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acid phosphatase type V, partial [Thallomys nigricauda]
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
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Name | Accession | Description | Interval | E-value | ||
MPP_superfamily super family | cl13995 | metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ... |
1-73 | 4.35e-35 | ||
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 cd07378: Pssm-ID: 472684 [Multi-domain] Cd Length: 286 Bit Score: 119.74 E-value: 4.35e-35
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Name | Accession | Description | Interval | E-value | ||
MPP_ACP5 | cd07378 | Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ... |
1-73 | 4.35e-35 | ||
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 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: 277324 [Multi-domain] Cd Length: 286 Bit Score: 119.74 E-value: 4.35e-35
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PTZ00422 | PTZ00422 | glideosome-associated protein 50; Provisional |
23-73 | 4.08e-05 | ||
glideosome-associated protein 50; Provisional Pssm-ID: 185607 [Multi-domain] Cd Length: 394 Bit Score: 39.42 E-value: 4.08e-05
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SbcD | COG0420 | DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair]; |
10-73 | 4.12e-04 | ||
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair]; Pssm-ID: 440189 [Multi-domain] Cd Length: 250 Bit Score: 36.43 E-value: 4.12e-04
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Name | Accession | Description | Interval | E-value | ||
MPP_ACP5 | cd07378 | Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ... |
1-73 | 4.35e-35 | ||
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 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: 277324 [Multi-domain] Cd Length: 286 Bit Score: 119.74 E-value: 4.35e-35
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PTZ00422 | PTZ00422 | glideosome-associated protein 50; Provisional |
23-73 | 4.08e-05 | ||
glideosome-associated protein 50; Provisional Pssm-ID: 185607 [Multi-domain] Cd Length: 394 Bit Score: 39.42 E-value: 4.08e-05
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MPP_superfamily | cd00838 | metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ... |
1-72 | 1.62e-04 | ||
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. Pssm-ID: 277317 [Multi-domain] Cd Length: 130 Bit Score: 36.86 E-value: 1.62e-04
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SbcD | COG0420 | DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair]; |
10-73 | 4.12e-04 | ||
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair]; Pssm-ID: 440189 [Multi-domain] Cd Length: 250 Bit Score: 36.43 E-value: 4.12e-04
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CpdA | COG1409 | 3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms]; |
7-71 | 4.20e-04 | ||
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms]; Pssm-ID: 441019 [Multi-domain] Cd Length: 234 Bit Score: 36.59 E-value: 4.20e-04
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Blast search parameters | ||||
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