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Conserved domains on  [gi|160333181|ref|NP_079786|]
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manganese-dependent ADP-ribose/CDP-alcohol diphosphatase [Mus musculus]

Protein Classification

metallophosphoesterase family protein; bifunctional metallophosphatase/5'-nucleotidase family protein( domain architecture ID 10164683)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)| bifunctional metallophosphatase/5'-nucleotidase contains an N-terminal metallophosphoesterase family domain that contains an active site consisting of two metal ions (usually manganese, iron, or zinc), and a 5'-nucleotidase C-terminal domain; similar to Escherichia coli UshA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 18-322 4.66e-111

Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that 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: 277341 [Multi-domain]  Cd Length: 245  Bit Score: 323.13  E-value: 4.66e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333181  18 FSFGVIADIQYADLEDGYNYQRSRRRYYrHSLIHLQGAIEDWNKESsMPCCVLQLGDIIDGYNAQYkVSEKSLELVMNTF 97
Cdd:cd07396    1 FSFGIIADIQYADIDDGKNLGTRRRYYR-NSLGVLERAVEEWNRES-NLAFVVQLGDIIDGYNAKD-RSKEALDAVLSIL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333181  98 QMLKVPVHHTWGNHEFYNFSRDYLAssklnskfledqiaqHPETTPSENYYAYHFVPFPKFRFILLDsydlsvlgidpss 177
Cdd:cd07396   78 DRLKGPVHHVLGNHEFYNFPREYLN---------------HLKTLNGEDAYYYSFSPGPGFRFLVLD------------- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333181 178 pkyeqcmkmlrehnpnvelnspqglsepqYVQFNGGFSQEQLNWLNEVLTFSDTNQEKVVIVSHLPIYPEASDSVCLAWN 257
Cdd:cd07396  130 -----------------------------FVKFNGGIGEEQLAWLRNELTSADANGEKVIVLSHLPIYPEAADPQCLLWN 180

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160333181 258 YVDALSIIWSHKCVVCFLAGHTHDGGYSEDPFGVHHVNLEGVIETAPDSQAFGTVHVFPDKMLLK 322
Cdd:cd07396  181 YEEVLAILESYPCVKACFSGHNHEGGYEQDSHGVHHVTLEGVLETPPDSQAFGTAYVYEDHMVVR 245
 
Name Accession Description Interval E-value
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 18-322 4.66e-111

Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that 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: 277341 [Multi-domain]  Cd Length: 245  Bit Score: 323.13  E-value: 4.66e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333181  18 FSFGVIADIQYADLEDGYNYQRSRRRYYrHSLIHLQGAIEDWNKESsMPCCVLQLGDIIDGYNAQYkVSEKSLELVMNTF 97
Cdd:cd07396    1 FSFGIIADIQYADIDDGKNLGTRRRYYR-NSLGVLERAVEEWNRES-NLAFVVQLGDIIDGYNAKD-RSKEALDAVLSIL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333181  98 QMLKVPVHHTWGNHEFYNFSRDYLAssklnskfledqiaqHPETTPSENYYAYHFVPFPKFRFILLDsydlsvlgidpss 177
Cdd:cd07396   78 DRLKGPVHHVLGNHEFYNFPREYLN---------------HLKTLNGEDAYYYSFSPGPGFRFLVLD------------- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333181 178 pkyeqcmkmlrehnpnvelnspqglsepqYVQFNGGFSQEQLNWLNEVLTFSDTNQEKVVIVSHLPIYPEASDSVCLAWN 257
Cdd:cd07396  130 -----------------------------FVKFNGGIGEEQLAWLRNELTSADANGEKVIVLSHLPIYPEAADPQCLLWN 180

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160333181 258 YVDALSIIWSHKCVVCFLAGHTHDGGYSEDPFGVHHVNLEGVIETAPDSQAFGTVHVFPDKMLLK 322
Cdd:cd07396  181 YEEVLAILESYPCVKACFSGHNHEGGYEQDSHGVHHVTLEGVLETPPDSQAFGTAYVYEDHMVVR 245
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
18-319 8.11e-12

