| IED ID | IndEnz0002007459 |
| Enzyme Type ID | protease007459 |
| Protein Name |
Genome polyprotein Cleaved into: P1; Capsid protein VP0 VP4-VP2 ; Capsid protein VP4 P1A Virion protein 4 ; Capsid protein VP2 P1B Virion protein 2 ; Capsid protein VP3 P1C Virion protein 3 ; Capsid protein VP1 P1D Virion protein 1 Fragment |
| Gene Name | |
| Organism | Echovirus 16 (strain Harrington) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Picornavirales Picornaviridae Enterovirus Enterovirus B Echovirus E16 Echovirus 16 (strain Harrington) |
| Enzyme Sequence | MGAQVSTQKTGAHETLLEAAQGATINYTNINYYKDAASNSANRQDFSQDPSKFTEPVKDIMIKSMPALNSPSAEECGYSDRVRSITLGNSTITTQESANVVVAYGRWPKYLEDDQATAEDQPTQPDVATCRFYTLESVQWEANSAGWWWKFPEALKDMGLFGQNMYYHYLGRAGYTIHVQCNASKFHQGCLLVVCVPEAEMGCAKPDENVDATNLTNGENTCELTAGAAPAEKGKVQTAVCNATMGVAVGNLTIFPHQWINLRTNNCATIVMPYINSVPMDNMFRHYNFTLMVIPFVPLTSMGGSTYVPITVTIAPMCAEYNGLRLSTQHQGLPVMNVPGSNQFLTSDNFQSPCAMPEYDVTPPLDIPGEVNNLMEVAEVDSVVPVNNLSDNVKTIKAYQIPVSAGDSSRPEAVFKFQLDPGSGSVLKHTLLGEIINYYAHWSGSIKLTFVFCGSAMATGKLLIAYSPPGASAPATRKDAMLGTHIIWDLGLQSSCVLCVPWISQTHYRMVERDEYTTAGYISCWYQTNIIVPPDTPSQCYMLCLASACNDFSVRMLKDTPFIQQEAKLQGEPGKAIESAISRVADTISSGPTNSEQVPALTAAETGHTSQVVPGDTIQTRHVKNYHSRSESTIENFLCRSACVHIARYEAGANASNEDRFVRWEINNKELVQLRRKCEMFTYLRYDVEVTFVITSQQDQGTDLSQDMPVLTHQVMYVPPGGSVTKQGDSYAWQTSTNPSVFWTEGNAPPRMSIPFISIGNAYSSFYDGWSHFSQKGVYGYNTLNKMGTLFVRHVNKETPKPVTSTVRVYFKPKHIRAWIPRPPRLCPYKYKANVNFDVTAITDSRLTITTVPQVEHNLRTA |
| Enzyme Length | 862 |
| Uniprot Accession Number | Q66790 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms the vertices of the capsid (By similarity). Capsid protein VP1 interacts with host cell receptor to provide virion attachment to target host cells (By similarity). This attachment induces virion internalization (By similarity). Tyrosine kinases are probably involved in the entry process (By similarity). After binding to its receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP1 N-terminus (that contains an amphipathic alpha-helix) and capsid protein VP4 are externalized (By similarity). Together, they shape a pore in the host membrane through which viral genome is translocated to host cell cytoplasm (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Capsid protein VP4]: Lies on the inner surface of the capsid shell (By similarity). After binding to the host receptor, the capsid undergoes conformational changes (By similarity). Capsid protein VP4 is released, Capsid protein VP1 N-terminus is externalized, and together, they shape a pore in the host membrane through which the viral genome is translocated into the host cell cytoplasm (By similarity). {ECO:0000250|UniProtKB:P03300}.; FUNCTION: [Capsid protein VP0]: Component of immature procapsids, which is cleaved into capsid proteins VP4 and VP2 after maturation (By similarity). Allows the capsid to remain inactive before the maturation step (By similarity). {ECO:0000250|UniProtKB:P03300}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Chain (7); Initiator methionine (1); Lipidation (1); Non-terminal residue (1); Site (2) |
| Keywords | Autocatalytic cleavage;Capsid protein;Eukaryotic host gene expression shutoff by virus;Eukaryotic host translation shutoff by virus;Host cytoplasm;Host gene expression shutoff by virus;Host-virus interaction;Lipoprotein;Magnesium;Myristate;Pore-mediated penetration of viral genome into host cell;Viral attachment to host cell;Viral penetration into host cytoplasm;Virion;Virus entry into host cell |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}. |
| Modified Residue | |
| 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: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and a molecule of genomic RNA generates the provirion. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: During virion maturation, immature virions are rendered infectious following cleavage of VP0 into VP4 and VP2. This maturation seems to be an autocatalytic event triggered by the presence of RNA in the capsid and it is followed by a conformational change infectious virion. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP4]: Myristoylation is required during RNA encapsidation and formation of the mature virus particle. {ECO:0000250|UniProtKB:P03300}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 95,399 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |