| IED ID | IndEnz0002000875 |
| Enzyme Type ID | protease000875 |
| Protein Name |
RNA1 polyprotein P1 Cleaved into: P1A protein 1A Protease cofactor ; Putative ATP-dependent helicase EC 3.6.4.- 1B Membrane-binding protein NTP-binding protein NTB ; Viral genome-linked protein 1C-VPg ; Picornain 3C-like protease 3C-like protease EC 3.4.22.- 1D-PRO ; RNA-directed RNA polymerase EC 2.7.7.48 1E-POL |
| Gene Name | |
| Organism | Raspberry ringspot virus (strain cherry) (RpRSV) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Picornavirales Secoviridae Comovirinae Nepovirus Raspberry ringspot virus Raspberry ringspot virus (strain cherry) (RpRSV) |
| Enzyme Sequence | MGWTCPVQGCMYSRSTWSNRGLKEDGLSSTMRCPGAMCGAMLVRSEPVQAPKATVVPQTPVTAVRPKRTVVSATPLRKQDCVVVVEVGFPALLSLEYPALAGRARHTGEFDSALLARKPSNGGTARAPTGWFKPRVVRTQPAKKALPSWVSEARRLIKGALEGSNAFGPRYCREKFPKARLVWVLGMLSKSSPPSVAIGRQLKKSFLALQARIARALAKKQSARAARRQEACRKIRLALQQARGIAALERQQARQLSGAGLYSVRLCTKRALSPIVEVPKRHKKKAISLPSPVSVQEFPEGLVGPNFWETSGLLNCVASPQRREDLVFPVYGIDSCRTDPEYFVVGPKSPSKIMGDTKPRLPTCPAEALNLLWASNLFEDWELDIIGQMVSDGLLTSQAFLDGCTLVSYYGQEQMVDSFHCLLQDPVPAEVAEALAVDVQALDFDAVFGCGISDFLRGTRDAMKGWIMDPVIAKSTTWCNTIIDKVRALFDQYFAPFHKIIDGMSYVNSLWAKCKEWAQSVLKNGSQLFSVMWETHCVSFVIIITCACTLLVENVLKELRLISRVGTLTSCVISGALGILGCGYILAKCEDLAVVSASIRAFLGVLLCPPTMEAVDLNQSLIPEEIQATSWTGVDRVLGALNAVGSGLTGFNTDTIIYWGRFAQSFDGMRRGKDAVCALAACLFEKLGTVYNRVTGKEAAFFHELSSLVSIDVQGWLNSSRRVMAESIAFAKSDAVAFATVERLINDGETIQLTAASAPKSHSMQFGQILAERLRELRTLRNDMAHAGSFEGRRCVPFWLYIYGPPGVGKTTTMHEFSQALLTAFEFPSDSLTSKSATDKYWSLYRRQALVQIDDLGAISESGMEQEMMNIVSSATYNPTMAVANEKTTLFDSKFIVSTSNNYSAGTDAKIHDRKAFNRRRRVVIKTRGKAGVAFNPHDSTAAAEFCVVERDDRAETPIWVQSGEAPDDKELYWMDFRTTVAYVIEQARIHHNAEDIEQAQYSMKHSRTRQLYQVCENYIGEVKMSVANFVPGDMLGAWNLEPKGRFFYSCVDGRVYSYDPEQKAHDEGPVDKALDFEQICLEKLSYTLQADIQGGPKSATAGIFLRSMVSGECAVESVDKLNRSASREHLIFFKNLSLADRVYLRLVQKRILQLAMVGDPLGLRSYTVMMEGFQNSYNYVKENGGRLLLILCSCMLLGIACYTFFNALAILIGGTSVAAGAAAMVDIGACGSTSTYASEYGAKMGRRNMPHRSREIPAVWSEETGHDEKWQLCGLLETCRSDMPAVHVNLVPGNKFAITKHQAQAIPDGSSVGLSVAGRSFRTFQWRASALTEYAESEICTYFDSRIPSLGKQAMKMYSDSDLDALNVKYFSTRTLHFRLVDDQVEKRHWDADACVISTPKTIVSTINGVIYRQEIPTAITYRRESVKHDCGALVFTEVRGKPKAVGMLVGTLGGTTYVCKFPHIEVDAFACVPDIRGFNLEAGVSTLGYSKLGWLDRRHQPHNSEKTEFVPIPEKYHMDDVPCKIPAVLSAKDPRLADIPQCMGYDPYKQGMEKFAHPMQEIDEQLLATVCDEIAQEFHDVGVRGRMVSMDEAINGHHKYEIPSFYVEGASTRELNELRTSCSAEVWCCDPRSDIEFEYPRIIPGPVESKWKCESTCCGCTFKSGGTEAIISFVKARSPCCEEIFFDGLDLTTSEGYPLFLDRPAGAKGKERFFEGSENQKFLIPDCPLDVQLKKGIEETHLGTPQLIIKESAKDELLKEGKVLPSEGMPGTRLFSICPAWYNIVVRQHFVYIAESVRKRRRTLSSQVGIVVGSREWDDLAARLRSKKNDKMYCCDYSKFDGLMTPQIVHAITNIYERMFSGNDGMSQFRQNLLMGICNRISICGSQVYRVEAGMPSGFALTVDFNSIFNEILVRCAYRSLVPEIERPFFSNNVVLIVYGDDNVLGIHPNIESAFNGNAIKAYMKEELGIKITDGADKLSPVICARPLEQCEFLKRTWRKDRQYGLYRAPLVETSIYSCLRYVRLQNYDWQAPLLQNVQGSLYEASLHGPDMHARIYKHFATHFPKWVEEHELYTYEQCRTRFIAAKNGDFNFHPASAQMGHVFSQQTEIQELSQSQNPKRCFQLHPKIHICGPGHNEQDCFYVDVRVKGKITKGKGFHHAPVFSAGSGQLGTVKWASSFRSSSACPMRDLAVDAFKRGECVYFRDNGELINAWLAAINFGMSINADGLDGLLQVYRNQGPTHLDDLSFYFEGGVVGVPAPAHLMVYGTDTSILNRLCPKTVLESAPPPGRSSNVSERSQVQTFLHMSPKPCFITLKGSGKVCHGLRCNNSCRGHISCTDVVRNSAANQRAAMLDVLRRGCYNIQ |
| Enzyme Length | 2367 |
| Uniprot Accession Number | Q6W8W4 |
| Absorption | |
| Active Site | ACT_SITE 1302; /note=For picornain 3C-like protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222; ACT_SITE 1339; /note=For picornain 3C-like protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222; ACT_SITE 1432; /note=For picornain 3C-like protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; |
| DNA Binding | |
| EC Number | 3.6.4.-; 3.4.22.-; 2.7.7.48 |
| Enzyme Function | FUNCTION: Picornain 3C-like protease is a thiol protease that cleaves the P1 and P2 polyproteins. {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 804..811; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00551 |
| Features | Active site (3); Chain (5); Domain (3); Nucleotide binding (1); Topological domain (2); Transmembrane (1) |
| Keywords | ATP-binding;Covalent protein-RNA linkage;Helicase;Host endoplasmic reticulum;Host membrane;Hydrolase;Membrane;Nucleotide-binding;Nucleotidyltransferase;Protease;RNA-binding;RNA-directed RNA polymerase;Thiol protease;Transferase;Transmembrane;Transmembrane helix;Viral RNA replication |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Viral genome-linked protein]: Host endoplasmic reticulum lumen {ECO:0000250}.; SUBCELLULAR LOCATION: [Putative ATP-dependent helicase]: Host endoplasmic reticulum membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}. |
| Modified Residue | |
| Post Translational Modification | PTM: Specific enzymatic cleavages by picornain 3C-like protease in vivo yield mature proteins. Picornain 3C-like protease is autocatalytically processed (By similarity). {ECO:0000250}.; PTM: VPg is uridylylated by the polymerase and is covalently linked to the 5'-end of genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity). {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 263,135 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:21248 |
| Cross Reference Brenda |