Function and Biology Details
Reactions catalysed:
GTP + a 5'-diphospho-[mRNA] = diphosphate + a 5'-(5'-triphosphoguanosine)-[mRNA]
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).
TSAVLQ-|-SGFRK-NH(2) and SGVTFQ-|-GKFKK the two peptides corresponding to the two self-cleavage sites of the SARS 3C-like proteinase are the two most reactive peptide substrates. The enzyme exhibits a strong preference for substrates containing Gln at P1 position and Leu at P2 position.
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- Ubiquitin domain
- Ubiquitin-like domain
- Peptidase C16, coronavirus
- Ubiquitin conserved site
- Ubiquitin-like domain superfamily
- Papain-like viral protease, palm and finger domains, coronavirus
- Papain-like protease, thumb domain superfamily, coronavirus
- NSP3, second ubiquitin-like (Ubl) domain, coronavirus
1 more domain
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Ubiquitin and 3C-like proteinase nsp5 (preferred)
PDBe Complex ID:
PDB-CPX-143073 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):