The domain within your query sequence starts at position 2264 and ends at position 2488; the E-value for the JmjC domain shown below is 3.29e-53.

MPTRYEDFLRCLPLPEYCNPEGKFNLASHLPGFFVRPDLGPRLCSAYGVAAAKDHDIGTT
NLHIEASDVVNVLVYVGIAKGNGVLSKAGILKKFEEEELDDVLRKRLKDSSEIPGALWHI
YAGKDVDKIREFLQKISKEQGLEVLPEHDPIRDQSWYVNRKLRQRLLEEYGVRACTLIQF
LGDAIVLPAGTLHQVQNFHSCVQVTEDFVSPEHLVQSFHLTQELR

JmjC

A domain family that is part of the cupin metalloenzyme superfamily.		 JmjC
SMART accession number:SM00558
Description: Probable enzymes, but of unknown functions, that regulate chromatin reorganisation processes (Clissold and Ponting, in press).
Interpro abstract (IPR003347):

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 later found without the JmjN domain in organisms from bacteria to human [ (PUBMED:10838566) (PUBMED:11165500) ].

Proteins containing JmjC domain are predicted to be metalloenzymes that adopt the cupin fold and are candidates for enzymes that regulate chromatin remodelling [ (PUBMED:11165500) ]. 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. Based on the crystal structure of JmjC domain containing protein FIH and JHDM3A/JMJD2A, the JmjC domain forms an enzymatically active pocket that coordinates Fe(III) and alphaKG. Three amino-acid residues within the JmjC domain bind to the Fe(II) cofactor and two additional residues bind to alphaKG [ (PUBMED:16983801) ].

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) ]. JmjC domain proteins may be protein hydroxylases that catalyse a novel histone modification [ (PUBMED:15809658) ]. The human JmjC protein named Tyw5p unexpectedly acts in the biosynthesis of a hypermodified nucleoside, hydroxy-wybutosine, in tRNA-Phe by catalysing hydroxylation [ (PUBMED:20739293) ].

Family alignment:
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There are 36166 JmjC domains in 36140 proteins in SMART's nrdb database.

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