Function and Biology Details
Reactions catalysed:
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine(4) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(4)
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine(9) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(9)
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine(36) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(36)
S-adenosyl-L-methionine + a [histone H4]-L-lysine(20) = S-adenosyl-L-homocysteine + a [histone H4]-N(6)-methyl-L-lysine(20)
S-adenosyl-L-methionine + a [histone H4]-N(6)-methyl-L-lysine(20) = S-adenosyl-L-homocysteine + a [histone H4]-N(6),N(6)-dimethyl-L-lysine(20)
Biochemical function:
- not assigned
Biological process:
- not assigned
Cellular component:
- not assigned
Sequence domains:
Structure analysis Details
Assembly composition:
hetero trimer (preferred)
Assembly name:
Histone-lysine N-methyltransferase PRDM9 and DNA (preferred)
PDBe Complex ID:
PDB-CPX-509399 (preferred)
Entry contents:
1 distinct polypeptide molecule
2 distinct DNA molecules
2 distinct DNA molecules
Macromolecules (3 distinct):
Histone-lysine N-methyltransferase PRDM9
Molecule details ›
Chains: E, F
Length: 144 amino acids
Theoretical weight: 16.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
Sequence domains: Zinc finger, C2H2 type
Length: 144 amino acids
Theoretical weight: 16.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
- Canonical:
Q9NQV7 (Residues: 717-858; Coverage: 16%)
Sequence domains: Zinc finger, C2H2 type
