ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q6L1P9 | MDYIIEDGFHFDIKNGKSPSYLINKYRTGHVIGNVYLLNKYEAFYLYLKNKISIDDEFFNGNIKFYMAYENLIGSGLYVKILNDCFMCRKSRNSRYKKVRFMPDDILLSFKDLYSDDSNIYITVDEEYESVYYSMERIDIKGSRKDDFSAASIDVSSGAYFGMNCPEWFGIDFHGKRLLNDYEIRFLNNDVKSNVDVIYKDLIKRGFIVKSGFKYGSNFRIYKNSMNEHSDYLVNYMDHDLWYVIARAVRLASNVRKRLIISGIIDNDPVYIKIERIKDIKTIL | Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a s... |
Q8ZVI1 | MIGYLRGLAVIVEDVEFARRLYKEGFYGRFLGYDKVKRDEVEKINAPLILGLYEALYLAEKGRLKVMGEDGREVAPEELAALGRERMRNFDEIYKIYKYFRDLGYVVKSGLKFGALFSVYEKGPGIDHAPMVVVFLEPDKGISATDITRGGRLSHSVRKTWTLATVLRQTGEVVLLGFGWARL | Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a s... |
A1RSY7 | MKGVLKGLAVVVEDVEFARKLYKEGFYGRFLGYDKVRREEVDKISAPLILALYEALYLAERGKLKVVSKNGTEVLPEKLIELGREKIKNFDDIYKIYKYFRDLGYVVKSGLKFGALFSVYERGPGIDHAPMVVVFLEPDRGISATDITRGGRLSHSVKKTFTLATVSKQTGEVVLLGFSWAKL | Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a s... |
Q975R3 | MIGELVKDKILIKNIEDARLIYKMGYYGKPIGISKPKSAEEINSELILSLIEGVYLVKKGKLEIVSNGERLDFERLYQIGVTQIPRFRILYSVYEDLREKGYVVRSGIKYGADFAVYTIGPGIEHAPYLVIALDENSQISSNEILGFGRVSHSTRKELILGIVNLTNGKIRYIMFKWLKM | Function: Endonuclease that removes tRNA introns. Cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3' cyclic phosphate and 5'-OH termini. Recognizes a pseudosymmetric substrate in which 2 bulged loops of 3 bases are separated by a s... |
Q9N2K0 | MIFAGKAPSNTSTLMKFYSLLLYSLLFSFPFLCHPLPLPSYLHHTINLTHSLLAASNPSLVNNCWLCISLSSSAYTAVPAVQTDWATSPISLHLRTSFNSPHLYPPEELIYFLDRSSKTSPDISHQQAAALLRTYLKNLSPYINSTPPIFGPLTTQTTIPVAAPLCISWQRPTGIPLGNLSPSRCSFTLHLRSPTTNINETIGAFQLHITDKPSINTDKLKNISSNYCLGRHLPCISLHPWLSSPCSSDSPPRPSSCLLIPSPENNSERLLVDTRRFLIHHENRTFPSTQLPHQSPLQPLTAAALAGSLGVWVQDTPFST... | Function: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has lost its original fusogenic properties but has immunosuppressive pro... |
P61559 | MIFAGKAPSNTSTLMKFYSLILYSLLFSFPFLCHPLPLPSYLHHTINLTHSLLAASNPSLANNCWLCISLSSSAYTAVPALQTDRATSPVSLHLQTSFNSPHLYPPEELIYFLDRSIKTSPDISHQQAAALLHTYLKHLSPYINSTPPIFGPLTTQTTIPVAAPLCISRRRPTGIPLGNLSPSRCSFTLHLRSPTTNITETIGAFQLHITDKPSINTDKLKNISSHYCLGRHLPCISLHPWLPSPCSSDCPPRPSSCLLIPSPENNSESLLVDTRRFLIHHENRTSPSTQLPHQSPLQPLTAAALAGSLGVWIQDTPFST... | Function: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution.
PTM: Specific enzymatic cleavages in vivo yield the mature SU and TM proteins.
Sequence Mass (Da): 49843
... |
Q9NX77 | MWTVPSFTNDSYQVYNVFSTNSFQLLTVKRTPHEAWRVPLTTKTNKTKGLPDCPKKPTNGPFIVTSILWDNCNAPKAVVLQTLAMGIVIDWAPKGHYWQDCSSKNTLCSEFIYSLDYIEHGWQSYTMRQRVSPYPFKWMDTGIAPPRPKIIHPFFTPEHPELWKLAAALSGIKIWNTTYQLLRTKTKTPTFNITLISEWVIPIRSCVKPPYMLLVGNIIMMPDAQTIECHNCKLFTCIDATFNPTTSILLVRAREGVWIPVSLHRPWESSPSIHIVNEVLKDILKRTKRFIFTLIAVLAGLLAVTATAATAGVAIRSSVQ... | Function: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution (By similarity).
PTM: Specific enzymatic cleavages in vivo yield the mature SU and TM proteins.
Location T... |
O42043 | MVTPVTWMDNPIEVYVNDSVWVPGPTDDRCPAKPEEEGMMINISIGYHYPPICLGRAPGCLMPAVQNWLVEVPTVSPNSRFTYHMVSGMSLRPRVNCLQDFSYQRSLKFRPKGKTCPKEIPKGSKNTEVLVWEECVANSVVILQNNEFGTIIDWAPRGQFYHNCSGQTQSCPSAQVSPAVDSDLTESLDKHKHKKLQSFYLWEWEEKGISTPRPKIISPVSGPEHPELWRLTVASHHIRIWSGNQTLETRYRKPFYTIDLNSILTVPLQSCVKPPYMLVVGNIVIKPASQTITCENCRLFTCIDSTFNWQHRILLVRARE... | Function: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This envelope protein has superantigenic properties.
PTM: Specific enzymatic cleavages in vivo yield the ... |
Q9P6Q2 | MVKNLLLDIEGTVGSISFVKDKLFPYAASRYESYVNENYESDENLRELGKTPEEALINLRKLHAEGSKERSFKMVQGRIWKKGYESNELTSHLFPDVVPAIQRSLQLGMRVYIYSSGSVPAQKLYFEHSDAGNLLKYFSGYYDTTIGLKTECGSYVKIVGNSNPREWLFLSDNINELKAARKVGLHTGLVVRPGNDPVVDTSGFPVYNSFEILFTE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
A7E3Z4 | MEAKPRVKVVLLDIEGTVCPISFVKDVLFPYALAALPETLSTEWDSSSFLPYRSAFPPEHSSTPEALLSHVRDLMAQDLKIPYLKSLQGYLWLRGYESGTLKCPLFPDVYPAMKKWKENGAKICIYSSGSVAAQKLLWRYTAEGDLRGCIWNGVDGAEEIEGGYWDTVNAGLKQESTSYEKIAKANRALGEVGEWLFLSDNVKEVRAAKESGMKSFVVVREGNADVSVEEKNRQVLITSFREVEAMVEVTGESA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
D1ZPB8 | MAPVKVVLLDIEGTVCPISFVKDVLFPYALEALPGTLKAKWDSPGFASYRAAFPAEHAGSQETLAAHVRDLMSKDLKISYLKSLQGYLWETGYRNGELKAPLFADVAPQLARWREHNGAKVMIYSSGSVPAQKLLFGHTNGEPSDILPWLSDFFDTVNAGPKQEKASYEKIAAKHQEYPIGEWLFLSDNVKEVEAAKQAGMQSYIVDRPGNAELSEEARKEHRVVKSFEEIGDL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
C9SUS0 | MASATATTSAADLAAVKVVLLDIEGTVCPISFVKDVLFPYALQALPVTLDKKWDSPDFAPYRNAFPEPAASSRPVFEAHVADLVKRDVKVSYLKALQGYLWLAGYESGDIKAPLFPDVSPSMRAWHDAGIKLIIYSSGSVPAQKLLFGHTNASPPSLIPIISDWFDTVNAGMKMESSSYTSILSRYPDTQPQEWLFLSDNVDEVSAARAAGMHSLVVVRPGNAPLPECHVGEGQAVQTFEGLAVGGKRNESSKSS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
Q569R5 | MALFSVPTPVTTILLDIEGTTTPITFVKDVLFPYIKENIKKYLLEHWQEKECQEDITQLQKQAEKDSHIDGFVPIPSAISDNETENMIQAVVDNVYWQMSLDRKTTALKQLQGHMWRSAYITGQLKGEVYEDVVPSIRQWRELGFKLYIYSSGSVEAQKLLFGFSIEGNLLKLLDGHFDTTVGHKVESKSYRNIADSIRCSPENILFLTDVVKDMPLYLVTQESYPEAVIRGVCC | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
Q28C69 | MALFSVPPPVTVILLDIEGTTTPITFVKDVLFPYVKENIKKYLLEHWQEKECQEDVTQLQKQAEKDSHLDGFVPIPSGVSDNTTEHMIQAVVDNVYWQMSFDRKTTALKQLQGHMWRSAYISGQLKGEVYEDVVPSIRQWRELGIKLYIYSSGSIDAQKLLFGYSIEGDLLKLLDGHFDTNIGHKVESKSYRNIADNIGCLPENILFLTDVVKEALAAEKAGLHVAVVVRPGNAALTDEDKSNCCCITSFHQIHFPSQK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
Q6C8V1 | MATLLDIEGTVCSISFVHDILFPYALEKLPQLLKNEQFPIKPGGNQTSDLTPYLESFPEEYKQSAQALEDHVIDLTEKNVKAPYLKALQGYIWKSGYQSGEIKAPLYPDAVDYMKRVVDGGNKVFIYSSGSVPAQKLLFGYSSAGDLTPLISDYFDTVNAGPKMEAASYTTILKAIGFEADRVLFLSDNVREIEAAKKAGLRAYVAERPGNAKLTPQEKEDNVIKTSFEGIEI | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
P32626 | MGDNYSTYLLDIEGTVCPISFVKETLFPYFTNKVPQLVQQDTRDSPVSNILSQFHIDNKEQLQAHILELVAKDVKDPILKQLQGYVWAHGYESGQIKAPVYADAIDFIKRKKRVFIYSSGSVKAQKLLFGYVQDPNAPAHDSLDLNSYIDGYFDINTSGKKTETQSYANILRDIGAKASEVLFLSDNPLELDAAAGVGIATGLASRPGNAPVPDGQKYQVYKNFETL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy... |
A9AGW2 | MSAIVDIIGREILDSRGNPTVECDVLLESGTMGRAAVPSGASTGSREAIELRDGEAGRYNGKGVLKAVEHINTEISEAIMGLDASEQAFLDKTLLELDGTDNKSRLGANAMLAVSMAVAKAAAEEAGLPLYRYFGGSGAMQLPVPMMNIVNGGAHANNSLDIQEFMIVPVSQPTFREALRCGAEVFHALKKILSDRGMSTAVGDEGGFAPNFGSNDECLSTILQAIEKAGYRAGEDVLLALDCAASEFYHDGKYQLAGEGLQLSSAEFTDYLSTLADKFPIVSIEDGMHESDWDGWKLLTDRLGKKVQLVGDDLFVTNTR... | Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 45733
