVNIVAGKTVAPELIQGAANPERIAAEILAILGQPDRRKAIQEELSHLRDKLGLPGAAERAAVMALTLIKKSDC | 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-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Mass (Da): 41277
Sequence Length: 383
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.4.1.182
|
Q3A550 | MHEVKQPRRIMVVTGEASGDLHGAHLIEAAGKVDPGLSFFGVGGACMAKAGCEILIPGEDLAVMGLVEVLGHFPTIWRAFRKLKKILHGPQRPDALVLIDFAEFNLLLAAQAKKAGVPVLYYVSPQVWAWRRGRVRRIASVVDRLAAIFPFEPELYQGLDIDVEYVGHPLLDEFAITCERDAFLRRLGLDPARQVIGLFPGSRKNELKYIAETILQSAVKLREKHPDAQFLLPVASSFRRQDIEALVAPYGLPVTVVDEPIYDVINACDAVISVSGTVTLQVALVGTPMAIVYKMAPLSFAIGKRLIRVPHIGLANIVAGRGVVKEFIQEDATPAMISREIDAILTDAEYNRSIRGGLATVQQRMGEGGCAARVARMVSELCREIPGKERMV | 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-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Mass (Da): 42903
Sequence Length: 392
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.4.1.182
|
Q57310 | MRIFISTGEVSGDLQGSLLVGALRQQAEEQNLELELVGLGGEKMAAAGLTLLANTAAIGSVGLTESLRFIIPTWQIQQRVKRYLKTNPIDLLVLIDYMGPNLTIANYLRKTYPNLPILYYIAPQAWVWSPTKRETAQIMAVTDRLLAIFPGEAEFFQKQGLDVTWVGHPLLDRITKEAPSRGSAREKLGIDHNETVITLLPASRIQELRYLLPSICGAAQQLQSQLPNVKLLLPVSLKDYQPQIEQTLKEFNLTVQLLEGKETLTAIAAADLAITKSGTVNLEIALLNVPQVILYRVSPLTMAIARRIFKFNLPFVSPTNIVLNRGIMPELLQEQATASNIAQAGLELLLNGDRQAKIAQDYQELREALGEPGVCERAAQAVLEFANGQQKSRA | 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-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Mass (Da): 43468
Sequence Length: 394
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.4.1.182
|
Q3SKM8 | MVAGEASGDLLGAHFFDALKKNRPGLTAAGIAGPRMVEAGVKAIYPSEKLAVNGYVEVLRHLPELLWIRARITRHFLRERPRVFVGIDAPDFNFTLEAALKRAGVPTIHFVSPSIWAWRPERIERIKQAVSHMLVVFPFEEAIYRDAGIPVSYVGHPLADVIPLQAPTGAARATLGLGDGPIVALLPGSRLSEVDRHARLMLEAAMQVRAKEMDVRFVLPAASEAARERIARAAQGLDLPLTVLAGRSHQALAACDVAVVASGTATLEAALFKKPMVITYRVPALTARLMRKKALLPWIGLPNILARDFVVPERVQEAATPDALAADVLAWLGDAARRAALAVTFDALHRDLRQGASARIAAAIAPYLEAAR | 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-glucosamine = a lipid A disaccharide + H(+) + UDP
Sequence Mass (Da): 40189
Sequence Length: 372
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.4.1.182
|
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
Sequence Mass (Da): 33485
Sequence Length: 307
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 2/6.
EC: 3.5.1.108
|
P21645 | MPSIRLADLAQQLDAELHGDGDIVITGVASMQSAQTGHITFMVNPKYREHLGLCQASAVVMTQDDLPFAKSAALVVKNPYLTYARMAQILDTTPQPAQNIAPSAVIDATAKLGNNVSIGANAVIESGVELGDNVIIGAGCFVGKNSKIGAGSRLWANVTIYHEIQIGQNCLIQSGTVVGADGFGYANDRGNWVKIPQIGRVIIGDRVEIGACTTIDRGALDDTIIGNGVIIDNQCQIAHNVVIGDNTAVAGGVIMAGSLKIGRYCMIGGASVINGHMEICDKVTVTGMGMVMRPITEPGVYSSGIPLQPNKVWRKTAALVMNIDDMSKRLKSLERKVNQQD | 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 (3R)-3-hydroxyhexadecanoyl-ACP as the acyl donor in vitro, which is consistent with the structure of E.coli lipid A that contains over 95% (R)-3-hydroxytetradecanoate at the 2 and 2' positions.
Catalytic Activity: a (3R)-hydroxyacyl-[ACP] + a UDP-3-O-[(3R)-3-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 36038
Sequence Length: 341
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 3/6.
EC: 2.3.1.191
|
B2KAU6 | MQISLEELVKITGGELRGNKDFQITAPCSIDNPKEDAVCYFSDGSKAESISSIKAGCFILPSKIKETFKTDKNVIFADNPEWAFTLFLRHYDSSKPKFDRGVHPTAVIGKNVVLGNNITVGAYSVIEDDVTLGDNTVIYPHVYIGRRTFVGKDCILYPNVVVREECIIKDRVIIEAGATIGTDGFGFVLVNYKHEKIPQVGNVIIESDSEIGANTTIDRAKIDSTVIGVNVKVDNLTQLAHNVKVGQGSIIISQVGVAGSTEIGRGVVLAGQVGVAGHIKIGDGVQVGAQSGIMQDIPAGKKMFGTPVRDYMETLKLYAALPYLSEMVREFRKRKKTEENK | 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-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 37097
Sequence Length: 341
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q8R6D9 | MEYRVTDIITLLNAEYKGEVVEKVSKLSPFFHSDEKSLTFAADEKFLKNLSQTKAKVIIVPDIDLPLIEGKGYIVVKDSPRVIMPKLLHFFSRNLKKIEKMREDSAKIGENVDIAPNVYIGHDVVIGNNVKIFPNVTIGEGSIIGDGTVIYSNVSIREFVEIGKNCVIQPGAVIGSDGFGFVKVNGNNTKIDQIGTVIVEDEVEIGANTTIDRGAIGDTIIKKYTKIDNLVQIAHNDIIGENCLIISQVGIAGSTTIGNNVTLAGQVGVAGHLEIGDNTMIGAQSGVPGNVEANKILSGHPLVDHREDMKIRVAMKKLPELLKRVKALEEKK | 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-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 36064
Sequence Length: 332
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q74AT5 | MAVSKTLQELADYLGGTLVGDGSRQIVGVASLDDATDSQITFLANPRYAPKVASTRAGAVILPPGAERHNHNAIMVPNPYLAFARLLTLFYVAPRAARGVMDGAHVGRNVKLGSEITIHPGAVVGDNVTIGDRVTLHPGVVLYEGVTVGDDVTLHANVTVYQGCRIGNRVTIHGGTIIGSDGFGYAPDGDGWYKIPQLGNVVIEDDVEIGANAAIDRAALASTVIGKGTKVDNLVMIAHNCVIGENCMIVSQVGISGSTKLGRRVTLGGQVGVAGHLEIGDNAMIGAKSGVPGNVPSGTIMSGIPAFDHREWLRASAVVPKLPEMKRTVAALEKRLRELEEKLESAV | 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-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 36274
Sequence Length: 347
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q0BTL2 | MSVQEVVGDPRFFARSGPYDVAAVAEAVGASIPADCTLSLTGVAPLQIAGPSEVSFLDNRRYADALEQTRAGAVIIKADMVDRVPAGVIALVVPEPYLAWARVAALFYPLPPVQPGIHPSAVVDETACIDPSAQIGPLAVIEAGVEIGPDCRIAAHAVIGAGVKMGRSCRIGSHASLSHAILGDRVYVYPGVRIGQDGFGFAPSSEGFVTVPQLGRVVLENDVEVGANSTIDRGSMHDTVIGAGSRLDNLVMIAHNVRMGRACVIVSQVGISGSTTLGDHVVLAGQAGLIGHLKIGSGARIGAQAGVMADVPAGAEIVGSPAQPAKDFFRQIATLRRLARR | 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-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 35170
Sequence Length: 341
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q7VM24 | MAVFRLSELAEQIGATLKGNADLAITSIAALNNAEPTHITFISNAKYRSQLSQSKAGAIIVTAEDVEFCQATQNLLIVKDPYLAYALLAQYMDDLPKSANEISESAVISATAKLGKNVSIGANVVIESGVELADDITIGAGCFIGKNTKIGARSHLWANISVYHNVEIGSDCLIQSSAVIGSDGFGYANDKGRWIKIPQTGGVIIGNRVEIGACTCIDRGALDPTIIEDNVIIDNLCQIAHNVHIGFGTAIAGGVILAGSLKIGRFCQIGGASVINGHMEICDGAIITGMSMIMKPITEKGVYSSGIPAQTNKEWRKTAALTMNIADMNKRLKAIEKQLTE | 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-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 36051
Sequence Length: 341
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
Q2SBQ8 | MGKTDLSYTLADIAFRIGAELRGDGSVEVKGLATLQKAQAGQISFLANKNYLKHLKDTCASAVIIPSSFADQCSTNVLVMENSYFGYALCSQLFSPQWWSMSGISPSAAISESAKLGAGVTIGANVVIEEDAEIGEGAVIGPGCYIGAGSIIGAKTQLRPNVTVYHGVNIGARALIHSGAVIGSDGFGFAPNKGDWAKIAQLGGVVIGDDVEIGANTTIDRGALDDTVIETGAKLDNQIQIAHNVKVGAYTVIAACVGVSGSSSIGKHCMIGGGVGIAGHLEITDQVQITGMTLVTHNIKEPGVYSSGTAVEPNASWRKNVARFRQLDQLARRVRVLEQGGRRKSDAD | 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-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 36219
Sequence Length: 348
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
A1WT71 | MTSAMTVQELAARLGARLAGDGERPVCRAATLLGAGGDAVSFCTSKRHLPELRRSGAAAVLVRAEHEGDCPGTALVVEDPYLAFIEVVELLHPEPSAPPGIHPGAVVASDVVLGDGVSVGANAVIEAGVELGAGSTVAPGAFIGPGARLGTGSWLGPNAVLAGGCRTGERVRIHAGAVIGADGFGYAPLPDGQGWRKVPQIGGVDIGDDVEIGANATVDRGALEDTVIEAGVKLDDHVHIAHNCRVGARTVIAGGTLVAGSTTIGRDCLIGGLVAITDHIRIADGVSLMGMTGVTGSIRESGAYASPLPAQPVRQWRRNTVRFTQLEGLFRRVQALETGHGMVGDAGEERDD | 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-hydroxyacyl]-alpha-D-glucosamine = a UDP-2-N,3-O-bis[(3R)-3-hydroxyacyl]-alpha-D-glucosamine + H(+) + holo-[ACP]
Sequence Mass (Da): 35877
Sequence Length: 352
Pathway: Bacterial outer membrane biogenesis; LPS lipid A biosynthesis.
