Function and Biology Details
Reaction catalysed:
S-adenosyl-L-methionine + [peptide chain release factor 1 or 2]-L-glutamine = S-adenosyl-L-homocysteine + [peptide chain release factor 1 or 2]-N(5)-methyl-L-glutamine
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- S-adenosyl-L-methionine-dependent methyltransferase superfamily
- Protein-(glutamine-N5) methyltransferase, release factor-specific
- DNA methylase, N-6 adenine-specific, conserved site
- Methyltransferase small domain
- Methyltransferase HemK-like
- Release factor glutamine methyltransferase, N-terminal domain
Structure domain:
Structure analysis Details
Assembly composition:
homo dimer (preferred)
Assembly name:
Release factor glutamine methyltransferase (preferred)
PDBe Complex ID:
PDB-CPX-194553 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Release factor glutamine methyltransferase
Molecule details ›
Chains: A, B, C
Length: 282 amino acids
Theoretical weight: 31.65 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
Sequence domains:
Structure domains:
Length: 282 amino acids
Theoretical weight: 31.65 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9WYV8 (Residues: 1-282; Coverage: 100%)
Sequence domains:
Structure domains:
