Function and Biology Details
Reactions catalysed:
S-adenosyl-L-methionine + guanine(2445) in 23S rRNA = S-adenosyl-L-homocysteine + N(2)-methylguanine(2445) in 23S rRNA
S-adenosyl-L-methionine + guanine(2069) in 23S rRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(2069) in 23S rRNA
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- S-adenosyl-L-methionine-dependent methyltransferase superfamily
- THUMP domain
- Ribosomal RNA large subunit methyltransferase K/L-like, methyltransferase domain
- Ribosomal RNA large subunit methyltransferase K/L
- S-adenosylmethionine-dependent methyltransferase
- DNA methylase, N-6 adenine-specific, conserved site
Structure analysis Details
Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160015 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Ribosomal RNA large subunit methyltransferase K/L
Molecule details ›
Chains: A, B
Length: 702 amino acids
Theoretical weight: 78.96 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 702 amino acids
Theoretical weight: 78.96 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
- Canonical:
P75864 (Residues: 1-702; Coverage: 100%)
Sequence domains:
- RlmL ferredoxin-like domain
- THUMP domain
- RMKL-like, methyltransferase domain
- S-adenosylmethionine-dependent methyltransferase
