ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q7UM99 | MAKQIVFDDDARGPLLAGVSKLARAVRSTLGPRGRNAVLDKGWGSPKVTKDGVTVAEDIELDDPFENLGAQLVKEAASKTNDVAGDGTTTATVLSEAIFREGLKMVATGADPMALSRGIQKAVDTAIAQIAKMATPINEKSKSDIKQVATIAGNNDPQIGDVLADAFTKVGKNGVITVEEGRSNETYVDVVEGMQFDRGFLSPHFVTNQDEVTVELDDCYILLFEEKISNNKKMIPLLEAISKAKKPLLIIAEDTEGEALATLVVNKMRGILSACAVKAPGYGDRRKAILGDIAALTGGKAIFKDLGIDLESVKVSDLGR... | Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Catalytic Activity: ATP ... |
Q2JA12 | MAKDLRFNVEARRLLEAGVNALADAVKVTLGPKGRNAVIEKLTGPPTITNDGVTIAREIQLRNPFANMGAQLVKEVATKTNGTAGDGTTTATVLAQALVREGLHAVDGGANPMFLKNGIEAAVAALLEEFEKYRGEVEGEADLARVATLAANNDARIGDVVAAALGRVGCDGVVTVEESPIFGLEVSFVDGIELDNGYLSPYMVTDTERMEAAYTDPYILLTNEKISQVQTLMPVLELVTRAGGQLIVFAENVEGPALGMLVANNVHGTFRSAVVRAPGFGHRRLAELNDLAVFLGGQVITADAGLSLDRVTLGQLGRCK... | Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Catalytic Activity: ATP ... |
Q7WZ32 | MAKEVVYRGSARQRMMQGIEILARAAIPTLGATGPSVMIQHRADGLPPISTRDGVTVANSIVLKDRVANLGARLLRDVAGTMSREAGDGTTTAIVLARHIAREMFKSLAVGADPIALKRGIDRAVARVSEDIGARAWRGDKESVILGVAAVATKGEPGVGRLLLEALDAVGVHGAVSIELGQRREDLLDVVDGYRWEKGYLSPYFVTDRARELAELEDVYLLMTDREVVDFIDLVPLLEAVTEAGGSLLIAADRVHEKALAGLLLNHVRGVFKAVAVTAPGFGDKRPNRLLDLAALTGGRAVLEAQGDRLDRVTLADLGR... | Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Catalytic Activity: ATP ... |
P49818 | AKDVXFGXDARAL | Function: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondria... |
Q5ZL72 | MLRLPAVLRQIRPVSRALAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKAIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARAIAKEGFEKISKGANPVEIRRGVMLAVDAITAELKKLSKPVTTPEEIAQVATISANGDQEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTAKGQKCEFQDAYVLISEKKISSVQSIVPALEIANSHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIAT... | Function: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondria... |
P10809 | MLRLPTVFRQMRPVSRVLAPHLTRAYAKDVKFGADARALMLQGVDLLADAVAVTMGPKGRTVIIEQSWGSPKVTKDGVTVAKSIDLKDKYKNIGAKLVQDVANNTNEEAGDGTTTATVLARSIAKEGFEKISKGANPVEIRRGVMLAVDAVIAELKKQSKPVTTPEEIAQVATISANGDKEIGNIISDAMKKVGRKGVITVKDGKTLNDELEIIEGMKFDRGYISPYFINTSKGQKCEFQDAYVLLSEKKISSIQSIVPALEIANAHRKPLVIIAEDVDGEALSTLVLNRLKVGLQVVAVKAPGFGDNRKNQLKDMAIAT... | Function: Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondria... |
Q5PPV4 | MWVFGYGSLIWKVDFPYVEKLVGYIMCYSRRFWQGSTDHRGVPGKPGRVVTLVEDPEGCVWGVAYRLPEGKEEEVKAYLDFREKGGYRTSTVVFYPKDPSIQPFNVLLYIGTCDNPNYLGPAPLEDIAEQILNAVGPSGRNTEYLFELANSLRNLVPEDADEHLFSLEKLVRQLSEAHRNLNHL | Function: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
Catalytic Activity: glutathione = 5-oxo-L-proline + L-cysteinylglycine
Sequence Mass (Da): 21002
Sequence Length: 184
EC: 4.3.2.7
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P39163 | MITRDFLMNADCKTAFGAIEESLLWSAEQRAASLAATLACRPDEGPVWIFGYGSLMWNPALEFTESCTGTLVGWHRAFCLRLTAGRGTAHQPGRMLALKEGGRTTGVAYRLPEETLEQELTLLWKREMITGCYLPTWCQLDLDDGRTVNAIVFIMDPRHPEYESDTRAQVIAPLIAAASGPLGTNAQYLFSLEQELIKLGMQDDGLNDLLVSVKKLLAENFPDGVLRPGFA | Function: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides.
Catalytic Activity: glutathione = 5-oxo-L-proline + L-cysteinylglycine
Sequence Mass (Da): 25512
Sequence Length: 231
EC: 4.3.2.7
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P87305 | MKTLSPEGSLWVFGYGSLIWHPPPHYDYSIPCFIKGYVRRFWMRSEDHRGTVNSPGLVLTLIPYEEWKQFSDWSFTPFDEGCWGMAFRIPAKYATQVREYLDDREVNGYTAHSVPVYAHTGDEIPVLENCLVYVGTSKSPQFQPSDDLTQMAKIISTRRGKSGDNFVYLFELAKCLRHLSPESKDIHVFELEAEVRKQMQKTR | Function: Gamma-glutamylcyclotransferase acting specifically on glutathione, but not on other gamma-glutamyl peptides. Allows utilization of gluthathione through subsequent cleavage of the Cys-Gly dipeptide by Cys-Gly metallodipeptidase dug1.
Catalytic Activity: glutathione = 5-oxo-L-proline + L-cysteinylglycine
Sequen... |
P32656 | MTNDNSGIWVLGYGSLIYKPPSHYTHRIPAIIHGFARRFWQSSTDHRGTPANPGRVATLIPYEDIIRQTAFLKNVNLYSESAPIQDPDDLVTIGVVYYIPPEHAQEVREYLNVREQNGYTLHEVEVHLETNREHEAELGEALEQLPRHNKSGKRVLLTSVYIGTIDNEAFVGPETVDETAKVIAVSHGPSGSNYEYLAKLEQALAQMPIMKERGRITDHYLTALLETVNKYR | Function: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. Allows utilization of gluthathione through subsequent cleavage of the Cys-Gly dipeptide by Cys-Gly metallodipeptidase DUG1.
Catalytic Activity: glutat... |
Q966X9 | MSHKVTKAHNGATLTVAVGELVEIQLPSNPTTGFAWYFEGGTKESPNESMFTVENKYFPPDSKLLGAGGTEHFHVTVKAAGTHAVNLTYMRPWTGPSHDSERFTVYLKAN | Function: Cysteine protease inhibitor . Inhibits cysteine protease cruzipain .
Sequence Mass (Da): 12040
Sequence Length: 110
Domain: The BC, DE and FG loops form a tripartite wedge that blocks the substrate-binding site of target cysteine proteases . The BC loop interacts with the catalytically active cysteine and his... |
P82963 | CHFKHRKQRFVDIGDSLLTLKLTHALSSSVQNFPSDAIKILNRLEELDLSNNRLRNVPDNSFHFLRSLKKVHLQDNTIEMIHRGTFQGDIHRDLTEVYFSFNSVRNVQQHTFADLIQLEQIHLDDNRIESLERRAFMNLKSLKRLNLKGNKIATIAYETFQNLPELEDLDLAYNSISSLDFNIFDQVGSLGMFHVNMSHNKLINLVVAPSVPFEQDTGLGGLQNIKVLDLSFNNITSVAKQFFRPVELSLMQLYLGHNKLLNATKDLFGNMPHLQVLDLSHNSLYELDFDTFRNTKKLQWLDTSHNRISEIPNDLFRFLG... | Function: Required for photoreceptor cell morphogenesis. Mediates homophilic cellular adhesion (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 88561
Sequence Length: 782
Subcellular Location: Cell membrane
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Q96JM3 | MEAFQELRKPSARLECDHCSFRGTDYENVQIHMGTIHPEFCDEMDAGGLGKMIFYQKSAKLFHCHKCFFTSKMYSNVYYHITSKHASPDKWNDKPKNQLNKETDPVKSPPLPEHQKIPCNSAEPKSIPALSMETQKLGSVLSPESPKPTPLTPLEPQKPGSVVSPELQTPLPSPEPSKPASVSSPEPPKSVPVCESQKLAPVPSPEPQKPAPVSPESVKATLSNPKPQKQSHFPETLGPPSASSPESPVLAASPEPWGPSPAASPESRKSARTTSPEPRKPSPSESPEPWKPFPAVSPEPRRPAPAVSPGSWKPGPPGSP... | Function: Required for proper alignment of chromosomes at metaphase and their accurate segregation during mitosis. Involved in the maintenance of spindle microtubules attachment to the kinetochore during sister chromatid biorientation. May recruit CENPE and CENPF to the kinetochore.
PTM: Phosphorylated by CDK1. Mitotic... |
Q8K327 | MEVCQELRKPALSLECGHCSFRGTDYENVQLHMGSIHPEFCDDMDAGGLGKLIFYQKSAKLFHCHKCFFTSKLYANVYYHITARHAASDKWSEQPKEQPSKDTESGKSPSPPERQNPAFDPAEARPTPALPMEAQKTSPSLCPESQASGPPVLEPQGAGPLISPEPQAPCLPAEASKAAPVPCPERVDPPCELPELEKPERGPSPESVKSALVSSKPPKHSSFADTGAAPSALSPESPVLATSPEPWGPSLSASPESRKPARTASPEPRKPSPAESPELWKPFPAIASEPRRPTPAVSPGSWKPGPPGSPRPWKSSPSAT... | Function: Required for proper alignment of chromosomes at metaphase and their accurate segregation during mitosis. Involved in the maintenance of spindle microtubules attachment to the kinetochore during sister chromatid biorientation. May recruit CENPE and CENPF to the kinetochore (By similarity).
PTM: Phosphorylated ... |
Q2QRN7 | MALLLWVFSCSLFSLWILSFMRSQATEARHGTLAVMCDERARILQDQVKVSMNHLQALAILVSTFHHSKSPSAIDQTTFARYVERTAFERPLTSGLAYAARVTHSERELFERQQAWSIRAMNFSSKRPRAEEYAPVIFAQDAYKHVVSIDMLSGAEDRGNLLRARESGKVVLTAPFQLLNKRIGVVLTYAVYKSELPLNATVHDRIQSSIGYLGGVFDIEGHVDKLLEKLAGKEPMTVNIYDTTGESMIRMYGSSNESASGMCHVSTLDFGDPLRKHEMHCRFTQGPPWPWLAVASSYGTLVISLLVGYIFHFTDKWIAK... | Function: Putative receptor kinase that may be involved in cytokinin signaling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 107228
Sequence Length: 948
Subcellular Location: Cell membrane
EC: 2.7.11.-
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P84072 | LRNVEQQCRADALVERAQELIHGQQ | Function: Inhibits cell-free translation in a rabbit reticulocyte lysate system.
Catalytic Activity: Endohydrolysis of the N-glycosidic bond at one specific adenosine on the 28S rRNA.
Sequence Mass (Da): 2905
Sequence Length: 25
EC: 3.2.2.22
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Q2INL1 | MSLAGGDRPIRVLVADDSELFRELLARVVAAEPGFEVAAVAADGDAAAAMARALRPDVVTMDLHMPDADGYSGIARIMAETPTPILVLTANPTEAAGFRALSLGALDILEKPSATADLGEYGRLIRSRLRLLAGVKVIRHLRGLRERRDAAPARAARVEVVVIGASLGGPRALAAVLRGLPPDFPAPIAVVQHIADGFTAGLAGWLAQESRLDVREARHGDPLRAGRVLIAPSGRHLVLGEGVARLSDAPPVDTFRPSVTPLFTSAARQYGRRCCGVLLTGMGRDGAEGLRVIKDAGGPTLAQDEATSAVFGMARAAVEL... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q8VL08 | MSDGFGRPPPPAPAGHPTGAAGGDPVRVMVVDDSAVIRGLLTRALEGDTEIRVVASVGDGQMAVNALQRNSLDVIVLDIEMPVMDGLTAIPKLLAVAPQVKIIMASTLTLRGADISMRCLSAGAADYIPKPTSTREIGGADAFKRELVSKVKALGAAARRAGSRTRGELRPLNPVPAAFLKREPPPVTLRPAPAVGSVGQVKPDVIAIGSSTGGPQALFEVLAHLKTGVTQPILITQHMPATFTTILAEHITRQCGMNAQEAKDGEPVVPGRCYIAPGDFHMLVTQRAGANVISLTKDPPENFCRPAVDPMMRSILRAFG... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q2L1D1 | MKKIRVICVDDSALVRGLMTEIINSHPDMEVVATAPDPLVARELIKQHNPDVLTLDVEMPRMDGLDFLEKLMRLRPMPVVMVSSLTERGGEITMRALELGAIDFVTKPRLGIRDGLLDYSELIADKIRAASRARLRGPAPVAAAALPARLRSPLNSSEKLVILGASTGGTEAIREVLLPLPPDSPAILITQHMPAGFTRSFAQRLDTLCAVTVREATHGERVLPGHVYLAPGGEQHMKLGRSGANYVIELEAGEPVNRHRPSVDVLFHSAAQAAGRNAIGVLLTGMGKDGAAGLLAMKRAGAYTLAQDEASCVVFGMPRE... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q2T8Y6 | MIRVVVVDDSMSMRTLLERIINGCDGMTCVGAAEDASAAREMIRALDPDVVTLDVEMPGMDGLEFLRRMMLLKPTPTIMVSGRTTSGSDAALRALELGAVDVIAKPLLTRPADLADYARDIAELIRGAAAARVKGGALAAASSAGRERACAHRPRGAKKAGIAATRLSRVIAIGASTGGTEALRTVLQDMSGTPPPILICQHMPEGFTASFAARLDAICGIRVKEAEQGEPLHYGCAYVAPGHSHLSLAATGRLYVCRLEASPPVNRHRPSVDVLFDSVARLAGKRALGAILTGMGKDGAAGLLRMRASGARTFAQDEPS... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q3ADA6 | MSKIRVLIVDDSALMRKYLREILEQDPEIEVIAVARNGREAVEKALELSPDVITMDINMPEMDGLTAIQYIMLHRPTPIIVISSLTQKGALTTFEALELGAVDYVAKPDGTVSLKIKEVAEEILQKVKAVAKSRGVVRLKARKERPFVQEVPKTRPVSPDTSFKKLILIGVSTGGPKALMEIIPRLPGNLDASVVIIQHMPEKFTASFAARLNNYSELYVKEAEDGESLERGKVLVARGGINLKLERKLGINVVRVRYTPLPRETIYWPSVDVAFRSALTVIEPHRIIAVLLTGMGDDGAQAMVEIKQKGGYTIAESEET... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q9AAK0 | MRVMIVDDSAVVRGMVTRWLEEAGFIIAAIAVDGGQALRKLADTSVDVCLLDIEMPVMSGLEALPKLLAAKPDLRVIMASTLTERGAEVTLRALDLGAADYIAKPSANKLGGADLYRKDLIEKVRHLGARAARPAPPQAAPRPTLAPPSSDPAGPIEAVVVASSTGGPPALRRFIAGLGADWTSPILIAQHMPPGFTRTLAQMLDPISHLTAREAQNGEPIVPGVIYVAPGDYHMTVRAAGGGGPSIHLDQGPEVNYCRPSADPLFESAARFWKGRVLGVVLTGMGRDGRDGAAVLAKVGGTIIAQDEATSVVWGMPGAV... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q8KLS5 | MKAAADRLMAARAREGRTRVLIVDDSAMVRQALALGLSTDPRLEVVGTASGAEAARAQMAALKPDVVTLDLEMPQMDGLTFLRSYMESAPVPTVVISSLTRTSGETAMRAMEAGAVDIISKPSLGAGQGLPAIMRDVCARVWAAARARLALPDGAAPAPVAPGASEDWIHALGASTGGVQALSRILPFFPAQSPGLLVVQHMPEGFTAAFARRLDALCRMRVREAADGDLVLPGLVLIAPGGLRHMEIERAGGVCRVRLVAGAPVSYSRPSVDRMFLSLAAAAGPRVSAALLTGMGRDGAAGLLAIRRAGGRTFAQDEGS... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q1LG90 | MRIGIVNDSALAVAALRRALALDTTLEIAWIAGDGEEAVRMAATQTPDLILMDLLMPVMDGVEATRRIMAESPCAIVVVTMDLGRNANQVFDAMGHGAIDAVDTPTLTDSDTKLAAGPLLRKIRNIARLLGGRGQAPHPLAAATPTPTAPRLVAIGASAGGPAALATLLGALPADFGAAVVAVQHVDEAFAQGMAEWLDAQCQLPVRLARAGEVPQAGAVVLAGTNDHLRLTSAGRLIYTPDPCDYLYRPSIDVFFESVVEHWRGEAIGVLLTGMGRDGAQGLKAMRERGFQTIAQDQATSAVYGMPKAAATLGAASEIL... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
P62637 | MISVVVVDDSAFMRKALSTMLEKDPEIRVVATARDGEEGLQVIRQHNPDVVTLDIEMPRMDGLTTLRHIMMEMPRPVLMVSSLTTEGAEATLKALELGAVDFIPKQLSKVSLDIVRIENDLREKVKEVSKRRMLRTPRPVRPAPTASAPAQTAQVASAAPATAPSRPAMPATRASRPVRDVVAIGVSTGGPPAVQKVLSQLPADFPASILIAQHMPAAFTGPFAKRLDGVCAISVKEAESGEKLKPGTAYIAPGGKHLRVEQRVSHMEVVVTTDPADALYKPSANVLMESVGQSMGRRALGVILTGMGSDGMEGMKVLKQ... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q30RX5 | MAIRVLIVDDSATARTVLKDVLSKDSEIEVIATAPDAYVARDKIVQLKPDVICLDVEMPRMDGISFLKKIMKYFPTPVLMVSSLTQDGAQVTFDALEAGAIDYVAKPHSNIYDGIDEIQKELIQKVKMVASSNLSARIEAAKAKTSTLEYKPKATYSLAQTTNKLIAIGASTGGTVALAELIARFTKDTPGVVVVQHMPSGFTNSFAQRLNSLCEVEVKEAEDGDIIGRGRVLVAPGDLHMVVRRDGGNYRVKLGTGEKISGHRPSVDVLFNSVASHVGSNAIGVLLTGMGSDGAKGMLKMKTSGASTIAQDEKSSIVWG... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q67P67 | MSDRVQRPIRVLVVDDSAFMRKVLTELLESDPLITVVGTARDGQDGLEKVLQLQPDVVTLDIEMPRLDGYGTLREIMARRPTPVVMVSSHTREGAEATIRALALGAVDFVAKPSGSISLNMHVARDELVAKVKAAAAATPRVRTAAVELAPVSPREKMQALAGLRRQTGFGDRLPRRLVLIGCSTGGPGALHQIIPRLPADLPAGVLVVQHMPPGFTRSLAQRLDELSAISVREARAGDPVRAGQVLVAPGGYHMLVDAEGRIALDQGPPVHGVRPAVDVTFESVLPVWKERLVGVILTGMGYDGAKGMAQLRKAGGWTI... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q3A5A8 | MPKKIRVLVIDDSALVRQILSKGLALDPSIEVVGTAGDPYIARDKIVKLQPDVLTLDVEMPRMDGVDFLRRLMPQYPLPVVMVSSLTQKGKQITLDSLDAGAVDFVSKPTSDIARGLKAMLSELCAKVKLASTANVSHWKAARTVVPARLKTLEKRALAESTDKVIAIGASTGGTEAIRKIIAQFPATMPGVVIVQHMPAGFTRLFAERLNQLCAMEVKEAATGDRIMPGRVLIGPGGFHMKVVRSGGFYQVRCEPGPPVKGHCPSVDVMMHSVAKHVGGNAIGVMLTGMGSDGAEGMRAMREAGARNLAQDEASCVVFG... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q5JF95 | MPLSKKIRVMVVDDSAFMRRILRDILESDPDIEVCCEARDGIEAIEKVKTEKPDVITLDIEMPRMNGLDALKFIMSKYPTPVIMVSALTQEGAEATIKALEYGAIDFIPKPSSSISINMRELRDEIIAKVKEAAKVPRRFLQLRRRRVLSEQLKKAKKVGEPARRAVAIAASTGGPQSLLKVFEKLPGELDAAILLVQHMPPGFTRSFAARLDRISKLNVKEAEDGEVVNKDWAYVAPGDYHMEVTLRNGKPTIKLYKGPKIHGVRPAADPMMKSVAEVFGRRTVGVVMTGMGRDGAEGIVAIKRKGGITIAQDKETSII... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q9WYN9 | MTDRVIRVLVVDDSAFMRMVLKDIIDSQPDMKVVGFAKDGLEAVEKAIELKPDVITMDIEMPNLNGIEALKLIMKKAPTRVIMVSSLTEEGAAITIEALRNGAVDFITKPHGSISLTFRQVAPELLEKIRQAMNVDPRTLLFKPKVSRLTITKPAVSGKIVVIGSSTGGPRSLDMIIPNLPKNFPAPIVVVQHMPPGFTKSLAMRLDSTSELTVKEAEDGEEVKPGFVYIAPGDFHLGLKAQNGKVFFFLDKSDKINNVRPAVDFTLDKAAEIYKSKTIAVILTGMGKDGTKGAFKVKFYGGTVIAEDKETCVVFGMPKS... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q3SIG0 | MKIKVLIVDDSALIRGVMREIINSQPDMEVVGVAPDPIAARELIKQTNPDVLTLDVEMPKMDGLEFLEKLMRLRPMPVVMVSSLTERGSEITMRALELGAVDFVTKPKMSIQSGMLEYTDLIADKIRIAARARIKPRTPHAQGGQSGTTLAAVRNPLTSSEKLIIIGASTGGTEAIKDFLMQLPPDSPGVLITQHMPEGFTRSFANRLDKLCKISVKEAEGGERVLPGHAYLAPGHSHLLLVRSGANYMTKLDQGPPVNRHRPSVDVLFNSAALTAGKNAVGVILTGMGKDGAAGMLEMKKAGGYNLAQDEASCVVFGMP... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
P62646 | MEDIRVLIVDDSALMRNLIGKIVDATPGLKIADKAMNGRFALQKLERVAPDVIVLDLEMPEMNGIEFLRELKKQNIKIPVVILSSIAKEGAKVTMDCLELGACDFITKPSGSESANLTTVSETLSKMLLAYGRRHQIETGTRSTDTTNSFSEPFKSTIPKPMTAAEPQKEEKPTPQREHGNIQIIAIGISTGGPNALRQVFASIDKDLPQPIVVVQHMPPGFTKEFALSLDKICPLEVKEAEDGDLIKPGRILIAPGGKHLVVEKRSLAAVAKVIDTEPQSGHKPSVDVLFGSVAKEYQNHALGIIMTGMGKDGAENITK... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
O83639 | MKNTNDIAVLIVDDSALMRKVIGKVIEGAPGLSIAGKAMNGRFALDMLERVQPDVILLDLEMPHMNGLQFLEQRKRLRIDIPVIILSSIAKEGARVTMQCLELGASDFVTKPFGSESAHLRTVSRKIVDYVTAYGRRYKLLRRTRRCLAMDTPVERPAGEEDLNCLDTQERASLPSVCARAPARDRASYTITPTEGARQTRIVPLRESGALQIIAIGVSTGGPSALRHIFAQLDADLPQPVVVVQHMPAGFTREFAYSLNQVCALEVKEAQEGDLVRRGRVLIAPGDRHLTVERRSLATVAHINSDEPENGHRPSVDVLF... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q10WZ6 | MPKFRILIVDDSVIVRRIINNILSESDWIEVVGVAPSGQIALAKIPQVNPDLIILDVEMPEIDGLETLKRIRQTYKQLPVIMFSAITQRGAIATLDALTLGANDYITKPANMGSKEKAIEYIRKQLIPKIQVFCHRKVSLTKHCLAPSMTSFQRKTSTQLLTLKLEIVAIGVSTGGPQALYQLLHKFPASFRVPIVIVQHMPPVFTTRLAERLSSQCKIPVHEAKDRDVIKSGEAWIAPGNYHIILVREGKQVRIQTIQTPPENSCRPAVDVLFRSVAKLYQGAVLGVVLTGMGQDGLHGCTSIREMGGQVLVQDQASSV... | Function: Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irrever... |
Q221I2 | MNMFASGTAALPLRASGVVVAPTVLAGGALSRVDQLKAQIRNPGEASFFYRDHHFQYDAVKVLPGEYFVSAEDLVIMTVLGSCISACIWDGRVRAGGMNHFMLPDGDSVDGFGRYGSYAMELLINELLKKGARRESMQAKVFGGAAVMAGFTTMNVGERNTKFVLDYLATERIPVVSQDVLDIHPRKVCFFPVTGKVLVKRLAHSHPETLAVEERKGNAATVAKATSGGSVDLF | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 25245
Sequence Length: 234
EC: 3.5.1.44
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Q2INJ4 | MTRTTGAAPDRAAPAAGETPGGGGRAQVYLHAGQIAVAAEPTAIVTVLGSCVAVCLHDPVARVGGMNHFLLPLHVEREQSARFGTVAVPQLVEAVVRAGARRASLVAKVFGGASVIGAFRGARNLGDENVQLALRLLDEARIPVLDRDVGGARGRKLIFHVDDGAAWVRQL | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 17754
Sequence Length: 171
EC: 3.5.1.44
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Q2STS7 | MSGLPIATNLYFDAHFHRRGVKLLPNEFYTTREDMVLVTVLGSCVAACLHDPIARIGGMNHFMLPDDGADPSAAASESMRYGAYAMEVLINELIKAGGRRERFEAKVFGGAAVLAGMTTINIGDRNADFVRRYLALERIRITAEDLQGVHPRKVAFMPHTGQAMVKKLRVQAPDVAEREAALAREAAGPRGERAARARPRVELFGTPAPKAQATPRIELFGTRATQPATRKQEA | Function: Probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis.
Catalytic Activity: H2O + L-glutaminyl-[protein] = L-glutamyl-[protein] + NH4(+)
Sequence Mass (Da): 25594
Sequence Length: 234
EC: 3.5.1.44
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P71403 | MKLLVVDDSSTMRRIIKNTLSRLGYEDVLEAEHGVEAWEKLDANADTKVLITDWNMPEMNGLDLVKKVRSDSRFKEIPIIMITTEGGKAEVITALKAGVNNYIVKPFTPQVLKEKLEVVLGTND | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Chemotactic response regulator protein that modulates the rotation direction of bacterial flagellar motors. Plays an important role in the colonization and infection of Helicobacter pylori . Upon phosphorylation by CheA, interacts with the flagellar motor protein FliM... |
A0A0H3AMJ9 | MEAILNKNMKILIVDDFSTMRRIVKNLLRDLGFNNTQEADDGLTALPMLKKGDFDFVVTDWNMPGMQGIDLLKNIRADEELKHLPVLMITAEAKREQIIEAAQAGVNGYIVKPFTAATLKEKLDKIFERL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Acts as a response regulator to control chemotaxis . Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors . Switches the flagellar rotation by binding to the flagellar motor switch protein FliM . In its active (phosphorylated... |
P24072 | MAHRILIVDDAAFMRMMIKDILVKNGFEVVAEAENGAQAVEKYKEHSPDLVTMDITMPEMDGITALKEIKQIDAQARIIMCSAMGQQSMVIDAIQAGAKDFIVKPFQADRVLEAINKTLN | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. Phosphorylated CheY interacts with the flagella switch components FliM and FliY, which causes counterclockwise rotation of the flagella, resulting in smooth swimming.
PTM:... |
P0AE68 | MADKELKFLVVDDFSTMRRIVRNLLKELGFNNVEEAEDGVDALNKLQAGGYGFVISDWNMPNMDGLELLKTIRADGAMSALPVLMVTAEAKKENIIAAAQAGASGYVVKPFTAATLEEKLNKIFEKLGM | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors. In its active (phosphorylated or acetylated) form, CheY exhibits enhanced binding to a switch component, FliM, at the flagellar motor which induces a change from countercl... |
P33665 | MHSQHRTARIALAVVLTAIPASLATAGVGYASTQASTAVKAGAGLDDPHKKEIAMELVSSAENSSLDWKAQYKYIEDIGDGRGYTGGIIGFCSGTGDMLELVQHYTDLEPGNILAKYLPALKKVNGSASHSGLGTPFTKDWATAAKDTVFQQAQNDERDRVYFDPAVSQAKADGLRALGQFAYYDAIVMHGPGNDPTSFGGIRKTAMKKARTPAQGGDETTYLNAFLDARKAAMLTEAAHDDTSRVDTEQRVFLKAGNLDLNPPLKWKTYGDPYVINS | Function: Aids in the defense against invading fungal pathogens by degrading their cell wall chitosan.
Catalytic Activity: Endohydrolysis of beta-(1->4)-linkages between D-glucosamine residues in a partly acetylated chitosan.
