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
Sequence domains:
Structure domain:
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Leader protease (preferred)
PDBe Complex ID:
PDB-CPX-136753 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leader protease
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 173 amino acids
Theoretical weight: 19.78 KDa
Source organism: Foot-and-mouth disease virus (strain O1)
Expression system: Escherichia coli BL21(DE3)
UniProt:
Structure domains: Cysteine proteinases
Length: 173 amino acids
Theoretical weight: 19.78 KDa
Source organism: Foot-and-mouth disease virus (strain O1)
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P03305 (Residues: 29-201; Coverage: 7%)
Structure domains: Cysteine proteinases