EC: 2.3.1.191
|
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 glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: H2O + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine = 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + 2 H(+) + UMP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 27705
Sequence Length: 246
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 4/6.
Subcellular Location: Cell inner membrane
EC: 3.6.1.54
|
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 glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: H2O + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine = 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + 2 H(+) + UMP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 26325
Sequence Length: 237
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 4/6.
Subcellular Location: Cell inner membrane
EC: 3.6.1.54
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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 glycolipid that anchors the lipopolysaccharide to the outer membrane of the cell.
Catalytic Activity: H2O + UDP-2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosamine = 2-N,3-O-bis[(3R)-3-hydroxytetradecanoyl]-alpha-D-glucosaminyl 1-phosphate + 2 H(+) + UMP
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 28233
Sequence Length: 243
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 4/6.
Subcellular Location: Cell inner membrane
EC: 3.6.1.54
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Q2T0K1 | MSARPGLLARAEARLTREWQRRGALAWALTPFACAFGAIAALRRAAYARGWKARVDCGVPVVVVGNVTVGGTGKTPTVIALVDALRAAGFTPGVVSRGYGAKIVAPTAVTPASAPQQAGDEPLLIARRTLAPVWVCPDRVAAVRALKAAHPEVDVVVSDDGLQHYRLARAVEIVVFDHRLGGNGFLLPAGPLREPLSRRRDATLVNDPYSRALPPWPDTFALSLAPGDAWHLARPSRRKPLAQFAGERVLAAAGIGAPERFFATLRAAGVTPATRALPDHYAFATNPFVDDHFDAILITEKDAVKLGTSWRDARIWVVPVEAALDPRLIALVVEKLRGRTSA | 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
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
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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
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
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Q4FS43 | MNIETTITRAWQRQAAWLWLLLPVSWLYSLLMILRRQAYKAGIFSSYRAPIPVMVIGNITVGGSGKTPLIIALVRHLQQQGIKVGVISRGYGGDSSQMPALVNTESVPNIVGDEPCLIVNMTGVAMAVCPNRQQAMTTLLASYPDLQLIIADDGLQHYALQRDIEWIVVDAARGFGNKQLLPTGFLREPMSRLKGANVVYHQKADSLSSTDDKYDDTCPPTKRLRMHLQPDNLERLWSFDTQSDGLATVKAMAPEKGSRVHAVSGIGYPQRFFDTLDTLGFQVSPHPYPDHHDFSLTELLRYTEHPIIVTSKDAVKIRALLMQETINQTNQTNQTLSDEYNELGSRLWVLPVTAVLSDGCYEILQQQLQTLNIAISSKEHERVIT | 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
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
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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
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
|
P58185 | MASEAPPFWWEEPDWKVLALSPLSAVYALVAGRVMRRARREKIEAPVLCVGNFTVGGTGKTPVAIALAQQAKRMQLKPGFLSRGHGGSFAEPHVVDAHHDAAKHVGDEPLLLAEHAPVAVTPNRAAGARLLMAKHGCDFLIMDDGFQSARIHIDYALIVVDARYGIGNGRVIPGGPLRAKIVDQLVFTSGLLKMGEGTAADAVVRQAARAGRPIFEARAEPISKAGLAGKRFLAFAGIGHPDKFFDTVREAGGEVVLSKPFPDHHFYAEDELAELAAVARAEGLGLITTAKDAARLRHGASQDFLNRLEVLEIDTVFELDHAPERIIEETLDAWRQRKLRS | 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
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
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Q7UNW7 | MSWDYRPLLSGQSRDPFSSMARGALWCASGFYNVAARHRRRQYDSGNREICNAGVPVISVGNLTTGGTGKTPVVADLCRRLRAMDFRVTIISRGYGASDGRMNDEAMELQERLPDVPHVQHPDRVEAARIAVEELAAEVLVMDDGFQHRRLQRDLDIVVIDATCPFGYGHVLPRGTLREPLDSVTRADWVLITRVDQVDPEEVLAIRSTIAQHAPDCPVLETEHRPSTIQSSVGDWEAIEVLIDQPVALVSAIGNPDAFEQTVLDCGAIVVDHLRLPDHDSYERATREKLRSWVTKLKGGPQPPQRLLCTHKDAVKLATDSIAGVPLGYMPIELAYRTSEEPLQLRLELLMGGSVENQSSRDDSA | 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
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
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B6IXD8 | MKAPAFWYAPPGTARPLLSALLTPAALAWTAATRRRLSGTRPWHAPVPVICVGNLVAGGAGKTPVVLDLLSRLRRGGLDAHALSRGHGGRLPGPLRVDPARHTAAEVGDEPLLLAAAAPAWIARDRAAGARAAADAGAGVLVLDDGFQNPGIAKDLSLLVVDGDAGFGNGRVIPAGPLREPVADGLARAQAVLLLGEDRRGTADLCRGRLPVLRGRLVPDPQAAADLEGRRVLAFAGIGRPEKLFRTLEALGADVVARLPFPDHHPFTAAELRALLDRAAALDALPVTTQKDLVRLPAELRGQVRALPVSIAWEEPDTLDRLLAPLLSGKDDHGQAQ | 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
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
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Q2RWV9 | MRAPEFWHKDGFAARLLEPVGLVYAALTRHRVARPPGVRLGIPVVCVGNLTAGGAGKTPVALAVMDALRRRGVVGHFLSRGYGGKMEGPVAVDPVGHGPEDVGDEPLLLANSAPCWVSRNRASGGLVAEGAGAQAVVMDDGHQNPSLAKDLSLVVVDGGYGFGNGRYIPAGPLRESIEAGLARAGAVILIGSDSENLAARIPPHLKAGVPLLTARLEPGPEAARLVGRKVVAFAGIGRPEKFFATLTALGARVVARHPFADHYPYAEADIQPILDEAYGLGAVPVTTSKDAVRLPPDQRPQVDVVGVRVVFDEPLAFEALIDRLILGRLPS | 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
Pathway: Glycolipid biosynthesis; lipid IV(A) biosynthesis; lipid IV(A) from (3R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] and UDP-N-acetyl-alpha-D-glucosamine: step 6/6.
EC: 2.7.1.130
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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 type I membrane protein
Sequence Mass (Da): 32082
Sequence Length: 294
Domain: The transmembrane domain is necessary for interaction with KCNMA1.
Subcellular Location: Cell membrane
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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 response to antibiotics and environmental stresses.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16399
Sequence Length: 152
Subcellular Location: Cell membrane
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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 Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 18600
Sequence Length: 165
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
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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 Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17437
Sequence Length: 164
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
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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 Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19818
Sequence Length: 168
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
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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 Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17083
Sequence Length: 159
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
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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 Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17937
Sequence Length: 166
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
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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 Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16658
Sequence Length: 152
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell membrane
EC: 3.4.23.36
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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 Ala) have small, neutral side chains.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19285
Sequence Length: 166
Pathway: Protein modification; lipoprotein biosynthesis (signal peptide cleavage).
Subcellular Location: Cell inner membrane
EC: 3.4.23.36
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Q1C138 | MPHTVATPPPLLQVRGISKQFSGVVVLKSIDFTLQPGQVHALLGGNGAGKSTLMKIIAGILPPDTGVIEMNGQPCFNLTPAKAHQLGIYLVPQEPMLFANLSVQENILFRLPKHQADKKKMAQLLKNLGCHLDLSVSAGSLEVADQQLVEIMRGLIRDSHILILDEPTASLTPAETHRLFSQIRMLLQQGVGVVFISHKLPEIRQLADWVSVMRDGGIALSGATADFSTEDMIQAMTPEAQKGALTDSQKLWLELPGNRRAQSHAQSQQPVIHVHDLSGEGFAHISFHVQAGEILGLAGVVGAGRTELAETLYGLRPASTGNVILEEVNITAMKTANRLAAGLVYLPEDRQASGLYLDAPLSWNVCALAHDRQGLWTQPAQEAAVLERYRRALNIKFSHLEQPVRTLSGGNQQKLLIAKCLEANPLLLIIDEPTRGVDVSARSDIYQLIRSIAEQQVAIIFISSDLEEVVQMADRVLVMHQGEINGALSGAAMNVDTIMHMAFGEHRSASEPQGGTASSAENKGASC | 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-tetrahydroxytetrahydrofuranSide 2 + [AI-2-binding protein]Side 1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56928
Sequence Length: 527
Subcellular Location: Cell inner membrane
EC: 7.6.2.13
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Q9HCC9 | MMNRFRKWLYKPKRSDPQLLARFYYADEELNQVAAELDSLDGRKDPQRCTLLVSQFRSCQDNVLNIINQIMDECIPQDRAPRDFCVKFPEEIRHDNLAGQLWFGAECLAAGSIIMNRELESMAMRPLAKELTRSLEDVRGALRDQALRDLNTYTEKMREALRHFDVLFAEFELSYVSAMVPVKSPREYYVQQEVIVLFCETVERALDFGYLTQDMIDDYEPALMFSIPRLAIVCGLVVYADGPLNLDRKVEDMSELFRPFHTLLRKIRDLLQTLTEEELHTLERNLCISQDVEFPIRADVQGPAALAPALSAPLPPEGPLSAKAKDPDAELACSMQYDDQELEQLSRMVHRAGDEMSSLLSPPIACQSPAHRPGAEGSPGGEASPGRPRLRSGSDEEERVFFMDDVEGTAEALARPESPAGPFGWAGSTWADPQEKGQGGPGGAAGISLPASEKEEDLSNNNLEAEGTDGASLAGTSSCSCLDSRLHLDGWEVGADDAETAEMIAHRTGGMKLSATVIFNPKSPTSLDSAVATQEAASEPVAEGMDGGPHKLSTGATNCLLHSCVCCGSCGDSREDVVERLREKCSPGGVIGASYAAGLAKASDRAPERQEEAPPPSEDASNGREPKAPTSDKCLPHTSGSQVDTASGLQGEAGVAGQQEPEARELHAGSPSAHEAPQALSGSSSSTAGSCSSDKMGPEAAPAATHAAPQATREKIRSRFHGSHDLIHRLFVCISGVADQLQTNYASDLRSILKTLFEVMATKPETDDKEKLRKVTQTLRSAALEDCALCQETLSSSELAAKTRDGDFEDPPEWVPDEACGFCTACKAPFTVIRRKHHCRSCGKIFCSRCSSHSAPLPRYGQVKPVRVCTHCYMFHVTPFYSDKAGL | 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): 96490
Sequence Length: 887
Domain: The FYVE-type zinc finger mediates the interaction with phosphatidylinositol 3-phosphate (PI3P) and localization to early endosome membranes when not monoubiquitinated at Lys-87.
Subcellular Location: Cytoplasm
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Q6ZPK7 | MMNRFRKWLYKPKRSDPQLLAQFYYADEELNQVAAELDSLDGRKEPQRCTLLVSQFRSCQDNVLNIINQIMEECIPQDRAPRDFCVKFPEEIRHDNLAGQLWFGAECLAAGSIIMNRELESMAMRPLAKELTRSLEDVRGTLRDQALRDLNTYTEKMREALRRFDVLFAEFELSYVSAMVPVKSPREYYVQQEVIVLFCETVERALDFGYLTQDMIDDYEPALMFTIPRLAIVCGLVVYADGPLNLDRKVEDMSELFRPFHTLLRKIRDLLQALTEEELHTLERSLCVSQDVELPIRADTQAPSALAPTFSASLPPEETLSASANNPEAELACSMQYDDQELEELSRMVHRAGDEMSSLLSPPSACQSPAHRPGSEASPRGEASPARARLKSGSDEEERVFFMDDVEVTESPARPESPGNTFELTQGNAQQRGQDGQSGEVGVEAPALVKEEDWSNNNVEGDKIKLASLMGSTSCSCLDSQLYLDGWEVSAEDAETAEMIAHRTGGMKLSATVIFNPKSPTSQDSAVAAQEAPGHGTSPLEPRAEGTGDNSHKLSTTATNCLLHSCVCCGSCGDSRDDAVERLREKCGPGSVISASNPSVSLAKGGDKEPERIDEAQPSDVTLPAEDASNRQEPKAPASSKCLAHTSGPQVDTASRLQGEGEVKGQPEPEARKQDPEKSPVVSGDSPRGDVAQTEHQHLLGSSSTVGSCSLDNTRLDVATAAMPVTPMATREKIRSRFHGSHDLIHRLFVCISGVADQLQTNYASDLRSILKTLFEVMATKPETDDKEKLKKVTQTLRSAALEDCALCQETVSSSELAAKTRDGDFEDPPEWVPDEACGFCTSCKAPFTVIRRKHHCRSCGKIFCSRCSSHSAPLPRYGQVKPVRVCTHCYMFHVTPFYSDKTGM | 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.
Sequence Mass (Da): 99787
Sequence Length: 905
Domain: The FYVE-type zinc finger mediates the interaction with phosphatidylinositol 3-phosphate (PI3P) and localization to early endosome membranes when not monoubiquitinated at Lys-87.
Subcellular Location: Cytoplasm
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Q0P4S0 | MMNRFRKWLYKPKRSDPQLLAQFYYADEELNQVAAELDSLDGRKDPQRCTLLVNQFRSCQDNVLNIINQIMEECIAHERANRDFCVKFPEEIRHDNLAGQLWFGAECLAAGSIIMNREIESMAMRPLAKDLTRSLEEVRNLIRDQALRDLNIYTEKMKESLRHFDVLFAEFELSYVSAMVPVKSPKEYYVQQEVIVLFCETVERALKLGYLTQDMIDDYEPALMFTIPRLAIVCGLVVYAEGPLNLERKPEDMSELFRPFHTLLRKIRDLLQTLTEDELHTLERNLCISQDVEFPANADPEVPSAISPVLVTALPTEEPPMAKAENTEVELACSMQYDEQELEQLNMMVHRVGDEMSSLLSPPSVYQSPAHRANTSNEASPCRRALDNLTDEEDRVFFMEDLDGSGEVLARSRPSETTISWVNNSCYNAKQPALYQDSVLQNGDLADVVSVKDGQRDISNNNNIDGSKMLAASASLQNSCSCLEAPESQLYLNGWDTNGEDAETAEIIAHRTGGMKISATVIFNPKSLTNSPETSPNLASNRIPSSSDPLTSNEEDESHKLSIAATNCLINSCVCCGSCEDTREDSLEGLRNVPSSGKVINASYSLIKSKELGHLDRSDCTVSAKELLKMDSPTVLLAEKETTRQEQPYPNSSKCLPLNSGSQVEMDSESDEPLTASRDQLRSESNRQETGNKERPSEEVEEPPSDRASADNITSSSSSQDGLRDSALSSISSSDYESVSVTTCSLSSIDSLSSCSSDDIDQEEIQLALQAAKIASRQKIRSRFHSSNDLIHRLFVCISGVADQLQTNYASDLRSILKTLFEVMATKQETDDKGKQKKANQGLRSAALEDCALCQETITSSELAAKARDGEFEDPPDWVPDEVCSLCTACKAPFTVIRRKHHCRSCGKIFCSRCSSHSAPLPRYGQMKPVRVCTHCYMFHVTPFYSDRAGM | 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.
Sequence Mass (Da): 106143
Sequence Length: 951
Domain: The FYVE-type zinc finger mediates the interaction with phosphatidylinositol 3-phosphate (PI3P) and localization to early endosome membranes when not monoubiquitinated at Lys-87.
Subcellular Location: Cytoplasm
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Q8I4E2 | MAQVKAEYDFQSQPNTGELSISAGEVLTVIRENIDGGWIEGRNVRGSVGLFPESYVTPYQASRPPPVLPPPLPPTSSGPPAASSRPFDDWGGASEVAAPPSYGAQHHHQPTPSVPEVTRSSYPSQNDDFDDEWTDEDDEQEPTRPNVQSSIGSNSRRDLSRSHSEHGGPDRGSNKVNKNINRFSNFVKSGVEAYVIGESKTTSQISERHEVVMNNGIIQWKPIQQYYTCIVDKPKKESKLKGLKSFIAYSITSSLTNIQRQVSRRYKHFDWLHEQLSAKYVLIPIPPLPEKQVAGRYEEDLIDHRKHILQLWVNKICRHPVLSQSEVWLHFISCTDEKDWKNGKRRAEKDEYIGGAFLNCITVPHQPLDPNNVDMQVERFQRSVKTSEEAMRVMQERMNMFQKVFAGPVKQNWQKMGSAFKTLQQSFEIDETVASRRLTEALAYTASEYHEIGQVFDAHTKNDMEPVLENLYSYKGTVQNVPDIIQVHKQAVQKFRDSEGRLSSAEAEKMKQRIDAMSYTVIAEVQHQTAEKVEDMKSTMGTYLKKQAMFYQEVATKLTSLAARYD | 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 dyn-1. These are events leading to phagosome maturation which is a step in apoptotic cell corpse clearance. Binds phosphatidylinositol-3,4,5-trisphosphate.
Sequence Mass (Da): 64329
Sequence Length: 566
Domain: The BAR and PX domains are required for recruitment to the phagosome.
Subcellular Location: Cytoplasm
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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 | MMARFVSVSSCQFHFGFREVSPPSVTSYPRRFEVSDRRFPAIPIKCSSSEPENGEDSAPSLSSSSSSSTSEVSTSNSSTYNWYTGIGGIGMLDTAYLTYLKVTGSDAFCPIGGGTCGDVLNSDYAVVFGVPLPVIGFVMYGVVTALSAELGEGNLPFGISKSNGRFALFGITTAMASASAYFLYILSTKLSGSSCLYCLVSAFLSFSLFFLSVKDVKLQEIQQVVGLQICLAIIVVASLTASYSTAQPIPSRSGDIELPYFRTEISSSSSPYAIALAKHLNSIGAKMYGAFWCSHCLEQKEMFGREAAKELNYVECFPDGYKKGTKILKACADAAIEGFPTWIINDKVLSGEIELAELAEMTGFSLDQANETNQLQ | 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 in the thylakoid lumen. Involved in the formation of disulfide bonds in the lumenal protein FKBP13. In vitro, reduces phylloquinone (vitamin K1) and menaquinone (vitamin K2) to their respective quinol. Cannot reduce phylloquinone epoxide to phylloquinone . Plays an important role in regulating the thylakoid lumen redox .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40401
Sequence Length: 376
Domain: Cysteine residues from the thioredoxin-like domain participate in a series of disulfide-exchange reactions that regenerate the redox-active cysteine residues in the transmembrane domain.
Subcellular Location: Plastid
EC: 1.17.4.-
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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 Ragulator plays a dual role for the small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD): it (1) acts as a guanine nucleotide exchange factor (GEF), activating the small GTPases Rag and (2) mediates recruitment of Rag GTPases to the lysosome membrane . Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated . LAMTOR1 is directly responsible for anchoring the Ragulator complex to the lysosomal membrane . LAMTOR1 wraps around the other subunits of the Ragulator complex to hold them in place and interacts with the Rag GTPases, thereby playing a key role in the recruitment of the mTORC1 complex to lysosomes . Also involved in the control of embryonic stem cells differentiation via non-canonical RagC/RRAGC and RagD/RRAGD activation: together with FLCN, it is necessary to recruit and activate RagC/RRAGC and RagD/RRAGD at the lysosomes, and to induce exit of embryonic stem cells from pluripotency via non-canonical, mTOR-independent TFE3 inactivation (By similarity). Also required for late endosomes/lysosomes biogenesis it may regulate both the recycling of receptors through endosomes and the MAPK signaling pathway through recruitment of some of its components to late endosomes . May be involved in cholesterol homeostasis regulating LDL uptake and cholesterol release from late endosomes/lysosomes . May also play a role in RHOA activation .
PTM: N-terminal myristoylation and palmitoylation mediates its recruitment to lysosome membranes, thereby promoting localization of the Ragulator complex to lysosomes . N-myristoylation by NMT1 is required for palmitoylation at Cys-3 and Cys-4 . May be palmitoylated by ZDHHC3 .
Location Topology: Lipid-anchor
Sequence Mass (Da): 17745
Sequence Length: 161
Subcellular Location: Lysosome membrane
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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 Ragulator plays a dual role for the small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD): it (1) acts as a guanine nucleotide exchange factor (GEF), activating the small GTPases Rag and (2) mediates recruitment of Rag GTPases to the lysosome membrane. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. LAMTOR1 is directly responsible for anchoring the Ragulator complex to the lysosomal membrane. LAMTOR1 wraps around the other subunits of the Ragulator complex to hold them in place and interacts with the Rag GTPases, thereby playing a key role in the recruitment of the mTORC1 complex to lysosomes.
PTM: N-terminal myristoylation and palmitoylation mediates its recruitment to lysosome membranes, thereby promoting localization of the Ragulator complex to lysosomes. N-myristoylation by NMT1 is required for palmitoylation at Cys-3 and Cys-4.
