ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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A9HKQ4 | MRLAFMGTPDFAVPALHALHEAGHEIAVVYSQPPRPAGRGQAVRPQPVHLAAEALGIPVRVPTRLRANHDEHAFFRALDLDAAVVAAYGLILPGAMLTPRAGARLNVHASLLPRWRGAAPIQAAILAGDDESGVTIMQMDEGLDTGAMLLTGRVALTPATTASTLHDDLAAMGGRLIVAALANSETAAIPQPAEGATYAARLTREDGRIDWTRDAVDIDRQVRALTPWPGTFTTLDGTVLKIGAATPIDGPRDAVPGTVLDDRLTVACGQGTLRLTRIQRPGRGMMEADAFLRGQPVPVGTRLGS | 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... |
O85732 | MSQALRIVFAGTPEFAAEHLKALLDTPHRIVAVYTQPDRPAGRGQKLMPSAVKSLALEHGLPVMQPQSLRNAEAQAELAALRADLMVVVAYGLILPQAVLDIPRLGCINSHASLLPRWRGAAPIQRAVEAGDAESGVTVMQMEAGLDTGPMLLKVSTPISAADTGGSLHDRLAALGPKAVIEAIAGLAAGTLHGEIQDDALATYAHKLNKDEARLDWSRPAVELERQVRAFTPWPVCHTSLADAPLKVLGASLGQGSGAPGTILEASRDGLLVACGEGALRLTRLQLPGGKPLAFADLYNSRREQFAAGQVLGQ | 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... |
A8F525 | MKILFLGTPLYASRHLEALLSAGHMVIGVITQPDKPAGRGLRMVHSPVKDLALKNKIPVFESLKDFPFDRLTPDIGIVVAYGGLIKKKFLDLIPFGYYNIHPSLLPKYRGAAPINRALENGEKMTGVSLFKLTEKLDAGPIVLQVEISVDCFETFDSLENRMIEAGKKILCDFLKNPESFELREQDHSQASYAPKITPADLFVDFRKDSEAVKNKIRAYDSRPGARTFFHGEQVKLFGAVAIEKCHSGEPGTIVHIDDKGAYVTTSDGIIVISQIQFPSKKKMSFLSALNGRMLRVKDRFQS | 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... |
Q0IAL3 | MNILFWGTPDYAVPTLMALHQAGHTIVGVVTQPDRRRGRGKTLVPSAVKAKAIKMGLRVFTPERIKQDETCQQQLAELQPDLSVVVAFGQILPKNVLNQPPLGCWNGHGSLLPRWRGAGPIQWSILEGDPETGVGVMAMEEGLDTGPVLIERNLPIGLLDNGHTLAERMSVLTAELMVEAMPLIESAGQGSEPERRARLKVMNQSDRSGDASYARMLTKQDHQIDWSASALNIHRKVMALYPNAVTLWNDKRLKLLHCEPLIDRLREELPAEVHPLIGRWPTGGHPPGTVLESVKGLGVVVSTSGCPILVRAAQLEGKGR... | 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... |
Q0AXL4 | MRIVFMGTSHFAIPSLKALIASEHEIAGVVSQPDKQRGRGRKVTPTPVKEIAEQYKLELLQTANIKTPESIKRIKQWKPELIIVVSYGQIIPLSILEYPRHGCINVHASLLPRYRGAAPVQRALMDGIKSSGITIMFMDEGLDTGDIIMQEAIAVDDNINHGELEKILADMGADLLLQVVDRLVQGEKLPRVVQDDSQASYAARISKEDEIINWSEPAYAIHNRIRALNPQPGAYSYINGTKVKIFASKVRSEAGSGVIAEVIEVDKNTFQVQTGEGILEVLEIQKAGKKRMPTSEFLKGFTLHPGVLLGSKEG | 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... |
Q55163 | MMKTVFFGTPDFAVPTLEALLGHPDIDVLAVVSQPDRRRGRGSKLIPSPVKEVAVQAGIPVWQPERVKRCQETLAKLKNCQADFFVVVAYGQLLSPEILVMPRLGCVNVHGSLLPKYRGAAPLQWAIANGETETGVTTMLMDEGMDTGAMLLKTTTPIGLMDNLTAIGDRLARSGAELLVQTLKDLDAGQLQPIPQTETEATYAPLLKKGDFVINWHRSALEIHNQVRGFAPACHTAWGEQILKIISTVPLGAEFFPLLPEKYQDLATAYLNYSLEAGEPGNIIGTIKNWGPVLETGNGHLLLEQVQPPGKKPQSGWDFI... | 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... |
A6LJK9 | MRILFLGTPDFASVHLEFLMKNGFDVVAVISQPDKPKGRGKKILPTPVKEVALKYNIPVFQPKKLNKEGLKIIENLKPDIGIVVAYGKLLKPPFLNTLEFYNVHASLLPSYRGAAPIQRVLENGEKRTGITIFKIGEGMDDGPIALKKEVEVGEFETFGELYEKLLDLGKKALIEFLNNYPIELIPQEGKVSFAPKITKEDLKLDFSKDVTFVKNKIRAYDPLPGVRVLFKRKIVKLFGVFSVLENSSREIGKIISIDKEGALISCENGSVKVRYIQFPGKRKMTFFEAKNGCLIKEGECFDC | 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... |
Q9WYZ8 | MRIVFVGTPEFAAEILEHLIKNGFNVVGVVTQPDKPRGRGRKVAPTPVKAVAEKHEVPFIQPESINKKEALEFLRSVRPDVIIVASYGKILGEKVLSLPRLGCYNIHPSLLPKYRGASPIQRVLENGEERTGVTIYKMVKELDAGPIALQKEISVDPFETFDQLEKRLIELSKEMLIEFLEKLKTGNIELKEQDHSRATYAPMIKKEDLIVDFSKDAESVKNKIRAYDSRPGARAFLGNVEVKLFGVTAIDSSGDEPGLINYIDREGAWIGTGDGKVKVRYIQFPGKKKMTFWEAKNGRLIIEGMRFERRYES | 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... |
Q5SLH3 | MRVAFFGTPLWAVPVLDALRKRHQVVLVVSQPDKPQGRGLRPAPSPVARYAEAEGLPLLRPARLREEAFLEALRQAAPEVAVVAAYGKLIPKEALDIPPHGFLNLHPSLLPKYRGAAPVQRALLAGERETGVSIMRLDEGLDTGPLYAVWRTPILPDEDAVALGNRLRDKGVELLLEVLERLPELTPRPQEGEASYAPPLSKEEGRLDFGESAEALYRRHRAVQPWPGSYFFHRGQRVKALRLRPEPGEGEPGVVARVGPEGVVVGTASGLLLLLEVQPEGRRAMPAADWARGYGVAPGTRLGQV | 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... |
P0AC25 | MKADNPFDLLLPAAMAKVAEEAGVYKATKHPLKTFYLAITAGVFISIAFVFYITATTGTGTMPFGMAKLVGGICFSLGLILCVVCGADLFTSTVLIVVAKASGRITWGQLAKNWLNVYFGNLVGALLFVLLMWLSGEYMTANGQWGLNVLQTADHKVHHTFIEAVCLGILANLMVCLAVWMSYSGRSLMDKAFIMVLPVAMFVASGFEHSIANMFMIPMGIVIRDFASPEFWTAVGSAPENFSHLTVMNFITDNLIPVTIGNIIGGGLLVGLTYWVIYLRENDHH | Function: Involved in the bidirectional transport of formate during mixed-acid fermentation . Functions to maintain relatively constant intracellular formate levels during growth, using different mechanisms for efflux and uptake of the anion (By similarity). Is impermeable to water .
Catalytic Activity: formate(in) = f... |
P43756 | MASENQKLSSVALTPVEATDYAENTATYKANKRPFLSFMSGISAGACIALAFVFYTTTQTASAGAPWGLTKLVGGLVFSLGVIMVVILGSELFTSSTLTLVARVGGRITTTQMIRNWIVVYLGNFVGGLFIAAVIWFSGQTMAANGQWGLTILATAQHKIHHTWFEAFNLGILCNIMVCVAVWMSYSGKTVTDKAFIMIMPIGLFVASGFEHCVANMFMIPMGIITAHFSTPEFWQQIGVDPMKYADLDLYHFIVKNLIPVTLGNIVGGAICIGVFQRYLTKTH | Function: Involved in the bidirectional transport of formate during mixed-acid fermentation. Functions to maintain relatively constant intracellular formate levels during growth, using different mechanisms for efflux and uptake of the anion.
Catalytic Activity: formate(in) = formate(out)
Location Topology: Multi-pass m... |
P77733 | MRNKLSFDLQLSARKAAIAERIAAHKIARSKVSVFLMAMSAGVFMAIGFTFYLSVIADAPSSQALTHLVGGLCFTLGFILLAVCGTSLFTSSVMTVMAKSRGVISWRTWLINALLVACGNLAGIACFSLLIWFSGLVMSENAMWGVAVLHCAEGKMHHTFTESVSLGIMCNLMVCLALWMSYCGRSLCDKIVAMILPITLFVASGFEHCIANLFVIPFAIAIRHFAPPPFWQLAHSSADNFPALTVSHFITANLLPVMLGNIIGGAVLVSMCYRAIYLRQEP | Function: Involved in the bidirectional transport of formate during mixed-acid fermentation.
Catalytic Activity: formate(in) = formate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30565
Sequence Length: 282
Subcellular Location: Cell inner membrane
|
P46009 | MFFGDGGQLLSDKSLTGSAGGGNNRMKFNILPLAFFIGIIVSPARAELYFNRRFLSDDPDAVADLSAFTQGQELPPGVYRVDIYLNDTYISTRDVQFQMSQDGKQLAPCLSPEHMSAMGVNRYAVPGMERLPADTCTSLNSMIQGATFRFDVGQQRLYLTVPQLYMSNQARGYIAPEYWDNGITAALLNYDFSGNRVRDTYGGTSDYAYLNLKTGLNIGSWRLRDNTSWSYSAGKGYSQNNWQHINTWLERDIVSLRSRLTMGDSYTRGDIFDGVNFRGIQLASDDNMVPDSQRGYAPTIHGISRGTSRISIRQNGYEIY... | Function: Involved in the export and assembly of the F1C fimbriae subunits across the outer membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 96211
Sequence Length: 875
Subcellular Location: Cell outer membrane
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P60622 | MSEMVHSRLKQGQGPAAAQQSFYPPGSPASVHKGATCFECDITFNNINNFYVHKRLYCSSRHQQGETGGLVKEGAVTAAAPPVSHAASPQARPVSRAASASPSCPDPAPGGTASEPKVVEVKIEDPGLKDATCSSSSEGEGPGGGQASEGSQSPSGSAEDQDDDPTRTFCQACNIRFSRHDNYIVHKRFYCASRHDPTNQRPHSGKAAFLPQPIRTRKRKKMYE | Function: Transcription regulator that modulates expression mediated by transcription factors of the GATA family. Cofactor that acts via the formation of a heterodimer with transcription factors of the GATA family. Such heterodimer can both activate or repress transcriptional activity, depending on the cell and promote... |
Q8IX07 | MSRRKQSNPRQIKRSLGDMEAREEVQLVGASHMEQKATAPEAPSPPSADVNSPPPLPPPTSPGGPKELEGQEPEPRPTEEEPGSPWSGPDELEPVVQDGQRRIRARLSLATGLSWGPFHGSVQTRASSPRQAEPSPALTLLLVDEACWLRTLPQALTEAEANTEIHRKDDALWCRVTKPVPAGGLLSVLLTAEPHSTPGHPVKKEPAEPTCPAPAHDLQLLPQQAGMASILATAVINKDVFPCKDCGIWYRSERNLQAHLLYYCASRQGTGSPAAAATDEKPKETYPNERVCPFPQCRKSCPSASSLEIHMRSHSGERPF... | Function: Transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation. Essential cofactor that acts via the formation of a heterodimer with transcription factors of the GATA family GATA1, GATA2 and GATA3. Such heterodimer can both activate or repress transcriptional activit... |
O35615 | MSRRKQSNPRQIKRSLRDMEAGEEAKAMDSSPKEQEAPDPEAPAIEEPPSPPREDVSPPAVPAPPESPEDPEDMEGQELEMRPQDEEKEEKEEEAAMASPWSGPEELELALQDGQRCVRARLSLTEGLSWGPFYGSIQTRALSPEREEPGPAVTLMVDESCWLRMLPQVLTEEAANSEIYRKDDALWCRVTKVVPSGGLLYVRLVTEPHGAPRHPVQEPVEPGGLAPVHTDIQLLPQQAGMASILATAVINKDVFPCKDCGIWYRSERNLQAHLLYYCASRQRAGSPVSATEEKPKETYPNERVCPFPQCRKSCPSASSL... | Function: Transcription regulator that plays an essential role in erythroid and megakaryocytic cell differentiation. Essential cofactor that acts via the formation of a heterodimer with transcription factors of the GATA family GATA1, GATA2 and GATA3. Such heterodimer can both activate or repress transcriptional activit... |
C0R292 | MSNILDGRELAKEIKERIKKETEILEKKPRIDFLYFEDDKSTEVYFTRAKKQAESVGMIGSLHNLPVNTTEKDFLTLIEYLNEESETSGIMIQMPLPKHISKKKVYETISIEKDADAISHVNLGRIFIGDSNLAPCTAKSAMALIEKSGINIEGANAVVIGRSEIVGKPLAHLLLQKSATVTIAHSKTKNLKELCKNADILCVSIGKAEFITGEYIKEGAVVIDVGINVLEDGSLKGDVNFEEASKLASYITPVPNGVGSVTVSMLLDNVLYLHKNIINKK | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
Q8K979 | MSAIIIDGIKIAKKIELNLLKKIEEREKNKKRIPGLAVILIGKNPASEIYVKRKISVCKKVGFISKYWSFPINVDEKDILNLIEKLNNNINIDGILVQLPIPKQINYYKIFSSIRPDKDVDGFHPYNTGSLCQRNPTLRACTPKGIITMLNYTKIKTHGLNAVMVGASNIVGRPMSMELLLAGCTTTVTHRFTKNLRHHIKNADLLVVAIGKPNFLHGDWIKEGAIVIDVGINKLKDGSIVGDVDFKSASLKAAYITPVPGGVGPITVITLLENTLEACEKYHEF | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
B4U8W9 | MNILDGKSLAKKIKHNIKQEVKHLERKPKLVVVLVGDDQASLVYVKNKVQACADVGFSSQLDMFEKDVEEDVLLNHIKSLNEQEDVDGILVQLPLPSHISMQKVIDTIDPSKDVDGFHPQNMGKLFSGDLENAFIPCTPLGIKLLLDEYNIDLKGKNVCIVGAGFIVGKPLSMLMLNYDATVSVCHKYTKDIVEYTKTADILISATGVPFLIKDYMVKEGAVVIDVGISKVNGKIVGDVDFESISQKASFITPVPGGVGPMTVATLLLNTLKAYKQRI | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
Q1II76 | MLATILDGNKISAEIKTEVAAEVAELKAKGLTPGLAVVLVGHNPASEIYVRNKVKACEMTGIYSEQHTPPDTVSTADLLQLVESLNRRNDIDGILVQLPLPKQVDSKKILLAVSPEKDVDGFHPMNVGYLSTVRPGLVPCTPAGCMEILRRSNVPVEGADAVVVGRSDIVGKPIAMLLTNANATVTICHSKTHDLPAVCRRADILVAAIGRPGMITPDFVKPGATVLDVGINKITDRAEFEKFFAGDAKREAAFAKNGSTLVGDCHPKVAEVAGAFTPVPGGVGPLTIAMLMANTVKAAKLRRGNTV | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
C5CI88 | MGILLDGKPVAKMIYAEIKEWLGNLQEKPPKLVLFCSEPDDSTKTYMNSIVKRGGKLGISVEICHAGENPVEEIKKLNESRDVAGVMIMHPLKNVDEKLVVSALSLEKDVEGRTPGNLGGIMTGDESFAPPTAEAVMEILRFYDVSLSGKDVTIVGRSTTVGKPLSMLMLKKGIDATVTICHSRTKNLVEKIKRANVLVSAVGRAGFITKEMVGKDSIIIDVGINLYDGKIVGDVDFEQVEPEVAAITPVPGGVGIVTTAILFRHFMVSSRRMVGRR | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
A8YVX0 | MGKVLDGKTFANLLGQNLKEKVKKLKDEGITPHFCVINIGDDPASKIYVRTKKRRAEKMGIIQDIYQMSADTKQEEAIALIDKLNADPAINGLMVQLPAPKQIDTDALIERIDPNKDADGLTPANIGHLWMDKHFVEPATAEGIIALLKHYEIPLEGKNVVIIGRSNIVGKPLAALMLEQNATVTIAHSRTKNLGEITKKADVLVSATGQAFLVKADMVKDGAVVVDVGMNHVDGKLVGDVDFDNVKEKASYITPVPGGVGPLTVQFLMEAVVKLTRRQNDR | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
Q9CH85 | MNLIDGKALAAKMQAELKVKVDKLKEADNVPGLAVILVGEDPASQIYVRNKARQATAIGLNSSVVRLPETVSEQELLDLIEQYNQSEQWHGILVQLPLPEHISEEKVLLAIDPEKDVDGFHPMNMGRLWSGNPLMIPSTPAGIMEMFREYDVELSGKRAVVIGRSNIVGKPMAQLLMMADATVTIAHSKTENLRELTKEADVLVVAIGRDRMIKAEDVKEGAVVIDVGMNRDEDGKLHGDVDFDEVKDVASLITPVPGGVGPMTITMLMEQTVRAASRKMNENK | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
A5V1H2 | MTAIILDGRALAKTLREELRADTQAFIQNNGIAPSLAVVKIAGDPASDRYTRTIRKGCEEIGITFTDHTLPPETTQAMLEETISALSFDRTIHGILLHLPLPPGLDSARAIAQIDPAKDVDGVHPYNAGLLAMGRPGLIPNTPAGGMELLLRNNIPLKGQHATVVGRSVVVGKPMALLLLNEHATVTIAHSRTKDLAAVVRSADIVVAATGKPGLITGDMVKPGAVVVDFGVNVLEDGRVVGDVDFDSVVNVASAITPVPGGTGPVTNVMLLRNVLRAAQQQLASRHH | Function: Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = 5,10-methenyltetrahydrofolate + NADPH
Sequence Mass (Da... |
O04862 | MSILKCLGVRGNQLCAARNYLKVLGFSSFHTAPNSSIEIQTQDEEVVIALGSNVGDRLHNFKEALKLMRKSGIHITRHASLYETAPAYVTDQPRFLNSAVRADTKLGPHELLAALKRIEKDMGRTDGIRYGPRPIDLDILFYGKFKVRSDILTVPHERIWERPFVMAPLMDLLGTAIDSDTVASWHSFSGHSGGLNALWEKLGGESLIGEEGMYRVMPVANGLLDWSRRTLVMGILNLTPDSFSDGGNFQSVKSAVSQARLMISEGADIIDIGAQSTRPMASRISAEEELGRLIPVLEAVMSIPEVEGKLISVDTFYSEV... | Function: Catalyzes the first two consecutive steps of tetrahydrofolate biosynthesis.
Catalytic Activity: 6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)
Sequence Mass (Da): 56455
Sequence Length: 515
Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amin... |
Q9CGE1 | MNEDLIAEIQALSAIGSEEKFSEIIRLLKNSTLELRGKKNPDLQLSASALVFKKHKLFFIEHPYQKELLLPAGHVELGEKPLETAIREFHEETGFSASESGKLVDVNLINIPYNKIKNEKEHQHIDFRFLLELKEKEAGLAELPFFLLDRTEAPDEFKKYYQYKR | Function: Probably mediates the removal of pyrophosphate from dihydroneopterin triphosphate (DHNTP), a possible step in the pterin branch of the folate synthesis pathway.
Sequence Mass (Da): 19157
Sequence Length: 165
Pathway: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-d... |
O02761 | ERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLSGGLPEAATPESEEAFTLPLLNDPEPKPSLEPVKSISNVELKAEPFDDFLFPASSRPSGSETSRSVPDVDLSGSFYAADWEPLHSNSLGMGPMVTELEPLCTPVVTCTPGCTTYTS | Function: Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex, at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. Has a critical function in regulating the developme... |
Q9FZC4 | MKEALFGLYLVLLVSGLEAAVTKPNSGNFIECLRYQASPENPITDAIFTVDNTTTFLSSYVSYTKNTRFSNPNNKNLLAIVVAKDVSHVQATVVCAKSNGIQIRIRSGGHDNEGLSYVSSVPFVILDMHKLRDITVDVSSKKAWVQAGATLGELYVKIDEASQTLAFPAGICATVGAGGHISGGGYGNLMRKFGTTVDHVIDAELVDVNGKLLNRSTMGEDLFWAIRGGGGASFGVILSWKINLVEVPKIFTVFQVNKTLEQGGTDVVYKWQLVANKFPDNLFLRAMPQVVNGTKHGERTIAIVFWAQFLGRTDELMEIM... | Cofactor: Binds 1 FAD per subunit in a bicovalent manner.