Sequence Length: 427
Pathway: Carbohydrate degradation; gly... |
Q27527 | MPITKIHARQIYDSRGNPTVEVDLFTEKGVFRAAVPSGASTGVHEALELRDGDKAVHLGKGVLKAVSNINEKIAPALIAKGFDVTAQKDIDDFMMALDGSENKGNLGANAILGVSLAVAKAGAVHKGLPLYKYIAELAGTGKVVLPVPAFNVINGGSHAGNKLAMQEFMILPVGASSFAEAMRMGSEVYHHLKAEIKKRYGLDATAVGDEGGFAPNIQDNKEGLDLLNTAIDKAGYTGKISIGMDVAASEFFKDGKYDLDFKNPASDSSKWLSGEQLTELYQSFIKEYPVVSIEDAFDQDDWDNWGKFHGATSIQLVGDD... | Cofactor: Mg(2+) is required for catalysis and for stabilizing the dimer.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 46617
Sequence Length: 434
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Subcellular Location: Cyto... |
Q8RI55 | MTGIVEVIGREILDSRGNPTVEVDVILECGAKGRAAVPSGASTGSHEAVELRDEDKGRYLGKGVLKAVNNVNTEIREALLGMDALNQVEIDKVMLELDRTPNKGRLGANAILGVSLAVAKAAAEALGQPLYKYLGGVNSKELPLPMMNILNGGAHADSAVDLQEFMIQPVGAKSFREAMQMGAEVFHHLGKILKANGDSTNVGNEGGYAPSKIQGTEGALALISEAVKAAGYELGKDITFALDAASSEFCKEVNGKYEYHFKREGGVVRTTDEMIKWYEELINKYPIVSIEDGLGEDDWDGWVKLTKAIGDRVQIVGDDL... | Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 46680
Sequence Length: 434
Pathway: Carbohydrate degradation; gly... |
Q74AR6 | MSEITDVYAREILDSRGNPTLEVEVFLESGVMGRAAVPSGASTGEREALELRDGDASRYLGKGVLKAVDNVNDIIAEQLIGMEATDQVGIDRRMLELDGTEYKSTLGANAILGVSLAVAKAAAEEVGLPLYQYIGGCNARELPLPMMNILNGGAHADNNVDIQEFMIMPAGARSFSEALRMGAEVFHALKSVLKGKGYNTAVGDEGGFAPNLKSNEEALEVIMEAIAKAGYKAGEDILLALDVASSELFKDGKYFLENEAKPEKTADELIDFYENLVNKYPIISIEDGMAENDWEGWKKITDRLGKRVQLVGDDLFVTNT... | Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 46442
Sequence Length: 428
Pathway: Carbohydrate degradation; gly... |
Q8IJN7 | MAHVITRINAREILDSRGNPTVEVDLETNLGIFRAAVPSGASTGIYEALELRDNDKSRYLGKGVQKAIKNINEIIAPKLIGMNCTEQKKIDNLMVEELDGSKNEWGWSKSKLGANAILAISMAVCRAGAAANKVSLYKYLAQLAGKKSDQMVLPVPCLNVINGGSHAGNKLSFQEFMIVPVGAPSFKEALRYGAEVYHTLKSEIKKKYGIDATNVGDEGGFAPNILNANEALDLLVTAIKSAGYEGKVKIAMDVAASEFYNSENKTYDLDFKTPNNDKSLVKTGAQLVDLYIDLVKKYPIVSIEDPFDQDDWENYAKLTA... | Cofactor: Binds 2 Mg(2+) ions per subunit . Mg(2+) is required for catalysis and for stabilizing the dimer . Unlike for mammalian and yeast enolases, Mg(2+) is dispensable to form an active closed conformation . Inhibited by high levels of Mg(2+) (By similarity).
Function: Glycolytic enzyme that catalyzes the conversio... |
Q7RA60 | MIINPKNYEHIFYSRGNPTVEVDLETTLGIFRAAVPSGASTGIYEALELRDNDKSRYLGKGVQQAIKNINEIIAPKLIGLDCREQKKIDNMMVQELDGSKTEWGWSKSKLGANAILAISMAICRAGAAANKTSLYKYVAQLAGKNTEKMILPVPCLNVINGGSHAGNKLSFQEFMIVPVGAPSFKEAMRYGAEVYHTLKSEIKKKYGIDATNVGDEGGFAPNILNAHEALDLLVASIKKAGYENKVKIAMDVAASEFYNSETKTYDLDFKTPNNDKSLVKTGQELVDLYIELVKKYPIISIEDPFDQDDWENYAKLTEAI... | Cofactor: Binds 2 Mg(2+) ions per subunit (By similarity). Mg(2+) is required for catalysis and for stabilizing the dimer (By similarity). Unlike for mammalian and yeast enolases, Mg(2+) is dispensable to form an active closed conformation (By similarity). Inhibited by high levels of Mg(2+) (By similarity).
Function: G... |
P84541 | AAVPSGASTGVYEALELRFRAPVEPY | Cofactor: Mg(2+) is required for catalysis and for stabilizing the dimer.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 2751
Sequence Length: 26
Pathway: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.
Subcellular Location: Cytopl... |
B2RLL7 | MEIVKIIGREILDSRGNPTVEVDVHLACGIIGRAAVPSGASTGENEAIELRDQDKARYCGKGVLKAVKNVNEVIDPALCGMSVLEQTAIDRKLIELDGTKTKSNLGANAMLGVSLAVAKAAAAYLDIPLYRYIGGSNTYVLPVPMMNIINGGSHSDAPIAFQEFMIRPVGACCFREGLRMGAEVFHALKKVLHDRGLSTAVGDEGGFAPALNGTEDAIESILKAVEAAGYVPGKDITIAMDCASSEFFKDGIYDYTKFEGEKGKKRSIDEQVAYLTELVGKYPIDSIEDGMSENDWEGWKKLTVALGDKVQLVGDDLFVT... | Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 45849
Sequence Length: 425
Pathway: Carbohydrate degradation; gly... |
Q9HJT1 | MELPIEEIKVRKVLDSRGNFTVEADVTVPNGFGRTSAPAGASTGETEVIAFSKSGIDASIQFFESKVKRSLIGFNALDQSGFDKLLTDIDGSGNFSNLGGNLATALSMSVAKAAAQSLGIPLYRYVGGIRSTIPRPMGNVIGGGKHARNGTSIQEFLVSAQGSTFLESAYINVLVHRRIGDMLSDKFKDISIGVGDERTWSVNLSDEEAFEILNEAVKEISSEKKVKIYTGVDFAADSLYENGKYVYKHTTKSRDEQIDYAISISKDFGVYYIEDPMYDTDFDGFAEITARIGDRSLIVGDDLYTTNPDRIRKGVEKKST... | Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 43402
Sequence Length: 401
Pathway: Carbohydrate degradation; gly... |
P42848 | MYVEIVDVRAREVLDSRGNPTVEAEVVLEDGTMGRAIVPSGASTGKFEALEIRDKDKKRYLGKGVLKAVENVNETIAPALIGMNAFDQPLVDKTLIELDGTENKSKLGANAILAVSMAVARAAANYLGLPLYKYLGGVNAKVLPVPLMNVINGGQHADNNLDLQEFMIVPAGFDSFREALRAGAEIFHTLKKILHEAGHVTAVGDEGGFAPNLSSNEEAIKVLIEAIEKAGYKPGEEVFIALDCAASSFYDEEKGVYYVDGEEKSSEVLMGYYEELVAKYPIISIEDPFAEEDWDAFVEFTKRVGNKVQIVGDDLYVTNV... | Function: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Catalytic Activity: (2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate
Sequence Mass (Da): 46870
Sequence Length: 429
Pathway: Carbohydrate degradation; gly... |
D5CHP5 | MIWKRHLSLDALNATSQNTLVAHLGIVYTRLGDDMLEAEMPVDARTHQPFGLLHGGASAALAETLGSMAGFLMTRDGQNVVGTELNATHHRAVAQGTVRGVCQPMHLGRSSQSWEIVVFDEQGRRCCTCRLSTMVLG | Function: Required for optimal enterobactin synthesis. Acts as a proofreading enzyme that prevents EntB misacylation by hydrolyzing the thioester bound existing between EntB and wrongly charged molecules.
Sequence Mass (Da): 14858
Sequence Length: 137
Pathway: Siderophore biosynthesis; enterobactin biosynthesis.
Subcel... |
A6T644 | MAWKRELTLAALNASSENTMVAHLGIIYTRLEAGLLEAEMPVDARTHQPFGLLHGGASAALAETLGSMAGWLMTEEGQCVVGTELNATHHRPVSSGKVRGECRPLHLGRQSQSWEIVVYDEKGRRCCTCRLGTAVLG | Function: Required for optimal enterobactin synthesis. Acts as a proofreading enzyme that prevents EntB misacylation by hydrolyzing the thioester bound existing between EntB and wrongly charged molecules (By similarity).
Sequence Mass (Da): 14799
Sequence Length: 137
Pathway: Siderophore biosynthesis; enterobactin bios... |
Q8ZR29 | MIWKRHLTLDELNATSQNTLVAHLGIVYTRLGDDVLEAEMPVDARTHQPFGLLHGGASAALAETLGSMAGYLMTRDGQCVVGTELNATHHRAISQGKVRGVCLPLHLGRQNQSWEITLFDEQGRRCCTCRLGTAVMG | Function: Required for optimal enterobactin synthesis. Acts as a proofreading enzyme that prevents EntB misacylation by hydrolyzing the thioester bound existing between EntB and wrongly charged molecules.
Sequence Mass (Da): 14939
Sequence Length: 137
Pathway: Siderophore biosynthesis; enterobactin biosynthesis.
