| Type: | Domain | Name: | Ulp1 protease family, C-terminal catalytic domain |
| Description: | This entry represents the C-terminal part of ubiquitin-like proteases that displays full proteolytic activity [].Deubiquitinating enzymes (DUB) form a large family of cysteine protease that can deconjugate ubiquitin or ubiquitin-like proteins from ubiquitin-conjugatedproteins. They can be classified in 3 families according to sequence homology [, ]: ubiquitin carboxyl-terminal hydrolases (UCH),ubiquitin-specific processing proteases (UBP), and ubiquitin-like proteases (ULP) () specific for deconjugating ubiquitin-like proteins. In contrast to the UBP pathway, which is veryredundant (16 UBP enzymes in yeast), there is few ubiquitin-like protease (only one in yeast, ULP1).ULP1 catalyses two critical functions in the SUMO/Smt3 pathway via its cysteine protease activity. ULP1 processes the Smt3 C-terminal sequence(-GGATY) to its mature form (-GG), and it deconjugates Smt3 from the lysine epsilon-amino group of the target protein [].Crystal structure of yeast ULP1 bound to Smt3 [] revealed that the catalyticand interaction interface is situated in a shallow and narrow cleft where conserved residues recognise the Gly-Gly motif at the C-terminal extremity ofSmt3 protein. Ulp1 adopts a novel architecture despite some structural similarity with other cysteine protease. The secondary structure is composedof seven alpha helices and seven beta strands. The catalytic domain includes the central alpha helix, beta-strands 4 to 6, and the catalytic triad(Cys-His-Asp). | Short Name: | Peptidase_C48_C |
