ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A1A652 | MSATGNKVFAPAIFFIAAREALEASLVIGILSGMLENLVVHTKSAEDLAAHDSLTESEKHEVEQKKRALVRKLRKIVLLGALTGLLIAFAIGAAFLAVFYTQVNDLYGKAEELWEGIFNLVAVLLITPMSLAILRAGNSKRKWKRKLENAFSHQNIQPNHRRDEEGEATVVNANHSDDSASASSSSARQAAEEEAGTKTTRTEKLNPLEAVDVVPSMSGDQRRKRGGLRGLFSKPSGAVNDLKLRMNRGTLALFTIPLITTLREGLEGVVFIGGVSLGLPATSIPLPAIVGLAVGLGIGFLIFRSGNLVSVRIFLVFSTC... | Function: Permease for high affinity iron uptake .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53084
Sequence Length: 486
Subcellular Location: Cell membrane
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Q9ZQG8 | MATVRISSTSMTKAVLRSQTTNKLITNKSYNLSVGSTKRVSRSFGLKCSANSGGATMSAVYKVKLLGPDGQEDEFEVQDDQYILDAAEEAGVDLPYSCRAGACSTCAGQIVSGNVDQSDGSFLEDSHLEKGYVLTCVAYPQSDCVIHTHKETELF | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Sequence Mass (Da): 16634
Sequence Length: 155
Subcellular Location: Plastid
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P27788 | MSTSTFATSCTLLGNVRTTQASQTAVKSPSSLSFFSQVTKVPSLKTSKKLDVSAMAVYKVKLVGPEGEEHEFDAPDDAYILDAAETAGVELPYSCRAGACSTCAGKIESGSVDQSDGSFLDDGQQEEGYVLTCVSYPKSDCVIHTHKEGDLY | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Sequence Mass (Da): 16123
Sequence Length: 152
Subcellular Location: Plastid
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P14938 | ATYKVKFITPEGEQEVECDDDVYVLDAAEEAGIDLPYSCRAGSCSSCAGKVVSGSVDQSDQSFLDDDQIAEGFVLTCAAYPTSDVTIETHREEDMV | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Sequence Mass (Da): 10338
Sequence Length: 96
Subcellular Location: Plastid
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P49522 | MATYKVTLLSEEHDIDATIDCNDDVFLLDAAEEQGIELPYSCRAGACSTCAGKVTEGDIDQSEQTFLDDDQVGAGFVLTCIAYPKSDCTVLVHQEDELY | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Sequence Mass (Da): 10789
Sequence Length: 99
Subcellular Location: Plastid
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P21149 | MLSQVCRFGTITAVKGGVKKQLKFEDDQTLFTVLTEAGLMSADDTCQGNKACGKCICKHVSGKVAAEDDEKEFLEDQPANARLACAITLSGENDGAVFEL | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions. It links pyruvate:ferredoxin oxidoreductase to hydrogenase.
Sequence Mass (Da): 10675
Sequence Length: 100
Subcellular Location: Hydrogenosome
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Q84VG7 | MSDSDMDIDDDEVEQKVQVHTIVRESELFDKPPIQASNSHNDVKRHSVTTPLDEQSKIIKEQAFAQDNGTLPRFPAPGIPPRSFFTGGGGNEPEQKRAALPCKFFAKGWCFNGVSCKFLHVKENSNCTSQQLAENSMAGNGGIRSDLERRILDSREGVRVSQLSENGVTSLPTREDISFMNPQRVFSSMSFVNPPGSQRVFPFNNEMRFMPSFENIRRESLKQTYGADFTDNRSLVINNANSFALRSSFVHEHRPSISSYLKTDMGSAGPAWTGSLSSSVPMNDRASTVGDFENGNSLSGSGSLPTLQGVAVSSDKGAEA... | Function: Transcriptional activator involved in the FRIGIDA-mediated vernalization pathway, but not in the autonomous flowering pathway. Acts cooperatively with FRI (FRIGIDA) or FRL1 (FRIGIDA-LIKE 1) to promote FLC (FLOWERING LOCUS C) expression. Required for the stabilization of the FRI-C complex.
Sequence Mass (Da): ... |
P70377 | MAAAIASSLIRQKRQAREREKSNACKCVSSPSKGKTSCDKNKLNVFSRVKLFGSKKRRRRRPEPQLKGIVTKLYSRQGYHLQLQADGTIDGTKDEDSTYTLFNLIPVGLRVVAIQGVQTKLYLAMNSEGYLYTSEHFTPECKFKESVFENYYVTYSSMIYRQQQSGRGWYLGLNKEGEIMKGNHVKKNKPAAHFLPKPLKVAMYKEPSLHDLTEFSRSGSGTPTKSRSVSGVLNGGKSMSHNEST | Function: Microtubule-binding protein which directly binds tubulin and is involved in both polymerization and stabilization of microtubules . Through its action on microtubules, may participate to the refinement of axons by negatively regulating axonal and leading processes branching . Plays a crucial role in neuron po... |
Q5AP52 | MKISNLIPAYLLPFSLFCQVLGAPTNGKRGNVVVVKVKTTVQQTQTDIQTISEATGTTTNYLINTSTETFTRYTATVTSTVYGVPHTYTTVATTPVSAADVIPNSENEVKSSPTESPVEQETSTSSTSVATTTTPVAKNPVSSQETSTPTPVPPETTSTSSSLLSSSQQTTTLAQVSETAINDTTESSGPTITGSVSSQTTDSWIIENISTVTSDGTCFVNYDYYYATETDDAEETTTLTSTITTTVTLN | Function: Putative adhesin which may be involved in cell adhesion and virulence (By similarity). Involved in the regulation of filamentous growth.
Location Topology: Lipid-anchor
Sequence Mass (Da): 26401
Sequence Length: 250
Subcellular Location: Secreted
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Q91V87 | MTRSPALLLLLLGALPSAEAARGPPRMADKVVPRQVARLGRTVRLQCPVEGDPPPLTMWTKDGRTIHSGWSRFRVLPQGLKVKEVEAEDAGVYVCKATNGFGSLSVNYTLIIMDDISPGKESPGPGGSSGGQEDPASQQWARPRFTQPSKMRRRVIARPVGSSVRLKCVASGHPRPDIMWMKDDQTLTHLEASEHRKKKWTLSLKNLKPEDSGKYTCRVSNKAGAINATYKVDVIQRTRSKPVLTGTHPVNTTVDFGGTTSFQCKVRSDVKPVIQWLKRVEYGSEGRHNSTIDVGGQKFVVLPTGDVWSRPDGSYLNKLL... | Function: Has a negative effect on cell proliferation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57013
Sequence Length: 529
Subcellular Location: Cell membrane
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P09769 | MGCVFCKKLEPVATAKEDAGLEGDFRSYGAADHYGPDPTKARPASSFAHIPNYSNFSSQAINPGFLDSGTIRGVSGIGVTLFIALYDYEARTEDDLTFTKGEKFHILNNTEGDWWEARSLSSGKTGCIPSNYVAPVDSIQAEEWYFGKIGRKDAERQLLSPGNPQGAFLIRESETTKGAYSLSIRDWDQTRGDHVKHYKIRKLDMGGYYITTRVQFNSVQELVQHYMEVNDGLCNLLIAPCTIMKPQTLGLAKDAWEISRSSITLERRLGTGCFGDVWLGTWNGSTKVAVKTLKPGTMSPKAFLEEAQVMKLLRHDKLVQ... | Function: Non-receptor tyrosine-protein kinase that transmits signals from cell surface receptors devoid of kinase activity and contributes to the regulation of immune responses, including neutrophil, monocyte, macrophage and mast cell functions, cytoskeleton remodeling in response to extracellular stimuli, phagocytosi... |
I1RC73 | MPPRRSHKKSRAGCRRCKNRKIKCDEVHPRCGNCAKHGVPCDFSNPDVLEELAISTNTSTESVGAPTPSPAPTVNFNSAPRTPLTRPRAPSSPARAPRPNPSPPTSVYSQPSISSSTNTIDHGERMLELRLMHHYTNVTSKTLLTNSPAAEDIWQRAVPQMAFSGNGKTYLADAILSVAALHLRSMSPNDKALVRASHAYSASSLSAFGASLGAGITPENAEALFLTATLIAFQASASRIFVKDDGDAAPGDPTVRYVPPLSWFHAFQGVKTVVANSWQWIHHSDIVKVIIDSQPSFQLNLNPRSPDSFFGHMLEGLADE... | Function: Transcription factor that targets gene promoters containing 2 conserved CGAA repeat sequences . Positively regulates the expression of ergosterol biosynthesis genes including CYP51A and CYP51B encoding the sterol 14-alpha demethylase, and ERG6A and ERG6B encoding the sterol 24-C-methyltransferase .
PTM: Phosp... |
O44827 | MSEKSRSDTSATASLSDSSKSPSSYSTPGTTTQKIIFPDGKLTKCLAFSAFVITLASFQFGYHIGCVNAPGGLITEWIIGSHKDLFDKELSRENADLAWSVAVSVFAVGGMIGGLSSGWLADKVGRRGALFYNNLLALAAAALMGLAKSVGAYPMVILGRLIIGLNCGFSSALVPMFLTEISPNNLRGMLGSLHQLLVTIAILVSQIFGLPHLLGTGDRWPLIFAFTVVPAVLQLALLMLCPESPKYTMAVRGQRNEAESALKKLRDTEDVSTEIEAMQEEATAAGVQEKPKMGDMFKGALLWPMSIAIMMMLAQQLSGI... | Function: Facilitative glucose transporter that plays a role in glucose metabolism and regulation of longevity. May also play a role in lipid metabolism. Glucose transport activity of isoform a is competitively inhibited by mannose, galactose and fructose, suggesting ability to transport also other hexose sugars.
