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Conserved domains on  [gi|219521899|ref|NP_001137155|]
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metallophosphoesterase MPPED2 isoform a [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 ...
 59-271 1.36e-61

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: 191.30  E-value: 1.36e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521899  59 RFVCISDTHSRTDGIQMPYGDILLHTGDFTELGLPSEVKKFNDWLGNLPYEYKIVIAGNHELTFDkefmadlvkqdyyrf 138
Cdd:cd07379    1 RFVCISDTHSRHPTISIPDGDVLIHAGDFTEGGTPDEVKKFLDWLKSLPHPHKIVIAGNHDLTLD--------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521899 139 psvsklkpedfdnvqslltnsiylqdsevtvkgfriygapwtpwfngwgfnlprgqslldkwnliPEGIDILMTHGPPLG 218
Cdd:cd07379   66 -----------------------------------------------------------------PEGTDILVTHGPPYG 80

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 219521899 219 FRDWVPKElQRVGCVELLNTVQrRIRPKLHVFGGIHEGYGIM----TDGYTTYINAS 271
Cdd:cd07379   81 HLDLGSSG-QRLGCEELLNTVQ-RVRPKLHVFGHIHEGYGIErvpdTDGETTFVNAS 135
 
Name Accession Description Interval E-value
MPP_239FB cd07379
Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein ...
 59-271 1.36e-61

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: 191.30  E-value: 1.36e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521899  59 RFVCISDTHSRTDGIQMPYGDILLHTGDFTELGLPSEVKKFNDWLGNLPYEYKIVIAGNHELTFDkefmadlvkqdyyrf 138
Cdd:cd07379    1 RFVCISDTHSRHPTISIPDGDVLIHAGDFTEGGTPDEVKKFLDWLKSLPHPHKIVIAGNHDLTLD--------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521899 139 psvsklkpedfdnvqslltnsiylqdsevtvkgfriygapwtpwfngwgfnlprgqslldkwnliPEGIDILMTHGPPLG 218
Cdd:cd07379   66 -----------------------------------------------------------------PEGTDILVTHGPPYG 80

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 219521899 219 FRDWVPKElQRVGCVELLNTVQrRIRPKLHVFGGIHEGYGIM----TDGYTTYINAS 271
Cdd:cd07379   81 HLDLGSSG-QRLGCEELLNTVQ-RVRPKLHVFGHIHEGYGIErvpdTDGETTFVNAS 135
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
59-271 1.64e-29

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 111.26  E-value: 1.64e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521899  59 RFVCISDTHSRTD-------GIQMPYGDILLHTGDFTELGLPSEVKKFNDWLGNLPYeYKIVIAGNHEltfDKEFMADLV 131
Cdd:COG2129    1 KILAVSDLHGNFDlleklleLARAEDADLVILAGDLTDFGTAEEAREVLEELAALGV-PVLAVPGNHD---DPEVLDALE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521899 132 KqdyyrfpsvsklkpedfdnvqsllTNSIYLQDSEVTVKGFRIYG---APWTPWfngWGFNLPRGQSLLDKW-NLIPEGI 207
Cdd:COG2129   77 E------------------------SGVHNLHGRVVEIGGLRIAGlggSRPTPF---GTPYEYTEEEIEERLaKLREKDV 129

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 219521899 208 DILMTHGPPLGFRDWVPKELQRVGCVELLNTVqRRIRPKLHVFGGIHEGYGIMTDGYTTYINAS 271
Cdd:COG2129  130 DILLTHAPPYGTTLDRVEDGPHVGSKALRELI-EEFQPKLVLHGHIHESRGVDKIGGTRVVNPG 192
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 59-152 1.55e-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: 40.66  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521899   59 RFVCISDTHSR---------TDGIQMPYG-DILLHTGDFTELGLPSEvkKFNDWLGNL-PYEYKIVIAGNHELTFDKEFM 127
Cdd:pfam00149   2 RILVIGDLHLPgqlddllelLKKLLEEGKpDLVLHAGDLVDRGPPSE--EVLELLERLiKYVPVYLVRGNHDFDYGECLR 79

                          90       100
                  ....*....|....*....|....*
gi 219521899  128 adlvKQDYYRFPSVSKLKPEDFDNV 152
Cdd:pfam00149  80 ----LYPYLGLLARPWKRFLEVFNF 100
 
Name Accession Description Interval E-value
MPP_239FB cd07379
Homo sapiens 239FB and related proteins, metallophosphatase domain; 239FB (Fetal brain protein ...
 59-271 1.36e-61

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: 191.30  E-value: 1.36e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521899  59 RFVCISDTHSRTDGIQMPYGDILLHTGDFTELGLPSEVKKFNDWLGNLPYEYKIVIAGNHELTFDkefmadlvkqdyyrf 138
Cdd:cd07379    1 RFVCISDTHSRHPTISIPDGDVLIHAGDFTEGGTPDEVKKFLDWLKSLPHPHKIVIAGNHDLTLD--------------- 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521899 139 psvsklkpedfdnvqslltnsiylqdsevtvkgfriygapwtpwfngwgfnlprgqslldkwnliPEGIDILMTHGPPLG 218
Cdd:cd07379   66 -----------------------------------------------------------------PEGTDILVTHGPPYG 80

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 219521899 219 FRDWVPKElQRVGCVELLNTVQrRIRPKLHVFGGIHEGYGIM----TDGYTTYINAS 271
Cdd:cd07379   81 HLDLGSSG-QRLGCEELLNTVQ-RVRPKLHVFGHIHEGYGIErvpdTDGETTFVNAS 135
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
59-271 1.64e-29

