Protein Domain : SWA2-like, ubiquitin-associated domain IPR015228

Type	Domain
Description	Ubiquitin-associated (UBA) domains contain approximately 40 residues and bind ubiquitin non-covalently. They adopt a secondary structure consisting of three α-helices, and have been identified in various modular proteins involved in protein trafficking, clathrin assembly/disassembly, DNA repair, proteasomal degradation, and cell cycle regulation. Proteins containing this domain include Swa2 and other uncharacterised hypothetical proteins from Saccharomyces. Swa2 is the yeast auxilin ortholog that is a multifunctional protein with three N-terminal clathrin-binding (CB) motifs, a ubiquitin-association (UBA) domain, a tetratricopeptide repeat (TPR) domain, and a C-terminal J-domain. It is required for disassembly of clathrin-coated vesicles (CCVs) in an ATP-dependent manner, as well as for cortical endoplasmic reticulum (ER) inheritance [ ]. 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 [].
Short Name	SWA2_UBA