Sequence Mass (Da): 29835
Sequence Length: 278
Subcellular Location: Secreted
EC: 3.2.1.132
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Q13231 | MVRSVAWAGFMVLLMIPWGSAAKLVCYFTNWAQYRQGEARFLPKDLDPSLCTHLIYAFAGMTNHQLSTTEWNDETLYQEFNGLKKMNPKLKTLLAIGGWNFGTQKFTDMVATANNRQTFVNSAIRFLRKYSFDGLDLDWEYPGSQGSPAVDKERFTTLVQDLANAFQQEAQTSGKERLLLSAAVPAGQTYVDAGYEVDKIAQNLDFVNLMAYDFHGSWEKVTGHNSPLYKRQEESGAAASLNVDAAVQQWLQKGTPASKLILGMPTYGRSFTLASSSDTRVGAPATGSGTPGPFTKEGGMLAYYEVCSWKGATKQRIQDQ... | Function: Degrades chitin, chitotriose and chitobiose. May participate in the defense against nematodes and other pathogens. Isoform 3 has no enzymatic activity.
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence Mass (Da): 51681
Sequen... |
Q9D7Q1 | MVQSLAWAGVMTLLMVQWGSAAKLVCYLTNWSQYRTEAVRFFPRDVDPNLCTHVIFAFAGMDNHQLSTVEHNDELLYQELNSLKTKNPKLKTLLAVGGWTFGTQKFTDMVATASNRQTFVKSALSFLRTQGFDGLDLDWEFPGGRGSPTVDKERFTALIQDLAKAFQEEAQSSGKERLLLTAAVPSDRGLVDAGYEVDKIAQSLDFINLMAYDFHSSLEKTTGHNSPLYKRQGESGAAAEQNVDAAVTLWLQKGTPASKLILGMPTYGRSFTLASSSDNGVGAPATGPGAPGPYTKDKGVLAYYEACSWKERHRIEDQKV... | Function: Degrades chitin, chitotriose and chitobiose. May participate in the defense against nematodes and other pathogens (By similarity).
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence Mass (Da): 51112
Sequence Length: 464
Subcel... |
Q9SLP4 | MASVSPSSLLLLFFALLSPLLPLTSALVFREYIGSQFNDVKFSDVPINPDVDFHFILAFAIDYTSGSSPTPTNGNFKPFWDTNNLSPSQVAAVKRTHSNVKVSLSLGGDSVGGKNVFFSPSSVSSWVENAVSSLTRIIKQYHLDGIDIDYEHFKGDPNTFAECIGQLVTRLKKNEVVSFVSIAPFDDAQVQSHYQALWEKYGHQIDYVNFQFYAYSARTSVEQFLKYFEEQSSNYHGGKVLVSFSTDSSGGLKPDNGFFRACSILKKQGKLHGIFVWSADDSLMSNNVFRYEMQAQSMLASVNSRDRAMYWSLL | Function: Able to cleave glycolchitin.
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence Mass (Da): 35091
Sequence Length: 314
EC: 3.2.1.14
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Q7M443 | ALFREYIGAQFNDVKFSDVPINPNVDFHFILAFAIDYTSGSSPTPTNGNFNPFWDTNNLSPSQVAAIKRTYNNVKVSVSLGGNSVGGERVFFNPSSVSSWVDNAVSSLTKIIKQYHLDGIDIDYEHFKGDPNTFAECIGQLVTRLKKNGVVSFVSIAPFDDAQVQSHYQALWEKYGHQIDYVNFQFYVYSSRMSVEQFLKYFEMQRSNYPGGKVLVSFSTDNSGGLKPRNGFFDACSILKKQGKLHGIFVWSADDSLMSNDVFKYEMQAQSLLAS | Function: Able to cleave glycolchitin.
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence Mass (Da): 30863
Sequence Length: 275
EC: 3.2.1.14
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A0A1B1J8Z2 | MIIKLLVALIHYLHETMAVQSIITTPLLVILMSLRSYAFTEPSLHRQQPPSKGGVRAAYWPAWSDFSTSSIDTNYFTHIYYAFVQPAPESFNLEITESYKKWAPKYDGIHNIRPRVTTLLSIGGGGNNATLFSEMASSKQNRASFINSTIHVARKHEFNGLDLDWEWPGDEKDMSNLALLLKEWYKALVVEANTSRKSRLLLTSAVYFNSTISLIGNGPRSYPVRAIRKYLDWASPMCFDYNGAWANETGFNAALYDPNSNISTKYGIGSWIGSGVPAEKLVMGLPLYGRAWELKDPNDHGVGAKAVGPAVDTDGSMDYD... | Function: Possesses chitinase activity in vitro toward glycol chitin, carboxymethyl-chitin, colloidal chitin, and the chitin oligosaccharides (N-acetylglucosamine) (GlcNAc)6 and (GlcNAc)5 . Hydrolyzes (GlcNAc)6 into (GlcNAc)4 and (GlcNAc)2, or two (GlcNAc)3 molecules . Has the capacity to inhibit hyphal growth of the f... |
I1S2K2 | MHFNTLTCVLVGLVAHTSAVPTKREAVNSCLTQAKVPTDAQGSQSWKEDGTAYNLRLPFEPAAIAVPTTVAQVSAAVECGAKHGVAISAKSGGHSYTSLGFGGEDGHLMIELDRMYSVKLAKDGTAKIQPGARLGHVATELWNQGKRALAHGTCPGVGLGGHALHGGYGMVARKHGLTLDLMIGATVVLPTGKVVHCSKTENSDLFWGIRGAGANFGVVVELEFQTFAAPEKITYFDIGLNWDQNTAPQGLYDFQEFGKGMPAEITMQMGVSKNGYSVDGAYIGDEASLRKALQPLVQKFGGVQVTATTVDWMGLVTHFA... | Cofactor: Binds 1 FAD per subunit in a bicovalent manner.
Function: Catalyzes the selective oxidation of C1 hydroxyl moieties on chitooligosaccharides with concomitant reduction of molecular oxygen to hydrogen peroxide. This results in the formation of the corresponding lactones, which typically undergo spontaneous hyd... |
P86181 | VSSVISSSLFEKMLLHRGFYTYDAFIAAAKSFPAFATTGSTDVRKREVAAFLAQTSHETTGGWPTAPDGPYELGSTSDYFGRGPIQISYNYNYGAAGKAIGVDLLRNPDLVTSDNTVEFKTALWFWMTPQSPKPSSHDVITGRWSPSSTDKAAGRVPGYGVLTNIIDGGVECGKGQESHVADRIGYYKDNLDCYNQKPFA | Function: This protein functions as a defense against chitin-containing fungal pathogens.
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence Mass (Da): 21728
Sequence Length: 200
EC: 3.2.1.14
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P29030 | MNRTTLILFFIILSNTITVIHGYVRGCYYTNWAQYRDGEGKFLPGNIPNGLCTHILYAFAKVDELGDSKPFEWNDEDTEWSKGMYSAVTKLRETNPGLKVLLSYGGYNFGSAIFTGIAKSAQKTERFIKSAIAFLRKNNFDGFDLDWEYPVGVAEEHAKLVEAMKTAFVEEAKTSGKQRLLLTAAVSAGKGTIDGSYNVESLGKNFDLLFLMSYDLHGSWEKNVDLHGKLHPTKGEVSGIGIFNTEFAADYWASKGMPKEKIIIGIPMYAQGWTLDNPSETAIGAAASRPSSASKTNPAGGTASYWEICKYLKEGGKETV... | Function: Microfilarial chitinase, which may function to degrade chitin-containing structures in the micro-filaria or in its mosquito vector during parasite development and transmission.
PTM: O-glycosylated.
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and c... |
P85084 | GIEKIISRSMFDQMLKHRNNPACPAKGFYTYDAFLAAAKSFPSFGTTGSTDVRKRELAAFLGQTSHETTGGWPSAPDGPYAWGYCFLKERNPSSNYCAPSPRYPCAPGKSYYGRGPLQLSWNYNYGPCGEALRVNLLGNPDLVATDRVLSFKTALWFWMTPQAPKPSCHDVLTGRWQPSAADTAAGRLPGYGVLTNLLNGGLECGKGPNPQVADRLGFFRRYCGLLGVGTGNNLDCYNQRPFG | Function: Defense against chitin-containing fungal pathogens. Shows activity on chitin, tetra-N-acetylglucosamine and chitosan.
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence Mass (Da): 26541
Sequence Length: 243
Subcellular Locatio... |
P80052 | QNCQCDTTIYCCSQHGYCGNSYDYCGPGCQAGPCWDPCEGDGTLTVSDIVTQEFWDGIASQAAANCPGKSFYTRSNFLEAVSAYPGFGTKCTDEDRKREIAAYFAHVTHETGHLCYIEERDGHANNYCQESQQYPCNPNKEYFGRGPMQLSWNYNYIDAGKELHFDGLNDPDIVGRDPIISFKTSLWFWIRKGVQYVILDPNQGFGATIRIINGGQECDGHNTAQMMARVGYYQEYCAQLGVSPGNNLPC | Function: Defense against chitin-containing fungal pathogens.
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence Mass (Da): 27908
Sequence Length: 250
EC: 3.2.1.14
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P36362 | MRATLATLAVLALATAVQSDSRARIVCYFSNWAVYRPGVGRYGIEDIPVEKCTHIIYSFIGVTEGNSEVLIIDPELDVDKNGFRNFTSLRSSHPSVKFMVAVGGWAEGSSKYSHMVAQKSTRMSFIRSVVSFLKKYDFDGLDLDWEYPGAADRGGSFSDKDKFLYLVQELRRAFIRVGKGWELTAAVPLANFRLMEGYHVPELCQELDAIHVMSYDLRGNWAGFADVHSPLYKRPHDQWAYEKLNVNDGLHLWEEKGCPSNKLVVGIPFYGRSFTLSAGNNNYGLGTFINKEAGGGDPAPYTNATGFWAYYEICTEVDKD... | Function: Digests chitin in the exoskeleton during the molting process.
