v5.1.0.3
Cicer data from the Legume Information System
| Type | Homologous_superfamily |
| Description | Antifungal protein consists of five antiparallel beta strands which are highly twisted creating a beta barrel stabilised by four internal disulphide bridges [ ]. A cationic site adjacent to a hydrophobic stretch on the protein surface may constitute a phospholipid binding site []. This superfamily represents an antifungal protein lysine rich domain, that contributes to the correct folding of the protein, which is necessary for its specific antifungal activity. It has been suggested that this domain might contribute to the cell wall and/or nucleic acids binding activity [ ]. |
| Short Name | Antifungal-protein_dom_sf |