Locat... |
O44616 | MNAVVASQNKNDRSFSNMESESSSNVEKSEKENHHQSLPDENWTPFLFFCISSIALASFQDGFQIGCINAPGPLIIDWIKKCHFELFGEVLSQYQADFIWSVAVSMFSVGGMFGSFCSGFLADKFGRKSTLLYNNILALLAAVCLSTSKLFNFYPMIVFGRFLVGLNCGITSGLVPMFLTELAPANLRGKCGSFHQLNISVAIVLSQALGLPQIFGTQVGWPYIFACVAIPTFLQLATIPFCVESPKYLISKLNDREEARRILEKLRGHTKVDEELEHMVQETMVTVEPLHQPGYVSLFKGDNQWPMIVSILMMFSQQFS... | Function: Appears to have no transport activity for glucose.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57609
Sequence Length: 516
Subcellular Location: Cell membrane
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Q9SRR2 | MDGLCYVIFIIFSLLSCAFSPLSYASPATFSRRHLLQAPVTDPSTFSPPFFPLYSSTSPPPPPSPPQPLPPPAPTFATFPANISALVLPRSPKPQTPSRTLLIPAISAVLAAATLIALAFFFYGRWRGQTSHFKDESKSLASDISQSQQQTLPCPPPRNNNTQNKLSVAPSTSDVLYLGNVVTSSGSGFVKPESPDISPLPPLPARSFLLQHHSEANLDEEEEDDDFYSPLASIAGQESRDRRINPYSNCSCSISSHSDSPAMSPSAAMSPPMNSTAPHWSTNQNTHSPSSPERTVRNNKRYGGQSLRMFSLWNQNLGFP... | Function: Might be involved in the organization and polarity of the actin cytoskeleton.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 93012
Sequence Length: 841
Subcellular Location: Membrane
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Q9MA60 | MVYFRQIFLMIIVVSLHCCKVRFFCIVANAKELDDWKVLTVENGERYRTHVGRYAGEEGGEKIKLRVLEKFRALLDLIKPSTSRRRNLAESASFSPWPAPSPSPFPNGGPIESPAYPPAPPRPIPPHLRRPLPQRTHPLEQPEIQRRKHEKGGTFKKILVPVVASTASAIGFVVCVVGVFCLCARRKRKMNGKTLSFKRKKGKSQSSTRKVSVNPTLDFLYLNSLGVDLERQNSVSVKEIRETEKDLNGINGGLLEEEVKRSIETEISHDWDNASSYSTKEIVSVHENDEEQTVNSVSVPVVVINDSSDDDESFHSVGGG... | Function: Might be involved in the organization and polarity of the actin cytoskeleton.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 98535
Sequence Length: 884
Subcellular Location: Membrane
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P02671 | MFSMRIVCLVLSVVGTAWTADSGEGDFLAEGGGVRGPRVVERHQSACKDSDWPFCSDEDWNYKCPSGCRMKGLIDEVNQDFTNRINKLKNSLFEYQKNNKDSHSLTTNIMEILRGDFSSANNRDNTYNRVSEDLRSRIEVLKRKVIEKVQHIQLLQKNVRAQLVDMKRLEVDIDIKIRSCRGSCSRALAREVDLKDYEDQQKQLEQVIAKDLLPSRDRQHLPLIKMKPVPDLVPGNFKSQLQKVPPEWKALTDMPQMRMELERPGGNEITRGGSTSYGTGSETESPRNPSSAGSWNSGSSGPGSTGNRNPGSSGTGGTAT... | Function: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of ... |
Q7M3I9 | TKDEGTFIAEGGGVR | Function: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of ... |
P14462 | ADGSDPAGGEFLEAGGGVR | Function: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen beta (FGB) and fibrinogen gamma (FGG), polymerize to form an insoluble fibrin matrix. Fibrin has a major function in hemostasis as one of the primary components of blood clots. In addition, functions during the early stages of ... |
Q6CZ45 | MNPHYARLVTLAAVSATAVALVLFVMKVFAWWHTGSVSLLASLVDSLVDIAASLVNLLVVRYSLQPADTEHAFGHGKAESLAALAQSMFISGSALFLILTGLQHSLEPQTLHAPEVGMWVTLIALVATLLLVSFQRWVVKHTHSQAVRADMLHYQSDLLMNGAILVALALSWKGITRADSLFALGIGVYILYSALRMGYDAVQSLLDRALPDEEHRAIAEVIVNWPGIRGAHALRTRRSGPTRFIQLHLEMDDALPLAEAHQIADDLEQALRKQFPGADIIIHQDPVSAVPENQRGRLTA | Function: Divalent metal cation transporter which exports Zn(2+), Cd(2+) and possibly Fe(2+). May be involved in zinc and iron detoxification by efflux.
Catalytic Activity: H(+)(out) + Zn(2+)(in) = H(+)(in) + Zn(2+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32762
Sequence Length: 300
Subce... |
P30130 | MSYLNLRLYQRNTQCLHIRKHRLAGFFVRLVVACAFAAQAPLSSADLYFNPRFLADDPQAVADLSRFENGQELPPGTYRVDIYLNNGYMATRDVTFNTGDSEQGIVPCLTRAQLASMGLNTASVAGMNLLADDACVPLTTMVQDATAHLDVGQQRLNLTIPQAFMSNRARGYIPPELWDPGINAGLLNYNFSGNSVQNRIGGNSHYAYLNLQSGLNIGAWRLRDNTTWSYNSSDRSSGSKNKWQHINTWLERDIIPLRSRLTLGDGYTQGDIFDGINFRGAQLASDDNMLPDSQRGFAPVIHGIARGTAQVTIKQNGYDI... | Function: Involved in the export and assembly of FimA fimbrial subunits across the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 96482
Sequence Length: 878
Subcellular Location: Cell outer membrane
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Q9FJL3 | MEDDFDTQNQFPEEEPEEMDMDLPDNDEADSAPYLKIGEEMEIGKSGLKKKLVKECEKWDTPENGDEVEVHYTGTLLDGTKFDSSRDRGTPFKFTLGQGHVIKGWDLGIKTMKKGENAIFTIPPELAYGETGSPPTIPPNATLQFDVELIAWRSVKDICGDGGVSKKIIVEGEKWEKPKDLDEVYVKYEARLEDGTIVGKSDGVEFTVKEGHFCPALSKAVKTMKRGEKVLLTVKPQYGFGEFGRPASDGLQAAIPPNATLQIDLELVSWKTVVEVTDDRKVIKKILKEGEGYERPNEGAIVKLKLIGKLQDGTTVFVKK... | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Co-chaperone that negatively modulates thermotolerance by interacting with FKBP62 and decreasing the HSFA2-mediated accumulation of chaperones of the small-HSPs family. Plays ... |
P81104 | XGESWETPETGDEVE | Function: PPIases accelerate the folding of proteins during protein synthesis.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 1676
Sequence Length: 15
EC: 5.2.1.8
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Q43207 | MDDDFDIPAGDDMMMGDGMGDFGGAEGPGMKVGEENEIGKQGLKKKLLKEGEGWDTPEVGDEVEVHYTGTLLDGKKFDSSRDRDDTFKFKLGQGQVIKGWDQGIKTMKKGENALFTIPPELAYGESGSPPTIPANATLQFDVELLSWTSVRDIAKDGGIFKKILKEGDKWENPKDPDEVFVKYEARLEDGTVVSKSEGVEFTVKDGHLCPALAKAVKTMKKGEKVLLAVKPQYGFGEMGRPAAGEGGAVPPNASLVIDLELVSWKTVTEIGDDKKILKKVLKEXEGYERPNEGAVVTVKITGKLQDGTVFLKKGHDEQEP... | Function: PPIases accelerate the folding of proteins during protein synthesis.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 62058
Sequence Length: 559
EC: 5.2.1.8
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O08437 | MNNFLKVSLLAAAVAVSLTACQKDEKTAANTAEVKAEASKPAEAPKAEAKSFEEQSGYAIGLSMGRYIANTLERQQELGIKLDNSVILKGVTDGLGKEAKMTDEEIQKVLQQYDAKINELTKAKADKDAVENQKKGEEYLAANAKKEGVKSTESGLQYQVEKMGTGAKPKATDIVKVHYTGTLTDGTKFDSSVDRGEPATFPLNQVIPGWTEGVQLMPVGSKFKFFLPSKLAYGEHGAGSIPANAVLVFDVELLAIEKPAADGDNAKK | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. FkpA probably acts in the folding of extracytoplasmic proteins.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (... |
P57599 | MILYVPKSFSISAPISDIHLQSVLETKNTFHNNNEKLGYILGLSFGNYVNQTFEKQKKIGIELDRNSLLKGIQDAISGNLKLSHQDISSGLKELEKKLKHATKIQLKKNAKENFIQGELYMKNFSKLKGVKKTSSGLLYLLERAGEGEALKDETKITVHYKGTLINGLEFDNSYKRGRPVSLRLKDVILGWKEGLKYIKKGGKIKLVIPPNLAYGTEEVNGIPANSTLIFDIELLDVVNGV | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 26946
Sequence Length: 241
EC: 5.2.1.8
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P45523 | MKSLFKVTLLATTMAVALHAPITFAAEAAKPATAADSKAAFKNDDQKSAYALGASLGRYMENSLKEQEKLGIKLDKDQLIAGVQDAFADKSKLSDQEIEQTLQAFEARVKSSAQAKMEKDAADNEAKGKEYREKFAKEKGVKTSSTGLVYQVVEAGKGEAPKDSDTVVVNYKGTLIDGKEFDNSYTRGEPLSFRLDGVIPGWTEGLKNIKKGGKIKLVIPPELAYGKAGVPGIPPNSTLVFDVELLDVKPAPKADAKPEADAKAADSAKK | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 28882
Sequence Length: 270
Subcellular Location: Periplasm
... |
Q9JYI8 | MNTIFKISALTLSAALALSACGKKEAAPASASEPAAASSAQGDTSSIGSTMQQASYAMGVDIGRSLKQMKEQGAEIDLKVFTEAMQAVYDGKEIKMTEEQAQEVMMKFLQEQQAKAVEKHKADAKANKEKGEAFLKENAAKDGVKTTASGLQYKITKQGEGKQPTKDDIVTVEYEGRLIDGTVFDSSKANGGPVTFPLSQVIPGWTEGVQLLKEGGEATFYIPSNLAYREQGAGDKIGPNATLVFDVKLVKIGAPENAPAKQPAQVDIKKVN | Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Location Topology: Lipid-anchor
Sequence Mass (Da): 28894
Sequence Length: 272
Subcellular Location: Cell membrane
EC: 5.2.1.8
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P0A9L3 | MTTPTFDTIEAQASYGIGLQVGQQLSESGLEGLLPEALVAGIADALEGKHPAVPVDVVHRALREIHERADAVRRQRFQAMAAEGVKYLEENAKKEGVNSTESGLQFRVINQGEGAIPARTDRVRVHYTGKLIDGTVFDSSVARGEPAEFPVNGVIPGWIEALTLMPVGSKWELTIPQELAYGERGAGASIPPFSTLVFEVELLEIL | Function: PPIases accelerate the folding of proteins (Probable). Catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides . Displays a preference for substrates with a lysyl residue in the P1 position .