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 63.94  E-value: 8.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333181  18 FSFGVIADIQYADLEdgynyqrsrrryYRHSLIHLQGAIEDWNKESsmPCCVLQLGDII-DGYNAQYkvsekslELVMNT 96
Cdd:COG1409    1 FRFAHISDLHLGAPD------------GSDTAEVLAAALADINAPR--PDFVVVTGDLTdDGEPEEY-------AAAREI 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333181  97 FQMLKVPVHHTWGNHEFYNFsrdylassklNSKFLEDQIAQHPETTpsenyyAYHFVPFPKFRFILLDSYDlsvlgidps 176
Cdd:COG1409   60 LARLGVPVYVVPGNHDIRAA----------MAEAYREYFGDLPPGG------LYYSFDYGGVRFIGLDSNV--------- 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333181 177 spkyeqcmkmlrehnpnvelnspqglsepqYVQFNGGFSQEQLNWLNEVLtfSDTNQEKVVIVSHLPIYPEAS--DSVCL 254
Cdd:COG1409  115 ------------------------------PGRSSGELGPEQLAWLEEEL--AAAPAKPVIVFLHHPPYSTGSgsDRIGL 162

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160333181 255 aWNYVDALSIIWSHKcVVCFLAGHTHDGGYSEdPFGVHHVNLEGVIETAPDSQAFGTVHVFPDKM 319
Cdd:COG1409  163 -RNAEELLALLARYG-VDLVLSGHVHRYERTR-RDGVPYIVAGSTGGQVRLPPGYRVIEVDGDGL 224
 
Name Accession Description Interval E-value
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 18-322 4.66e-111

Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that 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: 277341 [Multi-domain]  Cd Length: 245  Bit Score: 323.13  E-value: 4.66e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333181  18 FSFGVIADIQYADLEDGYNYQRSRRRYYrHSLIHLQGAIEDWNKESsMPCCVLQLGDIIDGYNAQYkVSEKSLELVMNTF 97
Cdd:cd07396    1 FSFGIIADIQYADIDDGKNLGTRRRYYR-NSLGVLERAVEEWNRES-NLAFVVQLGDIIDGYNAKD-RSKEALDAVLSIL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333181  98 QMLKVPVHHTWGNHEFYNFSRDYLAssklnskfledqiaqHPETTPSENYYAYHFVPFPKFRFILLDsydlsvlgidpss 177
Cdd:cd07396   78 DRLKGPVHHVLGNHEFYNFPREYLN---------------HLKTLNGEDAYYYSFSPGPGFRFLVLD------------- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333181 178 pkyeqcmkmlrehnpnvelnspqglsepqYVQFNGGFSQEQLNWLNEVLTFSDTNQEKVVIVSHLPIYPEASDSVCLAWN 257
Cdd:cd07396  130 -----------------------------FVKFNGGIGEEQLAWLRNELTSADANGEKVIVLSHLPIYPEAADPQCLLWN 180

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160333181 258 YVDALSIIWSHKCVVCFLAGHTHDGGYSEDPFGVHHVNLEGVIETAPDSQAFGTVHVFPDKMLLK 322
Cdd:cd07396  181 YEEVLAILESYPCVKACFSGHNHEGGYEQDSHGVHHVTLEGVLETPPDSQAFGTAYVYEDHMVVR 245
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
18-319 8.11e-12

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 63.94  E-value: 8.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333181  18 FSFGVIADIQYADLEdgynyqrsrrryYRHSLIHLQGAIEDWNKESsmPCCVLQLGDII-DGYNAQYkvsekslELVMNT 96
Cdd:COG1409    1 FRFAHISDLHLGAPD------------GSDTAEVLAAALADINAPR--PDFVVVTGDLTdDGEPEEY-------AAAREI 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333181  97 FQMLKVPVHHTWGNHEFYNFsrdylassklNSKFLEDQIAQHPETTpsenyyAYHFVPFPKFRFILLDSYDlsvlgidps 176
Cdd:COG1409   60 LARLGVPVYVVPGNHDIRAA----------MAEAYREYFGDLPPGG------LYYSFDYGGVRFIGLDSNV--------- 114

