CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
1 | Mainly Alpha |
|
1.10 | Orthogonal Bundle |
|
1.10.8 | Helicase, Ruva Protein; domain 3 |
|
1.10.8.10 | DNA helicase RuvA subunit, C-terminal domain |
Domain Context
CATH Clusters
| Superfamily | DNA helicase RuvA subunit, C-terminal domain |
| Functional Family | E3 ubiquitin-protein ligase CBL-B |
Enzyme Information
| 2.3.2.27 |
RING-type E3 ubiquitin transferase.
based on mapping to UniProt P22681
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)
| P22681 |
CBL_HUMAN
Homo sapiens
E3 ubiquitin-protein ligase CBL
|
PDB Structure
| PDB | 2JUJ |
| External Links | |
| Method | SOLUTION NMR |
| Organism | |
| Primary Citation |
Differential Ubiquitin Binding of the UBA Domains from Human c-Cbl and Cbl-b: NMR Structural and Biochemical Insights.
Protein Sci.
|