Location Topology: Lipid-anchor
Sequence Mass (Da): 17772
Sequence Length: 162
Subcellular Location: Lysosome membrane
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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 role for the small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD): it (1) acts as a guanine nucleotide exchange factor (GEF), activating the small GTPases Rag and (2) mediates recruitment of Rag GTPases to the lysosome membrane . Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated . Adapter protein that enhances the efficiency of the MAP kinase cascade facilitating the activation of MAPK2 (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13508
Sequence Length: 125
Subcellular Location: Late endosome membrane
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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 plays a dual role for the small GTPases Rag (RagA/RRAGA, RagB/RRAGB, RagC/RRAGC and/or RagD/RRAGD): it (1) acts as a guanine nucleotide exchange factor (GEF), activating the small GTPases Rag and (2) mediates recruitment of Rag GTPases to the lysosome membrane (By similarity). Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated (By similarity). Adapter protein that enhances the efficiency of the MAP kinase cascade facilitating the activation of MAPK2 .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 13480
Sequence Length: 125
Subcellular Location: Late endosome membrane
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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 modulating lamellar actomyosin retrograde flow that is crucial to cell protrusion and migration. Activates CDC42BPA/CDC42BPB and targets it to actomyosin through its interaction with MYO18A, leading to MYL9/MLC2 phosphorylation and MYH9/MYH10-dependent actomyosin assembly in the lamella.
PTM: Phosphorylated.
Sequence Mass (Da): 25891
Sequence Length: 239
Subcellular Location: Cytoplasm
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Q6TBX7 | MESSLFSPSSSSYSSLFTAKPTRLLSPKPKFTFSIRSSIEKPKPKLETNSSKSQSWVSPDWLTTLTRTLSSGKNDESGIPIANAKLDDVADLLGGALFLPLYKWMNEYGPIYRLAAGPRNFVIVSDPAIAKHVLRNYPKYAKGLVAEVSEFLFGSGFAIAEGPLWTARRRAVVPSLHRRYLSVIVERVFCKCAERLVEKLQPYAEDGSAVNMEAKFSQMTLDVIGLSLFNYNFDSLTTDSPVIEAVYTALKEAELRSTDLLPYWKIDALCKIVPRQVKAEKAVTLIRETVEDLIAKCKEIVEREGERINDEEYVNDADPSILRFLLASREEVSSVQLRDDLLSMLVAGHETTGSVLTWTLYLLSKNSSALRKAQEEVDRVLEGRNPAFEDIKELKYITRCINESMRLYPHPPVLIRRAQVPDILPGNYKVNTGQDIMISVYNIHRSSEVWEKAEEFLPERFDIDGAIPNETNTDFKFIPFSGGPRKCVGDQFALMEAIVALAVFLQRLNVELVPDQTISMTTGATIHTTNGLYMKVSQR | 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 . Possesses a major beta-carotene hydroxylase activity in planta when depleted in its preferred substrate alpha-carotene .
Catalytic Activity: alpha-carotene + O2 + reduced [NADPH--hemoprotein reductase] = alpha-cryptoxanthin + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Sequence Mass (Da): 60555
Sequence Length: 539
Subcellular Location: Plastid
EC: 1.14.14.158
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Q93VK5 | MAMAFPLSYTPTITVKPVTYSRRSNFVVFSSSSNGRDPLEENSVPNGVKSLEKLQEEKRRAELSARIASGAFTVRKSSFPSTVKNGLSKIGIPSNVLDFMFDWTGSDQDYPKVPEAKGSIQAVRNEAFFIPLYELFLTYGGIFRLTFGPKSFLIVSDPSIAKHILKDNAKAYSKGILAEILDFVMGKGLIPADGEIWRRRRRAIVPALHQKYVAAMISLFGEASDRLCQKLDAAALKGEEVEMESLFSRLTLDIIGKAVFNYDFDSLTNDTGVIEAVYTVLREAEDRSVSPIPVWDIPIWKDISPRQRKVATSLKLINDTLDDLIATCKRMVEEEELQFHEEYMNERDPSILHFLLASGDDVSSKQLRDDLMTMLIAGHETSAAVLTWTFYLLTTEPSVVAKLQEEVDSVIGDRFPTIQDMKKLKYTTRVMNESLRLYPQPPVLIRRSIDNDILGEYPIKRGEDIFISVWNLHRSPLHWDDAEKFNPERWPLDGPNPNETNQNFSYLPFGGGPRKCIGDMFASFENVVAIAMLIRRFNFQIAPGAPPVKMTTGATIHTTEGLKLTVTKRTKPLDIPSVPILPMDTSRDEVSSALS | 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
Sequence Length: 595
Subcellular Location: Plastid
EC: 1.14.-.-
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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 sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD) (By similarity).
Catalytic Activity: S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = (S)-4,5-dihydroxypentane-2,3-dione + L-homocysteine
Sequence Mass (Da): 17904
Sequence Length: 158
EC: 4.4.1.21
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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 sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
Catalytic Activity: S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = (S)-4,5-dihydroxypentane-2,3-dione + L-homocysteine
Sequence Mass (Da): 17164
Sequence Length: 151
EC: 4.4.1.21
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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 sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
Catalytic Activity: S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = (S)-4,5-dihydroxypentane-2,3-dione + L-homocysteine
Sequence Mass (Da): 16768
Sequence Length: 151
EC: 4.4.1.21
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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 sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
Catalytic Activity: S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = (S)-4,5-dihydroxypentane-2,3-dione + L-homocysteine
Sequence Mass (Da): 16932
Sequence Length: 151
EC: 4.4.1.21
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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 sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
Catalytic Activity: S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = (S)-4,5-dihydroxypentane-2,3-dione + L-homocysteine
Sequence Mass (Da): 17114
Sequence Length: 154
EC: 4.4.1.21
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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 sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
Catalytic Activity: S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = (S)-4,5-dihydroxypentane-2,3-dione + L-homocysteine
Sequence Mass (Da): 17212
Sequence Length: 155
EC: 4.4.1.21
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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 sensing. Catalyzes the transformation of S-ribosylhomocysteine (RHC) to homocysteine (HC) and 4,5-dihydroxy-2,3-pentadione (DPD).
Catalytic Activity: S-(5-deoxy-D-ribos-5-yl)-L-homocysteine = (S)-4,5-dihydroxypentane-2,3-dione + L-homocysteine
Sequence Mass (Da): 17395
Sequence Length: 158
EC: 4.4.1.21
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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 bioluminescence cycle begins with the hispidin synthetase that catalyzes the formation of hispidin which is further hydroxylated by the hispidin-3-hydroxylase, yielding the fungal luciferin 3-hydroxyhispidin. The luciferase then produces an endoperoxide as a high-energy intermediate with decomposition that yields oxyluciferin and light emission. Oxyluciferin can be recycled to caffeic acid by caffeoylpyruvate hydrolase (Probable).
Catalytic Activity: 3-hydroxyhispidin + O2 = (E)-caffeoylpyruvate + CO2 + hnu
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 30381
Sequence Length: 267
Subcellular Location: Membrane
EC: 1.-.-.-
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Q7Z3F1 | MNSNLPAENLTIAVNMTKTLPTAVTHGFNSTNDPPSMSITRLFPALLECFGIVLCGYIAGRANVITSTQAKGLGNFVSRFALPALLFKNMVVLNFSNVDWSFLYSILIAKASVFFIVCVLTLLVASPDSRFSKAGLFPIFATQSNDFALGYPIVEALYQTTYPEYLQYIYLVAPISLMMLNPIGFIFCEIQKWKDTQNASQNKIKIVGLGLLRVLQNPIVFMVFIGIAFNFILDRKVPVYVENFLDGLGNSFSGSALFYLGLTMVGKIKRLKKSAFVVLILLITAKLLVLPLLCREMVELLDKGDSVVNHTSLSNYAFLYGVFPVAPGVAIFATQFNMEVEIITSGMVISTFVSAPIMYVSAWLLTFPTMDPKPLAYAIQNVSFDISIVSLISLIWSLAILLLSKKYKQLPHMLTTNLLIAQSIVCAGMMIWNFVKEKNFVGQILVFVLLYSSLYSTYLWTGLLAISLFLLKKRERVQIPVGIIIISGWGIPALLVGVLLITGKHNGDSIDSAFFYGKEQMITTAVTLFCSILIAGISLMCMNQTAQAGSYEGFDQSQSHKVVEPGNTAFEESPAPVNEPELFTSSIPETSCCSCSMGNGELHCPSIEPIANTSTSEPVIPSFEKNNHCVSRCNSQSCILAQEEEQYLQSGDQQLTRHVLLCLLLIIGLFANLSSCLWWLFNQEPGRLYVELQFFCAVFNFGQGFISFGIFGLDKHLIILPFKRRLEFLWNNKDTAENRDSPVSEEIKMTCQQFIHYHRDLCIRNIVKERRCGAKTSAGTFCGCDLVSWLIEVGLASDRGEAVIYGDRLVQGGVIQHITNEYEFRDEYLFYRFLQKSPEQSPPAINANTLQQERYKEIEHSSPPSHSPKT | 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 . Upon cholesterol starvation, GPR155/LYCHOS is unable to perturb the association between GATOR1 and KICSTOR, leading to mTORC1 signaling inhibition .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 96919
Sequence Length: 870
Subcellular Location: Lysosome membrane
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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 substrate, and catalyzes the conversion of lycopene to the C(45) intermediate dihydroisopentenyldehydrorhodopin (DH-IDR) and the conversion of isopentenyldehydrorhodopin (IDR) to the C(50) carotenoid dihydrobisanhydrobacterioruberin (DH-BABR) . Can also catalyze the conversion of lycopene to tetrahydrobisanhydrobacterioruberin (TH-BABR) (Probable).
Catalytic Activity: all-trans-lycopene + dimethylallyl diphosphate + H2O = dihydroisopentenyldehydrorhodopin + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32067
Sequence Length: 294
Pathway: Carotenoid biosynthesis.
Subcellular Location: Cell membrane
EC: 2.5.1.150
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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 substrate, and catalyzes the conversion of lycopene to the C(45) intermediate dihydroisopentenyldehydrorhodopin (DH-IDR) and the conversion of isopentenyldehydrorhodopin (IDR) to the C(50) carotenoid dihydrobisanhydrobacterioruberin (DH-BABR) (By similarity). Can also catalyze the conversion of lycopene to tetrahydrobisanhydrobacterioruberin (TH-BABR) .
Catalytic Activity: all-trans-lycopene + dimethylallyl diphosphate + H2O = dihydroisopentenyldehydrorhodopin + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29589
Sequence Length: 275
Pathway: Carotenoid biosynthesis.
