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Conserved domains on  [gi|688578496|ref|XP_009304625|]
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manganese-dependent ADP-ribose/CDP-alcohol diphosphatase isoform X1 [Danio rerio]

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 ...
 6-309 2.83e-112

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: 325.44  E-value: 2.83e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688578496   6 FTFGLIADVQYADIEDGENYLRTRRRYYrGSADLLRDAVLQWRRER-VQCVVQLGDIIDGHNRRrDASDRALDTVMAELD 84
Cdd:cd07396    1 FSFGIIADIQYADIDDGKNLGTRRRYYR-NSLGVLERAVEEWNRESnLAFVVQLGDIIDGYNAK-DRSKEALDAVLSILD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688578496  85 ACSVDVHHVWGNHEFYNFSRPSLLSSRlnsaqrtgtdtgsDLIGDDIYAYEFSPAPNFRFVLLDaydlsvigreeesekh 164
Cdd:cd07396   79 RLKGPVHHVLGNHEFYNFPREYLNHLK-------------TLNGEDAYYYSFSPGPGFRFLVLD---------------- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688578496 165 thswriltqhnhnlqdlnqppvsvgleqrFVKFNGGFSEQQLQWLDAVLTLSDHKQERVLIFSHLPVHPCAADPICLAWN 244
Cdd:cd07396  130 -----------------------------FVKFNGGIGEEQLAWLRNELTSADANGEKVIVLSHLPIYPEAADPQCLLWN 180

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688578496 245 HEAVLSVLRSHQSVLCFIAGHDHDGGRCTDSSGAQHITLEGVIETPPHSHAFATAYLYEDRMVMK 309
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 ...
 6-309 2.83e-112

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: 325.44  E-value: 2.83e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688578496   6 FTFGLIADVQYADIEDGENYLRTRRRYYrGSADLLRDAVLQWRRER-VQCVVQLGDIIDGHNRRrDASDRALDTVMAELD 84
Cdd:cd07396    1 FSFGIIADIQYADIDDGKNLGTRRRYYR-NSLGVLERAVEEWNRESnLAFVVQLGDIIDGYNAK-DRSKEALDAVLSILD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688578496  85 ACSVDVHHVWGNHEFYNFSRPSLLSSRlnsaqrtgtdtgsDLIGDDIYAYEFSPAPNFRFVLLDaydlsvigreeesekh 164
Cdd:cd07396   79 RLKGPVHHVLGNHEFYNFPREYLNHLK-------------TLNGEDAYYYSFSPGPGFRFLVLD---------------- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688578496 165 thswriltqhnhnlqdlnqppvsvgleqrFVKFNGGFSEQQLQWLDAVLTLSDHKQERVLIFSHLPVHPCAADPICLAWN 244
Cdd:cd07396  130 -----------------------------FVKFNGGIGEEQLAWLRNELTSADANGEKVIVLSHLPIYPEAADPQCLLWN 180

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688578496 245 HEAVLSVLRSHQSVLCFIAGHDHDGGRCTDSSGAQHITLEGVIETPPHSHAFATAYLYEDRMVMK 309
Cdd:cd07396  181 YEEVLAILESYPCVKACFSGHNHEGGYEQDSHGVHHVTLEGVLETPPDSQAFGTAYVYEDHMVVR 245
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
6-267 6.36e-12

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 64.33  E-value: 6.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688578496   6 FTFGLIADVQYADIEDGEnylrtrrryyrgSADLLRDAVLQWRRERVQCVVQLGDIIDghnrrrDASDRALDTVMAELDA 85
Cdd:COG1409    1 FRFAHISDLHLGAPDGSD------------TAEVLAAALADINAPRPDFVVVTGDLTD------DGEPEEYAAAREILAR 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688578496  86 CSVDVHHVWGNHEFYNFsRPSLLSSRLNSAQRTGTDtgsdligddiYAYEFspaPNFRFVLLDAydlsvigreeesekht 165
Cdd:COG1409   63 LGVPVYVVPGNHDIRAA-MAEAYREYFGDLPPGGLY----------YSFDY---GGVRFIGLDS---------------- 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688578496 166 hswriltqhnhnlqdlnqppvsvgleQRFVKFNGGFSEQQLQWLDAvlTLSDHKQERVLIFSHLPVHP--CAADPICLaW 243
Cdd:COG1409  113 --------------------------NVPGRSSGELGPEQLAWLEE--ELAAAPAKPVIVFLHHPPYStgSGSDRIGL-R 163

                        250       260
                 ....*....|....*....|....
gi 688578496 244 NHEAVLSVLRSHQSVLCFiAGHDH 267
Cdd:COG1409  164 NAEELLALLARYGVDLVL-SGHVH 186
 
Name Accession Description Interval E-value
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 6-309 2.83e-112