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (... |
P74838 | MSDVVETLRLPNGATVAHVNAGEAQFLYREIFTDRCYLRHGVELRPGDVVFDVGANIGMFMLFAHLEHPGVTVHAFEPAPVPFAALRANAVRHRVAGRVDQCAVSDEAGVRRMTFYPDATLMSGFHPDAAARKELLRTLGLNGGYTAEDVDMMLAQLPDTGEEIETSVVRLSDVIAERGIAAIGLLKIDVEKSERRVLAGVEDADWPRIRQVVAEVHDVDGALGEVVALLRGHGFTVVAEQDPLFAGTEIHQVAARRTAG | Function: Involved in the biosynthesis of FK506, which is a macrolide antibiotic with immunosuppressant activity. Catalyzes the transfer of a methyl group from S-adenosyl-L-methionine to the 31-O-position of 31-O-demethyl-FK506. Also catalyzes the methylation of 31-O-demethylimmunomycin, the C31 transmethylation reacti... |
Q9KID9 | MTDAGRQGRVEALSISVTAPYCRFEKTGSPDLEGDETVLGLIEHGTGHTDVSLVDGAPRTAVHTTTRDDEAFTEVWHAQRPVESGMDNGIAWARTDAYLFGVVRTGESGRYADATAALYTNVFQLTRSLGYPLLARTWNYVSGINTTNADGLEVYRDFCVGRAQALDEGGIDPATMPAATGIGAHGGGITCVFLAARGGVRINIENPAVLTAHHYPTTYGPRPPVFARATWLGPPEGGRLFISATAGILGHRTVHHGDVTGQCEVALDNMARVIGAENLRRHGVQRGHVLADVDHLKVYVRRREDLDTVRRVCAARLSST... | Function: Involved in the biosynthesis of the macrocyclic amino acid-linked polyketides FK506 and FK520 which are potent immunosuppressants that prevent T-cell proliferation through initial binding to the immunophilin FKBP12. Catalyzes the hydrolysis of chorismate via a 1,4-conjugate elimination of water to yield (4R,5... |
Q554J3 | MGVEITIIKEGKGNIPPVGSNVTVHHAGTLTNGTVFDSSRKRGQPFNFKLGAGQVIKGWDEGVAKMKVGETSKLTISPDFGYGARGAGGVIPPNATLVFEVELITFK | Function: PPIases accelerate the folding of proteins by catalyzing the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 11242
Sequence Length: 107
EC: 5.2.1.8
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Q4WHX4 | MRILLLSALFLSLTTLVLSADLGIEKTHVVECNRKTTKGDTVHMHYRGTLAADGSEFDSSYGRNQPLKFKLGAGRVIKGWDEGLLDMCVGEKRTLTIPPEYGYGERGIGPIPGGATLIFETELVQIEGVNNDEL | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 14638
Sequence Length: 134
Subcellular Loca... |
Q2UPT7 | MRFSIFSTLLVSLATLSTAAELGIEKTHEVECTRKTVKGDTVQMHYKGTLQSDGSEFDSSYKRNSPLKFKVGSGMVIKGWDEGLLDMCIGEKRTLTIPPEYGYGSRGVGPIPGGATLIFETELVGIDGVSKDEL | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 14524
Sequence Length: 134
Subcellular Loca... |
O17798 | MSNISWYRHCSVRLQLVTLALFLLLGSASLGSAHIDEEFEDDVTTTISSIASPMRRTYTNEWAVRIAGGKVEEANRLANKYGYTNLGPIIPGDEYYLFRDDRKKSRSSRKTRSLSANQLQHEEDVMWMEQQVAKRRVKRGYRRIRRHTDDNDIFEEDDDGTQISKSRNRKHPDPNDPLWTDMWYLNRGEHHSDSTTRMDHNVKEAWDLGYTGKGVVVTILDDGLERTHPDISPNYDERASYDVNDRDNDPMPRYEFSDENRHGTRCAGEVAAIFNNSLCIVGIAYNANIGGIRMLDGDVTDAVEAASVGHNADYIDIYSA... | Cofactor: Binds 3 calcium ions per subunit.
Function: Furin-like protease which cleaves proproteins at the RX(K/R)R consensus motif . During neuronal development, regulates the formation and extension of dendrite branches and cellular positioning of various type of neurons . Together with chin-1 and cdc-42, plays a rol... |
Q9H9S5 | MRLTRCQAALAAAITLNLLVLFYVSWLQHQPRNSRARGPRRASAAGPRVTVLVREFEAFDNAVPELVDSFLQQDPAQPVVVAADTLPYPPLALPRIPNVRLALLQPALDRPAAASRPETYVATEFVALVPDGARAEAPGLLERMVEALRAGSARLVAAPVATANPARCLALNVSLREWTARYGAAPAAPRCDALDGDAVVLLRARDLFNLSAPLARPVGTSLFLQTALRGWAVQLLDLTFAAARQPPLATAHARWKAEREGRARRAALLRALGIRLVSWEGGRLEWFGCNKETTRCFGTVVGDTPAYLYEERWTPPCCLR... | Function: Catalyzes the transfer of a ribitol 5-phosphate from CDP-L-ribitol to the ribitol 5-phosphate previously attached by FKTN/fukutin to the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglyc... |
O75072 | MSRINKNVVLALLTLTSSAFLLFQLYYYKHYLSTKNGAGLSKSKGSRIGFDSTQWRAVKKFIMLTSNQNVPVFLIDPLILELINKNFEQVKNTSHGSTSQCKFFCVPRDFTAFALQYHLWKNEEGWFRIAENMGFQCLKIESKDPRLDGIDSLSGTEIPLHYICKLATHAIHLVVFHERSGNYLWHGHLRLKEHIDRKFVPFRKLQFGRYPGAFDRPELQQVTVDGLEVLIPKDPMHFVEEVPHSRFIECRYKEARAFFQQYLDDNTVEAVAFRKSAKELLQLAAKTLNKLGVPFWLSSGTCLGWYRQCNIIPYSKDVDL... | Function: Catalyzes the transfer of a ribitol-phosphate from CDP-ribitol to the distal N-acetylgalactosamine of the phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-3-N-acetylglucosamine-beta-4-(phosphate-6-)mannose), a carbohydrate structure present in alpha-dystroglycan (DAG1) . This constitutes th... |
Q2IQP0 | MSPLTRIALALAASAALVLALTACGPAHVAGYVPKRRDYAVPDASGQDTQAASAGSTWREGRAASMLYTDARALRENDLVVVRIEEIADAKRSADTDLTRRSELNASIEAFLTSLSTPYALKGGADSGFKGLGSTARTERLTATVPAVVRKVLPNGNLFIEGHRVVLVNAEEQHFYISGVVRPIDIDQENGVKSSMVADAEIEFTGRGVLSDNQRQGWLSRLLGWFWPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24659
Sequence Length: 229
Subcellular Location: Cell outer membrane
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O67609 | MLYLFFALIFIISCSTKVESKKKYTYSFPKTYKEEKPTRGSLFKSPQSAYLYGSVRASEVGDVIYIRVIESINAIESVSTNVGRSTSFSNAISSFFGVHPATLKNLGAGGKSSFASKGGSKFQQSGVLTTTLAGRVVKVFPNGTMLVEAKKYIEVNGVKREFLLRGIVRPEDIDSNNTVTSDKIADMEIFFEGRGYIVRGGEPGWLAKIFAILFPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23767
Sequence Length: 216
Subcellular Location: Cell outer membrane
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A8IPJ4 | MKPVILATASALLLAACQTNSYDSLAYGPTLTPVGQGLEAGRMPVPQPFQQAKERTFRSAYNLNSQSMYRALRAAAVGDVIRITIDIDDKAQLDNNTNRSRKSASDVGFASALNLSGFQSGSTSGSASGNLGLTGDTSTDGKGKIDRSEKLRLSLAAVVTEVMPNGNLVINGSQEILVNYEVRVLTLGGIVNPLDVTSNNTVAYDKVAEARISYAGRGRLNDVQQPAWGQRLFDAVNPM | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 25383
Sequence Length: 239
Subcellular Location: Cell outer membrane
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A1K945 | MKALALLAVLLLSGCASIYSTPPTAIHQPMSARPDMRAQAVPATGSIYQPSQARPLFEDRRARNVGDIITINLVERNTAQKSANASATRGSAITGGISLTAPNIASLANAKLNGLQADVGLDSDFSGEGAAAANNVFNGTISVTVIDVYPNGNLLVSGEKMVAINQGNEFIRFSGVINPTTVTAANTVQSTQVADARIEYRGSGFIDESNTMGWLQRFFVAIAPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 23588
Sequence Length: 225
Subcellular Location: Cell outer membrane
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Q7WJD2 | MMLKTVLRLPVCAALLALAAGCAMIPPEPVVTGPLTAPPPPPPQPSARPNGSIYQPSAYGNYPLFEDRRPRNVGDIVTIVLEEKTNAAKGVATNTSRDGSATLGVAAAPRFMDGIINDKLDTDISGGNTANGTGKSSANNTFTGTITTTVIGVLPNGNLQIAGEKQIAINRGSEYVRFSGVVDPRSITGSNTVSSTRVADARIEYRSKGVMDEVQTMGWLQRFFLIASPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 24206
