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Conserved domains on  [gi|1252414580|ref|NP_001343484|]
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metallophosphoesterase MPPED2 isoform b [Mus musculus]

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 ...
 72-145 2.91e-32

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: 111.95  E-value: 2.91e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1252414580  72 DKWnLIPEGIDILMTHGPPLGFRDWVPKElQRVGCVELLNTVQRrIRPKLHVFGGIHEGYGIM----TDGYTTYINAS 145
Cdd:cd07379    61 DLT-LDPEGTDILVTHGPPYGHLDLGSSG-QRLGCEELLNTVQR-VRPKLHVFGHIHEGYGIErvpdTDGETTFVNAS 135
 
Name Accession Description Interval E-value
MPP_239FB cd07379
Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein ...
 72-145 2.91e-32

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: 111.95  E-value: 2.91e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1252414580  72 DKWnLIPEGIDILMTHGPPLGFRDWVPKElQRVGCVELLNTVQRrIRPKLHVFGGIHEGYGIM----TDGYTTYINAS 145
Cdd:cd07379    61 DLT-LDPEGTDILVTHGPPYGHLDLGSSG-QRLGCEELLNTVQR-VRPKLHVFGHIHEGYGIErvpdTDGETTFVNAS 135
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
22-145 1.11e-19

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 81.60  E-value: 1.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414580  22 DFDNVQSLL--TNSIYLQDSEVTVKGFRIYG---APWTPWfngWGFNLPRGQSLLDKW-NLIPEGIDILMTHGPPLGFRD 95
Cdd:COG2129    67 DDPEVLDALeeSGVHNLHGRVVEIGGLRIAGlggSRPTPF---GTPYEYTEEEIEERLaKLREKDVDILLTHAPPYGTTL 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1252414580  96 WVPKELQRVGCVELLNTVqRRIRPKLHVFGGIHEGYGIMTDGYTTYINAS 145
Cdd:COG2129   144 DRVEDGPHVGSKALRELI-EEFQPKLVLHGHIHESRGVDKIGGTRVVNPG 192
 
Name Accession Description Interval E-value
MPP_239FB cd07379
Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein ...
 72-145 2.91e-32

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: 111.95  E-value: 2.91e-32
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1252414580  72 DKWnLIPEGIDILMTHGPPLGFRDWVPKElQRVGCVELLNTVQRrIRPKLHVFGGIHEGYGIM----TDGYTTYINAS 145
Cdd:cd07379    61 DLT-LDPEGTDILVTHGPPYGHLDLGSSG-QRLGCEELLNTVQR-VRPKLHVFGHIHEGYGIErvpdTDGETTFVNAS 135
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
22-145 1.11e-19

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 81.60  E-value: 1.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1252414580  22 DFDNVQSLL--TNSIYLQDSEVTVKGFRIYG---APWTPWfngWGFNLPRGQSLLDKW-NLIPEGIDILMTHGPPLGFRD 95
Cdd:COG2129    67 DDPEVLDALeeSGVHNLHGRVVEIGGLRIAGlggSRPTPF---GTPYEYTEEEIEERLaKLREKDVDILLTHAPPYGTTL 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1252414580  96 WVPKELQRVGCVELLNTVqRRIRPKLHVFGGIHEGYGIMTDGYTTYINAS 145
Cdd:COG2129   144 DRVEDGPHVGSKALRELI-EEFQPKLVLHGHIHESRGVDKIGGTRVVNPG 192
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 82-142 2.61e-05

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: 41.87  E-value: 2.61e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1252414580  82 DILMTHGPPLGFRDWVPKELQRvgCVELLNTVQRRIRPKLHVFGGIHEGYGIMTDGYTTYI 142
Cdd:cd00838    68 DILVTHGPPYDPLDEGSPGEDP--GSEALLELLDKYGPDLVLSGHTHVPGRREVDKGGTLV 126
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 68-145 1.33e-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: 40.37  E-value: 1.33e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1252414580  68 QSLLDKWNLIPEGIDILMTHGPPLG-FRDWVPKELQrVGCVELLNTVQRRiRPKLHVFGGIHEGYGIMTDGYTTYINAS 145
Cdd:cd07392   114 YSKLGLLNVKLPGRLILVTHAPPYGtAVDRVSSGVH-VGSKAIRKFIEEF-QPLLCICGHIHESRGIDKIGNTLVVNPG 190
 
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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