Subcellular Location: Cell membrane
EC: 2.5.1.150
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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 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): 21179
Sequence Length: 194
EC: 3.2.1.17
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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): 21385
Sequence Length: 195
EC: 3.2.1.17
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Q86UE4 | MAARSWQDELAQQAEEGSARLREMLSVGLGFLRTELGLDLGLEPKRYPGWVILVGTGALGLLLLFLLGYGWAAACAGARKKRRSPPRKREEAAAVPAAAPDDLALLKNLRSEEQKKKNRKKLSEKPKPNGRTVEVAEGEAVRTPQSVTAKQPPEIDKKNEKSKKNKKKSKSDAKAVQNSSRHDGKEVDEGAWETKISHREKRQQRKRDKVLTDSGSLDSTIPGIENTITVTTEQLTTASFPVGSKKNKGDSHLNVQVSNFKSGKGDSTLQVSSGLNENLTVNGGGWNEKSVKLSSQISAGEEKWNSVSPASAGKRKTEPSAWSQDTGDANTNGKDWGRSWSDRSIFSGIGSTAEPVSQSTTSDYQWDVSRNQPYIDDEWSGLNGLSSADPNSDWNAPAEEWGNWVDEERASLLKSQEPIPDDQKVSDDDKEKGEGALPTGKSKKKKKKKKKQGEDNSTAQDTEELEKEIREDLPVNTSKTRPKQEKAFSLKTISTSDPAEVLVKNSQPIKTLPPATSTEPSVILSKSDSDKSSSQVPPILQETDKSKSNTKQNSVPPSQTKSETSWESPKQIKKKKKARRET | 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 has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 63837
Sequence Length: 582
Subcellular Location: Endoplasmic reticulum membrane
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Q9Z1W6 | MAARSWQDELAQQAEEGSARLRELLSVGLGFLRTELGLDLGLEPKRYPSWVILVGTGALGLLLLFLLGYGWAAACAGARKKRRSPPRKREEVTPPTPAPEDPAQLKNLRSEEQKKKNRKKLPEKPKPNGRTVEIPEDEVVRTPRSITAKQPPETDKKNEKSKKNKKKSKSDAKAVQNSSRHDGKEVDEGAWETKISHREKRQQRKRDKVLTDSGSLDSTIPGIENTITVTTEQLTTASFPVGSKKNKGDSHLNVQVSNFKSGKGDSTLQVSSGLNENITVNGGGWSEKSVKLSSQLSAGEEKWNSVPPASAGKRKTEQSAWTQDPGDTNANGKDWGRNWSDRSIFSGIGSTAEPVSQSTTSDYQWDGSRNQPHIDDEWSGLNGLSSADPSSDWNAPAEEWGNWVDEDRASLLKSQEPISNDQKDSDDDKEKGEGALPTGKSKKKKKKKKKQGEDNSITQDTEDLEKDTREELPVNTSKARPKQEKACSLKTMSTSDPVEVLIKNSQPIKTLPPAISAEPSVTLSKGDSDKSSSQVPPMLQDTDKPKSNAKQNSVPPSQTKSETNWESPKQIKKKKKARRET | 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 has an effect on bone and brain metastasis, possibly by enhancing the seeding of tumor cells to the target organ endothelium. Induces chemoresistance (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 63969
Sequence Length: 581
Subcellular Location: Endoplasmic reticulum membrane
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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 peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 16373
Sequence Length: 147
EC: 3.2.1.17
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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 N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 16239
Sequence Length: 147
Subcellular Location: Secreted
EC: 3.2.1.17
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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-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.
Sequence Mass (Da): 14452
Sequence Length: 127
Subcellular Location: Secreted
EC: 3.2.1.17
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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 | MIHLMIMMLERVGIIVILGFILAHTKLFRQALQNQDGYKGKAILISIFSLFSIISNYTGIEIQRNMIVNNDWVFTIDPSGSIANTRILGVEIGGLLGGPFVGAGIGILAGLHRFSLGGSTALSCAVSSILAGVLAGLIGRYFTKRYRMPTPRIAALVGIGMESLQMIIILLMAKPFSDAWELVSMIGIPMILINGTGSFIFLSIIQAIIRKEEQARALETHRVLTIADQTLPFFRQGLNENSCKSVAAIIHKLTGTDAVSLTDKEKILAHVGAGMDHHIPSKSLITGLSKKVIKTGHIMKAISQEEIECTHAECPLHAAIVLPLTSNGNTIGTLKMYFKSPAGLSQVEEELAEGLAMLFSTQLELGEAELQSKLLKDAEIKALQAQVNPHFLFNAINTISALCRTDVEKTRKLLLQLSVYFRSNLQGARQLLIPLSKELNHLNAYLSLEQARFPGKYKIELNIDSRLEQIEIPPFVLQVLVENALRHAFPKKQDICKVTVCVLSDDASVYMKVADNGRGIPPDVLPELGKKPFPSKEGTGTALYNLNQRLIGLFGQQAALHISSEVHKGTEVSFQVPMQQMKEGEEHAQGVNS | 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 Location: Cell membrane
EC: 2.7.13.3
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Q8EQQ2 | MIELTIVLFQRIGLLLLMAFILTRIPRFRSLLDKDITLKTVIYHSLIFGLISIIGAHVGVVMIGNELIMQAWIINVAENEVLIGFSIVVVMIAGLLGGPFLGLGTGMVAGLYIIFLGGGGWVANSLINPLAGLLTGWAGQFFSDDRVMSPNKALFIGIFPPVLHMGLLLIMLPDQQIGVQIVNTIGIPLVVTNSIALTIFTMMIRLALNETEQEAALETNRALTIAEKALPLLSEEPGTMNARKMAKLLFKELDIAAISITNRTTVLSHVGLGDDHHQPGEPLKMRLSKKAVKDGRIQIAYHQSDIQCGVENCKLKTAIMVPIYRSGEVIGLINLYYRHSQQITAVEITLAKGLGTIISNQISGLEAEKMKKLLKEAKMRNLQAQINPHFLFNTFHLIHSLLRVDAEKARHILVQLSQFMRANLKIASESLVPLHKELEHLQAYLEIVQARFPDQISTSIHVDDYLLDIEIPPATLQPLVENSIQHGLSLSTSKGILTINITKTDNNVSIVLLDNGQGFEEKLLPILGKKPLHQNENKGNGIALYNINQRLISLLGEDSQLHIQNTDKGSMVQFILPYRNCKKIM | 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 Location: Cell membrane
EC: 2.7.13.3
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Q2FK10 | MLSLTMLLLERVGLIIILAYVLMNIPYFKNLMNRRRTWKARWQLCIIFSLFALMSNLTGIVIDHQHSLSGSVYFRLDDDVSLANTRVLTIGVAGLVGGPFVGLFVGVISGIFRVYMGGADAQVYLISSIFIGIIAGYFGLQAQRRKRYPSIAKSAMIGIVMEMIQMLSILTFSHDKAYAVDLISLIALPMIIVNSVGTAIFMSIIISTLKQEEQMKAVQTHDVLQLMNQTLPYFKEGLNRESAQQIAMIIKNLMKVSAVAITSKNEILSHVGAGSDHHIPTNEILTSLSKDVLKSGKLKEVHTKEEIGCSHPNCPLRAAIVIPLEMHGSIVGTLKMYFTNPNDLTFVERQLAEGLANIFSSQIELGEAETQSKLLKDAEIKSLQAQVSPHFFFNSINTISALVRINSEKARELLLELSYFFRANLQGSKQHTITLDKELSQVRAYLSLEQARYPGRFNININVEDKYRDVLVPPFLIQILVENAIKHAFTNRKQGNDIDVSVIKETATHVRIIVQDNGQGISKDKMHLLGETSVESESGTGSALENLNLRLKGLFGKSAALQFESTSSGTTFWCVLPYERQEEE | 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 is autophosphorylated at a histidine residue and transfers its phosphate group to the conserved aspartic acid residue in the regulatory domain of LytR. In turn, LytR binds to the upstream promoter regions of target genes including lrgA and lrgB, to positively regulate their expression. Possesses also a phosphatase activity that dephosphorylates and thus inactivates LytR.
PTM: Autophosphorylated on His-390.
Location Topology: Multi-pass membrane protein
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 65029
Sequence Length: 584
Subcellular Location: Cell membrane
EC: 2.7.13.3
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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 binding activity is necessary for the phosphorylation and oligomerization . Phosphorylation up-regulates viral RNA synthesis, replication, and pathogenesis in vivo .
Sequence Mass (Da): 21234
Sequence Length: 187
Domain: Contains a zinc-finger domain on its N-terminus essential for its function . Contains an oligomerization domain (By similarity). The central globular core is responsible for binding to RNA and phosphoprotein (By similarity).
Subcellular Location: Virion
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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 to poly(A)-rich sequences . Plays a role in the association of the matrix protein with the nucleocapsid, which initiates assembly and budding . Also, can activate host NF-kappa-B through association with host RELA .
PTM: Phosphorylated by host in infected cells . Only dephosphorylated M2-1 is competent for viral mRNA binding . Cyclic turnover of phosphorylation-dephosphorylation of M2-1 is required for efficient viral transcription .
Sequence Mass (Da): 22154
Sequence Length: 194
Domain: Contains a zinc-finger domain on its N-terminus essential for its anti-termination function . Contains an oligomerization domain . The central globular core is responsible for binding to RNA and phosphoprotein .
Subcellular Location: Virion
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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 poly(A)-rich sequences. Plays a role in the association of the matrix protein with the nucleocapsid, which initiates assembly and budding.
PTM: Phosphorylated by host in infected cells. Only dephosphorylated M2-1 is competent for viral mRNA binding. Cyclic turnover of phosphorylation-dephosphorylation of M2-1 is required for efficient viral transcription.
Sequence Mass (Da): 20204
Sequence Length: 176
Domain: Contains a zinc-finger domain on its N-terminus essential for its anti-termination function. Contains an oligomerization domain. The central globular core is responsible for binding to RNA and phosphoprotein.
