The domain within your query sequence starts at position 16 and ends at position 50; the E-value for the JmjN domain shown below is 3.3e-15.



PFAM accession number:PF02375
Interpro abstract (IPR003349):

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 [ (PUBMED:10838566) (PUBMED:11165500) ].

JmJC domains are predicted to be metalloenzymes that adopt the cupin fold, and are candidates for enzymes that regulate chromatin remodelling. The cupin fold is a flattened beta-barrel structure containing two sheets of five antiparallel beta 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, C2H2, ARID/BRIGHT and zinc fingers [ (PUBMED:11165500) (PUBMED:12446723) ]. The JmjC has been shown to function in a histone demethylation mechanism that is conserved from yeast to human [ (PUBMED:16362057) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry JmjN