Function and Biology Details
Reactions catalysed:
Cleavage of peptide bonds with very broad specificity.
Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
- Nucleophile aminohydrolases, N-terminal
- Proteasome, subunit alpha/beta
- Peptidase T1A, proteasome beta-subunit
- Proteasome alpha-subunit, N-terminal domain
- Proteasome component (PCI) domain
- ATPase, AAA-type, core
- Proteasome subunit beta 4
- P-loop containing nucleoside triphosphate hydrolase
53 more domains
Structure analysis Details
Assembly composition:
hetero 47-mer (preferred)
Entry contents:
33 distinct polypeptide molecules
Macromolecules (33 distinct):