InterPro domain: IPR004274

Yeast FCP1 is an essential protein serine phosphatase ( 3.1.3.16 ) 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 residuescharacteristic of a large family of metal-dependent phosphohydrolases andphosphotransferases. The first aspartate residue is likely to participatein catalysis, whereas the second could have a role in substrate recognition[ 1 , 2 , 3 , 4 ].

1. 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, 14300-5
2. An unusual eukaryotic protein phosphatase required for transcription by RNA polymerase II and CTD dephosphorylation in S. cerevisiae. Mol. Cell 4, 55-62
3. Defining the active site of Schizosaccharomyces pombe C-terminal domain phosphatase Fcp1. J. Biol. Chem. 278, 13627-32
4. A protein phosphatase functions to recycle RNA polymerase II. Genes Dev. 13, 1540-52