Sequence Length: 230
Subcellular Location: Cell outer membrane
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Q2YJ67 | MNKAILAVAMVLLLAGCATKPEEIGRAPDLSPVAAHLGMQNNPQFNGYPARPGKASYSLWDQRSTNFFKDPRAATPGDVLTVIISINDRANLDNKTDRERVSKGIYGGGGSFATSSITGAAAGGDMDASVNTHSDSKSKGKGTIERSEDIRLQIAAIVTDTLPNGNLIIRGSQEVRVNNELRVLNVAGVVRPRDISGNNTISYDKIAEARISYGGRGRLSEIQQPPYGQQILDQFSPF | Function: Assembles around the rod to form the L-ring and probably protects the motor/basal body from shearing forces during rotation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 25471
Sequence Length: 238
Subcellular Location: Cell outer membrane
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P26477 | MSIDRTSPLKPVSTVQTRETSDTPVQKTRQEKTSAATSASVTLSDAQAKLMQPGVSDINMERVEALKTAIRNGELKMDTGKIADSLIREAQSYLQSK | Function: Responsible for the coupling of flagellin expression to flagellar assembly by preventing expression of the flagellin genes when a component of the middle class of proteins is defective. It negatively regulates flagellar genes by inhibiting the activity of FliA by directly binding to FliA.
Sequence Mass (Da): ... |
O25026 | MKKSKHLKRPYLKRSHLKHSDKASSFKGLLKKEDNVISLENFKPKESEDLLENFSNKKDMQELLGLLNQFILQSYKVEKEFKDYKALYEWVIEILPQAIWVVNENGSFFYKNSLANQSHEVFNKAKLENFNTEIEHENKSYLVQQNSIQGKQIITATDISAQKRQERLASMGKISAHLAHEIRNPVGSISLLASVLLKHANEKTKPIVVELQKALWRVERIIKATLLFSKGIQANRTKQSLKTLESDLKEALNCYTYSKDIDFLFNFSDEEGFFDFDLMGIVLQNFLYNAIDAIEALEESEQGQVKIEAFIQNEFIVFTI... | Function: Member of the two-component regulatory system FlgR/FlgS that induces the transcriptional induction of the genes needed in motility and flagellar biogenesis . Also plays an essential role in bacterial survival at pH 2.5 independently of FlgR . Functions as a sensor protein kinase which is autophosphorylated at... |
O67265 | MRGKEFWIILAVVLILSAIIIPIPALLLDLLLTLSITFSLTVLLLTFFIKNPLEFSSFPSVLLLGTLLRLSLNIAAARRILLHGHEGTHAAGKVIEAFGKLVAGGDVVVGLIVFLIFIVINFIVITKGAERISEVAARFTLDALPGKQMSIDADLNAGLITEEEAKRRRQELEKEANFYAAMDGASKFIRGDAIAALIILFLSLVGGLLIGIGIRGMDLASAVKTYTILSIGEGLASQVPALLLSTAAGVLTTKMSSRENLGEAISEELTKQPRALLFSAGVLGFIGLIPGLPTLPFLAMSAILAGAYYLVQQSLKEREL... | Function: Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 75392
Sequence Length: 678
Subcellular Location: Cell membrane
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P35620 | MSTRDLSVLISVVLIVAMLVIPFPPWLLSILIIINISLALIVLLTTMNMQEALQFSIFPSLLLLLTLFRLGLNVSTTRSILSHGEGGKVVETFGNFVVGGNVLVGLVVFIILIIIQFIVITKGAERVSEVAARFTLDAMPGKQMSIDADLNAGMITEQEAKHRREKVAREADFYGAMDGASKFVKGDAIAGIIIVMINIIFGIVIGMLQQGMSIQEAASHFTMLTVGDGIVSQIPALLISTATGIVVTRAASEGNLGHDITGQLFAYPKLLYVAAATIMLLGIFTPIGILLTGPLAGLLAFGAYTLSKSGKEKEEVDEIL... | Function: Involved in the export of flagellum proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73977
Sequence Length: 677
Subcellular Location: Cell membrane
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Q44909 | MLDARKNSILGYLGLNNKSDLIISVGLIFVVAGFILPLPAVILDVLITVNLVISLLIILIVLYSKRSLDFSVFPTLLLVMTIFGLVLNISSTRLILTKGINFDGQMIRTFGTFVVGSSGIQGLVIGFIIFIIIIAVQFIVITKGATRVAEVAARFALDALPGKQMAIDSAYSSGNLTEEEATRQKNDLQSEVNFYGAMDGASKFVSGNVKVGFLITLINILGGLLVGITLQGLNFNEALNNYVSLTVGDGLVSQLPSLLISTSTGLIVTRSISKNSFGGEIFDQFTNHLGIYWIVSGFLLFLAFLPGFPTLILMFLSLSI... | Function: Required for formation of the rod structure of the flagellar apparatus. Together with FliI and FliH, may constitute the export apparatus of flagellin (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76969
Sequence Length: 697
Subcellular Location: Cell membrane
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O25119 | MATKLTPKQKAQLDELSMSEKIAILLIQVGEDTTGEILRHLDIDSITEISKQIVQLNGTDKQIGAAVLEEFFAIFQSNQYINTGGLEYARELLTRTLGSEEAKKVMDKLTKSLQTQKNFAYLGKIKPQQLADFIINEHPQTIALILAHMEAPNAAETLSYFPDEMKAEISIRMANLGEISPQVVKRVSTVLENKLESLTSYKIEVGGLRAVAEIFNRLGQKSAKTTLARIESVDNKLAGAIKEMMFTFEDIVKLDNFAIREILKVADKKDLSLALKTSTKDLTDKFLNNMSSRAAEQFVEEMQYLGAVKIKDVDVAQRKI... | Function: One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation. Required for flagellum synthesis an... |
Q51464 | MSENRLAAKLTKVDKAAILLLSLGETDAAQVLRHMGPKEVQRVGVAMASMRNVHREQVEQVMGEFVEVVGDQTSLGVGADGYIRKMLTQALGEDKANNLIDRILLGGSTSGLDSLKWMEPRAVADVIRYEHPQIQAIVVAYLDPDQAAEVLSHFDHKVRLDIVLRVSSLNTVQPSALKELNLILEKQFAGNSNATRTTMGGVKRAADIMNYLDSSIEGQLMDSIREVDEDLSGQIEDLMFVFDNLADVDDRGIQALLREVSSDVLVLALKGSDEAIREKVFKNMSKRAAELLRDDLEAKGPVRVSEVEGAQKEILTIARR... | Function: FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation ... |
P0A1K0 | MSNLSGTDKSVILLMTIGEDRAAEVFKHLSTREVQALSTAMANVRQISNKQLTDVLSEFEQEAEQFAALNINANEYLRSVLVKALGEERASSLLEDILETRDTTSGIETLNFMEPQSAADLIRDEHPQIIATILVHLKRSQAADILALFDERLRHDVMLRIATFGGVQPAALAELTEVLNGLLDGQNLKRSKMGGVRTAAEIINLMKTQQEEAVITAVREFDGELAQKIIDEMFLFENLVDVDDRSIQRLLQEVDSESLLIALKGAEPPLREKFLRNMSQRAADILRDDLANRGPVRLSQVENEQKAILLIVRRLAETGE... | Function: FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation ... |
P95715 | MSNLTGTDKSVILLMTIGEDRAAEVFKHLSQREVQTLSAAMANVTQISNKQLTDVLAEFEQEAEQFAALNINANDYLRSVLVKALGEERAASLLEDILETRDTASGIETLNFMEPQSAADLIRDEHPQIIATILVHLKRAQAADILALFDERLRHDVMFVSHLWRRAASALAELTEVLNGLLDGQNLKRSKMGGVRTAAEIINLMKTQQEEAVITAVREFDGELAQKIIDEMFLFENLVDVD | Function: FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation ... |
Q9WY63 | MPEKKIDGRRKAAVLLVALGPEKAAQVMKHLDEETVEQLVVEIANIGRVTPEEKKQVLEEFLSLAKAKEMISEGGIEYAKKVLEKAFGPERARKIIERLTSSLQVKPFSFVRDTDPVQLVNFLQSEHPQTIAVVLSYLDPPVAAQILGALPEELQTEVLKRIALLERTSPEVVKEIERNLEKKISGFVSRTFSKVGGIDTAAEIMNNLDRTTEKKIMDKLVQENPELADEIRRRMFVFEDILKLDDRSIQLVLREVDTRDLALALKGASDELKEKIFKNMSKRAAALLKDELEYMGPVRLKDVEEAQQKIINIIRRLEEA... | Function: One of the proteins that forms a switch complex that is proposed to be located at the base of the basal body. This complex interacts with chemotaxis proteins (such as CheY) in addition to contacting components of the motor that determine the direction of flagellar rotation (By similarity).
