v5.1.0.3
Cicer data from the Legume Information System
| Type | Homologous_superfamily |
| Description | Bypass of forespore C (BofC) is a monomer made up of two domains, an N-terminal and a C-terminal domain. The N-terminal domain of BofC is composed of a four-stranded β-sheet covered by an α-helix. The β-sheet has a beta2-beta1-beta4-beta3 topology, where strands beta1 and beta2 and strands beta3 and beta4 are connected by β-turns, whereas strands beta2 and beta3 are joined by an α-helix that runs across one face of the β-sheet. This domain is similar to the third immunoglobulin G-binding domain of protein G from Streptococcus, the latter belonging to a large and diverse group of cell surface-associated proteins that bind to immunoglobulins. It has been hypothesised that this domain may be a mediator of protein-protein interactions involved in proteolytic events at the cell surface [ ]. |
| Short Name | BOFC_N_sf |