This entry represents the adenylyl cyclase-associated protein 2 (CAP2) from vertebrates []. It shares around 64% amino acid identity with CAP1, which regulates the actin cytoskeleton, cofilin function, and cell adhesion []. Like CAP1, CAP2 contains a C-terminal actin-binding domain that may regulate actin remodelling in response to cellular signals and is required for normal cellular morphology, cell division, growth and locomotion in eukaryotes []. However, the function of CAP2 is still not clear.
This entry represents a domain found in the E2/UBC superfamily of proteins found in several bacteria. The active site residues are similar to the eukaryotic E2 proteins but lack the conserved asparagine [, ]. Members of this family are usually fused to an E1 domain at the C terminus. The protein is usually in the gene neighbourhoodof a gene encoding a member of the pol-beta nucleotidyltransferase superfamily []. Many of the operons in this family are in ICE-like mobile elements and plasmids [].Proteins containing this domain include CD-NTase-associated protein 2 (Cap2) from Escherichia coli. Cap2 is associated with CD-NTase protein, which synthesizes cyclic nucleotides in response to infection; these serve as specific second messenger signals [].
