ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
C8V329 | MAGAFDFDLEKNPPVVQSTADNSSDGAVPGETFTYGDSTYAKIQRLAAELNIEQRGIERVPAAEQTDTSVFNIGSMWLAANMVVSSFAIGVLGKSVYSLGFVDAILTVLFFNLLGIMTVCFFSCFGPFGLRQMVFSRLWFGWYVTKGFAVLNILACLGWSAANAIVGAQMLHAVNSDVPGFAAILIISICTLLVTFAGYKVVHLYEYWSWIPTFIVFMIILGTFAHSGDFQNIPMGVGTSEMGSVLSFGSAVYGFATGWTSYAADYTVYQPANRSKRKIFLSTWLGLIVPLLFVEMLGVAVMTATDIKGSKYDVGYATSG... | Function: This permease has a broad specificity towards purines, and also transports cytosine, but neither uracil nor thymine. Contributes very little in purine uptake. Its major role may be the uptake of cytosine.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55197
Sequence Length: 508
Subcellular... |
P17064 | MLEEGNNVYEIQDLEKRSPVIGSSLENEKKVAASETFTATSEDDQQYIVESSEATKLSWFHKFFASLNAETKGVEPVTEDEKTDDSILNAASMWFSANMVIASYALGALGPMVFGLNFGQSVLVIIFFNIMGLIFVAFFSVFGAELGLRQMILSRYLVGNVTARIFSLINVIACVGWGIVNTSVSAQLLNMVNEGSGHVCPIWAGCLIIIGGTVLVTFFGYSVIHAYEKWSWVPNFAVFLVIIAQLSRSGKFKGGEWVGGATTAGSVLSFGSSIFGFAAGWTTYAADYTVYMPKSTNKYKIFFSLVAGLAFPLFFTMILG... | Function: This permease has a broad specificity towards purines, and also transport cytosine and 5-methylcytosine but neither uracil nor thymine.
PTM: Not N-glycosylated.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 58201
Sequence Length: 533
Subcellular Location: Membrane
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O59834 | MSSTELSEKDLAYLREAIKVSQQARDEGQHPFGCIIVDENDNVIMSAGNRVPDGDVTQHAETRAVGLITKTRRDLEKCTLYTSTEPCAMCSGAIFWSGIRRMIFGLSNENLIKLTQKSGECPPLYINSRDILGAASHPIEVVGPYIEDEAIIPHKGFWDGGR | Function: Catalyzes the hydrolytic deamination of cytosine to uracil or 5-methylcytosine to thymine. Is involved in the pyrimidine salvage pathway, which allows the cell to utilize cytosine for pyrimidine nucleotide synthesis.
Catalytic Activity: cytosine + H(+) + H2O = NH4(+) + uracil
Sequence Mass (Da): 17882
Sequenc... |
O04584 | MAVSFQTKNPLRPITNIPRSYGPTRVRVTCSVTTTNPQLNHENLVVEKRLVNPPLSKNNDPTLQSTWTHRLWVAAGSTTIFASFAKSIIGGFGSHLWLQPALACYAGYVFADLGSGVYHWAIDNYGGASTPIVGAQLEASQGHHKYPWTITKRQFANNSYTIARAITFIVLPLNLAINNPLFHSFVSTFAFCILLSQQFHAWAHGTKSKLPPLVMALQDMGLLVSRKDHPGHHQAPYNSNYCVVSGAWNKVLDESNLFKALEMALFFQFGVRPNSWNEPNSDWTEETETNFFTKI | Function: Fatty acid desaturase involved in the production of chloroplast-specific phosphatidylglycerol molecular species. Catalyzes the formation of a trans double bond introduced close to the carboxyl group of palmitic acid, which is specifically esterified to the sn-2 glyceryl carbon of phosphatidylglycerol (By simi... |
Q8WSF3 | MSLAVSLRRALLVLLTGAIFILTVLYWNQGVTKAQAYNEALERPHSHHDASGFPIPVEKSWTYKCENDRCMRVGHHGKSAKRVSFISCSMTCGDVNIWPHPTQKFLLSSQTHSFSVEDVQLHVDTAHREVRKQLQLAFDWFLKDLRLIQRLDYVGSSSEPTVSESSSKSRHHADLEPAATLFGATFGVKKAGDLTSVQVKISVLKSGDLNFSLDNDETYQLSTQTEGHRLQVEIIANSYFGARHGLSTLQQLIWFDDEDHLLHTYANSKVKDAPKFRYRGLMLDTSRHFFSVESIKRTIVGMGLAKMNRFHWHLTDAQSF... | Function: Involved in brain restructurization via hormonal control during metamorphosis. Implicated in N-glycan processing.
Catalytic Activity: Hydrolysis of terminal non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
Sequence Mass (Da): 75486
Sequence Length: 660
EC: 3.2.1.52
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Q52078 | MAGNKSVVYHGTRDLRVETVPYPKLEHNNRKLEHAVILKVVSTNICGSDQHIYRGRFIVPKGHVLGHEITGEVVEKGSDVELMDIGDLVSVPFNVACGRCRNCKEARSDVCENNLVNPDADLGAFGFDLKGWSGGQAEYVLVPYADYMLLKFGDKEQAMEKIKDLTLISDILPTGFHGCVSAGVKPGSHVYIAGAGPVGRCAAAGARLLGAACVIVGDQNPERLKLLSDAGFETIDLRNSAPLRDQIDQILGKPEVDCGVDAVGFEAHGLGDEANTETPNGALNSLFDVVRAGGAIGIPGIYVGSDPDPVNKDAGSGRLH... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Active against a range of primary alcohols as well as some secondary alcohols. Exhibits higher activity against alcohols with longer carbon chains.
Catalytic Activity: 2 formaldehyde + H2O = formate + H(+) + methanol
Sequence Mass (Da): 42981
Sequence Length: 399
EC:... |
Q9EY50 | MPVLNLNDPQAVERYEEFMRQSPYGQVTQDLGWAKVKNNWEPVDVYLEDDQGAIIAAMSMLLGDTPTDKKFAYASKGPVMDVTDVDLLDRLVDEAVKALDGRAYVLRFDPEVAYSDEFNTTLQDHGYVTRNRNVADAGMHATIQPRLNMVLDLTKFPDAKTTLDLYPSKTKSKIKRPFRDGVEVHSGNSATELDEFFKTYTTMAERHGITHRPIEYFQRMQAAFDADTMRIFVAEREGKLLSTGIALKYGRKIWYMYAGSMDGNTYYAPYAVQSEMIQWALDTNTDLYDLGGIESESTDDSLYVFKHVFVKDAPREYIGE... | Function: Involved in the synthesis of the bacterial cell wall. Catalyzes the addition of alanine into the interchain peptide bridge of peptidoglycan precursor using aminoacyl-tRNA(Ala) as amino acid donor. This alanine is added to the epsilon-amino group of the L-lysine of the peptidoglycan UDP-N-acetyl-alpha-D-muramo... |
Q9SXQ6 | MGIKGLTKLLADNAPKAMKEQKFESYFGRRIAVDASMSIYQFLIVVGRTGMETLTNEAGEVTSHLQGMFNRTIRLLEAGIKPVYVFDGKPPDLKKQELAKRYSKREDATKELTEAVEEGDKDAIEKFSKRTVKVTKQHNEECKRLLRLMGVPVVEAPCEAEAECAALCINDMVYAVASEDMDSLTFGAPRFLRHLMDPSSKKIPVMEFEVAKVLEELELTMDQFIDLCILSGCDYCDSIKGIGGQTALKLIRQHGSIESILENINKDRYQIPEDWPYQEARRLFKEPNVTLDIPELKWNAPDEEGLVEFLVKENGFNQDR... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. Du... |
B8AMS4 | MGIKGLTKLLAEHAPGAAVRRRVEDYRGRVVAIDTSLSIYQFLIVVGRKGTEVLTNEAGEVTSHLQGMLNRTVRILEAGIKPVFVFDGEPPDMKKKELAKRSLKRDGSSEDLNRAIEVGDEDLIEKFSKRTVKVTKKHNEDCKRLLSLMGVPVVQAPGEAEAQCAALCENHKVFAIASEDMDSLTFGARRFLRHLTDLSFKRSPVTEFEVSKVLEELGLTMDQFIDLCILSGCDYCENIRGIGGQRALKLIRQHGYIEEVVQNLSQTRYSVPEDWPYQEVRALFKEPNVCTDIPDFLWTPPDEEGLINFLAAENNFSPDR... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. Du... |
O04397 | MAHSALSQVSVAVPLQTDSSFRRSTFKATSITFSDRSSWISMPPIDLKAAPSRNQHIVCMSVQQASKAKVSVSPLSLEDAKEPPLNIYKPKEPYTATIVSVERLVGPKAPGETCHIVIDHDGNLPYWEGQSYGVIPPGENPKKPGNPHNVRLYLIASTRYGDSFDGKTASLCVRRAVYYDPETGKEDPSKNGVCSNFLCDSKPGDKVKITGPSGKIMLLPEEIPNATHIMIGTGTGVAPFRGYLRRMFMESVPTKFNGLAWLFLGVANTDSLLYDDEFTKYLNDYPGNFRYDRALSREQKNNKGGKMYVQDKIEEYSDEI... | Function: May play a key role in regulating the relative amounts of cyclic and non-cyclic electron flow to meet the demands of the plant for ATP and reducing power. Is involved in nitrate assimilation.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequen... |