Function: Flavin-dependent oxidoreductase involved in the biosynthetic pathway to 4-hydroxyindole-3-carbonyl nitrile (4-OH-ICN), a cyanogenic metabolite required for inducible pathogen defense. Converts indole cyanohydrin into indole-3-carbonyl nitrile (ICN).
PT... |
P22414 | MSPVDFKDKVVIITGAGGGLGKYYSLEFAKLGAKVVVNDLGGALNGQGGNSKAADVVVDEIVKNGGVAVADYNNVLDGDKIVETAVKNFGTVHVIINNAGILRDASMKKMTEKDYKLVIDVHLNGAFAVTKAAWPYFQKQKYGRIVNTSSPAGLYGNFGQANYASAKSALLGFAETLAKEGAKYNIKANAIAPLARSRMTESILPPPMLEKLGPEKVAPLVLYLSSAENELTGQFFEVAAGFYAQIRWERSGGVLFKPDQSFTAEVVAKRFSEILDYDDSRKPEYLKNQYPFMLNDYATLTNEARKLPANDASGAPTVSL... | Function: Second trifunctional enzyme acting on the beta-oxidation pathway for fatty acids, possessing hydratase-dehydrogenase-epimerase activities. Converts trans-2-enoyl-CoA via D-3-hydroxyacyl-CoA to 3-ketoacyl-CoA.
Catalytic Activity: a (3R)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O
Sequence Mass (Da): 99469
Seque... |
Q01373 | MAEQLRFDGQVVVVTGAGGGLGKAYCLFFGSRGASVVVNDLGASFKGEGNSTKAADVVVNEIKAAGGKAVANYDSVENGDKIIETAIKEFGRIDILINNAGILRDISFKNMKDEDWDLIFKVHVKGSYKTARAAWPYFRKQKFGRVINTASAAGLFGNFGQANYSAAKLGMVGFTETLAKEGLKYNIISNVIAPIAASRMTETVMPPDLLALMKPEWVVPLVAVLVHKNNTSETGSIFEVGGGHVAKLRWERSSGLLLKADESYTPGAIIKKWDQVTDFSNPQYPTGPNDFLALLEESLKLGPNDPGEKVDFKGRVALVT... | Function: Second trifunctional enzyme acting on the beta-oxidation pathway for fatty acids, possessing hydratase-dehydrogenase-epimerase activities. Converts trans-2-enoyl-CoA via D-3-hydroxyacyl-CoA to 3-ketoacyl-CoA.
Catalytic Activity: a (3R)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O
Sequence Mass (Da): 96326
Seque... |
Q02207 | MPGNLSFKDRVVVITGAGGGLGKVYALAYASRGAKVVVNDLGGTLGGSGHNSKAADLVVDEIKKAGGIAVANYDSVNENGEKIIETAIKEFGRVDVLINNAGILRDVSFAKMTEREFASVVDVHLTGGYKLSRAAWPYMRSQKFGRIINTASPAGLFGNFGQANYSAAKMGLVGLAETLAKEGAKYNINVNSIAPLARSRMTENVLPPHILKQLGPEKIVPLVLYLTHESTKVSNSIFELAAGFFGQLRWERSSGQIFNPDPKTYTPEAILNKWKEITDYRDKPFNKTQHPYQLSDYNDLITKAKKLPPNEQGSVKIKSL... | Function: Second trifunctional enzyme acting on the beta-oxidation pathway for fatty acids, possessing hydratase-dehydrogenase-epimerase activities. Converts trans-2-enoyl-CoA via D-3-hydroxyacyl-CoA to 3-ketoacyl-CoA.
Catalytic Activity: a (3R)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O
Sequence Mass (Da): 98703
Seque... |
Q9DBY0 | MMVESASETIRSAPSGQNGVGSLSAQADGGGGAGTAGTAPAAGRDASGREAASGGADSNGEMSPAELLHFQQQQALQVARQFLLQQASSLNSPGNNDSKQSASAVQVPVSVAMMSQQMLTPQQMQQILSPPQLQALLQQQQALMLQQLQEYYKKQQEQLHLQLLTQQQAGKQQPKEALGNKQLAFQQQLLQMQQLQQQHLLNLQRQGLVSLQPSQASGPLQALPQAVCPTDLPQLWKGEGAPGQPAEDSGRQEGLDLASTAVTATSFASPPKVSPPLSHHPLPNGQPTVLTSRRDSSSHEETPSSHPLYGHGECKWPGCE... | Function: Transcriptional repressor that represses lung-specific expression.
Sequence Mass (Da): 85981
Sequence Length: 795
Domain: The leucine-zipper is required for dimerization and transcriptional repression.
Subcellular Location: Nucleus
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Q4VYR7 | MMVESESIRSTPTSQNGVGSLPNQSDSCVGREGSGSGETNGELNPAELLHFQQQQALQMARQLLLQQATCLNSPSTDNKQPSVQVPVSVAMMSPQMITPQQMQQILSPAQLQAVLQQQQALMLQQLQEYYKKQQEQLHLQLLSQQQAGKQQPKELALGNKQLAFQQQLLQMQQLQQQHLINLQRQNLVGLQSGQGPVPMQSLPQVSPSDLHQLLKEMSSSQEESSKQDTVDLMTSITTSFPTTKVSPPTMHPSLSNGQNTRRESTSHYESSHLLYGHGECRWPGCEALCEDMGQFIKHLNTEHALDDRSTAQCRVQMQVV... | Function: Transcriptional repressor.
Sequence Mass (Da): 71245
Sequence Length: 641
Domain: The leucine-zipper is required for dimerization and transcriptional repression.
Subcellular Location: Nucleus
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A1X158 | MARNMNILTLFAVLIGSASAVYHPPSWTAWIAPKPWTAWKVHPPAWTAWKAHPPAWTAWKATPKPWTAWKAPPPAWTAWKATPKPWTAWKAPPPTWTAWKATPKPWTAWKAPPPAWTAWKATLKPWTAWKATPKPWTAWKATPKPWTAWKATPKPWTAWKATPKPWTAWKATPKPWTVWKATPKPWTAWKATPKPWTAWKAPPPAWSAWKATPKPWTVWKATPKPWTAWKATPKPWTAWKATPKPWTVWKATPKPWTAWKAPPPAWTAWKATPKPWTAWKAPPPTWTAWKATPKPWTAWKAPPPAWSAWKATPKPWTAWK... | Function: Provides adhesiveness to the mussel's foot. Mussels produce one of the strongest water insoluble glues. The mussel's adhesive is a bundle of threads, called a byssus, formed by a fibrous collagenous core coated with adhesive proteins (By similarity).
Sequence Mass (Da): 63248
Sequence Length: 561
Domain: Almo... |
A1X159 | MARNMNILTLFAVLLGSASAVYHPPSWTAWIAPKPWTAWKVPPPAWTAWKAHPPAWTAWKATPKPWTAWKAPPPAWTAWKATPKPWTAWKAPPPTWTAWKATPKPWTAWKAPPPVWTAWKATPKPRTAWKAPPPTWTAWKAAPKPWTAWKATPKPWTAWKAPPPAWTAWKATPKPWTAWKATPKPWTAWKATPKPWTAWKATPKPWTVWKATPKPWTAWKAPPPAWTAWKATPKPWTAWKAPPPAWTAWKATPKPWTAWKAPPPAWTAWKATPKPWTAWKATPKPWTAWKATPKPWTAWKATPKPWTAWRATPPPTWTAW... | Function: Provides adhesiveness to the mussel's foot. Mussels produce one of the strongest water insoluble glues. The mussel's adhesive is a bundle of threads, called a byssus, formed by a fibrous collagenous core coated with adhesive proteins (By similarity).
Sequence Mass (Da): 48043
Sequence Length: 431
Domain: Almo... |
Q25460 | TKHEPVYKPVKTSYSAPYKPPTYQPLKKKVDYRPTKSYPPTYGSKTNYLPLAKKLSSYKPIKTTYNAKTNYPPVYKPKMTYPPTYKPKPSYPPTYKSKPTYKPKITYPPTYKAKPSYPSSYKPKKTYPPTYKPKLTYPPTYKPKPSYPPTYKPKPSYPPSYKTKKTYPSSYKAKPSYPPTYKAKPSYPPTYKAKPSYPPTYKAKPTYKAKPTYPSTYKAKPSYPPTYKAKPTYKAKPSYPPTYKAKPSYPPTYKAKPSYPPTYKAKPTYKAKPTYKAKPTYKAKPSYPPTYKAKPSYPPTYKAKPSYPPTYKAKPSYPPT... | Function: Provides adhesiveness to the mussel's foot. Mussels produce one of the strongest water insoluble glues. The mussel's adhesive is a bundle of threads, called a byssus, formed by a fibrous collagenous core coated with adhesive proteins.
PTM: Hydroxylated on second and third proline and last tyrosine residues (t... |
P55044 | MPELPEVETTLRGIAPHIEGKTVEAVVLRQLKLRWQINPDLGEILSGRQVLSCGRRAKYLLIRFQTGVLLIHLGMSGSLRIFTPSDGRIGRPDRHDHVDIVFSDGTVMRYRDPRKFGAILWYEGIEEHHPLLEKLGPEPLSEAFCADYLYARLKAQKRAVKLALMDNAVVVGVGNIYANESLFRAGISPHRPANRLKKKECALLVETVKAVLQRAIETGGSTLRDFVDSDGKSGYFQQEYTVYGRHNQPCPRCGGLVVKETLGQRGTFYCPNCQK | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
Q0AD66 | MPELPEVEVTRRGIDAHLAGRYITQVKIRNYALRWPVSPELITLLPGQRINTITRRAKYLLFACSKGTLIIHLGMSGSLRVLPVSTPSLLHDHFELWLDNEKMLRFRDPRRFGVILWWDGDVRQHPLLQKLGPEPLSDAFNGLFLHEKIQRRSISIKEALMNQHIVVGIGNIYANEALFHAGISPLIAAGSLSTALCARLVDAVKMTLQRAIEAGGSSLRDFTDCDGSPGCFQQQYWVYGRTGQPCRKCGALVSKTRQGQRSSFFCAQCQK | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
Q82S12 | MPELPEVEITRRGIDTHLAGRVITQISIRNPVLRWPISAGLIALLPGQRINAIARRAKYLLFACSRGTLIMHLGMSGNLRVLPESTPPQLHDHFDLQVDNGMMLRFRDPRRFGAILWWDGDIRQHPLLQKLGPEPLSDDFDGQFLYTKTRGRNASIKEVLMNQHIVVGIGNIYANEALFQAGISPLAAAGSLNTMQCERLVDAVKATLLRAIKAGGSSLRDFTDCEGSPGYFQQQYWVYGRAGQSCRQCGELVSKTRQGQRSTFFCARCQH | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
Q5YS09 | MPELPEVEVVRRGLAEHVAGRVVGAVTITHPRSVRRHLAGSADLAARMTGRRVRAAQRRGKYLWLTFDEPGAADETALDAALVVHLGMSGQMLVQPAAAPVEKHAHIRAALDDGSELRFVDQRTFGGWALAPLAEVDGSLVPEPVAHIARDPLDPRFDAESVVAAIRAKNSEIKRVLLDQTVVSGIGNIYADESLWRAGINGNRLASGLTRPAVRRLLAEVRAVMLEALAAGGTSFDALYVNVNGQSGYFERALAVYGRQDEPCRRCGAPIVREKFMNRSSYSCPRCQPRPRRR | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
B2J5G0 | MPELPEVETVRKGLNQLTLNQEITGGDVLLNRTIAYPFSVGEFVDGIEKNAIATWHRRGKYLLAELSSPCSTSWLGVHLRMTGQLLWLHRDEPLHKHTRVRLFFGDQQELRFVDQRTFGKIWWVPPGVAVESIITGLAKLAADPFSPEFSVEYLASKLKNRRRPIKTALLDQSVVAGLGNIYADEALFKSGILPETLCIDLQLKQIELLRTAIIQVLETSIEAGGTTFSNFLNVKGTNGNYGGVAWVYNRAGEPCRVCGMPIQRIRLAGRSSHFCSECQTLRGVENRERRD | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
Q8EPE6 | MPELPEVETIKETLKLFVCNKTIKHIDIEWPNMIKHPDDVEEFKALVTGQTIRSMGRKGKFLLFYLDEYVLISHLRMEGKYSVHSPGDPVKKHTHVTFYFSNGEELRYNDVRKFGTMHVYPIGEEFMHKPLNQLGPDPFDTSFNLEYFYEKLKRTDRYIKTALLDQSIVTGLGNIYVDETLFRANVHPLKRCSKLSKQEVKKLQINAKETLRDAIKAGGTTIRSYVNTQGDMGMFQQDLYVYGQHSKPCRVCGADIIKIKVGGRGTHLCPTCQPNKQGVR | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
Q47S77 | MPELPEVEVVRRGLEKWVVGASFGEVEVLHPRAVRRHAPGAADFAARVSGCGVTEARRRGKYLWLTLDSGEALLAHLGMSGQLLVQPRHAAAERHLRVRLPLTARQGHDPEAPQELRFVDQRTFGHLLVDRLVDDGTGTGLPSVISHIARDPLDPAFDEDAFAAALCRKRTELKRALLDQSLISGIGNIYADEALWMSQLHWATPTEALSRSQVATLLAAVREVMVAALAQGGTSFDSLYVNVNGESGYFARSLNAYGRNDQPCARCGTPIQRETFMNRSSYSCPRCQPRPRHARA | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
B9L1Z5 | MPELPEVETIRRTLAPVLIGALVIGALRGEHPEDILLDPWPVFARRVRRHRIVALERRGKYLAARFEDGDRLVIHLGMTGELRLSHPATAPGKHCHLALVLRSLRPLPPSLVDQRQRFLLRYLDIRRFGRIALLDQAGWETFTARLGPEPLDPTLDPRALWSRLRERRTAIKAALLDQALLAGIGNIYADEALFQARLHPARRCQTLSLDEVERLLVALRTVLSAAIENAGTTIRDYRDGQGRAGSFQSRLQVYGKPAGTPCPRCGTGLARIRIAGRSSVFCPRCQPLH | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
Q9PQ76 | MPELPEVQTIVDYLNHHVLDIFIKKTIVHLPKILKNKTPQEFEKLLINHKIVKIKRLGKYLLFFLSNNLVLSVHLRMEGKFYYQAKEEWFNLAHTHIIIEFNNGMQLRYNDTRQFGTFHIYEQQSFLDSKELKKIALDPLDNNFSAQYLYEKLKKSNKAIKTALLDQSVVSGIGNIYADEILFAAKIFPTILAKNLTLKNYEKITKEAQRILLLSIKNKGTTIHTYKFGNDETGLFQKMLLVHTHAKEPCQICGTIIQKTKVNGRGTYYCPNCQN | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
A5CX90 | MPELPEIETIKRGLTSLIINQKVNKAILHRENLRWVIPKHLSTTLTNQLISTIDRRGKYLLIKFKVGTLIIHLGMSGSIKVVNTNTPLLKHEHFELQLKNGTSMRLKDPRRFGAVLFSKDGSHKLLDSLGVEPLKTSFYDGYLYQKSRNKQQNIKAFIMDNKIVVGVGNIYACESLFMAGINPKLKAGSISKTRYNVLTQCIKNILTQAIEAGGTTLQDFVQVNGNPGYFTQNLSVYGCKNKKCYRCKGIIIKFVQNQRSTFYCKKCQT | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
Q7MPS3 | MPELPEVEVSRMGITPHLLNQTIQSLIFRTPKLRWVIPSELKKLQGQVIRHIGRRAKYLIIETDVGSAIVHLGMSGSLRVLDADFPAGKHDHVDLKLSNGKVLRYNDPRRFGAWLYAAPGEDHDVLGNIGPEPLTDAFDGQYMFEKAQGKRVAVKQFIMDNKIVVGVGNIYASESLFRSRILPTRATMSLSAEEWQRLVSHIKQTLQTAIEQGGTTLKDFSQADGKPGYFAQELQVYGKAGESCPECGEAIQELKIGQRNTFYCSYCQC | Cofactor: Binds 1 zinc ion per subunit.
Function: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG). Has AP (apurinic/apyrimidinic) lyase... |
Q92837 | MPCRREEEEEAGEEAEGEEEEEDSFLLLQQSVALGSSGEVDRLVAQIGETLQLDAAQHSPASPCGPPGAPLRAPGPLAAAVPADKARSPAVPLLLPPALAETVGPAPPGVLRCALGDRGRVRGRAAPYCVAELATGPSALSPLPPQADLDGPPGAGKQGIPQPLSGPCRRGWLRGAAASRRLQQRRGSQPETRTGDDDPHRLLQQLVLSGNLIKEAVRRLHSRRLQLRAKLPQRPLLGPLSAPVHEPPSPRSPRAACSDPGASGRAQLRTGDGVLVPGS | Function: Positively regulates the Wnt signaling pathway by stabilizing beta-catenin through the association with GSK-3. May play a role in tumor progression and collaborate with PIM1 and MYC in lymphomagenesis.
PTM: Phosphorylated.
Sequence Mass (Da): 29093
Sequence Length: 279
Subcellular Location: Cytoplasm
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Q54XL6 | MEINNSNNNNNYVCAQHNRIEHANHHDLPDSDSDSSSREEELMNSSGGGNGKEPIGEKKKLPSHISEVISNERRESIIRELQQIKTISDYPSQANQYNLIEPIGEGTEGRVFKAYCIPLKENVAIKVVELDKMDPQFVKDVIKEVKVMNGNNHPNLIHYHTSFLENNQLWLVMDYLGGGSLADIMKFKYPDGIPEVLAVTVLKSLLKGLEYLHSHQRIHRDLKSDNILIGEDGAIELADFGVSAMFEKNTCCSRKTIVGTPCWMAPEIISERGYNQGVDIWSFGITAIELIRGKPPGYDLPPSKVFMNLLFGNSPSLQEE... | PTM: Undergoes autophosphorylation in the catalytic domain.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 64223
Sequence Length: 574
EC: 2.7.11.1
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Q797E6 | MDVFSEYLAGIADPFHRERTEEVLTWIKNKYPNLHTEIKWNQPMFTDHGTFIIGFSVSKKHLAVAPEKVTIAHVEDDIVKAGYDYTEQLIRIPWNGPVDYTLLEKMIEFNILDKADCSTFWRK | Cofactor: Binds 1.0 Fe(2+) to 1.5 to 3.2 Fe(2+) per monomer .