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: 325.44  E-value: 2.83e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688578496   6 FTFGLIADVQYADIEDGENYLRTRRRYYrGSADLLRDAVLQWRRER-VQCVVQLGDIIDGHNRRrDASDRALDTVMAELD 84
Cdd:cd07396    1 FSFGIIADIQYADIDDGKNLGTRRRYYR-NSLGVLERAVEEWNRESnLAFVVQLGDIIDGYNAK-DRSKEALDAVLSILD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688578496  85 ACSVDVHHVWGNHEFYNFSRPSLLSSRlnsaqrtgtdtgsDLIGDDIYAYEFSPAPNFRFVLLDaydlsvigreeesekh 164
Cdd:cd07396   79 RLKGPVHHVLGNHEFYNFPREYLNHLK-------------TLNGEDAYYYSFSPGPGFRFLVLD---------------- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688578496 165 thswriltqhnhnlqdlnqppvsvgleqrFVKFNGGFSEQQLQWLDAVLTLSDHKQERVLIFSHLPVHPCAADPICLAWN 244
Cdd:cd07396  130 -----------------------------FVKFNGGIGEEQLAWLRNELTSADANGEKVIVLSHLPIYPEAADPQCLLWN 180

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 688578496 245 HEAVLSVLRSHQSVLCFIAGHDHDGGRCTDSSGAQHITLEGVIETPPHSHAFATAYLYEDRMVMK 309
Cdd:cd07396  181 YEEVLAILESYPCVKACFSGHNHEGGYEQDSHGVHHVTLEGVLETPPDSQAFGTAYVYEDHMVVR 245
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
6-267 6.36e-12

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 64.33  E-value: 6.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688578496   6 FTFGLIADVQYADIEDGEnylrtrrryyrgSADLLRDAVLQWRRERVQCVVQLGDIIDghnrrrDASDRALDTVMAELDA 85
Cdd:COG1409    1 FRFAHISDLHLGAPDGSD------------TAEVLAAALADINAPRPDFVVVTGDLTD------DGEPEEYAAAREILAR 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688578496  86 CSVDVHHVWGNHEFYNFsRPSLLSSRLNSAQRTGTDtgsdligddiYAYEFspaPNFRFVLLDAydlsvigreeesekht 165
Cdd:COG1409   63 LGVPVYVVPGNHDIRAA-MAEAYREYFGDLPPGGLY----------YSFDY---GGVRFIGLDS---------------- 112

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688578496 166 hswriltqhnhnlqdlnqppvsvgleQRFVKFNGGFSEQQLQWLDAvlTLSDHKQERVLIFSHLPVHP--CAADPICLaW 243
Cdd:COG1409  113 --------------------------NVPGRSSGELGPEQLAWLEE--ELAAAPAKPVIVFLHHPPYStgSGSDRIGL-R 163

                        250       260
                 ....*....|....*....|....
gi 688578496 244 NHEAVLSVLRSHQSVLCFiAGHDH 267
Cdd:COG1409  164 NAEELLALLARYGVDLVL-SGHVH 186
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 199-308 5.81e-07

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: 49.58  E-value: 5.81e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688578496 199 GGFSEQQLQWLDAvlTLSDHKQERVLIFSHLPVHPCA---ADPICLAwNHEAVLSVLRSHQSVLCFIAGHDHdggRCTDS 275
Cdd:cd07402  124 GELSDEQLDWLEA--ALAEAPDRPTLIFLHHPPFPLGipwMDAIRLR-NSQALFAVLARHPQVKAILCGHIH---RPISG 197

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 688578496 276 S--GAQHITLEGV-IETPPHSHAFAT-AYLYEDRMVM 308
Cdd:cd07402  198 SfrGIPFSTAPSTcHQFALDLDDFALdAEAPGPRNLL 234
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 46-105 2.45e-03

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: 37.63  E-value: 2.45e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 688578496  46 QWRRERVQCVVQLGDIIDGHNRRRDASDRALdtvmaELDACSVDVHHVWGNHEFYNFSRP 105
Cdd:cd00838   21 LAKAEKPDLVICLGDLVDYGPDPEEVELKAL-----RLLLAGIPVYVVPGNHDILVTHGP 75
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 191-288 7.86e-03

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: 37.30  E-value: 7.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688578496 191 EQRFVKFNGGFSEQQLQWLDAVLTLSdhKQERVLIFSHLPVHPCAA--DPICLAWNheaVLSVLRSHqSVLCFIAGHDHD 268
Cdd:cd07378  145 GQPRGPPNKKLAETQLAWLEKQLAAS--KADYKIVVGHYPIYSSGEhgPTKCLVDI---LLPLLKKY-KVDAYLSGHDHN 218

                         90       100
                 ....*....|....*....|
gi 688578496 269 ggrctdssgAQHITLEGVIE 288
Cdd:cd07378  219 ---------LQHIVDESGTY 229
 
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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