v5.1.0.3
Cicer data from the Legume Information System
| Type | Domain |
| Description | F-box proteins have a bipartite structure: they contain a carboxy-terminal domain that interacts with substrates and a 42-48 amino-acid F-box domain which binds to the protein Skp1. A subset of F-box proteins ischaracterized by a ~180-residue carboxy-terminal region, which has been called the F-box-associated (FBA) domain [, ]. A FBA domain has also been identifiedin the catfish, tilapia, and zebrafish nonspecific cytotoxic cell receptor proteins (NCCRP-1), which do not contain the F-box domain. NCCRP-1 mayfunction as an antigen recognition molecule and, as such, may participate in innate immunity in teleosts [, ]. The FBA domain is likely to be aglycoprotein-binding module [ , ]. This entry represents the FBA domain, which is an ellipsoid composed of a ten-stranded antiparallel beta- sandwich with two α-helices []. |
| Short Name | F-box-assoc_dom |