CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.40 | Herpes Virus-1 |
|
3.30.40.10 | Zinc/RING finger domain, C3HC4 (zinc finger) |
Domain Context
CATH Clusters
| Superfamily | Zinc/RING finger domain, C3HC4 (zinc finger) |
| Functional Family | Ubiquitin carboxyl-terminal hydrolase 8 |
Enzyme Information
| 3.4.19.12 |
Ubiquitinyl hydrolase 1.
based on mapping to UniProt N1P0J5
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
-!- Links to polypeptides smaller than 60 residues are hydrolyzed more readily than those to larger polypeptides. -!- Isoforms exist with quantitatively different specificities among the best known being UCH-L1 and UCH-L3, major proteins of the brain of mammals. -!- Inhibited by ubiquitin aldehyde (in which Gly76 is replaced by aminoacetaldehyde). -!- Belongs to peptidase family C12.
|
UniProtKB Entries (2)
| N1NXA6 |
N1NXA6_YEASC
Saccharomyces cerevisiae CEN.PK113-7D
SAGA-associated factor 11
|
| P53165 |
SGF73_YEAST
Saccharomyces cerevisiae S288C
SAGA-associated factor 73
|
PDB Structure
| PDB | 4W4U |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Uncovering the role of Sgf73 in maintaining SAGA deubiquitinating module structure and activity.
J.Mol.Biol.
|
