CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.80 | Alpha-Beta Horseshoe |
|
3.80.10 | Leucine-rich repeat, LRR (right-handed beta-alpha superhelix) |
|
3.80.10.10 | Ribonuclease Inhibitor |
Domain Context
CATH Clusters
| Superfamily | Ribonuclease Inhibitor |
| Functional Family | E3 ubiquitin-protein ligase SspH2 |
Enzyme Information
| 6.3.2.- |
Acid--amino-acid ligases (peptide synthases).
based on mapping to UniProt P0CE12
|
| 2.3.2.27 |
RING-type E3 ubiquitin transferase.
based on mapping to UniProt P0CE12
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine.
-!- The RING domain of E3 ubiquitin transferase serves as a mediator bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin an the epsilon-amino group of an L-lysine residue of the acceptor protein. -!- The RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin (unlike the HECT domain, EC 2.3.2.26). -!- RING-type ubiquitin transferases may occur as single-chain enzymes but also in dimeric forms or in multi-subunit assemblies. -!- Formerly EC 6.3.2.19 and EC 6.3.2.21.
|
UniProtKB Entries (1)
| P0CE12 |
SSPH2_SALTY
Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
E3 ubiquitin-protein ligase SspH2
|
PDB Structure
| PDB | 3G06 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
A family of Salmonella virulence factors functions as a distinct class of autoregulated E3 ubiquitin ligases.
Proc.Natl.Acad.Sci.USA
|
