ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A8FTT1 | MPNMRHRVNSLTEEHEENMQMSKLTGHLSSISTLFPVKNDASQTLTLGQLGLGCPCQLVSLWHYLRKNSPSRAVNIKIFESQFDALADFNLKLASLTSPDPRLPRDDEQSTMVEALLRADIVAIEGCQRLIFDDGRVILDIYLGDTLSQLKCILPTSVKGDMTDNSALIAHWNITEKVKAGSLDQAMLWQIAKLSRDNAALSFTDPESKETRQMMALARSVGLRTLETTVSETTVPETQQQTENKNLDTASDAIPLQERRALRHAQSDKFQYCPVSAANEGDEDCDGEIAIIGGGVASTHLALSLAQRNKKVRIFCSDAN... | Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to fo... |
A9WKE3 | MNDTIAAIATPPGEGGIGIIRLSGPDAQSIALRIFRPVRPGRLRSHRVRYGHVIGPDGEVIDEALLTLMAAPHSFTREDVVEISCHGGALPVQLTLEAALAAGARLANPGEFTLRAFLNGRIDLSQAEATLDVIRAQTSAGLAIAQAQLGGWLAREVRAARTAILEPLAYITALIDFPEEGIEPQTVAGPIEQALATVERLLAGADQGMVLRNGARVVLVGRPNVGKSSLLNALLRVERAIVTPIPGTTRDTLEEMANLAGVPVVLIDTAGMRTSTDPVEQIGVERAAAALAGADLALLVFDSSQPFTPEDEAMLVATAD... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 47166
Sequence Length: 452
Subcellular Locatio... |
Q9Z768 | MLKHDTIAAIATPPGEGSIAVVRLSGPQAIVIADRIFSGSVASFASHTIHLGQVIFEETLIDQALLLLMRSPRSFTGEDVVEFQCHGGFFACSQILDALIALGARPALPGEFSQRAFLNGKIDLVQAEAIQNLIVAENIDAFRIAQTHFQGNFSKKIQEIHTLIIEALAFLEVLADFPEEEQPDLLVPQEKIQNALHIVEDFISSFDEGQRLAQGTSLILAGKPNVGKSSLLNALLQKNRAIVTHIPGTTRDILEEQWLLQGKRIRLLDTAGQRTTDNDIEKEGIERALSAMEEADGILWVIDATQPLEDLPKILFTKPS... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 48715
Sequence Length: 442
Subcellular Locatio... |
Q8KAS1 | MSPSDLHLPVPGHPIAAIATPVGVGALAIVRISGAGVLDLADRVFRKVHGSGKLAEAAGYTAHFGRLYDGEEMVDEVIALVFRAPRSFTAEQMVEFTCHGGPVVVGRVLRLMLDNGCRLAEPGEFTRRAFLNGRIDLLQAEAIGEMIHARTESAYRTAVSQMKGDLSVRLGGLREQLIRSCALIELELDFSEEDVEFQSRDELTMQIETLRSEVNRLIDSYQHGRIVSEGVSTVIAGKPNAGKSTLLNTLLGQERAIVSHMPGTTRDYIEECFIHDKTMFRLTDTAGLREAGEEIEHEGIRRSRMKMAEADLILYLLDLG... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 51817
Sequence Length: 473
Subcellular Locatio... |
A0M2N6 | MKLNDTIVALATPSGAGAIAIIRVSGPDALEIVAPLFKAKSKKDLAKQPTHTLHLGNVMDGERTIDEVLASVFRAPKSYTGEETVELSCHGSPYIQQEIIQLLIRKSCRSAEAGEFTLRAFLNAKMDLSQAEAVADLINSENAASHQMAMQQMRGGFSNEIQKLREELLNFASLIELELDFAEEDVEFANRDQFKDLVSKIQTVLKRLLDSFATGNVLKNGIPVAIVGEPNVGKSTLLNALLNEERAIVSEIAGTTRDTIEDEMSIGGVGFRFIDTAGIRETKDVVESIGIKKTFEKISQAQVVVYLVDSSQIAVNRERL... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 52259
Sequence Length: 474
Subcellular Locatio... |
Q1QS99 | MTATPLYRQDTIAAIATPPGRGGVGIIRLSGPASRDLAERILGHCPAPRHAHYGPFYDADAQVLDEGIALFFPGPHSFTGEDVLELQGHGGPVIMDLLLARCVALGARLARPGEFSERAFLNDKLDLAQAEAIADLIDASSRAAAENALRSLQGEFSTRVSALVDKLIELRMFVEAAIDFPEEEIDFLADGKVAAMLQGAQETLGEVRAAAGQGALMREGMNVVIAGRPNAGKSSLLNALTERDSAIVTDIEGTTRDVLREYIHIDGMPLHVIDTAGLRDTPDAIEKIGVARAWEEIEKADRVLLLVDATTTTQTDPMQL... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 49247
Sequence Length: 458
Subcellular Locatio... |
A9KLX9 | MKTDTIAAIATGLSNAGISIVRISGDQAFAVIDKIFQTKSKAKRLSEMDSHTVHYGYIVDEEEIIDEVMVIIMRAPRSYTMEDSIEIDCHGGITVTKKVLEAVLKAGARIAEPGEFTKRAFLNGRIDLSQAEAVIDVIHANNELALKNSMKQLKGNVLHKVKDVRHSIILDTAYIEAALDDPEHISLEGFSDKLRDNVIGSIKELSELINTSENGRMIKEGIRTVILGRPNAGKSSLLNLMVGEERAIVTEIAGTTRDTIEETVFLNGLCLNLIDTAGIRETSDLVEKLGVEKSLKSAKEADLIICVIDASTPLNQDDKE... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 50743
Sequence Length: 458
Subcellular Locatio... |
Q1MPF1 | MCDTIAAIATPSGTGGIGIIRISGPKSKERLTELFHSVSPKFTDFKPWMLHRGYLVAPTNEFLDDILAVYMPAPYTFTGEDVVELHCHGGHFLLLTILETVLCKNIRLAKPGEFSQRAFLNGRMDLTQAEAVAELIAASSRNEVLLASNRLKGLLGQKIIDIRRRIEELRVWICLAVDFPEEESGIFPLEKFINGLLEIHEIIQKLIHAAERSRCWKEGVTVALAGAVNAGKSSLLNALLGKERAIVTEHPGTTRDFLEECIIVNSLSIRLIDTAGLRVTSDPIEEQGIQKGREKIDEADVILFIIDGTVGVTEESKLLI... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 50924
Sequence Length: 459
Subcellular Locatio... |
Q49UI4 | MDLDTITSISTPMGEGAIGIVRLSGVDAVDIADKLYKGKERLEDVTSHTINYGHIIDPESNEVVEEVMVSVLRAPKTFTREDIVEINCHGGILTINRILELTMTYGARMADPGEYTKRAFLNGRIDLSQAEAVMDFIRSKTDRASKVAMNQIEGRLSDMIKRQRQSILEILAQVEVNIDYPEYDDVEDATTEVLLGKSNEIKTEINKLLDTGTQGKIMREGLSTVIVGKPNVGKSSMLNNLIQDNKAIVTEVPGTTRDTLEEYVNVRGVPLRLVDTAGIRDTEDIVERIGVERSRKALGEADLILFVLNYNERLTDEDRK... | Cofactor: Binds 1 potassium ion per subunit.
Function: Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Sequence Mass (Da): 51382
Sequence Length: 459
Subcellular Locatio... |
P53163 | MSLRILAKRSSSIWMKTRVTPALISPITITTRFNSTTTTAPSHKDDVRPVDPKISKIVQDISQLTLLETSSLINELKTVLNIPEISMPMGGFMAGAAGAGAGNVPSSTGEAGSGAEEEAKPEAKTVFTVKLDSFDTKTKAKVIKEVKGLLGLSLVEAKKFVEAAPKVLKENVAKDDAEKIKKTLEDLGAKVSLE | Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitoch... |
B2X050 | MAEKTTSTRYAVVTGGNKGIGYETCRQLASKGVVVVLTSRDEKKGIEAIERLKEESNFTDEHILFHQLDIMDPASISSLVNLIKTKFGRLDILINNAGISGVMVEGDVQVLKEILERYISIVFTEDENGEEGGWTKSGPGSVTNYELTKECIETNYYGAKRMTEAFIPLLQLSNSPRIVNVASSMGKLKLLCNKWAIEVLRDADSLTEEKVDQVVNEFLKDFTEKSTESKGWPSYFTAYKVSKASLIAYTRVLATKYPNFRINSVCPGYCKTDVNANTGSLTAGEGAESLVNLALLPNDGPSGLFFYRKEVTFF | Function: Involved in basal resistance against pathogens.
Catalytic Activity: (+)-neomenthol + NADP(+) = (1R,4S)-menthone + H(+) + NADPH
Sequence Mass (Da): 34758
Sequence Length: 314
EC: 1.1.1.208
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Q2ULB2 | MHFSSLSLPLTALSLVTPSLAYPQFKFEQRVARSNSSESRANAVKEAFVHAWDGYMQYAYPHDELHPISNGVGDSRNGWGASAVDALSTAVIMGNETIVNQILDHIATIDYSKTDDQVSLFETTIRYLGGMLSGYDLLKGPASNLVKDQAKVKTLLDQSQNLADVLKFAFDTPSGIPYNNINITSHGNDGATTNGLAVTGTLVLEWTRLSDLTGDTEYAQLSQKAEDYLLNPSPKSAEPFEGLVGSHINISNGAFADGQVSWNGGDDSFYEYLIKMYVYDPKRFSTYGDRWVKAAESSIKHLASHPEKRPDLTFLASYND... | Cofactor: Ca(2+). Can also use Mg(2+), but with lower efficiency.
Function: Involved in the maturation of Asn-linked oligosaccharides. Progressively trims 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-Ma... |
Q12563 | MHLPSLSLSLTALAIASPSAAYPHFGSSQPVLHSSSDTTQSRADAIKAAFSHAWDGYLQYAFPHDELHPVSNGYGDSRNGWGASAVDALSTAVIMRNATIVNQILDHVGKIDYSKTNTTVSLFETTIRYLGGMLSGYDLLKGPVSDLVQNSSKIDVLLTQSKNLADVLKFAFDTPSGVPYNNLNITSGGNDGAKTNGLAVTGTLALEWTRLSDLTGDTTYADLSQKAESYLLNPQPKSAEPFPGLVGSNINISNGQFTDAQVSWNGGDDSYYEYLIKMYVYDPKRFGLYKDRWVAAAQSTMQHLASHPSSRPDLTFLASY... | Cofactor: Ca(2+). Can also use Mg(2+), but with lower efficiency.
Function: Involved in the maturation of Asn-linked oligosaccharides. Progressively trims 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-Ma... |
E9CXX8 | MKGSPVLAVCAAALTLIPSVVALPMIDKDLPSSISQSSDKTSQERAEAVKAAFRFAWEGYLEHAFPNDELHPVSNTPGNSRNGWGASAVDALSTAIIMDMPDVVEKILDHISNIDYSQTDTMCSLFETTIRYLGGMISAYDLLKGPGSHLVSDPAKVDVLLAQSLKLADVLKFAFDTKTGIPANELNITDKSTDGSTTNGLATTGTLVLEWTRLSDITGDPEYGRLAQKGESYLLNPQPSSSEPFPGLVGRTIDIETGLFRDDYVSWGGGSDSFYEYLIKMYVYDKGRFGKYKDRWVTAAESTIEHLKSSPSTRKDLTFV... | Cofactor: Ca(2+). Can also use Mg(2+), but with lower efficiency.
Function: Alpha-mannosidase involved in the maturation of Asn-linked oligosaccharides. Progressively trims 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... |
Q5BF93 | MRTLLALAALAGFAAARVPAYAITRPVMRSDSRADAVKEAFSHAWDGYYNYAFPHDELHPISNGYGDSRNHWGASAVDALSTAIMMRNATIVNQILDHIAAVDYSKTNAMVSLFETTIRYLAGMISGYDLLKGPAAGLVDDSRVDVLLEQSQNLAEVLKFAFDTPSGVPYNMINITSGGNDGATTNGLAVTGTLVLEWTRLSDLTGNDEYARLSQRAEDYLLHPEPAQYEPFPGLIGSAVNIADGKLANGHISWNGGADSYYEYLIKMYVYDPERFGLYRDRWVAAAESSINHLASHPSTRPDVTFLATYNEEHQLGLTS... | Cofactor: Ca(2+). Can also use Mg(2+), but with lower efficiency.
Function: Involved in the maturation of Asn-linked oligosaccharides. Progressively trims 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-Ma... |
Q50103 | MFVNLTCLSEGNGSRGKALAESTQAELKTSWYLLGPAFVAAIAYVDPGNVAANVSSGAQFGYLQLWVVVVANVLAGLVQYLSAKLGLVTGQSLPQAISKQMSHPFRLGFWLQAELVAMATDVAEIVGGAIAFHILFRVSLLLGGVITGTVSLLLLMVKDRRGQLLFERVITGLLFVIVVGFTSSFFVATPSPEDMVNGLLPRFQGTESVLLAAAIIGATVMPHAVYLHSGLALDRHGHPHAGRSRRRLLRVTRLDVILAMTIAGIVNTAMLLVAAINLQHHQVTAYIEGTYTAIQDTLGATIAMLFAIGLLASSLASASV... | Function: H(+)-stimulated, divalent metal cation uptake system.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45137
Sequence Length: 426
Subcellular Location: Cell membrane
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P9WIZ4 | MAGEFRLLSHLCSRGSKVGELAQDTRTSLKTSWYLLGPAFVAAIAYVDPGNVAANVSSGAQFGYLLLWVIVAANVMAALVQYLSAKLGLVTGRSLPEAIGKRMGRPARLAYWAQAEIVAMATDVAEVIGGAIALRIMFNLPLPIGGIITGVVSLLLLTIQDRRGQRLFERVITALLLVIAIGFTASFFVVTPPPNAVLGGLAPRFQGTESVLLAAAIMGATVMPHAVYLHSGLARDRHGHPDPGPQRRRLLRVTRWDVGLAMLIAGGVNAAMLLVAALNMRGRGDTASIEGAYHAVHDTLGATIAVLFAVGLLASGLASS... | Function: H(+)-stimulated, divalent metal cation uptake system. Transports zinc and iron. Can also interact with manganese and copper (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45004
Sequence Length: 428
Subcellular Location: Cell membrane
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Q9PB87 | MSPITILLIGIAMSTDAFAAAIGKGAAIGKPRLRDALYVAVIFGVIETATPIAGWLLGQIASHYIATFDHWIAFGLLSGLGIHMIVNGLKNNGNTCKDNADTHNRNSRWLPLAATALATSIDAAAIGISLAFLDIHISIVAAVIGLCTFTMVIFGVMLGRVLGTFVGNRAEIVGGIILIIVGSTILYEHLSNNG | Function: Probably functions as a manganese efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20252
Sequence Length: 194
Subcellular Location: Cell inner membrane
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A1JM85 | MNLSATLVLAFAMSMDAFAASIGKGASLHKPRFREAIRTGLIFGVIEAITPLIGWCIGLFASQYILEWDHWIAFSLLFILGCRMIFEGAKQQVEETEKMRSHSFWVLVMTAIATSLDAMAIGVGLAFLQVNIVHTAMAIGLATMIMATLGMLIGRYIGPLLGKRAEIIGGIVLIGIGFNILYEHIYRLA | Function: Probably functions as a manganese efflux pump.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20650
Sequence Length: 189
Subcellular Location: Cell inner membrane
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Q747W9 | MELIDSFGRRINYLRLSVTDRCNLRCSYCMPAEGVEKLAHGDILSYEDLFRIARAAVAIGIEKIRITGGEPLVRKGIVPFLARIAAIEGLRQLVLTTNGLLLPEMAADLRSAGVQRLNISLDSLRADTFRAITRIGELQRVLDGIAAADAAGFPPPKINMVVMRGVNDGEVADFARLTIDRPCTVRFIEYMPATRENNWQSLTVPGREILDRISASYELEPVEKGACAGPSRDFRIRGAAGTLGVITAVSGHFCGDCNRVRVTSTGMAKSCLFSDEGFDLRPFLETSDPIILQEALRRIVGVKPERHGMSACKAEHQAFS... | Cofactor: Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived substrate.
Function: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate.
Ca... |
Q8UER6 | MSDGQKLTHIDASGEAHMVDVGDKAETVRVAVAEGFVKMKPETLALIRDGNAKKGDVIGTARLAGIMAAKQTANLIPLCHPLMLTKVAVDITEDTGLPGLRVEAMVKLSGKTGVEMEALTAVSIACLTIYDMAKAADKGMEIVNIRLLEKSGGKSGDFRRQES | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 17236
Sequence Length: 163
Pathway: Cofactor ... |
Q21R65 | MNALTHFDAQGQAHMVDVAGKAATHRIGIAGGRIEMLPSTLAIIEAGTAKKGDVLGIARIAGIMAAKKTSELIPLCHPLALTRVAIDFETDQADETRASSIFCTATVETVGATGVEMEALTAVQVALLTIYDMCKAVDRGMVMTGIKLLEKHGGKSGSFVNGT | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 16968
Sequence Length: 163
Pathway: Cofactor ... |
Q0VQ23 | MTEQRFTHLDDSGRAQMVDVTDKDITQRAATAQARVRMQPSTLQMILAGEHPKGDVLATARIAGIQAAKKTWDLIPLCHPLLLTGITVTIEPEADDALCVQATCKLKGTTGVEMEALTAASVACLTLYDMCKAVDRCMVIESVCLLEKSGGRSGTFRRER | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 17364
Sequence Length: 160
Pathway: Cofactor ... |
A8EX06 | MELTHLDDKNRPKMVDVSSKSETKRVAVASGEIKMSKEAYQAIISNNTKKGPVLQTAVIAAILGTKKTHELIPMCHPLLLTGIDCDIEEIPQNNTFKLYVTARLNGQTGVEMEALTGVSIGLLTIYDMVKAIDKSMIISNVQLESKSGGKSGDFKR | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 17006
Sequence Length: 156
Pathway: Cofactor ... |
O66810 | MRTVDITTKIETLREAKAYGRIRLKPETVKLIKENKVPKGNLVEATKLSGIFGAKKTGELLPFCHPIPLDFVALEVKVNEDNLEVFSTVRGIARTGYEMEALTAVTTALLNVYDMCKALDDSMVIEEVKLLEKSGGKSDWFRRLDGVKVNLHAENEGLRKIAEDYLKELGATFAEEAELYISIGDNLPINKEIRSLERVISLYDFRRNPKEVGKEIRVGWSDDALIIILPESEEKIRFFFETFGGIIGNLLCRR | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 28737
Sequence Length: 254
Pathway: Cofactor ... |
O28132 | MELTHIEDGKVRMVDVSHKDDVDRIAVAEGYIRLRSSTIEAIINKEVAKGNVIAAANIAGVMAVKKTPELIPMCHPIPITSVKFDFDIESVGIRVKCTVKSKGKTGVEMEALTGVSVALLTIWDMVKSLEKDERGNYPKTLIEVIRVVEKVKGGKE | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 17101
Sequence Length: 156
Pathway: Cofactor ... |
P26944 | MTDQPLAGFTHFDAEGRAVMVDVSGKADTERSATARGSVLMQPETLALILQGGVKKGDVLSVARLAGIMGAKRTPDLIPLCHPLMLTSVKVD | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 9674
Sequence Length: 92
Pathway: Cofactor bi... |
C1DPC3 | MLTHLDSRGHAHMVDVTDKASTAREAEAEAWVRMRPETLELIQKGGHPKGDVFAVARIAGIMAAKKTHELIPLCHPLLLTGIKVELSAEGEDRVRIVARCKLAGQTGVEMEALTAASVAALTLYDMCKAVDRGLLIEQVRLLEKKGGKSGHYQAGQAM | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 17077
Sequence Length: 158
Pathway: Cofactor ... |
Q749N8 | MSFNHFDDQGRAIMVDVSGKQPTLRTATAAATVSMQPDTLADLLAGRTTKGDVLGVARIAGIAAAKKTPELIPLSHPLAIHHAAIDFDTDQACGTVTVRATVRAFERTGVEMEAMTSAAVAALTIYDMCKGADKGITIGQIRLLFKEGGKSGTWQREEGQ | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 16913
Sequence Length: 160
Pathway: Cofactor ... |
C5D4E6 | MSSFTHFNEQGRAKMVDITEKEDTIRVAVAQTSVTVNKEIYEKMTNRMIEKGDVLAVAQVAGIMAAKKTSDLIPMCHPLMLKGVDIQFAWHVEEEKALYQLLITVTVKTKGSTGVEMEALTAASVCALTVYDMCKALDKGMVIGPTYLVEKSGGKSGHYQRENSSVGGFANEQ | Function: Catalyzes the conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate to cyclic pyranopterin monophosphate (cPMP).
Catalytic Activity: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate
Sequence Mass (Da): 18911
Sequence Length: 173
Pathway: Cofactor ... |
Q8XZR3 | MPTIRVQEADFDLGAEIAALRAGRPQIGAVASFIGTVRDINDGSGVSEMELEHYPGMTEKALANIVDAAMQRWDLIDALVIHRVGKLRPEDQIVLVAVASGHRGEAFAACEFIMDYLKSEAPFWKKEQTAQGARWVDARVTDERALARWGIVTDNASAATAQAASANDQNQKDRDA | Function: Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity).
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cycli... |
Q984P0 | MSAVLAPTVRIQRQDFDVAAEIAALTQGRADVGAVVSFSGLCRDEQGALSALELEHYPGMAEAEIGRIAAEAVERWPLQGLTVIHRHGKIRPGENIVLVVAASAHRQAAFEAANFLMDYLKSRAPFWKKEHRTDGSEGGWVEAKETDTQAAKRWKSSSE | Function: Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity).
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cycli... |
P65399 | MHETRIVVGPAPFSVGEEYSWLAARDEDGAVVTFTGKVRNHNLGDSVKALTLEHYPGMTEKALAEIVAKARSRWPLGRVTVIHRVGELWPGDEIVFVGVTSAHRSSAFDAGQFIMDYLKTRAPFWKREATPEGDRWVEARDSDQQLAKRW | Function: Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity).
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cycli... |
Q9ZIM9 | MKQFEIVTEPIQTEQHRDFTLNPHQGAVVVFTGHVREWTKGIRTEHLEYEAYIPMAEKKLAQIGDEINEQWPGTIVSIVHRIGPLKISDIAVLIAVSSPHRKDAYAANEYAIDRIKEVVPIWKKEIWEDGAEWIGHQRGYHDDAVERGQN | Function: Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity).
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cycli... |
Q5HLX8 | MKQFEIVTQPIETEQYRDFTINERQGAVVVFTGHVREWTKGIRTQHLEYEAYIPMAEKKLAQIGKEIEEKWPGTITTIVHRIGPLQISDIAVLIAVSSPHRKAAYAANEYAIERIKEIVPIWKKEIWEDGAEWQGHQKGTYNEAKKGKAR | Function: Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity).
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cycli... |
Q56210 | MPDLLTCDRHQIELSLAPIPLSAAAEFCHDDRYGAFASFVGWVRRVNVGRLVTGITYQSFQPLCRTVLTEICQEAEQVFGQELRIYVQHRLGETRVGDPTVLIGVGAIHRDEACEACRYVIEELKHRAPIWKLEHYEDGDSGWVPGNCLCQERRSRDRRGSTGPE | Function: Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity).
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cycli... |
Q97CL5 | MINTYVEITEKDINPLDLINRVRRPDAGAIVTFEGTVRNDSDGVRVTALYYEAYKEMAEMQIADLIDEAKKKYNILDAAVCHRIGLVGLTEDSVVISVSSAHRSSAFEACRYIIDTIKERVPIWKRDILENGNGSWH | Function: Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity).
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cycli... |
Q9KT77 | MDHRVSVQKEDFSVAQEYEALAQGSQAGAVVTFVGKVRDMNLGDNVVGLHLEHYPGMTEKSLLEICDMAQERWPLQRVRVIHRIGDMLSGDQIVLVGVSSAHRNAAFAACEFIMDYLKTRAPFWKKELTTEASRWIDSRDSDHQAAQRWE | Function: Converts molybdopterin precursor Z into molybdopterin. This requires the incorporation of two sulfur atoms into precursor Z to generate a dithiolene group. The sulfur is provided by MoaD (By similarity).
Catalytic Activity: 2 [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-NH-CH2-C(O)SH + cycli... |
Q98MK2 | MRRDIAGIVLAGGQSRRMGGGDKSLLPLGSGSVLDQILSRFGPQIEILALSANGDPERFSRFGLPVLADTVEGFAGPLAGILTGLEWAIAGTPCKAVVTAAGDTPFLPLDLVDRLAAAARDHPGSIAVASSAGRRHPTFALWPTECRDALRHFLVDEDNRRVSDFIERHGHVEVEFRFVQSAGLDPFFNINVPDDLAQAARLLQSMTS | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 22239
Sequence Length... |
Q92PB2 | MTGAPSHATFPPAVILAGGLSSRMGRPKAGLVLGGRSMLTRVIERLRPQVAGIAINLNADPDPASAFGLEVVPDTIPGFVGPLAGILAAMRHTVRKSPGASHVLTVPVDTPLFPKSLAARLKTAITSGGEIAVAFSAGEMHPLFALWPVALADDLEAWIHADEKRRVRAFIARHESATVEFPLIPTAAGPLDPFFNINTPEELRQAEAWLPYLEDREP | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 23198
Sequence Length... |
Q7UYZ6 | MRNELTAMPHAAPPPLLGVLLAGGRSSRMGTPKALLPHPSGGTFLTHSLDRLRLVCEEKIVVSLASEAHRAQVQLPPSVPALFDSQPALGPAMGVSVALQHASSNGFAGCLFTPVDLPDLSVDDLLSLVHAWRESPTQIVLAQQTDPERLQPLVGIYPVACMDSIQRVVESEHRSLYRSLRSSDHQTVAIPSTRLRNVNTPADLGPPFDST | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 22640
Sequence Length... |
Q9X7K0 | MRIAGIILAGGQGRRMGREKALVPLSGVPLIARVLALAPQVEAVAISANGDPGRFGLGLPVLPDRPGESGLGPMAGIRAGLDWAAGIGAEALVSTATDTPFLPEDLVERLAAAAPAHAQSFGRDHYTAALWRVATVPRIDALFAADERRIARLSGGAVAVPFDTTPDPFANLNTPEDLARAEDRLRQNAP | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 19752
Sequence Length... |
Q2IYY0 | MFGRRSMADPPAPPAIILAGGLAQRMGGGDKALRMVGGRTLLALVIDRLASQCDILALSANGDPARFADYDLPVIADPVDGFRGPLAGVLAGLDWVAEHRPAARWMLSTPADCPFLPRDLVARLHQARIDQQADIAVAASAGRSHPVIALWPVGLRIDLRRALLADDIRKVDRFTARYPRAMAEWPVEPADPFFNANTPQDLAEAEGLAMREPD | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 23100
Sequence Length... |
A8GLJ4 | MHEEITGIILAGGRATRMGGEDKGLIQIAGIPLYQYVLSRLRPQVSLMAISANRNQARYGESGLPIVSDLTPDFSGPLAGMLAGLKHAATEWVVFVPCDVPDFPATLVDQLWQQKGSSLAAYASDGERAHPTLALLHTSLAPQLKEYLARGERKLMLFLDAAGARKIAFSGQQAAFHNLNTREDCLRWQQEKGLTNE | Function: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor.
Catalytic Activity: GTP + H(+) + Mo-molybdopterin = diphosphate + Mo-molybdopterin guanine dinucleotide
Sequence Mass (Da): 21485
Sequence Length... |
Q8IU29 | MTVLSQIIKPDDMIKITSEFARLGDRCYLDNAGATLYPKSLITSINEDLLKNVYMNPHTDKNTKDYIEQIRCLILKHFNTDPSTYTLIFTSGTTQALKLVIESFQFMKNEDDDLNCGSFVYLEDNHTSVVGLRELAVDKDAEVVHIAHEDFLNVINTKAKQTSKYTNGGNCLVAYPAQSNFNGFKYPLNCIENIKNGCLNNHLKKHLCEINSDWYVLLDAAAYVATSKLDLAKVQPDFVSLSFYKIFGFPTGLGALLVKKSSENVLSQKRYFGGGTVDALLSNEHYHIKREIFHERFEDGSLSFLSIISLKQCLDTMYRI... | Function: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form.
Catalytic Activity: AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine + th... |
A6SRX6 | MEEYNKAVEEFRKHEYPMLKDAVYLDHAGTTLYSKSLMERYMGDMMSNLYGNPHSASTSSQLSTSRIENTRLNVLQFFNADPEDFDVVFVANATAGIKLVMDAFRCQEDGFLYGYHQDSHTSLVGVREDAVSSRCLDDDAVECWLSGSEALVRNEHNSEIGLFAYPAQSNLDGRRLPLSWPERVRNLSYEAQANTYTLLDASALVSTSPLDLSDVSKAPDFTVLSFYKIFGFPDLGALIVRKDSGAILQTRKYFGGGTVEVVVCLKEQWHAPKGQSLHENLEDGTLPFHNIMALEAAIDVHKSLYGSMECIANHTTFLAR... | Function: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form.
Catalytic Activity: AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine + th... |
Q9N0E7 | MAGGAAHPGAELLPFARFLDSSLQPLVYGYGRGTLHELRAREFGRLAGTVYLDHAGTTLFPQSQITSFMKDLMENVYGNPHSQNISSKLTHDTVEQVRFRILAHFHTSPEDYTVIFTSGSTAALKLVAEAFPWVSPGPEGSGSCFCYLTDSHTSVVGMRKITAAMNVSSIPVRPEDMWSAERQDAAAAGDPAGQPPHLFCYPAQSNFSGTRYPLSWIGEVKSGRRRPASRPGKWFVLLDAAAFVGTSPLDLSVHQADFVPISFYKIFGFPTGLGALLVNNRLAALLRKTYFGGGTAAAYLAGDDFYVPRESVAERFEDGT... | Function: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form.
Catalytic Activity: AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine + th... |
A8X493 | MPYLDHAGSTLPSKTQLEELAKLQTQLILANPHSHHSTAIKTQQIVSSARHRILRYFNTTADDYFVVFTNNTTHALKIVAENFNFGHRTQEGVVSEISAVLKGGPSNFAYFNDSHHSVVGLRHVVLGKVDAISCVNEDVVKEECIPKVENSLFVFTAMSNFLIPFQINEKLISGWSVCVDAAALVSGTRLDLTAHRPNFVAFSFYKIFGYPTGIGALLVKKDSSKSIEKTSFAGGTVQSVDEMTMHFVIRDFERAYEEGTINSYGIAQLQKGFEEIERCGGMQAIRAHTYDLRSKAVQILQSKTHPNGKKVVEIYSQPHI... | Function: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form.
Catalytic Activity: AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine + th... |
Q2HE65 | MARTDDQAKSVDTRYNARVESLRDKEYPMLNGSIYLDHAGTTPYPKSLMDRFAKEMTSNLFGNPHSASASSQLSTARIEDIRLRVLRFFNADPAEFDLVFVANATAGIKLVADALRTAPDGFDYSYHQASHTSLIGVREEARNSLCLDDQEVDDWLGGGCPFENDSEDRPVLFAYPAQSNMDGRRYPLNWAEKVCRGGTRKTYTLLDAAALVCSSPLDLSQANAAPDFTVLSFYKIFGFPDLGALIVRRDAEEAFDTRRYFGGGTVDMVVCLKEQWHAPKAQFLHERLEDGTLPVHSIIALDAALDVHKQLFGSMRDVAS... | Function: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form.
Catalytic Activity: AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine + th... |
A2VD33 | MDTRSLQDFQDLCTFDVFKSFGHYYGYGVDQQALIDQEFKRIKGVTYLDHAGTTLFPESLIKGFHDDISRNVYGNPHSHNSSSRLTHDTVESVRYKILAHFNTSPEDYSVIFTSGCTAALKLVADTFPWKPMSNKEPGSQFCYLTDNHTSVVGIRGATALQGVGTISVSPREVETRARNKTQTNGEEECSTPHLFCYPAQSNFSGRKYSLSYVKGIQSQQLYPACEHHGQWFVLLDAACFVSCSPLDLSQYPADFVPISFYKMFGFPTGLGALLVRNEAAEVLRKTYFGGGTAAAYLVEENYFIPKPNLASRFEDGTISF... | Function: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form.
Catalytic Activity: AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine + th... |
Q559G8 | MLIFIISIIITIASIIFLFETVFNKNSNTINNNNNSNNNNNNNNNNNNNNNNNKNNIKENNIDKNKEIKIKEKLILNNNDPKENDLKYKEEFNNFLNKFSKNQEYGYKDNLIDNELRNHYNNNNNNNNNNNNNNKDDQFPKLKDIVYLDHAASTLASMNQIEEISKELKNSMFCNPHSVNPIGLKTKEEVDSIRENILNYFNAPYRQYSVIFTSGCTDSLKKVGEYFAWTKNSKFYYSLESHNSLLGIREYACESIGGSSTTSFQPIPSLYFKCNNNQFNDILEIIGNNDDNNNESYSLFGYPGQCNYSGTKYPLELINR... | Function: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form.
Catalytic Activity: AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine + th... |
Q9VRA2 | MTSYRPEFSASEQSQIDAEFSRLASNKSVYLDHAGTTLYAESQVTAAAEQLQRNVICNPHTCRLTGDFVDQVRFKILEFFNTTAEDYHVIFTANATAALSLVAENFDFGSSGEFHFCQENHTSVLGMRERVRENGIYMLRENEISGGKHKANGKVHEVSGKTGNSLLTFSAQCNFSGYKIPLEVIEQIQIDGLAKPGKELWSSLGEKKKNMHNDYYICLDAASFVATSPLDLQKYRPDYVCLSFYKIFGYPTGVGALLVSRRGAEVFQKRRFFGGGTINYAYPHAMDYQLRETFHQRYEDGTLPFLSIVGLLEGFRTLER... | Function: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form.
Catalytic Activity: AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine + th... |
Q2K2X0 | MTLIVEAKQRLGAFSLDAAFTSEGGVTAFFGRSGSGKTSLIRIIAGLARPDGGRVVLDGERLTETTAGIFVPKHRRRFGYVFQEARLFPHLSVRANLSYGRWFAPKAGRSESFDHIIDLLGIETLLERSPAKLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDEARKAEILPYLERLRDETEIPIVYVSHSIAEVARLANQVVVLSDGKVQATGPAVDILSRPSAAADRKEAGALLEGTVESFDARHRLSTVTLKSSQLHIPSAVLTPGRPVRIRIPSRDVMLATARPEGLSALNILEGRIEAISPGEDGTVEIRIDCA... | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38324
Sequence Length: 3... |
Q92LU2 | MRLEVEARLRLGSFAIDAAFGSEGGVTALFGRSGSGKTSLVNIIAGLLRPDQGRVVLDGDTIADSERRLFTPVHRRRFAYVFQEARLFPHLSVRGNLAYGRWFAGAARSGPEFGRIVEMLGIGHLLDRMPSKLSGGERQRVAIGRALLAFPRLLLMDEPLAALDDARKAEILPYLERLRDETRIPIVYVSHSVAEVARLAERVVVMENGRVKASGKTAAVLNEPFPTSGPGRREAGALIEGIVDSHDEGHELTVVRAGDCLIRVPHLVAEPGQRLRLYIAARDVMLATRRPEGISALNVLPGTIVGLSSPRQGSIDVRVD... | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38720
Sequence Length: 3... |
Q08381 | MISARFSGRQGDFTLDAAFDVPGQGVTALFGPSGCGKTTVLRCMAGLTRLPGGHLVVNGVTWQEGRQITPPHRRAVGYVFQEASLFTHLSVRENLVYGLRRARGPLRISEAEVTQLLGIDPLLRRPTATLSGGERQRVAIGRALLSQPELLLMDEPLSALDRISRDEILPYLERLHASLQMPVILVSHDLSEVERLADTLVLMEAGRVRAAGPIAAMQADPNLPLIHRPDLAAVIEGVVIALDPAYGLSTLQVPGGRIVVPGNLGPIGARRRLRVPATDVSLGRHAPTDTTILNALPAVILGAEAAEGYQITVRLALGAS... | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38546
Sequence Length: 3... |
Q2J1U0 | MRAIAPRSIRGEFRGRLGGFALDAAFSVPATGITGLFGPSGCGKSTVLRCLAGLQRLPGGRCDVDGDVWQDEATFLKPHQRPIGYVFQEASLFQHLSVRANLLYGAPRGGADAAEGAVGFDEVIELLGLSHLLDRAPRNLSGGERQRVAIGRALLSQPKLLLMDEPLSALDRLTKDEILPFLERLHARLSLPVIYVSHDITEIERLADHLILMRAGKVLAAGPLTELQSDPALPLATARDAAVNVDAIAESYDSVYGLLTLRLDGGRLLVPSAPVQPGEARRIRIAAGDVSLAREAPHRTSILNILPARIATTSPVGPNE... | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40103
Sequence Length: 3... |
Q21BF6 | MRDVSRSIQAQFRGALGRFALDAAFTVPATGITGLFGPSGCGKSTVLRCIAGLQQLPGSTFAIDGDVWQDASQFRQPHQRPIGYVFQEASLFAHLSVKANLLYGAPRDAAHARDSITFDEVIELLGLAALLERSPRHLSGGERQRVAIGRALLSQPKLLLMDEPLSALDRLTKDEILPFLERLHERLALPVIYVSHDMAEIERLADHLVLMRKGQVLAAGPLAALQSDPALPLAASRDAAVNFEATVEDYDPGYGLLTVAVDGGRLLVPAPPAQRGEHRRLRIAAGDVSLARELPHNTSILNVLPARIVSHNPLGDSEIL... | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40798
