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Conserved domains on  [gi|1993939471|ref|XP_039597997|]
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acid phosphatase type 7 isoform X2 [Polypterus senegalus]

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; ...
 216-519 1.03e-132

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: 387.04  E-value: 1.03e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 216 NWSPRFALFGDLG---NENPQSLARLQKDAqiGMYDFILHIGDFAYDMEEDNARIGDEFMRQIQSIAAYVPYMTCPGNHE 292
Cdd:cd00839     2 DTPLKFAVFGDMGqntNNSTNTLDHLEKEL--GNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 293 QAYNFSNYRNRFSMP---------GDTESLWYSWNVGPAHIISFSTEVYFYLDYglnLLFRQYQWLEKDLKEAnkpeNRR 363
Cdd:cd00839    80 ADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLAKV----DRS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 364 ERPWIITMGHRPMYCSNDDKDDCTLFESYVrlgrndtkppaPGLEELFYLYGVDLELWAHEHSYERLWPVYGFQVFNgSK 443
Cdd:cd00839   153 RTPWIIVMGHRPMYCSNDDDADCIEGEKMR-----------EALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVAN-SK 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993939471 444 EQPYVNPKAPVHIITGSAGCREEHD-GFVPKPREWSAFRSTDYGYTRMQVLNSTHLYIEQVSDDQsGRVIDSVWIVK 519
Cdd:cd00839   221 DNIYTNPKGPVHIVIGAAGNDEGLDdAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVRNQD-GQVADSFWIVK 296
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 117-210 1.50e-17

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: 77.84  E-value: 1.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 117 PEQIHLSYPGNPRSVVITWTTFNKTDT-LVEYGVWGEKLFDKATQgscTMFEDGGTEKRSLFIHRVTLQDLKPGLAYVYH 195
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSWVTPSAVTSpVVQYGTSSSALTSTATA---TSSTYTTGDGGTGYIHRATLTGLEPGTTYYYR 77

                          90
                  ....*....|....*.
gi 1993939471 196 CGSEE-GWSEILFFNT 210
Cdd:pfam16656  78 VGDDNgGWSEVYSFTT 93
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 216-519 1.03e-132

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: 387.04  E-value: 1.03e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 216 NWSPRFALFGDLG---NENPQSLARLQKDAqiGMYDFILHIGDFAYDMEEDNARIGDEFMRQIQSIAAYVPYMTCPGNHE 292
Cdd:cd00839     2 DTPLKFAVFGDMGqntNNSTNTLDHLEKEL--GNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 293 QAYNFSNYRNRFSMP---------GDTESLWYSWNVGPAHIISFSTEVYFYLDYglnLLFRQYQWLEKDLKEAnkpeNRR 363
Cdd:cd00839    80 ADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLAKV----DRS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 364 ERPWIITMGHRPMYCSNDDKDDCTLFESYVrlgrndtkppaPGLEELFYLYGVDLELWAHEHSYERLWPVYGFQVFNgSK 443
Cdd:cd00839   153 RTPWIIVMGHRPMYCSNDDDADCIEGEKMR-----------EALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVAN-SK 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993939471 444 EQPYVNPKAPVHIITGSAGCREEHD-GFVPKPREWSAFRSTDYGYTRMQVLNSTHLYIEQVSDDQsGRVIDSVWIVK 519
Cdd:cd00839   221 DNIYTNPKGPVHIVIGAAGNDEGLDdAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVRNQD-GQVADSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 117-517 2.14e-43

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 159.46  E-value: 2.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 117 PEQIHLSYPGnPRSVVITWTTFNKTDTLVEYGVWGEKLFDKATQGSCTMFEDggTEKRSLFIHRVTLQDLKPGLAYVYHC 196
Cdd:PLN02533   44 PDQVHISLVG-PDKMRISWITQDSIPPSVVYGTVSGKYEGSANGTSSSYHYL--LIYRSGQINDVVIGPLKPNTVYYYKC 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 197 GSEEGWSEilfFNTIKEGNNWSPRFALFGDLGNE--NPQSLARLQKDAqigmYDFILHIGDFAY-DMEEDnarIGDEFMR 273
Cdd:PLN02533  121 GGPSSTQE---FSFRTPPSKFPIKFAVSGDLGTSewTKSTLEHVSKWD----YDVFILPGDLSYaNFYQP---LWDTFGR 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 274 QIQSIAAYVPYMTCPGNHE-------QAYNFSNYRNRFSMP----GDTESLWYSWNVGPAHIISFSTevyfYLDYGLNll 342
Cdd:PLN02533  191 LVQPLASQRPWMVTHGNHElekipilHPEKFTAYNARWRMPfeesGSTSNLYYSFNVYGVHIIMLGS----YTDFEPG-- 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 343 FRQYQWLEKDLKEAnkpeNRRERPWIITMGHRPMYCSNDdkddctlfesyVRLGRNDTKPPAPGLEELFYLYGVDLELWA 422
Cdd:PLN02533  265 SEQYQWLENNLKKI----DRKTTPWVVAVVHAPWYNSNE-----------AHQGEKESVGMKESMETLLYKARVDLVFAG 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 423 HEHSYERLWPVYgfqvfngskeQPYVNPKAPVHIITGSAGCREEHDGFVPKPR-EWSAFRSTDYGYTRMQVLNSTHLYIE 501
Cdd:PLN02533  330 HVHAYERFDRVY----------QGKTDKCGPVYITIGDGGNREGLATKYIDPKpDISLFREASFGHGQLNVVDANTMEWT 399

                         410
                  ....*....|....*..
gi 1993939471 502 -QVSDDQSGRVIDSVWI 517
Cdd:PLN02533  400 wHRNDDDQSVASDSVWL 416
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
220-432 1.44e-24

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 102.08  E-value: 1.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 220 RFALFGDL------GNENPQSLARLQKDAQIGMYDFILHIGDFAYDMEEDNARIGDEFMRQIQsiaayVPYMTCPGNHE- 292
Cdd:COG1409     2 RFAHISDLhlgapdGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG-----VPVYVVPGNHDi 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 293 QAYNFSNYRNRFSMPgDTESLWYSWNVGPAHIISFSTEVYfYLDYGlNLLFRQYQWLEKDLKEANKpenrrerPWIITMG 372
Cdd:COG1409    77 RAAMAEAYREYFGDL-PPGGLYYSFDYGGVRFIGLDSNVP-GRSSG-ELGPEQLAWLEEELAAAPA-------KPVIVFL 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 373 HRPMYCSNDDKDDCTLfesyvrlgRNdtkppAPGLEELFYLYGVDLELWAHEHSYERLWP 432
Cdd:COG1409   147 HHPPYSTGSGSDRIGL--------RN-----AEELLALLARYGVDLVLSGHVHRYERTRR 193
Metallophos_C pfam14008
Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of ...
 452-514 2.87e-22

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: 89.89  E-value: 2.87e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993939471 452 APVHIITGSAGCREehDGFVPKPREWSAFRSTDYGYTRMQVLNSTHLYIEQVSDDqSGRVIDS 514
Cdd:pfam14008   1 APVHIVIGAAGNIE--GLFVPPQPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSD-DGTVLDS 60
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 117-210 1.50e-17

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: 77.84  E-value: 1.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 117 PEQIHLSYPGNPRSVVITWTTFNKTDT-LVEYGVWGEKLFDKATQgscTMFEDGGTEKRSLFIHRVTLQDLKPGLAYVYH 195
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSWVTPSAVTSpVVQYGTSSSALTSTATA---TSSTYTTGDGGTGYIHRATLTGLEPGTTYYYR 77

                          90
                  ....*....|....*.
gi 1993939471 196 CGSEE-GWSEILFFNT 210
Cdd:pfam16656  78 VGDDNgGWSEVYSFTT 93
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 216-519 1.03e-132

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: 387.04  E-value: 1.03e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 216 NWSPRFALFGDLG---NENPQSLARLQKDAqiGMYDFILHIGDFAYDMEEDNARIGDEFMRQIQSIAAYVPYMTCPGNHE 292
Cdd:cd00839     2 DTPLKFAVFGDMGqntNNSTNTLDHLEKEL--GNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 293 QAYNFSNYRNRFSMP---------GDTESLWYSWNVGPAHIISFSTEVYFYLDYglnLLFRQYQWLEKDLKEAnkpeNRR 363
Cdd:cd00839    80 ADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLAKV----DRS 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 364 ERPWIITMGHRPMYCSNDDKDDCTLFESYVrlgrndtkppaPGLEELFYLYGVDLELWAHEHSYERLWPVYGFQVFNgSK 443
Cdd:cd00839   153 RTPWIIVMGHRPMYCSNDDDADCIEGEKMR-----------EALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVAN-SK 220

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1993939471 444 EQPYVNPKAPVHIITGSAGCREEHD-GFVPKPREWSAFRSTDYGYTRMQVLNSTHLYIEQVSDDQsGRVIDSVWIVK 519
Cdd:cd00839   221 DNIYTNPKGPVHIVIGAAGNDEGLDdAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVRNQD-GQVADSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 117-517 2.14e-43

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 159.46  E-value: 2.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 117 PEQIHLSYPGnPRSVVITWTTFNKTDTLVEYGVWGEKLFDKATQGSCTMFEDggTEKRSLFIHRVTLQDLKPGLAYVYHC 196
Cdd:PLN02533   44 PDQVHISLVG-PDKMRISWITQDSIPPSVVYGTVSGKYEGSANGTSSSYHYL--LIYRSGQINDVVIGPLKPNTVYYYKC 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 197 GSEEGWSEilfFNTIKEGNNWSPRFALFGDLGNE--NPQSLARLQKDAqigmYDFILHIGDFAY-DMEEDnarIGDEFMR 273
Cdd:PLN02533  121 GGPSSTQE---FSFRTPPSKFPIKFAVSGDLGTSewTKSTLEHVSKWD----YDVFILPGDLSYaNFYQP---LWDTFGR 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 274 QIQSIAAYVPYMTCPGNHE-------QAYNFSNYRNRFSMP----GDTESLWYSWNVGPAHIISFSTevyfYLDYGLNll 342
Cdd:PLN02533  191 LVQPLASQRPWMVTHGNHElekipilHPEKFTAYNARWRMPfeesGSTSNLYYSFNVYGVHIIMLGS----YTDFEPG-- 264

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 343 FRQYQWLEKDLKEAnkpeNRRERPWIITMGHRPMYCSNDdkddctlfesyVRLGRNDTKPPAPGLEELFYLYGVDLELWA 422
Cdd:PLN02533  265 SEQYQWLENNLKKI----DRKTTPWVVAVVHAPWYNSNE-----------AHQGEKESVGMKESMETLLYKARVDLVFAG 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 423 HEHSYERLWPVYgfqvfngskeQPYVNPKAPVHIITGSAGCREEHDGFVPKPR-EWSAFRSTDYGYTRMQVLNSTHLYIE 501
Cdd:PLN02533  330 HVHAYERFDRVY----------QGKTDKCGPVYITIGDGGNREGLATKYIDPKpDISLFREASFGHGQLNVVDANTMEWT 399

                         410
                  ....*....|....*..
gi 1993939471 502 -QVSDDQSGRVIDSVWI 517
Cdd:PLN02533  400 wHRNDDDQSVASDSVWL 416
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
220-432 1.44e-24

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 102.08  E-value: 1.44e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 220 RFALFGDL------GNENPQSLARLQKDAQIGMYDFILHIGDFAYDMEEDNARIGDEFMRQIQsiaayVPYMTCPGNHE- 292
Cdd:COG1409     2 RFAHISDLhlgapdGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG-----VPVYVVPGNHDi 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 293 QAYNFSNYRNRFSMPgDTESLWYSWNVGPAHIISFSTEVYfYLDYGlNLLFRQYQWLEKDLKEANKpenrrerPWIITMG 372
Cdd:COG1409    77 RAAMAEAYREYFGDL-PPGGLYYSFDYGGVRFIGLDSNVP-GRSSG-ELGPEQLAWLEEELAAAPA-------KPVIVFL 146

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 373 HRPMYCSNDDKDDCTLfesyvrlgRNdtkppAPGLEELFYLYGVDLELWAHEHSYERLWP 432
Cdd:COG1409   147 HHPPYSTGSGSDRIGL--------RN-----AEELLALLARYGVDLVLSGHVHRYERTRR 193
Metallophos_C pfam14008
Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of ...
 452-514 2.87e-22

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: 89.89  E-value: 2.87e-22
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993939471 452 APVHIITGSAGCREehDGFVPKPREWSAFRSTDYGYTRMQVLNSTHLYIEQVSDDqSGRVIDS 514
Cdd:pfam14008   1 APVHIVIGAAGNIE--GLFVPPQPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSD-DGTVLDS 60
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 117-210 1.50e-17

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: 77.84  E-value: 1.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 117 PEQIHLSYPGNPRSVVITWTTFNKTDT-LVEYGVWGEKLFDKATQgscTMFEDGGTEKRSLFIHRVTLQDLKPGLAYVYH 195
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSWVTPSAVTSpVVQYGTSSSALTSTATA---TSSTYTTGDGGTGYIHRATLTGLEPGTTYYYR 77

                          90
                  ....*....|....*.
gi 1993939471 196 CGSEE-GWSEILFFNT 210
Cdd:pfam16656  78 VGDDNgGWSEVYSFTT 93
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 220-317 4.28e-09

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: 54.53  E-value: 4.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 220 RFALFGDL-GNENPQSLARLQKD-AQIGMYDFILHIGDFAydmeeDNARIGDEFMRQIQSIAAYVPYMTCPGNHEQAY-- 295
Cdd:pfam00149   2 RILVIGDLhLPGQLDDLLELLKKlLEEGKPDLVLHAGDLV-----DRGPPSEEVLELLERLIKYVPVYLVRGNHDFDYge 76

                          90       100
                  ....*....|....*....|....
gi 1993939471 296 --NFSNYRNRFSMPGDTESLWYSW 317
Cdd:pfam00149  77 clRLYPYLGLLARPWKRFLEVFNF 100
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 220-495 4.51e-07

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: 51.56  E-value: 4.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 220 RFALFGDLG-----------NENPQSLARLQKDAQIgmyDFILHIGDFAYD---MEEDNARIGDEFmRQIQSIAA-YVPY 284
Cdd:cd07378     2 RFLVLGDWGgkpnpyttaaqSLVAKQMAKVASKLGI---DFILSLGDNFYDdgvKDVDDPRFQETF-EDVYSAPSlQVPW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 285 MTCPGNH--------EQAYNFSNYRNRFSMPgdteSLWYSWNVgpaHIISFSTEV-YFYLD-------YG---------- 338
Cdd:cd07378    78 YLVLGNHdhrgnvsaQIAYTQRPNSKRWNFP----NYYYDISF---KFPSSDVTVaFIMIDtvllcgnTDdeasgqprgp 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 339 --LNLLFRQYQWLEKDLKEANKPenrrerpWIITMGHRPMYCSNDDKDDCTLFESYVrlgrndtkppaPGLEElfylYGV 416
Cdd:cd07378   151 pnKKLAETQLAWLEKQLAASKAD-------YKIVVGHYPIYSSGEHGPTKCLVDILL-----------PLLKK----YKV 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 417 DLELWAHEHSYErlwpvygfqvfngskeqpYVNPKAPVH-IITGSAGCREEHDGFVPK-PREW----SAFRSTDYGYTRM 490
Cdd:cd07378   209 DAYLSGHDHNLQ------------------HIVDESGTYyVISGAGSKADPSDIHRDKvPQGYllffSGFYSSGGGFAYL 270


