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PROSITE documentation PDOC50802 |
An homology region containing four conserved motifs has been identified in proteins from eukaryotes, several groups of viruses and the pathogenic bacteria Chlamydia pneumoniae [1]. None of these proteins has a known biochemical function but low sequence similarity with the polyprotein regions of arteriviruses has lead to suggest that it could possess cysteine protease activity [1]. In this case, the conserved cysteine and aspartate in motif I and the histidine in motif IV could be the catalytic residues. Motifs II and III have a more limited sequence conservation and could be involved in substrate recognition [1].
It has been proposed that the eukaryotic proteins containing an OTU domain could mediate proteolytic events involved in signaling associated with the modification of chromatin structure and control of cell proliferation [1].
Some proteins containing a OTU domain are listed below [1]:
The profile we developed covers the entire OTU domain.
Last update:December 2001 / First entry.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Makarova K.S. Aravind L. Koonin E.V. |
Title | A novel superfamily of predicted cysteine proteases from eukaryotes, viruses and Chlamydia pneumoniae. | |
Source | Trends Biochem. Sci. 25:50-52(2000). | |
PubMed ID | 10664582 |