InterPro domain: IPR003349

The JmjN and JmjC domains are two non-adjacent domains which have beenidentified in the jumonji family of transcription factors. Although it wasoriginally suggested that the JmjN and JmjC domains always co-occur and mightform a single functional unit within the folded protein, the JmjC domain waslatter found without the JmjN domain in organisms from bacteria to human[ 1 , 2 ].

JmJC domains are predicted to be metalloenzymes that adopt the cupin fold, and are candidates for enzymes that regulate chromatinremodelling. The cupin fold is a flattened beta-barrel structure containingtwo sheets of five antiparallel beta strands that form the walls of a zinc-binding cleft. JmjC domains were identified in numerous eukaryotic proteinscontaining domains typical of transcription factors, such as PHD, C2H2, ARID/BRIGHT and zinc fingers [ 3 , 3 ]. TheJmjC has been shown to function in a histone demethylation mechanism that isconserved from yeast to human [ 4 ].

1. Evidence of domain swapping within the jumonji family of transcription factors. Trends Biochem. Sci. 25, 274-6
2. JmjC: cupin metalloenzyme-like domains in jumonji, hairless and phospholipase A2beta. Trends Biochem. Sci. 26, 7-9
3. Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha. J. Biol. Chem. 278, 1802-6
4. Histone demethylation by a family of JmjC domain-containing proteins. Nature 439, 811-6