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 | Putative E3 ubiquitin-protein ligase UBR5 |
Enzyme Information
| 2.3.2.26 |
HECT-type E3 ubiquitin transferase.
based on mapping to UniProt O95071
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.
-!- In the first step the enzyme transfers ubiquitin from the E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) to a cysteine residue in its HECT domain (which is located in the C-terminal region), forming a thioester bond. -!- In a subsequent step the enzyme transfers the ubiquitin to an acceptor protein, resulting in the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon- amino group of an L-lysine residue of the acceptor protein. -!- Cf. EC 2.3.2.27 and EC 2.3.2.31.
|
UniProtKB Entries (2)
| P0CH28 |
UBC_BOVIN
Bos taurus
Polyubiquitin-C
|
| O95071 |
UBR5_HUMAN
Homo sapiens
E3 ubiquitin-protein ligase UBR5
|
PDB Structure
| PDB | 2QHO |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Structural basis of ubiquitin recognition by the ubiquitin-associated (UBA) domain of the ubiquitin ligase EDD.
J.Biol.Chem.
|
