Function and Biology

Crystal structure of methyltransferase domain of human Histone-lysine N-methyltransferase SETMAR

Source organism: Homo sapiens
Biochemical function: zinc ion binding
Biological process: histone lysine methylation
Cellular component: nucleus

EC 2.1.1.357: [Histone H3]-lysine(36) N-dimethyltransferase

Reaction catalysed:
(1a) S-adenosyl-L-methionine + a [histone H3]-L-lysine(36) = S-adenosyl-L-homocysteine + a [histone H3]-N(6)-methyl-L-lysine(36)
Systematic name:
S-adenosyl-L-methionine:[histone H3]-L-lysine(36) N(6)-dimethyltransferase

GO terms

Biochemical function:
Biological process:
Cellular component:

Sequence families

Pfam Protein families (Pfam)
PF05033
Domain description: Pre-SET motif
Occurring in:
  1. Histone-lysine N-methyltransferase SETMAR
1 copy of Pfam domain PF05033 (Pre-SET motif) in Histone-lysine N-methyltransferase SETMAR in PDB 3bo5.

PF00856
Domain description: SET domain
Occurring in:
  1. Histone-lysine N-methyltransferase SETMAR
1 copy of Pfam domain PF00856 (SET domain) in Histone-lysine N-methyltransferase SETMAR in PDB 3bo5.

InterPro InterPro annotations
IPR007728
Domain description: Pre-SET domain
Occurring in:
  1. Histone-lysine N-methyltransferase SETMAR
IPR001214
Domain description: SET domain
Occurring in:
  1. Histone-lysine N-methyltransferase SETMAR

Structure domain

CATH CATH domain
2.170.270.10
Class: Mainly Beta
Architecture: Beta Complex
Topology: Beta-clip-like
Homology: SET domain
Occurring in:
  1. Histone-lysine N-methyltransferase SETMAR
1 copy of CATH domain 2.170.270.10 (Beta-clip-like) in Histone-lysine N-methyltransferase SETMAR in PDB 3bo5.