Subcellular Location: Virion
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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 | MEEEEGAVAKEWGTTPAGPVWTAVFDYEAAGDEELTLRRGDRVQVLSQDCAVSGDEGWWTGQLPSGRVGVFPSNYVAPGAPAAPAGLQLPQEIPFHELQLEEIIGVGGFGKVYRALWRGEEVAVKAARLDPEKDPAVTAEQVCQEARLFGALQHPNIIALRGACLNPPHLCLVMEYARGGALSRVLAGRRVPPHVLVNWAVQVARGMNYLHNDAPVPIIHRDLKSINILILEAIENHNLADTVLKITDFGLAREWHKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKRLEVIEQSALFQMPLESFHSLQEDWKLEIQHMFDDLRTKEKELRSREEELLRAAQEQRFQEEQLRRREQELAEREMDIVERELHLLMCQLSQEKPRVRKRKGNFKRSRLLKLREGGSHISLPSGFEHKITVQASPTLDKRKGSDGASPPASPSIIPRLRAIRLTPVDCGGSSSGSSSGGSGTWSRGGPPKKEELVGGKKKGRTWGPSSTLQKERVGGEERLKGLGEGSKQWSSSAPNLGKSPKHTPIAPGFASLNEMEEFAEAEDGGSSVPPSPYSTPSYLSVPLPAEPSPGARAPWEPTPSAPPARWGHGARRRCDLALLGCATLLGAVGLGADVAEARAADGEEQRRWLDGLFFPRAGRFPRGLSPPARPHGRREDVGPGLGLAPSATLVSLSSVSDCNSTRSLLRSDSDEAAPAAPSPPPSPPAPTPTPSPSTNPLVDLELESFKKDPRQSLTPTHVTAACAVSRGHRRTPSDGALGQRGPPEPAGHGPGPRDLLDFPRLPDPQALFPARRRPPEFPGRPTTLTFAPRPRPAASRPRLDPWKLVSFGRTLTISPPSRPDTPESPGPPSVQPTLLDMDMEGQNQDSTVPLCGAHGSH | 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 | MEEEEGAAAREWGATPAGPVWTAVFDYEAVGDEELTLRRGDRVQVLSQDCAVSGDEGWWTGQLPSGRVGVFPSNYVAPAAPAAPSDLQLPQEIPFHELQLEEIIGVGGFGKVYRAVWRGEEVAVKAARLDPERDPAVTAEQVRQEARLFGALQHPNIIALRGACLSPPNLCLVMEYARGGALSRVLAGRRVPPHVLVNWAVQVARGMNYLHNDAPVPIIHRDLKSINILILEAIENHNLADTVLKITDFGLAREWHKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLPIPSTCPEPFARLLEECWDPDPHGRPDFGSILKQLEVIEQSALFQMPLESFHSLQEDWKLEIQHMFDDLRTKEKELRSREEELLRAAQEQRFQEEQLRRREQELAEREMDIVERELHLLMSQLSQEKPRVRKRKGNFKRSRLLKLREGSSHISLPSGFEHKITVQASPTLDKRKGSDGASPPASPSIIPRLRAIRLTPMDCGGSSGSGTWSRSGPPKKEELVGGKKKGRTWGPSSTLQKERAGGEERLKALGEGSKQWSSSAPNLGKSPKHTPMAPGFASLNEMEEFAEADEGNNVPPSPYSTPSYLKVPLPAEPSPCVQAPWEPPAVTPSRPGHGARRRCDLALLSCATLLSAVGLGADVAEARAGDGEEQRRWLDSLFFPRPGRFPRGLSPTGRPGGRREDTAPGLGLAPSATLVSLSSVSDCNSTRSLLRSDSDEAAPAAPSPPPSPLAPSPSTNPLVDVELESFKKDPRQSLTPTHVTAAHAVSRGHRRTPSDGALRQREPLELTNHGPRDPLDFPRLPDPQALFPTRRRPLEFPGRPTTLTFAPRPRPAASRPRLDPWKLVSFGRTLSISPPSRPDTPESPGPPSVQPTLLDMDMEGQSQDNTVPLCGVYGSH | 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 | MDGLPKDEAFLWQSSKDNKENGVWSDVQSYGVSNPLWMAVFDYEPTAEEELTLRRGDLVEILSKDSTVSGDEGWWTGKIKDKVGIFPSNYVVSDDKYTTLTGAPKQCPLPLEIEFDELNLDEIIGVGGFGKVYKGLWRDEEVAVKAVRHDPDEDINVTAENVRQEAKIFCMLCHPNIIALTGVCLKPPHLCLVMEYARGGPLHRALAGKKVPAHVLVNWAVQIAKGMTYLHNEAIVPIIHRDLGSSNILILEKAENDDLFNKTLNITDFGLAREWQKTTKMSAAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLPIPSTCPEPFVRILEACWDPDPHSRPTFSCILEQLTTIEQSAMFQMPLESFHSLQEDWRLEIQQMFDELRTKEKELRSREEELVRAAEEQRILEDLLKRREQELAEREIDIVERELNIIMYQMYQEKPKVKKRKGNFKKSRLKLKDGNRISLPSGFEHKITVQASPMLDKCKGQGTSSYSPPGSPLIIPRLRAIRLTPVDGSKTWGRSSVLKKEEVTTSNKKKGRTWGPSSTQQKERVGGEERLKTLGEGNKQWSSSAPNLGKSPKHTPISVGFASLTEMEEYADSDGSVPQSPYSQSYLTLPVQSDHRSHPEDTAHAGAPSSDSPKRGSQSRRKSELVLLGCASLLAAVALGSDLSELVPQEEKRKGIFQWAGRGPRRRASSPSRSMSYGEDSVIPSSSVTLISLSSISDCNSTRSLIRSDSDDIGLDHDNVSSGRGVKEDRGQQPNVGSNPLVDYKVESFKRDPKQSLTPTHVTVGRNNTTETRGHRRTPSDGAIRQVTQGHKRSPSDGSTPYQCEPEPSPFPRLPDPHFVFPPPVRRKDTGVERPTSLEFAPRPRPSSNRPRMDPWKFVSLSQTHSSSPSSGGGDACSSGSAEGAQVADVEETLLDMEVEGQRLDSTVPLCGLGLRPTTDPFFKYGNRRVLMKELSISLLQYKVESGVLL | 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 Mass (Da): 111875
Sequence Length: 1005
EC: 2.7.11.25
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Q16584 | MEPLKSLFLKSPLGSWNGSGSGGGGGGGGGRPEGSPKAAGYANPVWTALFDYEPSGQDELALRKGDRVEVLSRDAAISGDEGWWAGQVGGQVGIFPSNYVSRGGGPPPCEVASFQELRLEEVIGIGGFGKVYRGSWRGELVAVKAARQDPDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEALVPVIHRDLKSNNILLLQPIESDDMEHKTLKITDFGLAREWHKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEALEAQVLREMPRDSFHSMQEGWKREIQGLFDELRAKEKELLSREEELTRAAREQRSQAEQLRRREHLLAQWELEVFERELTLLLQQVDRERPHVRRRRGTFKRSKLRARDGGERISMPLDFKHRITVQASPGLDRRRNVFEVGPGDSPTFPRFRAIQLEPAEPGQAWGRQSPRRLEDSSNGERRACWAWGPSSPKPGEAQNGRRRSRMDEATWYLDSDDSSPLGSPSTPPALNGNPPRPSLEPEEPKRPVPAERGSSSGTPKLIQRALLRGTALLASLGLGRDLQPPGGPGRERGESPTTPPTPTPAPCPTEPPPSPLICFSLKTPDSPPTPAPLLLDLGIPVGQRSAKSPRREEEPRGGTVSPPPGTSRSAPGTPGTPRSPPLGLISRPRPSPLRSRIDPWSFVSAGPRPSPLPSPQPAPRRAPWTLFPDSDPFWDSPPANPFQGGPQDCRAQTKDMGAQAPWVPEAGP | 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 of BRAF, but does not phosphorylate BRAF directly. Influences microtubule organization during the cell cycle.
PTM: Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation. Thr-277 is likely to be the main autophosphorylation site. Phosphorylation of Ser-555 and Ser-556 is induced by CDC42.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 92688
Sequence Length: 847
Subcellular Location: Cytoplasm
EC: 2.7.11.25
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Q66HA1 | MEPLKNLFLKSPLGSWNGSGSGGGGGSGGVRPEGSPKATAAYANPVWTALFDYEPNGQDELALRKGDRVEVLSRDAAISGDEGWWAGQVGGQVGIFPSNYVSRGGGPPPCEVASFQELRLEEVIGIGGFGKVYRGSWRGELVAVKAARQDPDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAVQIARGMHYLHCEALVPVIHRDLKSNNILLLQPIEGDDMEHKTLKITDFGLAREWHKTTQMSAAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTLPIPSTCPEPFAQLMADCWAQDPHRRPDFASILQQLEALEAQVLREMPRDSFHSMQEGWKREIQGLFDELRAKEKELLSREEELTRAAREQRSQAEQLRRREHLLAQWELEVFERELTLLLQQVDRERPHVRRRRGTFKRSKLRARDGGERISMPLDFKHRITVQASPGLDRRRNVFEVGAGDSPTFPRFRAIQLEPAESGQTWGRQSPRRLDDSSNGERRACWAWGPSSPKPGEAQNGRRRSRMDEATWYLDSDDSSPLGSPSTPPALNGNPPRPSPEPEEPRRSGPTERGNSSGTPKLIQRALLRGTALLASLGLGRDLQPPGGLSRERGESPTAPPPAQMASPCPPDLPSTPLIHLSQATPDARGPLTPAPLLLDLGVSSGQPSAKSPRREETRGRTVSPPPGISRSAPGTPGTPRSPPLGLISRPRPSPLRNRIDPWSFVSAGPRPSPLPSPQPAPRRAPWTLFPDSDPFWDSPPANPFRGGSQDCRTQTKDVGAQAPWAPEAGP | 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 of BRAF, but does not phosphorylate BRAF directly. Influences microtubule organization during the cell cycle (By similarity).
PTM: Autophosphorylation on serine and threonine residues within the activation loop plays a role in enzyme activation. Thr-278 is likely to be the main autophosphorylation site. Phosphorylation of Ser-556 and Ser-557 is induced by CDC42 (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 93109
Sequence Length: 850
Subcellular Location: Cytoplasm
EC: 2.7.11.25
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Q12852 | MACLHETRTPSPSFGGFVSTLSEASMRKLDPDTSDCTPEKDLTPTHVLQLHEQDAGGPGGAAGSPESRASRVRADEVRLQCQSGSGFLEGLFGCLRPVWTMIGKAYSTEHKQQQEDLWEVPFEEILDLQWVGSGAQGAVFLGRFHGEEVAVKKVRDLKETDIKHLRKLKHPNIITFKGVCTQAPCYCILMEFCAQGQLYEVLRAGRPVTPSLLVDWSMGIAGGMNYLHLHKIIHRDLKSPNMLITYDDVVKISDFGTSKELSDKSTKMSFAGTVAWMAPEVIRNEPVSEKVDIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNSLHLPVPSSCPDGFKILLRQCWNSKPRNRPSFRQILLHLDIASADVLSTPQETYFKSQAEWREEVKLHFEKIKSEGTCLHRLEEELVMRRREELRHALDIREHYERKLERANNLYMELNALMLQLELKERELLRREQALERRCPGLLKPHPSRGLLHGNTMEKLIKKRNVPQKLSPHSKRPDILKTESLLPKLDAALSGVGLPGCPKGPPSPGRSRRGKTRHRKASAKGSCGDLPGLRTAVPPHEPGGPGSPGGLGGGPSAWEACPPALRGLHHDLLLRKMSSSSPDLLSAALGSRGRGATGGAGDPGSPPPARGDTPPSEGSAPGSTSPDSPGGAKGEPPPPVGPGEGVGLLGTGREGTSGRGGSRAGSQHLTPAALLYRAAVTRSQKRGISSEEEEGEVDSEVELTSSQRWPQSLNMRQSLSTFSSENPSDGEEGTASEPSPSGTPEVGSTNTDERPDERSDDMCSQGSEIPLDPPPSEVIPGPEPSSLPIPHQELLRERGPPNSEDSDCDSTELDNSNSVDALRPPASLPP | 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 in cytosol under basal conditions and dephosphorylated when membrane-associated (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 93219
Sequence Length: 859
Domain: Interacts with MBIP through the leucine-zipper motif.