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence Mass (Da): 62204
Sequence Length: 554
Subcellular Location: Secreted
EC: 3.2.1.14
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P41684 | MLYKLLNVLWLVAVSNAIPGTPVIDWADRNYALVEINYEATAYENLIKPKEQVDVQVSWNVWNGDIGDIAYVLFDEQQVWKGDAESKRATIKVLVSGQFNMRVKLCNEDGCSVSDPVLVKVADTDGGHLAPLEYTWLENNKPGRREDKIVAAYFVEWGVYGRNFPVDKVPLPNLSHLLYGFIPICGGDGINDALKTIPGSFESLQRSCKGREDFKVAIHDPWAAVQKPQKGVSAWNEPYKGNFGQLMAAKLANPHLKILPSIGGWTLSDPFYFMHDVEKRNVFVDSVKEFLQVWKFFDGVDIDWEFPGGKGANPSLGDAD... | Function: Plays a role in host liquefaction to facilitate horizontal transmission of the virus by hydrolyzing beta-chitin and by regulating the cysteine protease VCATH. Localized in the host reticulum endoplasmic via its KDEL motif, interacts with and thus prevents VCATH secretion before host cell lysis occurs.
Catalyt... |
P9WJX7 | MTAPTGTSATTTRPWTPRIATQLSVLACAAFIYVTAEILPVGALSAIARNLRVSVVLVGTLLSWYALVAAVTTVPLVRWTAHWPRRRALVVSLVCLTVSQLVSALAPNFAVLAAGRVLCAVTHGLLWAVIAPIATRLVPPSHAGRATTSIYIGTSLALVVGSPLTAAMSLMWGWRLAAVCVTGAAAAVALAARLALPEMVLRADQLEHVGRRARHHRNPRLVKVSVLTMIAVTGHFVSYTYIVVIIRDVVGVRGPNLAWLLAAYGVAGLVSVPLVARPLDRWPKGAVIVGMTGLTAAFTLLTALAFGERHTAATALLGTG... | Function: Active efflux pump that plays an important role in chloramphenicol resistance . Overexpression causes pyrazinamide resistance .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42911
Sequence Length: 413
Subcellular Location: Cell membrane
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A7YN26 | MLLRLCIIATLLVSHCVAVSTSPATRDTNGEGLLVQTSSGPIQGFFNQTAPDVRQWLGVPFAEPPVGDLRFSSPVKKQPNGTVNAFALPSSCIQQTSNSSTIYTTYETGFLISGGDSEDCLYLSIWAPRIENIQSQQRPLPVLLYIPGGGFTSGGEASLYKIPDKWVQRTQSHIVVIMNYRVNVFGFPNAEGLSEPNVGLLDQRMAVEWVAANIANFGGDPARIALWGQSAGAASVTAYSYGYPEDPIVAALIADSGAPNIVDNEDYAHTNFTFLASLVGCDGLSSTEELSCMRNVSARKLQTALSTYSGSPSISFTPAV... | Function: Extracellular chlorogenic acid esterase that releases caffeic acid from chlorogenic acid (CGA) contained in natural substrates such as apple marc and coffee pulp . Shows no activity towards 5-O-p-coumaroyl quinic acid, another quinic ester derivative, and rosmarinic acid, another caffeic ester derivative .
Ca... |
P32750 | NTDQSFPGFPGSEMWNPNTDLSEDCLYLNVWIPTPKPKNATVMIWIYGGGFQTGTSSLPVYDGKFLARVERVIVVSVNYRVGALGFLALPGNPEAPGNLGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAGSVGLHL | Function: Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters (By similarity).
Catalytic Activity: an acylcholine + H2O = a carboxylate + choline + H(+)
Sequence Mass (Da): 15086
Sequence Length: 141
Subcellular ... |
P06276 | MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIPYAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDCLYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALGFLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPGSHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEILLNEAFVVPYGTPLSVNFGP... | Function: Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters.
PTM: N-glycosylated. No other PTM detected . The major N-glycan structures are of the complex diantennary type with 1 and 2 N-acetylneuraminic acid m... |
Q5UR02 | MTDHKIIMLLLLGIYCIQATQFTQVNIDNGPIKGTLQYVEGRAIRVFKGIPFAEPPVNNLRWKAPVPYTKKWHNPLNTTEYKPKCPQYVAPGTVPEPRGISEDCLYTNVWAPVPEYHGETFPVMVWIHGGAFISGSPEDFGVGNFSILAVTKRIIIVAASYRVNAFGFFSSELLGKSQLEARGVYGLLDQRLGLKWVKNNIAAFGGKSKDITIYGQSAGGISVCLQAVTPLNDLPGEKLFTRVIGSSGYCDILPMTNNSADAGLVQKLNCTTKECLYALPWQNITNAVGPGFLSFQPTVGINKFLPDQPISLLADRTNPR... | Function: May be involved in the disruption of the host membrane.
Catalytic Activity: an acylcholine + H2O = a carboxylate + choline + H(+)
Sequence Mass (Da): 64868
Sequence Length: 579
EC: 3.1.1.8
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P23472 | MAKRTQAILLLLLAISLIMSSSHVDGGGIAIYWGQNGNEGTLTQTCSTRKYSYVNIAFLNKFGNGQTPQINLAGHCNPAAGGCTIVSNGIRSCQIQGIKVMLSLGGGIGSYTLASQADAKNVADYLWNNFLGGKSSSRPLGDAVLDGIDFDIEHGSTLYWDDLARYLSAYSKQGKKVYLTAAPQCPFPDRYLGTALNTGLFDYVWVQFYNNPPCQYSSGNINNIINSWNRWTTSINAGKIFLGLPAAPEAAGSGYVPPDVLISRILPEIKKSPKYGGVMLWSKFYDDKNGYSSSILDSVLFLHSEECMTVL | Function: Bifunctional enzyme with lysozyme / chitinase activity. May have a role in plugging the latex vessel and cessation of latex flow.
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence Mass (Da): 33718
Sequence Length: 311
Subcell... |
P23473 | GGIAIYWGQNGNEGTLTQTCNTGKYSYVNIAFLNKFGNGQTPEINLA | Function: Bifunctional enzyme with lysozyme/chitinase activity.
Catalytic Activity: Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
Sequence Mass (Da): 5040
Sequence Length: 47
Subcellular Location: Secreted
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Q8LE58 | MGNTDKLMNQIFELKFTSKSLQRQARKCEKEERSEKLKVKKAIEKGNMDGARIYAENAIRKRSEQMNYLRLSSRLDAVVARLDTQAKMATITKSMTNIVKSLESSLTTGNLQKMSETMDSFEKQFVNMEVQAEFMDNAMAGSTSLSTPEGEVNSLMQQVADDYGLEVSVGLPQPAGHAIPTKTEEKVEEDDLTRRLAELKARG | Function: Involved in ESCRT-dependent multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. Mediates the MVB sorting of the auxin carriers PIN1, PIN2 and AUX1. Required for embryonic axis establishment and seedling growth . Required for autophagic degradation of plastid proteins. Promot... |
Q6PHF0 | MDDTLFQLKFTSKQLERLAKKAEKDSKSEQAKVKKALQQKNVECARVYAENAIRKKNEGLNWLRMASRVDAVASKVQTALTMKGVAKNMTQVTKALDKALSSMDLQKVSAVMDKFETQVQNLDVHTSVMEDSMSSATTLSTPQQQVDDLILQIAEESGLEVEDQLSQLPAGASALGETSARAQEKEDQLSRRLAALRN | Function: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and sci... |
Q9HD42 | MDDTLFQLKFTAKQLEKLAKKAEKDSKAEQAKVKKALLQKNVECARVYAENAIRKKNEGVNWLRMASRVDAVASKVQTAVTMKGVTKNMAQVTKALDKALSTMDLQKVSSVMDRFEQQVQNLDVHTSVMEDSMSSATTLTTPQEQVDSLIMQIAEENGLEVLDQLSQLPEGASAVGESSVRSQEDQLSRRLAALRN | Function: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and sci... |
Q921W0 | MDDTLFQLKFTAKQLEKLAKKAEKDSKAEQAKVKKALQQKNVECARVYAENAIRKKNEGVNWLRMASRVDAVASKVQTAVTMKGVTKNMAQVTKALDKALSAMDLQKVSAVMDRFEQQVQNLDVHTSVMEDSVSSATTLTTPQEQVDSLIVQIAEENGLEVLDQLSQLPEGASAVGESSVRSQEDQLSRRLAALRN | Function: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and sci... |
Q6NUD8 | MDDTLFQLKFTAKQLEKLAKKAEKDSNTEQAKVKKALQQKNVEVARVYAENAIRKKNEGLNWLRMASRVDAVASKVQTAVTMKGVTKNMAQVTKALDKALSSMDLQKVSAVMDKFDQQVQNLDVHTSVMEDSMSSAMTLTTPQEQVDNLIVQIAEENGLEVMDQLNQLPQGASSVGESSTRTQEDQLSRRLASLRN | Function: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and sci... |
