InterPro domain: IPR042460

This superfamily represents a domain is found in DCN1-like proteins. Proteins of the DCN family may contribute to neddylation of cullin components of SCF-type E3 ubiquitin ligase complexes, which are multi-protein complexes required for polyubiquitination and subsequent degradation of target proteins by the 26S proteasome [ 1 , 2 ].

The structure of this domain is composed entirely of alpha helices [ 3 , 4 ]. It has been referred to as potentiating neddylation domain (PONY) and can be found in association with an N-terminal UBA domain. The PONY domain contains a cullin-binding surface within its C-terminal region and is sufficient to promote neddylation [ 5 , 5 ].

1. The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae. Nature 435, 1257-61
2. SCCRO (DCUN1D1) is an essential component of the E3 complex for neddylation. J. Biol. Chem. 283, 33211-20
3. Structural basis for the function of DCN-1 in protein Neddylation. J. Biol. Chem. 282, 24490-4
4. Dcn1 functions as a scaffold-type E3 ligase for cullin neddylation. Mol. Cell 29, 23-35
5. Structural Conservation of Distinctive N-terminal Acetylation-Dependent Interactions across a Family of Mammalian NEDD8 Ligation Enzymes. Structure 21, 42-53