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333181 177 spkyeqcmkmlrehnpnvelnspqglsepqYVQFNGGFSQEQLNWLNEVLtfSDTNQEKVVIVSHLPIYPEAS--DSVCL 254
Cdd:COG1409  115 ------------------------------PGRSSGELGPEQLAWLEEEL--AAAPAKPVIVFLHHPPYSTGSgsDRIGL 162

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 160333181 255 aWNYVDALSIIWSHKcVVCFLAGHTHDGGYSEdPFGVHHVNLEGVIETAPDSQAFGTVHVFPDKM 319
Cdd:COG1409  163 -RNAEELLALLARYG-VDLVLSGHVHRYERTR-RDGVPYIVAGSTGGQVRLPPGYRVIEVDGDGL 224
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 100-295 2.87e-05

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: 45.01  E-value: 2.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333181 100 LKVPVHHTWGNHEFY-NFSRDYLASSKLNSKFledqiaqhpETTPseNYYAYHFVPFPKF----RFILLDSYDLSvlgid 174
Cdd:cd07378   73 LQVPWYLVLGNHDHRgNVSAQIAYTQRPNSKR---------WNFP--NYYYDISFKFPSSdvtvAFIMIDTVLLC----- 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333181 175 psspkyeQCMKMLREHNPNVELNspqglsepqyvqfnGGFSQEQLNWLNEVLTFSDtnQEKVVIVSHLPIYPEAS--DSV 252
Cdd:cd07378  137 -------GNTDDEASGQPRGPPN--------------KKLAETQLAWLEKQLAASK--ADYKIVVGHYPIYSSGEhgPTK 193

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 160333181 253 CLAWnyvDALSIIWSHKcVVCFLAGHTHDGGYSEDPFGVHHVN 295
Cdd:cd07378  194 CLVD---ILLPLLKKYK-VDAYLSGHDHNLQHIVDESGTYYVI 232
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 52-280 3.50e-05

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: 44.58  E-value: 3.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333181  52 LQGAIEDWNKESSMPCCVLQLGDIIDGYnaqykvSEKSLELVMNTFQMLKVPVHHTWGNHEFynfsRDYLAssklnsKFL 131
Cdd:cd07402   26 LAAAVAQVNALHPRPDLVVVTGDLSDDG------SPESYERLRELLAPLPAPVYWIPGNHDD----RAAMR------EAL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 160333181 132 EDQiaqhpetTPSENYYAYHFVPFPKFRFILLDSydlsvlgidpsspkyeqcmkmlrehnpnvelnspqglSEPQYVQfn 211
Cdd:cd07402   90 PEP-------PYDDNGPVQYVVDFGGWRLILLDT-------------------------------------SVPGVHH-- 123

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 160333181 212 GGFSQEQLNWLNEVLtfSDTNQEKVVIVSHLPIYPEAS---DSVCLAwNYVDALSIIWSHKCVVCFLAGHTH 280
Cdd:cd07402  124 GELSDEQLDWLEAAL--AEAPDRPTLIFLHHPPFPLGIpwmDAIRLR-NSQALFAVLARHPQVKAILCGHIH 192
MPP_Dcr2 cd07383
Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; ...
 69-116 6.38e-03

Saccharomyces cerevisiae DCR2 phosphatase and related proteins, metallophosphatase domain; DCR2 phosphatase (Dosage-dependent Cell Cycle Regulator 2) functions together with DCR1 (Gid8) in a common pathway to accelerate initiation of DNA replication in Saccharomyces cerevisiae. Genetic analysis suggests that DCR1 functions upstream of DCR2. DCR2 interacts with and dephosphorylates Sic1, an inhibitor of mitotic cyclin/cyclin-dependent kinase complexes, which may serve to trigger the initiation of cell division. DCR2 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: 277329 [Multi-domain]  Cd Length: 202  Bit Score: 37.27  E-value: 6.38e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 160333181  69 VLQLGDIIDGYNAQYKVSEKSLELVMNTFQMLKVPVHHTWGNHEFYNF 116
Cdd:cd07383   46 VVLTGDLITGENTADDNATSYLDKAVSPLVERGIPWAATFGNHDGYDW 93
 
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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