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-protein ligase SIAH2 |
Enzyme Information
2.3.2.27 |
RING-type E3 ubiquitin transferase.
based on mapping to UniProt P61092
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.
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UniProtKB Entries (1)
P61092 |
SIA1A_MOUSE
Mus musculus
E3 ubiquitin-protein ligase SIAH1A
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PDB Structure
PDB | 1K2F |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | Escherichia |
Primary Citation |
Siah ubiquitin ligase is structurally related to TRAF and modulates TNF-alpha signaling.
Nat.Struct.Biol.
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