serine/threonine-protein phosphatase CPPED1 isoform X3 [Mus musculus]
Protein Classification
metallophosphoesterase family protein( domain architecture ID 46112)
metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| MPP_superfamily super family | cl13995 | metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ... |
53-120 | 6.50e-39 | ||
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. The actual alignment was detected with superfamily member cd07395: Pssm-ID: 472684 [Multi-domain] Cd Length: 263 Bit Score: 133.21 E-value: 6.50e-39
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| MPP_CSTP1 | cd07395 | Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ... |
53-120 | 6.50e-39 | ||
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete S-transactivated protein 1) is an uncharacterized Homo sapiens protein with a metallophosphatase domain, that is transactivated by the complete S protein of hepatitis B virus. CSTP1 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. Pssm-ID: 277340 [Multi-domain] Cd Length: 263 Bit Score: 133.21 E-value: 6.50e-39
|
||||||
| Name | Accession | Description | Interval | E-value | ||
| MPP_CSTP1 | cd07395 | Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete ... |
53-120 | 6.50e-39 | ||
Homo sapiens CSTP1 and related proteins, metallophosphatase domain; CSTP1 (complete S-transactivated protein 1) is an uncharacterized Homo sapiens protein with a metallophosphatase domain, that is transactivated by the complete S protein of hepatitis B virus. CSTP1 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. Pssm-ID: 277340 [Multi-domain] Cd Length: 263 Bit Score: 133.21 E-value: 6.50e-39
|
||||||
| Blast search parameters | ||||
|