Function: Plays an essential role in iron intracellular trafficking to iron cofactor biogenesis systems including iron-sulfur cluster (Fe-S) or heme assembly . Promotes the biosynthesis of iron-sulfur clusters by delivering Fe to the complex composed of the... |
Q9LFC6 | MSVGVPVNPSSSSQLPAAPTTTTRRRVADSQEDHSHVNTVGGGNAVVYVPDEEETATSCCGGGGGGGSLSCCPSGSHHNYLVGFLSLRKFRLVWMLMVENKSKWTAGIARNMRSTTNLGRFILTLLSILVVTFFLIVALSGGVGRRRKHVEKHEFVVSIHPRPTIEKIIREDESSNSFQVLVPKTTSIPEIWNQPEVGNYQKCVARPKNQRPIKQTNGYLLVHANGGLNQMRTGICDMVAIAKIMNATLVLPFLDHSSFWSDPSSFKDIFDWKHFIKVLAEDVNIVEYLPQEFASIKPLEKNPVSWSKSSYYRNSISKLL... | Function: Glycosyltransferase required for normal cell adhesion and cell wall integrity.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 71307
Sequence Length: 631
Pathway: Glycan metabolism.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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A0A0S6XHF8 | MVIFKSPLPVGQHQSLEVIAPVGELALNVHLALAKQHEVKPPFIDVMSGKAWHAEEIRDRVDHLARVLAKQFGWQPNVGTPWDKVVAIYSYNTVDFIILSWAVHRLGGLCLLLHSTSSAGEIAAHLKRVQCAAIFTNEPLLATTRKARELLNGEPQKIFILDVANELLPEGHVNSDLTTVEQLAQKGAELEALEPLKWDAVNGRDQVAYLCPTSGTSGAQKLAKVTHGGLLANAVQTVAHELKTNQGKTEVGLNFLPCSHIYGMMLSHTMATRGDCMVLHPFFDLKRVLGSIARFRIERLYLVPSIISALTRNPFLLDMV... | Function: Acyl-CoA ligase; part of the gene cluster that mediates the biosynthesis of the antifungal antibiotic FR901469, an inhibitor of beta-1,3-glucansynthase, exerting antifungal activity against the pathogenes Candida albicans and Aspergillus fumigatus . FR901469 is a cyclic depsipeptide containing 12 amino acid r... |
Q0ZQ46 | MRNDLVLEDTTLRDGEQTPGVAFSKETKTAILNALIEAGVTSIEIGIPAMGGEELDFIKSVVDRQDEARLVVWHRGVREDVERSLDLGFTSVHVGLPTSAGHLKASVRKDRTWLLATARDMVKMAKDRGAFVSISAEDIARTEISFLQEYAGVVAEAGADRLRLSDTVGLLGPEAYGERVAAVLSAADIDVQCHAHNDFGLATANTLAGLKAGARYFHVTVNAIGERAGMADLAQVVVALKKLYDRDLGIDLTKLKKVSRLVAEAAGHQVLPWQPITGDNVFAHESGIHANGMFRDTSSFEPFPPEHVGGERRYVLGKHS... | Function: Involved in the biosynthesis of the phosphonic acid antibiotic FR900098, a potential anti-malarial drug, which acts as a potent inhibitor of 1-deoxy-D-xylulose 5-phosphate reductoisomerase (DXR), the first enzyme in the nonmevalonate pathway for isoprenoid biosynthesis. Catalyzes the condensation between acet... |
A0A0S6XGG4 | MTDSPAPRASVQLIQTGGAAMPLVLIHDACGTIYTYHALSKLGRTVYGIGNPRFEKCTSWTGGIGEMAACYHAAIKQRIRRGKILVGGWSLGGVIALEIARLFADDAAIHVHGVVLIDSPFPSKATVTGEDLQLPPLPPGLPANRRQSVAFAMREAVDLLGDWDPKASWQRADKKPPPAALIRALDYLPGSSADAQRDEFLVDRMRTQKLLGWENSGLDFIRATYEAPGHHWGIFSSENVACLSDTLSKACAELEVVDGGR | Function: Thioesterase; part of the gene cluster that mediates the biosynthesis of the antifungal antibiotic FR901469, an inhibitor of beta-1,3-glucansynthase, exerting antifungal activity against the pathogenes Candida albicans and Aspergillus fumigatus . FR901469 is a cyclic depsipeptide containing 12 amino acid resi... |
A0A0S6XGG5 | MSLPNPFLIRPAPKKGKKGAPLVLLHDGGGTIFSYLQLGALGRDVYGIHNTRPGPTGVWEGGIAQMAAEYLDLIKTVVPSGPIIIGGWSLGGLVSFEMARQMAASAGSSSSSEQLQVLGLIMIDSRHPSTFTDKELVLPDSIKPAIRESIQHNMTQSRQLIRDYSTPSWPQGSQPPPTMFLRATRDLDGVPLPIQADAASSTRNGRMEGWREYEHDFIREVVEVEGTHFSIFEDQNIGELDKKLLAACKTLDRGVKS | Function: Thioesterase; part of the gene cluster that mediates the biosynthesis of the antifungal antibiotic FR901469, an inhibitor of beta-1,3-glucansynthase, exerting antifungal activity against the pathogenes Candida albicans and Aspergillus fumigatus . FR901469 is a cyclic depsipeptide containing 12 amino acid resi... |
A0A0S6XGJ8 | MSQQEAVDAAFLPTLDLSRLVSSDAEERQKLVRACEVYGFFYLDLRSDAELIALWTGVLDLMGQYFNLSLDEKMRDSRNSDTHGYEPVATSTGAQDDLPDYYESLKASRDEVLTQSSKLAPAVKANHALLNRFIERAHAVTMMILRQLSIALELDDSHKFEAFHRHSEESLSTLSMFRYPKQEVLDVGVGHNKHTDIGTLTFLLCQQQGLQVLSKDPVGWRFVQPLPGCAVINVGDTLRFLSGSRFRSAVHRVIPVDQLQRQDRFSIAYFLRAENNATLNAVGGRTVSAKDWHDEKFDVFRKSREAQASDDVLTGGMERD... | Function: 2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the antifungal antibiotic FR901469, an inhibitor of beta-1,3-glucansynthase, exerting antifungal activity against the pathogenes Candida albicans and Aspergillus fumigatus . FR901469 is a cyclic depsipeptide conta... |
A0A0S6XHQ0 | MSFDSIPILDLSLARNEETKPAFLRDLRHTLLEVGFLYIKNTGIPETLISDVIAQGKAFFDLPDEEKLAIEMKNKPSFLGYSRLGMEVTRFKVDWREQLDLSTPHPMPGPDDPLYYNLLAPNQWPSTPGFREVYEDYMTRMGKMSIEFTSLIAEAIGLPADAFDRFFDASQQHKLKIVKYPDLAELGVEGEAQGVGPHKDSMLTSYLLQASHHRGLQVQNHEGEWIDCPPIDGTLVVAVGQGMQALTRGVCLSTTHRVLSPARGAGARYSIPFFQGVSYDATFESMDVPESVTALRDEVQARRGAKQDDVEFTFRPGQWD... | Function: 2-oxoglutarate-dependent dioxygenase; part of the gene cluster that mediates the biosynthesis of the antifungal antibiotic FR901469, an inhibitor of beta-1,3-glucansynthase, exerting antifungal activity against the pathogenes Candida albicans and Aspergillus fumigatus . FR901469 is a cyclic depsipeptide conta... |
Q08908 | MLFARLVLLLVYLAPGSLAKPASTKKRTQWDQIAIDACAKELESHKFDTDVKGRHATLCTYEPALGSWLHCAKDVLDSRKKSKKIFEKTFSKINQYCHDYHKDEVVSNEEYYRIFANASLFIRPLDEVKENIRYPVTPNKASLDRWVWAYFGPLDNIDKGNVYGVTICLYWIGVLFIAAVYHFLNFSRLKQTVFKNKVSAFLRGHYVLPALVHNHAMSVGRWFFIGLVPTRLETLVLFGYVLLHGFLLSSYNFDHNELLSDRRSQVLIFLSDRAGILAFAHFPLIVLFGGKNSTMTWLTGIRYTAFITYHKWLGRFMLVD... | Function: Metalloreductase responsible for reducing extracellular iron and copper prior to import. Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores. Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity... |
Q12473 | MHRTLLFLTWLISLTKAFNIKLPHTEKKDHLESNAVLACASYINTLKWSFDSSVVPGFYSTICSYSPAFDTWSLCIFNSLTDQIIPMDNTSFEESLGNVRKTCSFVDKKFSNISLEQYYSSLNNASSHALEDYGSIESLSTSIRVDRETRSRWIRAFHAHAYNLDISSVYGAYLTYYFVIVGIIAVFFHMSHYNGLNRALFASRFVNYIRGHFVLPTFLVDKHANHFKFLNVEVFTGLMPNSLEAWIIFGYTLANIIFLSISYIIDPYNLIFNSHLSQFTRLLADRSGILAFTQFPLIIIFTARNSFLEFLTGVKFNSFI... | Function: Metalloreductase responsible for reducing vacuolar iron and copper prior to transport into the cytosol. Catalyzes the reduction of Fe(3+) to Fe(2+) and Cu(2+) to Cu(+), respectively, which can then be transported by the respective vacuolar efflux systems to the cytosol.
Catalytic Activity: 2 a Fe(II)-sideroph... |
Q12333 | MIEERDLVLSNGIHCIADIHSELYARLKKESQAATPWVYQKQYGKFVTYFVAVIIFLSLIKKLAFMYYDSSEEFLPEKKNSPTTPSVFLARIMTKLVAFNRYICYRKFPTLIFSYLGIPTSVGTFLVVMATTLYTLLYCFVPHPFYRPCAGFGSPPLSVRAGIMAISLVPFVFSLSGKINVIGWLVGLSYEKINIYHQWASILCLFFSWVHVIPFLRQARHEGGYERMHQRWKASDMWRSGVPPILFLNLLWLSSLPIARRHFYEIFLQLHWILAVGFYISLFYHVYPELNSHMYLVATIVVWFAQLFYRLAVKGYLRPG... | Function: Cell surface metalloreductase. May be involved in copper homeostasis.
Catalytic Activity: 2 a Fe(II)-siderophore + H(+) + NADP(+) = 2 a Fe(III)-siderophore + NADPH
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70905
Sequence Length: 620
Subcellular Location: Cell membrane
EC: 1.16.1.9
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Q75CQ8 | MGGAWQEAVVRSIGAADERMVRLSGWASLALALGLVCVVVPVVNYMRLNPWVFRVMHHWRHHVMRRHGAMCRKLVQQRTLWLALLWCMLGGACAVVGSADVVVVTKRLGRVAAAFMPALFLLTLRPSPLPYTLYLSLLPMHKWLGRVVVLQATVHSALYTWYFATSGKMAKMKKTANWMGAVALLAFVLIAATSLPAVRRRRFRTFYYVHYVGTWVSVLAVHVHSRPPVTTYTVLNVALLLYQAWYRISRMSTTTVTVVPISTSLALLEFPLADLVEKPQLPSGHVRINLRAPSILGRVFQHIMPMQHPFTVASLPTDTT... | Function: Is required for the uptake of Fe(3+) ions. May participate in the transport of electrons from cytoplasm to an extracellular substrate (Fe(3+) ion) via FAD and heme intermediates. Involved in iron homeostasis (By similarity).
Catalytic Activity: 2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-siderophore ... |
Q12209 | MNLKSIVSWFKEHLPSFDVDVDKHFRTLRVRKYSQICLLISFIIICVIIPLMNYLLLTDKFFKICHHLKHHVFNRRSWVHKTHMYHKQSLQLCLICFVFTSFFVIQGANGDLLEITKRMGRISVALMPPLLFLTLRPSPLPHTLYLALLPLHKWISRIVVLESILHTWFYLYYMYINDTLYVKMRKLPNIYGVIALGLFLLIAITSVRYARRWSYRVFYYVHYVSTWLILVFLHYHARPGISYYTTLNVLILTGQIVYRLHITNVTRVTIVPISSSLSLLEFPLTDLPKKPILPGGHLRINIYHRNFLRRFFSHLIPFQH... | Function: Required for the uptake of Fe(3+) ions. May participate in the transport of electrons from cytoplasm to an extracellular substrate (Fe(3+) ion) via FAD and heme intermediates (By similarity). Involved in iron homeostasis.
