Function and Biology Details
Reactions catalysed:
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:
- not assigned
Biological process:
- not assigned
Cellular component:
Sequence domain:
Structure analysis Details
Assembly composition:
homo 24-mer (preferred)
Assembly name:
Polyprotein (preferred)
PDBe Complex ID:
PDB-CPX-101065 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Polyprotein
Molecule details ›
Chains: a, b, c, d, e, f, g, h, i, j, k, l, m, n, o, p, q, r, s, t, u, v, w, x
Length: 267 amino acids
Theoretical weight: 29.94 KDa
Source organism: Potato virus Y
Expression system: Escherichia coli
UniProt:
Length: 267 amino acids
Theoretical weight: 29.94 KDa
Source organism: Potato virus Y
Expression system: Escherichia coli
UniProt:
- Canonical:
A0A0C4URS3 (Residues: 2795-3061; Coverage: 9%)
