|PROSITE documentation PDOC00792 [for PROSITE entry PS01032]|
Protein phosphatases remove phosphate groups from various proteins that are the key components of a number of signalling pathways in eukaryotes and prokaryotes. Protein phosphatases that dephosphorylate Ser and Thr residues are classified into the phosphoprotein (PPP) and the protein phosphatase Mg(2+)- or Mn(2+)-dependent (PPM) families. The core structure of PPMs is the 300-residue PPM-type phosphatase domain that catalyzes the dephosphorylation of phosphoserine- and phosphothreonine-containing protein. The PPM-type phosphatase domain is found as a module in diverse structural contexts and is modulated by targeting and regulatory subunits [1,2,3,4].
Some proteins known to contain a PPM-type phosphatase domain are listed below:
The PP2C-type phosphatase domain consists of 10 segments of β-strands and 5 segments of α-helix and comprises a pair of detached subdomains. The first is a small β-sandwich with strand β1 packed against strands β2 and β3; the second is a larger β-sandwich in which a four-stranded β-heet packs against a three-stranded β-sheet with flanking α-helices (see <PDB:3T9Q>) [1,3].
As a signature pattern, we selected the best conserved region which is located in the N-terminal part and contains a perfectly conserved tripeptide. This region includes a conserved aspartate residue involved in divalent cation binding . We also developed a profile that covers the entire PPM-type phosphatase domain.Last update:
February 2015 / Text revised; profile added.
PROSITE methods (with tools and information) covered by this documentation:
|1||Authors||Das A.K. Helps N.R. Cohen P.T.W. Barford D.|
|Title||Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution.|
|Source||EMBO J. 15:6798-6809(1996).|
|Title||Protein phosphatase 2C (PP2C) function in higher plants.|
|Source||Plant Mol. Biol. 38:919-927(1998).|
|3||Authors||Levdikov V.M. Blagova E.V. Rawlings A.E. Jameson K. Tunaley J. Hart D.J. Barak I. Wilkinson A.J.|
|Title||Structure of the phosphatase domain of the cell fate determinant SpoIIE from Bacillus subtilis.|
|Source||J. Mol. Biol. 415:343-358(2012).|
|4||Authors||Mori Y. Takegawa K. Kimura Y.|
|Title||Function analysis of conserved amino acid residues in a Mn(2+)-dependent protein phosphatase, Pph3, from Myxococcus xanthus.|
|Source||J. Biochem. 152:269-274(2012).|