The domain within your query sequence starts at position 480 and ends at position 556; the E-value for the DUSP domain shown below is 4e-39.

PAGAEPYEFVSLEWLQKWLDESTPTKPIDNNACLCSHDKLHPDKISIMKRISEYAANIFY
SRYGGGPRLTVKALCKD

The domain was found using the schnipsel database

DUSP

Domain in ubiquitin-specific proteases.

• SMART accession number: SM00695
• Description: -
• 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:

  • Mammalian ubiquitin carboxyl-terminal hydrolase 4 (USP4),
  • Mammalian ubiquitin carboxyl-terminal hydrolase 11 (USP11),
  • Mammalian ubiquitin carboxyl-terminal hydrolase 15 (USP15),
  • Mammalian ubiquitin carboxyl-terminal hydrolase 20 (USP20),
  • Mammalian ubiquitin carboxyl-terminal hydrolase 32 (USP32),
  • Vertebrate ubiquitin carboxyl-terminal hydrolase 33 (USP33),
  • Vertebrate ubiquitin carboxyl-terminal hydrolase 48 (USP48).
• GO function: thiol-dependent ubiquitin-specific protease activity (GO:0004843)

There are 5789 DUSP domains in 4820 proteins in SMART's nrdb database.

Cellular role (predicted cellular role)

Cellular role: signalling

Metabolism (metabolic pathways involving proteins which contain this domain)

% proteins involved	KEGG pathway ID	Description
100.00	map00680	Methane metabolism

This information is based on mapping of SMART genomic protein database to KEGG orthologous groups. Percentage points are related to the number of proteins with DUSP domain which could be assigned to a KEGG orthologous group, and not all proteins containing DUSP domain. Please note that proteins can be included in multiple pathways, ie. the numbers above will not always add up to 100%.

Structure (3D structures containing this domain)

3D Structures of DUSP domains in PDB

PDB code	Title
1w6v	Solution structure of the DUSP domain of hUSP15
3jyu	Crystal structure of the N-terminal domains of the ubiquitin specific peptidase 4 (USP4)
3lmn	Oligomeric structure of the DUSP domain of human USP15
3ppa	Structure of the Dusp-Ubl domains of Usp15
3pv1	Crystal structure of the USP15 DUSP-UBL domains
3t9l	Structure of N-terminal DUSP-UBL domains of human USP15
4a3o	Crystal structure of the USP15 DUSP-UBL monomer
4a3p	Structure of USP15 DUSP-UBL deletion mutant
4mel	Crystal Structure of the human USP11 DUSP-UBL domains
4mem	Crystal Structure of the rat USP11 DUSP-UBL domains
5ctr	5CTR
5jjw	5JJW

Links (links to other resources describing this domain)

• INTERPRO: IPR006615