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 |
Enzyme Information
| 3.4.21.105 |
Rhomboid protease.
based on mapping to UniProt P44783
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)
| P44783 |
GLPG_HAEIN
Haemophilus influenzae Rd KW20
Rhomboid protease GlpG
|
PDB Structure
| PDB | 2NR9 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
The crystal structure of the rhomboid peptidase from Haemophilus influenzae provides insight into intramembrane proteolysis.
Proc.Natl.Acad.Sci.USA
|
