Function and Biology Details
Reactions catalysed:
S-adenosyl-L-methionine + adenine in DNA = S-adenosyl-L-homocysteine + N-6-methyladenine in DNA
Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates
Biochemical function:
Biological process:
Cellular component:
- not assigned
Sequence domains:
- N4/N6-methyltransferase, Type III restriction-modification enzyme EcoPI Mod subunit-like
- P-loop containing nucleoside triphosphate hydrolase
- S-adenosyl-L-methionine-dependent methyltransferase superfamily
- Type III R-M EcoP15I, C-terminal
- DNA methylase, N-6 adenine-specific, conserved site
- DNA methylase N-4/N-6
- Type III restriction enzyme, C-terminal endonuclease domain
- Helicase/UvrB, N-terminal
Structure analysis Details
Assembly composition:
hetero pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-118371 (preferred)
Entry contents:
2 distinct polypeptide molecules
2 distinct DNA molecules
2 distinct DNA molecules
Macromolecules (4 distinct):
Type III restriction-modification enzyme EcoP15I Mod subunit
Molecule details ›
Chains: A, B
Length: 644 amino acids
Theoretical weight: 74.19 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 644 amino acids
Theoretical weight: 74.19 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical:
P12364 (Residues: 1-644; Coverage: 100%)
Sequence domains:
Type III restriction-modification enzyme EcoP15I Res subunit
Molecule details ›
Chain: C
Length: 970 amino acids
Theoretical weight: 111.11 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
Sequence domains:
Length: 970 amino acids
Theoretical weight: 111.11 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
- Canonical: Q5ZND2 (Residues: 1-970; Coverage: 100%)
Sequence domains:
