1 Contains
| DB identifier | Type | Name |
|---|---|---|
| IPR000222 | Binding_site | PPM-type phosphatase, divalent cation binding |
| Type: | Domain | Name: | PPM-type phosphatase domain |
| Description: | Protein phosphatases remove phosphate groups from various proteins that are the key components of a number of signalling pathways in eukaryotes andprokaryotes. Protein phosphatases that dephosphorylate Ser and Thr residues are classified into the phosphoprotein (PPP) and the protein phosphataseMg(2+)- or Mn(2+)-dependent (PPM) families. The core structure of PPMs is the 300-residue PPM-type phosphatase domain that catalyzes the dephosphorylationof phosphoserine- and phosphothreonine-containing protein. The PPM-type phosphatase domain is found as a module in diverse structural contexts and ismodulated by targeting and regulatory subunits [, , , ].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 andbeta3; 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 [, ].This entry represents a conserved region found in the N-terminal part that contains a perfectly conserved tripeptide. | Short Name: | PPM-type_phosphatase_dom |
| DB identifier | Type | Name |
|---|---|---|
| IPR000222 | Binding_site | PPM-type phosphatase, divalent cation binding |
