Detail Information for IndEnz0002000871
IED ID IndEnz0002000871
Enzyme Type ID protease000871
Protein Name RNA1 polyprotein
Genome polyprotein B
P1

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 Cherry rasp leaf virus (isolate Potato/United States) (CRLV)
Taxonomic Lineage Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Picornavirales Secoviridae Cheravirus Cherry rasp leaf virus (CRLV) Cherry rasp leaf virus (isolate Potato/United States) (CRLV)
Enzyme Sequence MGIFTLCSCGVPCPTRSFYRRHMASGCDLLPTRQQLADVGYTEPTVIAEVVTPPTQAPLELFVEISPPVLAPFEPSVEISLPIQAPAEPIVEASPPAATQFVGIEALIASGPCFFGSFGPFEEYYSSPVGPLTRFDTLRREGHCAARARVAAVAAKAVIVQQTLSETAAAMRATLPLWMKGQVAPPVKSKRALKREAKAKAKADYLASDEAYYKATDGLTALPPGVSRDVHMRQLDAMEVAYLAHVGDVAARGFQRRQVLRAAYKARCEKRAFKRFLEEVDFLCLPVHIVDKIQTPFDGEQAAAPEMQKGMVYATSRRQVKTRRSFSSFLPKEDFSFTLGVCPARSPTVTPSSTPSTSRSSSPEPRVSSPSGVLPEKAACIGFCSHGSECTEHFCFGYLNLKSEALASQYLAWLLQTKLPGGISCFELEVSSYLEQCQDTMEAIDLWWHAMDRYCFNFKSSKYVILDNFLCKHSIAKDQTPREFLAKHRIAKAKALHRVPSRKEKMQALCEQRADKAWDAYIELNKNCKVGEGPLEYLKAAKDRCVEFFSPFTKYCNEAIRSLNPLVAILGPFKDGFWTCFNNLREKCLKMVNDHWLAFAAGTTLVLSLIFLLCIICLVKIFSILIANLGLGVVAITTLVTALVVGFFLFNGMLEQAADLQLCSLVASDFLNFLAQNQGSALVAGTMASVQDDLRGQGVSWCFSALYKLISRVVPVGIKETSILFNSIGNVSRSANHSKDFFLNMKEMACSWMDALSDAMALISDDSVSAMQVLKHLCEHDFLDWAKKVERYAGETYDSLIISPAERLKILRILADQQESFQKAFYNPRIASKAPRLMLTEFNRLSTLLRDAHNALSRASLFDRQRTPPFWVHLYSENGGTGKSMAMMPLGNHMLDAIGEPKTCRFVTRNVASKFLNGYQHQPCFLMDEFGAAPKQDYSDEVTMLDLVSPNALTLNMAAIGEKNTMFTSKLIISTANRRLAHPDVKLGANLDGFLRRRNILAEVVLVSGKPHFHEFNLLAPRTEQKVYLNRAMQESQVPDPLTPQEFYSLCTENFVNFLNQQSSTVAMSAGLNYVRSSDFSHLKDFLLFKIGLDFEENEVERIVTDYGNSLKNETIFPPEHEQIFQKWKDALDSLTLPELVSLLDKSVSETFVYTLISENHPNVVMSSLTPYECMIYAICKKKYREGTEAKLPFPEGETTSYGASFLSFVAQVALCIPKWALFCVALCAVLLVGYLIIKFAIFLFSGVVTLLGALAFSNLSGDGAEDSPSFDTNRKRGGVKFEYSTKWDASSTNRFAESYSENGTIPAGTSWADFFGEGPEEEPSQSLLNLLKHQVVLIAEPTKVVYNCIALGGRNFLITKHVWDLMPACNYGLYGYAVAKDRIFISPRIRPCAQLKGRDLVIVQLPDSVPPFTSLPRDIFLENMAKAPKTANACLVVAKPLFERRSVAKLEQTIYPFKQLPQVHSKDTYSCGSLGSKQMPACYSYVFETYAGLCTSPLIAQEGGRCIILGLHVVGDRSKMGYAQIVTLDDFSDVALSDKVGQGPEEMYIPTKNSECFGSVTKLGAWTGPKPYFLEKTSLIPSLISTSIDVERTTEPAILSQRDKRLKDSINPEFDVFLEGMKKYAVEAHSLDEDLEVFEDALDRVFLEIPEHACEDLTNDQVCNGIEDDPYAEGIVMQTAEGFPFCTQRPAGASGKSWLFAGAPGDWHIVPGSLLANEMHKKEVAPSRGLFEPLIGIDFPKDEKVDSSKVYIKPKTRLFTILPVDYNILVRKYFLSSVSHIMTQHNTIPVKVGIDCLSNEWSILYHQLRSKGTNWFNGDYSRFDGITPRNVLQGIVKRINKFYNNKNSLAITDSNLSINSDLARSLLTDMASTRYGLTNGDLWYVTSGIPSGFPLTVIVNSLVNNFFIHFSYIKLMKREELNSLYPLHSFRQMVAYATYGDDNLVSVNDVITEKFNLVKIADLLAEHGVTLKNGADKNEEILSPFYPLEKVDFLKRKFVHYQGHVVAPLNPVNITERLHWIRKGLGEADATLENCSSAAFEALFHGRCYYDTLVAKIYKACAASKLSIQLPTYNDALAIFLSNDSFAKAIQTISLDLPKAIFVNKSNYFVSEIFPDVFFCSNERNVTLHKLLEITTTRNICYISRNYESRNSSRGLFSLKGEGWALAPVSARLVVYKNMQKPVYFVDEANDGLALAYCLDYMLRIKGVSRSRLAQVLYNIFGHDETLCSRIASNFSLLDSNKYMPPHKK
Enzyme Length 2250
Uniprot Accession Number Q6EWG9
Absorption
Active Site ACT_SITE 1362; /note=For picornain 3C-like protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222; ACT_SITE 1400; /note=For picornain 3C-like protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222; ACT_SITE 1495; /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 probably cleaves the B and M polyproteins.; FUNCTION: Viral genome-linked protein (VPg) plays a role in RNA replication. {ECO:0000250}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (5); Compositional bias (1); Domain (3); Modified residue (1); Region (1); Site (4); Transmembrane (1)
Keywords ATP-binding;Covalent protein-RNA linkage;Helicase;Host membrane;Hydrolase;Membrane;Nucleotide-binding;Nucleotidyltransferase;Phosphoprotein;Protease;RNA-directed RNA polymerase;Reference proteome;Thiol protease;Transferase;Transmembrane;Transmembrane helix;Viral RNA replication
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Putative helicase]: Host membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Modified Residue MOD_RES 1299; /note=O-(5'-phospho-RNA)-serine; /evidence=ECO:0000250
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: Viral genome-linked protein (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 251,009
Kinetics
Metal Binding
Rhea ID RHEA:21248
Cross Reference Brenda