The domain within your query sequence starts at position 1 and ends at position 65; the E-value for the DUSP domain shown below is 6.5e-17.
XAIDNQPLVTQEPVKATSLTLEGGRLKRTPQLIHGRDYEMVPEPVWRALYHWYGSNLALP RPVIK
DUSP |
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PFAM accession number: | PF06337 |
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Interpro abstract (IPR006615): | Deubiquitinating enzymes (DUB) form a large family of cysteine protease that can deconjugate ubiquitin or ubiquitin-like proteins 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 [ (PUBMED:16298993) ]. 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 [ (PUBMED:16298993) ]. The function of the DUSP domain is unknown but it may play a role in protein/protein interaction or substrate recognition. This domain is associated with ubiquitin carboxyl-terminal hydrolase family 2 ( IPR001394 MEROPS peptidase family C19). They are a family 100 to 200kDa peptides which includes the Ubp1 ubiquitin peptidase from yeast; others include:
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GO function: | thiol-dependent ubiquitin-specific protease activity (GO:0004843) |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry DUSP