<p> Cyclase-associated proteins (CAPs) are highly conserved monomeric actin-binding proteins present in a wide range of organisms including yeast, fly, plants, and mammals. CAPs are multifunctional proteins that contain several structural domains. CAP is involved in species-specific signalling pathways [<cite idref="PUB00042568"/>, <cite idref="PUB00042569"/>, <cite idref="PUB00042570"/>, <cite idref="PUB00007159"/>]. Only yeast CAPs are involved in adenylate cyclase activation. The C-terminal domain of CAP proteins is responsible for G-actin-binding that regulates actin remodelling in response to cellular signals and is required for normal cellular morphology, cell division, growth and locomotion in eukaryotes.</p><p>In <taxon tax_id="562">Escherichia coli</taxon>, three Min proteins (MinC, MinD and MinE) negatively regulate FtsZ assembly at the cell poles in order to ensure the Z-ring only assembles at cell midpoint. MinC inhibits formation of the Z-ring by preventing FtsZ assembly. MinD binds to MinC near the cell poles, sequestering MinC away from the cell midpoint so the Z-ring can form there. MinC is an oligomer, probably a dimer, that consists of two domains: the N-terminal domain is responsible for FtsZ inhibition, while the C-terminal domain is responsible for binding to MinD and to a component of the division septum [<cite idref="PUB00008426"/>, <cite idref="PUB00042573"/>].</p><p>This entry represents a structural domain found at the C-terminal of CAP proteins as well as MinC. This domain has a superhelical structure, where the superhelix turns are made of either two (CAP) or three (MinC) beta-strands each.</p> Cyclase-associated protein CAP/septum formation inhibitor MinC, C-terminal