PROSITE documentation PDOC51676FF domain domain profile
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 α-helices arranged in an orthogonal bundle with a 3(10) helix in the loop between the second and third α helices (see <PDB:1H40>). The two highly conserved phenylalanine residues are in the middle of the first and third α helices, and form part of the hydrophobic core of the protein [3,4,5,6.].
The profile we developed covers the entire FF domain.
Last update:June 2013 / First entry.
-------------------------------------------------------------------------------
PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Bedford M.T. Leder P. |
| Title | The FF domain: a novel motif that often accompanies WW domains. | |
| Source | Trends Biochem. Sci. 24:264-265(1999). | |
| PubMed ID | 10390614 |
| 2 | Authors | Morris D.P. Greenleaf A.L. |
| Title | The splicing factor, Prp40, binds the phosphorylated carboxyl-terminal domain of RNA polymerase II. | |
| Source | J. Biol. Chem. 275:39935-39943(2000). | |
| PubMed ID | 10978320 | |
| DOI | 10.1074/jbc.M004118200 |
| 3 | Authors | Allen M. Friedler A. Schon O. Bycroft M. |
| Title | The structure of an FF domain from human HYPA/FBP11. | |
| Source | J. Mol. Biol. 323:411-416(2002). | |
| PubMed ID | 12381297 |
| 4 | Authors | Gasch A. Wiesner S. Martin-Malpartida P. Ramirez-Espain X. Ruiz L. Macias M.J. |
| Title | 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. | |
| Source | J. Biol. Chem. 281:356-364(2006). | |
| PubMed ID | 16253993 | |
| DOI | 10.1074/jbc.M508047200 |
| 5 | Authors | Bonet R. Ramirez-Espain X. Macias M.J. |
| Title | 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. | |
| Source | Proteins 73:1001-1009(2008). | |
| PubMed ID | 18536009 | |
| DOI | 10.1002/prot.22127 |
| 6 | Authors | Bonet R. Ruiz L. Morales B. Macias M.J. |
| Title | Solution structure of the fourth FF domain of yeast Prp40 splicing factor. | |
| Source | Proteins 77:1000-1003(2009). | |
| PubMed ID | 19722265 | |
| DOI | 10.1002/prot.22547 |
PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.
View entry in original PROSITE document format
View entry in raw text format (no links)