JmjN

Small domain found in the jumonji family of transcription factors		 JmjN
SMART accession number:SM00545
Description: To date, this domain always co-occurs with the JmjC domain (although the reverse is not true).
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) ].

Family alignment:
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There are 6190 JmjN domains in 6180 proteins in SMART's nrdb database.

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