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

Journal article

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.

Authors: Clissold, P; Ponting, C

• Journal: Trends in biochemical sciences
• Volume: 26
• Issue: 1
• Pages: 7-9
• Publication date: 2001-01-01
• DOI: 10.1016/s0968-0004(00)01700-x
• ISSN: 0968-0004
• Language: English
• Keywords: Transcription Factors; Intracellular Signaling Peptides and Proteins; Carrier Proteins; Chromatin; Amino Acid Motifs; Nerve Tissue Proteins; Retinoblastoma-Binding Protein 2; DNA; Phospholipases A; Evolution, Molecular; Animals; Humans; Protein Structure, Tertiary; Amino Acid Sequence; Tumor Suppressor Proteins; Binding Sites; Molecular Sequence Data; Group IV Phospholipases A2; Proteins