Function and Biology Details
Reactions catalysed:
S-adenosyl-L-methionine + a 5'-(5'-triphosphoguanosine)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-[mRNA]
S-adenosyl-L-methionine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(ribonucleotide)-[mRNA] = S-adenosyl-L-homocysteine + a 5'-(N(7)-methyl 5'-triphosphoguanosine)-(2'-O-methyl-ribonucleotide)-[mRNA]
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
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).
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
3C-like proteinase nsp5 (preferred)
PDBe Complex ID:
PDB-CPX-143092 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3C-like proteinase nsp5
Molecule details ›
Chains: A, B
Length: 306 amino acids
Theoretical weight: 33.22 KDa
Source organism: Tylonycteris bat coronavirus HKU4
Expression system: Escherichia coli
UniProt:
Sequence domains: Coronavirus endopeptidase C30
Structure domains:
Length: 306 amino acids
Theoretical weight: 33.22 KDa
Source organism: Tylonycteris bat coronavirus HKU4
Expression system: Escherichia coli
UniProt:
- Canonical:
P0C6W3 (Residues: 3292-3597; Coverage: 4%)
Sequence domains: Coronavirus endopeptidase C30
Structure domains:
