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 |
Enzyme Information
2.3.2.27 |
RING-type E3 ubiquitin transferase.
based on mapping to UniProt Q96EP0
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)
Q96EP0 |
RNF31_HUMAN
Homo sapiens
E3 ubiquitin-protein ligase RNF31
|
PDB Structure
PDB | 4DBG |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
A non-canonical UBA-UBL interaction forms the linear-ubiquitin-chain assembly complex
Embo Rep.
|