| Type: | Domain | Name: | Ubiquitin-associated domain, SWA2-type |
| Description: | Ubiquitin-associated (UBA) domains contain approximately 40 residues and bind ubiquitin non-covalently. They adopt a secondary structure consisting of three alpha-helices, and have been identified in various modular proteins involved in protein trafficking, clathrin assembly/disassembly, DNA repair, proteasomal degradation, and cell cycle regulation. The N-terminal region of SWA2, the Saccharomyces cerevisiae orthologue of mammalian auxilin, has a characteristic three-helix UBA fold. However, the third helix in SWA2 UBA contains a bulkier tyrosine in place of smaller residues found in other UBAs, and cannot pack as close to the second helix []. This entry represents an SWA2-type UBA. | Short Name: | SWA2_UBA |
