Conserved Site

Proteasome beta-type subunit, conserved site (IPR016050)

Short name: Proteasome_bsu_CS


The proteasome (or macropain) (EC: [PMID: 7682410, PMID: 2643381, PMID: 1317508, PMID: 7697118, PMID: 8882582] is a multicatalytic proteinase complex in eukaryotes and archaea, and in some bacteria, that seems to be involved in an ATP/ubiquitin-dependent nonlysosomal proteolytic pathway. In eukaryotes the proteasome is composed of 28 distinct subunits which form a highly ordered ring-shaped structure (20S ring) of about 700 kDa. Most proteasome subunits can be classified, on the basis on sequence similarities into two groups, alpha (A) and beta (B). These are arranged in four rings of seven proteins, consisting of a ring of alpha subunits, two rings of beta subunits, and a ring of alpha subunits. In eukaryotes, each alpha and each beta ring consists of different proteins. Three of the beta subunits are peptidases in subfamily T1A, and each has a distinctive specificity (trypsin-like, chymotrypsin-like and glutamyl peptidase-like). The peptidases are N-terminal nucleophile hydrolases in which the N-terminal threonine is the nucleophile in the hydrolytic reaction [PMID: 9087403]. In the immunoproteasome, the catalytic components are replaced by three specialist, catalytic beta subunits [PMID: 22341445]. In bacteria and archaea there is only one alpha subunit and one beta subunit, and each ring is a homoseptamer.

This entry represents a conserved sequence region found in the N-terminal region of these proteins.

GO terms

Biological Process

GO:0051603 proteolysis involved in cellular protein catabolic process

Molecular Function

GO:0004175 endopeptidase activity

Cellular Component

GO:0005839 proteasome core complex

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns