Detail Information for IndEnz0002000869
IED ID IndEnz0002000869
Enzyme Type ID protease000869
Protein Name RNA1 polyprotein
B RNA polyprotein
Bottom component polyprotein
Genome polyprotein B
P1

Cleaved into: Protease cofactor
32 kDa protein
; Putative helicase
EC 3.6.4.-
58 kDa protein
Membrane-binding protein
NTP-binding protein
NTB
; Viral genome-linked protein
VPg
; Picornain 3C-like protease
3C-like protease
EC 3.4.22.-
24 kDa protein
; RNA-directed RNA polymerase
EC 2.7.7.48
87 kDa protein
Gene Name
Organism Cowpea mosaic virus (strain SB) (CPMV)
Taxonomic Lineage Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Picornavirales Secoviridae Comovirinae Comovirus Cowpea mosaic virus (CPMV) Cowpea mosaic virus (strain SB) (CPMV)
Enzyme Sequence MGLPEYEADSEALLSQLTIEFTPGMTVSSLLAQVTTNDFHSAIEFFAAEKAVDIEGVHYNAYMQQIRKNPSLLRISVVAYAFHVSDMVAETMSYDVYEFLYKHYALFISNLVTRTLRFKELLLFCKQQFLEKMQASIVWAPELEQYLQVEGDAVAQGVSQLLYKMVTWVPTFVRGAVDWSVDAILVSFRKHFEKMVQEYVPMAHRVCSWLSQLWDKIVQWISQASETMGWFLDGCRDLMTWGIATLATCSALSLVEKLLVAMGFLVEPFGLSGIFLRTGVVAAACYNYGTNSKGFAEMMALLSLAANCVSTVIVGGFFPGEKDNAQSSPVILLEGLAGQMQNFCETTLVSVGKTCTAVNAISTCCGNLKALAGRILGMLRDFIWKTLGFETRFLADASLLFGEDVDGWLKAISDLRDQFIAKSYCSQDEMMQILVLLEKGRQMRKSGLSKGGISPAIINLILKGINDLEQLNRSCSVQGVRGVRKMPFTIFFQGKSRTGKSLLMSQVTKDFQDHYGLGGETVYSRNPCDQYWSGYRRQPFVLMDDFAAVVTEPSAEAQMINLISSAPYPLNMAGLEEKGICFDSQFVFVSTNFLEVSPEAKVRDDEAFKNRRHVIVQVSNDPAKAYDAANFASNQIYTILAWKDGRYNTVCVIEDYDELVAYLLTRSQQHAEEQEKNLANMMKSATFESHFKSLVEVLELGSMISAGFDIIRPEKLPSEAKEKRVLYSIPYNGEYCNALIDDNYNVTCWFGECVGNPEQLSKYSEKMLLGAYEFLLCSESLNVVIQAHLKEMVCPHHYDKELNFIGKIGETYYHNQMVSNIGSMQKWHRAILFGIGVLLGKEKEKTWYQVQVANVKQALYDMYTKEIRDWPMPIKVTCGIVLAAIGGSAFWKVFQQLVGSGNGPVLMGVAAGAFSAEPQSRKPNRFDMQQYRYNNVPLKRRVWADAQMSLDQSSVAIMSKCRANLVFGGTNLQIVMVPGRRFLACKHFFTHIKTKLRVEIVMDGRRYYHQFDPANIYDIPDSELVLYSHPSLEDVSHSCWDLFCWDPDKELPSVFGADFLSCKYNKFGGFYEAQYADIKVRTKKECLTIQSGNYVNKVSRYLEYEAPTIPEDCGSLVIAHIGGKHKIVGVHVAGIQGKIGCASLLPPLEPIAQAQGAEEYFDFLPAEENVSSGVAMVAGLKQGVYIPLPTKTALVETPSEWHLDTPCDKVPSILVPTDPRIPAQHEGYDPAKSGVSKYSQPMSALDPELLGEVANDVLELWHDCAVDWDDFGEVSLEEALNGCEGVEYMERIPLATSEGFPHILSRNGKEKGKRRFVQGDDCVVSLIPGTTVAKAYEELEASAHRFVPALVGIECPKDEKLPMRKVFDKPKTRCFTILPMEYNLVVRRKFLNFVRFIMANRHRLSCQVGINPYSMEWSRLAARMKEKGNDVLCCDYSSFDGLLSKQVMDVIASMINELCGGEDQLKNARRNLLMACCSRLAICKNTVWRVECGIPSGFPMTVIVNSIFNEILIRYHYKKLMREQQAPELMVQSFDKLIGLVTYGDDNLISVNAVVTPYFDGKKLKQSLAQGGVTITDGKDKTSLELPFRRLEECDFLKRTFVQRSSTIWDAPEDKASLWSQLHYVNCNNCEKEVAYLTNVVNVLRELYMHSPREATEFRRKVLKKVSWITSGDLPTLAQLQEFYEYQRQQGGADNNDTCDLLTSVDLLGPPLSFEKEAMHGCKVSEEIVTKNLAYYDFKRKGEDEVVFLFNTLYPQSSLPDGCHSVTWSQGSGRGGLPTQSWMSYNISRKDSNINKIIRTAVSSKKRVIFCARDNMVPVNIVALLCAVRNKLMPTAVSNATLVKVMENAKAFKFLPEEFNFAFSDV
Enzyme Length 1866
Uniprot Accession Number P03600
Absorption
Active Site ACT_SITE 987; /note="For picornain 3C-like protease activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01222, ECO:0000269|PubMed:1887592"; ACT_SITE 1023; /note="For picornain 3C-like protease activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01222, ECO:0000269|PubMed:1887592"; ACT_SITE 1113; /note="For picornain 3C-like protease activity"; /evidence="ECO:0000255|PROSITE-ProRule:PRU01222, ECO:0000269|PubMed:1887592"
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:0000269|PubMed:16453750, ECO:0000269|PubMed:16789216, ECO:0000269|PubMed:8811039}.; 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:0000269|PubMed:11883002, ECO:0000269|PubMed:16453534}.; FUNCTION: [Protease cofactor]: Down-regulates the RNA1 polyprotein processing and enhances trans-cleavage of RNA2 polyproteins (PubMed:1413528). 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 (PubMed:12021362). {ECO:0000269|PubMed:12021362, ECO:0000269|PubMed:1413528}.; 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:0000269|PubMed:12021362}.; FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral genome. {ECO:0000305|PubMed:1431806}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding NP_BIND 494..501; /note="ATP"; /evidence="ECO:0000255|PROSITE-ProRule:PRU00551, ECO:0000305|PubMed:7964626"
Features Active site (3); Chain (6); Domain (3); Initiator methionine (1); Modified residue (1); Mutagenesis (11); Nucleotide binding (1); Site (4); Transmembrane (1)
Keywords ATP-binding;Covalent protein-RNA linkage;Direct protein sequencing;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:0000305}; Single-pass membrane protein {ECO:0000305}. Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:12021362}.; SUBCELLULAR LOCATION: [RNA-directed RNA polymerase]: Host endoplasmic reticulum {ECO:0000269|PubMed:10864669}.; SUBCELLULAR LOCATION: [Protease cofactor]: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:12021362}.
Modified Residue MOD_RES 920; /note=O-(5'-phospho-RNA)-serine; /evidence=ECO:0000269|Ref.5
Post Translational Modification PTM: [RNA1 polyprotein]: Specific enzymatic cleavages by picornain 3C-like protease in vivo yield mature proteins (PubMed:16789216, PubMed:16789257, PubMed:7964626, PubMed:1431806). Picornain 3C-like protease is autocatalytically processed. {ECO:0000269|PubMed:1431806, ECO:0000269|PubMed:16789216, ECO:0000269|PubMed:16789257, ECO:0000269|PubMed:7964626}.; 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:0000269|Ref.5}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 209,810
Kinetics
Metal Binding
Rhea ID RHEA:21248
Cross Reference Brenda