| IED ID | IndEnz0002000863 |
| Enzyme Type ID | protease000863 |
| Protein Name |
RNA1 polyprotein Genome polyprotein B Cleaved into: Protease cofactor; Putative helicase EC 3.6.4.- Membrane-binding protein NTP-binding protein NTB ; Viral genome-linked protein VPg ; Picornain 3C-like protease 3C-like protease EC 3.4.22.- ; RNA-directed RNA polymerase EC 2.7.7.48 |
| Gene Name | |
| Organism | Broad bean wilt virus 2 (BBWV-2) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Picornavirales Secoviridae Comovirinae Fabavirus Broad bean wilt virus 2 (BBWV-2) |
| Enzyme Sequence | MDFSTMQVVVGFLKTSMGLQSIRDIVQKAKVDEKDKTLLHIHLCFFHANEMARDLNEGMDVSQIHSSAAIKYRAAIVTRHVKMNVETGGYDRKRMVEYNNETCVNWFSCEFKEEKEESQELPVDEDCVEEIVENFLENCGISDQNDQISTTSNANYAFGQGLYEYATRVSDAIVAVISGSIKKGIDEFLDKVYAAMSQIFAAWMPKIRAAFQWFENIKEVVKNWARTMHEKINCILVGMEDCLYMGAGLVAATCIVTLLEKFMVVTKILPAPCGAATLFLTTAMATISAAYVCTKAVEKSVMLTNVLHFVTTNCQIVLNALFNHDATKKELGANQNEGEAPTGVGQFGISTMLQDVANLMSTWSTNSVTEIGRTFGAISQIKNGILALRDMVYFVFEKLSDLAHKVLGFESQVLADLTILLGENVADWLSECDCMVSYMLEFNSRNREIFDRLSQLIEKGRLIRTGVLRTGHRGSSQVMALVTKALEKLIELHNSVVMSGSNTTRKAPFMVFFTGASGTGKTSVVQRVAINWLQEEQLGTNEIYSRNGQDPFWSGYKRHAVVTYDDFGAVPGTTSNEAEIINVISRNPYATVMAGLAEKGMYFDSRLVLASRNFLAANPESGVHDSEAYERRRHAVIRVSLKPGVPYNADDPCANQTYTLLDSKTPFREIQTFETYAELWSYLYTSFKEHEVQEELYLKSLPILDSDKKEALEGLVGLTVIATSFAPKAVMQYGMEKFPGHHFLVSDGEKCYFWHGDGSVESASVEQMQLSKQDVAQLKQQGLSTAMMYKDLAKAFPTLNSLAVLYAKNIVVKRWVGPDLEPTKTCEDVYMREQIGNLPKWQRAYLYVLSKYLTTQSPRGWFMECLEETKKNLRATYLWEYKQWPLPLKLALGSLIAIMAGGAIWYSLQSLWCMSGDASFVAGAATVFSVSSFAGQSDIPNRDNSERSFRNRKVRARTWQGQSSCFGDSALWIAETCMATLTFSNVRTQVCLAPGRGFFGVNHCLAAIPAGVMVKMDSSIGVTYFVWGKEKLLQFDGNEIALYMTSTLPKTVDSLLGRIHFDVETLPKTFSAVFFSYKYDPMIQQMVPELGSVTCKVHNKAYTLAHGEYRREIPQSLSYEASTVAGDCGSLILAEIEGKFKLVGMHVAFNGREGSASFMPYHASLDQKVGQGDFMLKYQEWAEPKILGPGCRAMGLIDPEHALAASGKTTFVETPEEWHLDYPCDKLPSVLARGDPRLAGTVHADYDPFASGMSKYAKEAGPFDAASLKQVCSGIVEIWEDASADFPMDEVDLDTAINGLENVEFFDALVLGTSEGFPYRLDRGPGDKGKSRYVSGESGSLKITDEGVLSDIAWFEEVSKTQVPDLYCIECVKDERLPIRKVLHEPKSRLFTVLPMSYNIVIRKKFLNFVRFFMKRRDVLTAQVGINPYSREWTRMANKLLSKGNNILCCDYSRFDGFLPKCIMNEIGNMIARLMKTDEVSRTQIKNLMLACTSRYAMCNRVLYRVENGIPSGFPLTVIVNSILNEILVKYAYWHCFEDNPSVQSNFDAHVSMVVYGDDNLISVSDAISSRFDGNFLVSFMEGLGIKVTDGIDKTKVGIEFRRLENCDFLKRSFKMSPDGTWRSPMSKESLWPQLHFVKAKKLEMAEAYINNCNNILRELWLHDVKEAEEFRNKVLRNLRWIGHEQLLNMQQLAVFHSEQMNGVSDFLSTCVTVDSIPLMDPLVPGMLPVKTSEIIPRVFVAAEKHFEGNFNDFFTISITTSRKFEEDKGFVLLFPYGAGRGGLPTTQFMRENVIRKGCSIQKKFRQAYEKGNNILFISQSSVVPSYVFAVMLLHSIGAISRLSSNKALTQAMQTCKRLEYLPKEYEEFF |
| Enzyme Length | 1870 |
| Uniprot Accession Number | Q9WNW0 |
| Absorption | |
