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PROSITE documentation PDOC50600 [for PROSITE entry PS50600]

Ubiquitin-like protease family profile





Description

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 <PDOC00127>), ubiquitin-specific processing proteases (UBP) (see <PDOC00750>), 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 α helices and seven β strands. The catalytic domain includes the central α helix, β-strands 4 to 6, and the catalytic triad (Cys-His-Asp) (see <PDB:1EUV>).

We developed a profile directed against the C-terminal part of ULP proteins that displays full proteolytic activity [4].

Note:

These proteins belong to family C48 in the classification of peptidases [E1].

Last update:

May 2008 / Text revised.

Technical section

PROSITE method (with tools and information) covered by this documentation:

ULP_PROTEASE, PS50600; Ubiquitin-like protease family profile  (MATRIX)


References

1AuthorsChung C.H., Baek S.H.
TitleDeubiquitinating enzymes: their diversity and emerging roles.
SourceBiochem. Biophys. Res. Commun. 266:633-640(1999).
PubMed ID10603300
DOI10.1006/bbrc.1999.1880

2AuthorsHochstrasser M.
TitleUbiquitin-dependent protein degradation.
SourceAnnu. Rev. Genet. 30:405-439(1996).
PubMed ID8982460
DOI10.1146/annurev.genet.30.1.405

3AuthorsLi S.J., Hochstrasser M.
TitleA new protease required for cell-cycle progression in yeast.
SourceNature 398:246-251(1999).
PubMed ID10094048
DOI10.1038/18457

4AuthorsMossessova E., Lima C.D.
TitleUlp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast.
SourceMol. Cell 5:865-876(2000).
PubMed ID10882122

E1Sourcehttp://www.uniprot.org/docs/peptidas



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