CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.20 | Up-down Bundle |
|
1.20.1540 | Rhomboid-like fold |
|
1.20.1540.10 | Rhomboid-like |
Domain Context
CATH Clusters
| Superfamily | Rhomboid-like |
| Functional Family | Rhomboid protease GlpG |
Enzyme Information
| 3.4.21.105 |
Rhomboid protease.
based on mapping to UniProt P09391
Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different transmembrane domains.
-!- These endopeptidases are multi-spanning membrane proteins. -!- Their catalytic site is embedded within the membrane and they cleave type-1 transmembrane domains. -!- Important for embryo development in Drosophila melanogaster. -!- Rhomboid is a key regulator of EGF receptor signaling and is responsible for cleaving Spitz, the main ligand of the Drosophila EGF receptor pathway. -!- Parasite-encoded rhomboid enzymes are also important for invasion of host cells by Toxoplasma and the malaria parasite. -!- Belongs to peptidase family S54.
|
UniProtKB Entries (1)
| P09391 |
GLPG_ECOLI
Escherichia coli K-12
Rhomboid protease GlpG
|
PDB Structure
| PDB | 3UBB |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Conformational Change in Rhomboid Protease GlpG Induced by Inhibitor Binding to Its S' Subsites.
Biochemistry
|