|PROSITE documentation PDOC51394 [for PROSITE entry PS51394]|
The PFU (for PLAA family ubiquitin binding domain) is an ubiquitin binding domain with no homology to several known ubiquitin binding domains (e.g., UIM, NZF, UBA, UEV, UBP, or CUE domains). The PFU domain appears to be unique to the PLAA family of proteins. A single member of this family of proteins exists in every eukaryotic species examined. Each of these homologues possesses identical domain structure: an N-terminal domain containing seven WD40 repeats (see <PDOC00574>), a central PFU domain, and a C-terminal PUL domain, which directly binds to Cdc48, a member of the AAA-ATPase family of molecular chaperone . In addition to ubiquitin, the PFU domain of DOA1 has been shown to bind to the SH3 domain (see <PDOC50002>) .
Secondary structure predictions of the PFU domain suggest the presence of an extensive length of β-sheet, N-terminal to an α-helical region .
Some proteins known to contain a PFU domain are listed below:
The profile we developed covers the entire PFU domain.Last update:
July 2008 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Mullally J.E. Chernova T. Wilkinson K.D.|
|Title||Doa1 is a Cdc48 adapter that possesses a novel ubiquitin binding domain.|
|Source||Mol. Cell. Biol. 26:822-830(2006).|
|2||Authors||Ren J. Pashkova N. Winistorfer S. Piper R.C.|
|Title||DOA1/UFD3 plays a role in sorting ubiquitinated membrane proteins into multivesicular bodies.|
|Source||J. Biol. Chem. 0:0-0(2008).|