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  Domain Name: MPP_superfamily
metallophosphatase superfamily, metallophosphatase domain. Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.
No pairwise interactions are available for this conserved domain.

Total Mutations Found: 37
Total Disease Mutations Found: 29
This domain occurred 20 times on human genes (31 proteins).



  NIEMANN-PICK DISEASE, INTERMEDIATE, PROTRACTED NEUROVISCERAL
  NIEMANN-PICK DISEASE, INTERMEDIATE, PROTRACTED NEUROVISCERAL, INCLUDED
  NIEMANN-PICK DISEASE, TYPE A
  NIEMANN-PICK DISEASE, TYPE B
  SPONDYLOENCHONDRODYSPLASIA WITH IMMUNE DYSREGULATION


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Range on the Protein:  

   Protein ID            Protein Position

Domain Position:  


Feature Name:Total Found:
active site
metal binding site

























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Please Cite: Peterson, T.A., Adadey, A., Santana-Cruz ,I., Sun, Y., Winder A, Kann, M.G., (2010) DMDM: Domain Mapping of Disease Mutations. Bioinformatics 26 (19), 2458-2459.

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