B1HW35 | MQHVYDVTIIGGGPAGLYSAFYSGLRGLKTKLIESQSQLGGKVLLYPEKLIWDIGGQPPILGEKFVKQLIQQAKTFDPTILTNTKVDFIERQEHLFIVHTATGERHYSKTVLLAVGGGIINPQKLTLEGAEKYEMSNLHYTVQSYKRFVNRDILISGGGNAAIDWAVELSPLAKSVTVVYRKDTLSAHEATVKEAIDAGVLIECNTTITKLLANDDKTAIQLVRCENSKTKESYTRQIDEVIISHGYNCEASLTFDEAISIPKKDDYYFEGKATGETAQPGIFAAGDILSFEGKINLLLGTFQDAANAVNSIKTYLEPTA... | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 38560
Sequence Length: 349
EC: 1.18.1.2
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A9NFF6 | MLEVLIIGAGPTGLYAAFLAGLRNLKAAVIESSAEPGGQLTAVYKDKYIYDIPGFPKITAKDYIDGQVLQYERFKSDLPIYYNEEAIDIKKHDDHFIVTTTTKTIETKFVLIAHGGGGFVPQKLKIDEHYDNILYFIKDLNQFKDKKIVVLGGGDSALDWAIDLSEYTKDVTLVHRRDEFRALQSSVDHFREKGTILTPYIVDTVEGNDKLVHTLVLKHAKTHERLNLDADYIVVNYGFVLTKSRLDEWGIEGEKGLIKVDYTMKTSLDGIYAAGNGIDYPGKVKLISTGQGEAATAIQSITTLLYPEKTRKFEHSTALI... | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 36026
Sequence Length: 322
EC: 1.18.1.2
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A1TRN6 | MENARLIEADAVVIGAGPVGLFQVFQLGLQGIAAHVVDALPHVGGQCAELYADKPIYDIPGVPVCTGRELVALLNRQIAPFSPQLHLSQRVETLQPAPDGGFLFATDAGAALHARTVFIAAGVGAFVPRTLKIDGIERFHGTQVFHHEEPAPTRGRQVVVLGGEDTAVARAIACAEPGPEAAASVTLVHRRDAFQAAPQDLARLQALRDSGRIRVLAAQVTGIEAAAQAGTPEPGRLTGVRLLASDGTEQGLPLDTLLLCLGVSPRLGPVADWGLALERKQVKVDTATFSAGVPGLYAVGDINTYPGKRKLILCGFHEAT... | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 37297
Sequence Length: 358
EC: 1.18.1.2
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A0LT79 | MLIVGAGPAGLYAAYYAGFRAMSVVVLDSLTEPGGQLAALYPEKVIYDVGGIPAILGRELAADLYKQAMTYNPVMLLGHGADQLFRLDDGSFLVTTTTGLLIHAKAIIVTAGIGVFTPRRLPVGQEYEGRGLRYFVPNPQELAGKRILVVGGGDSAVDYALMLEKVAASVTLIHRRHEFRAHEASVEQLRASSVRILTPYQVSAVYGDDRVTAVDVTDHDTKHVERLDVDEIVAALGFVAELGPLAEWGMELRQRHIVVDTTMATSVPRIYAAGDIADYPGKVKLISVGFGEAAIAVNNAAVAIDPSKKLFPGHSSDPDR... | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 34930
Sequence Length: 325
EC: 1.18.1.2
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A1W6V2 | MHPSPSSPTPQAADAVVIGAGPVGLFQVFQLGLQGIAAHLVDALPHVGGQCAELYPDKPIYDIPGIPVCTGLGLVELLQRQIAPFAPTLHLGQQIHALAAQADGRILLTTTAGTALLARSVFIAAGVGAFVPRAIKAEGVEALAPGQLLYHPDAATATRAATGKRVVVHGGDEAAVQAALDCVDAAAQVLLLHRRDAFQAAPAPLAQLQALREAGRIQVVIGQITGVETAPDGTLQALALLDPQGQPQRQPLDLLLAYLGISPRLGPIADWGLAMDRKQLAVDTATFATSVPGIYAVGDINTYPGKRKLILCGFHEATLA... | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 36785
Sequence Length: 354
EC: 1.18.1.2
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Q5PAR7 | MAIIGAGPVGLFTVFQAGMLGMSACVIDALSEVGGQCAVLYPEKPIYDIPAYPVTLARDLVNNLKRQADPFKPTYLLGHTAEQVLEEGEHFVVVTDKKVGVRCRAIVIAAGSGGFGPNRPPLDGITEYEDKSVFYHVSDVSRFRGKRVVIAGGGDSAADWAVSLSEVADSVHVIHRRHSFRCAPNTLRNLESLAERGQIKLLVPYQLAGLAGSDGMLNGVIIRNISSKEETRIDADFLLPFFGISAKLGPIANWGLGVESFYIPIDQSTCRTARTRIYAVGDVAHYQGKLKLILVGFSESALACHDIYKVLFPETPLNFQ... | Cofactor: Binds 1 FAD per subunit.
Catalytic Activity: H(+) + NADP(+) + 2 reduced [2Fe-2S]-[ferredoxin] = NADPH + 2 oxidized [2Fe-2S]-[ferredoxin]
Sequence Mass (Da): 35705
Sequence Length: 329
EC: 1.18.1.2
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Q2FNC9 | MGVALRDILTDLKRPAETDELKGVAAIDAFNALYQFLSIIRQPDGTPLMDDSGRITSHLSGIFFRTANFLTQGIRPVFIFDGKSPEMKGRTIQERRDVREESKEKWDQAKKEGDLAGAFRYAMSSTAIDAYILSSARQLIQLMGLPVVDAPSEGEAQGAYMVLKGDADYVVSQDYDTLLFGTPVLVRNLTISGKRRLHGRQITVQPERIVLSDVLSTLDITREQLIEIAILTGTDFNPGIRGIGAKTGLKKIKSGEFDSIIREKLPDFDPEPVRSFFLNPPVTDSYTLDPGRIDRDGIRAFLCGEHGFSQDRVDPVLDKI... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. Du... |
Q58839 | MGVQFGDFIPKNIISFEDLKGKKVAIDGMNALYQFLTSIRLRDGSPLRNRKGEITSAYNGVFYKTIHLLENDITPIWVFDGEPPKLKEKTRKVRREMKEKAELKMKEAIKKEDFEEAAKYAKRVSYLTPKMVENCKYLLSLMGIPYVEAPSEGEAQASYMAKKGDVWAVVSQDYDALLYGAPRVVRNLTTTKEMPELIELNEVLEDLRISLDDLIDIAIFMGTDYNPGGVKGIGFKRAYELVRSGVAKDVLKKEVEYYDEIKRIFKEPKVTDNYSLSLKLPDKEGIIKFLVDENDFNYDRVKKHVDKLYNLIANKTKQKT... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. Du... |
A5UL52 | MGVKLKDIIQPEQIDFKDLKGRAISIDAFNTLYQFLSTIRQRDGRPLSDSNGNITSHLSGILYRNSSMIEKDIKPIYVFDGTPSYLKQETIDQRRQTREESEKKWKEALAKQDTQEARKYAMRSSKLSPYIIESSKKLLTMMGIPYIEAYGEGEAQAAYLVENGDAWAVASQDYDCLLFGAKRVVRNLAINSNLGDLEYYNLKRVLDELDINREQLIDMGILIGTDFSEGLKGVGAKTALKLAKKGELENKLAKLQEESSHDISEVREIFLNHNVNTNYKIRWKKPAKNDIIDFLCEEHGFSQDRVSKACDKLKNLNSSQ... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. Du... |
Q2NFD4 | MGVKFKDITNPEPIEMKELEGKILTVDASNVIYKFLSSMRQTDGTPLRDLNGHITSHLNGIMFQTSTLIEKDIKPVYVFDGKAPDLKKETQEERINIKKESEKKYLEAKEVGDVVAARKYAARTTHLNKEIIKSSKKLLDLMGIPYVQARTEGEAQASYMVSQNDAWAVVSQDYDCLQFGATRMIRNLKLSKSNSKNLELISLEKTLKELNLTREQLVDVAMLVGTDFNKGVYGIGAKKGIKLIHKYGTLEKALESLNETMEVDAELIREIFLNPNVVHNYTIEFKRPKKSQLLDFLCGEHDFDERRTISAIKKLQAKTA... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. Du... |
O27670 | MGVKLRDVVSPRRIRLEDLRGRTVAVDAANTLYQFLSSIRQRDGTPLMDSRGRVTSHLSGILYRTAAVMEREIRVIYVFDGRSHHLKGETVSRRADIRKKSEVEWKRALEEGDIDRAKKYAVRSSRMSSEILESSKRLLELLGIPYVQAPGEGEAQASYMVKMGDAWAVASQDYDCLLFGAPRVVRNLTLSGKLEDPEIIELESTLRELSISHTQLVDMALLVGTDFNEGVKGIGARRGLKLIREKGDIFKVIRDLEADIGGDPQVLRRIFLEPEVSEDYEIRWRKPDVEGVIEFLCTEHGFSEDRVRAALKKFEGASST... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. Du... |
Q3IPG8 | MGNADLRTLAAIEPKPFDELGGSVVAVDAHNWLYRYLTTTVKFTRSEAYTTADGEEVANLIGVVQGLPKFFEHDVTPVFVFDGGVSDLKADEVEKRRDQRERYEAQLEAAKERDETDAAEIAALESRTQRLTDTIVETTRELLARLDVPVVEAPAEGEAQAAHMARRGDADYVGSEDYDALLLGAPYTLRGLTSNGDPECMDFEATLSTHDLSWEGLVDAAILMGTDFNEGLSGVGPKTAVKLIHEHGDLRSVLAARDDDIPHADRIRELFLDPAVTDDYDYDTDIDPDFERAREFVTETWGVPADEVERGFERIEESVI... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. Du... |
A9A4B0 | MGLNLKDLVVREKTTLEAFSNKVIAIDAYNAIYQFLASIRGPDGLQLSDSEGRITSHLSGLLYRNVNFLSLGIKPVYVFDGKPPSLKTAEIERRKQIKMDATIKYEKAIADGNMEDARKYAQQTTSMKDGMVKESKQLLTYFGIPYIEAPSEGEATAAHLTNTGQAYASASQDFDSILCGAKRLVRNFTNSGRRKIPNKNTYIDIVPEIIETQKTLDSLELTREELIDVGILIGTDFNPNGFERVGPKTALKMIKQHSKLEEIPQIQEQLEEIDYQEIRKIFLNPEVADVKEIVFENVNYEGMSNYLVRERSFSEDRVNS... | Cofactor: Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding.