Sequence Length: 3... |
Q2RWI9 | MLDIDVLRQQGALRLSIAFRAGKGVTALFGRSGAGKTSVISMVAGLSRPDGGRIVVDDRVLFDGAKGIDLAPEKRRVGYVFQEGRLFPHLTVRQNLAFGMNRVPAAERYVGEDDVVDLLGISALLDRRPAKLSGGEKQRVAIGRALLASPRILLMDEPLASLDAQRKDEVLPFIARLPRRFSIPILYVSHAMDEVLRLADTLVLIAEGQVAASGPLEEVLARPDIPDFAAQRDAGAVVAAKVAGRDIPFGATLLDTPAGLLRTRPIDLPLGTKVRVRIAAADISLALERPRMVSVQNILAATILAIGEPEDGRLSVDLDA... | Function: Part of the ABC transporter complex ModABC involved in molybdenum import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 39673
Sequence Length: 3... |
Q3S2U5 | MASHQSEKEKPQSCTTEVQVSHVTGLKLGLVVTSVTLVVFLMLLDMSIIVTAIPHITAQFHSLGDVGWYGSAYLLSSCALQPLAGKLYTLLTLKYTFLAFLGVFEVGSALCGAARCSTMLIVGRAVAGMGGSGLTNGAITILASAAPKQQQPLLIGIMMGLSQIAIVCGPLLGGAFTQHASWRWCFYINLPVGALAAILLLAIHIPKSVPTSDCTMPAPRAVGVRVILSQLDLLGFVLFAAFAVMISLALEWGGSDYMWDSSVIIGLFCGAGISLVVFGFWERYVGNSMAMIPFSVASRRQVWCSCLFLGFFSGALLTFS... | Function: Efflux pump; part of the gene cluster that mediates the biosynthesis of monakolin K, also known as lovastatin, and which acts as a potent competitive inhibitor of HMG-CoA reductase .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57408
Sequence Length: 543
Subcellular Location: Membrane
|
Q9UQ07 | MKNYKAIGKIGEGTFSEVMKMQSLRDGNYYACKQMKQRFESIEQVNNLREIQALRRLNPHPNILMLHEVVFDRKSGSLALICELMDMNIYELIRGRRYPLSEKKIMHYMYQLCKSLDHIHRNGIFHRDVKPENILIKQDVLKLGDFGSCRSVYSKQPYTEYISTRWYRAPECLLTDGFYTYKMDLWSAGCVFYEIASLQPLFPGVNELDQISKIHDVIGTPAQKILTKFKQSRAMNFDFPFKKGSGIPLLTTNLSPQCLSLLHAMVAYDPDERIAAHQALQHPYFQEQRKTEKRALGSHRKAGFPEHPVAPEPLSNSCQI... | Function: Able to phosphorylate several exogenous substrates and to undergo autophosphorylation. Negatively regulates cilium length in a cAMP and mTORC1 signaling-dependent manner.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 48014
S... |
Q9WVS4 | MKNYKAIGKIGEGTFSEVMKMQSLRDGNYYACKQMKQHFESIEQVNSLREIQALRRLNPHPNILALHEVVFDRKSGSLALICELMDMNIYELIRGRRHPLSEKKIMLYMYQLCKSLDHMHRNGIFHRDVKPENILVKQDVLKLGDFGSCRSVYSKQPYTEYISTRWYRAPECLLTDGFYTYKMDLWSAGCVFYEIASLQPLFPGVNELDQISKIHDVIGTPCQKTLTKFKQSRAMSFDFPFKKGSGIPLLTANLSPQCLSLLHAMVAYDPDERIAAHQALQHPYFQVQRAAETQTLAKHRRAFCPKFSMVPESSSHNWSF... | Function: Able to phosphorylate several exogenous substrates and to undergo autophosphorylation . Negatively regulates cilium length in a cAMP and mTORC1 signaling-dependent manner .
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 48065... |
P44206 | MKLKSLLIACLLSSLSFSALADRIITDQLDRKVTIPDHINRAVVLQHQTLNIAVQLDATKQIVGVLSNWKKQLGKNYVRLAPELENMAMPGDLNSVNIESLLALKPDVVFVTNYAPSEMIKQISDVNIPVVAISLRTGEVGEKGKLNPTLTDEDKAYNDGLKQGIELIAEVFEKKQQGDELVKAAFANRKLLADRLGDVSADKRVRTYMANPDLGTYGSGKYTGLMMEHAGAYNVAAATIKGFKQVSLENVLEWNPAVILVQDRYPDVVPQILNDQGWANIQALKDKKVFLMPEYAKAWGYPMPEALALGEVWLAKALYP... | Function: Part of the ABC transporter complex MolBCA involved in molybdate import . Functions as a low-affinity molybdate transporter . Binds to both molybdate and tungstate, but not to sulfate or phosphate .
Sequence Mass (Da): 39205
Sequence Length: 351
Domain: Nucleotide binding is coupled to a conformational shift ... |
Q57130 | MQPDSYPKILFGLTLLLVITAVISLGIGRYSLSVPQIGQILWAKATALEIDPVQQQVIFQVRLPRILTALCVGAGLALSGVVLQGIFRNPLVNPHIIGVTSGSAFGGTLAIFFGFSLYGLFTSTILFGFGTLALVFLFSFKFNQRSLLMLILIGMILSGLFSALVSLLQYISDTEEKLPSIVFWLMGSFATSNWEKLLFFFVPFLLCSSILLSLSWRLNLLSLDEKEAKALGVKMAPLRWLVIFLSGSLVACQVAISGSIGWVGLIIPHLSRMLVGANHQSLLPCTMLVGATYMLLVDNVARSLSDAEIPISILTALIGA... | Function: Part of the ABC transporter complex MolBCA involved in molybdate import . Responsible for the translocation of the substrate across the membrane . Functions as a low-affinity molybdate transporter .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36531
Sequence Length: 337
Domain: The trans... |
Q57399 | MNKALSVENLGFYYQAENFLFQQLNFDLNKGDILAVLGQNGCGKSTLLDLLLGIHRPIQGKIEVYQSIGFVPQFFSSPFAYSVLDIVLMGRSTHINTFAKPKSHDYQVAMQALDYLNLTHLAKREFTSLSGGQRQLILIARAIASECKLILLDEPTSALDLANQDIVLSLLIDLAQSQNMTVVFTTHQPNQVVAIANKTLLLNKQNFKFGETRNILTSENLTALFHLPMFEQQAQYKESFFTHFVPLYKTLLK | Function: Part of the ABC transporter complex MolBCA involved in molybdate import . Responsible for energy coupling to the transport system . Functions as a low-affinity molybdate transporter .
Catalytic Activity: ATP + H2O + molybdate(out) = ADP + H(+) + molybdate(in) + phosphate
Location Topology: Peripheral membrane... |
Q10459 | MHINTPVLLAIIYFLVFAPKSADAWWLLSKTDTSSANSGSSPILCKNVPGLTPQQKRMCHENPNIIKYLISGLRSALHTCEYTFQREAWNCTLTLPGVGTSPLQIASRESAYVYAISAAGVSHSLARACSKGLIDDCGCGETPQGSGSVAVSQASSRSSSDFVWAGCSDNVKFGNTFGRKFVDQYDRQHATEPRSQMNLHNNRVGRRLLVNAMNKECKCHGVSGSCVTKTCWKVMPKFDEFASRLHQKYQLAKLVTNNDQKLTVRSSPSAGSSGRSERFARNMDASSKQMRNELIYLDASPNYCAIDVKDRECGENCPNI... | Function: Ligand for members of the frizzled family of seven transmembrane receptors. Required in embryonic development for endoderm specification and the correct positioning and orientation of the mitotic spindles and division planes in blastomere cells . Involved in cleavage axis determination . Binds to receptor tyr... |
Q9XTC6 | MDNSSQSKPSSSSSSHSPSPAAITPTQRTTRDSGLCSTIDIPEIQAQCIDNLNSHYLGKGTYGLVEKTRYRKTRQDDFRPAAIKYSSQLHMATLIREAKVMWDLRNHPNIIKIYGLYKSPRNGQGVVMEYMDCGSMADLLYDRTHINYTIDHVASWMFQLSSAVDFFHSNSQVHRDLKLQNMLLSDRYRTMKLCDFGTFTSMHQSMTSNRGTPITMAPEVFRCEQYNMKSDIYSIGIIMWQIIARNHPYRRDLSVPGLLYNVATANLRPQELECNPILSEFYKKCWNDNADIRPTSSECVEYFTLLKDEYPNGSVPLSDS... | Function: Part of the Wnt signaling pathway essential for the specification of the mesodermal cell fate in early embryos. Stimulates the wrm-1/lit-1-dependent phosphorylation of pop-1 and plays a role in the initial nuclear accumulation of wrm-1.
