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CATH Superfamily 2.60.40.2360

Intracellular proteinase inhibitor BsuPI

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:

"
Intracellular proteinase inhibitor BsuPI
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.

Superfamily: Intracellular proteinase inhibitor BsuPI

Structural domains comprising this superfamily share the structure of the Intracellular protease inhibitor protein (IPI), which has been named BsuPI in Bacillus subtilis and has been reported to be an inhibitor of the intracellular subtilisin Isp1 from the same organism. The structure of proteins in this family adopt a beta barrel topology and constitut a variant of the all-beta, immunoglobulin (Ig) fold. It is likely that IPI is important for protein-protein interactions, of which inhibition of Isp1 is one PMID:24555072.

GO Diversity

Unique GO annotations
0 Unique GO terms

EC Diversity

Unique EC annotations
0 Unique EC terms

Species Diversity

Unique species annotations
617 Unique species

Sequence/Structure Diversity

Overview of the sequence / structure diversity of this superfamily compared to other superfamilies in CATH. Click on the chart to view the data in more detail.

Superfamily Summary

A general summary of information for this superfamily.
Structures
Domains: 1
Domain clusters (>95% seq id): 1
Domain clusters (>35% seq id): 1
Unique PDBs: 1
Alignments
Structural Clusters (5A): 1
Structural Clusters (9A): 1
FunFam Clusters: 0
Function
Unique EC:
Unique GO:
Taxonomy
Unique Species: 617