Function: Structure-specific nuclease with 5'-flap endonuclease and 5'-3' exonuclease activities involved in DNA replication and repair. Du... |
P00240 | AYKVTLKTPSGDQTIEVSPDAYILDAAEEAGLDLPYSCRAGACSSCAGKVEAGTIDQSDQSFLDDDQQGRGFVLTCVAYATSDCTISTHQEESLY | 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): 10065
Sequence Length: 95
Subcellular Location: Plastid
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P00237 | AYKVTLKTPDGDITFDVEPGERLIDIGSEKADLPLSCQAGACSTCLGKIVSGTVDQSEGSFLDDEQIEQGYVLTCIAIPESDVVIETHKEDEL | 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): 9962
Sequence Length: 93
Subcellular Location: Plastid
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P70451 | MGFGSDLKNSQEAVLKLQDWELRLLETVKKFMALRIKSDKEYAYTLQNLCNQVDKESTVQVNYVSNVSKSWLLMIQQTEQLSRIMKTHAEDLNSGPLHRLTMMIKDKQQVKKSYVGIHQQIEAEMIKVTKTELEKLKSSYRQLIKEMNSAKEKYKEALAKGKETEKAKERYDKATMKLHMLHNQYVLALKGAQLHQSQYYDTTLPLLLDSVQKMQEEMIKALKGIFDDYSQITSLVTEEIVNVHKEIQMSVEQIDPSTEYNNFIDVHRTTAAKEQEIEFDTSLLEENENLQANEIMWNNLTADSLQVMLKTLAEELTQTQ... | Function: Tyrosine-protein kinase that acts downstream of cell surface receptors for growth factors and plays a role in the regulation of the actin cytoskeleton, microtubule assembly, lamellipodia formation, cell adhesion, cell migration and chemotaxis. Acts downstream of EGFR, KIT, PDGFRA and PDGFRB. Acts downstream o... |
P85121 | ATYYKVKLLTPEGEKEFECPDDVYILDNAEEIGIDLPYSCRAGSCSSCAGKVVSGKVDNSDNSFLNDDNMDAGYVLTCHAYANSDVVIETHKEEEV | 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): 10521
Sequence Length: 96
Subcellular Location: Plastid
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O04166 | MAAAAMTSIVPVASIAPVSKVANVRPSSVSVAKAFGLKSRSMGRLTCMATYKVTFLDGETGAENVVECSDEEYVLDAAERAGMDLPYSCRAGACSSCAGIIKAGEVDQSDQSFLDDSQIDDGFVLTCVAYPASDCIILTHQEENM | 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): 15217
Sequence Length: 145
Subcellular Location: Plastid
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Q8IED5 | MNIVILLLILTFSIKHSNTYKLKNTYIPINYMYHNNKNILRSQKSKLFLNFLSNNQLANSNKQTCFFKSNIKSSISNIDNYDYIRKRYINTSNKNKLFYNITLRTNDGEKKIECNEDEYILDASERQNVELPYSCRGGSCSTCAAKLVEGEVDNDDQSYLDEEQIKKKYILLCTCYPKSDCVIETHKEDELHDM | Cofactor: Binds 1 2Fe-2S cluster.
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions . By transferring electrons to 4-hydroxy-3-methylbut-2-enyl diphosphate reductase LytB/IspH, plays a role in the terminal step of the DOXP/MEP pathway for isoprenoid precurso... |
P18820 | AKKYKVRLLSEAEGIDVTIDSADDVYILDAAEE | 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): 3641
Sequence Length: 33
Subcellular Location: Plastid
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P34806 | MVSGVSRNAARTSSGCIVALVSTDDDYTSQDVTTIPQAIRFPSSCLVTYSCVSCYLAIPSGKLHAASSFEHVLECTVAPVSEYVKSVFVGSSIECTGRSGSVTFALV | 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): 11179
Sequence Length: 107
Subcellular Location: Hydrogenosome
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O15552 | MLPDWKSSLILMAYIIIFLTGLPANLLALRAFVGRIRQPQPAPVHILLLSLTLADLLLLLLLPFKIIEAASNFRWYLPKVVCALTSFGFYSSIYCSTWLLAGISIERYLGVAFPVQYKLSRRPLYGVIAALVAWVMSFGHCTIVIIVQYLNTTEQVRSGNEITCYENFTDNQLDVVLPVRLELCLVLFFIPMAVTIFCYWRFVWIMLSQPLVGAQRRRRAVGLAVVTLLNFLVCFGPYNVSHLVGYHQRKSPWWRSIAVVFSSLNASLDPLLFYFSSSVVRRAFGRGLQVLRNQGSSLLGRRGKDTAEGTNEDRGVGQGE... | Function: G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyr... |
Q8VCK6 | MTPDWHSSLILTAYILIFLTGLPANLLALRAFMGRVRQPQPAPVHILLLNLTLADLLLLLLLPFRIVEAASNFRWYLPKIVCALTGFGFYSSIYCSTWLLAGISMERYLGVAFPVQYKLSRRPLYGVIAALVAWIMSFGHCTIVIIVQYLNSTEQVGTENQITCYENFTQEQLDVVLPVRLELCLVLFFVPMAVTIFCYWRFVWIMLTQPHVGAQRRRRAVGLAVVTLLNFLVCFGPYNMSHLVGFYLRQSPSWRVEAVVFSSLNASLDPLLFYFSSSVVRRAFGKGLLLIRNPASSMLGRGAKETVEGTKMDRGGSQAE... | Function: G protein-coupled receptor that is activated by a major product of dietary fiber digestion, the short chain fatty acids (SCFAs), and that plays a role in the regulation of whole-body energy homeostasis and in intestinal immunity. In omnivorous mammals, the short chain fatty acids acetate, propionate and butyr... |
Q7TMA4 | MSPECAQTTGPGPSHTLDQVNRTHFPFFSDVKGDHRLVLSVVETTVLGLIFVVSLLGNVCALVLVARRRRRGATASLVLNLFCADLLFTSAIPLVLVVRWTEAWLLGPVVCHLLFYVMTMSGSVTILTLAAVSLERMVCIVRLRRGLSGPGRRTQAALLAFIWGYSALAALPLCILFRVVPQRLPGGDQEIPICTLDWPNRIGEISWDVFFVTLNFLVPGLVIVISYSKILQITKASRKRLTLSLAYSESHQIRVSQQDYRLFRTLFLLMVSFFIMWSPIIITILLILIQNFRQDLVIWPSLFFWVVAFTFANSALNPIL... | Function: G-protein-coupled receptor for long-chain fatty acids (LCFAs) with a major role in adipogenesis, energy metabolism and inflammation. Signals via G-protein and beta-arrestin pathways . LCFAs sensing initiates activation of phosphoinositidase C-linked G proteins GNAQ and GNA11 (G(q)/G(11)), inducing a variety o... |
S0ECT9 | MVPSLITPPPSRSGEATPQKDACLNPVNIAEPEGHWIKLPEALFSSIMAVEPEVNPLYRTSKALSDEWLKTALRMNDKTAVIWSRLDIAYMSAICAPHADLETLKLMNDWNGWVFAFDDPFDEGTFANDPIKAAEEVIYTLATLDNIHPVVSPDENPLRHTLQSCWMRFRERSSPSLQYRWKKHLTMYCVGVLQQVGVQHRATRPTIEEYMDMRAGCVGAYPCIGLMEFAEGIDIPQNVMDHPSMQAISRITCDLVTLQNDLCSYRKDLIQGEESNIIFILKDQGMTDQQAVDQIGEMLYDCYRRWHMALANLPFWGEGI... | Cofactor: Binds 3 Mg(2+) ions per monomer.
