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Conserved domains on  [gi|20129007|ref|NP_572662|]
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uncharacterized protein Dmel_CG1637, isoform C [Drosophila melanogaster]

Protein Classification

purple acid phosphatase family protein( domain architecture ID 11244682)

purple acid phosphatase (PAP) family protein contains an active site consisting of two metal ions (usually manganese, iron, or zinc), similar to PAP, a binuclear metallohydrolase that catalyzes the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters, and anhydrides

CATH:  3.60.21.10
EC:  3.1.3.-
Gene Ontology:  GO:0042578|GO:0046872|GO:0016311
PubMed:  25837850|8683579

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 139-440 3.40e-122

purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs 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: 277318 [Multi-domain]  Cd Length: 296  Bit Score: 357.38  E-value: 3.40e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007 139 WSPSLAIFGDMG---NENAQSMGRLQQDTERgmYDAIIHVGDFAYDMDTSNAAVGDAFMRQIESVAAYVPYMVCPGNHEE 215
Cdd:cd00839   3 TPLKFAVFGDMGqntNNSTNTLDHLEKELGN--YDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007 216 KYNFSNYRARFNMP---------GETDSLWYSFNLGPVHFVSFSTEVYYFLSYgfkLLTKQFEWLERDLAEAnlpeNRAK 286
Cdd:cd00839  81 DYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLAKV----DRSR 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007 287 RPWIITYGHRPMYCSDDKEYDCnsqletyirqGLPMLKWFGLEDLFYKHGVDVEIFAHEHFYTRLWPIYDYKVYNGSaEA 366
Cdd:cd00839 154 TPWIIVMGHRPMYCSNDDDADC----------IEGEKMREALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVANSK-DN 222

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129007 367 PYTNPKAPIQIITGSAGCKEEREP-FSNDLPIWNAYHSNDYGYTRLKAHNGTHLHFEQVSdDQNGAIVDSFWVIK 440
Cdd:cd00839 223 IYTNPKGPVHIVIGAAGNDEGLDDaFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVR-NQDGQVADSFWIVK 296
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 38-132 3.64e-21

Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple acid phosphatase proteins.


:

Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 87.47  E-value: 3.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007    38 PEQVHLSFGDNLRDIVVTWSTRSSPNASVVKFSRNYlKDEPIMVNGTWQRFVDGGKkaRTQYIHNVELKDLEPDTRYEYS 117
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSWVTPSAVTSPVVQYGTSS-SALTSTATATSSTYTTGDG--GTGYIHRATLTGLEPGTTYYYR 77

                          90
                  ....*....|....*.
gi 20129007   118 CGSP-LGWSAVFNFKT 132
Cdd:pfam16656  78 VGDDnGGWSEVYSFTT 93
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 139-440 3.40e-122

purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs 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: 277318 [Multi-domain]  Cd Length: 296  Bit Score: 357.38  E-value: 3.40e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007 139 WSPSLAIFGDMG---NENAQSMGRLQQDTERgmYDAIIHVGDFAYDMDTSNAAVGDAFMRQIESVAAYVPYMVCPGNHEE 215
Cdd:cd00839   3 TPLKFAVFGDMGqntNNSTNTLDHLEKELGN--YDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007 216 KYNFSNYRARFNMP---------GETDSLWYSFNLGPVHFVSFSTEVYYFLSYgfkLLTKQFEWLERDLAEAnlpeNRAK 286
Cdd:cd00839  81 DYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLAKV----DRSR 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007 287 RPWIITYGHRPMYCSDDKEYDCnsqletyirqGLPMLKWFGLEDLFYKHGVDVEIFAHEHFYTRLWPIYDYKVYNGSaEA 366
Cdd:cd00839 154 TPWIIVMGHRPMYCSNDDDADC----------IEGEKMREALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVANSK-DN 222

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129007 367 PYTNPKAPIQIITGSAGCKEEREP-FSNDLPIWNAYHSNDYGYTRLKAHNGTHLHFEQVSdDQNGAIVDSFWVIK 440
Cdd:cd00839 223 IYTNPKGPVHIVIGAAGNDEGLDDaFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVR-NQDGQVADSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 20-438 3.10e-38