Location Topology: ... |
Q9X4Q9 | MAKDNKDGGEVVESTIDISEIPGEEKAAILLLSLNEEDAAGIIRHLEPKQVQRVGSAMARAKDLSQTKVSAVHRAFLEDIQKYTNIGMGSEDFLRNALVAALGADKANNLVDQILLGTGSKGLDSLKWMDPRQVASIIINEHPQIQTIVLSYLEPDQSAEILAQFAQRDALDLLMRIANLEEVQPSALAELNEIMEKQFAGQAGAQAAKIGGLKAAADIMNYLDNNIESVLMEGMREKDEDLATQIQDLMFVFENLVEVDDQGIQKLLRDVPQDVLQKALKGADDTLREKIFKNMSKRAAEMMKDDLEAMPPIKVSDVEA... | Function: FliG is one of three proteins (FliG, FliN, FliM) that forms the rotor-mounted switch complex (C ring), located at the base of the basal body. This complex interacts with the CheY and CheZ chemotaxis proteins, in addition to contacting components of the motor that determine the direction of flagellar rotation ... |
O34171 | MTMPESMLSESKLSGWAISPKLAQLASLAGHYADPEFSVAHGGHVRTIAAGHYTVSGLSRHVRLGEFVAHRSATGIHLGEVVRVEPDICYVCPIEPGEPIGIHDTVIRKGAFRVSPDESWCGRTINALGEPIDGQGPLASGIVRRSISNNAPPSMTRKRVETPFKTGVRAIDIFSPLCLGQRLGIFAGSGVGKSTLLSMLAKADAFDKVVIALVGERGREVREFIEDTMGDNMSKSVAVVATSDESPMLRKMAPLSAVTIAEHFRDQGDNVLLIIDSVTRFAHAIREVAVASGEPPVARGYPASVFTELPRLLERAGPGA... | Function: Probable catalytic subunit of a protein translocase for flagellum-specific export, or a proton translocase involved in local circuits at the flagellum.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Sequence Mass (Da): 50807
Sequence Length: 473
Subcellular Location: Cytoplasm
EC: ... |
O67531 | MKGIRRNLQKSYLKRCSEMYLRGLKVSGEIVSAKGIYLEAILPFANIGNEVEIQSNSRRIRGEVIGFSGDKVLVMPYEPVFGLRKGDKVLLKNELVSTKTGNGVVGKVVDPFGNPLDGGFIGFVEEKGLELPQINPLYRERIREVFDTGVRSVNALFTLGKGQKIGIFAGAGVGKSTLLGMITRHSKADVVVLALIGERGREVKEFLEEVLGEEGLKKSVVVVSTADQSPILKVKGAISAVVHAHHFASQGKDVLLLMDSITRLALAQREIGLAAGEPPTLKGFTPSVFQLLTRIAESCGAFKKGSITGIFTVLVEGDDI... | Function: Probable catalytic subunit of a protein translocase for flagellum-specific export, or a proton translocase involved in local circuits at the flagellum.
Catalytic Activity: ATP + 4 H(+)(in) + H2O = ADP + 5 H(+)(out) + phosphate
Sequence Mass (Da): 48507
Sequence Length: 443
Subcellular Location: Cytoplasm
EC: ... |
Q10F03 | MLPLLLPLPVTPPPPLPSPTLTLAPASAPRRRLVLLAAAAPHHHHHHRRRRVYRRQRAAPTQTRAPRRTLSASNAARGEEDLEEAIYEFMRRSDKPGAFPTRAELVAAGRADLAAAVDACGGWLSLGWSSGGAEAGRASSSVGVHPDYPPEAGAAAAAGGASDLAQGAVWASSREAEASPSGRQPETEEEETETKFGTGLDGMLTRLQRERERVRPPLPRSSDGAGGERDNVALMGQSGAPSHSATGGRYTPKVPDNGNIHSYHPQNGALEHNKSSKSLTNDAWRTWSLDKGGFSDFQAAEIHSTNSRKSFRHDGLDILA... | Function: Involved in compound starch granule formation and starch synthesis in endosperm. May act as a regulatory scaffolding protein and affect starch synthesis and compound starch granule formation through direct interaction with isoamylase 1 (ISA1). Binds starch, amylopectin and amylose through its C-terminal carbo... |
Q7UQJ2 | MAMIDLTHDWQLLAQNPAGGLNSSSLLLLVGVFLALFFAAVLGFFFLRYGKLWFQAFMSDADVQLLNLIRMHFTKVNPNVIVQAKVMVAQAGLNIGRRDGISTHRLEAHYLAGGNVMNVIHAIIAAHRAQIPLEFDQAAAIDLAGRDVLDAVQTSVYPKVIDCPDPKRSGKTTLSAITKNGVELRVRTRVTVRTNIEQLIGGATEDTVIARVGEAIISSIGSAETHFKVLENPDMITRVVLSRGLDAQTAFEIVSIDIADIDVGENIGARLQNDQAEADTRVARAQAERRRAEAIAAEQQMNARVSENRSRLVLAEADVP... | Function: Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. Flotillins are thought to be important factors in membrane fluidity.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 37257
Seque... |
Q7UQD2 | MRRPMIASLLLDTLPLAQMPKVTTALLIGALVIFAGIVVVLFIFTSYFGLWIQSVLTGSKISFGNLIGMTFRKVNTRAIVRSKIMATQAGLDDPELTVGALEAHYLAGGNVQQVIRALIAAKKAKTISLTFREATAIDLAGRDVLESVQTSVYPKVIDCPPRGSAKPSLDAVAKDGIQLKVRARVTVRANLQQLIGGATEETIIARVGEGIVSAIGSADDHKAVLENPDVISKAVLVKKLDSQTAFEIVSIDIADIDVGANIGARLQADQAEADTAVARANAEGRRAAAVAEEQEMQAEIAKSQAQVVEAQSDVPRAMAE... | Function: Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. Flotillins are thought to be important factors in membrane fluidity.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 38691
Seque... |
Q5WHE8 | MNDSTIFVLIAIALAIILIAILFTFVPVALWISAIAAGVKIGIFELVGMRLRRVVPARVVNPLIKAVKAGLDLDTSRLEGHYLAGGNVDRVVNALIAAQRANIDLSFERAAAIDLAGRDVLEAVQMSVNPKVIETPFIAGVAMDGIEVKAKARITVRANIDRLVGGAGEDTVIARVGEGIVSTIGSQNDHKKVLENPDMISQTVLSKGLDSGTAFEILSIDIADIDIGKNIGAELQTDQAQADKNIAQAKAEERRAMAVAKEQEMKARVEEMRAKVVEAEAEVPMALSEALRQGHMGVMDYMNYQNVMADTDMRDSISKA... | Function: Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. Flotillins are thought to be important factors in membrane fluidity.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 36663
Seque... |
B3ETU2 | MTYLYDNSTLWIPILLGFLLFLYFFPVNLWITALFSGVRVSLFELVFMRIRRVPPRVIVESMITATKAGLQVTTTEIETHYLAGGNVPSVIRALISADKANIKLTFKQATAIDLAGRDVFQAVQISVNPKVINTPSVAAVAADGIQLVTKARVTVRANIQQLVGGAGEDTILARVGEGIVTSIGSAASHKEVLANPDQISKLVLQRGLDAGTAFEILSIDIADVDVGENIGAKLQIDQANADLRVAEAKAEERRAMAVAVEQEMRAKSQEARAQVILAESEIPKAMSAALKSGHIGVMDYYRMQNIKADTNMRAAISGEG... | Function: Found in functional membrane microdomains (FMM) that may be equivalent to eukaryotic membrane rafts. FMMs are highly dynamic and increase in number as cells age. Flotillins are thought to be important factors in membrane fluidity.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 35915
Seque... |
Q6FRT5 | MYIGAFQDTLFVDMLEYFGWVTVGKEYLDIYRPNGVPVAPNAVAASISGKEEMKQDNQTSTDSMSTSTQQETDASNEDIERAMDTDNGLDKAMSGGQGVFGTEEDDSSTKDASKPEEADPFLVEFLGEDDPRKPWNWSFSKKTFVIVQLMVLTCINYMGSSIYTPGQEQIQHEFHVGHVVGTLNLSMYVLGYAIGPIIFSPLSEVSSIGRMPLYLWTFILFTILQVACALVRNIAGLVILRFITGILCSPVLATGGASVGDVCFPRYVPRFLGAWAVGAVAAPVMAPILGAAMVVAKDWRWIFWLMLFMCGATLLSIIFF... | Function: Multidrug transporter that confers resistance to 5-flucytosine (5-FC) and clotrimazole . Further confers azole drug resistance . Plays direct roles in extrusion of 5-flucytosine and clotrimazole .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65989
Sequence Length: 589
Subcellular Locatio... |
Q9NLA1 | MPINYNRNAVELKLSSQLLQWLDQRLPLGDPMRIPSIDSYKYIQDLGKGRFGTVCKFSNGNTFETVKKVDLTIFNHWTQSETKVSNRLDTFLYEFRHLHKVTNDNNRIVNFLGIYADSNQMYIMSEYLPRGSVKDLLVKETLGEDTAIKYLMETVEALDYLHNLSPPVIHRDIKAANLLITSNDSIKLANFGLVRDLAVDGFGIAIASEITLDFRATLLYVAPEVLSSALGPGNRNAYELPADIWALGCTFIEMLLKRPPHFEYFGHIDEIPKVLLGYAKSEDGKVLPYTSEVLVPSSSNCVQKIVDLVFIKSPEHRPNT... | Function: Probable serine-threonine protein kinase involved in the control of defecation rhythms. Required to increase the length of defecation cycle period. Acts in a cell-functional rather than developmental aspect in the regulation of defecation rhythms.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-p... |
Q6RKD8 | MDLRDWLFLCYGLIAFLTEVIDSTTCPSVCRCDNGFIYCNDRGLTSIPSDIPDDATTLYLQNNQINNAGIPQDLKTKVKVQVIYLYENDLDEFPINLPRSLRELHLQDNNVRTIARDSLARIPLLEKLHLDDNSVSTVSIEEDAFADSKQLKLLFLSRNHLSSIPSGLPHTLEELRLDDNRISTIPLHAFKGLNSLRRLVLDGNLLANQRIADDTFSRLQNLTELSLVRNSLAAPPLNLPSAHLQKLYLQDNAISHIPYNTLAKMRELERLDLSNNNLTTLPRGLFDDLGNLAQLLLRNNPWFCGCNLMWLRDWVRARAA... | Function: Plays a role in fibroblast growth factor-mediated signaling cascades that lead to the activation of MAP kinases . Promotes neurite outgrowth via FGFR1-mediated activation of downstream MAP kinases. Promotes an increase both in neurite number and in neurite length . May play a role in cell-cell adhesion and ce... |
Q8BLU0 | MGLQTTKWPGRGAFILKFWLIISLGLYLQVSKLLACPSVCRCDRNFVYCNERSLTSVPLGIPEGVTVLYLHNNQINNAGFPAELHNVQSVHTVYLYGNQLDEFPMNLPKNVRVLHLQENNIQTISRAALAQLLKLEELHLDDNSISTVGVEDGAFREAISLKLLFLSKNHLSSVPVGLPVDLQELRVDENRIAVISDMAFQNLTSLERLIVDGNLLTNKGIAEGTFSHLTKLKEFSIVRNSLSHPPPDLPGTHLIRLYLQDNQINHIPLTAFANLRKLERLDISNNQLRMLTQGVFDHLSNLKQLTARNNPWFCDCSIKW... | Function: Functions in cell-cell adhesion, cell migration and axon guidance. Mediates cell-cell adhesion via its interactions with ADGRL3 and probably also other latrophilins that are expressed at the surface of adjacent cells . May play a role in the migration of cortical neurons during brain development via its inter... |
Q9NZU0 | MISAAWSIFLIGTKIGLFLQVAPLSVMAKSCPSVCRCDAGFIYCNDRFLTSIPTGIPEDATTLYLQNNQINNAGIPSDLKNLLKVERIYLYHNSLDEFPTNLPKYVKELHLQENNIRTITYDSLSKIPYLEELHLDDNSVSAVSIEEGAFRDSNYLRLLFLSRNHLSTIPWGLPRTIEELRLDDNRISTISSPSLQGLTSLKRLVLDGNLLNNHGLGDKVFFNLVNLTELSLVRNSLTAAPVNLPGTNLRKLYLQDNHINRVPPNAFSYLRQLYRLDMSNNNLSNLPQGIFDDLDNITQLILRNNPWYCGCKMKWVRDWL... | Function: Functions in cell-cell adhesion, cell migration and axon guidance, exerting an attractive or repulsive role depending on its interaction partners. Plays a role in the spatial organization of brain neurons. Plays a role in vascular development in the retina (By similarity). Plays a role in cell-cell adhesion v... |
Q8BGT1 | MISPAWSLFLIGTKIGLFFQVAPLSVVAKSCPSVCRCDAGFIYCNDRSLTSIPVGIPEDATTLYLQNNQINNVGIPSDLKNLLKVQRIYLYHNSLDEFPTNLPKYVKELHLQENNIRTITYDSLSKIPYLEELHLDDNSVSAVSIEEGAFRDSNYLRLLFLSRNHLSTIPGGLPRTIEELRLDDNRISTISSPSLHGLTSLKRLVLDGNLLNNHGLGDKVFFNLVNLTELSLVRNSLTAAPVNLPGTSLRKLYLQDNHINRVPPNAFSYLRQLYRLDMSNNNLSNLPQGIFDDLDNITQLILRNNPWYCGCKMKWVRDWL... | Function: Functions in cell-cell adhesion, cell migration and axon guidance, exerting an attractive or repulsive role depending on its interaction partners . Plays a role in the spatial organization of brain neurons . Plays a role in vascular development in the retina . Plays a role in cell-cell adhesion via its intera... |
Q8GVE3 | MDTKHQDKPSILMLPWLAHGHIAPHLELAKKLSQKNFHIYFCSTPNNLQSFGRNVEKNFSSSIQLIELQLPNTFPELPSQNQTTKNLPPHLIYTLVGAFEDAKPAFCNILETLKPTLVMYDLFQPWAAEAAYQYDIAAILFLPLSAVACSFLLHNIVNPSLKYPFFESDYQDRESKNINYFLHLTANGTLNKDRFLKAFELSCKFVFIKTSREIESKYLDYFPSLMGNEIIPVGPLIQEPTFKEDDTKIMDWLSQKEPRSVVYASFGSEYFPSKDEIHEIASGLLLSEVNFIWAFRLHPDEKMTIEEALPQGFAEEIERN... | Function: Involved in the production of the bitter neohesperidosides in citrus. Shows a strict specificity for UDP-rhamnose as donor.
Catalytic Activity: flavanone 7-O-beta-D-glucoside + UDP-beta-L-rhamnose = flavanone 7-O-[alpha-L-rhamnosyl-(1->2)-beta-D-glucoside] + H(+) + UDP
Location Topology: Single-pass membrane ... |
Q96330 | MEVERVQDISSSSLLTEAIPLEFIRSEKEQPAITTFRGPTPAIPVVDLSDPDEESVRRAVVKASEEWGLFQVVNHGIPTELIRRLQDVGRKFFELPSSEKESVAKPEDSKDIEGYGTKLQKDPEGKKAWVDHLFHRIWPPSCVNYRFWPKNPPEYREVNEEYAVHVKKLSETLLGILSDGLGLKRDALKEGLGGEMAEYMMKINYYPPCPRPDLALGVPAHTDLSGITLLVPNEVPGLQVFKDDHWFDAEYIPSAVIVHIGDQILRLSNGRYKNVLHRTTVDKEKTRMSWPVFLEPPREKIVGPLPELTGDDNPPKFKPF... | Cofactor: Binds 1 ascorbate molecule per subunit.
