The domain within your query sequence starts at position 18 and ends at position 59; the E-value for the JmjN domain shown below is 1.7e-22.
ECPVFEPSWEEFTDPLSFIGRIRPFAEKTGICKIRPPKDWQP
JmjNSmall domain found in the jumonji family of transcription factors |
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| SMART accession number: | SM00545 |
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| 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: |
There are 6190 JmjN domains in 6180 proteins in SMART's nrdb database.
Click on the following links for more information.
- Evolution (species in which this domain is found)
- Literature (relevant references for this domain)
- Structure (3D structures containing this domain)
- Links (links to other resources describing this domain)