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 143.67  E-value: 3.10e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007   20 PGIRSTPI---DQDVDIVHyqPEQVHLSF--GDNLRdivVTWSTRSSPNASVVKFSrnylkdepimVNGTWQRFVDGGKK 94
Cdd:PLN02533  25 PGTRKNLVihpDNEDDPTH--PDQVHISLvgPDKMR---ISWITQDSIPPSVVYGT----------VSGKYEGSANGTSS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007   95 A-------RTQYIHNVELKDLEPDTRYEYSCGSPLGwSAVFNFKTPPAgeKWSPSLAIFGDMGnENAQSMGRLQQdTERG 167
Cdd:PLN02533  90 SyhylliyRSGQINDVVIGPLKPNTVYYYKCGGPSS-TQEFSFRTPPS--KFPIKFAVSGDLG-TSEWTKSTLEH-VSKW 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007  168 MYDAIIHVGDFAYDmdTSNAAVGDAFMRQIESVAAYVPYMVCPGNHE-EK------YNFSNYRARFNMP----GETDSLW 236
Cdd:PLN02533 165 DYDVFILPGDLSYA--NFYQPLWDTFGRLVQPLASQRPWMVTHGNHElEKipilhpEKFTAYNARWRMPfeesGSTSNLY 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007  237 YSFNLGPVHFVSFStevyyflSYG-FKLLTKQFEWLERDLAEAnlpeNRAKRPWIITYGHRPMYCSDDKEydcnsQLEty 315
Cdd:PLN02533 243 YSFNVYGVHIIMLG-------SYTdFEPGSEQYQWLENNLKKI----DRKTTPWVVAVVHAPWYNSNEAH-----QGE-- 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007  316 iRQGLPMLKwfGLEDLFYKHGVDVEIFAHEHFYTRLWPIYDYKvyngsaeapyTNPKAPIQIITGSAGCKEE-REPFSND 394
Cdd:PLN02533 305 -KESVGMKE--SMETLLYKARVDLVFAGHVHAYERFDRVYQGK----------TDKCGPVYITIGDGGNREGlATKYIDP 371

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 20129007  395 LPIWNAYHSNDYGYTRLKAHNGTHLHFE-QVSDDQNGAIVDSFWV 438
Cdd:PLN02533 372 KPDISLFREASFGHGQLNVVDANTMEWTwHRNDDDQSVASDSVWL 416
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
145-353 9.78e-23

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 96.30  E-value: 9.78e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007 145 IFGDMGNENAQSMGRLQQDTERGMYDAIIHVGDFAYDMDTSNAAVGDAFMRQIEsvaayVPYMVCPGNHEEKYNFS-NYR 223
Cdd:COG1409  11 LGAPDGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG-----VPVYVVPGNHDIRAAMAeAYR 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007 224 ARFNMPGeTDSLWYSFNLGPVHFVSFSTEVYYFlSYGFkLLTKQFEWLERDLAEanlpenrAKRPWIITYGHRPMycsdd 303
Cdd:COG1409  86 EYFGDLP-PGGLYYSFDYGGVRFIGLDSNVPGR-SSGE-LGPEQLAWLEEELAA-------APAKPVIVFLHHPP----- 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 20129007 304 keYDCNSQLETYIRQGlpmlkWFGLEDLFYKHGVDVEIFAHEHFYTRLWP 353
Cdd:COG1409 151 --YSTGSGSDRIGLRN-----AEELLALLARYGVDLVLSGHVHRYERTRR 193
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 38-132 3.64e-21

Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple acid phosphatase proteins.


Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 87.47  E-value: 3.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007    38 PEQVHLSFGDNLRDIVVTWSTRSSPNASVVKFSRNYlKDEPIMVNGTWQRFVDGGKkaRTQYIHNVELKDLEPDTRYEYS 117
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSWVTPSAVTSPVVQYGTSS-SALTSTATATSSTYTTGDG--GTGYIHRATLTGLEPGTTYYYR 77

                          90
                  ....*....|....*.
gi 20129007   118 CGSP-LGWSAVFNFKT 132
Cdd:pfam16656  78 VGDDnGGWSEVYSFTT 93
Metallophos_C pfam14008
Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of ...
 373-435 1.11e-18

Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of Purple acid phosphatase proteins.