Function: Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to the sesquiterpene koraiol.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O = diphosphate + koraiol
Sequence Mass (Da): 41636
Sequence Length: 365
Domain: The 2 conserved active-sit... |
S0EGZ9 | MPHKDLPIRPLVRAFDPVGPDTLGPPDLDFASLFRERNVPEDAPLTLYPEQLNVPWHTSLPWTRQSKWWVQGEAAGRDLVNRISADKASERGALPVEFMDERRKGKIDELVEDAVSCAVYLYPSSSPTRIELLTQALLLLFFHDDVMERGATQDDATVCDDFVTMIPKNKHMKRYFAEVLECDPILGPGLLRAIGLFVNAGRKKSPFKQDKYATLAEYLDYRRHDIAKPFMIAAIRFGSGVRQTPEETAPFAELEDLYVQHSILINDLYSYDKEMYEARTINGSVVNAVHVIEKLMCVPPHLAKTITRTMSFDVEKKYYA... | Cofactor: Binds 3 Mg(2+) ions per monomer.
Function: Terpene cyclase that catalyzes the cyclization of farnesyl diphosphate (FPP) to the spirocyclic sesquiterpene alpha-acorenol.
Catalytic Activity: (2E,6E)-farnesyl diphosphate + H2O = (-)-alpha-acorenol + diphosphate
Sequence Mass (Da): 42495
Sequence Length: 371
Doma... |
A0A7L8UVG6 | MTQIKLLLLSLAITAQSITYDLPSQWDHQWLTQQPLGSDTTCTTSHLTAFQMSKTKDPIFFSTGGTDPFLSPKMLPLNSTAGEQWEFDGVSPDAKMAFVFGFYRDPNYAILGSGNLRVSVEMLWPNGTRFAQVDYPTDSVIEECEWGTRGVWRADEFSYSFEVSRDLQTARVAMHTPQVTGVVYLDSESKPRYPDGKIYPSETSTSEALPYFHFVEPIPVAKSQVDLMILGESYVWSDGVGGMERLWGAFSWFTCLQGMNVVRLHAGPYALSLLSFTSNIKKGNEYPSIALFENGEPVFSSQRTEDSDTADYFTFTKTYD... | Function: Diels-Alderase; part of the gene cluster that mediates the biosynthesis of the cytotoxic leucine-containing cytochalasans, including aspochalasin C, aspochalasin E, TMC-169, flavichalasine F, aspergillin PZ, aspochalasin M and flavichalasine G . The first step in the pathway is catalyzed by the hybrid PKS-NRP... |
A0QNG6 | MQGLVLQLTRVGFLLLLWLFIWSVLRILRTDIYAPTGAVMVRRGLALRGSLLPNRQRRHVARQLVVTEGALAGTRITLGNQPVLIGRADDSTLVLTDDYASTRHARLSPRGSEWYVEDLGSTNGTYLDRAKVTTAVKVPIGAPVRIGKTVIELRP | PTM: Phosphorylated by PknB (By similarity). Dephosphorylated by PstP (By similarity).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17125
Sequence Length: 155
Subcellular Location: Cell membrane
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P35077 | MTDATNRFRPGLVGRALVRAGLLFAVAACAQAQLLPGARDLNRIDDRQRKEQLQRDIERALTRPPVELNPQSEAAAPARKPDATSGHTVTVHAVDLDFGVEGRLFDPAPLVQDYLNRPLDNEQLFLLVKALSAALYDRGYATSIVTFVPPGVVDGVLKLKVEWGRIKGWLIDGKPLEGTRDRMMVFSAMPGWQDKVLNVFDIDQAIYNINNGGKTGNITIVPADEYGYSYLDLQLQRRALPRVSLGMDNSGPGTPENGRYKYNASVTANDLLGLNDTLGLYIGNRYYRDAGHDAERNYDLMYSVPLGRTRLDLQTGYSTY... | Function: Member of a two partner secretion pathway (TPS) in which it mediates the secretion of filamentous hemagglutinin FHA (fhaB).
Sequence Mass (Da): 64446
Sequence Length: 584
Domain: In the crystal structure alpha helix H1 passes through the middle of the pore with its C-terminus in the periplasm and loop L6 also... |
Q54D73 | MLSQKSIQIIKSTVPLLEKYGVEITSLFYKNMFEAQPQFLNIFNHSNQRNQKQPVALANTILQSAIHIEKLNEINLMPIVHKHVALGITPEMYPIVGAHLLGAMKTVMQDEATPEIMAAWTEAYRAVAQAFMDAEEDLYFETEEQIGGWKDTREFVVDRIEEETPLIKSFYFKAYDGKEIATYIPGQYITVKITLPGDGVDVPTDKMRTYVRHYSLSDKPNDEYYRISIKKELGKNTPNGIVSNHFHNNIKVGDVVPMSVPAGDFVVNNDSETPILLICGGVGINPLFSMLKETLVQQPDRKINFIFSTHCESSQPFKEE... | Cofactor: Binds 1 FAD per subunit.
Function: Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the cell from various noxious nitrogen compounds. Therefore, plays a central role in the inducible r... |
Q9JXV4 | MNRTAFCCLSLTTALILTACSSGGGGVAADIGAGLADALTAPLDHKDKGLQSLTLDQSVRKNEKLKLAAQGAEKTYGNGDSLNTGKLKNDKVSRFDFIRQIEVDGQLITLESGEFQVYKQSHSALTAFQTEQIQDSEHSGKMVAKRQFRIGDIAGEHTSFDKLPEGGRATYRGTAFGSDDAGGKLTYTIDFAAKQGNGKIEHLKSPELNVDLAAADIKPDGKRHAVISGSVLYNQAEKGSYSLGIFGGKAQEVAGSAEVKTVNGIRHIGLAAKQ | Function: A bacterial surface lipoprotein that binds host (human) complement factor H (fH, gene CFH), binding contributes to the avoidance of complement-mediated lysis by N.meningitidis. Binding of fH to the bacteria surface is independent of bacterial sialic acid moieties . fH binding affinity is high enough that it m... |
C5B137 | MLTRIHGGRVVDPTAGRDAVGDVWIEDGRVVAPSERAPDQTIDATGCVVMAGGVEVHSHIAGGNVVMSRLLLPDLYVSESAPNGHPFAHAGGSGSWIGANYARMGYTTAVEPALPPSNALATHLELADIPLLDRGGLAVLGNDDHLLQLLRDGEGKQAVRDLVQQTLAHSRGLGVKCINAGGASAFKDGVLKLSLDDEIPCYGLSTRKIMSALLDAVEEIGVPHPLHVHCNNLGLPGADDSLVATLEAAEGRRIHFAHAQFYAYGVVDPENPMTGGFRSAAERINAAMEAHPNATYDVGQVVFGQTVTISLDILRQFGGR... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Involved in the transformation of 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) and formate via the formylmethanofuran (formyl-MFR). May be catalyze the hydrolysis of formylmethanofuran (formyl-MFR) to yield formate and MFR.
Catalytic Acti... |
C5B138 | MAAWVKGGAADVDAAVEAAADLLAASRVPVLAGLSAEVSALRAAYRLAETLGASLDPVSGPSVYAELGALSAGGAMSTTRAETIGRADVILIVGNRPWDGELIAEIAAAAPSRGRAAGSERALLSLGGPQNGAIRHVAYAADAGGLTISLGHLRAFAKGHLAGEAAFADLAKRLFAAQYGVIVYDPEEVGELGAEMLQGLIRDLNESTRFFALTLADPFQGRAAVQLSAWTTGQAPRVGFGRHQPEHDSWRFDSARQIAAGEADAALWLASLPAPRPAWLGSLPTIAIVGEGSQEAAGETAEVVITVGVPGQSVGGALWN... | Function: Involved in the transformation of 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) and formate via the formylmethanofuran (formyl-MFR).
Sequence Mass (Da): 37145
Sequence Length: 362
Pathway: One-carbon metabolism; formaldehyde degradation; formate from formaldehyde (H(4)MPT route): s... |
C5B135 | MSTLRLRGDLPERVDLLNITPLALSGLSEAEAGKLAIGTSRRGLTLGDVFEISLDGSDSLVIEGGSARLDRVGAALSQGSIRVEGDVGQRLGEGMAAGSLTVTGSAGPYAGTGATGGTITIEGDAGDHAGGAVYAAKAGLDGATLVIKGAAGDHLGDRMRRGMILAGSAGAFAASRMIAGTIVVSGALGDHPGYGMRRGTLIAGSHGTLLPTFVETGTPDLVFVRLLAQSLKHLGAAQASLLSGTLRRYSGDLATLGKGELFVPA | Function: Involved in the transformation of 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) and formate via the formylmethanofuran (formyl-MFR).
Sequence Mass (Da): 26463
Sequence Length: 265
Pathway: One-carbon metabolism; formaldehyde degradation; formate from formaldehyde (H(4)MPT route): s... |
Q49118 | MSDFTLNGIKVEDTFAEAFDVAGTAIIVTNDTPKWAMIAATVMTGFATSVIGCGAEAGIDAELSPDETPDGRPGVRILLFGFEPNGLKDQLLKRVGQCILTCPGTACFAGVEGPTKIKLGGAIRYFGDGFAVAKRLPDHEGKMRRYWRIPVMDGEFLCEDSVRAVDGAVGGGNLLFLGRKHADTLIVAEIAVEAAKAIPGAILPFPGGIVRSGSKVGGRTKGMMASTNDAYCPTLKGRAGSALPPECGVVLEIVIDALTSAAVAESMRAALHAATEIGAQHGLVAVTAGNYGGNLGRHHYHLRDLLEKPAA | Function: Involved in the transformation of 5-formyl tetrahydromethanopterin (5-formyl-H(4)MPT) to methanofuran (MFR) and formate via the intermediate formylmethanofuran (formyl-MFR). Catalyzes the transfer of a formyl group from 5-formyl-H(4)MPT to MFR to produce tetrahydromethanopterin (H(4)MPT) and formyl-MFR, which... |
P14463 | EDGSGEFLAEGGGVR | 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 ... |
P14536 | TKATEGEFLAEGGGVR | 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 ... |
Q7LZT3 | EDTGTFEEGHGGVR | 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.
PTM: Conversion of fibrinogen to fibrin is trigger... |
P68212 | TNSKEGEFIAEGGGVR | 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 ... |
P14465 | QPSYDYDEEEDDRAKLRLDAR | Function: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) 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... |
P68123 | ATDYDEEEDDRVKVRLDAR | Function: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) 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... |
P68118 | QHSTDYDEEEEDRAKLHLDAR | Function: Cleaved by the protease thrombin to yield monomers which, together with fibrinogen alpha (FGA) 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... |
Q23544 | MSVRRRTHSDDFSYLLEKTRRPSKLNVVQEDPKSAPPQGYSLTTVIIISVLVSLICQHFVPYAVSTLHTVIKNSPKQKSSPPPSNRLNIGFISGNSPEKYAPAVQKPTFLVDPIYDEKWKGIQTAVPVMSTQTDEKRENDPAKVKEAILAAKAAGRSRKDGNLERAMTIMEHAMALAPTNPQILIEMGQIREMHNELVEADQCYVKALAYDPGNSEALVLRARTTPLVSAIDRKMLRSVHDLRDEFNHLQHSTALRRMMRETYFLYVYHTVAIEGNTLSLGQTRAILESGMVIPGKSIREHNEVIGMDAALRFLNCSLLS... | Function: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-274 determines which of the two op... |
B3MK83 | MGATDQALEAESKTTEPPKTPPVPEQHDRPFLGRQANLCHLLVLLFSGGLAAITLHIFTSSNVGWRLRQLHHLPTAHYLQTRDEFAVYSVDELNAFKEFYDRSISDSVGSSYSEAEETNIKEALGALRLAQDMYLAGKDDKAARLFQHSLALAPRHPTVLLRYGEFLEHSQRNIVLADQYYFQALSISPSNSEALANRQRTADVVQSLDERRLESLDSKRDALSAIHESSAALRRAKKEAYFQHIYHTVGIEGNTMTLAQTRSILETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKMEITIKDILELHRRVLGHVDP... | Function: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context (By similarity). The side chain of Glu-252 determines which of the two op... |
Q8SWV6 | MGTEAEQPSPPAQQQDQENPPLCKAQNPKPARLYRFVLIFVAGSLAAWTFHALSSTNLVWKLRQLHHLPTAHYLQTRDEFALYSVEELNAFKEFYDKSVSDSVGASYTEAEQTNIKEALGALRMAQDLYLAGKDDKAARLFEHALALAPRHPEVLLRYGEFLEHNQRNIVLADQYYFQALTISPSNSEALANRQRTADVVQSLDERRLESLDSKRDALSAIHESNGALRRAKKEAYFQHIYHSVGIEGNTMTLAQTRSILETRMAVDGKSIDEHNEILGMDLAMKYINASLVQKIDITIKDILELHRRVLGHVDPIEGGE... | Function: Protein that can both mediate the addition of adenosine 5'-monophosphate (AMP) to specific residues of target proteins (AMPylation), and the removal of the same modification from target proteins (de-AMPylation), depending on the context . The side chain of Glu-247 determines which of the two opposing activiti... |
Q09920 | MNKFFSFPILGLLLTCVRFVVAKERLFEWNVTDVYDVDPDGSGNSRWVIGVNNKWPIDPLVVDYGDQVIIKMTNSLANNRTTSLHSHGLFQKFTPYMDGVPQSTQCEIPPGATFYYNYTALQNGTYWVHSHDMSQYPDGLRTPFIINALEEPYDYDEEYIISMTDWYYTPFNILVPDEFKTWKNPTGAEPVPDTGLFNDTANATFAMEPGKTYRLRFINIGAFNNYDVMIEDHNMTIIEVDGEYTEPQEVSSIHLTVAQRYSVLVTAKNSTDRNYAITAYMDESLFDTIPDNYNPNVTAWLSYNSDASYDLGPDIDEIDS... | Cofactor: Binds 4 Cu cations per monomer.
Function: Could be an iron transport multicopper oxidase, which is required for Fe(2+) high affinity uptake. May be required to oxidize Fe(2+) and release it from the transporter. Essential component of copper-dependent iron transport.
Location Topology: Single-pass type I memb... |
Q54Y27 | MNLSLPLNKDNSGNSGNSGNSGGSVCSSNNTLSPILSNSILSSPISSPRLISSSNNNNNNNNNNNNNNNNNNNNNNNNTINSDSNNNNNINNKPRKAGIQLDSDGCLIKRIIKEGYGEIPPPRSIVTVHYEGYLSNQVLFDSSVQRNSPFTFQMGTKSVIDAIELSISTMKVGQEAEIVTTQRYAFGKLGLPPFIPPNVSVIYKIKLLSYKLKSNDFTNFESLINKSKEEKEIGNQFFQKSNYKKSIRHYVKSIWILNDPEQTLGLNEMENKLLKDTLIILYLNLASCNIKLKDGKRGISNCEKILELGGNTTAKFYYRM... | 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): 40987
Sequence Length: 366
EC: 5.2.1.8
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Q9Y680 | MPKTMHFLFRFIVFFYLWGLFTAQRQKKEESTEEVKIEVLHRPENCSKTSKKGDLLNAHYDGYLAKDGSKFYCSRTQNEGHPKWFVLGVGQVIKGLDIAMTDMCPGEKRKVVIPPSFAYGKEGYAEGKIPPDATLIFEIELYAVTKGPRSIETFKQIDMDNDRQLSKAEINLYLQREFEKDEKPRDKSYQDAVLEDIFKKNDHDGDGFISPKEYNVYQHDEL | Function: PPIases accelerate the folding of proteins during protein synthesis.
PTM: Glycosylated.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 25794
Sequence Length: 222
Subcellular Location: Endoplasmic reticulum lumen
EC: 5.2.1.8
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Q14318 | MASCAEPSEPSAPLPAGVPPLEDFEVLDGVEDAEGEEEEEEEEEEEDDLSELPPLEDMGQPPAEEAEQPGALAREFLAAMEPEPAPAPAPEEWLDILGNGLLRKKTLVPGPPGSSRPVKGQVVTVHLQTSLENGTRVQEEPELVFTLGDCDVIQALDLSVPLMDVGETAMVTADSKYCYGPQGRSPYIPPHAALCLEVTLKTAVDGPDLEMLTGQERVALANRKRECGNAHYQRADFVLAANSYDLAIKAITSSAKVDMTFEEEAQLLQLKVKCLNNLAASQLKLDHYRAALRSCSLVLEHQPDNIKALFRKGKVLAQQG... | Function: Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The ac... |
O35465 | MASWAEPSEPAALRLPGAPLLEGFEVLDGVDDAEEEDDLSGLPPLEDMGQPTVEEAEQPGALAREFLAATEPEPAPAPAPEEWLDILGNGLLRMKTLVPGPKGSSRPLKGQVVTVHLQMSLENGTRVQEEPELAFTLGDCDVIQALDLSVPLMDVGETAMVTADSKYCYGPQGRSPYIPPHAALCLEVTLKTAEDGPDLEMLSGQERVALANRKRECGNAHYQRADFVLAANSYDLAIKAITSNTKVDMTCEEEEELLQLKVKCLNNLAASQLKLDHYRAALRSCSQVLEHQPDNIKALFRKGKVLAQQGEYSEAIPILR... | Function: Constitutively inactive PPiase, which becomes active when bound to calmodulin and calcium. Seems to act as a chaperone for BCL2, targets it to the mitochondria and modulates its phosphorylation state. The BCL2/FKBP8/calmodulin/calcium complex probably interferes with the binding of BCL2 to its targets. The ac... |
O95302 | MAFRGWRPPPPPLLLLLLWVTGQAAPVAGLGSDAELQIERRFVPDECPRTVRSGDFVRYHYVGTFPDGQKFDSSYDRDSTFNVFVGKGQLITGMDQALVGMCVNERRFVKIPPKLAYGNEGVSGVIPPNSVLHFDVLLMDIWNSEDQVQIHTYFKPPSCPRTIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITIPPFLAYGEDGDGKDIPGQASLVFDVALLDLHNPKDSISIENKVVPENCERISQSGDFLRYHYNGTLLDGTLFDSSYSRNRTFDTYIGQGYVIPGMDE... | Function: PPIases accelerate the folding of proteins during protein synthesis.
PTM: Phosphorylated.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 63084
Sequence Length: 570
Subcellular Location: Endoplasmic reticulum
EC: 5.2.1.8
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Q9Z247 | MALGARGWRRRSLLLLLLWVTGQAAPVLGLAVSSELQIQQSFVPDECPRTVHSGDFVRYHYVGTFLDGQKFDSSYDRDSTFNVFVGKGQLIAGMDQALVGMCVNERRLVTIPPNLAYGSEGVSGVIPPNSVLHFDVLLVDIWNSEDQVHIQTYFKPPSCPRTIQVSDFVRYHYNGTFLDGTLFDSSHNRMKTYDTYVGIGWLIPGMDKGLLGMCVGEKRIITVPPFLAYGEEGDGKDIPGQASLVFDVALLDLHNPKDTISIENKVVPENCERRSQSGDFLRYHYNGTLLDGTLFDSSYSRNHTFDTYIGQGYVIPGMDE... | Function: PPIases accelerate the folding of proteins during protein synthesis.
PTM: Phosphorylated.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 62995
Sequence Length: 570
Subcellular Location: Endoplasmic reticulum lumen
EC: 5.2.1.8
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Q10175 | MSKEETLYSVKVDQERVPLFDEDFYKGFRSELSVRFTMAALDPRAKSNDAVTVNVITRLEHPEEDGEESDEELFQEEKFTLCTLKKGSVYQQPIDIIFSPGEEVFFERVGGDIPVYLSGTCIITNIPEEEDSSDLENDFLYGADEFSSDEEEMDDISVTSSEEEEEENGARIEELNSDEEDAEQAEEEILEKPVPKDEVAEKHSKDKLKKEEKEKKTAVDVSDSVNGKKRKTEPAGEGEQTEKKSKSTKTYPKQVLEGNVTVQDKVKGDGPAAKRKKRVSMRYIGRLTNGKVFDKNITGKPFTFNLGLEEVIKGWDVGIV... | 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): 40540
Sequence Length: 362
EC: 5.2.1.8
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Q58235 | MVEKGKMVKISYDGYVDGKLFDTTNEELAKKEGIYNPAMIYGPVAIFAGEGQVLPGLDEAILEMDVGEEREVVLPPEKAFGKRDPSKIKLIPLSEFTKRGIKPIKGLTITIDGIPGKIVSINSGRVLVDFNHELAGKEVKYRIKIEEVVDDKKNIVKEIVKMYVPRLSDVKVTIRNGTVKIELPEFAPFIPNIQTAKMAIANEILKRLEDAEKVSFVETFERKKETKEENK | Function: Catalyzes the cis-trans isomerization of peptidyl prolyl bonds and accelerates protein folding (By similarity). Also exhibits chaperone-like activity .
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 25947
Sequence Length: 231
Domain: Contain... |
O27197 | MAVNKGDFIKIEFTGKVKETGEVFDTTYEEVAREAGLGIKKIFGPIPVVVGGGHLIKGLDEAVIGMEEGEEKHVEIEPEDAFGNRDPKLVQLIPMGEFKRQGIKPYPGMTLTVEGHEGRVLNVSGGRVRVDFNHELAGKTLEYDLKVKEIITDDAEKVKSMIQLHYPSQNMDIDKTEVKIEDGKVIIHMDEMTRFDNRSYMDVTLARFRIARDIWENIEGVEKVEFADVFEKRDMEAEEKEEEVEDAGED | Function: Catalyzes the cis-trans isomerization of peptidyl prolyl bonds and accelerates protein folding. Also exhibits chaperone-like activity . In vitro, can use oligopeptides such as N-succinyl-Ala-Leu-Pro-Phe-p-nitroanilide and N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide as substrates. The PPIase activity is much low... |
Q52081 | MNRLLSVFALGGAVLLAGCVAPTPSPTTRTMRRCCRAPRCRQRPTTVRSTRPVSSRTCTATARRSGWVTSSPSRSMSATSASKNAGSQIAKTSKTDIGLTSLFGSTPNTNNPFGGGDLSLEAGYSGDRATKGDSKATQGNTLTGSITVTVAEVLPNGNHRRARQKWLTLNTGEELVRIAGMVRADDIATDNTVPSTRVADARITYSGTGSFADASQPGWLDRFFISPLWPF | 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): 24489
Sequence Length: 231
Subcellular Location: Cell outer membrane
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Q3IDW1 | MRNIILFAAGTLLLSGCVSTQNSDVVQDDPYYAPMYPEPNVEPAVANGSLFNTYLSNDLYADKKALRTGDIITVKLQESTQASKAAKTETDKQSDAKLDPVIGLGGLPVNIGGDSIQFGIGSDASFKGDSKSNQSNSLAGDISVNVMRVLPNGNLVIRGEKWLTLNSGEEFIRLEGLVRPEDVTADNTVQSNRIANARIQYSGKGQTQEAQSAGWLTRFFSSSLFPF | 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): 24430
Sequence Length: 227
Subcellular Location: Cell outer membrane
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Q8XSW9 | MRILRLAALGTASLLAAACGMLPPPEPIVQGPTTARPPMPVMAPRQNGAIYQEVASGSGGFRGMFEDRRAHMVGDTITIVITENTAASKQTSGSVDRSGSKTTSVPTFAGMNPGVLSLLGVSASDANKFDSKGANGATNNFTATITVTVVEVLSNGNLVVSGEKQMAVGQGTESIKFSGVVNPTTVNNQNTVLSTQVADARMEYRGTGYVAEAQQMGWLSRFFLSVSPF | 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): 23835
Sequence Length: 229
Subcellular Location: Cell outer membrane
|
Q98HD3 | MIRRTLILCAVAALSGCGTNLREVGKEPSLSPVGSGIDGGNTSALYKYPEPPRAPVKKFSLWDDRQSRLFTDPRALSQGDILTVRIKINDRANFKNQNDRSRTANRKLGFDLSAQWDKWSTAGKGAGALNSATDTTADGEIKRSETLELNVAAIVTDVLPNGNLMITGSQEVRVNAELRVLTIAGIVRPADIGAENTIPYERIAEARISYGGRGRISEIQQPAYGQQVLDQVLPF | 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): 25524
