JmjCA domain family that is part of the cupin metalloenzyme superfamily.
|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 latter found without the JmjN domain in organisms from bacteria to human [(PUBMED:10838566), (PUBMED:11165500)].
The JmjC domain belongs to the Cupin superfamily [(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. 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)].
|GO function:||protein binding (GO:0005515)|
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- Evolution (species in which this domain is found)
- Literature (relevant references for this domain)
- Structure (3D structures containing this domain)
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