Function and Biology Details
Reactions catalysed:
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:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
Non-structural protein 3 (preferred)
PDBe Complex ID:
PDB-CPX-189162 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Non-structural protein 3
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 168 amino acids
Theoretical weight: 18.46 KDa
Source organism: Feline infectious peritonitis virus (strain 79-1146)
Expression system: Escherichia coli
UniProt:
Sequence domains: Macro domain
Structure domains: Leucine Aminopeptidase, subunit E, domain 1
Length: 168 amino acids
Theoretical weight: 18.46 KDa
Source organism: Feline infectious peritonitis virus (strain 79-1146)
Expression system: Escherichia coli
UniProt:
- Canonical:
Q98VG9 (Residues: 1331-1498; Coverage: 3%)
Sequence domains: Macro domain
Structure domains: Leucine Aminopeptidase, subunit E, domain 1
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ESRF BEAMLINE ID14-2
Spacegroup:
P213
Expression system: Escherichia coli