Q9SSM4 | MGNTDKLMNQIFDLKFTSKSLQRQSRKCEKEEKAEKLKVKKAIEKGNMDGARIYAENAIRKRSEQMNYLRLASRLDAVVARLDTQAKMTTITKSMTNIVKSLESSLATGNLQKMSETMDSFEKQFVNMEVQAEFMENAMAGSTSLSTPEGEVNSLMQQVADDYGLEVSVGLPQPAGHAIPTKTEEKVDEDDLSRRLAELKARG | Function: Involved in ESCRT-dependent multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs. Mediates the MVB sorting of the auxin carriers PIN1, PIN2 and AUX1. Required for embryonic axis establishment and seedling growth . Required for autophagic degradation of plastid proteins. Promot... |
Q7ZVB1 | MSSMEKHLFNLKFAAKELQRNSKKCDKEEKAEKVKVKKAIQKGNMEVARIHAENAIRQKNQSVNFLRMSARVDAVAARVQTAVTMNQVTKSMAGVVKGMDATLKSMNLEKISGLMEKFERQFETLDVQTAQMEDSMSSTTTLTTPQGQVDTLMMEMADEAGLDLNMELPQGQTGSVGTSVASAEQDELSQRLAKLRDQV | Function: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and sci... |
Q7LBR1 | MSNMEKHLFNLKFAAKELSRSAKKCDKEEKAEKAKIKKAIQKGNMEVARIHAENAIRQKNQAVNFLRMSARVDAVAARVQTAVTMGKVTKSMAGVVKSMDATLKTMNLEKISALMDKFEHQFETLDVQTQQMEDTMSSTTTLTTPQNQVDMLLQEMADEAGLDLNMELPQGQTGSVGTSVASAEQDELSQRLARLRDQV | Function: Probable peripherally associated component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and sci... |
Q5ZHN1 | MDLLFGRRKTPEELLRQNQRALTRAMRELDRERQKLEAQEKKIIIDIKKMAKQGQMDAVKIMAKDLVRTRRYVKKFITMRANVQAVSLKIQTLKSNNSMALAMKGVTKAMATMNRQLKLPQIQKIMMEFEKQAGIMDMKEELMNDAIDDAMGDEDDEEESDAVVSQVLDELGLNLTDELATLPPPGGSLAAGEGRAAEAAAALADADADLEERLKNLRRD | Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limi... |
Q7ZW25 | MESLFGRRKTPEEMLRQNQRALNRAMRDLDRERQRLEQQEKKIIADIKKMAKQGQMDAVKIMAKDLVRTRRYVKKFIMMRANIQAVSLKIQTLKSNNSMAQAMKGVTKAMATMNRQLKLPQIQKIMMEFERQSEIMDMKEEMMNDAIDDAMGDEDDEEESDAVVSQVLDELGLTLSDELSNLPATGGSLSVAAGKKAEPQPTLADADADLEERLNNLRRD | Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limi... |
O43633 | MDLLFGRRKTPEELLRQNQRALNRAMRELDRERQKLETQEKKIIADIKKMAKQGQMDAVRIMAKDLVRTRRYVRKFVLMRANIQAVSLKIQTLKSNNSMAQAMKGVTKAMGTMNRQLKLPQIQKIMMEFERQAEIMDMKEEMMNDAIDDAMGDEEDEEESDAVVSQVLDELGLSLTDELSNLPSTGGSLSVAAGGKKAEAAASALADADADLEERLKNLRRD | Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limi... |
Q9DB34 | MDLLFGRRKTPEELLRQNQRALNRAMRELDRERQKLETQEKKIIADIKKMAKQGQMDAVRIMAKDLVRTRRYVRKFVLMRANIQAVSLKIQTLKSNNSMAQAMKGVTKAMGTMNRQLKLPQIQKIMMEFERQAEIMDMKEEMMNDAIDDAMGDEEDEEESDAVVSQVLDELGLSLTDELSNLPSTGGSLSVAAGGKKAEATASALADADADLEERLKNLRRD | Function: Probable core component of the endosomal sorting required for transport complex III (ESCRT-III) which is involved in multivesicular bodies (MVBs) formation and sorting of endosomal cargo proteins into MVBs. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limi... |
Q5ZHQ5 | MAAPWVLPAPLSPAQLKRLEQHRYSSAGRSLLEPWLQPYWGWLVERLPPWLAPNAITLGGLLLNCLTALPLIASCPTATEQAPFWAYILGALGLFIYQSLDAIDGKQARRTNSSSPLGELFDHGCDSISTVFVVLGSCIAIRLGTNPDWLFFCCFVGLFMFYSAHWQTYVSGILRFGKVDVTEVQIAITMLLLVSAFCGTAVWDYKVHLVGLELKFFAVVGILCGTAVSCFNYFRIIFGGGVGKNGSTIAVAHMTKSEISLQDTAFIGPGLLFLDQYFNSFIDEYVVLWIALFISLFDMLRYATGVCLQIAAHLHIHVFR... | Function: Catalyzes the final step of de novo phosphatidylcholine (PC) synthesis, i.e. the transfer of choline phosphate from CDP-choline to the free hydroxyl of a diacylglycerol (DAG), producing a PC. It thereby plays a central role in the formation and maintenance of vesicular membranes.
Catalytic Activity: a 1,2-dia... |
Q8WUD6 | MAAGAGAGSAPRWLRALSEPLSAAQLRRLEEHRYSAAGVSLLEPPLQLYWTWLLQWIPLWMAPNSITLLGLAVNVVTTLVLISYCPTATEEAPYWTYLLCALGLFIYQSLDAIDGKQARRTNSCSPLGELFDHGCDSLSTVFMAVGASIAARLGTYPDWFFFCSFIGMFVFYCAHWQTYVSGMLRFGKVDVTEIQIALVIVFVLSAFGGATMWDYTIPILEIKLKILPVLGFLGGVIFSCSNYFHVILHGGVGKNGSTIAGTSVLSPGLHIGLIIILAIMIYKKSATDVFEKHPCLYILMFGCVFAKVSQKLVVAHMTKS... | Function: Catalyzes the final step of de novo phosphatidylcholine (PC) synthesis, i.e. the transfer of choline phosphate from CDP-choline to the free hydroxyl of a diacylglycerol (DAG), producing a PC. It thereby plays a central role in the formation and maintenance of vesicular membranes.
Catalytic Activity: a 1,2-dia... |
Q4KLV1 | MGLAEGLAARMAPHLYIQEPLSAQQLKKLEEHKYSASGRSLVEPPMQVYWNWLVEKVPLWLAPNTITMVGLLLNVLSTLILVCYCPTATEGAPFWTYLLCAIGLFVYQSLDAIDGKQARRTNSSSPLGEMFDHGCDSISIVFVNLGTIAAVRLGTLPGWMFYCCFVGMFMFYCAQWQTYVCGTLKFGIIDVTELQISVTVMFLMTAVCGPELWDYEIPFTGLPMKTIPLLGIIGGTVYSCSNYFRVILSGGVGKNGSTVAGTSVLSPGLHIGLVLLLALMIYKKSTTNLFLQNPCLYTLAFGFVSAKITIKLVIAHMTKS... | Cofactor: Is active in the presence of either Mg(2+) or Mn(2+), but not in Ca(2+) or Zn(2+). Binds 2 Mg(2+) ions per subunit.
Function: Catalyzes the final step of de novo phosphatidylcholine (PC) synthesis, i.e. the transfer of choline phosphate from CDP-choline to the free hydroxyl of a diacylglycerol (DAG), producin... |
Q2YQA5 | MSLPVTLSALDLGALLCSRICHDIISPVGAINNGLELLEEGGADEDAMALIKSSARNASARLQFARIAFGAAGSAGVQIDTGDAQNVATEYFRNEKPEFTWEGARVLLPKNKVKLLLNMLLIGNGAIPRGGSLAVRLEGSDTDPRFVITVKGRMLRVPPKFLELHSGAAPEEPIDAHSVQPYYTLLLAEEAGMKISIHATAEDIVFSAE | Function: Component of a regulatory phosphorelay system that controls B.abortus cell growth, division, and intracellular survival inside mammalian host cells. This signaling pathway is composed of CckA, ChpT, CtrA and CpdR. ChpT efficiently and specifically shuttles phosphoryl groups from the CckA kinase to the receive... |
Q5PXQ6 | MSTPVSAEQQAREQDLVERVLRSFDATADPRLKQVMQALTRHLHAFLREVRLTEAEWETGIGFLTDAGHVTNERRQEFILLSDVLGASMQTIAMNNEAHGDATEATVFGPFFVEGSPRIESGGDIAGGAAGEPCWVEGTVTDTDGNPVPDARIEVWEADDDGFYDVQYDDDRTAARAHLLSGPDGGYAFWAITPTPYPIPHDGPVGRMLAATGRSPMRASHLHFMVTAPGRRTLVTHIFVEGDELLDRDSVFGVKDSLVKSFERQPAGAPTPGGREIDGPWSRVRFDIVLAPA | Cofactor: Binds 1 Fe(3+) ion per subunit.
Function: Catalyzes the ortho-cleavage of the aromatic ring of hydroxyquinol.
Catalytic Activity: benzene-1,2,4-triol + O2 = 2 H(+) + maleylacetate
Sequence Mass (Da): 31967
Sequence Length: 293
Pathway: Aromatic compound metabolism; beta-ketoadipate pathway; 3-oxoadipate from ... |
F4IV45 | MSKESSPPKVPSTTMEYERRLEAAAEIILEKEAKFSNTPPDCSEFGVTATLKPHQVEGVSWLIQKYLLGVNVVLELDQMGLGKTLQAISFLSYLKFRQGLPGPFLVLCPLSVTDGWVSEINRFTPNLEVLRYVGDKYCRLDMRKSMYDHVKKSSKGHFLPFDVLLTTYDIALVDQDFLSQIPWQYAIIDEAQRLKNPNSVLYNVLLEQFLIPRRLLITGTPIQNNLTELWALMHFCMPLVFGTLDQFLSAFKETGDGLSGLDVSNDKETYKSLKFILGAFMLRRTKSLLIESGNLVLPPLTELTVMVPLVSLQKKIYTSI... | Function: Probable helicase-like transcription factor.
Sequence Mass (Da): 98867
Sequence Length: 877
Subcellular Location: Nucleus
EC: 3.6.4.-
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Q9ZUL5 | MKRDFDEISEEEWSQHSFNASRVLKRPRTPKKTRAATNPTPSIESFAFRRPSTAMTIESNSSDGDCVEIEDLGDSDSDVKIVNGEDLLLEDEEEVEETKVVMRAARVGRRFVIEDEEASDDDDDEAESSASEDEFGGGGGGSGGRRGEDEDVVGKALQKCAKISADLRKELYGTSSGVTDRYSEVETSTVRIVTQNDIDDACKAEDSDFQPILKPYQLVGVNFLLLLYKKGIEGAILADEMGLGKTIQAITYLTLLSRLNNDPGPHLVVCPASVLENWERELRKWCPSFTVLQYHGAARAAYSRELNSLSKAGKPPPFNV... | Function: DNA helicase that possesses intrinsic ATP-dependent nucleosome-remodeling activity and is both required for DNA repair and heterochromatin organization. Promotes DNA end resection of double-strand breaks (DSBs) following DNA damage: probably acts by weakening histone DNA interactions in nucleosomes flanking D... |
Q5AA40 | MSFGSFDHICNKTALPLCSVVGAVNQSAFFQRGIVPDCYARSVELANTMIFQIGNAFVHFGGLIILLIIIFNVRAKYTAIGRKEMLFFLYLAIGLIVSSLIVDCGVSPPSSTSYAYFVAVQIGLSSALCICLLYNGFLCFQFWEDGTSRSMWILRVGCFAWFAVNFIVCIITFKHWDTALDYRKTTTLFIFAYVLNAVILAVYVVSQIILVVFALESYWSLGAILLGVFFFVAGQVLTYVFSDKICRGASHYVDGLFFGSACNVFTFMMIYKFWDMITSDDLEFSVANVEQPINEFGVGADDEKRSSMFF | Function: Chaperone required for the export of the chitin synthase CHS3 from the endoplasmic reticulum.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34709
Sequence Length: 310
Subcellular Location: Endoplasmic reticulum membrane
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J9VMX7 | MVRHDPFTNSVSEDSSFTPSVNPSTPYPQSGHYRPYYPPQLTYCQGQQGYQYDHTGDVGYGGRSRRHGSWASVNNEDNEELTPLTTGPASSSTFLTTDPYLSGGPDLPLSSSSASISSAGADFLRRQTVPRRGATIKKIKLTNGNFIADYPVPGPVSSSVEAKWLNDKTSNEFWHMRYTAATCDPDDFTPENGWKLKTTSYNRETELLVAITSYNEDKILYARTLHNVMLNIRDICNTKASKFWRRSAEEGRPGWQKIVVALVADGLDPMDKQVLDVLQTIGVFQDGILKKEVDGKKTAAHIFEYTTQLSIDATPQLVQP... | Function: Polymerizes chitin, a structural polymer of the cell wall and septum, by transferring the sugar moiety of UDP-GlcNAc to the non-reducing end of the growing chitin polymer.
Catalytic Activity: [(1->4)-N-acetyl-beta-D-glucosaminyl](n) + UDP-N-acetyl-alpha-D-glucosamine = [(1->4)-N-acetyl-beta-D-glucosaminyl](n+... |
P0CM72 | MSDNAAFKFGSFDYICEHAALVVCPMLGDQQGMAPTCYSRNVQLGSQIIFQPATCILHIAALVMATIMLLHVRSKYTAVGRKEIVLFFYMYIWVELFAIFLDSAIIPTANKVYPWFAAIYAGSVGALYWCLLLNGFVGFQFHEDGTPMSLWFLRISSLVVGAVCFGIPVATFKGTSSSMSPTNTVGLFITYLVFPCVCVLIYFISQMLLVVRTLDDRWVIGDLLFMAGFYIAGVLLLVTFSVTICDAVKHYVDGVFFSTLAFLFAVMMVYKYWDSITKEDLEFSVGSKQAVWDVKDPLLATGMEYYEDDAQSAYRGAGGS... | Function: Chaperone required for the export of the chitin synthase CHS3 from the endoplasmic reticulum.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39829
Sequence Length: 361
Subcellular Location: Endoplasmic reticulum membrane
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Q5YCW8 | MSGFGDFTSICETAPLPLCASVGPTLQATGRTGIEPECYARNIELANTIIFEGAASVMHIVALIMTVIMILHVRSKFTAVGRKEILSFFYLYMLLTAMSLIIDAGVAPPGSDPYPYFVSVQNGLSSAVITCLLINGFVGFQLYEDGTPLSVWMMRISSLAAFAISFLVSLATFKSWAGLGPTNTVGLFVVLYLLNAVQLFVYVAMQILLVTRTLQDRWPLGDIAFGIFFFVAGQVLLYAFSSKICIAISHYLDGLFLATVCNLLGVMMVYKYWDSITKEDLEFSVGTRMNNWEVKELLPEEDRRATVFSEDPYAQSSSYD... | Function: Chaperone required for the export of the chitin synthase chs3 from the endoplasmic reticulum.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36844
Sequence Length: 334
Subcellular Location: Endoplasmic reticulum membrane
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P51080 | ITHLIVCTTSVDMPGADYQLTKLLGLRPYVKRYMMYQQGCFAGGTVLRLAKDLAENNKGARVLVVCSEVTAVTFRGPSDTHLDSLVGQALFGDGAAALIVGSDPVPEIEKPIFEMVWTAQTIAPDSEGAIDGHLREAGLTFHLLKDVPGIVSKNINKALVEAFEPLGISDYNSIFWIAHPGGPAILDQVEQKLALKPEKMKATREVLSEYGNMSSACVLFILDEMRKKSAQDGLKTTGEGLEWGVLFGFGPGLTIETVVLRSVTI | Function: The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin.
Catalytic Activity: 4-coumaroyl-CoA + 2 H(+) + 3 malonyl-CoA = 2',4,4',6'-tetrahydroxychalcone + 3 CO2 + 4 CoA
Sequen... |
Q7SB92 | MGKFGDFSSICRMAPIPLCASVGPITSIATGVGIEPDCYARNIEVANTIIFQGAASVMHIVALVMTVVMLLHVRGKFTAVGRKEITTFFYLYMILTFLSLCIDAGVIPPHSGSYPYFVAVQAGLASALVTCLVINGFVGFQLYEDGTPLSLWMLRLCSFVAFVISFLVGLATFKSWAGLGPTNTVGIFVVLYFLNALQLLLYVVMQIILVTRTLQDRWPLGDIAFGLFFFIAGQVILYAFSSPICEGISHYLDGLFFATTCNLLAVMMVYKYWDSITKEDLEFSVGTRMNNWEVKELLPQGPEEDRRATVYADPIYEGHY... | Function: Chaperone required for the export of the chitin synthase chs-3 from the endoplasmic reticulum.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39306
Sequence Length: 358
Subcellular Location: Endoplasmic reticulum membrane
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Q96UG7 | MPITKYKAAAVTSEPGWFDLEAGVVKTIDFINEAGQAECKLVAFPEVWIPGYPYWMWKVTYLQSLPMLKKYRENSLTVDSEEMRRIRRAARDNQIYVSLGFSEIDHATLYLAQVLIGPDGSVVNHRRKIKPTHVEKLVYGDGPGDTFMSVSETDIGRVGQLNCWENMNPFLKALNVSCGEQVHIAAWPVYPGRERQVAPDPATNYADPASDLVTPEYAIETGAWTLAPFQRLSVEGLKKNTPEGVEPETDPSVYNGHARIYRPDGSLVVKPDKDFDGLLFVDIDLNETHLTKVLADFAGHYMRPDLIRLLVDTRRKELIT... | Function: Catalyzes the hydration of cyanide to formamide. Degradation of cyanide may be important for plant pathogenic fungi in infection of cyanogenic plants. Also able to transform metal cyanides.
Catalytic Activity: formamide = H2O + hydrogen cyanide
Sequence Mass (Da): 40793
Sequence Length: 363
EC: 4.2.1.66
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P32964 | MPINKYKAAVVTSEPVWENLEGGVVKTIEFINEAGKAGCKLIAFPEVWIPGYPYWMWKVNYLQSLPMLKAYRENSIAMDSSEMRRIRAAARDNQIYVSIGVSEIDHATLYLTQVLISPLGDVINHRRKIKPTHVEKLVYGDGSGDSFEPVTQTEIGRLGQLNCWENMNPFLKSLAVARGEQIHVAAWPVYPDLSKQVHPDPATNYADPASDLVTPAYAIETGTWVLAPFQRISVEGLKRHTPPGVEPETDATPYNGHARIFRPDGSLYAKPAVDFDGLMYVDIDLNESHLTKALADFAGHYMRPDLIRLLVDTRRKELVT... | Function: Catalyzes the hydration of cyanide to formamide. Degradation of cyanide may be important for plant pathogenic fungi in infection of cyanogenic plants.
Catalytic Activity: formamide = H2O + hydrogen cyanide
Sequence Mass (Da): 40899
Sequence Length: 368
EC: 4.2.1.66
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E3RV84 | MPLTKYKAAAVTSEPCWFDLTAGVQKTIDFINEAGAAGCKLVAFPEVWIPGYPYWMWKVNYQQSLPLLKKYRENSLPIDSEEFRKIRRAARDNQIHVSLGFSEIDHATCYLTQTLIDPTGEVINHRRKIKPTHVEKLVYGDGAGDTFKSVTQTELGRLGQLNCWENMNPFLKALNVSEGEQIHIAAWPVYPGKETLNYPDPATNVAEPASDLVTPAYAIETGTWTLAPFQRLSKEGLKINTPEGIEPETDPSTYNGHARIYRPDGSLYAKPDKDFDGLMFVDIDLNECQLTKALADFSGHYMRPDLIRLLVDTRRKELVT... | Function: Catalyzes the hydration of cyanide to formamide. Degradation of cyanide may be important for plant pathogenic fungi in infection of cyanogenic plants (By similarity) . Can also transform some nitriles like 2-cyanopyridine and fumaronitrile .
Catalytic Activity: formamide = H2O + hydrogen cyanide
Sequence Mass... |
Q9LI74 | MFVRIGFVVAASIAAVTVKRLNVKPSKPSKPSDNGEGGDKEQSVDPDYNLNDKNLQEEEEEEEEEVKLINSVINQTRGSFSDYLDDDILPEFEDLLSGEIEYPLPDDDNNLEKAEKERKYEVEMAYNDGELERLKQLVKELEEREVKLEGELLEYYGLKEQESDIVELQRQLKIKTVEIDMLNITINSLQAERKKLQEELSQNGIVRKELEVARNKIKELQRQIQLDANQTKGQLLLLKQHVSSLQMKEEEAMNKDTEVERKLKAVQDLEVQVMELKRKNRELQHEKRELSIKLDSAEARIATLSNMTESDKVAKVREEV... | Function: Required for the positioning and movement of chloroplasts. Interacts with profilin and actin independent of its polymerization status. Regulates chloroplast localization by anchoring chloroplasts to the plasma membrane and forming a bridge to the actin cytoskeleton.
Location Topology: Peripheral membrane prot... |
Q9GYF0 | MRTSQAIFILIFLDSVRNQSPQVIPAKWDVVYEKETGHNMSLTVFRFQVKEQYSVARIIMSCNESTEHNPLLAVFREKLAILSLQVPLIVDNYEYSQVARTLCPFTEYKEGEAFTVEVTSSRPVHYNFRAELVQNFYLYNNSQRLVTASASEPVYLRYDIPGDVDSVAVHLDSNSTICMTVSVQKIGCPVFDLPDNVNSMGLHQTMTTSATIPVEKSRMSSFYVVFVVNTNDDLCSEILSIKPNKPTKFPLRMKSFNVTIESSMKIFDYTIPIVFWACILLLVTIVVFVYHYFDGIWERRFVSRAYTHLEDNAQEQRIRD... | Function: Cholesterol-binding protein which is involved in dietary cholesterol uptake from the environment . Does not play a role in double-stranded RNA transport in contrast to other SID1 family members .
Catalytic Activity: cholesterol(in) = cholesterol(out)
Location Topology: Multi-pass membrane protein
Sequence Mas... |
Q5T280 | MAERGRKRPCGPGEHGQRIEWRKWKQQKKEEKKKWKDLKLMKKLERQRAQEEQAKRLEEEEAAAEKEDRGRPYTLSVALPGSILDNAQSPELRTYLAGQIARACAIFCVDEIVVFDEEGQDAKTVEGEFTGVGKKGQACVQLARILQYLECPQYLRKAFFPKHQDLQFAGLLNPLDSPHHMRQDEESEFREGIVVDRPTRPGHGSFVNCGMKKEVKIDKNLEPGLRVTVRLNQQQHPDCKTYHGKVVSSQDPRTKAGLYWGYTVRLASCLSAVFAEAPFQDGYDLTIGTSERGSDVASAQLPNFRHALVVFGGLQGLEAG... | Function: Required for association of the centrosomes with the poles of the bipolar mitotic spindle during metaphase . Also involved in chromosome alignment . May promote centrosome maturation probably by recruiting A-kinase anchor protein AKAP9 to centrosomes in early mitosis . Binds specifically to miRNA MIR145 hairp... |
Q3UHX9 | MAERPRKRPCGPGEHGQRVEWRKWKQQKKEEKKKWKDLKIMKKLERQRAQEEEAKRQEEEEEAAAQRSNQGRPYTLSVALPGSILDNAQSPELRTYLAGQIARACTIFCVDEIVVFDEEGQDTKSVEGEFRGVGKKGQACVQLARILQYLECPQYLRKAFFPKHQDLQFAGILNPLDSPHHMRQDEESEFREGVVVDRPTKAGHGSLVNCGMKKEVKIDKKLDPGLRVTVRLNQQQLPECKTYKGTVVSSQDPRTKAGLYWGYTVRLASCLSAVFAEAPFQDGYDLTIGTSERGSDVASAQLPSFRHALVVFGGLQGLEA... | Function: Required for association of the centrosomes with the poles of the bipolar mitotic spindle during metaphase. Also involved in chromosome alignment. May promote centrosome maturation probably by recruiting A-kinase anchor protein AKAP9 to centrosomes in early mitosis. Binds specifically to miRNA MIR145 hairpin,... |
Q7YZS9 | MMFRLTSVSCFLLVIACLNLFQVVLTSRCFPPGIYCTPYLPCCWGICCGTCRNVCHLRIGKRATFQE | Function: Kappa-conotoxins bind and inhibit voltage-gated potassium channels. This toxin inhibits the mammalian potassium channels Kv1.1/KCNA1 and Kv1.3/KCNA3.
PTM: Contains 4 disulfide bonds. Here are reported disulfide bonds proposed in [PubMed:16268797], even if the connectivity known for the framework XI is I-IV, I... |
A6H7E2 | MEAKTLGTVTPRKPVLSVSARKIKDNAADWHNLILKWETLNDGGFATANSIANMKISLSSKDKIELASSGLASNDCAEKEHPEYSRELETLCEELQATLEGLTKIQMKMEKLSSTTKGVCELEDYHHGEERKRPPLFHTWPTAHFYEVSRKLSDMYSQELRLKRTVVEQLAHTADRDLALSYLSMWLHQPYLEAGSWLLLESMLLETGHRVL | Function: Component of the DNA replication complex, which interacts with two kinases, CDK2 and CDC7, thereby providing a functional and physical link between CDK2 and CDC7 during firing of the origins of replication. Regulates ATR-mediated checkpoint signaling in response to DNA damage. Also involved in the cytoplasmic... |
Q9BW66 | MEAKTLGTVTPRKPVLSVSARKIKDNAADWHNLILKWETLNDAGFTTANNIANLKISLLNKDKIELDSSSPASKENEEKVCLEYNEELEKLCEELQATLDGLTKIQVKMEKLSSTTKGICELENYHYGEESKRPPLFHTWPTTHFYEVSHKLLEMYRKELLLKRTVAKELAHTGDPDLTLSYLSMWLHQPYVESDSRLHLESMLLETGHRAL | Function: Component of the DNA replication complex, which interacts with two kinases, CDK2 and CDC7, thereby providing a functional and physical link between CDK2 and CDC7 during firing of the origins of replication . Regulates ATR-mediated checkpoint signaling in response to DNA damage . Also involved in the cytoplasm... |
Q9D0V8 | MEAKTLGIATPRKPVLSVSARKLKDNAADWHNLILKWDSLSDKGFTTASSIANLKVSLLSKEKVELESSSPASMEEEEKTNLDYDKGLEALCEELQAILDGLTKIQMKMEKLSSTTKGICELENYHYREESSRPPLFHTWPTAFFYEVSRRLSEAYKKELLLKHTIGAELAHTADRNLSLTYLSMWLHQPYIESNSKLQLESMLLETGHRAL | Function: Component of the DNA replication complex, which interacts with two kinases, CDK2 and CDC7, thereby providing a functional and physical link between CDK2 and CDC7 during firing of the origins of replication. Regulates ATR-mediated checkpoint signaling in response to DNA damage. Also involved in the cytoplasmic... |
A6XH05 | MSSLIMQVVIPKPAKFFHNNLFSLSSKRHRFSTTTTTRGGRWARCSLQTGNEIQTERRTGGYQPTLWDFSTIQSFDSEYKEEKHLMRAAGMIDQVKMMLQEEVDSIRRLELIDDLRRLGISCHFEREIVEILNSKYYTNNEIDERDLYSTALRFRLLRQYDFSVSQEVFDCFKNAKGTDFKPSLVDDTRGLLQLYEASFLSAQGEETLRLARDFATKFLQKRVLVDKDINLLSSIERALELPTHWRVQMPNARSFIDAYKRRPDMNPTVLELAKLDFNMVQAQFQQELKEASRWWNSTGLVHELPFVRDRIVECYYWTTG... | Cofactor: Binds 3 Mg(2+) or Mn(2+) ions per subunit.
Function: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products, components of the chemical defense arsenal . Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into 1,8-cineole, and, as minor products, alpha-terpineol, beta-... |
Q9LQF2 | MEGVGLRAVGSHCSLSEMDDLDLTRALDKPRLKIERKRSFDERSMSELSTGYSRHDGIHDSPRGRSVLDTPLSSARNSFEPHPMMAEAWEALRRSMVFFRGQPVGTLAAVDNTTDEVLNYDQVFVRDFVPSALAFLMNGEPDIVKHFLLKTLQLQGWEKRVDRFKLGEGVMPASFKVLHDPIRETDNIVADFGESAIGRVAPVDSGFWWIILLRAYTKSTGDLTLSETPECQKGMKLILSLCLAEGFDTFPTLLCADGCSMIDRRMGVYGYPIEIQALFFMALRSALSMLKPDGDGREVIERIVKRLHALSFHMRNYFWL... | Function: Cytosolic invertase that specifically cleaves sucrose into glucose and fructose and is involved in the regulation of multiple tissue development including primary root elongation, root hair growth, leaf and silique development, and floral transition . Is involved in osmotic stress-induced inhibition on latera... |
Q69T31 | MELAVGAGGMRRSASHTSLSESDDFDLSRLLNKPRINVERQRSFDDRSLSDVSYSGGGHGGTRGGFDGMYSPGGGLRSLVGTPASSALHSFEPHPIVGDAWEALRRSLVFFRGQPLGTIAAFDHASEEVLNYDQVFVRDFVPSALAFLMNGEPEIVRHFLLKTLLLQGWEKKVDRFKLGEGAMPASFKVLHDSKKGVDTLHADFGESAIGRVAPVDSGFWWIILLRAYTKSTGDLTLAETPECQKGMRLILSLCLSEGFDTFPTLLCADGCCMIDRRMGVYGYPIEIQALFFMALRCALQLLKHDNEGKEFVERIATRLH... | Function: Cytosolic invertase that cleaves sucrose into glucose and fructose and is involved in the regulation of primary root elongation, lateral root formation, floral transition and pollen development.
Catalytic Activity: Hydrolysis of terminal non-reducing beta-D-fructofuranoside residues in beta-D-fructofuranoside... |
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