Subcel... |
P98073 | MGSKRGISSRHHSLSSYEIMFAALFAILVVLCAGLIAVSCLTIKESQRGAALGQSHEARATFKITSGVTYNPNLQDKLSVDFKVLAFDLQQMIDEIFLSSNLKNEYKNSRVLQFENGSIIVVFDLFFAQWVSDENVKEELIQGLEANKSSQLVTFHIDLNSVDILDKLTTTSHLATPGNVSIECLPGSSPCTDALTCIKADLFCDGEVNCPDGSDEDNKMCATVCDGRFLLTGSSGSFQATHYPKPSETSVVCQWIIRVNQGLSIKLSFDDFNTYYTDILDIYEGVGSSKILRASIWETNPGTIRIFSNQVTATFLIESD... | Function: Responsible for initiating activation of pancreatic proteolytic proenzymes (trypsin, chymotrypsin and carboxypeptidase A). It catalyzes the conversion of trypsinogen to trypsin which in turn activates other proenzymes including chymotrypsinogen, procarboxypeptidases, and proelastases.
PTM: The chains are deri... |
P54355 | MFILNFNKMKNVKLLLMLGTAALLAACSNEADSLTTSIDAPVTASIDLQSVSYTDLATQLNDVSDFGKMIILKDNGFNRQVHVSMDKRTKIQLDNENVRLFNGRDKDSTSFILGDEFAVLRFYRNGESISYIAYKEAQMMNEIAEFYAAPFKKTRAINEKEAFECIYDSRTRSAGKDIVSVKINIDKAKKILNLPECDYINDYIKTPQVPHGITESQTRAVPSEPKTVYVICLRENGSTIYPNEVSAQMQDAANSVYAVHGLKRYVNFHFVLYTTEYSCPSGDAKEGLEGFTASLKSNPKAEGYDDQIYFLIRWGTWDNK... | Cofactor: Binds 1 zinc ion per subunit.
Function: Diarrheal toxin that hydrolyzes gelatin, azocoll, actin, tropomyosin, and fibrinogen.
Catalytic Activity: Broad proteolytic specificity, bonds hydrolyzed includes -Gly-|-Leu-, -Met-|-Leu-, -Phe-|-Leu-, -Cys-|-Leu-, -Leu-|-Gly-.
Sequence Mass (Da): 45411
Sequence Length:... |
P61550 | MGPEAWVRPLKTAPKPGEAIRLILFIYLSCFFLPVMSSEPSYSFLLTSFTTGRVFANTTWRAGTSKEVSFAVDLCVLFPEPARTHEEQHNLPVIGAGSVDLAAGFGHSGSQTGCGSSKGAEKGLQNVDFYLCPGNHPDASCRDTYQFFCPDWTCVTLATYSGGSTRSSTLSISRVPHPKLCTRKNCNPLTITVHDPNAAQWYYGMSWGLRLYIPGFDVGTMFTIQKKILVSWSSPKPIGPLTDLGDPIFQKHPDKVDLTVPLPFLVPRPQLQQQHLQPSLMSILGGVHHLLNLTQPKLAQDCWLCLKAKPPYYVGLGVEA... | Function: Retroviral envelope proteins mediate receptor recognition and membrane fusion during early infection. Endogenous envelope proteins may have kept, lost or modified their original function during evolution. This endogenous envelope protein has lost its original fusogenic properties.
PTM: The CXXC motif is highl... |
P0AEJ4 | MRRLRFSPRSSFARTLLLIVTLLFASLVTTYLVVLNFAILPSLQQFNKVLAYEVRMLMTDKLQLEDGTQLVVPPAFRREIYRELGISLYSNEAAEEAGLRWAQHYEFLSHQMAQQLGGPTEVRVEVNKSSPVVWLKTWLSPNIWVRVPLTEIHQGDFSPLFRYTLAIMLLAIGGAWLFIRIQNRPLVDLEHAALQVGKGIIPPPLREYGASEVRSVTRAFNHMAAGVKQLADDRTLLMAGVSHDLRTPLTRIRLATEMMSEQDGYLAESINKDIEECNAIIEQFIDYLRTGQEMPMEMADLNAVLGEVIAAESGYEREIE... | Function: Member of the two-component regulatory system EnvZ/OmpR involved in osmoregulation (particularly of genes ompF and ompC) as well as other genes . EnvZ functions as a membrane-associated protein kinase that phosphorylates OmpR in response to environmental signals; at low osmolarity OmpR activates ompF transcri... |
P0DTM4 | MEAVIKAFLTGYPGKTSKKDSKEKPLATSKKDPEKTPLLPTRVNYILIIGVLVLCEVTGVRADVHLLEQPGNLWITWANRTGQTDFCLSTQSATSPFQTCLIGIPSPISEGDFKGYVSDNCTTLGTDRLVSSADFTGGPDNSTTLTYRKVSCLLLKLNVSMWDEPHELQLLGSQSLPNITNIAQISGITGGCVGFRPQGVPWYLGWSRQEATRFLLRHPSFSKSTEPFTVVTADRHNLFMGSEYCGAYGYRFWNMYNCSQVGRQYRCGNARSPRPGLPEIQCTRRGGKWVNQSQEINESEPFSFTVNCTASSLGNASGCC... | Function: The surface protein (SU) attaches the virus to the host cell entry receptor TVA . This interaction triggers the refolding of the transmembrane protein (TM) thereby unmasking its fusion peptide and the formation of a reactive thiolate on Cys-100 to activate its fusogenic potential. Fusion occurs at the host ce... |
P33498 | FPILPGVWVDSTQGNFTKPKALPPAIFLICGDRAWQGIPSRPVGGPCYLGKLTMLAPNHTDIHKILANSSQTGVRHFRSVSHLDDTCSDEVQLWGPTARIFASILAPGVAAAQALREIERLACWSVKQANLTTSLLGDLLDDVTSIRHAVLQNRAAIDFLLLAHGHGCKDIAGMCCFNLSDHSEAIQKKFQLMKEHVNKIGVDSDPIGSWLRGLFGGIGEWAIHLLKGLLLGLVVILLLVVCLPCLLQFVSSSTRKM | Function: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).... |
P03399 | MDCLTDLRSTEGKVDQAGKTLILLVVWWGFGTTAEGHPLQQLWELPCDCSGGYVSPDLPITPTPSIAVASPLPDLRVWLQGSWGWGGGFRQQWECVFKPKIIPSVQEQPGPCECLTIATQMHSTCYEKAQECTLLGKTYFTAILQKTKLGSYEDGPNKLLQASCTGIWETSMLGPRCPCVCLDGGGPTDRFGRICAEGLEEIIRHSYPSVQYHPLALPRPRGVDLDPQTSDILEATHQVLNATNPQLAENCWLCMTLGTQSPQPSRRMAMSLSMEIAVLASLSGATHRVNRCQLLCREADNRTGIPVGYVHFTNCTSIQE... | Function: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).... |
P31796 | MDCLTNLRSAEGKVDQASKILILLVAWWGFGTTAEGYPLQQLWELPCDCSGGYVSSIPTYYTYSLDCGGSTAYLTYGSGTGSWSWGGGFKQQWECVFKPKIIPSVQGQPGPCPSECLQIATQMHSTCYEKTQECTLLGKTYFTAILQKTKLGSYEDGPNKLIQASCTGTVGKPVCWDPVAPVYVSDGGGPTDMIREESVRERLEEIIRHSYPSVQYHPLALPRSRGVDLDPQTSDILEATHQVLNATNPKLAENCWLCMTLGTPIPAAIPTNGNVTLDGNCSLSLPFGCNPPGSIDVSCYAGEADNRTGIPVGYVHFTNC... | Function: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).... |
P03398 | VAAAQALREIERLACWSVKQANLTTSLLGDLLDDVTSIRHAVLQNRAAIDFLLLAHGHGCEDIAGMCCFNLSDHSESIQKKFQLMKEHVNKIGVDSDPIGSWLRGLFGGIGEWAVHLLKGLLLGLVVILLLVVCLPCLLQFVSSSIRKMIDNSLGYREERKKFQEAYKQPERVV | Function: The transmembrane protein (TM) acts as a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (hepta... |
P10269 | MGFTTKIIFLYNLVLVYAGFDDPRKAIELVQKRYGRPCDCSGGQVSEPPSDRVSQVTCSGKTAYLMPDQRWKCKSIPKDTSPSGPLQECPCNSYQSSVHSSCYTSYQQCRSGNKTYYTATLLKTQTGGTSDVQVLGSTNKLIQSPCNGIKGQSICWSTTAPIHVSDGGGPLDTTRIKSVQRKLEEIHKALYPELQYHPLAIPKVRDNLMVDAQTLNILNATYNLLLMSNTSLVDDCWLCLKLGPPTPLAIPNFLLSYVTRSSDNISCLIIPPLLVQPMQFSNSSCLFSPSYNSTEEIDLGHVAFSNCTSITNVTGPICAV... | Function: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).... |
P19557 | MDQDLDGAERGERGGGSEELLQEEINEGRLTAREALQTWINNGEIHPWVLAGMLSMGVGMLLGVYCQLPDTLIWILMFQLCLYWGLGETSRELDKDSWQWVRSVFIIAILGTLTMAGTALADDDQSTLIPNITKIPTKDTEPGCTYPWILILLILAFILGILGIILVLRRSNSEDILAARDTIDWWLSANQEIPPKFAFPIILISSPLAGIIGYYVMERHLEIFKKGCQICGSLSSMWGMLLEEIGRWLARREWNVSRVMVILLISFSWGMYVNRVNASGSHVAMVTSPPGYRIVNDTSQAPWYCFSSAPIPTCSSSQWG... | Function: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).... |
P51519 | MPKERRSRRRPQPIIRWVSLTLTLLALCQPIQTWRCSLSLGNQQWMTTYNQEAKFSISIDQILEAHNQSPFCPRSPRYTLDFVNGYPKIYWPPPQGRRRFGARAMVTYDCEPRCPYVGADHFDCPHWDNASQADQGSFYVNHQILFLHLKQCHGIFTLTWEIWGYDPLITFSLHKIPDPPQPDFPQLNSDWVPSVRSWALLLNQTARAFPDCAICWEPSPPWAPEILVYNKTISGSGPGLALPDAQIFWVNTSLFNTTQGWHHPSQRLLFNVSQGNALLLPPISLVNLSTVSSAPPTRVRRSPVAALTLGLALSVGLTGI... | Function: The surface protein (SU) attaches the virus to the host cell by binding to its receptor. This interaction triggers the refolding of the transmembrane protein (TM) and is thought to activate its fusogenic potential by unmasking its fusion peptide. Fusion occurs at the host cell plasma membrane (By similarity).... |
Q9VQB7 | MPILPILIGILHLSLAEDAKHLDGFSLPSLPSEHLIRYLNTFPKLKQQLPTNLTGKGTISSACWGHERDCTPAGRFQTPQCPGEHTGWARSKEAQVRTFYNQADFGYIQEQLSQLTPQCVPTYLGDSSLECTHYLRFCRGRNLLFDFRGLEQREERIRYHMDVLGPGQLLGHCKLNRTRLSGEMEHIGSALQSWGPELRNFDVLPHPVLESGLCDVVVNTPTFIMKIDATYNMYHHFCDFFNLYASLFVNQSHPAAFNTDVQILIWETYPYDSPFRDTFKAFSQRPVWTLSDVEGKRVCFKNVVLPLLPRMIFGLFYNTP... | Function: Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in extracellular proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Specifically glycosylates the Thr residue located between the fifth and sixth conserved cysteines... |
