| IED ID | IndEnz0002008051 |
| Enzyme Type ID | protease008051 |
| Protein Name |
Genome polyprotein Cleaved into: Leader protein L ; Capsid protein VP0 VP4-VP2 ; Capsid protein VP4 P1A Rho Virion protein 4 ; Capsid protein VP2 Beta P1B Virion protein 2 ; Capsid protein VP3 Gamma P1C Virion protein 3 ; Capsid protein VP1 Alpha P1D Virion protein 1 Fragment |
| Gene Name | |
| Organism | Mengo encephalomyocarditis virus (strain 37A) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Pisuviricota Pisoniviricetes Picornavirales Picornaviridae Cardiovirus Cardiovirus A Encephalomyocarditis virus Mengo encephalomyocarditis virus Mengo encephalomyocarditis virus (strain 37A) |
| Enzyme Sequence | MATTMEQEICAHSMTFEECPKCSALQYRNGFYLLKYDEEWYPEELLTDGEDDVFDPDLDIEVVFETQGNSTSSDKNNSSSEGNEGVIINNFYSNQYQNSIDLSANATGSDPPKTYGQFSNLLSGAVNAFSNMLPLLADQNTEEMENLSDRVSQDTAGNTVTNTQSTVGRLVGYGTVHDGEHPASCADTASEKILAVERYYTFKVNDWTSTQKPFEYIRIPLPHVLSGEDGGVFGAALRRHYLVKTGWRVQVQCNASQFHAGSLLVFMAPEYPTLDVFAMDNKWSKDNLPNGTRTQANRKGPFAMDHQNFWQWTLYPHQFLNLRTNTTVDLEVPYVNIAPTSSWTQHASWTLVIAVVAPLTYSTGASTSLDITASIQPVRPVFNGLRHEVLSRQSPIPVTIREHAGTWYSTLPDSTVPIYGKTPVAPANYMVGEYKDFLEIAQIPTFIGNKVPNAVPYIEASNTAVKTQPLAVYQVTLSCSCLANTFLAALSRNFAQYRGSLVYTFVFTGTAMMKGKFLIAYTPPGAGKPTSRDQAMQATYAIWDLGLNSSYSFTVPFISPTHFRMVGTDLVNITNADGWVTVWQLTPLTYPPGCPTSAKILTMVSAGKDFSLKMPISPAPWSPQGVENAEKGVTENTDATADFVAQPVYLPENQTKVAFFYDRSSPIGAFTVKSGSLESGFAPFSNQACPNSVILTPGPQFDPAYDQLRPQRLTEIWGNGNEETSEVFPLKTKQDYSFCLFSPFVYYKCDLEVTLSPHTSGNHGLLVRWCPTGTPNKPTTQVLHEVSSLSEGRTPQVYSAGPGTSNQISFVVPYNSPLSVLPAVWYNGHKRFDNTGYLGIAPNSDFGTLFFAGTKPDIKFTVYLRYKNMRVFCPRPTVFFPWPTSGDKIDMTPRAGVLMLE |
| Enzyme Length | 901 |
| Uniprot Accession Number | P32540 |
| Absorption | |
| Active Site | |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | |
| DNA Binding | |
| EC Number | |
| Enzyme Function | FUNCTION: [Leader protein]: Forms a complex with host RAN and probably binds to exportins carrying activated MAPK in order to mediate the hyperphosphorylation of host Phe/Gly containing nuclear pore proteins (Nups) resulting in cessation of active nucleocytoplasmic transport (By similarity). Proteins with NLS signals fail to import, cellular mRNAs fail to export, and some proteins small enough for diffusion are not retained anymore (efflux) (By similarity). The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity). {ECO:0000250|UniProtKB:Q66765}.; FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. {ECO:0000250|UniProtKB:P12296}.; FUNCTION: [Capsid protein VP2]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. {ECO:0000250|UniProtKB:P12296}.; FUNCTION: [Capsid protein VP3]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3. Together they form an icosahedral capsid composed of 60 copies of each VP1, VP2, and VP3, with a diameter of approximately 300 Angstroms.VP4 lies on the inner surface of the protein shell formed by VP1, VP2 and VP3. All the three latter proteins contain a beta-sheet structure called beta-barrel jelly roll. VP1 is situated at the 12 fivefold axes, whereas VP2 and VP3 are located at the quasi-sixfold axes. {ECO:0000250|UniProtKB:P12296}.; 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). After genome has been released, the channel shrinks (By similarity). {ECO:0000250|UniProtKB:P03300, ECO:0000250|UniProtKB:P12296}.; FUNCTION: [Capsid protein VP0]: VP0 precursor is a component of immature procapsids. {ECO:0000250|UniProtKB:P08617}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Beta strand (2); Chain (7); Helix (2); Lipidation (1); Non-terminal residue (1); Site (3); Zinc finger (1) |
| Keywords | 3D-structure;Capsid protein;Host cytoplasm;Host-virus interaction;Lipoprotein;Metal-binding;Myristate;T=pseudo3 icosahedral capsid protein;Viral attachment to host cell;Virion;Virus entry into host cell;Zinc;Zinc-finger |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P12296}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniProtKB:P12296}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP1]: Virion {ECO:0000250|UniProtKB:P12296}. Host cytoplasm {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: [Leader protein]: Phosphorylated. {ECO:0000250|UniProtKB:Q66765}.; PTM: [Genome polyprotein]: Specific enzymatic cleavages by the viral protease in vivo yield a variety of precursors and mature proteins (By similarity). The polyprotein seems to be cotranslationally cleaved at the 2A/2B junction by a ribosomal skip from one codon to the next without formation of a peptide bond (By similarity). This process would release the P1-2A peptide from the translational complex (By similarity). {ECO:0000250|UniProtKB:P03304}.; 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 is followed by a conformational change of the particle. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP4]: Myristoylation is required during RNA encapsidation and formation of the mature virus particle. {ECO:0000250|UniProtKB:Q66282}. |
| Signal Peptide | |
| Structure 3D | NMR spectroscopy (1) |
| Cross Reference PDB | 2BAI; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 99,652 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | |
| Cross Reference Brenda |