| IED ID | IndEnz0002018975 |
| Enzyme Type ID | protease018975 |
| Protein Name |
Capsid protein alpha Cleaved into: Capsid protein beta EC 3.4.23.44 Coat protein beta Nodavirus endopeptidase ; Peptide gamma Coat protein gamma |
| Gene Name | alpha |
| Organism | Black beetle virus (BBV) |
| Taxonomic Lineage | Viruses Riboviria Orthornavirae Kitrinoviricota Magsaviricetes Nodamuvirales Nodaviridae Alphanodavirus Black beetle virus (BBV) |
| Enzyme Sequence | MVRNNNRRRQRTQRIVTTTTQTAPVPQQNVPKQPRRRRNRARRNRRQGRAMNMGALTRLSQPGLAFLKCAFAPPDFNTDPGKGIPDRFEGKVVTRKDVLNQSINFTANRDTFILIAPTPGVAYWVADVPAGTFPISTTTFNAVNFPGFNSMFGNAAASRSDQVSSFRYASMNVGIYPTSNLMQFAGSITVWKCPVKLSNVQFPVATTPATSALVHTLVGLDGVLAVGPDNFSESFIKGVFSQSVCNEPDFEFSDILEGIQTLPPANVTVATSGQPFNLAAGAEAVSGIVGWGNMDTIVIRVSAPTGAVNSAILKTWACLEYRPNPNAMLYQFGHDSPPCDEVALQEYRTVARSLPVAVIAAQNASMWERVKSIIKSSLAMASNVPGPIGIAASGLSGLSALFEGFGF |
| Enzyme Length | 407 |
| Uniprot Accession Number | P04329 |
| Absorption | |
| Active Site | ACT_SITE 75 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Hydrolysis of an asparaginyl bond involved in the maturation of the structural protein of the virus, typically -Asn-|-Ala- or -Asn-|-Phe-.; EC=3.4.23.44; |
| DNA Binding | |
| EC Number | 3.4.23.44 |
| Enzyme Function | FUNCTION: Capsid protein alpha self-assembles to form an icosahedral procapsid with a T=3 symmetry, about 30 nm in diameter, and consisting of 60 capsid proteins trimers. In addition, calcium ions are incorporated per capsid during assembly. The capsid encapsulates the two genomic RNAs. Capsid maturation occurs via autoproteolytic cleavage of capsid protein alpha generating capsid protein beta and the membrane-active peptide gamma (By similarity). {ECO:0000250}.; FUNCTION: Peptide gamma is a membrane-disrupting peptide produced by virus maturation, thereby creating the infectious virion. After penetration into the host cell, peptide gamma is probably exposed/released in endosomes, where it disrupts the endosomal membrane, facilitating translocation of viral RNA into the cytoplasm (By similarity). {ECO:0000250}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Beta strand (18); Chain (3); Compositional bias (2); Disulfide bond (1); Helix (10); Metal binding (2); Region (1); Turn (3) |
| Keywords | 3D-structure;Aspartyl protease;Calcium;Capsid protein;Disulfide bond;Hydrolase;Metal-binding;Protease;T=3 icosahedral capsid protein;Virion |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: [Capsid protein alpha]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein beta]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Peptide gamma]: Virion {ECO:0000305}. Note=Located inside the capsid and probably externalized in early endosomes. {ECO:0000305}. |
| Modified Residue | |
| Post Translational Modification | PTM: Capsid protein alpha autocatalytically maturates into capsid protein beta and peptide gamma. {ECO:0000250}. |
| Signal Peptide | |
| Structure 3D | X-ray crystallography (1) |
| Cross Reference PDB | 2BBV; |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 43,838 |
| Kinetics | |
| Metal Binding | METAL 249; /note=Calcium; /evidence=ECO:0000250; METAL 251; /note=Calcium; /evidence=ECO:0000250 |
| Rhea ID | |
| Cross Reference Brenda |