PROSITE documentation PDOC51183

JmjN and JmjC domains profiles

The JmjN and JmjC domains are two non-adjacent domains which have been identified in the jumonji family of transcription factors. Although it was originally suggested that the JmjN and JmjC domains always co-occur and might form a single functional unit within the folded protein, the JmjC domain was latter 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 (see <PDB:1H2K>), and are candidates for enzymes that regulate chromatin remodelling. The cupin fold is a flattened β-barrel structure containing two sheets of five antiparallel β strands that form the walls of a zinc-binding cleft. JmjC domains were identified in numerous eukaryotic proteins containing domains typical of transcription factors, such as PHD (see <PDOC50016>), C2H2 (see <PDOC00028>), ARID/BRIGHT and zinc fingers [2,3]. The JmjC has been shown to function in a histone demethylation mechanism that is conserved from yeast to human [4].

In addition to eukaryotic transcription factors of the jumonji family, a JmjC domain is also found in the following proteins:

• Eukaryotic transcription factors of the jumonji family.
• Mammalian hairless. In human, defects in HR are the cause of alopecia universalis congenita (ALUNC) [MIM:203655]. ALUNC is a rare autosomal recessive form of hair loss characterized by hair follicles without hair.
• Mammalian F-box/LRR-repeat protein 10 (FBXL10) and 11 (FBXL11) or JmjC domain-containing histone demethylase 1B (JHDM1B) or 1A (JHDM1A).
• Human retinoblastoma-binding protein 2.
• Several putative chromatin-associated proteins.
• Bacillus subtilis hypothetical protein yxbC.
• Escherichia coli hypothetical protein ycfD.
• Neisseria meningitidis Z2491 hypothetical protein NMA0679.

The profiles we developed cover the entire JmjN and JmjC domains.