Function and Biology Details
Reactions catalysed:
a 5'-end (5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleosidein mRNA + S-adenosyl-L-homocysteine.
a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA +S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleoside) in mRNA + S-adenosyl-L-homocysteine + H(+).
RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate.
a 5'-end diphospho-ribonucleoside in mRNA + GTP + H(+) = a 5'-end(5'-triphosphoguanosine)-ribonucleoside in mRNA + diphosphate.
Thiol-dependent hydrolysis of ester, thioester, amide, peptide andisopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residueprotein attached to proteins as an intracellular targeting signal).
TSAVLQ-|-SGFRK-NH2 and SGVTFQ-|-GKFKK the two peptides corresponding tothe two self-cleavage sites of the SARS 3C-like proteinase are the twomost reactive peptide substrates. The enzyme exhibits a strong preferencefor substrates containing Gln at P1 position and Leu at P2 position.
ATP + H2O = ADP + phosphate + H(+).
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
SARS-CoV-2 NSP9 complex (preferred)
PDBe Complex ID:
PDB-CPX-145080 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3C-like proteinase nsp5
Molecule details ›
Chain: A
Length: 306 amino acids
Theoretical weight: 33.83 KDa
Source organism: Severe acute respiratory syndrome coronavirus 2
Expression system: Escherichia coli
UniProt:
Sequence domains: Coronavirus endopeptidase C30
Length: 306 amino acids
Theoretical weight: 33.83 KDa
Source organism: Severe acute respiratory syndrome coronavirus 2
Expression system: Escherichia coli
UniProt:
- Canonical:
P0DTD1 (Residues: 3264-3569; Coverage: 4%)
Sequence domains: Coronavirus endopeptidase C30
