InterPro: IPR004843 Metallophosphoesterase

Protein phosphorylation plays a central role in the regulation of cell functions [1], causing the activation or inhibition of many enzymes involved in various biochemical pathways [2]. Kinases and phosphatases are the enzymes responsible for this, and may themselves be subject to control through the action of hormones and growth factors [1]. Serine/threonine (S/T) phosphatases catalyse the dephosphorylation of phosphoserine and phosphothreonine residues. In mammalian tissues four different types of PP have been identified and are known as PP1, PP2A, PP2B and PP2C. Except for PP2C, these enzymes are evolutionary related. The catalytic regions of the proteins are well conserved and have a slow mutation rate, suggesting that major changes in these regions are highly detrimental [1].

The metallo-phosphoesterase motif is found in a large number of proteins invoved in phosphoryation. These include serine/threonine phosphatases, DNA polymerase, exonucleases, and other phosphatases.