| Active Site | ACT_SITE 1003; /note=For picornain 3C-like protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222; ACT_SITE 1039; /note=For picornain 3C-like protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222; ACT_SITE 1128; /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]: Thiol protease that cleaves the RNA1 and RNA2 polyproteins. {ECO:0000250|UniProtKB:P03600}.; FUNCTION: [Viral genome-linked protein]: Plays a role in RNA replication. It is covalently linked to the 5'terminus of both viral single-stranded RNA1 and RNA2 molecules. {ECO:0000250|UniProtKB:P03600}.; FUNCTION: [Protease cofactor]: Down-regulates the RNA1 polyprotein processing and enhances trans-cleavage of RNA2 polyproteins. The protease cofactor and the putative helicase seem to target the replication complexes to ER membranes. Their physical association causes the membrane rearrangement of host ER that may result in formation of the small membranous vesicles that are the site of viral RNA synthesis. {ECO:0000250|UniProtKB:P03600}.; FUNCTION: [Putative helicase]: The protease cofactor and the putative helicase seem to target the replication complexes to ER membranes. Their physical association causes the membrane rearrangement of host ER that may result in formation of the small membranous vesicles that are the site of viral RNA synthesis. {ECO:0000250|UniProtKB:P03600}.; FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral genome. {ECO:0000250|UniProtKB:P03600}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | NP_BIND 515..522; /note=ATP; /evidence=ECO:0000255|PROSITE-ProRule:PRU00551 |
| Features | Active site (3); Chain (6); Domain (3); Modified residue (1); Nucleotide binding (1); Site (4); Transmembrane (1) |
| Keywords | ATP-binding;Covalent protein-RNA linkage;Helicase;Host cytoplasm;Host endoplasmic reticulum;Host membrane;Hydrolase;Membrane;Nucleotide-binding;Nucleotidyltransferase;Phosphoprotein;Protease;RNA-directed RNA polymerase;Thiol protease;Transferase;Transmembrane;Transmembrane helix;Viral RNA replication |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Putative helicase]: Host membrane {ECO:0000250|UniProtKB:P03600}; Single-pass membrane protein {ECO:0000250|UniProtKB:P03600}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P03600}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host endoplasmic reticulum {ECO:0000250|UniProtKB:P03600}.; SUBCELLULAR LOCATION: [Protease cofactor]: Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P03600}. |
| Modified Residue | MOD_RES 937; /note=O-(5'-phospho-RNA)-serine; /evidence=ECO:0000250|UniProtKB:P03600 |
| Post Translational Modification | PTM: [RNA1 polyprotein]: Specific enzymatic cleavages by picornain 3C-like protease in vivo yield mature proteins. Picornain 3C-like protease is autocatalytically processed. {ECO:0000250|UniProtKB:P03600}.; PTM: [Viral genome-linked protein]: 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. {ECO:0000250|UniProtKB:P03600}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 210,038 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:21248 |
| Cross Reference Brenda |