Detail Information for IndEnz0002013798
IED ID IndEnz0002013798
Enzyme Type ID protease013798
Protein Name Replicase polyprotein P2AB
Cleaved into: N-terminal protein; Serine protease
EC 3.4.21.-
; VPg; RNA-directed RNA polymerase
EC 2.7.7.48
RdRp
Gene Name ORF2A-2B
Organism Cocksfoot mottle virus (isolate Dactylis glomerata/Norway/CfMV-NO/1995) (CfMV)
Taxonomic Lineage Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Sobelivirales Solemoviridae Sobemovirus Cocksfoot mottle virus Cocksfoot mottle virus (isolate Dactylis glomerata/Norway/CfMV-NO/1995) (CfMV)
Enzyme Sequence MGCSVVGNCKSVMLMSRMSWSKLALLISVAMAAAMTDSPPTLICMGILVSVVLNWIVCAVCEEASELILGVSLETTRPSPARVIGEPVFDPRYGYVAPAIYDGKSFDVILPISALSSASTRKETVEMAVENSRLQPLESSQTPKSLVALYSQDLLSGWGSRIKGPDGQEYLLTALHVWETNISHLCKDGKKVPISGCPIVASSADSDLDFVLVSVPKNAWSVLGVGVARLELLKRRTVVTVYGGLDSKTTYCATGVAELENPFRIVTKVTTTGGWSGSPLYHKDAIVGLHLGARPSAGVNRACNVAMAFRVVRKFVTVENSELYPDQSSGPARELDAETYTERLEQGIAFTEYNISGITVKTSDREWTTAEALRVARYKPLGGGKAWGDSDDEDTQETAIRPLNLPAGGLPTGQSALGQLIEYAGYVWRDEGIINSNGMPFRSAGKSSCRFREAVCRAVHRDVRAAETEFPELKELAWPSRGSKAEIGSLLFQAGRFERVEAPANLQLAITNLQAQYPRSRPRSCFRREPWCREDFVAEIEKIAHSGEINLKASPGVPLAEIGVSNQQVIDVAWPLVCEAVVERLHALASVDPRQHDWSPEELVKRGLCDPVRLFVKQEPHSRQKIEQGRFRLISSVSLVDQLVERMLFGPQNTTEIALWHSNPSKPGMGLSKASQVALLWEDLARKHQTHPGAMADISGFDWSVQDWELWADVSMRIELGSFPALMAKAAISRFYCLMNATFQLTNGELLTQELPGLMKSGSYCTSSSNSRIRCLMAELIGSPWCIAMGDDSVEGWVDDAPRKYSALGHLCKEYEACPVLPNGDLKEVSFCSHLISKGRAELETWPKCLFRYLSGPHDVESLEMELSSSRRWGQIVRYLRRIGRVSGNDGEERSSNESPATTKTQGSAAAWGPPQEAWPVDGASLSTFEPSSSGWFHLEGW
Enzyme Length 942
Uniprot Accession Number Q0PW25
Absorption
Active Site ACT_SITE 176; /note=For protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01216; ACT_SITE 209; /note=For protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01216; ACT_SITE 276; /note=For protease activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01216
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 3.4.21.-; 2.7.7.48
Enzyme Function FUNCTION: [Serine protease]: Responsible for cleavage of polyprotein P2A and replicase polyprotein P2AB.; FUNCTION: [VPg]: Covalently attached to the 5' extremity of the genomic and subgenomic RNAs. It may serve as a primer for the replicase.; FUNCTION: [RNA-directed RNA polymerase]: Replicates the viral genome. {ECO:0000255|PROSITE-ProRule:PRU00539}.
Temperature Dependency
PH Dependency
Pathway
nucleotide Binding
Features Active site (3); Chain (5); Compositional bias (1); Domain (2); Modified residue (2); Region (1); Sequence conflict (5); Site (4); Transmembrane (2)
Keywords Covalent protein-RNA linkage;Direct protein sequencing;Host membrane;Hydrolase;Membrane;Nucleotide-binding;Nucleotidyltransferase;Phosphoprotein;Protease;RNA-directed RNA polymerase;Reference proteome;Ribosomal frameshifting;Serine protease;Transferase;Transmembrane;Transmembrane helix;Viral RNA replication
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Replicase polyprotein P2AB]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [N-terminal protein]: Host membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Modified Residue MOD_RES 339; /note=Phosphothreonine; by host; /evidence=ECO:0000269|PubMed:21068217; MOD_RES 390; /note=Phosphoserine; by host; /evidence=ECO:0000269|PubMed:21068217
Post Translational Modification PTM: The polyprotein is proteolytically cleaved into several chains by the viral protease. {ECO:0000269|PubMed:11038392, ECO:0000269|PubMed:21068217}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 103,355
Kinetics
Metal Binding
Rhea ID RHEA:21248
Cross Reference Brenda