PTM: May be autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protei... |
A0A0K3AWM6 | MHRHILILFLFGCLSADQRLSSTSISSMNGFSTTRKCEHITIPMCKNLDYNQTVFPNLLGHTTQSEAGPAIAQFNPLIKVKCSEDIRLFLCTVYAPVCTVLEKPIQPCRELCLSAKNGCESLMKKFGFQWPDQLDCNKFPVTDLCVGKNSSESSNSKNYRSSNDVTFGVSTIANEVVLSPKKCPHHMHTTSGSHFSLPLLSGRLPECSLTCEADNQVPMMFDGRVRRILRIWTAAWSVACFVCSLFTLVTFLVDLSRFAYPVRPILYLAFCYLAISTVYMIGVVGEDGFACGTYGSTPTTLVTQGGENVGCSALAVVHYF... | Function: Receptor for Wnt proteins . Most frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of gsk-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes (Probable). A second signaling pathway invo... |
Q21154 | MTQDKPIVETISNAGEQVTNVFGQFWQLVTSKNTTNNGDSKPIKIEQLPIYAEDNAPLKQKFLPEEPLPLQREFATIRIACEQEYDRVAERFKVVDCAMTQTKKAATKCNAYLTEEWTALPKAAAITVGGMAGFVLGLKRGPVGRLLTTTIGLATMAAFCYPIEAVDVAKTGRAHAEQTWYSFQESPTPSAIVKTNLSPPK | Function: Sustains mitochondrial morphology probably through maintaining cristae morphology . May act as a component of the MICOS complex, a large protein complex of the mitochondria (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 22082
Sequence Length: 201
Subcellular Location: Mito... |
Q46203 | MKKLLKSALLFAATGSALSLQALPVGNPAEPSLLIDGTMWEGASGDPCDPCATWCDAISIRAGYYGDYVFDRVLKVDVNKTFSGMAATPTQATGNASNTNQPEANGRPNIAYGRHMQDAEWFSNAAFLALNIWDRFDIFCTLGASNGYFKASSAAFNLVGLIGFSAASSISTDLPMQLPNVGITQGVVEFYTDTSFSWSVGARGALWECGCATLGAEFQYAQSNPKIEMLNVTSSPAQFVIHKPRGYKGASSNFPLPITAGTTEATDTKSATIKYHEWQVGLALSYRLNMLVPYIGVNWSRATFDADTIRIAQPKLKSEI... | Function: In elementary bodies (EBs, the infectious stage, which is able to survive outside the host cell) provides the structural integrity of the outer envelope through disulfide cross-links with the small cysteine-rich protein and the large cysteine-rich periplasmic protein. It has been described in publications as ... |
Q7RTY1 | MELKKSPDGGWGWVIVFVSFLTQFLCYGSPLAVGVLYIEWLDAFGEGKGKTAWVGSLASGVGLLASPVCSLCVSSFGARPVTIFSGFMVAGGLMLSSFAPNIYFLFFSYGIVVGLGCGLLYTATVTITCQYFDDRRGLALGLISTGSSVGLFIYAALQRMLVEFYGLDGCLLIVGALALNILACGSLMRPLQSSDCPLPKKIAPEDLPDKYSIYNEKGKNLEENINILDKSYSSEEKCRITLANGDWKQDSLLHKNPTVTHTKEPETYKKKVAEQTYFCKQLAKRKWQLYKNYCGETVALFKNKVFSALFIAILLFDIGG... | Function: Extracellular pH-and Na(+)-sensitive low-affinity creatine transporter . Functions also as a pH-independent carnitine efflux transporter .
Catalytic Activity: creatine(in) = creatine(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55794
Sequence Length: 509
Subcellular Location: Cell m... |
M0RCI4 | MGFQKSPDGGWGWVIVVVSFFTQFLCYGSPLAVGVLYVEWLDAFGEGKGKTAWVGSLASGVGLLASPVCSLFVSSFGARPVTIFSGFLVAGGLMLSSLAPNIYFLFFSYGIVVGLGCGLLYTATVTITCQYFDSRRGLALGLISTGSSVGLFIYAALQRMLIEFYGLDGCLLIVGALALNILACGSLMRPLQTSDCPFPEKIAPENVPDRYSIYNEKEKNQEETMTFQDKGYSNEDKCLPNGDWGRETSLPKNPTGAAHTKEPEPYKKKVVEQTNFCKQLAKRKWQVYRNYCGETASLFKNKVFSALFVAILLFDIGGFP... | Function: Extracellular pH-and Na(+)-sensitive low-affinity creatine transporter . Functions also as a pH-independent carnitine efflux transporter (By similarity).
Catalytic Activity: creatine(in) = creatine(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55569
Sequence Length: 508
Subcellular L... |
Q44456 | MNIVIGLIITFGCIIGGYMAMGGHLNVLVQPFELMIIGGAGLGGFIMANPMKVVKDSGKALGEAFKHSVPKERNYLDVLGVLYSLMRDLRTKSRNEIEAHIDNPEESSIFQSAPSVLKNKELTSFICDYVRLIIIGNARSHEIEALMDEEIETILHDKLKPYHAITTMGDSFPAIGIVAAVLGVIKAMGKINESPEVLGGLIGAALVGTMLGIILSYSICNPLASQVKIVRTKQHRLYIIVKQTLIAYMNGSVPQVALEYGRKTISNYERPSIDAVEQEMMNPGGENKAA | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31529
Sequence Length: 290
Subcellular Location: Cell inner membrane... |
O67122 | MDVGTIIGIIAAFLLILISILIGGSITAFINVPSIFIVVGGGMAAAMGAFPLKDFIRGVLAIKKAFLWKPPDLNDVIETIGEIASKVRKEGILALEGDIELYYQKDPLLGDMIRMLVDGIDINDIKATAEMALAQLDEKMSTEVAVWEKLADLFPAFGMIGTLIGLIQMLRNLNDPSALGPGMAVALITTLYGAILANAFAIPVANKLKKAKDMEVLVKTIYIEAIEKIQKGENPNVVKQEAAIMLGVELPEEV | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27263
Sequence Length: 254
Subcellular Location: Cell membrane
|
P28611 | MDKTSLIGIILAFVALSVGMVLKGVSFSALANPAAILIIIAGTISAVVIAFPTKEIKKVPTLFRVLFKENKQLTIEELIPMFSEWAQLARREGLLALEASIEDVDDAFLKNGLSMAVDGQSAEFIRDIMTEEVEAMEDRHQAGAAIFTQAGTYAPTLGVLGAVIGLIAALSHMDNTDELGHAISAAFVATLLGIFTGYVLWHPFANKLKRKSKQEVKLREVMIEGVLSVLEGQAPKVIEQKLLMYLPAKDRLKFAEQGEAQNGEKKEEEA | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29339
Sequence Length: 270
Subcellular Location: Cell membrane
|
Q44902 | MNLASIIGWGVGFGAILISMAFTPTGLGVFWDLSSVFITVVGSFSALMASSEVVAVKKIPTYLGFFFRRNSYAKVSIIKILVELSEKARKEGLLSLDDELEQINDPFFKSGMRLVVDGADPEVIRTMLYLELDQMQERHKVGSDLFKTWAKLAPAFGMTGTLIGLVALLGNLEDKSALGSSMAVALITTLYGTIMANLMFTPVQLKLEKIDTEEAAVKTMIIEGVLSIQSGDNPRILEQKLMTFLTPKDRSQLNSSIGGE | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28354
Sequence Length: 260
Subcellular Location: Cell inner membrane... |
Q53174 | MDIAAAIGLIGAIVMVVGSMIYAGGVAPFVDIPSLVIVVAGTAFIVLAMKPLPVFLGHFKAMMKVFKPSRFDMNEVISTMVELSNLARKDGIMALEGKAVPDAFFEKGLQLLVDGTDEAKLVKQLKYEIKAMKARHEAYQGAVKAWIDIGPAMGMVGTLIGLVLMLGNMSDPKSIGPAMAVALLTTLYGALMANVIFAPILNKLEGYSADEVTYRELVIEGLRGIARGESARMIEDQMVCALDRKQQMKRKAA | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27195
Sequence Length: 253
Subcellular Location: Cell inner membrane... |
P09348 | MLILLGYLVVLGTVFGGYLMTGGSLGALYQPAELVIIAGAGIGSFIVGNNGKAIKGTLKALPLLFRRSKYTKAMYMDLLALLYRLMAKSRQMGMFSLERDIENPRESEIFASYPRILADSVMLDFIVDYLRLIISGHMNTFEIEALMDEEIETHESEAEVPANSLALVGDSLPAFGIVAAVMGVVHALGSADRPAAELGALIAHAMVGTFLGILLAYGFISPLATVLRQKSAETSKMMQCVKVTLLSNLNGYAPPIAVEFGRKTLYSSERPSFIELEEHVRAVKNPQQQTTTEEA | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel. Overexpression of MotA, with or without MotB, restores motility in a pdeH disruption, (a c-di-GMP phosphodiesterase) suggesting there is an interaction... |
P65411 | MDLSTILGLVLAVASISLGDILEDGNPLHIIHLSSVIIIVPTSLFAAMTGTHARYVKAAYKEIKIVFLNPKINLNETIKNLVELATLARKDGVLSLEGRVAQIEDDFTRNGLSMIIDGKDLKSVKESLEISIEEMEEYYHGAAHYWETAGETAPTMGLVGAVMGLMLALQKLDNPAEMAAGIAGAFTATVTGIMCSYAIFGPFGHKLKAKSKDIIKEKTVLLEGILGIANGENPRDLENKLLNYIAPGEPKKSQFEG | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27710
Sequence Length: 257
Subcellular Location: Cell inner membrane... |
