Function and Biology Details
Reaction catalysed:
Hydrolysis of an asparaginyl bond involved in the maturation of the structural protein of the virus, typically -Asn-|-Ala- or -Asn-|-Phe-.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
hetero 420-mer (preferred)
Assembly name:
Membrane-lytic peptide gamma and RNA (preferred)
PDBe Complex ID:
PDB-CPX-191582 (preferred)
Entry contents:
2 distinct polypeptide molecules
1 distinct RNA molecule
1 distinct RNA molecule
Macromolecules (3 distinct):
Capsid protein beta
Molecule details ›
Chains: A, B, C
Length: 355 amino acids
Theoretical weight: 38.43 KDa
Source organism: Pariacoto virus
UniProt:
Sequence domains: Peptidase A6 family
Structure domains: Jelly Rolls
Length: 355 amino acids
Theoretical weight: 38.43 KDa
Source organism: Pariacoto virus
UniProt:
- Canonical:
Q9J7Z0 (Residues: 7-361; Coverage: 89%)
Sequence domains: Peptidase A6 family
Structure domains: Jelly Rolls
Membrane-lytic peptide gamma
Molecule details ›
Chains: D, E, F
Length: 40 amino acids
Theoretical weight: 4.25 KDa
Source organism: Pariacoto virus
UniProt:
Length: 40 amino acids
Theoretical weight: 4.25 KDa
Source organism: Pariacoto virus
UniProt:
- Canonical: Q9J7Z0 (Residues: 362-401; Coverage: 10%)
