CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.2010 | Zincin-like |
|
3.30.2010.10 | Metalloproteases ("zincins"), catalytic domain |
Domain Context
CATH Clusters
| Superfamily | Metalloproteases ("zincins"), catalytic domain |
| Functional Family | CAAX prenyl protease |
Enzyme Information
| 3.4.24.84 |
Ste24 endopeptidase.
based on mapping to UniProt O75844
The peptide bond hydrolyzed can be designated -C-|-A-A-X in which C is an S-isoprenylated cysteine residue, A is usually aliphatic and X is the C-terminal residue of the substrate protein, and may be any of several amino acids.
-!- One of two enzymes that can catalyze this processing step for mating a-factor in Saccharomyces cerevisiae. -!- Subsequently, the S-isoprenylated cysteine residue that forms the new C-terminus is methyl-esterified and forms a hydrophobic membrane- anchor. -!- Belongs to peptidase family M48.
|
UniProtKB Entries (1)
| O75844 |
FACE1_HUMAN
Homo sapiens
CAAX prenyl protease 1 homolog
|
PDB Structure
| PDB | 4AW6 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The Structural Basis of Zmpste24-Dependent Laminopathies.
Science
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