CATH Classification

Domain Context

CATH Clusters

Superfamily Classic Zinc Finger
Functional Family Recombination activating gene 1

Enzyme Information
RING-type E3 ubiquitin transferase.
based on mapping to UniProt P15919
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 -!- RING-type ubiquitin transferases may occur as single-chain enzymes but also in dimeric forms or in multi-subunit assemblies. -!- Formerly EC and EC
Acting on ester bonds.
based on mapping to UniProt P15919

UniProtKB Entries (1)

Mus musculus
V(D)J recombination-activating protein 1

PDB Structure

External Links
Organism Escherichia
Primary Citation
Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster.
Bellon, S.F., Rodgers, K.K., Schatz, D.G., Coleman, J.E., Steitz, T.A.