Function and Biology Details
Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
ATP + H(2)O = ADP + phosphate
Biochemical function:
- not assigned
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
3C-like serine proteinase and Ubiquitin (preferred)
PDBe Complex ID:
PDB-CPX-143341 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Nsp2 cysteine proteinase
Molecule details ›
Chain: A
Length: 142 amino acids
Theoretical weight: 15.23 KDa
Source organism: Equine arteritis virus
Expression system: Escherichia coli
UniProt:
Sequence domains: Equine arterivirus Nsp2-type cysteine proteinase
Structure domains: Cathepsin B; Chain A
Length: 142 amino acids
Theoretical weight: 15.23 KDa
Source organism: Equine arteritis virus
Expression system: Escherichia coli
UniProt:
- Canonical:
P19811 (Residues: 261-392; Coverage: 4%)
Sequence domains: Equine arterivirus Nsp2-type cysteine proteinase
Structure domains: Cathepsin B; Chain A
Ubiquitin
Molecule details ›
Chain: B
Length: 76 amino acids
Theoretical weight: 8.56 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: 76 amino acids
Theoretical weight: 8.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical: P0CG48 (Residues: 609-683; Coverage: 11%)
Sequence domains: Ubiquitin family
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1