Pssm-ID: 464064 [Multi-domain]  Cd Length: 60  Bit Score: 79.49  E-value: 1.11e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20129007   373 APIQIITGSAGCKEErePFSNDLPIWNAYHSNDYGYTRLKAHNGTHLHFEQVSDDqNGAIVDS 435
Cdd:pfam14008   1 APVHIVIGAAGNIEG--LFVPPQPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSD-DGTVLDS 60
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 139-440 3.40e-122

purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs 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: 277318 [Multi-domain]  Cd Length: 296  Bit Score: 357.38  E-value: 3.40e-122
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007 139 WSPSLAIFGDMG---NENAQSMGRLQQDTERgmYDAIIHVGDFAYDMDTSNAAVGDAFMRQIESVAAYVPYMVCPGNHEE 215
Cdd:cd00839   3 TPLKFAVFGDMGqntNNSTNTLDHLEKELGN--YDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007 216 KYNFSNYRARFNMP---------GETDSLWYSFNLGPVHFVSFSTEVYYFLSYgfkLLTKQFEWLERDLAEAnlpeNRAK 286
Cdd:cd00839  81 DYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLAKV----DRSR 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007 287 RPWIITYGHRPMYCSDDKEYDCnsqletyirqGLPMLKWFGLEDLFYKHGVDVEIFAHEHFYTRLWPIYDYKVYNGSaEA 366
Cdd:cd00839 154 TPWIIVMGHRPMYCSNDDDADC----------IEGEKMREALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVANSK-DN 222

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20129007 367 PYTNPKAPIQIITGSAGCKEEREP-FSNDLPIWNAYHSNDYGYTRLKAHNGTHLHFEQVSdDQNGAIVDSFWVIK 440
Cdd:cd00839 223 IYTNPKGPVHIVIGAAGNDEGLDDaFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVR-NQDGQVADSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 20-438 3.10e-38

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 143.67  E-value: 3.10e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007   20 PGIRSTPI---DQDVDIVHyqPEQVHLSF--GDNLRdivVTWSTRSSPNASVVKFSrnylkdepimVNGTWQRFVDGGKK 94
Cdd:PLN02533  25 PGTRKNLVihpDNEDDPTH--PDQVHISLvgPDKMR---ISWITQDSIPPSVVYGT----------VSGKYEGSANGTSS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007   95 A-------RTQYIHNVELKDLEPDTRYEYSCGSPLGwSAVFNFKTPPAgeKWSPSLAIFGDMGnENAQSMGRLQQdTERG 167
Cdd:PLN02533  90 SyhylliyRSGQINDVVIGPLKPNTVYYYKCGGPSS-TQEFSFRTPPS--KFPIKFAVSGDLG-TSEWTKSTLEH-VSKW 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007  168 MYDAIIHVGDFAYDmdTSNAAVGDAFMRQIESVAAYVPYMVCPGNHE-EK------YNFSNYRARFNMP----GETDSLW 236
Cdd:PLN02533 165 DYDVFILPGDLSYA--NFYQPLWDTFGRLVQPLASQRPWMVTHGNHElEKipilhpEKFTAYNARWRMPfeesGSTSNLY 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007  237 YSFNLGPVHFVSFStevyyflSYG-FKLLTKQFEWLERDLAEAnlpeNRAKRPWIITYGHRPMYCSDDKEydcnsQLEty 315
Cdd:PLN02533 243 YSFNVYGVHIIMLG-------SYTdFEPGSEQYQWLENNLKKI----DRKTTPWVVAVVHAPWYNSNEAH-----QGE-- 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007  316 iRQGLPMLKwfGLEDLFYKHGVDVEIFAHEHFYTRLWPIYDYKvyngsaeapyTNPKAPIQIITGSAGCKEE-REPFSND 394
Cdd:PLN02533 305 -KESVGMKE--SMETLLYKARVDLVFAGHVHAYERFDRVYQGK----------TDKCGPVYITIGDGGNREGlATKYIDP 371

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*
gi 20129007  395 LPIWNAYHSNDYGYTRLKAHNGTHLHFE-QVSDDQNGAIVDSFWV 438
Cdd:PLN02533 372 KPDISLFREASFGHGQLNVVDANTMEWTwHRNDDDQSVASDSVWL 416
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
145-353 9.78e-23

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 96.30  E-value: 9.78e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007 145 IFGDMGNENAQSMGRLQQDTERGMYDAIIHVGDFAYDMDTSNAAVGDAFMRQIEsvaayVPYMVCPGNHEEKYNFS-NYR 223
Cdd:COG1409  11 LGAPDGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG-----VPVYVVPGNHDIRAAMAeAYR 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007 224 ARFNMPGeTDSLWYSFNLGPVHFVSFSTEVYYFlSYGFkLLTKQFEWLERDLAEanlpenrAKRPWIITYGHRPMycsdd 303
Cdd:COG1409  86 EYFGDLP-PGGLYYSFDYGGVRFIGLDSNVPGR-SSGE-LGPEQLAWLEEELAA-------APAKPVIVFLHHPP----- 150

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 20129007 304 keYDCNSQLETYIRQGlpmlkWFGLEDLFYKHGVDVEIFAHEHFYTRLWP 353
Cdd:COG1409 151 --YSTGSGSDRIGLRN-----AEELLALLARYGVDLVLSGHVHRYERTRR 193
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 38-132 3.64e-21

Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple acid phosphatase proteins.


Pssm-ID: 465220 [Multi-domain]  Cd Length: 93  Bit Score: 87.47  E-value: 3.64e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007    38 PEQVHLSFGDNLRDIVVTWSTRSSPNASVVKFSRNYlKDEPIMVNGTWQRFVDGGKkaRTQYIHNVELKDLEPDTRYEYS 117
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSWVTPSAVTSPVVQYGTSS-SALTSTATATSSTYTTGDG--GTGYIHRATLTGLEPGTTYYYR 77

                          90
                  ....*....|....*.
gi 20129007   118 CGSP-LGWSAVFNFKT 132
Cdd:pfam16656  78 VGDDnGGWSEVYSFTT 93
Metallophos_C pfam14008
Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of ...
 373-435 1.11e-18

Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of Purple acid phosphatase proteins.


Pssm-ID: 464064 [Multi-domain]  Cd Length: 60  Bit Score: 79.49  E-value: 1.11e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20129007   373 APIQIITGSAGCKEErePFSNDLPIWNAYHSNDYGYTRLKAHNGTHLHFEQVSDDqNGAIVDS 435
Cdd:pfam14008   1 APVHIVIGAAGNIEG--LFVPPQPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSD-DGTVLDS 60
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 143-239 2.85e-07

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: 48.75  E-value: 2.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007   143 LAIFGDM-GNENAQSMGRLQQDT-ERGMYDAIIHVGDFAYDMDTSnaavgDAFMRQIESVAAYVPYMVCPGNHE----EK 216
Cdd:pfam00149   3 ILVIGDLhLPGQLDDLLELLKKLlEEGKPDLVLHAGDLVDRGPPS-----EEVLELLERLIKYVPVYLVRGNHDfdygEC 77

                          90       100
                  ....*....|....*....|...
gi 20129007   217 YNFSNYRARFNMPGETDSLWYSF 239
Cdd:pfam00149  78 LRLYPYLGLLARPWKRFLEVFNF 100
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 145-346 1.44e-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: 46.55  E-value: 1.44e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007 145 IFGDMG-----------NENAQSMGRLQQDterGMYDAIIHVGDFAYDmdtsnAAVGD----AFMRQIESV----AAYVP 205
Cdd:cd07378   5 VLGDWGgkpnpyttaaqSLVAKQMAKVASK---LGIDFILSLGDNFYD-----DGVKDvddpRFQETFEDVysapSLQVP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007 206 YMVCPGNHEEKYNFS--------NYRARFNMPgetdSLWYSFNlgpVHFVSFSTEV--------------YYFLSYG--- 260
Cdd:cd07378  77 WYLVLGNHDHRGNVSaqiaytqrPNSKRWNFP----NYYYDIS---FKFPSSDVTVafimidtvllcgntDDEASGQprg 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007 261 ---FKLLTKQFEWLERDLAEAnlpenraKRPWIITYGHRPMYCSddKEYDCNSQLetyIRQGLPMLKwfgledlfyKHGV 337
Cdd:cd07378 150 ppnKKLAETQLAWLEKQLAAS-------KADYKIVVGHYPIYSS--GEHGPTKCL---VDILLPLLK---------KYKV 208


