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JmjC: cupin metalloenzyme-like domains in jumonji, hairless and phospholipase A2beta.

On the basis of significant sequence similarity, we have identified JmjC domains in more than 100 eukaryotic and bacterial sequences. These include human hairless, mutated in individuals with alopecia universalis, retinoblastoma-binding protein 2 and several putative chromatin-associated proteins. JmjC domains are predicted to be metalloenzymes that adopt the cupin fold, and are candidates for enzymes that regulate chromatin remodelling.[1]

References

  1. JmjC: cupin metalloenzyme-like domains in jumonji, hairless and phospholipase A2beta. Clissold, P.M., Ponting, C.P. Trends Biochem. Sci. (2001) [Pubmed]
 
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