Function and Biology Details
Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Hydrolyzes glutaminyl bonds, and activity is further restricted by preferences for the amino acids in P6 - P1' that vary with the species of potyvirus, e.g. Glu-Xaa-Xaa-Tyr-Xaa-Gln-|-(Ser or Gly) for the enzyme from tobacco etch virus. The natural substrate is the viral polyprotein, but other proteins and oligopeptides containing the appropriate consensus sequence are also cleaved.
Hydrolyzes a Gly-|-Gly bond at its own C-terminus, commonly in the sequence -Tyr-Xaa-Val-Gly-|-Gly, in the processing of the potyviral polyprotein.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
Structure domain:
Structure analysis Details
Assemblies composition:
Assembly name:
Capsid protein (preferred)
PDBe Complex ID:
PDB-CPX-137890 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nuclear inclusion protein A
Molecule details ›
Chains: A, B
Length: 242 amino acids
Theoretical weight: 27.53 KDa
Source organism: Tobacco etch virus
Expression system: Escherichia coli
UniProt:
Structure domains: Trypsin-like serine proteases
Length: 242 amino acids
Theoretical weight: 27.53 KDa
Source organism: Tobacco etch virus
Expression system: Escherichia coli
UniProt:
- Canonical:
P04517 (Residues: 2038-2279; Coverage: 8%)
Structure domains: Trypsin-like serine proteases