Q5NDL2 | MLMLFVFGVLLHEVSLSGQNEAPPNTHSIPGEPLYNYASIRLPEEHIPFFLHNNRHIATVCRKDSLCPYKKHLEKLKYCWGYEKSCKPEFRFGYPVCSYVDMGWTDTLESAEDIFWKQADFGYARERLEEMHVLCQPKETSDSSLVCSRYLQYCRATNLYLDLRNIKRNHDRFKEDFFQSGEIGGHCKLDIRTLTSEGQRKSPLQSWFAELQSYTQLNFRPIEDAKCDIVIEKPTYFMKLDAGVNMYHHFCDFINLYITQHVNNSFSTDVYIVMWDTSSYGYGDLFSDTWNAFTDYDVIHLKTYDSKRVCFKEAVFSLLP... | Function: Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in extracellular proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Specifically glycosylates the Thr residue located between the fifth and sixth conserved cysteines... |
Q08CY9 | MVPLWLLLLFHVIHFSHGNEIDSAASNGSALSYHYGKLYLPDDHIPYYLHSNRHIAALCRRDPHCPFKQHLQNLNSCWGYEKSCTKGHGYSYPVCDQVDFGWAKTIEESQEVFWKQADFGYVKERLAETQILCRPQEQGDSMLACSRNLQHCRATNLYLDLRNPRRGQENFKEDFLQEGEIGGRCNLDKQALLSQGAWKSPLQSWFAELQSYSSLTFKPVEDAHCDIIIDKPTYFMKLDAGVNMYHHFCDFVNLYITQHVNNSFSTDINIVMWTTSVYGYGDLFSDTWKAFTDYDITHLKAYDNKRVCFKDAVFALLPRM... | Function: Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in extracellular proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Specifically glycosylates the Thr residue located between the fifth and sixth conserved cysteines... |
Q8LC53 | MTKFVRKYMFCLVLVFAACSLVVNSIRTPPLKNTVNGGEKKNADIEQAQTHHKKEISKNGGVEMEMYPTGSSLPDCSYACGACSPCKRVMISFECSVAESCSVIYRCTCRGRYYHVPSRA | Function: Controls stomatal patterning. Regulates the number of cells that enter, and remain in, the stomatal lineage by inhibiting protodermal cells from adopting the meristemoid mother cell (MMC) fate in a non-cell-autonomous manner. Mediates stomatal development inhibition. MEPF2: mobile signal controlling stomatal ... |
Q9SV72 | MKHEMMNIKPRCITIFFLLFALLLGNYVVQASRPRSIENTVSLLPQVHLLNSRRRHMIGSTAPTCTYNECRGCRYKCRAEQVPVEGNDPINSAYHYRCVCHR | Function: Positively regulates stomatal density and patterning. Acts by competing with EPF2 (AC Q8LC53) for the same receptors, ERECTA (AC Q42371) and TMM (AC Q9SSD1). Not cleaved by the protease CRSP (AC Q9LNU1) .
Sequence Mass (Da): 11840
Sequence Length: 102
Domain: The loop (82-95) connecting the two anti-parallel ... |
Q95XR4 | MSANRTVTVFSSSAEDQEPIELAEDSLQNLDKMLAEEKEEHQLLKDEVVLLRKENVEAKTYSTLLEIMLDEAEEKASSAQETTSEENNLKILNRDLVAENLELKEMKEELRKIWLSDSKKFQEALTRISDENTKLQKDCHELESIRQCAQFALDNCNEELEKTQTENEEHESRIETLEREVCEKDIAMKDIVERKDEISLQLELQTKEFTSALNDLMYGREDTLKQIHQMKENWKVKQNEFEVEITKLKSQNDYFDSERLQLTDRIRALLNELSDVRLELGSTRLAMKEKAEVTEAVTSFNKDLRDKLEDEIARLGECLQ... | Function: Involved in autophagy . Thought to act as an adapter protein that brings PGL granules to autophagic structures containing lgg-1 . Association with other adapters such as sepa-1 is required for the accumulation and degradation of germ cell specific P-granules by autophagy in somatic cells . This ensures exclus... |
Q45409 | MTQNLPQPPAVNAPENELDLVRYLDVLVANRWLIAGIAAAVMLLGAAYAFLARPVYEADIMVQVEDNPNSAKSLLGDVSSLFDVKTDANAEIEILRSRMVVGKAVDNLHLYITAKPRYFPLIGAWISSRATRLSEPGLFGLGGYVWGTESIDVDGFDVPEALEGQPFKLIVLGNGRYRLENKSLDAPIEGVVGEPLEAKQSIGTIQLQVNNLTAKAGATFELERDSRLKTMEMLQDKLKIAEKGKQSGIIGASLDGTNPALTAAIMNQIATEYVAQNIKRKAEEAERSLVFLDGLLPQLKLELERAEMKYNEMRNLRGTF... | Function: Probably involved in polymerization and/or export of exopolysaccharide EPS I which functions as a virulence factor. May be involved in an ATP-dependent process in the pathway for EPS I production, possibly export of the trimeric repeat units across the inner membrane or their polymerization.
Catalytic Activit... |
P71052 | MIIALDTYLVLNSVIAGYQFLKDSYQFYDSGALLLTAVSLLLSYHVCAFLFNQYKQVWTYTGLGELIVLLKGITLSAAVTGVIQYAVYHTMFFRLLTACWVLQLLSIGGTRILSRVLNESIRKKRCASSRALIIGAGSGGTLMVRQLLSKDEPDIIPVAFIDDDQTKHKLEIMGLPVIGGKESIMPAVQKLKINYIIIAIPSLRTHELQVLYKECVRTGVSIKIMPHFDEMLLGTRTAGQIRDVKAEDLLGRKPVTLDTSEISNRIKGKTVLVTGAGGSIGSEICRQISAFQPKEIILLGHGENSIHSIYTELNGRFGKH... | Function: Involved in biofilm formation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66266
Sequence Length: 598
Subcellular Location: Cell membrane
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P52641 | MKKVLVVFGTRPEAIKMAPLVKALQADASLQCGVCVTAQHREMLDQVLRLFDIRPDYDLNVMKPGQDLYELTSNILTGVKSVLESFEPDLVLVHGDTSTTLATTLAAYYKQVPVGHIEAGLRTGNLYSPWPEEVNRKVTGSLAALHFAPTERSRRNLLNEGVPADAVVVTGNTVIDALLSVRQRLQTDTALCRNTASLIPYNIGERRIVLVTGHRRESFGDGFERICSTLTSIARAHPDVDIVYPVHLNPNVREPVGRLLKGIANIHLIEPLDYLPFVYLMDKAHIILTDSGGIQEEAPSLGKPVLVMRDTTERPEAVEA... | Function: May be involved in synthesis of N-acetyltrideoxygalactose, a component of exopolysaccharide EPS I which functions as a virulence factor.
Catalytic Activity: UDP-N-acetyl-alpha-D-glucosamine = UDP-N-acetyl-alpha-D-mannosamine
Sequence Mass (Da): 40944
Sequence Length: 375
Pathway: Glycan metabolism; exopolysac... |
Q45411 | MQKTAPRPLPARISFLSASVLGLGAAVASRGAVFVSNILLAHSLTVHDFGLFSYAYVTALNLGLFLATGVSQAAGHVLPLIENPERKRTQLCAFIVLLMALIAVAAAALYLSSASISVAAFGSEQGSGALRMAAIVLIATAFTQALQSFQYAMHEHRSSATISIGAAVLLLTMLWAMGPIRQPALALTIFLAVNAGAAVSQLLVLARATPSQRGPWRTGREELRLAVKHALPSVLTTSMGAPVHWICLSMLAAMTDGAHQLALFSVAFQWYIAITFIPATLGNLALPFLARHAGATETTVRQRFRSALLFGGGLSLALGC... | Function: Probably involved in polymerization and/or export of exopolysaccharide EPS I which functions as a virulence factor. May play a role in export of EPS I or its intermediates across the membranes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45766
Sequence Length: 436
Subcellular Location: ... |
Q45412 | MKYSAPIRLNALSAIVSHHGVLVVIGMLLAVPMAFPLFPIAATYCAAILAILLPLGRLQHVLATASSIAFAWLLTLRNPSRGLVEAGLGDDALHYMNAFYEFQQNYCCSPLDVLKTGIRSAGGGEPIFWYLSYGVAKLFDTPLMVWAILIFISLMLVWIAIYRSTERFAYVVFVAYLSTITLYALQGSAIRQAVAVGLVMVALDLLIRRRLVWAACVGLLAAGTHSSAAALLLVCATVMLFLSKDYGMLARKASWLGQLGRLLVLLVLAVAAVAFGSAEFVMSKIQARLSENQTGSAWEFQLAVEAVLACLFAWLFRMKL... | Function: Probably involved in polymerization and/or export of exopolysaccharide EPS I which functions as a virulence factor. May play a role in export of EPS I or its intermediates across the membranes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46012
Sequence Length: 418
Subcellular Location: ... |
P71056 | MIVYAVNMGIVFIWSWFAKMCGGRDDSLATGYRPNKLLIWIPLASLVLVSGLRYRVGTDFQTYTLLYELAGDYQNVWQIFGFGTAKTATDPGFTALLWLMNFITEDPQIMYFTVAVVTYSFIMKTLADYGRPFELSVFLFLGTFHYYASFNGIRQYMVAAVLFWAIRYIISGNWKRYFLIVLVSSLFHSSALIMIPVYFIVRRKAWSPAIFGLSALFLGMTFLYQKFISVFVVVLENSSYSHYEKWLMTNTNGMNVIKIAVLVLPLFLAFCYKERLRSLWPQIDIVVNLCLLGFLFGLLATKDVIFARFNIYFGLYQMIL... | Function: May be involved in the production of the exopolysaccharide (EPS) component of the extracellular matrix during biofilm formation. EPS is responsible for the adhesion of chains of cells into bundles. Required for biofilm maintenance.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42555
Seque... |
Q83VR1 | MEKHIKHAIRWPSLDTIPWAWVAIAIGLLILYFPTFWDLFHGLWGTERHAHGPIVFFVSIWFFYFKFKQLPEYGITYDPSPKLGWPILVLGLLLFILGRSQTLLIFEVGSLIPVLLGITLIFMGTRVAKFLWFAFFFLCFVVPLPAFVVDAATLPMKTAVSFATAHILYALDYPIARTGVMLTIGQYQLLVADACAGLNSLFTLEVLGLLYMNVTHHESPFRNFMLAVLIIPISFIANVTRVIVLALITYHWGDAAGQGFLHEFSGIVLFITALMLVIATDSLLRFFSRKFEKVPSTQSVDLKR | Function: Transpeptidase that recognizes and modifies its substrate by proteolytic cleavage of a sorting signal. Following cleavage, a covalent intermediate is formed via a thioester bond between the exosortase and its substrate, which is then transferred and covalently attached to the cell membrane (By similarity). Th... |
P71060 | MKFTINFSANLTAFLLSVFLSVWMTPFIVKTLGVEAFGFVHLTQNVINYFSVITVALSSVVVRFFSVAAHRGEREKANAYISNYLAASVLISLLLLLPLAGSAFFIDRVMNVPQALLADVRLSILIGSVLFILTFLMAGFGAAPFYANRLYITSSIQAVQMLIRVLSVLLLFACFAPKIWQIQLAALAGAVIASVLSFYFFKKLIPWFSFRMKDLSFRTSKELFQAGAWSSVNQIGVLLFLQIDLLTANLMLGASASGKYAAIIQFPLLLRSLAGTVASLFAPIMTSYYSKGDMEGLMNYANKAVRLNGLLLALPAALLG... | Function: May be involved in the production of the exopolysaccharide (EPS) component of the extracellular matrix during biofilm formation. EPS is responsible for the adhesion of chains of cells into bundles.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55055
Sequence Length: 505
Subcellular Locati... |
P45781 | MRAKQRGVALIVILLLLAVMVSIAATMAERLFSQFQRATHQLNYQQAYWYSLGVEALAKKGIEQSYQDSETINLSQPWALKEQTYPLDYGQVRGKIRDMQACFNLNALAGVKLTPDSVKKPYLLTVLQALLEGLEVESYQAEVIADSTLEFIDKDDSVRTAYGVEDSYYESMIPAYMAADTWLADASEWRAVQQVGGETMNKALPYVCALPTDQWRLNVNTLPAEQAALLAAMFSPTLSPESAKTLLEGRPFDGWASVDDFLAQSALTGVDNAVREEAKKYLSVDSHYFELDAQVLVDTSRVRIRSLFYSNDKKTATVIR... | Function: Component of the type II secretion system required for the energy-dependent secretion of extracellular factors such as proteases and toxins from the periplasm. Plays a role in pseudopilus assembly and seems to control its length. Interacts with the pseudopilus tip complex that is critical for the recognition ... |
Q09523 | MIIKRLNFSCRLFSTASTSTSYEKTPIQPATKCLQLAVIGAPNVGKSLLTNSLIRCPLSAVSSKMDTTTRNISASICSDSTQLVFVDSPGAVSTSHVRQTMKKTSATSGDRVLQDPERALQRAQHVLVVQDSTAPGAYIHHRVLHMLHRYSHVPSILVMNKIDLVMRRSDLLPLVEILTNGQLSDNQQISTKPAQIGRLGKSLSTNIQSSSSFKPSDEKWQSQFRELIQKPTWKCSYSETRSLFRTICGWSGFERVFFVSSLNGEGIDELRDHLMSISPQGEWKMQDGMPTGESAQQLCIDSIRAAVLDTTPSDVAYTVQ... | Function: Probable GTPase that plays a role in the mitochondrial ribosomal small subunit assembly (By similarity). Specifically binds the 12S mitochondrial rRNA (12S mt-rRNA) to a 33 nucleotide section delineating the 3' terminal stem-loop region (By similarity). May act as a chaperone that protects the 12S mt-rRNA on ... |
Q8JIF5 | MAAPWLQRWRGAYAGPSGPLRLVRLHGVQRSSWRAAHAAAGAFGAGPHPGPPQRAANPGPGPHPPPVATSREKHARIVQGRPDQPAEPKVLRISIIGAPNSGKSTLSNQLLGRKVFPVSKKVHTTRCKARGVITHEDTQLIILDTPGLTSPMKAKRHKLEAAMLTDPWDSMKHADLVLVLVDVSDHWTRNSLSLEVLKCLSQFPHIPSVLVLNKVDLLKKKIILLGLINELTEGIVNGKKLKVRSEFEYNSSSPAKTVLKVTQTPPPENRARESPCQLETDKAQEGSSLDNSSDVKASESSLDTEAREQKPYKYGDQKNR... | Function: Probable GTPase that plays a role in the mitochondrial ribosomal small subunit assembly. Specifically binds the 12S mitochondrial rRNA (12S mt-rRNA) to a 33 nucleotide section delineating the 3' terminal stem-loop region. May act as a chaperone that protects the 12S mt-rRNA on the 28S mitoribosomal subunit du... |
B0S6U7 | MTLRSCETFLRRSLRFSTALNLTAFPEHEQLYLRVSSGCSVFRPQTVRKCLFHWTPACTVSQGVFLDRLQKGAAVTDESLCNQPVSVSPDRAQQFSLLMKDPDQPENAKSLKVAIVGSPNAGKSTLTNQLLGRKLFAVSSKVHTTRSRAVGVLTENDTQIVLLDTPGLTTQIKAKRHQLENSLLVDPFKSLKEADLVVVLVDVSDKWTRSKLSYEVLKCLALNPDVPAVLVLNKVDLLKNKALLLDITAQLTEGMVNGKKIRIHGASKPVRKAAAGANSRLKEKKAAGSLEDEADHEDKLKALKSHGGWPHFKDVFMLSS... | Function: Probable GTPase that plays a role in the mitochondrial ribosomal small subunit assembly. Specifically binds the 12S mitochondrial rRNA (12S mt-rRNA) to a 33 nucleotide section delineating the 3' terminal stem-loop region. May act as a chaperone that protects the 12S mt-rRNA on the 28S mitoribosomal subunit du... |
O75616 | MAAPSWRGARLVQSVLRVWQVGPHVARERVIPFSSLLGFQRRCVSCVAGSAFSGPRLASASRSNGQGSALDHFLGFSQPDSSVTPCVPAVSMNRDEQDVLLVHHPDMPENSRVLRVVLLGAPNAGKSTLSNQLLGRKVFPVSRKVHTTRCQALGVITEKETQVILLDTPGIISPGKQKRHHLELSLLEDPWKSMESADLVVVLVDVSDKWTRNQLSPQLLRCLTKYSQIPSVLVMNKVDCLKQKSVLLELTAALTEGVVNGKKLKMRQAFHSHPGTHCPSPAVKDPNTQSVGNPQRIGWPHFKEIFMLSALSQEDVKTLK... | Function: Probable GTPase that plays a role in the mitochondrial ribosomal small subunit assembly. Specifically binds the 12S mitochondrial rRNA (12S mt-rRNA) to a 33 nucleotide section delineating the 3' terminal stem-loop region. May act as a chaperone that protects the 12S mt-rRNA on the 28S mitoribosomal subunit du... |
Q9CZU4 | MAAPRRYCAGLVRALLGARQVGSHAGREWLAPPGCLLGNQARCVSCVVGSTFSGPLLASASSRYGQDSALDRILGFSQPDSSLVPSVPAVSVHRDEQNLLLVHTPDMPENPRVLRVVLLGAPNAGKSTLSNQLLGRKVFPVSKKVHTTRCQALGVITEKETQVILLDTPGIISPVKQKRHHLERSLLEDPWTSMESADLVVVLVDVSDKWTRSRLNPQVLQCLTKFSQVPSILVLNKVDCLKQKSVLLELTAALTEGVVNGKKLNIKQALRSRSSTHCPGPETEGPNAHSVRNPQRIGWPYFQEIFMLSALNNKDVNTLK... | Function: Probable GTPase that plays a role in the mitochondrial ribosomal small subunit assembly. Specifically binds the 12S mitochondrial rRNA (12S mt-rRNA) to a 33 nucleotide section delineating the 3' terminal stem-loop region. May act as a chaperone that protects the 12S mt-rRNA on the 28S mitoribosomal subunit du... |
B5X2B8 | MAFRVSISTFGKSLRVRRVANVSAPLANASPFLRTGWAARPPGTNNGHGFRFTPACFITSDAFLSRLAKGKAETDDTHYHHPASVLPDSAEQLSLLVKDPDQPENSKVLRVAIIGAPNAGKSTLSNQLLGRKVFAVSKKVHTTRARALGVLTEDDTQIILLDTPGLTTPTKVKRHQLEKSLLEDPWNTVKEAGLVVVMVDVSDKWACNKLDFEVLKCLTQHPDVPAVLVLNKVDLLKSKSRLLEITADLTCGVVNGRKLQVRRVIKPPWAERRTDREARTSGSGDEEKPGGDVADGEGSEALSGLSKEQLRALKTQQGWA... | Function: Probable GTPase that plays a role in the mitochondrial ribosomal small subunit assembly. Specifically binds the 12S mitochondrial rRNA (12S mt-rRNA) to a 33 nucleotide section delineating the 3' terminal stem-loop region. May act as a chaperone that protects the 12S mt-rRNA on the 28S mitoribosomal subunit du... |
Q9NZ08 | MVFLPLKWSLATMSFLLSSLLALLTVSTPSWCQSTEASPKRSDGTPFPWNKIRLPEYVIPVHYDLLIHANLTTLTFWGTTKVEITASQPTSTIILHSHHLQISRATLRKGAGERLSEEPLQVLEHPRQEQIALLAPEPLLVGLPYTVVIHYAGNLSETFHGFYKSTYRTKEGELRILASTQFEPTAARMAFPCFDEPAFKASFSIKIRREPRHLAISNMPLVKSVTVAEGLIEDHFDVTVKMSTYLVAFIISDFESVSKITKSGVKVSVYAVPDKINQADYALDAAVTLLEFYEDYFSIPYPLPKQDLAAIPDFQSGAME... | Cofactor: Binds 1 zinc ion per subunit.
Function: Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC... |
A6QPT7 | MANSCRKLIFNIYVVFYCSAVIMPQICICSQFTSSPIDQFNKDPKAFPVATNGEIFPWHELRLPTVVIPLHYDLLIHPNLTSLDFVASEKIEVLVRDATQFIILHSKDLEILNASLQSEEDVRYKKPGENLTVLSYPAHQQIALLVPEKLRAHLRYSVAIDFQAKLADGFEGFYKSTYRTLGGETRTIAVTDFEPTEARMAFPCFDEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLEDHFETTVRMSTYLVAYIVCDFTSVSGTASSGVKVSIYASPDKWSQTHYALEASVKLLDFYENYFDIHYPLPKLDLV... | Cofactor: Binds 1 zinc ion per subunit.
Function: Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC... |
Q6P179 | MFHSSAMVNSHRKPMFNIHRGFYCLTAILPQICICSQFSVPSSYHFTEDPGAFPVATNGERFPWQELRLPSVVIPLHYDLFVHPNLTSLDFVASEKIEVLVSNATQFIILHSKDLEITNATLQSEEDSRYMKPGKELKVLSYPAHEQIALLVPEKLTPHLKYYVAMDFQAKLGDGFEGFYKSTYRTLGGETRILAVTDFEPTQARMAFPCFDEPLFKANFSIKIRRESRHIALSNMPKVKTIELEGGLLEDHFETTVKMSTYLVAYIVCDFHSLSGFTSSGVKVSIYASPDKRNQTHYALQASLKLLDFYEKYFDIYYPL... | Cofactor: Binds 1 zinc ion per subunit.
Function: Aminopeptidase that plays a central role in peptide trimming, a step required for the generation of most HLA class I-binding peptides. Peptide trimming is essential to customize longer precursor peptides to fit them to the correct length required for presentation on MHC... |
B9DNL3 | MTEHKSGFVAIIGRPNVGKSTFMNRVLGHKIAIMSDKAQTTRNKIHGVMTEDDAQIIFVDTPGIHKPKHKLGDYMMKVAKNTLTEVDAVIFMVNANEEIGRGDEYIMEMLKNIKTPVFLVINKIDLVHPDQIMPIIESYEKHMHFTEAVPMSALEGLNVDHFINVLKSYMPEGPQYYPDGQISDHPEQFVVSELIREKVLHLTSEEIPHSIGVNVDRMVKQSEDRVRIEATIYVERDSQKGIVIGKGGKKLKEIGKRARIDIENLLGSKVYLDLWVKVQKDWRNKVNFIRQMGYIEDQD | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34208
Sequence Length: ... |
Q9RDF2 | MSVRTQSSEEPAETVHRAGFACFVGRPNAGKSTLTNALVGQKVAITSNRPQTTRHTVRGIVHREDAQLILVDTPGLHKPRTLLGERLNDVVRTTWAEVDVIGFCLPANEKLGPGDRFIAKELAGIRKTPKVAIVTKTDLVDSKTLAEQLIAIDQLGKELGIAWAEIVPVSATANQQVDLLADLLTPLLPEGPALYPEGDLTDEPEQVMVAELIREAALEGVRDELPHSIAVVVEEMLPREDRPADKPLLDIHANVYIERPSQKGIIIGPKGKRLKDVGIKSRTQIEALLGTPVFLDLHVKVAKDWQRDPKQLRRLGF | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34783
Sequence Length: ... |
B2FPX8 | MSEQTPHHCGSVAVIGRPNVGKSTLTNALVGAKVSIVSNRPQTTRHRLLGIATYPEGQLVLVDTPGLHKVQKRAMNRVMNRAARGSLEGVDAGLLVIEAGRWDEEDSLAFNVLRDAGIPVVLVVNKIDRLKEKGALLPFLQQVTEGRDFAAVHPISAQKRNGLEALVRDVLKLLPEAPPMFGEDEITDRSQRFLAGELVREQLMRQLGEELPYATTVEIERFTEDGNLLRIGAVIWVEREGQKAIVIGKGGARLKEIGAKSRLQMERLFGAKVFLETWVRVREGWSDDEAALKAFGYE | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 32944
Sequence Length: ... |
P37214 | MSFKSGFVAILGRPNVGKSTFLNHVMGQKIAIMSDKAQTTRNKIMGIYTTDKEQIVFIDTPGIHKPKTALGDFMVESAYSTLREVDTVLFMVPADEKRGKGDNMIIERLKAAKVPVILVINKIDKVHPNQLLEQIDDFRNQMDFQEIVPISALQGNNVSHLVDLLVDHLEEGFQYFPADQITDHPERFLVSEMIREKVLLLTREEIPHSVAVVIDSMARDEETHKIHIRATIMVERDSQKGIIIGKKGAMLKKIGQMARRDIELMLGDKVYLETWVKVKKNWRDKKLDLADFGYNKKEY | Function: An essential GTPase that binds both GDP and GTP, with rapid nucleotide exchange. Plays a role in 16S rRNA processing and 30S ribosomal subunit biogenesis and possibly also in cell cycle regulation and energy metabolism (By similarity). Has GTPase activity, binds both GDP and GTP, does not bind UTP, CTP or ATP... |
P18414 | MNPFRILGDLSHLTSILILIHNIKTTRYIEGISFKTQTLYALVFITRYLDLLTFHWVSLYNALMKIFFIVSTAYIVVLLQGSKRTNTIAYNEMLMHDTFKIQHLLIGSALMSVFFHHKFTFLELAWSFSVWLESVAILPQLYMLSKGGKTRSLTVHYIFAMGLYRALYIPNWIWRYSTEDKKLDKIAFFAGLLQTLLYSDFFYIYYTKVIRGKGFKLPK | Function: Required for the retention of luminal endoplasmic reticulum proteins. Determines the specificity of the luminal ER protein retention system. Also required for normal vesicular traffic through the Golgi. This receptor strongly recognizes H-D-E-L and weakly recognizes D-D-E-L and K-D-E-L.
Location Topology: Mul... |
Q4F7G0 | MESERLESHLLNKQEEEASSFTSGLLLSTSVVVAGSFCYGCAMSYSSPAQSKIMEELGLSVADYSFFTSVMTLGGMITAVFSGKISALVGRRQTMWISDVCCIFGWLAVAFAHDIIMLNTGRLFLGFGVGLISYVVPVYIAEITPKTFRGGFSYSNQLLQCLGISLMFFTGNFFHWRTLALLSAIPSAFQVICLFFIPESPRWLAMYGQDQELEVSLKKLRGENSDILKEAAEIRETVEISRKESQSGIRDLFHIGNAHSLIIGLGLMLLQQFCGSAAISAYAARIFDKAGFPSDIGTTILAVILIPQSIVVMLTVDRWG... | Function: Sugar transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51053
Sequence Length: 462
Subcellular Location: Membrane
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Q93YP9 | MSFRDDNTEEGRNDLRRPFLHTGSWYRMGSRQSSMLESSQVIRDSSISVLACVLIVALGPIQFGFTCGYSSPTQAAITKDLGLTVSEYSVFGSLSNVGAMVGAIASGQIAEYVGRKGSLMIAAIPNIIGWLSISFAKDTSFLYMGRLLEGFGVGIISYTVPVYIAEIAPQTMRGALGSVNQLSVTIGIMLAYLLGLFVPWRILAVLGVLPCTLLIPGLFFIPESPRWLAKMGLTDDFETSLQVLRGFETDITVEVNEIKRSVASSSKRSAVRFVDLKRRRYYFPLMVGIGLLALQQLGGINGVLFYSSTIFESAGVTSSN... | Function: Sugar transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52787
Sequence Length: 488
Subcellular Location: Membrane
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Q3ECP7 | MRGEIDEANLAPETSLINKENQDSSATITTTLLLTTFVAVSGSFVFGSAIGYSSPVQSDLTKELNLSVAEYSLFGSILTIGAMIGAAMSGRIADMIGRRATMGFSEMFCILGWLAIYLSKVAIWLDVGRFLVGYGMGVFSFVVPVYIAEITPKGLRGGFTTVHQLLICLGVSVTYLLGSFIGWRILALIGMIPCVVQMMGLFVIPESPRWLAKVGKWEEFEIALQRLRGESADISYESNEIKDYTRRLTDLSEGSIVDLFQPQYAKSLVVGVGLMVLQQFGGVNGIAFYASSIFESAGVSSKIGMIAMVVVQIPMTTLGV... | Function: Sugar transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 50740
Sequence Length: 470
Subcellular Location: Membrane
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Q9FRL3 | MSFRDDNEEARNDLRRPFIHTGSWYRMGSRQSSMMGSSQVIRDSSISVLACVLIVALGPIQFGFTCGYSSPTQAAITKDLGLTVSEYSVFGSLSNVGAMVGAIASGQIAEYIGRKGSLMIAAIPNIIGWLCISFAKDTSFLYMGRLLEGFGVGIISYTVPVYIAEIAPQNMRGGLGSVNQLSVTIGIMLAYLLGLFVPWRILAVLGILPCTLLIPGLFFIPESPRWLAKMGMTDEFETSLQVLRGFETDITVEVNEIKRSVASSTKRNTVRFVDLKRRRYYFPLMVGIGLLVLQQLGGINGVLFYSSTIFESAGVTSSNA... | Function: Sugar transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52901
Sequence Length: 487
Subcellular Location: Membrane
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P93051 | MSKASDAVREPLVDKNMAGSKPDQPWMVYLSTFVAVCGSFAFGSCAGYSSPAQAAIRNDLSLTIAEFSLFGSLLTFGAMIGAITSGPIADLVGRKGAMRVSSAFCVVGWLAIIFAKGVVALDLGRLATGYGMGAFSYVVPIFIAEIAPKTFRGALTTLNQILICTGVSVSFIIGTLVTWRVLALIGIIPCAASFLGLFFIPESPRWLAKVGRDTEFEAALRKLRGKKADISEEAAEIQDYIETLERLPKAKMLDLFQRRYIRSVLIAFGLMVFQQFGGINGICFYTSSIFEQAGFPTRLGMIIYAVLQVVITALNAPIVD... | Function: Sugar transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49700
Sequence Length: 463
Subcellular Location: Membrane
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Q0WQ63 | METRKDDMEKRNDKSEPLLLPENGSDVSEEASWMVYLSTIIAVCGSYEFGTCVGYSAPTQFGIMEELNLSYSQFSVFGSILNMGAVLGAITSGKISDFIGRKGAMRLSSVISAIGWLIIYLAKGDVPLDFGRFLTGYGCGTLSFVVPVFIAEISPRKLRGALATLNQLFIVIGLASMFLIGAVVNWRTLALTGVAPCVVLFFGTWFIPESPRWLEMVGRHSDFEIALQKLRGPQANITREAGEIQEYLASLAHLPKATLMDLIDKKNIRFVIVGVGLMFFQQFVGINGVIFYAQQIFVSAGASPTLGSILYSIEQVVLTA... | Function: Sugar transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51024
Sequence Length: 470
Subcellular Location: Membrane
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Q7XA64 | MEGENSSIEKGLLLIRKEESANTTPFLVFTTFIIVSASFSFGVALGHTAGTMASIMEDLDLSITQFSVFGSLLTFGGMIGALFSATIADSFGCKMTLWITEVFCISGWLAIALAKNIIWLDLGRFFVGIGVGLLSYVVPVYIAEITPKTVRGTFTFSNQLLQNCGVATAYYLGNFMSWRIIALIGILPCLIQLVGLFFVPESPRWLAKEGRDEECEVVLQKLRGDEADIVKETQEILISVEASANISMRSLFKKKYTHQLTIGIGLMLLQQLSGSAGLGYYTGSVFDLAGFPSRIGMTVLSIVVVPKAILGLILVERWGR... | Function: Sugar transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35713