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 111.26  E-value: 1.64e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521899  59 RFVCISDTHSRTD-------GIQMPYGDILLHTGDFTELGLPSEVKKFNDWLGNLPYeYKIVIAGNHEltfDKEFMADLV 131
Cdd:COG2129    1 KILAVSDLHGNFDlleklleLARAEDADLVILAGDLTDFGTAEEAREVLEELAALGV-PVLAVPGNHD---DPEVLDALE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521899 132 KqdyyrfpsvsklkpedfdnvqsllTNSIYLQDSEVTVKGFRIYG---APWTPWfngWGFNLPRGQSLLDKW-NLIPEGI 207
Cdd:COG2129   77 E------------------------SGVHNLHGRVVEIGGLRIAGlggSRPTPF---GTPYEYTEEEIEERLaKLREKDV 129

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 219521899 208 DILMTHGPPLGFRDWVPKELQRVGCVELLNTVqRRIRPKLHVFGGIHEGYGIMTDGYTTYINAS 271
Cdd:COG2129  130 DILLTHAPPYGTTLDRVEDGPHVGSKALRELI-EEFQPKLVLHGHIHESRGVDKIGGTRVVNPG 192
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
58-273 1.15e-08

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 54.31  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521899  58 TRFVCISDTHSRTDGIQMPYG--------------DILLHTGDFTELGLPSEVKKFNDWLGNLPYEYkIVIAGNHEL--- 120
Cdd:COG1409    1 FRFAHISDLHLGAPDGSDTAEvlaaaladinaprpDFVVVTGDLTDDGEPEEYAAAREILARLGVPV-YVVPGNHDIraa 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521899 121 ---TFDKEFMADLVKQDYYRFpsvsklkpeDFDNVQslltnsIYLQDSEVTVKGFRIYGAPWTPWFngwgfnlprgQSLL 197
Cdd:COG1409   80 maeAYREYFGDLPPGGLYYSF---------DYGGVR------FIGLDSNVPGRSSGELGPEQLAWL----------EEEL 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 219521899 198 DKwnlIPEGIDILMTHGPPLGFRDWVPKELQRvGCVELLNTVQRRiRPKLHVFGGIHEGYGIMTDGYTTYINASTC 273
Cdd:COG1409  135 AA---APAKPVIVFLHHPPYSTGSGSDRIGLR-NAEELLALLARY-GVDLVLSGHVHRYERTRRDGVPYIVAGSTG 205
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 59-152 1.55e-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: 40.66  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521899   59 RFVCISDTHSR---------TDGIQMPYG-DILLHTGDFTELGLPSEvkKFNDWLGNL-PYEYKIVIAGNHELTFDKEFM 127
Cdd:pfam00149   2 RILVIGDLHLPgqlddllelLKKLLEEGKpDLVLHAGDLVDRGPPSE--EVLELLERLiKYVPVYLVRGNHDFDYGECLR 79

                          90       100
                  ....*....|....*....|....*
gi 219521899  128 adlvKQDYYRFPSVSKLKPEDFDNV 152
Cdd:pfam00149  80 ----LYPYLGLLARPWKRFLEVFNF 100
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 79-118 2.05e-04

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: 40.74  E-value: 2.05e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 219521899  79 DILLHTGDFTELGLPSEVKKFNDWLGNLPYEYKIVIAGNH 118
Cdd:cd07400   32 DLVVVTGDLTQRARPAEFEEAREFLDALEPEPVVVVPGNH 71
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 208-268 2.93e-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: 39.94  E-value: 2.93e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219521899 208 DILMTHGPPLGFRDWVPKELQRvgCVELLNTVQRRIRPKLHVFGGIHEGYGIMTDGYTTYI 268
Cdd:cd00838   68 DILVTHGPPYDPLDEGSPGEDP--GSEALLELLDKYGPDLVLSGHTHVPGRREVDKGGTLV 126
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 61-122 6.83e-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: 38.79  E-value: 6.83e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 219521899  61 VCISDTHSRTDG---------IQMPYGDILLHTGDFTELGLPSEVKKFNDWLGNLPYEYKIVIAGNHELTF 122
Cdd:cd00838    1 LVISDIHGNLEAleavleaalAKAEKPDLVICLGDLVDYGPDPEEVELKALRLLLAGIPVYVVPGNHDILV 71
MPP_PAE1087 cd07392
Pyrobaculum aerophilum PAE1087 and related proteins, metallophosphatase domain; PAE1087 is an ...
 194-271 9.60e-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: 39.22  E-value: 9.60e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 219521899 194 QSLLDKWNLIPEGIDILMTHGPPLG-FRDWVPKELQrVGCVELLNTVQRRiRPKLHVFGGIHEGYGIMTDGYTTYINAS 271
Cdd:cd07392  114 YSKLGLLNVKLPGRLILVTHAPPYGtAVDRVSSGVH-VGSKAIRKFIEEF-QPLLCICGHIHESRGIDKIGNTLVVNPG 190
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 60-118 3.79e-03

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 belong 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: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 38.03  E-value: 3.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219521899  60 FVCISDTHSRTDGIQMPYG---------------------DILLHTGDFTELGLPSEVKKFNDWLGNLPYEYkIVIAGNH 118
Cdd:cd07402    1 IAQISDTHLFAPGEGALLGvdtaarlaaavaqvnalhprpDLVVVTGDLSDDGSPESYERLRELLAPLPAPV-YWIPGNH 79
 
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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