Function: Catalyzes the formation of flavonols from dihydroflavonols. It can act on dihydrokaempferol to produce kaempferol, on dihydroquercetin to produce quercitin and on dihydromyricetin to produce myricetin. In vitro catalyzes the oxidation of both enantiomers of na... |
Q31HL0 | MQSFHVLQLIAVGFGGALGAMARFIVSNQVYAWWGRDFAWGTLVVNSLGSFAIGLIMILMIDKFHASVEMRSFLIVGFLGAFTTFSTFSFETYSFLQTGEITKAMLNIGVSVLTGLFAVWLGIWTGKQFFSP | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14554
Sequence Length: 132
Subcellular Location: Cell inner membrane
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B4U812 | MNYLAVLVGGGVGALVRYLVSIFIQKFVPNFPLGTMVINTTGAFLIGFLSIYLTEVIDAPPNIRLLLITGFLGGYTTFSTFTLEGIGLINNGDYLKAFYYIVGTNVIGFLFVALGRFLGGLL | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13155
Sequence Length: 122
Subcellular Location: Cell inner membrane
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Q0C3G9 | MNGFLLVALGGAIGASLRHGVGLVAVRHLPLGWPWGTSFVNIAGSLAMGLLAGWLALKAEGASQEARLFLATGVLGGFTTFSAFSLEVATMLRSGETLKAGLYAGVSVLLGVSALFIGLWMARRIFA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13092
Sequence Length: 127
Subcellular Location: Cell inner membrane
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Q5R0A9 | MNNLLLHFFCVAVGGAIGASARFAMVLAMQSFGVRAFPFATLTVNIIGSFFLGLLLAYAEQQPVSETTRLFLGVGLLGAFTTFSTFSVEVVALASQGELLKAALHIAFNVIICIAAVFAAMMLYSTTVK | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13662
Sequence Length: 129
Subcellular Location: Cell inner membrane
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A8AAZ9 | MKALVWVAVGGALGAIVRYFFYKFVPQVYDFPLATFLVNVVASFLLGFIIGAFEAKPWGQQLKLALATGFCGALSTFSTFAADNYILLRSSKYITAFVYTAVSVGLGIVSVALGEDLAQRLLK | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13286
Sequence Length: 123
Subcellular Location: Cell inner membrane
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Q28US2 | MLRVFGHGTVGGAFPLPILTVNVLGSFLMGVFVVAAAHRGLTHLSPLVMTGLLGGFTTFSAFSLETVTLYERGDVGQAALYVALSVGLSIAGLMAGLWLARGVFA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 10825
Sequence Length: 105
Subcellular Location: Cell inner membrane
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Q1INF0 | MAIREYLWVSLGGIVGACARYFLSRFTAKITGTSFPWGTLLINITGSFVLGLFLVYTTERVFVDPKWRLLIAIGFCGAYTTFSSYAYESMVYFQQGNWGLFAGNVLANNILCLAAVLGAGALVRSI | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13815
Sequence Length: 126
Subcellular Location: Cell inner membrane
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Q5ZY60 | MVVAPYLAVAIGGSLGAMSRYLVTIMAQNAWGIKFPYGTLLVNTLGSFLAGFFLIVLVGRFSAEESFRLFLFTGFLGAFTTFSSFAAESLFMFEQGYWFKLMTNILVNNVGSLSMVFIGTLVAKYVLLGHQGSN | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14612
Sequence Length: 134
Subcellular Location: Cell inner membrane
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Q8EZS4 | MNFSKSLLLIAFGGTIGSIFRYLLQYWFGNVLGYSLPWGTLTANLLGSFLIGVVYAISDRFPLFDPQWKFLLASGFCGGFTTFSTFSYETFQMLKSGHYILFLGYICLSVVGGIGFAFAGVWMIKNF | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14173
Sequence Length: 127
Subcellular Location: Cell inner membrane
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A0L889 | MQIAWVALGGAIGAVARYVLSNAVYAWLGRAFPWGTLSVNLLGSFIMGLLFYLFTQRLMVPEALKPLVLVGGLGAFTTFSTFSLETLNLMQSGSWSLALLNMLSSVLLCVLAAYLGLVVGRLI | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13189
Sequence Length: 123
Subcellular Location: Cell inner membrane
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Q2W1R5 | MLTYALVALGSAIGGTLRYWLSMVIAEASAGTFPWATLVINVAGSAAIGLFATLTSVDGRVFVPSEWRTFFMVGICGGFTTFSSFSLQTLALAQDGDWLAAGLNVVGSVALCLLAVWLGHVAATIINR | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13348
Sequence Length: 128
Subcellular Location: Cell inner membrane
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Q65QC7 | MIMWQSLILISSGAALGASLRWGMGLILNPLFAAFSFGTLIANYLGCFIIGLIMAMIWQHPQFSGEWRLFMITGFLGSLTTFSSFSAEVMENFIQQKWLIGLGIMSAHLFGCLIFTGIGVLITRWLN | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14089
Sequence Length: 127
Subcellular Location: Cell inner membrane
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A1U6R3 | MWWSVLAVSVGAVIGANLRWGLGLWLNASYHAVPWGTLVANLSGGWLIGVLMAFFSQSSVLSPEWRLFAVTGLCGALTTFSTFSLEMFAALQEGKWGMALVGILAHVVGSILMTALGFLTFSLVRG | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13437
Sequence Length: 126
Subcellular Location: Cell inner membrane
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C6BTV9 | MHKYLYIAAGGAAGSLCRYLVSGVTQRMFATSFPIGTFSVNMIGCLFFGLVTGLFEERLGLPPEMRLLILTGFMGAFTTFSTYMFESTNLIKSGQWAMTALNIGGQSILGFACIVGGLALGRLIVS | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13482
Sequence Length: 126
Subcellular Location: Cell inner membrane
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Q87KE9 | MGQFSILGFIALGGAIGACSRYLVSEFCVLLFGRGFPYGTLTVNVVGSFIMGLLIAAFENEILATEPWRQVIGLGFLGALTTFSTFSMDNVLLMQQGAFFKMGLNILLNVVLSISAAWIGFQLLMRS | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13714
Sequence Length: 127
Subcellular Location: Cell inner membrane
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Q3BTX1 | MNAPVWWQQLLLAMTGGALGSGLRFAIGASLIQRFGTGFPWGTLTVNLLGSFVAGVLLVWLDARGPSSWPLRALLIVGVIGGLTTFSSLMMECLVFARTDRSTMIGIYLAVTLLAGLALVVAGARTGQWLVAR | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14064
Sequence Length: 133
Subcellular Location: Cell inner membrane
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Q5GZS7 | MRIATSYEMCAQCCCAAAKFADTLQTKPRRSHVTPIYTIAAISLGASLGALARYGLGLALNAIFPPLPIGTLAANLIAAYVVGVTIAYVGTVPGLSPLWRLFMITGLAGGLSTFSTFTAELFSLLREGRLGMSAGMLGLHVGGSLALLMLGMLTIGLLRKSSLGIAE | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 17294
Sequence Length: 167
Subcellular Location: Cell inner membrane
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Q9PDC5 | MNAVVWWQSLLLVMLGGAFGSGLRFVIGSCLLQRFGAGFPWGTLAVNLIGSFVAGFLLIWLDKRGSAGWSWRMLLIVGLIGGLTTFSSLMMECLVFVRSDRSLMVGLYLCITLLFGLLFVFLGARLGAFVCDDQRVLEIDRTA | Function: Fluoride-specific ion channel. Important for reducing fluoride concentration in the cell, thus reducing its toxicity.
Catalytic Activity: fluoride(in) = fluoride(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15691
Sequence Length: 143
Subcellular Location: Cell inner membrane
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F8JX40 | MTVHQAPGTPGSVISLRPRYDNWIGGDWKAPAEGRYFANPTPVTGEEYTEIARSTAADIDLALDAAHAAAPAWGRTAPAERAAVLGRIADRIEQHLTELAVAEVWDNGKPIREALAADLPLAVDHFRYFAGVLRAQEGSISQLDEDTVAYHFHEPLGVVGQIIPWNFPLLMAVWKLAPALAAGNAVVLKPAEQTPVSILVLMELIADILPPGVINVVNGFGIEAGKPLAINPRIAKVAFTGETTTGRLIMQYASQNLIPVTLELGGKSPNLFFEDVAAARDDFYDKALEGFTMFALNQGEVCTCPSRALIAGGIYDGFLG... | Function: Catalyzes the oxidation of fluoroacetaldehyde to fluoroacetate. Has high affinity for fluoroacetate and glycolaldehyde but not for acetaldehyde.
Catalytic Activity: fluoroacetaldehyde + H2O + NAD(+) = fluoroacetate + 2 H(+) + NADH
Sequence Mass (Da): 54570
Sequence Length: 507
EC: 1.2.1.69
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Q940U6 | MAALIRCCSSFSHTSGGQPPPRDKSRAPEIGKFATSIGYSVVRKPGDHPPFSKIIHSSSQPKERQGKGILQTPFASVGSLDKFSAFEGIGRLKLPVMAVLLTNSLQMATPLEALAAEICEPESSMFSMPILLLVALIGATVGGLLARQRKGELQRLNEQLRQINAALRRQAKIESYAPSLSYAPVGARIPDSEIIVEPKKQELISKLKTGKTFLRNQEPEKAYTEFKIALELAQSLKDPTEEKKAARGLGASLQRQGKYREAIQYHSMVLAISKRESEDSGITEAYGAIADCYTELGDLEKAGKFYDTYIARLETD | Function: Negative regulator of tetrapyrrole biosynthesis (including chlorophyll) in chloroplasts, probably via HEMA1 repression. Inhibits especially the magnesium ion Mg(2+) branch of tetrapyrrole biosynthesis, but independently of heme.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 34587
Sequenc... |
B8NHD7 | MRYLITGATGGLGGHILEYFIAQIPFSDFAASSSSPENRSRFESRGVNFRHLDYENPTTLNRALHDVENLLFISTNANVIDVEKVKRQHRNVVEAARKANVKHVWYTSLPFGGLTNDSEVSVQRAHLATEKMLKESGLTFTCIREGIYVEGFPLFLNWYPETTLLTLPRDGEIAFTSRVELAVCTARLMIQGGFENRIVLLTAGETITAKELVSVINETTGRRVELRYVSPDEFVDAGPRNDRGGKSRAFFETLVSLWESAASGELRTMDGLMAEILGRDPIPPRDAVRQLLVENRDHTWHQMYAKK | Function: NmrA-like family domain-containing oxidoreductase; part of the gene cluster that mediates the biosynthesis of flavunoidine, an alkaloidal terpenoid with a tetracyclic cage-like core connected to dimethylcadaverine via a C-N bond and acylated with 5,5-dimethyl-L-pipecolate . The tetracyclic core is synthesized... |
Q9N1F2 | MVKLNDEEGAAMAPGHQPTNGYLLVPGGEPPGKVSAELQNGPKAVCLTLNGVSRDSLAAAAEALCRPQTPLAPEEETQTRLLPTGPGEETPGTEGSPAPQTALSARRFVVLLIFSLYSLVNAFQWIQYSVISNVFEGFYGVSSLHIDWLSMVYMLAYVPLIFPATWLLDTRGLRLTALLGSGLNCLGAWVKCASVQQHLFWVTMLGQCLCSVAQVFILGLPSRIASVWFGPKEVSTACATAVLGNQLGAAIGFLLPPVLVPNTQNNTDLLACNISTMFYGTSSVATFLCFLTIIAFKEKPQYPPSQAQAALQNSPPAKYS... | Function: Heme b transporter that mediates heme efflux from the cytoplasm to the extracellular compartment. Heme export depends on the presence of HPX and is required to maintain intracellular free heme balance, protecting cells from heme toxicity. Heme export provides protection from heme or ferrous iron toxicities in... |
Q4WLW7 | MKLPAAAGDAIVIGPNAVRLIKSWGEQLCEEIEPHLSNATHAEMLDHHDRFIVRHELAGRGKGWFTNRGRLISILYEHARKLGIDIRLGSRVTKYWEEDGRAGVIVNDRERLAADCVICADGVHSAARAWLTGQVDTQQHSGWANFRAHMTTEQLAKDPEASWVLQGTREKDRVYVWFGDGINLAIMTMKRGQELAWALMHTDKFNAHESWAGGRASIDDALATLSPWPGRLRPSSVIRHTLPEKLVDHALIYRPPLDTWVSAGGRVMLIGDAAHPYFPVVGQGGSQAIEDGVVVATALELAGKENVPLALRIRATLTEE... | Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of the antitumor fumiquinazolines that confer a dual-usage capability to defend against phagocytes in the environment and animal hosts . The simplest member is fumiquinazoline F (FQF) with a 6-6-6 tricyclic core derived from ... |
Q4WLW6 | MQYIPFLISGLVPVALSKSLFEATSNTRIDGNDIAAIFGPVLTPEAHIFLPSDGDYDDNVMARWSTFNDPSYVATVKPATETDVQAIREYQVSTAASHNITFFATGGGHGVKLNFGNVQNAINIELSLLDFIDLDLDNEVVTIGPGVENAQLYDLLSSVGKETALTGERCVNTIGPTLGGGLGPLYGIRGPQVDSLVSARLVTASGDVITVSRSENRDLFWAIRGAGANFGIVTSATYRIYDQTNGGMAVSAQFAFAPAVNRSVFDLMESMNDEYPPGMSGGMILSYNHTTNEPSVQWNLLFMGSNEDAQPWLDKIQALG... | Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of the antitumor fumiquinazolines that confer a dual-usage capability to defend against phagocytes in the environment and animal hosts . The simplest member is fumiquinazoline F (FQF) with a 6-6-6 tricyclic core derived from an... |
Q4WLW9 | MPEDKVEAIEHVESSRHDATVNEKAIADFLNAEKEMTTWQAVRAHRRLLLFAAYRVTHLAILPFVCASNYGYDTVSNGSSIAMPAFIMSFGAMNHATGSMYLPSIWTSLWTSMTNLGQALGSLIAGFLAERIGRRWTAVSLAILSIVGTFILVFSSTRGMLLVGKTMNGAVVGGLMAIGTTYAADVAPIKLRGALLQAIVFFGVAMQGVSLGIVRAFILDMRPLAWKIVFGIQWAFATLVLIAAFLVPESPVFYVAHGKHDKAQSALRRLHGSSDQYLHIRYGAIVHALDEERKQQSESVSWAELFKGCNLKRTITIGFI... | Function: MFS transporter; part of the gene cluster that mediates the biosynthesis of the antitumor cytotoxic peptidyl alkaloids fumiquinazolines that confer a dual-usage capability to defend against phagocytes in the environment and animal hosts . Probably involved in fumiquinazolines metabolism and transport .
Locati... |
Q493I2 | MVHSKSLRIAFFGTTSFAAWHLHTLAHLSTHQIIAVFTQEIQISTCKSFLSLHKIAKKYNISLFQSRTLSISDIIYIIKKINVDLIVVVSYGLILPQEILNIPRLGCINVHGSLLPRWRGPAPIQRALEYGDSITGITIIQMDLGIDTGDILHIMPCKIFPKDTSCTLSNRLVNIGSAMLSQVLDQFILGTFTLIPQDSTYATYAHKLNKQEARINWNLSAIQLERCIRAFNPWPISFFQIKNDRIRVWDAEVSNQNINNYSSSTSILPGTILAAHPNGIYVVTGSGILILTMLQISGKKITSVRDLLNAYKEWFKPNSV... | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
Q2L0K7 | MRLVFAGTPEFARLALEALLAAGHEIPLVLTQPDRPAGRGLKLTPSPVKEAALAAGIEVAQPRSLRLDGRYPDEALAAQARLVAVAPEVMVVAAYGLILPRWTLALPARGCLNIHASLLPRWRGAAPIQRAIEAGDARTGVTIMQMDDGLDTGDMLLERTVPIGAETTAAVLHDELARVGAEAIVAALADLPALAPRKQPEQGVTYAAKLDKAEAALKLDESAELLARRIRAFNPVPGASLRLPGLNEPVKVWQAEALPESSPAAPGTVLRASAQGVDIATGQGVLRLLELQKAGGKRQSAEVFVRGWQPA | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
O51091 | MKIFFVSSSSIALEVFKEIVKHYEVVGVLTLPDRPKGRGQKLSQNVIKSEAIARNIKVLDPLILDDNVLNLVRDLNPDLMLVFSYGKIFKKEFLDLFPKGCINVHPSLLPKYRGVSPIQSAILNGDCVSGVTIQSMALEMDSGNILVQKNFKIRSYDTSHDISKLVSSLSPSLVLEALEKISKGFLGIPQKSSEATFCSFLKKESGFIDFNLSAFEIKNKINACNPWPLVRVRLDYNDIIFHRADFLEVDLYKERKIGEIVDFNPEKGLFVNTGKGILLLLEVQRPGRKVLDFKSFYNGSRQLIGQVFSSIE | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
Q89BP0 | MPLRLIFMGTPDFSVPTLLELVAHGHEIVAVYTRAPKPGGRRGLQLQPTPVEEAARRLGVPVLTPKTLKTEEALEEFRAFDADAAVVVAYGMILPQAILDAPKLGCYNLHASLLPRWRGAAPINRAIMADDAESGVMVMKMDVGLDTGDVAMAERLAITDTMTAADLHDRLSRLGADLMVRAMAALDRGGLQLKKQSEDGVTYAAKIDKAEARIDWTKPARAVLRHIHGLSPFPGAWAELAGVSENARVKILRCELAKGSGAPGEVLDDQLTIACGEGAIRIIELQREGKARMQATDFLRGVPLKAGAKFT | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
Q8RDM3 | MKIIFMGTPTFAVPSLEKIYKEHEIISVFTKVDKPNARGKKINYSPIKEFALANNLKIYQPENFKDNTLIEEIRNMQADLIVVVAYGKILPKEVIDIPKYGVINLHSSLLPRFRGAAPINAAIINGDTKSGISIMYVEEELDAGDVILQEETEISDEDTFLSLHDRLKDMGADLLLKAIELIKKGEVKAQKQDKKLVTFVKPFRKEDCKIDWTKTSREIFNFIRGMNPIPTAFSNLNGTIIKIYETKINDKVYNNATCGEVVEYLKGKGIVVKTSDGSLIISSAKPENKKQMSGVDLINGKFLKIGEKLC | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
Q74GW4 | MAGLRIIFMGTPEFACPTLRKLIERGEEVIAVVTQPDRPKGRGQKLVPPPVKALAQEHDIPVLQPLKVRTPESVDEIRRLAPDLIVVVAFGQILPQSLLDIPKHGCINIHASLLPRYRGAAPLNWCLINGETETGITTMMMDAGLDTGDMLVKRAIPIGPDEDAQSLHDRLSQLGAETIDETLDLLLAGKLVREKQDDSLTCYAPMLKKEDGLVDWTREPVQVKNQVRGFTPWPGAYTFLDGKTLKLYRVAVAGETGEPGEILRVGREGILVGCGSGSILIQELQLEGRKRLPTAEFLAGFRLEPGTRLGEAGSVEH | Function: Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Catalytic Activity: (6S)-1... |
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