The domain within your query sequence starts at position 78 and ends at position 368; the E-value for the PP2C_SIG domain shown below is 6.09e0.



Sigma factor PP2C-like phosphatases
SMART accession number:SM00331
Description: -
Interpro abstract (IPR001932):

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 catalyses 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 [ (PUBMED:9003755) (PUBMED:9869399) (PUBMED:22115775) (PUBMED:22668558) ].

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 governed 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 catalysing 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-sheet packs against a three-stranded beta-sheet with flanking alpha-helices [ (PUBMED:9003755) (PUBMED:22115775) ].

This entry represents a conserved region found in the N-terminal part that contains a perfectly conserved tripeptide.

GO function:phosphatase activity (GO:0016791)
Family alignment:
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There are 114813 PP2C_SIG domains in 114809 proteins in SMART's nrdb database.

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