Catalytic Activity: 2 a Fe(II)-siderophore + H(+) + NAD(+) = 2 a Fe(III)-siderophore + N... |
Q4WR75 | MLLVSCLIILLHLQNALSQIIPPNERCVTAVYTAYEYLSFSGQPNKGLWAPRCRNRLHVLSIYAASDLYCSDAEREAGFAQLDDQCRQYAGVDLIPRQEFAPNLTHEAISQMRVVEFGELPKKGPLDTPILISKSYYSRVFRTIDAWQFELWSHYAFGYLGYAYWTVVIAAGALHKLVLHAISVKRAPSLPPFPFLLLIYYWIQTNLIIPAPLASSRRRLLWWTFPGRIHAIVVLLFWILSIVLCLIGYRTFSDNIYWPDISAQLLRYVADRTGILSFANVPLLWLFAGRNNIFIWATGWSYSTFNIFHRHVAWIATLQA... | Function: Ferric reductase involved in adaptation to iron starvation and which is most likely part of the reductive iron assimilatory system (RIA), a siderophore-independent high affinity iron uptake mechanism .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 84747
Sequence Length: 743
Subcellular Lo... |
Q9ASS2 | MQQGDYNSYYHHQYSQFQNPTPNPNPNPNPSPPAPATVAGPTDLTRNTYASAPPFTGGYGSADYSNYSQNYTPYGQNSEHVPPSAPSFTSPSQPPPSPPATSLNPNSYSTFNQPPPPPTIHPQPLSSYGSFDSTAPYQQPTSQHMYYSPYDQHQTSGYSSAPPPSSAPAPNPNPAPYSSSLYSAPPYSSGGSSIPPSYEKPSVKFDQSGYDGYNRSRSDLGSDLYGKRSDSGEYPAFEDSYGDGVYAYQGGKVEPYGSRGTAPKSSNSTLFDDYGRSISFSSSGRDSSVSSNSAKIVRAVPKADVQEDSTGGVQKFRVKL... | Function: Endosomal sorting complex required for transport (ESCRT) component regulating multivesicular body (MVB) protein sorting and plant growth . Required for the formation of intra-luminal vesicles (ILVs)in MVBs . Binds to phosphatidylinositol-3-phosphate (PI3P) and ubiquitin . Controls IRT1 recycling to the plasma... |
Q8DF91 | MSEEVSKNLSETLFVKHKQAKETSALTQYMPTSQSLLDEIKEKNGFSWYRNLRRLQWVWQGVDPIEQEQVLARIASSKHSRTDEQWLDTVMGYHSGNWAYEWTRLGMEHQKRAGEMTNEAASEALFSASLCYSIAGYPHLKSDNLAIQAQVLANSAYLEAAKKSKYIIKQLEIPFEKGKITAHLHLTNTDKPHPVVIVSAGLDSLQTDMWRLFRDHLAKHDIAMLTVDMPSVGYSSKYPLTEDYSRLHQAVLNELFSIPYVDHHRVGLIGFRFGGNAMVRLSFLEQEKIKACVILGAPIHDIFASPQKLQQMPKMYLDVL... | Function: Catalyzes the hydrolysis of esters . In vitro, prefers short chain alkanoate ester as substrate. Displays highest activity towards p-nitrophenyl acetate (pNPA). Has weaker activity towards p-nitrophenyl butyrate (pNPB) .
Catalytic Activity: a carboxylic ester + H2O = a carboxylate + an alcohol + H(+)
Sequence... |
S0ASL9 | MDRPNKAIYLYQTSKGNHEIRTIQEPYVPKDAQSLVDVQYSGINPADTRHVYMDMSNYVAGYEFAGTVKQVGPKSPFKIGQEIFGISIPYNNRPNYLGAHQSFLLAENFMTFARPDHLDPITAATLLAGGGTAMDGLLNVLGYGFPPAGIPGDDPTNVPILIWGGAGGVGQAAVQLAKAAGFFPIITTASQQNHDVMKQLGASHVFNYKSPSVVQDIRNLLESKGWSLKTVFDAVSTGLGVFDGLTEEQEKAVQQKYNQSSSAMARQCCDPNIPDSELRLTSVLPVKMDPNYVFCLNFRPVEILDIGGEVTKDTKEEEMT... | Function: Trans-enoyl reductase; part of the gene cluster that mediates the biosynthesis of fusaridione A, a bright yellow trans-fused decalin-containing tetramic acid with antimicrobial activity . The PKS module of fsdS catalyzes the formation of the polyketide unit which is then conjugated to L-tyrosine by the conden... |
Q5SBL1 | MGSAGDDYEYVFPDISVENERLAGQHAGIKVGMGGRLCMAPLDLTRPNLRIFDGGTSDGYWLDDLKKELAHPETCDLIGGDVTGERFPTNPPPGVKLEVQSSTGPFPSDWLQSFDLVHQRLTLAGLGNQSEHCVEQLMSLVKPGGWIQLVELDNSSHEPNGPAVKTLGALVARLAEGMGADLKYRGGGMEKWVRDKGFIRVGSILAPVCMGAECPVPNMRDQTTKAFSFTAEQLIKACKRFPGGLKVMTDEEAEGLVGRLEDELRTRGGYFPVRVVWGKRPVDQ | Function: Methyltransferase; part of the gene cluster that mediates the biosynthesis of fusaridione A, a bright yellow trans-fused decalin-containing tetramic acid with antimicrobial activity . The PKS module of fsdS catalyzes the formation of the polyketide unit which is then conjugated to L-tyrosine by the condensati... |
S0AU91 | MKGNEFRNQTQTTIKNELAEWSDNSNNSQVDYASNAPSGDHVLVDWDGPNDPKNPKNWPHSAFLIHTILVSMLCLAGNLATTMYAPGAAQLAVEFKTRDTTTIALTVSIYLLGFALAPMVTSPLSEVYGRLIVYHTSNIFFLGFNLACAFSSNIGMFIAFRFLAGCAGSAPMTVGGGTIADFAASPEKNNTALRLFALGPLLGPVIGPIVGGFVAENIGWRWTFRIMSIVIAVLSILSCIFLRETSAAAILGRRGARITKETGKPFMIPGPMPGMPPKPQQPTKEIVSRSLVRPMKMLIFLPQVLILSFYTAFVFGLIYL... | Function: Efflux pump that might be required for efficient secretion of fusaridione A or other secondary metabolies produced by the fusaridione A gene cluster .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55704
Sequence Length: 509
Subcellular Location: Cell membrane
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Q5SBK7 | MSLNSASTREHPSEAWKSLAQYLPSRSTDLDYWWQRIGPSAALVLEKAGYSIKSQYDALLFLYHWVVPELGPSLLSTDHKWKSLLQGDGSAFELSWKWNTNDSPPEVRYVVEPINQFSGTLLDPLNSQPSMVFRHRLASILPNIDLTWCHHFAGSLFDHNKARLLREMMPEGHKMPAGYTVPSTLVALEFLQDGQVATKSYFIPRKHGQGVWLPIAQFEESIAELDPVNEARAAVVDFVSKDPESLTPIMLAVDDKDVSSARIKWYFATARTELSWAKEIMTLGGRITTKHLPHLEQQLDDLIELIKAVTGIASEYPQDV... | Function: Prenyltransferase; part of the gene cluster that mediates the biosynthesis of fusaridione A, a bright yellow trans-fused decalin-containing tetramic acid with antimicrobial activity . The PKS module of fsdS catalyzes the formation of the polyketide unit which is then conjugated to L-tyrosine by the condensati... |
Q12029 | MASSVPGPIDLPESRYDLSTYWGRIRHCAEISDPTMLLTTEKDLAHAREIISAYRHGELKETTPEFWRAKKQLDSTVHPDTGKTVLLPFRMSSNVLSNLVVTVGMLTPGLGTAGTVFWQWANQSLNVAVNSANANKSHPMSTSQLLTNYAAAVTASCGVALGLNNLVPRLKNISPHSKLILGRLVPFAAVVSAGIVNVFLMRGNEIRKGISVFDSNGDEVGKSKKAAFMAVGETALSRVINATPTMVIPPLILVRLQRGVLKGKSLGVQTLANLGLISVTMFSALPFALGIFPQRQAIHLNKLEPELHGKKDKDGKPIEK... | Function: Mitochondrial amino-acid transporter that mediates transport of serine into mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35414
Sequence Length: 327
Subcellular Location: Mitochondrion membrane
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P38777 | MTVQIPKLLFLHGFLQNGKVFSEKSSGIRKLLKKANVQCDYIDAPVLLEKKDLPFEMDDEKWQATLDADVNRAWFYHSEISHELDISEGLKSVVDHIKANGPYDGIVGFSQGAALSSIITNKISELVPDHPQFKVSVVISGYSFTEPDPEHPGELRITEKFRDSFAVKPDMKTKMIFIYGASDQAVPSVRSKYLYDIYLKAQNGNKEKVLAYEHPGGHMVPNKKDIIRPIVEQITSSLQEASE | Function: Serine hydrolase of unknown specificity.
Sequence Mass (Da): 27339
Sequence Length: 243
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q05015 | MTKNVLMLHGLAQSGDYFASKTKGFRAEMEKLGYKLYYPTAPNEFPPADVPDFLGEVIADAPGDGENTGVLAWLENDPSTGGYFIPQTTIDYLHNYVLENGPFAGIVGFSQGAGVAGYLATDFNGLLGLTTEEQPPLEFFMAVSGFRFQPQQYQEQYDLHPISVPSLHVQGELDTITEPAKVQGLYNSCTEDSRTLLMHSGGHFVPNSRGFVRKVAQWLQQLT | Function: Serine hydrolase of unknown specificity.
Sequence Mass (Da): 24534
Sequence Length: 223
Subcellular Location: Cytoplasm
EC: 3.1.-.-
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Q9SPK5 | MSSSTRKLEVVSPVPADIDIANSVEPLHISEIAKDLNINPLHYDLYGKYKAKVLLSAFDELQGQEDGYYVVVGGITPTPLGEGKSTTTVGLCQALGAYLDKKVVTCLRQPSQGPTFGIKGGAAGGGYSQVIPMDEFNLHLTGDIHAITASNNLLAAAIDTRIFHETSQSDKALFNRLCPPNKEGKRSFSDIMFRRLTKLGISKTSPEELTPEEIKKFARLDIDPASITWRRVMDVNDRFLRKITIGQGPEEKGMTRETGFDISVASEIMAVLALTTSLGDMRERLGKMVIGNSKAGDPITADDLGVGGALTVLMKDAINP... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 67802
Sequence Length: 634
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
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B1MY45 | MQTDIAIAQSAEILPITQIAEKAGLKPNEILPYGYDKAKIKLDPTISRKKDLGKLILVTSINPTPAGEGKSTVTVGLADALALAGKKTMIALREPSLGPVMGMKGGATGGGMSQVIPMADINLHFTGDFHALTAAHDTLAAVVDNSLQQGNPLNIDPRRIIWKRVLDINDRALRHITIGMGGPTSGVPREDGFDITVASELMAILTLSTDLMDLKARVARIVVGYTYDKVPVTVADLGVSGALAVLLKDAIMPNLVQTLAHTPAIIHGGPFANIAQGTNSILATKTALQLADYTVTEGGFGADLGGEKFLDVKVPILGKT... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 58270
Sequence Length: 554
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
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A5VHS9 | MTDIEIADQATLEPITEIAEKLGLSEDEIEQYGKYKAKIDLNVKPLPDKKHKLILVTSINPTPAGEGKSTVLIGLGDALNQLNYQTTIAMREPSMGPVFGIKGGATGGGYSQVVPMEDINLNFTGDLHALTSANNTLAALIDNYIMRDNAMNLDPRRIIWKRVEDVNDRALRNVVTGLGGPMAGVPRETGFDITAASELMAILCLSTSLHDLKERISRIVVGYTYDKEPVTVGQLNFQDAITIILKDALKPNLVQTLDHTPTIVHGGPFANIAHGCNSVLATQTALNLSDYTVTEAGFGADLGGEKFLDIKQRVLGKHPD... | Catalytic Activity: (6S)-5,6,7,8-tetrahydrofolate + ATP + formate = (6S)-10-formyltetrahydrofolate + ADP + phosphate
Sequence Mass (Da): 60252
Sequence Length: 553
Pathway: One-carbon metabolism; tetrahydrofolate interconversion.