Sequence Length: 327
Subcellular Location: Membrane
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Q69SP5 | MTPAPAAASYRALVALLLVAVAVADDGSTLLEIKKSFRNVDNVLYDWAGGDYCSWRGVLCDNVTFAVAALNLSGLNLGGEISPAVGRLKGIVSIDLKSNGLSGQIPDEIGDCSSLKTLDLSFNSLDGDIPFSVSKLKHIESLILKNNQLIGVIPSTLSQLPNLKILDLAQNKLSGEIPRLIYWNEVLQYLGLRGNNLEGSISPDICQLTGLWYFDVKNNSLTGPIPETIGNCTSFQVLDLSYNKLSGSIPFNIGFLQVATLSLQGNMFTGPIPSVIGLMQALAVLDLSYNQLSGPIPSILGNLTYTEKLYMQGNKLTGPI... | Function: Receptor kinase involved in the regulation of thermotolerance . Functions as positive regulator of heat tolerance . May be involved in the regulation of cell proliferation and cell growth .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass ty... |
I1Z695 | MTTTTTTRLLLAAILLAVAAADDDGQTLLEIKKSFRNVDNVLYDWAGDGAPRRYCSWRGVLCDNVTFAVAALNLSGLNLGGEISPAIGNLKSVESIDLKSNELSGQIPDEIGDCTSLKTLDLSSNNLGGDIPFSISKLKHLENLILKNNQLVGMIPSTLSQLPNLKILDLAQNKLNGEIPRLIYWNEVLQYLGLRSNNLEGSLSPEMCQLTGLWYFDVKNNSLTGIIPDTIGNCTSFQVLDLSYNRLTGEIPFNIGFLQVATLSLQGNNFSGPIPSVIGLMQALAVLDLSFNQLSGPIPSILGNLTYTEKLYLQGNRLTG... | Function: Receptor kinase that may be involved in the regulation of cell proliferation and cell growth.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 107717
Sequence Length: 986
Subcellular Location: Cell... |
Q42371 | MALFRDIVLLGFLFCLSLVATVTSEEGATLLEIKKSFKDVNNVLYDWTTSPSSDYCVWRGVSCENVTFNVVALNLSDLNLDGEISPAIGDLKSLLSIDLRGNRLSGQIPDEIGDCSSLQNLDLSFNELSGDIPFSISKLKQLEQLILKNNQLIGPIPSTLSQIPNLKILDLAQNKLSGEIPRLIYWNEVLQYLGLRGNNLVGNISPDLCQLTGLWYFDVRNNSLTGSIPETIGNCTAFQVLDLSYNQLTGEIPFDIGFLQVATLSLQGNQLSGKIPSVIGLMQALAVLDLSGNLLSGSIPPILGNLTFTEKLYLHSNKLT... | Function: Receptor kinase that, together with ERL1 and ERL2, regulates aerial architecture, including inflorescence (e.g. shoot apical meristem-originating organ shape, elongation of the internode and pedicels, and adaxial-abaxial polarity), and stomatal patterning (e.g. density and clustering), probably by tuning cell... |
O14944 | MTAGRRMEMLCAGRVPALLLCLGFHLLQAVLSTTVIPSCIPGESSDNCTALVQTEDNPRVAQVSITKCSSDMNGYCLHGQCIYLVDMSQNYCRCEVGYTGVRCEHFFLTVHQPLSKEYVALTVILIILFLITVVGSTYYFCRWYRNRKSKEPKKEYERVTSGDPELPQV | Function: Ligand of the EGF receptor/EGFR and ERBB4. Stimulates EGFR and ERBB4 tyrosine phosphorylation . Contributes to inflammation, wound healing, tissue repair, and oocyte maturation by regulating angiogenesis and vascular remodeling and by stimulating cell proliferation .
Location Topology: Single-pass type I memb... |
F4JTJ2 | MMQRRSPPKHRHDGTSPLPLGMDWSPPPRKWNGRDTVWPHDPRTGWSYCVTIPSWIVLPKSRNSDPVVFYRVQVSVQSPEGITTMRGVLRRFNDFLKLLTDLKRTFPRKGFPSAPPKGLLRMKSRAVLEERRCSLEEWITKLLSDIELARSVVVASFLELEAAARSACQDVDQNASDSNNDRSSTSSSPMVHPSLSLFHAGGSTLTSDYGSDTAYETSEVGSPSVGQDDISEIGTEDLTLDEDLTLTNPIEKLVNFSMSNIDEGLSMSETILEQLEDFPKHKVRSRYVNNILGKDVYNGNASKGVFLANNGSRLLSEPEP... | Function: Acts as an effector of RABF2A and RABF2B (By similarity). Involved in vacuolar transport of storage proteins. Regulates membrane trafficking to protein storage vacuoles (PSVs) . Binds specifically to phosphatidylinositol 3-monophosphate (PtdIns3P) (By similarity).
Location Topology: Peripheral membrane protei... |
Q9SM02 | MESQLWNWILPLLISSLLISFVAFYGFFVKPKRNGLRHDRKTVSTVTSDVGSVNITGDTVADVIVVGAGVAGSALAYTLGKDKRRVHVIERDLSEPDRIVGELLQPGGYLKLLELGIEDCVEEIDAQRVYGYALFKNGKRIRLAYPLEKFHEDVSGRSFHNGRFIQRMREKAASLPNVQLEQGTVLSLLEENGTIKGVRYKNKAGEEQTAFAALTIVCDGCFSNLRRSLCNPQVEVPSCFVGLVLENCNLPYANHGHVVLADPSPILMYPISSTEVRCLVDVPGQKVPSIANGEMKNYLKTVVAPQMPHEVYDSFIAAVD... | Function: Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis. Can produce not only oxidosqualene, but also 2,3:22,23-dioxidosqualene. Main squalene epoxidase in the root. Sqe1 mutants may show defects in membrane lipid raft... |
E9R5G2 | MATTPINGHATKSPSLDAAEARRLKHNHADVVIIGAGVLGCALAVALGRQGRSVILLEASLKEPDRIVGELLQPGGVQALEKLGLRDCLEGIDSIPVKGYYVSYFNDPVPIPYPKPTPASPPPEGRCFHHGRFVMKLREAAMACPNVSVVETKATDLVTCSHTQQVLGVECTSKDNVRACYFGHLTVVADGYASKFRKQHHPHTPKVSSRFWGLELIDTKLPMPYYGHVLLSDNAPILLYQIGTHETRILVDIPENLPSASVKNGGVKSHMRNVVLPSLPESVQPAFIAALEQGQLRSMPNSFLPAATNTTPGLVILGDA... | Function: Squalene epoxidase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (Probable). Erg1 catalyzes the epoxidation of squalene into 2,3-epoxysqualene (By similarity). The third module or late pathway involves the ergosterol synthesis itself through consecut... |
Q92206 | MSSVKYDAIIIGAGVIGPTIATAFARQGRKVLIVERDWSKPDRIVGELMQPAGIKALRELGMIKAINNIRAVDCTGYYIKYYDETITIPYPLKKDACITNPVKPVPDAVDGVNDKLDSDSTLNVDDWDFDERVRGAAFHHGDFLMNLRQICRDEPNVTAVEATVTKILRDPSDPNTVIGVQTKQPSGTVDYHAKLTISCDGIYSKFRKELSPTNVPTIGSYFIGLYLKNAELPAKGKGHVLLGGHAPALIYSVSPTETRVLCVYVSSKPPSAANDAVYKYLRDNILPAIPKETVPAFKEALEERKFRIMPNQYLSAMKQG... | Function: Squalene epoxidase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway . Erg1 catalyzes the epoxidation of squalene into 2,3-epoxysqualene . The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly ... |
I1RQ76 | MASILTTTEAQTRRREQYHEADVVVVGAGVFGCTMAFALANQGRSVLLLERWLKEPDRIVGELLQPGGVASLQKLGLGHCVEGIDAKPCYGYTIFYHGEKVLVPYPGIDDEGSPTHAWGGHSTGDRSTRPSGCSFHHGRFINKLRESCIAHKNITVVETEVVKTLRGEVSDQILGVESRTMNKETGKKEQDYYFGQLTIIADGYDSKWRQEVLKTKPKVCSKFYALELIDCDLPQPGHGHVIIGNAFPILLYQIGTHETRALIDVPQGIPEASPENGGVRGYIRNFVLPALPPSIRPSAEKALEDGKIPRSMPNSWLPPT... | Function: Squalene epoxidase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (By similarity). ERG1 catalyzes the epoxidation of squalene into 2,3-epoxysqualene (By similarity). The third module or late pathway involves the ergosterol synthesis itself through cons... |
Q14534 | MWTFLGIATFTYFYKKFGDFITLANREVLLCVLVFLSLGLVLSYRCRHRNGGLLGRQQSGSQFALFSDILSGLPFIGFFWAKSPPESENKEQLEARRRRKGTNISETSLIGTAACTSTSSQNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGLGDTVEGLDAQVVNGYMIHDQESKSEVQIPYPLSENNQVQSGRAFHHGRFIMSLRKAAMAEPNAKFIEGVVLQLLEEDDVVMGVQYKDKETGDIKELHAPLTVVADGLFSKFRKSLVSNKVSVSSHFVGFLMKNAPQFKAN... | Function: Catalyzes the stereospecific oxidation of squalene to (S)-2,3-epoxysqualene, and is considered to be a rate-limiting enzyme in steroid biosynthesis.
PTM: Ubiquitinated by MARCHF6 in response to high cholesterol levels in intracellular membranes, leading to proteasomal degradation.
Location Topology: Periphera... |
A2WWV5 | MAGSGVLEVHLVDAKGLTGNDFLGEIGKIDPYVVVQYRSQERKSSVARDQGKNPSWNEVFKFQINSTAATGQHKLFLRLMDHDTFSRDDFLGEATINVTDLISLGMEHGTWEMSESKHRVVLADKTYHGEIRVSLTFTASAKAQDHAEQVGGWAHSFRQ | Cofactor: Binds 3 Ca(2+) ions per C2 domain.
