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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958790624  91 RFVCVSDTHSRTDPIQMPYGDVLIHAGDFTELGLPSEVKKFNEWLGS 137
Cdd:cd07379     1 RFVCISDTHSRHPTISIPDGDVLIHAGDFTEGGTPDEVKKFLDWLKS 47

Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein 239) is thought to play a role in central nervous system development, but its specific role in unknown. 239FB is expressed predominantly in human fetal brain from a gene located in the chromosome 11p13 region associated with the mental retardation component of the WAGR (Wilms tumor, Aniridia, Genitourinary anomalies, Mental retardation) syndrome. Orthologous brp-like (brain protein 239-like) proteins have been identified in the invertebrate amphioxus group and in vertebrates. 239FB belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with 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. The MPP superfamily includes: 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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958790624  91 RFVCVSDTHSRTDPIQMPYGDVLIHAGDFTELGLPSEVKKFNEWLGS 137
Cdd:cd07379     1 RFVCISDTHSRHPTISIPDGDVLIHAGDFTEGGTPDEVKKFLDWLKS 47

Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein 239) is thought to play a role in central nervous system development, but its specific role in unknown. 239FB is expressed predominantly in human fetal brain from a gene located in the chromosome 11p13 region associated with the mental retardation component of the WAGR (Wilms tumor, Aniridia, Genitourinary anomalies, Mental retardation) syndrome. Orthologous brp-like (brain protein 239-like) proteins have been identified in the invertebrate amphioxus group and in vertebrates. 239FB belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with 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. The MPP superfamily includes: 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.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1958790624  91 RFVCVSDTHSRTDPIQMPYGDVLIHAGDFTELGLPSEVKKFNEWLGS 137
Cdd:cd07379     1 RFVCISDTHSRHPTISIPDGDVLIHAGDFTEGGTPDEVKKFLDWLKS 47

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958790624  90 TRFVCVSDTHSRTDPIQMPYG--------------DVLIHAGDFTELGLPSEVKKFNEWL 135
Cdd:COG1409     1 FRFAHISDLHLGAPDGSDTAEvlaaaladinaprpDFVVVTGDLTDDGEPEEYAAAREIL 60