CPDc

catalytic domain of ctd-like phosphatases
CPDc
SMART accession number:SM00577
Description: -
Interpro abstract (IPR004274):

Yeast FCP1 is an essential protein serine phosphatase (EC 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 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 [(PUBMED:9405607), (PUBMED:10445027), (PUBMED:12556522), (PUBMED:10385623)].

Family alignment:
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There are 13391 CPDc domains in 13352 proteins in SMART's nrdb database.

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