metallophosphoesterase domain-containing protein 1 isoform X1 [Rattus norvegicus]
metallophosphatase domain-containing protein( domain architecture ID 10164504)
metallophosphatase domain-containing protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc), similar to human metallophosphoesterase MPPED2 that may play a role in the development of the nervous system
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
MPP_239FB | cd07379 | Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein ... |
91-303 | 1.23e-65 | ||||
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. : Pssm-ID: 277325 [Multi-domain] Cd Length: 135 Bit Score: 202.86 E-value: 1.23e-65
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Name | Accession | Description | Interval | E-value | ||||
MPP_239FB | cd07379 | Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein ... |
91-303 | 1.23e-65 | ||||
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. Pssm-ID: 277325 [Multi-domain] Cd Length: 135 Bit Score: 202.86 E-value: 1.23e-65
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COG2129 | COG2129 | Predicted phosphoesterase, related to the Icc protein [General function prediction only]; |
91-303 | 9.75e-36 | ||||
Predicted phosphoesterase, related to the Icc protein [General function prediction only]; Pssm-ID: 441732 [Multi-domain] Cd Length: 211 Bit Score: 128.59 E-value: 9.75e-36
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Metallophos | pfam00149 | Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ... |
91-155 | 5.97e-04 | ||||
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues. Pssm-ID: 459691 [Multi-domain] Cd Length: 114 Bit Score: 39.12 E-value: 5.97e-04
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Name | Accession | Description | Interval | E-value | ||||
MPP_239FB | cd07379 | Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein ... |
91-303 | 1.23e-65 | ||||
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. Pssm-ID: 277325 [Multi-domain] Cd Length: 135 Bit Score: 202.86 E-value: 1.23e-65
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COG2129 | COG2129 | Predicted phosphoesterase, related to the Icc protein [General function prediction only]; |
91-303 | 9.75e-36 | ||||
Predicted phosphoesterase, related to the Icc protein [General function prediction only]; Pssm-ID: 441732 [Multi-domain] Cd Length: 211 Bit Score: 128.59 E-value: 9.75e-36
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CpdA | COG1409 | 3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms]; |
90-305 | 1.45e-11 | ||||
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms]; Pssm-ID: 441019 [Multi-domain] Cd Length: 234 Bit Score: 63.17 E-value: 1.45e-11
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MPP_PAE1087 | cd07392 | Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ... |
95-303 | 3.11e-10 | ||||
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an uncharacterized Pyrobaculum aerophilum protein with a metallophosphatase domain. The domain present in members of this family 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: 277338 [Multi-domain] Cd Length: 190 Bit Score: 58.48 E-value: 3.11e-10
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MPP_superfamily | cd00838 | metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ... |
240-302 | 3.38e-06 | ||||
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: 45.72 E-value: 3.38e-06
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MPP_1 | cd07400 | Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ... |
111-150 | 6.83e-05 | ||||
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the 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: 277345 [Multi-domain] Cd Length: 138 Bit Score: 42.28 E-value: 6.83e-05
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MPP_superfamily | cd00838 | metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ... |
93-154 | 2.17e-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: 40.71 E-value: 2.17e-04
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MPP_DR1119 | cd07393 | Deinococcus radiodurans DR1119 and related proteins, metallophosphatase domain; DR1119 is an ... |
110-286 | 3.15e-04 | ||||
Deinococcus radiodurans DR1119 and related proteins, metallophosphatase domain; DR1119 is an uncharacterized Deinococcus radiodurans protein with a metallophosphatase domain. The domain present in members of this family 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: 277339 [Multi-domain] Cd Length: 238 Bit Score: 41.71 E-value: 3.15e-04
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Metallophos | pfam00149 | Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ... |
91-155 | 5.97e-04 | ||||
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues. Pssm-ID: 459691 [Multi-domain] Cd Length: 114 Bit Score: 39.12 E-value: 5.97e-04
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Blast search parameters | ||||
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