Detail Information for IndEnz0002000864
IED ID IndEnz0002000864
Enzyme Type ID protease000864
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 RNA1
Organism Broad bean wilt virus 1 (strain Spinach/United States/ATCC PV-132/1963) (BBWV-1)
Taxonomic Lineage Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Picornavirales Secoviridae Comovirinae Fabavirus Broad bean wilt virus 1 (BBWV-1) Broad bean wilt virus 1 (strain Spinach/United States/ATCC PV-132/1963) (BBWV-1)
Enzyme Sequence MDSETIDMCVKFLKISFGLQSLKNLVKELFGGSELEKLAYVHAAFFHANEMAIHWNADLPWEEVMSSKRIKERFGYVKSHFLRNVVYNADASGQMIRYNTTTCEQWFCCNFNLASYSASYNSLVPEEGGSMPINEEAEIKIGQSLLTCAQSVTKAIYAKLSTLTTRSIQGFLECLRDAICGAFSSWLPCIRGAFAWFGNIIEVLKHWAGAAHEKLHNFLEGIEECLYMGLGLVASTCIVALIEKFLVTMSVISGPCGRPTLFLTSAMAIISSTYLLSKAVEKSSAFTMLLGFVTQSCQTVLGSLFGKSAKGSEEAQGQFGPSAMLESLATLVSSWSSSSVTEIGRTFGAISQIKNGIIALKDMALFVFSKLCEMASKVLGFESQILADLSIILGENVADWLDECDCMLAYLLEFNSNARDIFDRLSQLIEKGKAIRMGILRTTHRGPSQVLSLVTKALDKLTELHNSVIMSGANSTRKTPFMLFFTGKSGVGKTSVVQRMAANWLQQEQLGSNEVYSRNGLDPFWSGYKRQAVVTYDDFGAVPGSVSNEAEIINVVSSNPHSVMMADLKEKGMYFDSRLIIASSNFLAANPESGVHDSEAYERRRHVVVQVSLKEDMAYDPGNPCANQRYTLLESKAPFAEKAVFESYEELWSHVYNAFKAHEEKEKLFLSSLPIPERSEKEALQALIGICVMTTSYAPKAVIQYGIDHLVGYHYLISSAEHVYFWHEKGEVEIVPMHLMKLDKMDKATMASTSLKSALMCQDMAKNFPTLNPLAVLYAKNIVIRGWVDANLQASKKCEDSYMREQIESLPKWQRAYLHVLSGHIASNETRGWFLNCLEVTKSNSRSSYIWEYKSWPMPLKLALGSFLAILAGSAIFCSLQSLWSISGNASFVAGAASIFTIGSATAQSAPPNKDGSEYTYRNKKIKIRNWEGQGPCFGDSALWIAENCMATLVVMKDRVQVCMAPGRSFLGVNHFLRMIPNGVMVKLETGMTETYFVWEKSKLKLFENSEIALYTSSNLPKAPDSLVDRFHFDLETLPKTFPAQFFTYKFDKDMQQYVPELGELLCKKAERALCVVSGEYRRVISHHLTYRNPTVAGDCGGLVLAIIEGKCKLVGLHVASDGEEGAASPVPWDPDFKVAQGQSDFLLSYDEWAVPKVLGPGCKAVGIISPEHTVGSGGKTSFLETPIEWQLNRPCGKIPSILVKGDVRLAGTENADYDPFAVGMTKYAKEAGPFEPNGLDRVCESIAETWHDASDGFEFGPVDLEAALNGIENMEYFDALVLSTSEGYPYRLDRKPGEKGKARYVEGEPGNLEITDERILADIHWFEEISKTQVPDLYCIECVKDERLPVRKVIKEPKSRLFTVLPMSYNLAIRKKFLNFVRFIMKRRDVLPCQVGINPYSRQWGKVADRLLEKGNSILCCDYSRFDGFLPKCIMVKIAEMFSNIVGETGAEREQTKNLMLACCSRYAICGRVLYRVENGIPSGFPLTVIVNSILNEILIKYAYWKCFETESLIRDHFDTYVAMVVYGDDNLISVSEAISSKFNGNFLVNFMCNLGIKVTDGVDKTKVGIEFRTIEDCDFLKRKFKENADGTWSGVMAEEHLWPQLHFVKAKKVEMSEAYISNCNNILRELWLGSPEKAAAFRREVISKLKWVEPQRLLTISQVALFHNEQMNGEHPFVEACHQLENLELMAPLEPGMLPIKTQEIMPGLFVASEKNFTGNFDDYFTISITTNRKFEDGKGFQIIFPYGAGRGGLPSKAFMEQNVIRKGCAIQKAFKQGLEKGNKMLFISQSSVIPAYVFAIMLYRSVDRLPRALSNKALTSALGICKKLSYLPKDFPDLF
Enzyme Length 1842
Uniprot Accession Number Q76L40
Absorption
Active Site ACT_SITE 975; /note=For picornain 3C-like protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222; ACT_SITE 1011; /note=For picornain 3C-like protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222; ACT_SITE 1100; /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 487..494; /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;Reference proteome;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 909; /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 205,786
Kinetics
Metal Binding
Rhea ID RHEA:21248
Cross Reference Brenda