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 (see
<PDOC50181>) which binds to the protein Skp1. A subset of F-box proteins is
characterized by a ~180-residue carboxy-terminal region, which has been called
the F-box-associated (FBA) domain [1,2]. A FBA domain has also been identified
in the catfish, tilapia, and zebrafish nonspecific cytotoxic cell receptor
proteins (NCCRP-1), which do not contain the F-box domain. NCCRP-1 may
function as an antigen recognition molecule and, as such, may participate in
innate immunity in teleosts [2,3]. The FBA domain is likely to be a
glycoprotein-binding module [4,5].
The FBA domain is an ellipsoid composed of a ten-stranded antiparallel β-sandwich with two α-helices (see <PDB:1UMH>) .
Some proteins known to contain a FBA domain are listed below:
Mammalian F-box only protein 2.
Mammalian F-box only protein 6.
Mammalian F-box only protein 17.
Mammalian F-box only protein 27.
Mammalian F-box only protein 44.
Caenorhabditis elegans hypothetical protein C14B1.3.
The profile we developed covers the entire FBA domain.
July 2005 / First entry.
PROSITE method (with tools and information) covered by this documentation:
Winston J.T. Koepp D.M. Zhu C. Elledge S.J. Harper J.W.
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and
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(CC BY-NC-ND 4.0) License, see prosite_license.html.