Function: May play a role in plant defense signaling. Isoform 2 binds to phospholipids in a Ca(2+)-dependent manner in response to pathogen elicitors.
Sequence Mass (Da): 17736
Sequence Length: 159
Subcellular Location: Cytoplasm
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Q9C1W3 | MATQDADIIIIGAGITGCALGAALGRQGRKVLVLERDMSEPDRIVGELLQPGGIEALEKIGIADAVEGIDGQWTSGYQIFYGDSNVSVPYPSKPNGGAYQGIGFHYGRFVMNLRKALTSTPNVTVTEATVNELLRDETGEVITGVVTSSKKSESPVEYKAPLTIVCDGCFSKFRKAFIDHPIQVTDHFLGLILTNPDYIAPGRGHVILSKVAPMVLYPISSTEARILINYPGKNLPPMETLKKYVLESCVPNMPEKLRPSLKAAVYNDRLRSMPNQFLPPTVNRTKGMILVGDSNNMRHPLTGGGMTVCFHDAYLLSRFI... | Function: Squalene epoxidase; part of the third module of ergosterol biosynthesis pathway that includes by the late steps of the pathway . Erg1 catalyzes the epoxidation of squalene into 2,3-epoxysqualene . The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that main... |
P32476 | MSAVNVAPELINADNTITYDAIVIGAGVIGPCVATGLARKGKKVLIVERDWAMPDRIVGELMQPGGVRALRSLGMIQSINNIEAYPVTGYTVFFNGEQVDIPYPYKADIPKVEKLKDLVKDGNDKVLEDSTIHIKDYEDDERERGVAFVHGRFLNNLRNITAQEPNVTRVQGNCIEILKDEKNEVVGAKVDIDGRGKVEFKAHLTFICDGIFSRFRKELHPDHVPTVGSSFVGMSLFNAKNPAPMHGHVILGSDHMPILVYQISPEETRILCAYNSPKVPADIKSWMIKDVQPFIPKSLRPSFDEAVSQGKFRAMPNSYL... | Function: Squalene epoxidase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway . ERG1 catalyzes the epoxidation of squalene into 2,3-epoxysqualene . The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly ... |
B4YA15 | MADAKAQKRQKFDNVFPKLREELLAYLNQEGMPQDAVSWFQRNLDYNVPGGKLNRGISVVDSVEILKGRKLNDDEYFKAALLGWCVEFLQAFFLVSDDMMDQSVTRRGQPCWFRVEGINLIAINDSFMLEGAIYYLLKKHFRSEPYYVHLLELFHDTTFQTEIGQLIDLITAPEDHVDLSKFSLAKHQKIVIYKTAYYSFYLPVALAMYTCGVPHAPANDPYALAQSILIPLGEYFQVQDDFLDFAAPPEVLGKVGTDIVDNKCSWCVNAALARASPAQRRVLDDNYGLKDKEAEARVKALYEELGIRDEFAAYEERAYA... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Farnesyl pyrophosphate synthase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). The second module involves the formation of farnesyl diphosphate, which is also an important intermediate in t... |
O14230 | MSAVDKRAKFESALPVFVDEIVNYLKTINIPDDVTEWYKNSLFHNTLGGKYNRGLSVIDSYEILLGHPLDEAAYMKAAVLGWMVELLQSFFLIADDIMDASKTRRGQPCWYLMPGVGNIAINDAFMVESAIYFLLKKHFRQESCYVDLIELFHDVTFQTELGQQLDLLTAPEDSVDLSKFSLQKHSFIVIYKTAFYSFYLPVALAMHLAGVATPENLKCAQDILIILGKYFQVQDDYLDCYGDPTVTGKIGTDILDNKCSWIINLALAKCTPEQRVILDDNYGRKDSESEKRVKAVFEELNIRGEFENYEESEVSEIKKL... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Function: Farnesyl pyrophosphate synthase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway . Fps1 catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the r... |
Q9JLN5 | MERPSPCGSWLVGCLFTIAVFQPPVQVLGDAGKVYIAPLRDTANLPCPLFLWPNMVLSEMRWYRPGHLPRTQAVHVFRDGQDRDEDLMPEYKGRTALVRDAHKESYILQISNVRLEDRGLYQCQVWVGNSSREDNVTLQVAVLGSDPYIHVKGYDAGWIELLCQSVGWFPKPWTEWRDTTGRALLSLSEVHSLDENGLFRTAVSSRIRDNALGNVSCTIHNEALGQEKTTAMIIGAPERGSLSSPAVALSVVLPVLGLLILLGIWLICKQKKSKEKLLYEQAMEVENLLEDHAKEKGRLHKALKKLRSELKLKRAAANAG... | Function: Possible role as a cell-adhesion or receptor molecule of erythroid cells.
PTM: Glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 63512
Sequence Length: 566
Subcellular Location: Cell membrane
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P10738 | MNKNIKYSQNFLTSEKVLNQIIKQLNLKETDTVYEIGTGKGHLTTKLAKISKQVTSIELDSHLFNLSSEKLKSNTRVTLIHQDILQFQFPNKQRYKIVGNIPYHLSTQIIKKVVFESHASDIYLIVEEGFYKRTLDIHRTLGLLLHTQVSIQQLLKLPAECFHPKPRVNSVLIKLTRHTTDVPDKYWKLYTYFVSKWVNREYRQLFTKNQFHQAMKHAKVNNLSTVTYEQVLSIFNSYLLFNGRK | Function: This protein produces a dimethylation of the adenine residue at position 2085 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics.
Catalytic Activity: adenosine(2085) in 23S rRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(6)-dimethyladenosine(2085) ... |
P07287 | MSSSDEQPRPRRRNQDRQHPNQNRPVLGRTERDRNRRQFGQNFLRDRKTIARIAETAELRPDLPVLEAGPGEGLLTRELADRARQVTSYEIDPRLAKSLREKLSGHPNIEVVNADFLTAEPPPEPFAFVGAIPYGITSAIVDWCLEAPTIETATMVTQLEFARKRTGDYGRWSRLTVMTWPLFEWEFVEKVDRRLFKPVPKVDSAIMRLRRRAEPLLEGAALERYESMVELCFTGVGGNIQASLLRKYPRRRVEAALDHAGVGGGAVVAYVRPEQWLRLFERLDQKNEPRGGQPQRGRRTGGRDHGDRRTGGQDRGDRRT... | Function: This protein produces a dimethylation of the adenine residue at position 2085 in 23S rRNA, resulting in reduced affinity between ribosomes and macrolide-lincosamide-streptogramin B antibiotics.
Catalytic Activity: adenosine(2085) in 23S rRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(6)-dimethyladenosine(2085) ... |
P17261 | MVSLDDILGIVYVTSWSISMYPPIITNWRHKSASAISMDFVMLNTAGYSYLVISIFLQLYCWKMTGDESDLGRPKLTQFDFWYCLHGCLMNVVLLTQVVAGARIWRFPGKGHRKMNPWYLRILLASLAIFSLLTVQFMYSNYWYDWHNSRTLAYCNNLFLLKISMSLIKYIPQVTHNSTRKSMDCFPIQGVFLDVTGGIASLLQLIWQLSNDQGFSLDTFVTNFGKVGLSMVTLIFNFIFIMQWFVYRSRGHDLASEYPL | Function: Cystine/H(+) symporter that mediates export of cystine, the oxidized dimer of cysteine, from vacuoles/endodomes.
Catalytic Activity: H(+)(out) + L-cystine(out) = H(+)(in) + L-cystine(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30116
Sequence Length: 260
Subcellular Location: Endosom... |
P93825 | MLKTLLVQWLVFFFFFLIGSVVTAAEDDGSLSLCNCDDEDSLFSYETILNSQKVGDFLIAIAYFSIPIELVYFVSRTNVPSPYNWVVCEFIAFIVLCGMTHLLAGFTYGPHWPWVMTAVTVFKMLTGIVSFLTALSLVTLLPLLLKAKVREFMLSKKTRELDREVGIIMKQTETSLHVRMLTTKIRTSLDRHTILYTTLVELSKTLGLKNCAVWIPNEIKTEMNLTHELRPRIDDENENEHFGGYAGFSIPISESDVVRIKRSEEVNMLSPGSVLASVTSRGKSGPTVGIRVPMLRVCNFKGGTPEAIHMCYAILVCVLP... | Cofactor: Binds 1 copper ion per dimer.
Function: Ethylene receptor related to bacterial two-component regulators. Acts as a redundant negative regulator of ethylene signaling.
PTM: Autophosphorylated predominantly on Ser residues.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 72192
Sequence Length... |
P19785 | MTMTLHTKASGMALLHQIQGNELEPLNRPQLKMPMERALGEVYVDNSKPTVFNYPEGAAYEFNAAAAAAAAASAPVYGQSGIAYGPGSEAAAFSANSLGAFPQLNSVSPSPLMLLHPPPQLSPFLHPHGQQVPYYLENEPSAYAVRDTGPPAFYRSNSDNRRQNGRERLSSSNEKGNMIMESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCYEVGMMKGGIRKDRRGGRMLKHKRQRDDLEGRNEMGASGDMRAANLWPSPLVIKHTKKNSPALSLTADQMV... | Function: Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen r... |
P16058 | MLVRQSHTQISKPLGAPLRSRTTLESHVISPPKLSPQQPTTPNSNMYPEETRGGGGAAAFNYLDGGYDYTAPAQGPAPLYYSTTPQDAHGPPSDGSMQSLGSSPTGPLVFVSSSPQLSPQLSPFLHPPSHHGLPSQSYYLETSSTPLYRSSVVTNQLSASEEKLCIASDRQQSYSAAGSGVRVFEMANETRYCAVCSDFASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTMDRNRRKSCQACRLRKCYEVGMVKGGLRKDRGGRVLRKDKRYCGPAGDREKPYGDLEHRTAPPQDGGRNSSSSLNGGGGWRGPR... | Function: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues.
Sequence Mass (Da): 68084
Sequence Length: 622
Domain: Composed of three domains: a modulating N-terminal domain, a DNA-binding domain ... |
P49885 | PSGYAVREAGPPAYYRPNSDNRRQGGRERLASTSDKGSMAVESAKETRYCAVCNDYASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTIDKNRRKSCQACRLRKCY | Function: Nuclear hormone receptor. The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Ligand-dependent nuclear transactivation involves either direct homodimer binding to a palindromic estrogen r... |
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