Domain Architecture
| DUSP domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| solution structure of the dusp domain of husp15 | |||||||||
| Identifiers | |||||||||
| Symbol | DUSP | ||||||||
| Pfam | PF06337 | ||||||||
| InterPro | IPR006615 | ||||||||
| MEROPS | C19 | ||||||||
|
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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. The DUSP domain displays a tripod-like AB3 fold with a three-helix bundle and a three-stranded anti-parallel beta-sheet resembling the legs and seat of the tripod. Conserved residues are predominantly involved in hydrophobic packing interactions within the three alpha-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. The function of the DUSP domain is unknown but it may play a role in protein/protein interaction or substrate recognition.
Read more about this topic: Deubiquitinating Enzyme
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