Sequence Length: 235
Subcellular Location: Cell outer membrane
|
Q52950 | MRTRITAVLAAGLLAGCQNQAFNEIGRAPAMSPIGSGLQYTQTPQLAMYPKQPRHVTNGYSLWNDQQAALFKDARAINIGDILTVDIRIDDKASFENETDRSRKNSSGFNLGASGQSQTSDFAWSGDLEYGSNTKTEGDGKTERSEKLRLLVAAVVTGVLENGNLLISGSQEVRVNHELRILNVAGIVRPRDVDADNVISYDRIAEARISYGGRGRLTEVQQPPWGQQLVDLVSPL | 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): 25730
Sequence Length: 236
Subcellular Location: Cell outer membrane
|
Q6N2Z5 | MSKSVPLQRIVLVAALMATGGLAGGCSSIDRLAAIGERPALTPIENPTTQPGYKPVQMPMPKPEVASYNANSLWRNGSRAFFKDQRAAKVGDILTVTVNFTDKANIANETQRSRTSKEDSGITDFIGSKTITTPATAVLPGRILTTDSTSSSDGKGSVQRQEALQTNVAAVVTQVLPNGNLVVEGKQEIRVNFEIRELIVAGIVRPEDIQSDNTIDSSKIAQARIAYGGRGQITDVQQPRYGQQVMDVLLPF | 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): 27024
Sequence Length: 252
Subcellular Location: Cell outer membrane
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Q2RQF3 | MRRHSTRKTVARVAVVALAVGVLAGCNTFKRLSEIGDGPAMSGVDNPTLRPDYRPVSMPMPAPMVAEPNPSSLWVPGARSFFKDQRAGEVGDLLTVIVDISNEKATFANNLSRTRGNKEGANLTSFLGFEGTLADVLPDGVDPASLTSFGSDSKHTGNGSMARSETVSMRLAAVVLQILPNGNFVIAGKQEVRVNGELRELTVTGVIRPEDIRSDNTIFWHQIAEARISYGGRGTVTDMVEPRYGQQVYDILFPF | 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): 27550
Sequence Length: 255
Subcellular Location: Cell outer membrane
|
Q5LWX7 | MMQKCLSPKTLIAALVVLSACGRADHLGKAPSFTPNTESPEHVAMLWPGLPLHTQPQRSVDRASLWSGGQNSLLGDQRAMKKGDILTVVIEIDEKAEISNDTNRSRSGSESLGVPHLLGLPQRIDEKLPEGASMSNAVAVDSSSASGGKGSVKRKEKLTLRVAATVVDVLPNGVLSITGSQELRVNFELRELLVSGYVRPEDISRQNEITYDKIASARVSYGGRGQITDVQQPRYGQQVLDMVLPF | 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): 26569
Sequence Length: 246
Subcellular Location: Cell outer membrane
|
Q57QH8 | MQKYALHAYPVMALMVATLTGCAWIPAKPLVQGATTAQPIPGPVPVANGSIFQSAQPINYGYQPLFEDRRPRNIGDTLTIVLQENVSASKSSSANASRDGKTSFGFDTVPRYLQGLFGNSRADMEASGGNSFNGKGGANASNTFSGTLTVTVDQVLANGNLHVVGEKQIAINQGTEFIRFSGVVNPRTISGSNSVPSTQVADARIEYVGNGYINEAQNMGWLQRFFLNLSPM | 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): 24709
Sequence Length: 232
Subcellular Location: Cell outer membrane
|
O85806 | MGNMGTSELLKHIYDINLSYLLLAQRLINDEKASAMFRLGIDETMADALAQLTLPQMVKLAETNQLVCHFRFNESQTIERLTKESRVDDLQQIHTGILLSSHLLQELSSKDASPTKKRA | Function: Functions in complex with FlhC as a master transcriptional regulator that regulates transcription of several flagellar and non-flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the cl... |
P74931 | MMTQGAVLGLIREGVFQVVLLVAPVLCTALVVGLIVAIFQAVTSIQEQTLTFVPKMLTILGMIALLGGWMLTMLQNYTVRLFDIIPQLVRSGPV | Function: Role in flagellar biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 10186
Sequence Length: 94
Subcellular Location: Cell membrane
|
O67773 | MDKVTSEEFLITLLLSYFRIVSFLFTFPFYGSFLIPNTIRLYLAFALSFAVLSFINITPVKVNTFVEFLVYALNELLFGFSAGLILRLLFDALIIAGELIALHTGLGFLQMFIPGMTQMSLFSGFFTLYGTLIFLSLGGGEFIILGLAESFKRLPVGSFNIFYLNPEVFLNFFYESFRLGVKIAMPLILTALILNLVLAVVNRFIPQMNVFMVGLPLQVSIGLIILLLSLPLITITMSNHFQDFFKVFEYFIQSFKSP | Function: Role in flagellar biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29178
Sequence Length: 258
Subcellular Location: Cell membrane
|
P35537 | MNSIIDLFPAFLLVFIRISAFFVTIPLFGHRNVPAVHRIGFAFFLAVICFSTIDKPPSLEIDEHYMLLAFKEALVGLCLGLIAYMMIAAVQIAGSFIDFQMGFSIANVIDPQTGAQSPLIGQFIYTMALLFMLSVNAHHLLLDGIYYSFQYISVDQAFPNFGDEKFAYFIAKSFNAMFIIAFQMSAPVVASLFLVDLALGIVARTVPQLNVFVVGLPLKIAVSFIMLIVCMSVIFVVVRNVFSLTIETMRNLLALVGVS | Function: Role in flagellar biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28636
Sequence Length: 259
Subcellular Location: Cell membrane
|
Q44907 | MYYWDEILNLNFLVLKSFTILPVLVRIFMFLKFSPFFSTIKIGYFNFFFSLILSVIVVEKIKIIYPLDNMLSFALILLGEAILGLIQAFFVNIIFNVFHLVGFFFSNQIGLAYANIFDVFSEEDSMIISQIFAYLFLLLFLSSDFLLRFFVIGIHDSVLNIRVEHLVNMRNSGFVKLLLMSFGFLFEKALLISFPILSLLLLFYLVLGILSKSSPQINLLIISFSTSLFLGLLILYIGFPSLAISSKRVIELSLDSLASFLKLFSRVLK | Function: Role in flagellar biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30876
Sequence Length: 269
Subcellular Location: Cell membrane
|
P57186 | MLTFNSLQLITLISNFFWPMIRVLSFFSVAPIFKEKLINRKSKILLSGMISWLVWPFLPEVHTVLFSYFGFLLILQQILIGIVLGFTAQLLFATINLSGEIIGLQMGLSFATFFNNNSQIGTSIISRFLNILALFVFITLNMHLYLISIVIDSFYSMPIDGYFLNVNIFFILLKFSSSIFLNGLLLVLPIMIILLSISFVMSLLNRLSPQISIFSIGFPLNLILGMLMLYFLIPVMLPFLKKILDDLIFFMNNNLLHI | Function: Role in flagellar biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29518
Sequence Length: 258
Subcellular Location: Cell membrane
|
Q89AZ0 | MFQFNFNDFILFIYNLFFPAVRILALFSTAPLFNSKFIEKKIKLIMAFVISWIFSSFLPKVNIAIFSVDGILIIIEQMLIGILLGLTMQLIFSSIFMSGEIISLQMGLSFSSLFDFNSRSNLSALSHFVHIFLLLLFLEWNGHIWMLSALFDTFITIPIQKIYLDPNIFLKVVNFSKYIFFDSIMLLFPIIIVQLLLNLSIGILNRVAPQISILSLGFTVTLLVGIILLYFFIPIFPSSCIVIFRRLQSFVLTLFNS | Function: Role in flagellar biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29536
Sequence Length: 257
Subcellular Location: Cell membrane
|
Q45975 | MNAFATAFQVYVAALVFARVGAMVMTMPGIGDQAIPARIRLSFALLMALILAPLVQNTVGPIPSTLGGLGGAVIHEVLIGLMIGSVLRLFMTSLTTAGEIISMQTTLSFAQSTNPSMEGSSTAVATFLSMLGLTLVMATDLHHLFIAAIVKSYTIFPFTRAVPVNDAAALAVQTVAQSFSLGVQLAAPVIVFSLVFNLATGLVGRIMPAFQIFFVASPLSVILGLSLLALSLSGIAMVWTDRYRELLDIFT | Function: Role in flagellar biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26413
Sequence Length: 251
Subcellular Location: Cell membrane
|
P33135 | MLQVTSEQWLSWLNLYFWPLLRVLALISTAPILSERSVPKRVKLGLAMMITFAIAPSLPANDVPVFSFFALWLAVQQILIGIALGFTMQFAFAAVRTAGEIIGLQMGLSFATFVDPASHLNMPVLARIMDMLALLLFLTFNGHLWLISLLVDTFHTLPIGGEPLNSNAFLALTKAGSLIFLNGLMLALPLITLLLTLNLALGLLNRMAPQLSIFVIGFPLTLTVGISLMAALMPLIAPFCEHLFSEIFNLLADIISELPLI | Function: Role in flagellar biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28543
