v5.1.0.3
Cicer data from the Legume Information System
| Type | Conserved_site |
| Description | This entry represents a conserved site in the C-terminal of the CAP protein. Structurally, CAP is a protein of 474 to 551 residues, which consist of two domains separated by a proline-rich hinge. In budding and fission yeasts the CAP protein is a bifunctional protein whose N-terminal domain binds to adenylyl cyclase, thereby enabling that enzyme to be activated by upstream regulatory signals, such as Ras. The N terminus also catalyses cofilin-mediated severing of actin filaments [ ]. The C-terminal domain plays a role in in recycling cofilin-bound, ADP-actin monomers []. |
| Short Name | CAP_CS_C |