The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:
"PAC-like subunit
".
The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:
"This PAC2 (Proteasome assembly chaperone) family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 247 and 307 amino acids in length. These proteins function as a chaperone for the 26S proteasome. The 26S proteasome mediates ubiquitin-dependent proteolysis in eukaryotic cells. A number of studies including very recent ones have revealed that assembly of its 20S catalytic core particle is an ordered process that involves several conserved proteasome assembly chaperones (PACs). Two heterodimeric chaperones, PAC1-PAC2 and PAC3-PAC4, promote the assembly of rings composed of seven alpha subunits.
Structures | |
---|---|
Domains: | 26 |
Domain clusters (>95% seq id): | 9 |
Domain clusters (>35% seq id): | 7 |
Unique PDBs: | 9 |
Alignments | |
Structural Clusters (5A): | 1 |
Structural Clusters (9A): | 1 |
FunFam Clusters: | 33 |
Function | |
Unique EC: | |
Unique GO: | 10 |
Taxonomy | |
Unique Species: | 3716 |