EC: 6.3.4.3
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P43707 | MLNQIIINKLNDQINLEFYSSNVYLQMSAWCSKHGYEGAATFLLRHADEELEHMQKLFNYVSETSGMPILGKIDAPKHDYSSLREVFEITLEHEKLVTSKINELVEVTFESKDYSTFNFLQWYVAEQHEEEKLFSGIIDRFNLVGEDGKGLFFIDRELATLE | Function: Iron-storage protein.
Catalytic Activity: 4 Fe(2+) + 6 H2O + O2 = 12 H(+) + 4 iron(III) oxide-hydroxide
Sequence Mass (Da): 18896
Sequence Length: 162
Subcellular Location: Cytoplasm
EC: 1.16.3.2
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P0A9A0 | MLKPEMIEKLNEQMNLELYSSLLYQQMSAWCSYHTFEGAAAFLRRHAQEEMTHMQRLFDYLTDTGNLPRINTVESPFAEYSSLDELFQETYKHEQLITQKINELAHAAMTNQDYPTFNFLQWYVSEQHEEEKLFKSIIDKLSLAGKSGEGLYFIDKELSTLDTQN | Function: Iron-storage protein.
Catalytic Activity: 4 Fe(2+) + 6 H2O + O2 = 12 H(+) + 4 iron(III) oxide-hydroxide
Sequence Mass (Da): 19424
Sequence Length: 165
Subcellular Location: Cytoplasm
EC: 1.16.3.2
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E1WS50 | MISEKLQNAINEQISAEMWSSNLYLSMSFYFEREGFSGFAHWMKKQSQEEMGHAYAMADYIIKRGGIAKVDKIDVVPTGWGTPLEVFEHVFEHERHVSKLVDALVDIAAAEKDKATQDFLWGFVREQVEEEATAQGIVDKIKRAGDAGIFFIDSQLGQR | Function: May alleviate iron toxicity in the presence of oxygen.
Catalytic Activity: 4 Fe(2+) + 6 H2O + O2 = 12 H(+) + 4 iron(III) oxide-hydroxide
Sequence Mass (Da): 18064
Sequence Length: 159
EC: 1.16.3.2
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P52093 | MLSKDIIKLLNEQVNKEMNSSNLYMSMSSWCYTHSLDGAGLFLFDHAAEEYEHAKKLIVFLNENNVPVQLTSISAPEHKFEGLTQIFQKAYEHEQHISESINNIVDHAIKGKDHATFNFLQWYVSEQHEEEVLFKDILDKIELIGNENHGLYLADQYVKGIAKSRKS | Function: Iron-storage protein.
Catalytic Activity: 4 Fe(2+) + 6 H2O + O2 = 12 H(+) + 4 iron(III) oxide-hydroxide
Sequence Mass (Da): 19286
Sequence Length: 167
Subcellular Location: Cytoplasm
EC: 1.16.3.2
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Q8S2A7 | MSLSSLSRALARSARSSRQRQGSLLGGHGGLRASSPPLPCGELGFLRSYVTSVIGNRAAVASGAGKGGDWRFLLASRQFRRLFSDKSKKNHGKHSEEENKGKGDESDKSDSKKQSSSGDQWNFEESIKQFKDMIAPLFLFGLLLLSASASSSEQEISFQEFKNKLLEPGLVDHIVVSNKSIAKVYVRSSPSIDRIQDSDIHITTSHLPGIESPSSYKYYFNIGSVDSFEEKLQEAQKALEIDPHYYVPITYTTEAKWFEEVMKYVPTVLIIGLIYLLGKRIQNGFTVGGGPGKGGRSIFSIGKVQVTKLDKNSKNKVFFK... | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable ATP-dependent zinc metallopeptidase.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 88144
Sequence Length: 802
Subcellular Location: Mitochondrion inner membrane
EC: 3.4.24.-
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A9GAW6 | MNSWFLQVSKRLGPAGRRLWLLGFMGVVLAVTLGLALRAARESATQRTATYTELLQIAQAGQATAVEVSGDRFLVRQAGGAVVTAVVDEPTLRQELVSRFAGAGASVDFASREDPSRAASAVLPVVVLAAVGFALFTVSRRRSPKVFSDVKAGAARAAVRFADVAGMHEVKQELAETVEFLKSPDRFARLGGRPPRGVLLTGEPGTGKTLLARAVACEAGVRFLSASGSSFQEMFVGVGASRVRALFAEARKSAPCIVFIDEIDAVGRARAKGHGDSASAEHDQTLNQLLVEMDGFDHETGIVVIASTNRADMLDPALLR... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 64372
Sequence Length: 602
Subcell... |
D1C4U5 | MNPRPVRPGGSLQQSLLALGSLSVAVGLAVWQQRTLGRGRSDSVTAVERPETTFSDVAGLIEAKEELAEIVTFLRDPERFRRMGARMPRGVLLAGPPGTGKTLLARAVAGEAGVPFFAMSASQFVEVYVGVGAKRVRDLFAAARKASPAIVFIDEIDAIGRRRGDSQSHQEYEQTLNQVLVELDGFHPRQAVVVIAATNRSDILDPALLRPGRFDRRVELSLPDRAERAAILRVHAQDKPLAPDVDLDALAARTVGLSGADLENTLNEAALLALRRGGDEITQADLEEAVDRVIAGPSRRSRALSARERETIAVHEAGHA... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 52235
Sequence Length: 489
Subcel... |
P72991 | MSKNNKKWRNAGLYALLLIVVLALASAFFDRPTQTRETLSYSDFVNRVEANQIERVNLSADRTQAQVPNPSGGPPYLVNLPNDPDLINILTQHNVDIAVQPQSDEGFWFRIASTLFLPILLLVGIFFLFRRAQSGPGSQAMNFGKSKARVQMEPQTQVTFGDVAGIEQAKLELTEVVDFLKNADRFTELGAKIPKGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSEFVEMFVGVGASRVRDLFEQAKANAPCIVFIDEIDAVGRQRGAGLGGGNDEREQTLNQLLTEMDGFEGNTGIIIVAATNRPDVLDSALMRPG... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67250
Sequence Length: 616
Subcell... |
O80983 | MAWRRIITKVSSHERELSSLRSLLVRAYSSFPRVGVTGAVGGGGASLPRTRFQSSYVGSFARRVRDREEVNEVAHLRELIRRNDPEAVIRMFESQPSLHANASALSEYIKALVKVDRLDQSELVRTLQRGIAGVAREEETFGGLGAFRNVGKPTKDGVLGTASAPIHTISTERTHFKEQLWSTIRTIGVGFLLISGIGALIEDRGIGKGLGLHEEVQPSMDSSTKFSDVKGVDEAKAELEEIVHYLRDPKRFTRLGGKLPKGVLLVGPPGTGKTMLARAIAGEAGVPFFSCSGSEFEEMFVGVGARRVRDLFSAAKKCSP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable ATP-dependent zinc metallopeptidase. Involved in the assembly and/or stability of the complex V of the mitochondrial oxidative phosphorylation system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 77275
Sequence Length: 717
Subcellular Loc... |
A9EXK6 | MKQSHKTLLLWVLLIMMFLAIWQFLSPDSRPATQVAFSEFMAQVQVEAKDKDPHVESVTIKDREYTFWVKDPKSGTKTKKVTIGPDNADEITKTIVDNKVAVFFEKEDTSPFWPGAIMYLLPTVFLLVMFYLFMRQLQAGGGKAMSFGKSRARLLSEAQNKVTFADVAGIDEAKDELEEIIAFLKDPKKFQKLGGRIPKGVLMMGPPGTGKTLLARAIAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFEQGKKHAPCIIFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFESNEGVIIVAATNRPDVLDPAI... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71841
Sequence Length: 648
Subcell... |
D1C8C0 | MREPTNRQGSPGPGEPRPPAQGRPRFPTWILWVALLALALWNVYTFFWPSSGARLNIPYSAFIQQVEGENVSSVTIRGQRVSGTFTEEVRVAGDQVLSPGDPVPPGTSPNEIRTGTQFQTTIPENSQTELVPLLQSHGVTVKIDQAGGSVWPSLLATIVPLFLFIGLMVYLGRSMSRGQQNVFSFGRSKARVYDAERPRVTFADVAGEEEAKAELSEVVDFLRNPMKYHAIGARLPRGILLVGPPGTGKTLLARAVAGEAGVPFFSVSASEFVEMFVGVGASRVRDLFERAKASAPSIMFVDELDAVGRQRFAGLGGGND... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71751
Sequence Length: 658
Subcell... |
P73437 | MAIKPQPQWQRRLASVLLWGSTIYLLVNLLAPALFRSQPPQVPYSLFIDQVEGDKVASVYVGQNEIRYQLKPEAEDEGKEKAAEGQILRTTPIFDLELPKRLEAKGIEFAAAPPAKNSWFGTLLSWVIPPLIFVGIWSFFLNRNNNGAPGGALAFTKSKAKVYVEGDSTKVTFDDVAGVEEAKTELSEVVDFLKFPQRYTALGAKIPKGVLLVGPPGTGKTLLAKAAAGEAGVPFFIISGSEFVELFVGAGAARVRDLFEQAKKQAPCIVFIDELDAIGKSRASGAFMGGNDEREQTLNQLLTEMDGFSAAGATVIVLAA... | Cofactor: Binds 1 zinc ion per subunit.
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68199
Sequence Length: 628
Subcell... |
Q9FH02 | MATTSSNPLLLSSNFLGSQIIISAPTPKTTTKSLPFSVISRKRYQISQSEKLMKSLPSQAALAALLFSSSSPQALAVNEPVQPPAPTITAEAQSPNLSTFGQNVLMTAPNPQAQSSDLPDGTQWRYSEFLNAVKKGKVERVKFSKDGSVLQLTAVDNRRATVIVPNDPDLIDILAMNGVDISVSEGEGGNGLFDFIGNLLFPLLAFGGLFYLFRGGQGGAGGPGGLGGPMDFGRSKSKFQEVPETGVTFGDVAGADQAKLELQEVVDFLKNPDKYTALGAKIPKGCLLVGPPGTGKTLLARAVAGEAGVPFFSCAASEFV... | Cofactor: Binds 1 zinc ion per subunit.