                ....*....
gi 20129007 338 DVEIFAHEH 346
Cdd:cd07378 209 DAYLSGHDH 217
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 164-305 3.84e-04

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: 41.93  E-value: 3.84e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007 164 TERGMYDAIIHVGDFaYDMDTSNAAVGDAFMRQIESVAAY-VPYMVCPGNHEeKYNFS-NYRARFNMPGETDSLWYSFNL 241
Cdd:cd07396  42 NRESNLAFVVQLGDI-IDGYNAKDRSKEALDAVLSILDRLkGPVHHVLGNHE-FYNFPrEYLNHLKTLNGEDAYYYSFSP 119

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20129007 242 GP-VHFVsfsteVYYFLSYGFKLLTKQFEWLERDLAEANLPENRakrpwIITYGHRPMY-CSDDKE 305
Cdd:cd07396 120 GPgFRFL-----VLDFVKFNGGIGEEQLAWLRNELTSADANGEK-----VIVLSHLPIYpEAADPQ 175
PhoD COG3540
Phosphodiesterase/alkaline phosphatase D [Inorganic ion transport and metabolism];
99-203 6.03e-04

Phosphodiesterase/alkaline phosphatase D [Inorganic ion transport and metabolism];


Pssm-ID: 442761 [Multi-domain]  Cd Length: 482  Bit Score: 42.22  E-value: 6.03e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007  99 YIHNVELKDLEPDTRYEY--SCG---SPLGWsavfnFKTPPAGEKWSP-SLAIFGDMGNENA-----QSMGRLQqdterg 167
Cdd:COG3540  92 HTVKVDVTGLEPGTRYFYrfRAGgetSPVGR-----FRTAPAPGAPDRlRFAFASCQNYEGGyftayRAMAEED------ 160

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 20129007 168 mYDAIIHVGDFAY----DMDTSNAAVGDAFMRQIESVAAY 203
Cdd:COG3540 161 -PDFVLHLGDYIYedgpGPYGLPGLWRPEPSKEAETLADY 199
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 170-330 7.78e-04

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: 41.11  E-value: 7.78e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007 170 DAIIHVGDFAydmDTSNAAVGDAFMRQIESVAAyvPYMVCPGNHEEKYNFsnyRARFNMPGETDS--LWYSFNLGPVHFV 247
Cdd:cd07402  41 DLVVVTGDLS---DDGSPESYERLRELLAPLPA--PVYWIPGNHDDRAAM---REALPEPPYDDNgpVQYVVDFGGWRLI 112

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20129007 248 SFSTEVYYFlSYGFkLLTKQFEWLERDLAEAnlPEnrakRPWIITYGHRPMYCsddkeydcnsqletyirqGLPMLKWFG 327
Cdd:cd07402 113 LLDTSVPGV-HHGE-LSDEQLDWLEAALAEA--PD----RPTLIFLHHPPFPL------------------GIPWMDAIR 166


                ...
gi 20129007 328 LED 330
Cdd:cd07402 167 LRN 169
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 144-214 3.61e-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: 3.61e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20129007 144 AIFGD--MGNENAQSMGRLQQDTERGmYDAIIHVGDFAYDMDTSNAAVGDAFmrqiESVAAYVPYMVCPGNHE 214
Cdd:cd00838   1 LVISDihGNLEALEAVLEAALAKAEK-PDLVICLGDLVDYGPDPEEVELKAL----RLLLAGIPVYVVPGNHD 68
 
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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