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:
Sequence domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Nuclear inclusion protein A, TccC3, TcdB2 (preferred)
PDBe Complex ID:
PDB-CPX-137889 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nuclear inclusion protein A; TccC3; TcdB2
Molecule details ›
Chain: A
Length: 2410 amino acids
Theoretical weight: 272.97 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 2410 amino acids
Theoretical weight: 272.97 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
- Canonical:
Q8GF99 (Residues: 1-1474; Coverage: 100%) - Canonical: Q8GF97 (Residues: 1-680; Coverage: 71%)
- Canonical: P04517 (Residues: 2038-2273; Coverage: 8%)
Sequence domains:
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
SLS BEAMLINE X10SA
Spacegroup:
P3221
Expression system: Escherichia coli