Sequence Length: 261
Subcellular Location: Cell inner membrane
|
P54702 | MIQVTSEQWLYWLHLYFWPLLRVLALISTAPILSERAIPKRVKLGLGIMITLVIAPSLPANDTPLFSIAALWLAMQQILIGIALGFTMQFAFAAVRTAGEFIGLQMGLSFATFVDPGSHLNMPVLARIMDMLAMLLFLTFNGHLWLISLLVDTFHTLPIGSNPVNSNAFMALARAGGLIFLNGLMLALPVITLLLTLNLALGLLNRMAPQLSIFVIGFPLTLTVGIMLMAALMPLIAPFCEHLFSEIFNLLADIVSEMPINNNP | Function: Role in flagellar biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28925
Sequence Length: 264
Subcellular Location: Cell inner membrane
|
P74932 | MERSFDALFSQASLFFLAAVRVFALMFTVPLLSVRSVSRVVRVALAGLIAFLVLPLAYPAPMQVREFSAYYVLLLLGEGLLGILTGFFISVIFTTFSAAGQFFSYQMGFGTSEMYDTFAQIENPLMGQFLNFVAMLVFLQIKGFQILFLGGVLRSFQAVNCFVFLRKQEALLLFFTKALSALFLHAMTIALPIMGALLLIHVSMGLLTKAAPQMNLLSEGLPLTIVVTFVLLSVILPYMINLFVSILFGGFEMFEQLLVKLGKAL | Function: Role in flagellar biosynthesis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29313
Sequence Length: 265
Subcellular Location: Cell membrane
|
P15286 | MIQPISGPPPGQPPGQGDNLPSGTGNQPLSSQQRTSLESLMTKVTSLTQQQRAELWAGIRHDIGLSGDSPLLSRHFPAAEHNLAQRLLAAQKSHSARQLLAQLGEYLRLGNNRQAVTDYIRHNFGQTPLNQLSPEQLKTILTLLQEGKMVIPQPQQREATDRPLLPAEHNALKQLVTKLAAATGEPSKQIWQSMLELSGVKDGELIPAKLFNHLVTWLQARQTLSQQNTPTLESLQMTLKQPLDASELAALSAYIQQKYGLSAQSSLSSAQAEDILNQLYQRRVKGIDPRVMQPLLNPFPPMMDTLQNMATRPALWILLV... | Function: Acts as a regulator of flagellar gene expression by modulating the protein level of the anti sigma factor FlgM upon sensing ring completion or hook elongation. Flk could inhibit FlgM secretion by acting as a braking system for the flagellar-associated type III secretion (T3S) system. Plays a role in hindering... |
Q1EMV2 | MKDGMRVGERFTHDFVVPPHKTVRHLYPESPEFAEFPEVFATGFMVGLMEWACVRAMAPYLEPGEGSLGTAICVTHTAATPPGLTVTVTAELRSVEGRRLSWRVSAHDGVDEIGSGTHERAVIHLEKFNAKVRQKTPAG | Function: Hydrolyzes fluoroacetyl-CoA before it can react with citrate synthase, and thus confers fluoroacetate resistance. Cannot use acetyl-CoA as substrate.
Catalytic Activity: fluoroacetyl-CoA + H2O = CoA + fluoroacetate + H(+)
Sequence Mass (Da): 15257
Sequence Length: 139
EC: 3.1.2.29
|
Q3IUS7 | MKPRAVALVAGGGFAGALCRHGIAVVLPGTFPWGTLVVNVAGAFLLGAIVYGTERLRSVPESTRLVVATGFLSSFTTYSTFAGETIALAPRLAALNVVGNYALGFVAVLVAREVIRWRS | 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): 12393
Sequence Length: 119
Subcellular Location: Cell membrane
|
Q1QRN0 | MKWTFILAVAAGGSLGSVARYLVGIGFGRLLGPKFPWGTLFINITGSLLIGLFAGLFAIRWNLPQAVRIFLIVGICGGYTTFSTFSLDSFYLIERGEVAAAGAYMIASVVLSVGALIAGIQIVRVL | 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): 13333
Sequence Length: 126
Subcellular Location: Cell inner membrane
|
Q5YR86 | MVRRRHDGRGSDDRPTVRGGARVNIALVLLGGMLGAPVRYLIDRAVTARIDSPLPLGTLTVNIVGSAVLGGLIGASANGWLLTAAGTGFCGALTTFSTFGYETIRLVTDGAYGYALGNVVISVAASVGAVYAAVSLTNWVTP | 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): 14521
Sequence Length: 142
Subcellular Location: Cell membrane
|
Q318B0 | MKIKIYIYILLACYIASFLRLFINNNFIVSIIGSLLFGFFIDKRLSYSIEKIILSGFFSCFTSFSGFIYFLYKVFNQGDLMKFIIFCNLIIIINLLVMYFGFWISRKIT | 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): 12905
Sequence Length: 109
Subcellular Location: Cell inner membrane
|
Q7V9N6 | MHSKLNIQSKQLYKIFLLIVGSILGAILRWKLNNYFWVNISGAALLGLIVGLRAGSRIQFFLVIGFCGSFTTFSGWILDVFDLFRTGFFWKAAGLICSNLLGGFTALSVTFWIGRKIRHLFIPQ | 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): 13979
Sequence Length: 124
Subcellular Location: Cell inner membrane
|
Q46IH8 | MGIDIKNNTFFLISLGAFLGALFRWQIDEIFIVNLIGCFLLGFFNSLNILKRYKLTLCVGLCGSMTTFSSWMSHLYKLLNQGLYKLFLLNSLSIVLMGVLSIALGHIFAKRLNA | 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): 12845
Sequence Length: 114
Subcellular Location: Cell inner membrane
|
Q0S2P9 | MCAVSLTKPVAVVALGGALGASARFLLAELWPGIWTVLLINVVGSLLLGYLAETVGPDRLSRLFLGVGVLGGFTTFSTFAVDAVREDAVTATLYVVATLIPALLAARLGMLAGHRHRLARKAVA | 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): 12870
Sequence Length: 124
Subcellular Location: Cell membrane
|
Q214E8 | MSLDELRDRAALYALIAAGSVIGGCARYLVGVAQLSLLGTDFPWATLFVNVTGSFVIGFYAAIAGPDGRLFASSRQRQFVMTGICGGYTTFSGFSLETFQLLRTGHALAALINLGVSPMSWLVAVWLGHLVATRLNRLKGT | 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): 15033
Sequence Length: 141
Subcellular Location: Cell inner membrane
|
Q1AYN2 | MAPAELALTLAAAGAGSVLRYLLGGWVAHRMGPEFPWGTLAVNALGCLGLGLLQGAAPHDRALLLVLGSGLLAGFTTFSTLMLETANLATAGERDRAFSNIVGTLALGLFALSAGARAGAWAAG | 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): 12403
Sequence Length: 124
Subcellular Location: Cell membrane
|
Q82LR8 | MRADESGPERESREPTHIPGAEPELGGEPTPRGEPGPGFEPGPGGEPAPSRAPFRSRLRKGVLAAVALGGVLGGSARYALGLTFPTPRGTFPVTTFAVNVSGAFLLALLLVYVLEIWPPTRYVRPFAAVGFLGSFTTFSTWMVDTDRLLGHGHYAVAAFNVFGSLFAGLAATGLGLAIGRMALARRVRLAARHGRARRYGWWVR | 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): 21754
Sequence Length: 204
Subcellular Location: Cell membrane
|
Q8ZDB1 | MTAIDVMWVGLGGGIGSLLRWWIGLSIGKVYKGNFPLGTFLINISGAFVIGYLSILFSVDWRDRYGDLMNTAVLTGILGGYTTFSSMQLDAAKLATARGRAIAAGYLIISVLVGLAAAAFGAWLAY | 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): 13345
Sequence Length: 126
Subcellular Location: Cell inner membrane
|
A1TSC2 | MLLNIAVICLAACVGALMRWGFALWLNPGGLIPWGTLAVNLIGGYCIGIALAVFTSRPDIDPAWRLLVITGFLGTLTTFSSFSGEVVTMLMQQRFGLAFGTIALHLGGSLALTWAGMRSALWWLAR | 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): 13514
Sequence Length: 126
Subcellular Location: Cell inner membrane
|
Q6FF10 | MYSSLLSIACGAVLGAWLRWFVGLKFNSTFQNFPLGTILVNLVGGFIIGFAIALFANMQLSSNYKLFVITGFCGALTTFSTFSAEVIDLLQQQKYGFAIALITIHLMGSLLCTVLGLLSYQWLSQH | 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): 13799
Sequence Length: 126
Subcellular Location: Cell inner membrane
|
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