{PDOC50600} {PS50600; ULP_PROTEASE} {BEGIN} ****************************************** * Ubiquitin-like protease family profile * ****************************************** Deubiquitinating enzymes (DUB) form a large family of cysteine protease that can deconjugate ubiquitin or ubiquitin-like proteins from ubiquitin-conjugated proteins. They can be classified in 3 families according to sequence homology [1,2]: ubiquitin carboxyl-terminal hydrolases (UCH) (see ), ubiquitin-specific processing proteases (UBP) (see ), and ubiquitin-like proteases (ULP) (EC 3.4.22.68) specific for deconjugating ubiquitin-like proteins. In contrast to the UBP pathway, which is very redundant (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 [3]. Crystal structure of yeast ULP1 bound to Smt3 [4] revealed that the catalytic and interaction interface is situated in a shallow and narrow cleft where conserved residues recognize the Gly-Gly motif at the C-terminal extremity of Smt3 protein. Ulp1 adopts a novel architecture despite some structural similarity with other cysteine protease. The secondary structure is composed of 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) (see ). We developed a profile directed against the C-terminal part of ULP proteins that displays full proteolytic activity [4]. -Sequences known to belong to this class detected by the profile: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Note: These proteins belong to family C48 in the classification of peptidases [E1]. -Last update: May 2008 / Text revised. [ 1] Chung C.H., Baek S.H. "Deubiquitinating enzymes: their diversity and emerging roles." Biochem. Biophys. Res. Commun. 266:633-640(1999). PubMed=10603300; DOI=10.1006/bbrc.1999.1880 [ 2] Hochstrasser M. "Ubiquitin-dependent protein degradation." Annu. Rev. Genet. 30:405-439(1996). PubMed=8982460; DOI=10.1146/annurev.genet.30.1.405 [ 3] Li S.J., Hochstrasser M. "A new protease required for cell-cycle progression in yeast." Nature 398:246-251(1999). PubMed=10094048; DOI=10.1038/18457 [ 4] Mossessova E., Lima C.D. "Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast." Mol. Cell 5:865-876(2000). PubMed=10882122 [E1] https://www.uniprot.org/docs/peptidas -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}