{PDOC51676}
{PS51676; FF}
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* FF domain domain profile *
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The FF  domain  is  a  60  amino  acid  residue  phosphopeptide-binding module
containing two  conserved  phenylalanine  (FF)  residues that give name to the
domain. While  protein-interaction  modules are commonly found in functionally
unrelated proteins,  FF domains are primarily present in only three eukaryotic
protein families:

 - the splicing factors FBP11 and Prp40,
 - the transcription factor CA150,
 - p190 RhoGTPase-related proteins.

FF domains are found singly or in multiple copies but the number of FF domains
in protein sequences ranges, in general, between two and six [1,2,3,4,5,6].

The FF  domain  is  composed  of three alpha-helices arranged in an orthogonal
bundle with  a  3(10)  helix  in  the  loop between the second and third alpha
helices (see  <PDB:1H40>). The two highly conserved phenylalanine residues are
in the  middle  of  the  first  and  third alpha helices, and form part of the
hydrophobic core of the protein [3,4,5,6.].

The profile we developed covers the entire FF domain.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: June 2013 / First entry.

[ 1] Bedford M.T., Leder P.
     "The FF domain: a novel motif that often accompanies WW domains."
     Trends Biochem. Sci. 24:264-265(1999).
     PubMed=10390614
[ 2] Morris D.P., Greenleaf A.L.
     "The splicing factor, Prp40, binds the phosphorylated
     carboxyl-terminal domain of  RNA polymerase II."
     J. Biol. Chem. 275:39935-39943(2000).
     PubMed=10978320; DOI=10.1074/jbc.M004118200
[ 3] Allen M., Friedler A., Schon O., Bycroft M.
     "The structure of an FF domain from human HYPA/FBP11."
     J. Mol. Biol. 323:411-416(2002).
     PubMed=12381297
[ 4] Gasch A., Wiesner S., Martin-Malpartida P., Ramirez-Espain X.,
     Ruiz L., Macias M.J.
     "The structure of Prp40 FF1 domain and its interaction with the
     crn-TPR1 motif of  Clf1 gives a new insight into the binding mode of
     FF domains."
     J. Biol. Chem. 281:356-364(2006).
     PubMed=16253993; DOI=10.1074/jbc.M508047200
[ 5] Bonet R., Ramirez-Espain X., Macias M.J.
     "Solution structure of the yeast URN1 splicing factor FF domain:
     comparative analysis of charge distributions in FF domain
     structures-FFs and SURPs, two domains with a similar fold."
     Proteins 73:1001-1009(2008).
     PubMed=18536009; DOI=10.1002/prot.22127
[ 6] Bonet R., Ruiz L., Morales B., Macias M.J.
     "Solution structure of the fourth FF domain of yeast Prp40 splicing
     factor."
     Proteins 77:1000-1003(2009).
     PubMed=19722265; DOI=10.1002/prot.22547

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