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
Structure analysis Details
Assemblies composition:
Assembly name:
Helper component proteinase (preferred)
PDBe Complex ID:
PDB-CPX-161022 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Helper component proteinase
Molecule details ›
Chain: A
Length: 158 amino acids
Theoretical weight: 18.05 KDa
Source organism: Turnip mosaic virus
Expression system: Escherichia coli
UniProt:
Structure domains: Helper component proteinase
Length: 158 amino acids
Theoretical weight: 18.05 KDa
Source organism: Turnip mosaic virus
Expression system: Escherichia coli
UniProt:
- Canonical:
P89509 (Residues: 663-820; Coverage: 5%)
Structure domains: Helper component proteinase
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SSRF BEAMLINE BL17U
Spacegroup:
I422
Expression system: Escherichia coli
