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 dimer (preferred)
Assembly name:
Leader protease and Ubiquitin-like protein ISG15 (preferred)
PDBe Complex ID:
PDB-CPX-136752 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Leader protease
Molecule details ›
Chain: A
Length: 167 amino acids
Theoretical weight: 19.06 KDa
Source organism: Foot-and-mouth disease virus
Expression system: Escherichia coli
UniProt:
Structure domains: Cysteine proteinases
Length: 167 amino acids
Theoretical weight: 19.06 KDa
Source organism: Foot-and-mouth disease virus
Expression system: Escherichia coli
UniProt:
- Canonical:
P03305 (Residues: 29-195; Coverage: 7%)
Structure domains: Cysteine proteinases
Ubiquitin-like protein ISG15
Molecule details ›
Chain: B
Length: 78 amino acids
Theoretical weight: 8.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
Length: 78 amino acids
Theoretical weight: 8.81 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P05161 (Residues: 79-155; Coverage: 47%)
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
