|PROSITE documentation PDOC51283 [for PROSITE entry PS51283]|
Deubiquitinating enzymes (DUB) form a large family of cysteine protease that can deconjugate ubiquitin or ubiquitin-like proteins (see <PDOC00271>) from ubiquitin-conjugated proteins. All DUBs contain a catalytic domain surrounded by one or more subdomains, some of which contribute to target recognition. The ~120-residue DUSP (domain present in ubiquitin-specific proteases) domain is one of these specific subdomains. Single or tandem DUSP domains are located both N- and C-terminal to the ubiquitin carboxyl-terminal hydrolase catalytic core domain (see <PDOC00750>) .
The DUSP domain displays a tripod-like AB3 fold with a three-helix bundle and a three-stranded anti-parallel β-sheet ressembling the legs and seat of the tripod (see <PDB:1W6V>). Conserved residues are predominantly involved in hydrophobic packing interactions within the three α-helices. The most conserved DUSP residues, forming the PGPI motif, are flanked by two long loops that vary both in length and sequence. The PGPI motif packs against the three-helix bundle and is highly ordered .
Some proteins known to contain a DUSP domain are listed below:
The profile we developed covers the entire DUSP domain.Last update:
December 2006 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||de Jong R.N. AB E. Diercks T. Truffault V. Daniels M. Kaptein R. Folkers G.E.|
|Title||Solution structure of the human ubiquitin-specific protease 15 DUSP domain.|
|Source||J. Biol. Chem. 281:5026-5031(2006).|