CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.25 | Alpha Horseshoe |
|
1.25.40 | Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat |
|
1.25.40.560 |
Domain Context
CATH Clusters
| Superfamily | 1.25.40.560 |
| Functional Family | ubiquitin thioesterase ZRANB1 isoform X1 |
Enzyme Information
| 3.4.19.12 |
Ubiquitinyl hydrolase 1.
based on mapping to UniProt Q9UGI0
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 (1)
| Q9UGI0 |
ZRAN1_HUMAN
Homo sapiens
Ubiquitin thioesterase ZRANB1
|
PDB Structure
| PDB | 3ZRH |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
An Ankyrin-Repeat Ubiquitin-Binding Domain Determines Trabid'S Specificity for Atypical Ubiquitin Chains.
Nat.Struct.Mol.Biol.
|