Function: Part of a complex that function as an ATP-dependent zinc metallopeptidase. Involved in the thylakoid formation and in the removal of damaged D1 in the photosystem II, preventing cell death under high-intensity light conditions. Not involved in the degradation of the lig... |
Q8LQJ8 | MAWRRVLSQVARNRSAYAICNEIIYANPSRILRGDTIAGGTLRNLHERYQSSYVGSFARRMRQMDSPSEASLLKEIYRSDPERVIQIFESQPSLHSNPSALAEYVKALVRVDRLEDSTLLKTLQRGIAASAREEENLGSVSENLGSVSAFRSAGQVTKDGILGTANAPIHMVTAETGQFKEQLWRTFRSIALTFLLISGIGALIEDRGISKGLGLNEEVQPSMESNTKFSDVKGVDEAKAELEEIVHYLRDPKRFTRLGGKLPKGVLLVGPPGTGKTMLARAIAGEAGVPFFSCSGSEFEEMFVGVGARRVRDLFAAAKK... | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable ATP-dependent zinc metallopeptidase.
Sequence Mass (Da): 77434
Sequence Length: 715
Subcellular Location: Mitochondrion
EC: 3.4.24.-
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Q9SD67 | MTTTFEFLQPRIHGFATCCSSNSLLYSKASRFFNDRCRVYRQNPNRFVSNSITLPLQKKQVTVLRNHERFNLWDGFSRKKSRLVVNCQEDDQNESSSEEEESSQSTPAKSERKREKKEDKVWWSKGKKWQWQPIIQAQGIGVLLLQLSVVMFVMRLLRPGIPLPGSEPRIQTTFVSVPYSEFLSKVNSNQVQKVEVDGVQVLFKLRDDGKWQESETSRLSQSSESLLRTVAPTKRVVYSTTRPGDIKTPYEKMLGNNVEFGSPEKRSGGFFNSALIALFYIAVLAGLIRFPVSFSTSSTGQLRTRKAGGPDGGKVSGGGE... | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable ATP-dependent zinc metallopeptidase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87802
Sequence Length: 802
Subcellular Location: Plastid
EC: 3.4.24.-
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Q0DHL4 | MSLASLARALSRRSAPSSSRARQGFSLGGLGGTTRSPPPPSSPLPSLHGGEGGGLGLGFVRGYLTAALGRPAAVKAGTDWRSILANPQFRRLFSDGSKKNYENYYPKGKKEAPKGDGSNKSDSKQDSSTDDQWNFQETASKQLQNFLAPLLFLGLMLSSLSSSSSDQKEISFQEFKNKLLEPGLVDRIVVSNKSVAKVYVRSSPQSNSQGQNTDAIITTNDVPSKHTPSRYKYYFNIGSVDSFEEKLEEAQEALGVDPHDFVPVTYVAEVNWFQEVMRFAPTVFLVGLIYLMSKRMQSGFNIGGGPGKGGRGIFNIGKAQ... | Cofactor: Binds 1 zinc ion per subunit.
Function: Probable ATP-dependent zinc metallopeptidase.
Sequence Mass (Da): 90074
Sequence Length: 822
Subcellular Location: Mitochondrion
EC: 3.4.24.-
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O05560 | MASKTVARSGNRTSSLKATSRGVSQSRRPVPPRPRRNRPAERRNQSLLLAAGLTCGQAIRATWLVAAKGAGGAARSIGRARDIEPGHRRDGIALALLGLAVVVAASSWFDAARPIGAWVDAVLRTFIGSAVVVLPLVIAAVAVVLMRTQPNLDTRPRLILGATLIALSFLGLRHLWSGSPETPEVRRGAAGFLGFAIGGPLSDGLTAWIAAPLLFIGALFGLLLLTGTTVREVPEVLRGMFDTGLFQRDYDDQYDAEYRYDDIPGAPPEDFSGCYDGSLVGGGDAEQKVRGWPVTDLAEVSLQDDVPTTPEPAVQAGTAE... | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the ... |
P9WNA2 | MSSKTVARSGTRTSRSKATSRGASRSARSAVPRKRSRPVKGVGRPSRRHHRSLLVSTGLACGRAMRAVWMMAAKGTGGAARSIGRARDIEPGHRRDGIALVLLGLAVVVAASSWFDAARPLGAWVDALLRTFIGSAVVMLPLVAAAVAVVLMRTSPNPDSRPRLILGASLIGLSFLGLCHLWAGSPEAPESRLRAAGFIGFAIGGPLSDGLTAWIAAPLLFIGALFGLLLLAGITIREVPDAMRAMFGTRLLPREYADDFEDFADFDGDDADTVEVARQDFSDGYYDEVPLCSDDGPPAWPSAEVPQDDTATIPEASAGR... | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the ... |
Q8EQS7 | MAAKKRKKKRKNSKQVKRLKIELVGLLLIFLAIFGSGAAALSDGAIPGWLENLFQFFFGIWYFIASVFLLVTGFYLLVKRKLPDFLHRRMIGFYILLAGVLMLTHIQVLESLLVTTENTSIIGMSWTLFFDYVNGTGTLVQTGGGMIGAILFTFSHYMFSITGSKIVVVFCLLIGAIFLTNLSIGEVASKLFARVKAVSNIAIEKWTQYQTERRERKQQAYMDDESRQAVNESEDNMVTEIEVSEREEPFINDFTDVAYQNNATQATENKSPAKQAQSIKSDQEGQSDHSAEDSKDEAMPMTARENHDYELPMPDLLADP... | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the ... |
Q9CP13 | MIKRISEKFTPKQYLLAFFFLVGMLFGVYLIVAWSSYSPLDNSWASSSYIPTTINKAGRFGAWFIDLFFVLFGHVGHIIPFLIFGISFYFWRRKGKVPFSFFRLSLWLLGFSIFLCGVCVLFTLLFSNTPYYLSGGVLGGSLVTAFFPMLDFVGLMLSGTLLALLGFVLCSGTSLIRSCIYFYDWLTMKNPTQTQEEETISTTPVQQELALQEEPSIQSINEGERVFVSEAPSATMDEEKSLINIENLIQIQGLESASQAKESTIPTVPLDDVNQVELGGYAVEPELALPSVSVAFVEDTALSSSEAEHEDSKPFTTQIP... | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the ... |
Q9I0M3 | MRRKNSDLKDSTTASHAAAWRQQLHSRLKEGVLIALGALCLYLWMALLTYDSADPSWSHSSQVDQVQNAAGRLGAVSADILFMTLGYFAYLFPLLLGIKTWQVFRRRNLPWEWNTWLFSWRLVGLIFLILAGSALAYIHFHASGHMPASASAGGAIGQSLGRVAVDALNVQGSTLVFFALFLFGLTVFADLSWFKVMDVTGKITLDFFELIQNAFNRWMGARAERKQLVAQLREVDERVAEVVAPSVPDRREQSKAKERLLEREEALAKHMSEREKRPPPKIDPPPSPKAPEPSKRVLKEKQAPLFVDTAVEGTLPPLSL... | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the ... |
Q88FS8 | MKKSTATPAPLPVPLWRQQLHYRLKEGALIAVGALCLYLWMALLTYDTSDPGFSHTSNVDQVQNAAGRAGAYFADILFMVLGYFAYIFPLLLAVKTWQIFRERHQPWDWSGWLFSWRLIGLVFLVLSGAALAHIHFHPPASLPFSAGGALGESLGDLARNLLNVQGSTLMFIALFLFGLTVFTDLSWFKVMDLTGKITLDLFELVQGAATRWWEARNERKRLEAQLREDEPVFKAAPMAAEKREPAKPSLRERILKREEPPAQPVEPREPTLAREPIVPPRETAPEALAPRETVVPRQQHAAPTIVPPSAASRAPEPSKR... | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the ... |
Q92L89 | MSRSNTATLDSRSNRFVLTHFVWRQIASLAGFVLVGALALAIAALSTWNVADPSFSYATSNEPTNLLGYGGAVFADIFMQFFGLASVVALLPAVAWALVLIRGTHFDKVLKRLGLWFAGSVLASAALSCVPAPITWPLPNGLGGVFGDMILRFPALFTGTFPTGTFATVLACLFTAPAAWCLVYSAGLIGVSEDEEAEPAPEPAPSKARTIRDELEEEDEEGPLTVLMGSLAHMRYTAQARLRRAFGMGAKPAKRQYDEPYDFNNDEFGTLNEPVRPKAQAGRIEPSLDRSERRIVTPPPIMGDEDDPPFDIDERRPAGI... | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the ... |
Q9ZCD4 | MLFYINKILSNNKVQAVILWIIGLAIVIVLMSYNIDDPSFNSVTTEYPSNLIGIVGAYLSDFLYQFFGLTSFIIPLACFIWGRNCWYGRYRSAFIRIFVVLLALISSSTLLSKIKLELIPASAGGAIGIIVSNFCERFINQLYLLLIFPTFIILVVLLEIKFTAISNFMIKLSKFLTYWILLFFNYVLPRLSLIGLFPIKNNDKLNITSFYQKPASGKVKFTEEASLIPANPIKCFIKPVCTKISQNQIASLPPISLLCDPKNNHVKGASSSELKQKAEELLTVLNDFGVKGQIININQGPVVTQYEFEPAAGTKTSRVV... | Function: Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the ... |
P56096 | MTTDRNLFFCASLLIFLGVLMSYSLSTYTTVVLYHYGEFHFFIRQLVSAIIGIVIMWGLSRVDPSKWFSRLGFFLLFVPPLLIIGMFFLPESLSSSAGGAKRWIRLGFFSLAPLEFLKIGFTFFLAWSLSRTFVAKEKANVKEELITFVPYSVVFVALAIGVGVLQNDLGQIVLLGAVLAVLLVFSGGSVHLFGLIISGAFAISVLAIVTSEHRILRLKLWWSNLQNSLFTLLPDRLANALRISDLPESYQVFHAGNAMHNGGLFGQGLGLGQIKLGFLSEVHTDMVLAGIAEEWGFLGLCVCFILFSVLIVLIFRIANR... | Function: Peptidoglycan polymerase that is essential for cell division.
Catalytic Activity: [GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)](n)-di-trans,octa-cis-undecaprenyl diphosphate + beta-D-GlcNAc-(1->4)-Mur2Ac(oyl-L-Ala-gamma-D-Glu-L-Lys-D-Ala-D-Ala)-di-trans,octa-cis-undecaprenyl diphosphate = [G... |
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