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:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
3C-like proteinase nsp5 (preferred)
PDBe Complex ID:
PDB-CPX-145022 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Papain-like protease nsp3
Molecule details ›
Chains: A, B, C, D
Length: 176 amino acids
Theoretical weight: 18.99 KDa
Source organism: Severe acute respiratory syndrome coronavirus 2
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Macro domain
Length: 176 amino acids
Theoretical weight: 18.99 KDa
Source organism: Severe acute respiratory syndrome coronavirus 2
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P0DTD1 (Residues: 1023-1197; Coverage: 3%)
Sequence domains: Macro domain
