PP2C_SIGSigma factor PP2C-like phosphatases
|SMART accession number:||SM00331|
|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 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 [(PUBMED:9003755), (PUBMED:9869399), (PUBMED:22115775), (PUBMED:22668558)].
Some proteins known to contain a PPM-type phosphatase domain are listed below:
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 [(PUBMED:9003755), (PUBMED:22115775)].
This entry represents a conserved region found in the N-terminal part that contains a perfectly conserved tripeptide.
|GO function:||catalytic activity (GO:0003824)|
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- Evolution (species in which this domain is found)
- Metabolism (metabolic pathways involving proteins which contain this domain)
- Structure (3D structures containing this domain)
- Links (links to other resources describing this domain)