Subcellular Location: Cytoplasm
EC: 2.7.11.25
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O60476 | MTTPALLPLSGRRIPPLNLGPPSFPHHRATLRLSEKFILLLILSAFITLCFGAFFFLPDSSKHKRFDLGLEDVLIPHVDAGKGAKNPGVFLIHGPDEHRHREEEERLRNKIRADHEKALEEAKEKLRKSREEIRAEIQTEKNKVVQEMKIKENKPLPPVPIPNLVGIRGGDPEDNDIREKREKIKEMMKHAWDNYRTYGWGHNELRPIARKGHSPNIFGSSQMGATIVDALDTLYIMGLHDEFLDGQRWIEDNLDFSVNSEVSVFEVNIRFIGGLLAAYYLSGEEIFKIKAVQLAEKLLPAFNTPTGIPWAMVNLKSGVGRNWGWASAGSSILAEFGTLHMEFIHLSYLTGDLTYYKKVMHIRKLLQKMDRPNGLYPNYLNPRTGRWGQYHTSVGGLGDSFYEYLLKAWLMSDKTDHEARKMYDDAIEAIEKHLIKKSRGGLTFIGEWKNGHLEKKMGHLACFAGGMFALGADGSRADKAGHYLELGAEIARTCHESYDRTALKLGPESFKFDGAVEAVAVRQAEKYYILRPEVIETYWYLWRFTHDPRYRQWGWEAALAIEKYCRVNGGFSGVKDVYSSTPTHDDVQQSFFLAETLKYLYLLFSGDDLLPLDHWVFNTEAHPLPVLHLANTTLSGNPAVR | 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)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 73004
Sequence Length: 641
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 3.2.1.113
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Q9UKM7 | MAACEGRRSGALGSSQSDFLTPPVGGAPWAVATTVVMYPPPPPPPHRDFISVTLSFGENYDNSKSWRRRSCWRKWKQLSRLQRNMILFLLAFLLFCGLLFYINLADHWKALAFRLEEEQKMRPEIAGLKPANPPVLPAPQKADTDPENLPEISSQKTQRHIQRGPPHLQIRPPSQDLKDGTQEEATKRQEAPVDPRPEGDPQRTVISWRGAVIEPEQGTELPSRRAEVPTKPPLPPARTQGTPVHLNYRQKGVIDVFLHAWKGYRKFAWGHDELKPVSRSFSEWFGLGLTLIDALDTMWILGLRKEFEEARKWVSKKLHFEKDVDVNLFESTIRILGGLLSAYHLSGDSLFLRKAEDFGNRLMPAFRTPSKIPYSDVNIGTGVAHPPRWTSDSTVAEVTSIQLEFRELSRLTGDKKFQEAVEKVTQHIHGLSGKKDGLVPMFINTHSGLFTHLGVFTLGARADSYYEYLLKQWIQGGKQETQLLEDYVEAIEGVRTHLLRHSEPSKLTFVGELAHGRFSAKMDHLVCFLPGTLALGVYHGLPASHMELAQELMETCYQMNRQMETGLSPEIVHFNLYPQPGRRDVEVKPADRHNLLRPETVESLFYLYRVTGDRKYQDWGWEILQSFSRFTRVPSGGYSSINNVQDPQKPEPRDKMESFFLGETLKYLFLLFSDDPNLLSLDAYVFNTEAHPLPIWTPA | 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 trims the carbohydrates to Man(5-6)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)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 79580
Sequence Length: 699
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.2.1.113
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A2AJ15 | MYPPPAPPPAPHRDFISVTLSLGESYDNSKSRRRRSCWRKWKQLSRLQRNVILFVLGFLILCGFLYSLHTADQWKALSGRPAEVEKMKQEVLPVLPAPQKESAEQEGFADILSQKRQRHFRRGPPHLQIRPPNTVSKDGMQDDAKEREAALGKAQQEENTQRTVISWRGAVIEPEQATELPYKRAEASIKPLVLASKIWKEPAPPNERQKGVIEAFLHAWKGYQKFAWGHDELKPVSKTFSEWFGLGLTLIDALDTMWILGLKQEFKQARKWVSENLDFQKNVDVNLFESTIRILGGLLSTYHLSGDSLFLTKAEDFGKRLMPAFTTPSKIPYSDVNIGTGFAHSPQWTSDSTVAEVTSIQLEFRELSRLTGIKKFQEAVEEVTKHIHSLSGKKDGLVPMFINTNSGLFTHPGVFTLGARADSYYEYLLKQWIQGGKKETQLLEDYVKAIEGIKAHLLRQSQPRKLTFVGELAHGRFSAKMDHLVCFLPGTLALGVHHGLPADHMDLARALMETCYQMNQQMETGLSPEIAHFNMYPRADHKDVEVKPADRHNLLRPETVESLFYLYRVTRDRKYQDWGWEILQSFNKYTRVPSGGYSSINNVQNSHKPEPRDKMESFFVGETLKYLYLLFSDDLELLSLDSCVFNTEAHPLPIWAPA | 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 trims the carbohydrates to Man(5-6)GlcNAc(2) (By similarity).
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)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 75150
Sequence Length: 658
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.2.1.113
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Q9NR34 | MLMRKVPGFVPASPWGLRLPQKFLFLLFLSGLVTLCFGALFLLPHSSRLKRLFLAPRTQQPGLEVVAEIAGHAPAREQEPPPNPAPAAPAPGEDDPSSWASPRRRKGGLRRTRPTGPREEATAARGNSIPASRPGDEGVPFRFDFNAFRSRLRHPVLGTRADESQEPQSQVRAQREKIKEMMQFAWQSYKRYAMGKNELRPLTKDGYEGNMFGGLSGATVIDSLDTLYLMELKEEFQEAKAWVGESFHLNVSGEASLFEVNIRYIGGLLSAFYLTGEEVFRIKAIRLGEKLLPAFNTPTGIPKGVVSFKSGNWGWATAGSSSILAEFGSLHLEFLHLTELSGNQVFAEKVRNIRKVLRKIEKPFGLYPNFLSPVSGNWVQHHVSVGGLGDSFYEYLIKSWLMSGKTDMEAKNMYYEALEAIETYLLNVSPGGLTYIAEWRGGILDHKMGHLACFSGGMIALGAEDAKEEKRAHYRELAAQITKTCHESYARSDTKLGPEAFWFNSGREAVATQLSESYYILRPEVVESYMYLWRQTHNPIYREWGWEVVLALEKYCRTEAGFSGIQDVYSSTPNHDNKQQSFFLAETLKYLYLLFSEDDLLSLEDWVFNTEAHPLPVNHSDSSGRAWGRH | 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-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4 beta-D-mannose + N(4)-(alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 5A1,2)
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 70911
Sequence Length: 630
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 3.2.1.113
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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
Subcellular Location: Secreted
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A2R6F5 | MFAKLSLLSLLFSSAALGASNQTLSYGNIDKSATPEARALLKYIQLQYGSHYISGQQDIDSWNWVEKNIGVAPAILGSDFTYYSPSAVAHGGKSHAVEDVIQHAGRNGINALVWHWYAPTCLLDTAKEPWYKGFYTEATCFNVSEAVNDHGNGTNYKLLLRDIDAIAAQIKRLDQAKVPILFRPLHEPEGGWFWWGAQGPAPFKKLWDILYDRITRYHNLHNMVWVCNTADPAWYPGNDKCDIATIDHYPAVGDHGVAADQYKKLQTVTNNERVLAMAEVGPIPDPDKQARENVNWAYWMVWSGDFIEDGKQNPNQFLHKVYNDTRVVALNWEGA | 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
EC: 3.2.1.78
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G2Q4H7 | MARTLRYLLCGILALAAGSNAVPAARGSTRAAPAAEPSTSATTYEAEDAILSGTTVDTAQEGYTGSGYVTGFDEASDKITFEVESEATKLYDLSIRIAAIYGDKHTTVVLNGGASSDVSFPAGDTWVDVPAGQVLLNEGANTIEIVSNWGWYLVDSITLTPSAPRPEHQINRSLNNPSADASARALYDYLRSIYGKKILAGQQDLTWADYVTQQTGKTPALVSVDLMDYSPSRVERGTKGTSVEEAITHAERGGIVSALWHWNAPAGLYDTDEHPWWSGFYTDATDFDVAAALSSTDNANYTLLLRDIDAIAVQLKRLRDARVPVLWRPLHEAEGGWFWWGAKGPDPAKQLYALLYDRLVNHHGINNLIWVWNSLSPDWYPGDDTVDILSADVYAQGNGPMSTQYNQLIDLGKDKKMIAAAEVGAAPLPDLLQAYEAHWLWFAVWGDTFINNAEWNSPEVLKTVYTSDYVLTLDEIQGWQDS | 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-oligosaccharides such as M4 which is degraded slightly to M3 and M1, M5 which is mainly degraded to M4 and M1, and M6 which is mostly hydrolyzed to M4 and M2 . Shows no activity toward M2 and M3 manno-oligosaccharides .
Sequence Mass (Da): 52766
Sequence Length: 482
Subcellular Location: Secreted
EC: 3.2.1.-
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Q8VHC8 | MGASVLPLGLGAGDCQSSSGRRMSACLPRTALSFLLSLLLATPGARAAGYETCPMVQPGMLNVHLVAHTHDDVGWLKTVDQYYWGIHNDLQQAGVQYILDSVISALLAEPTRRFVYVEMAFFSRWWHQQTNETQEVVRRLVRQGRLEFANGGWVMNDEAATHYGAIVDQMTLGLRFLEDTFGSDGRPRVAWHIDPFGHSREQASLFAQMGFDGVFFGRIDYQDKLVRKKRREMELVWRASASLKAPAADLFTGVLPNNYGPPEGLCWDVLCADPPVVDDPRSPEYNAKKLVSYFLQLATAQGRYYRTNHTVMTMGSDFQYENANTWFKNLDKLIQLVNMQQANGSRVHVLYSTPACYLWELNKANLTWPVKEDDFFPYADGPHMFWTGYFSSRPALKRYERLSYNFLQVCNQLEAQVGPAANVGPYGHGDSSPLNQAMAVLQHHDAVSGTSKQHVADDYARQLAAGWGPCEVLLSNALAKLSGSKETFLFCRDLNISICPFSQTSERFQVLVYNPLGRKVDRMVRLPVRKGLFLIKDPGNNTVPSTVVELTSSGNPELLFPALVPALGFSVYSVTRVSDQNPQTRSQHSRPQKYSSPVLSIKNEYLRASFHPDTGLLSMIEVLDRKLTLPVNQAFFWYNASVGDKRSSQASGAYIFRPSQQWPFPVSHLARTRLVKTALVQEVHQNFTAWCSQVVRLYSGQRHLELEWTVGPIPVGDKWGKEIISRFDTPLETGGVFFTDSNGREVLERRRDYRPSWKLNQTEPVAGNYYPVNSRIYITDGKMQLTVLTDRSQGGSSMSDGSLELMVHRRLLKDDGRGVGEALQEPGSGGWVRGRHLLLLDTAREAAAEHRLLAEKELLAPQLVLAPGQGPSYHHDHHEAVPRKQFSGLRRQLPPSVRLLTLARWGPDTLLLRLEHQFALGEDSSRNLSLPVTLDLQDLFSTFTITRLQETTLAANQLRASASRLKWTTEIDPISRPAVPRLDPSSITLQPMEIRTFVASVQWEENS | 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: Lysosome
EC: 3.2.1.24
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O00754 | MGAYARASGVCARGCLDSAGPWTMSRALRPPLPPLCFFLLLLAAAGARAGGYETCPTVQPNMLNVHLLPHTHDDVGWLKTVDQYFYGIKNDIQHAGVQYILDSVISALLADPTRRFIYVEIAFFSRWWHQQTNATQEVVRDLVRQGRLEFANGGWVMNDEAATHYGAIVDQMTLGLRFLEDTFGNDGRPRVAWHIDPFGHSREQASLFAQMGFDGFFFGRLDYQDKWVRMQKLEMEQVWRASTSLKPPTADLFTGVLPNGYNPPRNLCWDVLCVDQPLVEDPRSPEYNAKELVDYFLNVATAQGRYYRTNHTVMTMGSDFQYENANMWFKNLDKLIRLVNAQQAKGSSVHVLYSTPACYLWELNKANLTWSVKHDDFFPYADGPHQFWTGYFSSRPALKRYERLSYNFLQVCNQLEALVGLAANVGPYGSGDSAPLNEAMAVLQHHDAVSGTSRQHVANDYARQLAAGWGPCEVLLSNALARLRGFKDHFTFCQQLNISICPLSQTAARFQVIVYNPLGRKVNWMVRLPVSEGVFVVKDPNGRTVPSDVVIFPSSDSQAHPPELLFSASLPALGFSTYSVAQVPRWKPQARAPQPIPRRSWSPALTIENEHIRATFDPDTGLLMEIMNMNQQLLLPVRQTFFWYNASIGDNESDQASGAYIFRPNQQKPLPVSRWAQIHLVKTPLVQEVHQNFSAWCSQVVRLYPGQRHLELEWSVGPIPVGDTWGKEVISRFDTPLETKGRFYTDSNGREILERRRDYRPTWKLNQTEPVAGNYYPVNTRIYITDGNMQLTVLTDRSQGGSSLRDGSLELMVHRRLLKDDGRGVSEPLMENGSGAWVRGRHLVLLDTAQAAAAGHRLLAEQEVLAPQVVLAPGGGAAYNLGAPPRTQFSGLRRDLPPSVHLLTLASWGPEMVLLRLEHQFAVGEDSGRNLSAPVTLNLRDLFSTFTITRLQETTLVANQLREAASRLKWTTNTGPTPHQTPYQLDPANITLEPMEIRTFLASVQWKEVDG | 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 three peptides (A, B and C). The A, B and C peptides are disulfide-linked.
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.
Sequence Mass (Da): 113744
Sequence Length: 1011
Subcellular Location: Lysosome
EC: 3.2.1.24
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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 UNC119 and UNC119B cargo adapters: may help the release of UNC119 and UNC119B cargo or the recycling of UNC119 and UNC119B . May play a role in ciliary membrane localization via its interaction with UNC119B and protein transport into photoreceptor cells .
PTM: Phosphorylated.
Sequence Mass (Da): 23083
Sequence Length: 206
Subcellular Location: Cytoplasm
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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 by the decarboxylase macB (By similarity). The cytochrome P450 monooxygenase macC then catalyzes the oxidation of m-cresol to toluquinol (By similarity). Epoxidation of toluquinol is then performed by the short chain dehydrogenase macD, with the help of macE, and a further prenylation by macG leads to 7-deacetoxyyanuthone A (By similarity). The next step is the hydroxylation of C-22 of 7-deacetoxyyanuthone A by the cytochrome P450 monooxygenase macH to yield 22-deacetylyanuthone A (By similarity). O-Mevalon transferase macI then attaches mevalon to the hydroxyl group of 22-deacetylyanuthone A to produce yanuthone E (By similarity). The terpene cyclase macJ catalyzes the cyclization of 22-deacetylyanuthone A to macrophorin A . MacJ is also able to catalyze cyclization of yanuthone E and 7-deacetoxyyanuthone A to their corresponding macrophorins . The macJ products can be further modified by macH and macJ, as well as by the FAD-dependent monooxygenase macF, to produce additional macrophorins, including 4'-oxomacrophorin A, 4'-oxomacrophorin D and 4'-oxomacrophorin E .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29359
Sequence Length: 258
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Membrane
EC: 4.2.3.-
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P91193 | MMQQQKPGKPKKINRIDKIKRLQINRSRRPDINQTVPSPLFYVRIVVTWLGMVSLDAMTGFRFELLWPTWLMIRAAAESIQMRNQHCVTTIANPTAARFSVLFICVTATSDLICYLFIPIRMLIFLATTYVWISLYYHTQGGFLRSLATVYGGERLQSWPIVFITCFIVIFELFLRIRSHPILISFFPNVAEYAGVSPVWPRSLNAFFGAHSIGYPVILITVSMHYYFNEWKLRRKQCDVSNRNEQLFRILVEGLPAEYEGPKDYTSQQCLEDDLYYLDPPVQTLQPMQAIQAASATPPTSSKKNGIHKRNGDVTSSTTTSSRKKKHNGNSGFNSTPPNDKKKGKSIRDVDMDDGDDSDDDYSYRDTSSSTIEDQRRGGGISIIRFIFSSAAWLFSFVFESSTPSENSLSNQQIDDDEDYEDGDGDKKNGRTDSMTSTTKGRANTMPSTTRSQNNNNSQKQQKQSNGKSHHQHSSHQNNHQKSNGNSNGHARGFAAVRDSSHDTNASNETDIRSMSRELESLRSEISSRRSQEEDFKLQVSMHESNETRLSQQLSNMRLKVEQMEIKCSSIERHRESDKHQLEQAERKYADLLGKKAEIEATLSAERKARMEVTSKKYDVAEHQRERERQLESEIDKLRIELKSKDESNMRMESELHGLRNYKEENDIDSLNMELRFVRDKSHQMEESLAGENKLKQSLFKCLGDARDTIKSLERRVQEFQIKNGSSIGGGSSETLMNGRSSTEANNENDTTASDQSSPHQHSAMGSPVPFAKMPLSVNVSNRHGSPFNGKVSPIASIGSVLAAAGGPAPPDYMMAVGANVTATTGPVPQKQPRAGFHGISRYNEFTNIASGGEHRLFDTPASAISASAINGSNPEDDFLMNKGKFGAPSQPAARLA | 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 small RNAs . In ASI neurons, promotes dauer formation in response to pheromones such as the ascarosides ascr#2 and ascr#3 .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 100707
Sequence Length: 897
Subcellular Location: Rough endoplasmic reticulum membrane
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Q2TLY2 | MKRRNADCSKLRRPLKRNRITEGIHSSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFFVCVAFTSDIICLLFIPKQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKHFHVDLCRPFAAHCIGYPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQRQERETEEATSKGMSEADSVLVAQNGTAINKKLPISLPELEYKEKGKDSAKDKKQQQHSIGINNNILQTVDAKLQDIEYMENHLNAKRLNNELGGSAENLFLKEEVGAGGGSAPSKHYKNSSPRSHNSTNGSVPSSSSNRSDKKQKCTGKNLAPHRDLMENCIPNNQLSKPDALVRLEQDIKKLKADLQASRQVEQDLRSQISSLSSAERSMRSELGQLRQENELLQNKLHNAVQAKQKDKQTIVQLEKRLKAEQEARAAVEKQLAEEKKRKKMEEATAARAVALAAASRGECTDSLKSRIRELESECKKLTHDMKLKEEQIRELELKAQELHKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKEQEIKELKQKIAEVMAVMPSITYSAETNNMTPVTPHYSSKFMDTSPSSLDPNASVYQPLKK | 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 | MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFFVCVAFTSDIICLLFIPVQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKHFHVDLCRPFAAHCIGYPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQLIQRQEREAEEAAAAAAAAASKSIHDVDSPAVAQNGSAGGKKPSSNTLPELEYREKERGKNESKKQHNHNQNHHSSTSSSILPSVDNKAQEMEYMENHVNSKRLSSSDLLGSTENLLKDEHSSSSSSSTSSNSNKNYKNASGGGGGGGSSSPRGHGTANGSVPSSSGPSSSASSSSKGDRKQKYGGGKNSASHRDPVENCIPNNQLSKPEALVRLEQDVKKLKADLQASRQTEQDLRSQLGSLGTSERSIRSELGQLRQENELLQNKLHNAVQAKQKDKQTLGQLEKRLKAEQEARAAAEKLLAEEKKRKKLEEATAARAVALAAATRGECTESLRRRISELEAECKKLTLDIKVKEDQIRELELKVQELHKYKENEKDTEVLMSALSAMQDKTQHLENSLSAETRIKLDLFSALGDAKRQLEIAQGQILQKDQEIKDLKQKIAEVMAVMPSVVYSADTGSMTPVTPHYSSKFMDTSPSGLDPNASVYQPLKK | 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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