O07886 | MDIASFIGLFGGFAIIIFGAVLGGSARGLFHVPSLLITVGGSYLTLFLTYPLSYAVGVFRVIARVFHAADFHEREIVQRLYALAEKSRRTGLLALEEEIQDFDDDFVRTGLRNVVDGVDGDAIKALMESELTHMEDRHNTWISLLNSWAALAPGYGMLGTVMGLIGMLATLEDKSSLGSNMATALITTFYGSLVQNWFITPVATKLQYQHDLEVKSKEMVIEGVLSIQAGDHPRVLAQRLLTYLSPKMRKELEMELIKD | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for rotation of the flagellar motor. Probable transmembrane proton channel (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28645
Sequence Length: 259
Subcellular Location: Cell inner membrane... |
P28612 | MARKKKKKHEDEHVDESWLVPYADILTLLLALFIVLYASSSIDAAKFQMLSKSFNEVFTGGTGVLDYSSVTPPENESDGIDEVKKEKEEKEKNKKEKEKAADQEELENVKSQVEKFIKDKKLEHQLETKMTSEGLLITIKDSIFFDSGKATIRKEDVPLAKEISNLLVINPPRNIIISGHTDNMPIKNSEFQSNWHLSVMRAVNFMGLLIENPKLDAKVFSAKGYGEYKPVASNKTAEGRSKNRRVEVLILPRGAAETNEK | Function: MotA and MotB comprise the stator element of the flagellar motor complex. Required for the rotation of the flagellar motor. Might be a linker that fastens the torque-generating machinery to the cell wall (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 29483
Sequenc... |
P0CAX7 | MINVQAKPAAAASLAAIAIAFLAGCSSTKPVSQDTSPKPATSPAAPVTTAAMADPAADLIGRGCAQYAAQNPTGPGSVAGMAQDPVATAASNNPMLSTLTSALSGKLNPDVNLVDTLNGGEYTVFAPTNAAFDKLPAATIDQLKTDAKLLSSILTYHVIAGQASPSRIDGTHQTLQGADLTVIGARDDLMVNNAGLVCGGVHTANATVYMIDTVLMPPAQ | Function: Induces expression of human (host) matrix metalloproteinase-9 (MMP9) in a TLR1/TLR2-dependent fashion; the acylated 20 first mature residues (residues 25-40) induce the most expression, but whole recombinant protein (non-acylated and non-glycosylated), and mannosylated but not acylated protein (residues 26-22... |
Q2M385 | MNNFRATILFWAAAAWAKSGKPSGEMDEVGVQKCKNALKLPVLEVLPGGGWDNLRNVDMGRVMELTYSNCRTTEDGQYIIPDEIFTIPQKQSNLEMNSEILESWANYQSSTSYSINTELSLFSKVNGKFSTEFQRMKTLQVKDQAITTRVQVRNLVYTVKINPTLELSSGFRKELLDISDRLENNQTRMATYLAELLVLNYGTHVTTSVDAGAALIQEDHLRASFLQDSQSSRSAVTASAGLAFQNTVNFKFEENYTSQNVLTKSYLSNRTNSRVQSIGGVPFYPGITLQAWQQGITNHLVAIDRSGLPLHFFINPNMLP... | Function: Plays a key role in the innate immune response following bacterial infection by inserting into the bacterial surface to form pores (By similarity). By breaching the surface of phagocytosed bacteria, allows antimicrobial effectors to enter the bacterial periplasmic space and degrade bacterial proteins such as ... |
Q752H4 | MKGLILVGGYGTRLRPLTLTVPKPLVEFCNRPMILHQIEALAAAGVTDIVLAVNYRPEVMVETLKKYEKQYGVSITFSVETEPLGTAGPLKLAEKVLKKDNSPFFVLNSDVICEYPFKELAAFHRAHGGKGTIVATKVDEPSKYGVIVHDIATPNLIDRFVEKPVEFVGNRINAGLYILNPEVIDLIELRPTSIEKETFPILVEQKSLYSFDLEGYWMDVGQPKDFLAGTVLYLNSLSKRHPEQLAKGDNIVGNVIIDPSAKISGSAKLGPDVVIGPNVTIGEGVRITRSVVLSDSTINDHSLVKSTIVGWHSTVGKWCR... | Function: Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint (By similarity).
Catalytic Activity: alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose
Sequence Mass (Da): 39471
Sequence Length: 361
Pathway: Nucl... |
Q4U3E8 | MKALILVGGFGTRLRPLTLTLPKPLVEFGNRPMILHQVESLAAAGVTDIVLAVNYRPDVMVAALKKYEEQYNVRIEFSVESEPLGTAGPLKLAEKILGKDDSPFFVLNSDIICDYPFKQLAEFHKKHGDEGTIVVTKVDEPSKYGVVVHKPNHPSRIDRFVEKPVEFVGNRINAGIYILNPSVLKRIELRPTSIEQETFPAICSDGQLHSFDLEGFWMDVGQPKDFLTGTCLYLTSLAKRNSKLLAPNSEPYVYGGNVMVDPSAKIGKNCRIGPNVVIGPNVVVGDGVRLQRCVLLENSKVKDHAWIKSTIVGWNSSVGK... | Function: Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint (By similarity).
Catalytic Activity: alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose
Sequence Mass (Da): 40124
Sequence Length: 364
Pathway: Nucl... |
O93827 | MKGLILVGGYGTRLRPLTLTLPKPLVEFGNRPMILHQIEALAAAGVTDIVLAVNYRPEVMVSTLKKYEEEYGVSITFSVEEEPLGTAGPLKLAEEVLKKDDSPFFVLNSDVICDYPFKELADFHKAHGAAGTIVATKVDEPSKYGVIVHDRDTPNLIDRFVEKPVEFVGNRINAGLYILNPSVIDLIEMRPTSIEKETFPILVEQKQLYSFDLEGYWMDVGQPKDFLSGTCLYLTSLSKKHPEKLCKEKYVHGGNVLIDPTAKIHPSALIGPNVTIGPNVVVGEGARIQRSVLLANSQVKDHAWVKSTIVGWNSRIGKWA... | Function: Involved in cell wall synthesis where it is required for glycosylation. Involved in cell cycle progression through cell-size checkpoint (By similarity).
Catalytic Activity: alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose
Sequence Mass (Da): 39975
Sequence Length: 362
Pathway: Nucl... |
A6QQZ7 | MPALSTGSGNDTGLYELLVALPAQLQPHVDSQEDLTFLWDVFGEKSLHSLVKIHEKLHYYEKQNPVPILQGAAALADDLAEELQNKPLNSEIRELLKLLSKPNVKALLSVHDTVAQKNYDPVLPPMPDDIDNEEDSVKIIRLVKNREPLGATIKKDEQTGAIVVARIMRGGAADRSGLIHVGDELREVNGIPVEDKRPEEIIQILAQSQGAITFKIIPSIKEETPSKEGKMFIKALFDYDPNEDKAIPCKEAGLSFKKGDILQIMSQDDATWWQAKHEGDANPRAGLIPSKHFQERRLALRRPEILVQPLKVSSRKSSGF... | Function: Acts as an important adapter that promotes epithelial cell polarity and tight junction formation via its interaction with DLG1. Involved in the assembly of protein complexes at sites of cell-cell contact (By similarity).
PTM: Phosphorylated by aPKC which promotes dissociation from the cell cortex.
Location To... |
Q5T2T1 | MPALSTGSGSDTGLYELLAALPAQLQPHVDSQEDLTFLWDMFGEKSLHSLVKIHEKLHYYEKQSPVPILHGAAALADDLAEELQNKPLNSEIRELLKLLSKPNVKALLSVHDTVAQKNYDPVLPPMPEDIDDEEDSVKIIRLVKNREPLGATIKKDEQTGAIIVARIMRGGAADRSGLIHVGDELREVNGIPVEDKRPEEIIQILAQSQGAITFKIIPGSKEETPSKEGKMFIKALFDYNPNEDKAIPCKEAGLSFKKGDILQIMSQDDATWWQAKHEADANPRAGLIPSKHFQERRLALRRPEILVQPLKVSNRKSSGF... | Function: Acts as an important adapter that promotes epithelial cell polarity and tight junction formation via its interaction with DLG1. Involved in the assembly of protein complexes at sites of cell-cell contact.
PTM: Phosphorylated by aPKC which promotes dissociation from the cell cortex.
Location Topology: Peripher... |
Q8BVD5 | MPALATGSACDMGLYELLAALPAQLQPHVDSQEDLTFLWDVFGEKSLHSLVKIHEKLHCYEKQNPLPILHGAAALADDLTEELQNKLPNSEIRELLKLLSKPNVKALLSVHDTVAQKSYDPVLPPVPDDIDDEEDSVKIIRLVKNSEPLGATIKKDEQTGAITVARIMRGGAADRSGLIHVGDELREVNGIPVEDKRPEEIIKILSQSKGAITFKIIPSTKEETPSKEGKIFIKALFDYDPKEDKAIPCKEAGLSFRKGDILQIMSQDDVTWWQAKHEGDANPRAGLIPSKHFQERRLALRRPEIVVQPLKLSNTKSSGF... | Function: Acts as an important adapter that promotes epithelial cell polarity and tight junction formation via its interaction with DLG1. Involved in the assembly of protein complexes at sites of cell-cell contact (By similarity).
PTM: Phosphorylated by aPKC which promotes dissociation from the cell cortex.
