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).
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.
ATP + H(2)O = ADP + phosphate
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
- NendoU domain, nidovirus
- NSP15, NendoU domain, coronavirus
- Endoribonuclease EndoU-like
- Nonstructural protein 15, middle domain, alpha/betacoronavirus
- Non-structural protein NSP15, middle domain superfamily
- Arterivirus Nsp11 N-terminal/Coronavirus NSP15 middle domain
- Nonstructural protein 15, middle domain, coronavirus
- Non-structural protein NSP15, N-terminal domain superfamily, coronavirus
4 more domains
Structure analysis Details
Assembly composition:
homo hexamer (preferred)
Assembly name:
SARS-CoV-2 NSP15 complex (preferred)
PDBe Complex ID:
PDB-CPX-145108 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule: