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Conserved domains on  [gi|966985828|ref|XP_014970004|]
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metallophosphoesterase MPPED2 isoform X2 [Macaca mulatta]

Protein Classification

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

CATH:  3.60.21.10
EC:  3.1.-.-
Gene Ontology:  GO:0042578|GO:0046872|GO:0016311
PubMed:  8003970|25837850

Graphical summary

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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 ...
 1-197 4.07e-53

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: 167.04  E-value: 4.07e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966985828   1 MPYGDILLHTGDFTELGLPSEVKKFNDWLGNLPYEYKIVIAGNHELTFDkefmadlvkqdyyrfpsvsklkpedfdnvqs 80
Cdd:cd07379   17 IPDGDVLIHAGDFTEGGTPDEVKKFLDWLKSLPHPHKIVIAGNHDLTLD------------------------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966985828  81 lltnsiylqdsevtvkgfriygapwtpwfngwgfnlprgqslldkwnliPEGIDILMTHGPPLGFRDWVPKElQRVGCVE 160
Cdd:cd07379   66 -------------------------------------------------PEGTDILVTHGPPYGHLDLGSSG-QRLGCEE 95

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 966985828 161 LLNTVQRrVRPKLHVFGGIHEGYGIM----TDGYTTYINAS 197
Cdd:cd07379   96 LLNTVQR-VRPKLHVFGHIHEGYGIErvpdTDGETTFVNAS 135
 
Name Accession Description Interval E-value
MPP_239FB cd07379
Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein ...
 1-197 4.07e-53

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: 167.04  E-value: 4.07e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966985828   1 MPYGDILLHTGDFTELGLPSEVKKFNDWLGNLPYEYKIVIAGNHELTFDkefmadlvkqdyyrfpsvsklkpedfdnvqs 80
Cdd:cd07379   17 IPDGDVLIHAGDFTEGGTPDEVKKFLDWLKSLPHPHKIVIAGNHDLTLD------------------------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966985828  81 lltnsiylqdsevtvkgfriygapwtpwfngwgfnlprgqslldkwnliPEGIDILMTHGPPLGFRDWVPKElQRVGCVE 160
Cdd:cd07379   66 -------------------------------------------------PEGTDILVTHGPPYGHLDLGSSG-QRLGCEE 95

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 966985828 161 LLNTVQRrVRPKLHVFGGIHEGYGIM----TDGYTTYINAS 197
Cdd:cd07379   96 LLNTVQR-VRPKLHVFGHIHEGYGIErvpdTDGETTFVNAS 135
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
5-197 9.27e-27

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 102.02  E-value: 9.27e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966985828   5 DILLHTGDFTELGLPSEVKKFNDWLGNLPYeYKIVIAGNHEltfDKEFMADLVKqdyyrfpsvsklkpedfdnvqsllTN 84
Cdd:COG2129   28 DLVILAGDLTDFGTAEEAREVLEELAALGV-PVLAVPGNHD---DPEVLDALEE------------------------SG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966985828  85 SIYLQDSEVTVKGFRIYG---APWTPWfngWGFNLPRGQSLLDKW-NLIPEGIDILMTHGPPLGFRDWVPKELQRVGCVE 160
Cdd:COG2129   80 VHNLHGRVVEIGGLRIAGlggSRPTPF---GTPYEYTEEEIEERLaKLREKDVDILLTHAPPYGTTLDRVEDGPHVGSKA 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 966985828 161 LLNTVqRRVRPKLHVFGGIHEGYGIMTDGYTTYINAS 197
Cdd:COG2129  157 LRELI-EEFQPKLVLHGHIHESRGVDKIGGTRVVNPG 192
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 5-78 2.73e-03

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: 36.42  E-value: 2.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966985828    5 DILLHTGDFTELGLPSEvkKFNDWLGNL-PYEYKIVIAGNHELTFDKEFMadlvKQDYYRFPSVSKLKPEDFDNV 78
Cdd:pfam00149  32 DLVLHAGDLVDRGPPSE--EVLELLERLiKYVPVYLVRGNHDFDYGECLR----LYPYLGLLARPWKRFLEVFNF 100
 
Name Accession Description Interval E-value
MPP_239FB cd07379
Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein ...
 1-197 4.07e-53

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: 167.04  E-value: 4.07e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966985828   1 MPYGDILLHTGDFTELGLPSEVKKFNDWLGNLPYEYKIVIAGNHELTFDkefmadlvkqdyyrfpsvsklkpedfdnvqs 80
Cdd:cd07379   17 IPDGDVLIHAGDFTEGGTPDEVKKFLDWLKSLPHPHKIVIAGNHDLTLD------------------------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966985828  81 lltnsiylqdsevtvkgfriygapwtpwfngwgfnlprgqslldkwnliPEGIDILMTHGPPLGFRDWVPKElQRVGCVE 160
Cdd:cd07379   66 -------------------------------------------------PEGTDILVTHGPPYGHLDLGSSG-QRLGCEE 95

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 966985828 161 LLNTVQRrVRPKLHVFGGIHEGYGIM----TDGYTTYINAS 197
Cdd:cd07379   96 LLNTVQR-VRPKLHVFGHIHEGYGIErvpdTDGETTFVNAS 135
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
5-197 9.27e-27

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 102.02  E-value: 9.27e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966985828   5 DILLHTGDFTELGLPSEVKKFNDWLGNLPYeYKIVIAGNHEltfDKEFMADLVKqdyyrfpsvsklkpedfdnvqsllTN 84
Cdd:COG2129   28 DLVILAGDLTDFGTAEEAREVLEELAALGV-PVLAVPGNHD---DPEVLDALEE------------------------SG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966985828  85 SIYLQDSEVTVKGFRIYG---APWTPWfngWGFNLPRGQSLLDKW-NLIPEGIDILMTHGPPLGFRDWVPKELQRVGCVE 160
Cdd:COG2129   80 VHNLHGRVVEIGGLRIAGlggSRPTPF---GTPYEYTEEEIEERLaKLREKDVDILLTHAPPYGTTLDRVEDGPHVGSKA 156

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 966985828 161 LLNTVqRRVRPKLHVFGGIHEGYGIMTDGYTTYINAS 197
Cdd:COG2129  157 LRELI-EEFQPKLVLHGHIHESRGVDKIGGTRVVNPG 192
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
5-199 1.62e-07

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 50.07  E-value: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966985828   5 DILLHTGDFTELGLPSEVKKFNDWLGNLPYEYkIVIAGNHEL------TFDKEFMADLVKQDYYRFpsvsklkpeDFDNV 78
Cdd:COG1409   36 DFVVVTGDLTDDGEPEEYAAAREILARLGVPV-YVVPGNHDIraamaeAYREYFGDLPPGGLYYSF---------DYGGV 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966985828  79 QSLLTNSIylqdsevtvkgfriygapWTPWFNGWgfnLPRGQ-----SLLDKwnlIPEGIDILMTHGPPLGFRDWVPKEL 153
Cdd:COG1409  106 RFIGLDSN------------------VPGRSSGE---LGPEQlawleEELAA---APAKPVIVFLHHPPYSTGSGSDRIG 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 966985828 154 QRvGCVELLNTVQRRvRPKLHVFGGIHEGYGIMTDGYTTYINASTC 199
Cdd:COG1409  162 LR-NAEELLALLARY-GVDLVLSGHVHRYERTRRDGVPYIVAGSTG 205
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 5-44 6.23e-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: 41.51  E-value: 6.23e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 966985828   5 DILLHTGDFTELGLPSEVKKFNDWLGNLPYEYKIVIAGNH 44
Cdd:cd07400   32 DLVVVTGDLTQRARPAEFEEAREFLDALEPEPVVVVPGNH 71
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 134-194 1.10e-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: 1.10e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966985828 134 DILMTHGPPLGFRDWVPKELQRvgCVELLNTVQRRVRPKLHVFGGIHEGYGIMTDGYTTYI 194
Cdd:cd00838   68 DILVTHGPPYDPLDEGSPGEDP--GSEALLELLDKYGPDLVLSGHTHVPGRREVDKGGTLV 126
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 120-197 3.41e-04

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: 39.99  E-value: 3.41e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 966985828 120 QSLLDKWNLIPEGIDILMTHGPPLG-FRDWVPKELQrVGCvELLNTVQRRVRPKLHVFGGIHEGYGIMTDGYTTYINAS 197
Cdd:cd07392  114 YSKLGLLNVKLPGRLILVTHAPPYGtAVDRVSSGVH-VGS-KAIRKFIEEFQPLLCICGHIHESRGIDKIGNTLVVNPG 190
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 5-78 2.73e-03

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: 36.42  E-value: 2.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 966985828    5 DILLHTGDFTELGLPSEvkKFNDWLGNL-PYEYKIVIAGNHELTFDKEFMadlvKQDYYRFPSVSKLKPEDFDNV 78
Cdd:pfam00149  32 DLVLHAGDLVDRGPPSE--EVLELLERLiKYVPVYLVRGNHDFDYGECLR----LYPYLGLLARPWKRFLEVFNF 100
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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