Yeast FCP1 is an essential protein serine phosphatase (EC 22.214.171.124) that
dephosphorylates the C-terminal domain (CTD) of RNA polymerase II. FCP1
orthologs are present in all known eukaryote proteomes. The N-terminal domain
of FCP1 corresponds to the catalytic unit of the phosphatase and has been
refered to as the FCP1 homology domain. The FCP1 homology domain, which is a
~180-residue module, is also found in many other proteins of unknown function.
It contains a DxDx(T/V) motif preceded by four hydrophobic residues
characteristic of a large family of metal-dependent phosphohydrolases and
phosphotransferases. The first aspartate residue is likely to participate
in catalysis, whereas the second could have a role in substrate recognition
The profile we developed covers the entire FCP1 homology domain.
March 2004 / First entry.
PROSITE method (with tools and information) covered by this documentation:
Archambault J., Chambers R.S., Kobor M.S., Ho Y., Cartier M., Bolotin D., Andrews B., Kane C.M., Greenblatt J.
An essential component of a C-terminal domain phosphatase that interacts with transcription factor IIF in Saccharomyces cerevisiae.
Proc. Natl. Acad. Sci. U.S.A. 94:14300-14305(1997).
PROSITE is copyright. It is produced by the SIB Swiss Institute
Bioinformatics. There are no restrictions on its use by non-profit
institutions as long as its content is in no way modified. Usage by and
for commercial entities requires a license agreement. For information
about the licensing scheme send an email to
or see: prosite_license.html.