IED ID | IndEnz0002009641 |
Enzyme Type ID | protease009641 |
Protein Name |
Genome polyprotein Cleaved into: Viral protein genome-linked VPg Protein 3B P3B ; Protease 3C EC 3.4.22.28 Picornain 3C P3C Fragment |
Gene Name | |
Organism | Echo 9 virus (EV-9) (Coxsackievirus A23) |
Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Picornavirales Picornaviridae Enterovirus Enterovirus B Echo 9 virus (EV-9) (Coxsackievirus A23) |
Enzyme Sequence | GAYTGMPNKKPKVPTLRQAKVQGPAFEFAVAMMKRNASTVKTEYGEFTMLGIYDRWAVLPRHAKPGPSILMNDQEVGVLDAKELVDKDGINLELTLLKLNRNEKFRDIRGFLAREEVEVNEAVLAINTSKFPNMYIPVGQVTDYGFLNLGGTPTKRMLMYNFPTRAGQCGGVLMSTGKVLGIHVGGNGHHGFSAALLRHYFNEEQ |
Enzyme Length | 205 |
Uniprot Accession Number | P08490 |
Absorption | |
Active Site | ACT_SITE 62; /note=For protease 3C activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222; ACT_SITE 93; /note=For protease 3C activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222; ACT_SITE 169; /note=For protease 3C activity; /evidence=ECO:0000255|PROSITE-ProRule:PRU01222 |
Activity Regulation | |
Binding Site | |
Calcium Binding | |
catalytic Activity | CATALYTIC ACTIVITY: [Protease 3C]: Reaction=Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.; EC=3.4.22.28; Evidence={ECO:0000255|PROSITE-ProRule:PRU01222}; |
DNA Binding | |
EC Number | 3.4.22.28 |
Enzyme Function | FUNCTION: [Viral protein genome-linked]: Acts as a primer for viral RNA replication and remains covalently bound to viral genomic RNA. VPg is uridylylated prior to priming replication into VPg-pUpU (By similarity). The oriI viral genomic sequence may act as a template for this. The VPg-pUpU is then used as primer on the genomic RNA poly(A) by the RNA-dependent RNA polymerase to replicate the viral genome (By similarity). Following genome release from the infecting virion in the cytoplasm, the VPg-RNA linkage is probably removed by host TDP2 (By similarity). During the late stage of the replication cycle, host TDP2 is excluded from sites of viral RNA synthesis and encapsidation, allowing for the generation of progeny virions (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Protease 3C]: Major viral protease that mediates proteolytic processing of the polyprotein (By similarity). Cleaves host EIF5B, contributing to host translation shutoff (By similarity). Cleaves also host PABPC1, contributing to host translation shutoff (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P03313}. |
Temperature Dependency | |
PH Dependency | |
Pathway | |
nucleotide Binding | |
Features | Active site (3); Chain (3); Domain (1); Modified residue (1); Non-terminal residue (2); Site (1) |
Keywords | Autocatalytic cleavage;Capsid protein;Covalent protein-RNA linkage;Host cytoplasm;Host-virus interaction;Hydrolase;Magnesium;Phosphoprotein;Protease;RNA-binding;T=pseudo3 icosahedral capsid protein;Thiol protease;Viral attachment to host cell;Virion;Virus entry into host cell |
Interact With | |
Induction | |
Subcellular Location | SUBCELLULAR LOCATION: [Viral protein genome-linked]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000250|UniProtKB:Q66478}.; SUBCELLULAR LOCATION: [Protease 3C]: Host cytoplasm {ECO:0000305}. |
Modified Residue | MOD_RES 3; /note=O-(5'-phospho-RNA)-tyrosine; /evidence=ECO:0000250|UniProtKB:P03300 |
Post Translational Modification | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250|UniProtKB:P03300}.; PTM: [Viral protein genome-linked]: VPg is uridylylated by the polymerase into VPg-pUpU. This acts as a nucleotide-peptide primer for the genomic RNA replication. {ECO:0000250|UniProtKB:P03300}. |
Signal Peptide | |
Structure 3D | |
Cross Reference PDB | - |
Mapped Pubmed ID | - |
Motif | |
Gene Encoded By | |
Mass | 22,716 |
Kinetics | |
Metal Binding | |
Rhea ID | |
Cross Reference Brenda |