CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.40 | Herpes Virus-1 |
|
3.30.40.10 | Zinc/RING finger domain, C3HC4 (zinc finger) |
Domain Context
CATH Clusters
| Superfamily | Zinc/RING finger domain, C3HC4 (zinc finger) |
| Functional Family | E3 ubiquitin/ISG15 ligase TRIM25 |
Enzyme Information
| 6.3.2.n3 |
ISG15--protein ligase.
based on mapping to UniProt Q14258
ATP + [ISG15] + [protein]-lysine = AMP + diphosphate + [protein]-N- ISGyllysine.
-!- The enzyme from human also functions as EC 2.3.2.27.
|
| 2.3.2.27 |
RING-type E3 ubiquitin transferase.
based on mapping to UniProt Q14258
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)
| P0CG47 |
UBB_HUMAN
Homo sapiens
Polyubiquitin-B
|
PDB Structure
| PDB | 5EYA |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Mechanism of TRIM25 Catalytic Activation in the Antiviral RIG-I Pathway.
Cell Rep
|
