Function and Biology Details
Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.
NTP + H(2)O = NDP + phosphate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
Capsid protein VP2 and RNA (preferred)
PDBe Complex ID:
PDB-CPX-136762 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct RNA molecules
2 distinct RNA molecules
Macromolecules (3 distinct):
RNA-directed RNA polymerase 3D-POL
Molecule details ›
Chain: A
Length: 481 amino acids
Theoretical weight: 54.11 KDa
Source organism: Foot-and-mouth disease virus (strain C1-Santa Pau)
Expression system: Escherichia coli BL21(DE3)
UniProt:
Structure domains:
Length: 481 amino acids
Theoretical weight: 54.11 KDa
Source organism: Foot-and-mouth disease virus (strain C1-Santa Pau)
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P03311 (Residues: 1858-2327; Coverage: 20%)
Structure domains:
