CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.418 | Actin-binding Protein, T-fimbrin; domain 1 |
|
1.10.418.20 |
Domain Context
CATH Clusters
| Superfamily | 1.10.418.20 |
| Functional Family | Ubiquitin-like-specific protease 1 |
Enzyme Information
| 3.4.22.68 |
Ulp1 peptidase.
based on mapping to UniProt Q02724
Hydrolysis of the alpha-linked peptide bond in the sequence Gly- Gly-|-Ala-Thr-Tyr at the C-terminal end of the small ubiquitin-like modifier (SUMO) propeptide, Smt3, leading to the mature form of the protein. A second reaction involves the cleavage of an epsilon-linked peptide bond between the C-terminal glycine of the mature SUMO and the lysine epsilon-amino group of the target protein.
-!- The enzyme from Saccharomyces cerevisiae can also recognize small ubiquitin-like modifier 1 (SUMO-1) from human as a substrate in both SUMO-processing (alpha-linked peptide bonds) and SUMO-deconjugation (epsilon-linked peptide bonds) reactions. -!- Ulp1 has several functions, including an essential role in chromosomal segregation and progression of the cell cycle through the G2/M phase of the cell cycle. -!- Belongs to peptidase family C48.
|
UniProtKB Entries (1)
| Q12306 |
SMT3_YEAST
Saccharomyces cerevisiae S288C
Ubiquitin-like protein SMT3
|
PDB Structure
| PDB | 1EUV |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast.
Mol.Cell
|