                  ....*
gi 1993939471 491 QVLNS 495
Cdd:cd07378   271 EITSS 275
PRK11340 PRK11340
phosphodiesterase YaeI; Provisional
 189-295 3.27e-04

phosphodiesterase YaeI; Provisional


Pssm-ID: 236899  Cd Length: 271  Bit Score: 42.53  E-value: 3.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 189 GLAYVYHCgsEEGWSEILFFNTIKEGNNWSP-RFALFGDLGNENPQSLARLQKDAQIGM---YDFILHIGDFA-YDMEED 263
Cdd:PRK11340   21 GFGYMHYW--EPGWFELIRHRLAFFKDNAAPfKILFLADLHYSRFVPLSLISDAIALGIeqkPDLILLGGDYVlFDMPLN 98

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1993939471 264 NArigdEFMRQIQSIAAYVPYMTCPGNHEQAY 295
Cdd:PRK11340   99 FS----AFSDVLSPLAECAPTFACFGNHDRPV 126
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 235-384 4.26e-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: 41.88  E-value: 4.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 235 LARLQKDAqigmyDFILHIGDFAYDMEEDNArigDEFMRQIQSIAAyvPYMTCPGNHEQAYNFSNYRNRfSMPGDTESLW 314
Cdd:cd07402    33 VNALHPRP-----DLVVVTGDLSDDGSPESY---ERLRELLAPLPA--PVYWIPGNHDDRAAMREALPE-PPYDDNGPVQ 101

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 315 YSWNVGPAHIISFSTEVYFYlDYGLnLLFRQYQWLEKDLKEAnkpenrRERPWIITMGHRPMYCSNDDKD 384
Cdd:cd07402   102 YVVDFGGWRLILLDTSVPGV-HHGE-LSDEQLDWLEAALAEA------PDRPTLIFLHHPPFPLGIPWMD 163
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
220-292 2.66e-03

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 39.23  E-value: 2.66e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1993939471 220 RFALFGDLgNENPQSLARLQKDAQIGMYDFILHIGDFAYDMEEDNARigdEFMRQIQSIAayVPYMTCPGNHE 292
Cdd:COG2129     1 KILAVSDL-HGNFDLLEKLLELARAEDADLVILAGDLTDFGTAEEAR---EVLEELAALG--VPVLAVPGNHD 67
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 243-387 5.47e-03

acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase (ASMase) is a ubiquitously expressed phosphodiesterase which hydrolyzes sphingomyelin in acid pH conditions to form ceramide, a bioactive second messenger, as part of the sphingomyelin signaling pathway. ASMase is localized at the noncytosolic leaflet of biomembranes (for example the luminal leaflet of endosomes, lysosomes and phagosomes, and the extracellular leaflet of plasma membranes). ASMase-deficient humans develop Niemann-Pick disease. This disease is characterized by lysosomal storage of sphingomyelin in all tissues. Although ASMase-deficient mice are resistant to stress-induced apoptosis, they have greater susceptibility to bacterial infection. The latter correlates with defective phagolysosomal fusion and antibacterial killing activity in ASMase-deficient macrophages. ASMase 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: 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: 277321 [Multi-domain]  Cd Length: 294  Bit Score: 38.82  E-value: 5.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 243 QIGMYDFILHIGDF-AYDMEEDNARIGDEFMRQI-QSIAAY---VPYMTCPGNHE--QAYNFSNYRNRFS---------- 305
Cdd:cd00842    66 NHPKPDFILWTGDLvRHDVDEQTPEETVESESNLtNLLKKYfpnVPVYPALGNHDsyPVNQFPPHSNSPSwlydalaelw 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1993939471 306 ---MPGDTESL-----WYSWNVGPA-HIISFSTEVY----FYLDYGLNLLFRQYQWLEKDLKEAnkpENRRERPWIItmG 372
Cdd:cd00842   146 kpwLPTEAKETfkkggYYSVDVKDGlRVISLNTNLYykknFWLYSNNTDPCGQLQWLEDELEDA---EQKGEKVWII--G 220

                         170
                  ....*....|....*
gi 1993939471 373 HRPMYcSNDDKDDCT 387
Cdd:cd00842   221 HIPPG-LNSYDADWS 234
 
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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