{PDOC00792}
{PS01032; PPM_1}
{PS51746; PPM_2}
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* PPM-type phosphatase domain signature and profile *
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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:

 - Bacillus  subtilis  stage  II  sporulation protein E (SpoIIE), controls the
   sporulation by  dephosphorylating  an  anti-transcription  factor  SpoIIAA,
   reversing the  actions  of  the SpoIIAB protein kinase in a process that is
   gouverned by the ADP/ATP ratio [levdikov].
 - Mycobacterium tuberculosis PP2C-family Ser/Thr phosphatase (PstP).
 - Eucaryotic  PP2C,  a negative regulator of protein kinase cascades that are
   activated as a result of stress.
 - Yeast  adenyl  cyclase,  plays  essential  roles  in regulation of cellular
   metabolism by catalyzing the synthesis of a second messenger, cAMP.
 - Mammalian mitochondrial pyruvate dehydrogenase phosphatase 1 (PDP1).
 - Plant kinase-associated protein phosphatase (KAPP), regulates receptor-like
   kinase (RLK) signalling pathways.
 - Plant absissic acid-insenstive 1 and 2 (ABI1 and ABI2), play a key absissic
   acid (ABA) signal transduction.

The PP2C-type phosphatase domain consists of 10 segments of beta-strands and 5
segments of alpha-helix and comprises a pair of detached subdomains. The first
is a  small  beta-sandwich  with strand beta1 packed against strands beta2 and
beta3; the  second  is  a  larger beta-sandwich in which a four-stranded beta-
heet packs  against  a  three-stranded  beta-sheet with flanking alpha-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 [1].  We  also  developed  a  profile  that covers the entire PPM-type
phosphatase domain.

-Consensus pattern: [LIVMFY]-[LIVMFYA]-[GSAC]-[LIVM]-[FYC]-D-G-H-[GAV]
                    [The D is a manganese ligand]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: February 2015 / Text revised; profile added.

[ 1] Das A.K., Helps N.R., Cohen P.T.W., Barford D.
     "Crystal structure of the protein serine/threonine phosphatase 2C at
     2.0 A resolution."
     EMBO J. 15:6798-6809(1996).
     PubMed=9003755
[ 2] Rodriguez P.L.
     "Protein phosphatase 2C (PP2C) function in higher plants."
     Plant Mol. Biol. 38:919-927(1998).
     PubMed=9869399
[ 3] Levdikov V.M., Blagova E.V., Rawlings A.E., Jameson K., Tunaley J.,
     Hart D.J., Barak I., Wilkinson A.J.
     "Structure of the phosphatase domain of the cell fate determinant
     SpoIIE from Bacillus subtilis."
     J. Mol. Biol. 415:343-358(2012).
     PubMed=22115775; DOI=10.1016/j.jmb.2011.11.017
[ 4] Mori Y., Takegawa K., Kimura Y.
     "Function analysis of conserved amino acid residues in a
     Mn(2+)-dependent protein  phosphatase, Pph3, from Myxococcus
     xanthus."
     J. Biochem. 152:269-274(2012).
     PubMed=22668558; DOI=10.1093/jb/mvs067

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