Detail Information for IndEnz0002018975
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