CATH Classification

Domain Context

CATH Clusters

Superfamily Zinc/RING finger domain, C3HC4 (zinc finger)
Functional Family E3 ubiquitin-protein ligase AMFR

Enzyme Information

2.3.2.27
RING-type E3 ubiquitin transferase.
based on mapping to UniProt Q9UKV5
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)

Q9UKV5
AMFR_HUMAN
Homo sapiens
E3 ubiquitin-protein ligase AMFR

PDB Structure

PDB 2LXH
External Links
Method SOLUTION NMR
Organism
Primary Citation
Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machine.
Das, R., Liang, Y.H., Mariano, J., Li, J., Huang, T., King, A., Tarasov, S.G., Weissman, A.M., Ji, X., Byrd, R.A.
Embo J.