Location To... |
Q99549 | MEQVAEGARVTAVPVSAADSTEELAEVEEGVGVVGEDNDAAARGAEAFGDSEEDGEDVFEVEKILDMKTEGGKVLYKVRWKGYTSDDDTWEPEIHLEDCKEVLLEFRKKIAENKAKAVRKDIQRLSLNNDIFEANSDSDQQSETKEDTSPKKKKKKLRQREEKSPDDLKKKKAKAGKLKDKSKPDLESSLESLVFDLRTKKRISEAKEELKESKKPKKDEVKETKELKKVKKGEIRDLKTKTREDPKENRKTKKEKFVESQVESESSVLNDSPFPEDDSEGLHSDSREEKQNTKSARERAGQDMGLEHGFEKPLDSAMSA... | Function: Heterochromatin component that specifically recognizes and binds methylated 'Lys-9' of histone H3 (H3K9me) and promotes recruitment of proteins that mediate epigenetic repression . Mediates recruitment of the HUSH complex to H3K9me3 sites: the HUSH complex is recruited to genomic loci rich in H3K9me3 and is r... |
Q3TYA6 | MAAAAEEGMSAAALVMSVPDSIGRSPESEGVGAGDEEKDAATKGTVAVGDSEEDGEDVFEVERILDMKCEGGKNLYKVRWKGYTSEDDTWEPEVHLEDCKEVLLEFRKKLAENKAKAVRKDIQRLSLNNDIFEADSDSDQQSDTKEDISPRKKKKKIKCKEETSPEDLRKKRTKMGKLKDKFKTELESTSEIIGFDVKTKKRIWEVKEELKDSKKPKKDEIKETKELKKANKRAEVRDLKIKIREDVKENRKTKKERYIESPLESESPNDSLILEDDSEDFISDNREENQNVRSVRDKTAQETVQEGIFEKHLDDLISIE... | Function: Heterochromatin component that specifically recognizes and binds methylated 'Lys-9' of histone H3 (H3K9me) and promotes recruitment of proteins that mediate epigenetic repression. Mediates recruitment of the HUSH complex to H3K9me3 sites: the HUSH complex is recruited to genomic loci rich in H3K9me3 and is re... |
Q9ZU25 | MYRTAASRARALKGVLTRSLRPARYASSSAVAETSSSTPAYLSWLSGGSRAALTSLDMPLQGVSLPPPLADKVEPSKLQITTLPNGLKIASETTPNPAASIGLYVDCGSIYEAPYFHGATHLLERMAFKSTLNRTHFRLVREIEAIGGNTSASASREQMSYTIDALKTYVPEMVEVLIDSVRNPAFLDWEVNEELRKMKVEIAELAKNPMGFLLEAIHSAGYSGPLASPLYAPESALDRLNGELLEEFMTENFTAARMVLAASGVEHEELLKVAEPLTSDLPNVPPQLAPKSQYVGGDFRQHTGGEATHFAVAFEVPGWN... | Function: Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54402
Sequence Length: 503
Subcellular Location: Mitochondrion... |
O04308 | MYRTAASRAKALKGILNHNFRASRYASSSAVATSSSSSSWLSGGYSSSLPSMNIPLAGVSLPPPLSDHVEPSKLKTTTLPNGLTIATEMSPNPAASIGLYVDCGSIYETPQFRGATHLLERMAFKSTLNRSHFRLVREIEAIGGNTSASASREQMGYTIDALKTYVPEMVEVLIDSVRNPAFLDWEVNEELRKVKVEIGEFATNPMGFLLEAVHSAGYSGALANPLYAPESAITGLTGEVLENFVFENYTASRMVLAASGVDHEELLKVVEPLLSDLPNVPRPAEPKSQYVGGDFRQHTGGEATHFALAFEVPGWNNEKE... | Function: Substrate recognition and binding subunit of the essential mitochondrial processing protease (MPP), which cleaves the mitochondrial sequence off newly imported precursors proteins.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 54053
Sequence Length: 499
Subcellular Location: Plastid
|
Q8AVM3 | MWVLILLLAGMPPVLCIDISMHPDAFGVVGKSIKLKCSFTSSYPISDIVAVDWTYRQLNGGSTVTILHFQNKPYPILEGPFKDRIIWEGDVRRGDASISLTDLRLTDNGTLSCIVWNPPDVHGNVPQTKLTVTIENLFFQFNTVILLSALVFIPSALVSLLLLIRMRRSINRGRTKNLKWRKKSPIEESQDCVYDDNENTPLHPTLPQEQSPGCFMKFCLRCLDDSDED | Function: Mediates homophilic cell-cell adhesion.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 25865
Sequence Length: 229
Subcellular Location: Membrane
|
O39519 | MERILYQVFPSDTNYSYDPPAVTAPSQGSSQTDFGKVVIALVVILVSVGVFYLAYTLFLKDCILLFKAKKQRTTTEIGFGQTPARNQDHPGP | Function: Involved in the viral transport within, and between cells.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 10172
Sequence Length: 92
Subcellular Location: Host membrane
|
Q67593 | MDPYGSRPSHPDDGALHGILVAFIAVLCLIGCLWAAYRLFLKECLTDCSQHTSSGVVAGPRPAATGPTAVVVHNGAEAQRSSAF | Function: Involved in the viral transport within, and between cells.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 8751
Sequence Length: 84
Subcellular Location: Host membrane
|
P0C648 | MDPQNALYYQPRVPTAAPTSGGVPWSRVGEVAILSFVALICFYLLYLWVLRDLILVLKARQGRSTEELIFGGQAVDRSNPIPNIPAPPSQGNPGPFVPGTG | Function: Involved in the viral transport within, and between cells.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 10906
Sequence Length: 101
Subcellular Location: Host membrane
|
P10838 | MAVHVENLSDLAKTNDGVAVSLNRYTDWKCRSGVSEAPLIPASMMSKITDYAKTTAKGNSVALNYTHVVLSLAPTIGVAIPGHVTVELINPNVEGPFQVMSGQTLSWSPGAGKPCLMIFSVHHQLNSDHEPFRVRITNTGIPTKKSYARCHAYWGFDVGTRHRYYKSEPARLIELEVGYQRTLLSSIKAVEAYVQFTFDTSRMEKNPQLCTKSNVNIIPPKAETGSIRGIAPPLSVVPNQGRESKVLKQKGGTGSKTTKLPSLEPSSGSSSGLSMSRRSHRNVLNSSIPIKRNQDGNWLGDHLSDKGRVTDPNPERL | Function: Plays an essential role in cell-to-cell movement and long-distance transport of the viral genome. Mechanistically, movement protein is recruited by viral replicase complexes formed on RNA1 to punctate structures on the host cortical endoplasmic reticulum. In turn, interacts with the viral genome and mediates ... |
Q2SF51 | MTVKKADVLLVGGGVMSTTLGTMLMQLDPSLNIVMVERLDHVAHESTYGWNNAGTGHAGYCELNYTPETGDGDIEITRALAINASFEVSLQFWSYLVERGGLPSPDEFINTCPHESFVWGESDIAFLRKRHQLLSAHHLFKDMEFSDDPRTLQDWMPLVMEHRDPMQKVAATRVRYGSDVDFGSLTRNMVEHLQKNANFELLLSHPVKSLKQTSDGRWNVQLSDSRNGGSKTIDAGFVFLGAGGGALPLLQKSGIAEGDGYGGFPVSGQWLVCKKPDIVKRHYAKVYGKAAIGAPPMSVPHLDTRIINGEPALLFGPYAG... | Catalytic Activity: (S)-malate + a quinone = a quinol + oxaloacetate
Sequence Mass (Da): 54587
Sequence Length: 497
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; oxaloacetate from (S)-malate (quinone route): step 1/1.
EC: 1.1.5.4
|
Q9Z9Q7 | MSSIQNKTDVILIGAGIMSATLGSLLKELKPEWEIKVFEKLANAGEESSNEWNNAGTGHAALCELNYTAEKSDGTIDISKAVKINEQFQISRQFWAYLVSQNLISNPQDFIMPIPHMSLVQGEDNVAYLKKRFKALSNIPLFEGMEFSNDPEKLKEWIPLVMEGRTSNEPIAATKIDSGTDVNFGALTRMLFEHLKEQNVEVHYKHSVKDIKRTSDGSWSVKVQEIESGTIEYHTANFVFIGGGGGSLPLLQKTGIPESKNIGGFPVSGLFMVCNNPEVVEQHHAKVYGKAKVGAPPMSVPHLDTRYIDNKKSLLFGPFA... | Catalytic Activity: (S)-malate + a quinone = a quinol + oxaloacetate
Sequence Mass (Da): 55081
Sequence Length: 500
Pathway: Carbohydrate metabolism; tricarboxylic acid cycle; oxaloacetate from (S)-malate (quinone route): step 1/1.
EC: 1.1.5.4
|
O24913 | MSMEFDAVIIGGGVSGCATFYTLSEYSSLKRVAIVEKCSKLAQISSSAKANSQTIHDGSIETNYTPEKAKKVRLSAYKTRQYALNKGLQNEVIFETQKMAIGVGDEECEFMKKRYESFKEIFVGLEEFDKQKIKELEPNVILGANGIDRHENIIGHGYRKDWSTMNFAKLSENFVEEALKLKPNNQVFLNFKVKKIEKRNDTYAVISEDAEEVYAKFVLVNAGSYALPLAQSMGYGLDLGCLPVAGSFYFVPDLLRGKVYTVQNPKLPFAAVHGDPDAVIKGKTRIGPTALTMPKLERNKCWLKGISLELLKMDLNKDVF... | Cofactor: The FAD is tightly bound.
Function: Catalyzes oxidation of malate to oxaloacetate in the citric acid cycle. Donates electrons to quinones of the electron transfer chain.
Catalytic Activity: (S)-malate + a quinone = a quinol + oxaloacetate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 5071... |
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