The domain within your query sequence starts at position 17 and ends at position 49; the E-value for the JmjN domain shown below is 9.4e-14.

MTFRPSMEEFREFNKYLAYMESKGAHRAGLAKC

JmjN

JmjN
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