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Conserved domains on  [gi|568944670|ref|XP_006539512|]
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acid phosphatase type 7 isoform X1 [Mus musculus]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 11244682)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc), similar to purple acid phosphatase (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.-.-
Gene Ontology:  GO:0042578|GO:0046872
PubMed:  25837850
SCOP:  3001067

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; ...
 189-487 6.14e-129

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: 376.25  E-value: 6.14e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 189 HWSPRLAVFGDMGA---DNPKALPRLRRDTqqGMFDAVLHVGDFAYNMDQDNARVGDRFMRLIEPVAASLPYMTCPGNHE 265
Cdd:cd00839    2 DTPLKFAVFGDMGQntnNSTNTLDHLEKEL--GNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 266 QRYNFSNYKARFSMP---------GDNEGLWYSWDLGPAHIISFSTEVYFFLHYgrhLIEKQFRWLENDLQKANKNRvaR 336
Cdd:cd00839   80 ADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLAKVDRSR--T 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 337 PWIITMGHRPMYCSNADLDDCTRHEsrvrkglhGKLFGLEDLFHKYGVDLEFWAHEHSYERLWPIYNYQVFNGSlESPYT 416
Cdd:cd00839  155 PWIIVMGHRPMYCSNDDDADCIEGE--------KMREALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVANSK-DNIYT 225

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568944670 417 NPRGPVHIITGSAGCEELL-TPFVRKPRPWSAVRVKEYGYTRMHILNGTHMHIQQVSdDQDGKIVDDVWVVR 487
Cdd:cd00839  226 NPKGPVHIVIGAAGNDEGLdDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVR-NQDGQVADSFWIVK 296
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 90-182 7.16e-20

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: 84.38  E-value: 7.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670   90 PEQIHLSYLGEPGTMTVTWTTW-APARSEVQFGSQlSGPLPFRAHGTARAFVDGGvlRRKLYIHRVTLRKLQPGAQYVYR 168
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSWVTPsAVTSPVVQYGTS-SSALTSTATATSSTYTTGD--GGTGYIHRATLTGLEPGTTYYYR 77

                          90
                  ....*....|....*
gi 568944670  169 CGS-SQGWSRRFRFT 182
Cdd:pfam16656  78 VGDdNGGWSEVYSFT 92
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 189-487 6.14e-129

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: 376.25  E-value: 6.14e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 189 HWSPRLAVFGDMGA---DNPKALPRLRRDTqqGMFDAVLHVGDFAYNMDQDNARVGDRFMRLIEPVAASLPYMTCPGNHE 265
Cdd:cd00839    2 DTPLKFAVFGDMGQntnNSTNTLDHLEKEL--GNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 266 QRYNFSNYKARFSMP---------GDNEGLWYSWDLGPAHIISFSTEVYFFLHYgrhLIEKQFRWLENDLQKANKNRvaR 336
Cdd:cd00839   80 ADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLAKVDRSR--T 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 337 PWIITMGHRPMYCSNADLDDCTRHEsrvrkglhGKLFGLEDLFHKYGVDLEFWAHEHSYERLWPIYNYQVFNGSlESPYT 416
Cdd:cd00839  155 PWIIVMGHRPMYCSNDDDADCIEGE--------KMREALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVANSK-DNIYT 225

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568944670 417 NPRGPVHIITGSAGCEELL-TPFVRKPRPWSAVRVKEYGYTRMHILNGTHMHIQQVSdDQDGKIVDDVWVVR 487
Cdd:cd00839  226 NPKGPVHIVIGAAGNDEGLdDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVR-NQDGQVADSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 90-485 1.73e-46

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 167.17  E-value: 1.73e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670  90 PEQIHLSYLGePGTMTVTWTTWAPARSEVQFGSqLSGPLPFRAHGTARAFvDGGVLRRKLYIHRVTLRKLQPGAQYVYRC 169
Cdd:PLN02533  44 PDQVHISLVG-PDKMRISWITQDSIPPSVVYGT-VSGKYEGSANGTSSSY-HYLLIYRSGQINDVVIGPLKPNTVYYYKC 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 170 G---SSQGWSrrFRFTALKNGVhwspRLAVFGDMGAD--NPKALPRLRRDTqqgmFDAVLHVGDFAY-NMDQDnarVGDR 243
Cdd:PLN02533 121 GgpsSTQEFS--FRTPPSKFPI----KFAVSGDLGTSewTKSTLEHVSKWD----YDVFILPGDLSYaNFYQP---LWDT 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 244 FMRLIEPVAASLPYMTCPGNHE-------QRYNFSNYKARFSMP----GDNEGLWYSWDLGPAHIISFSTEVYFflhygr 312
Cdd:PLN02533 188 FGRLVQPLASQRPWMVTHGNHElekipilHPEKFTAYNARWRMPfeesGSTSNLYYSFNVYGVHIIMLGSYTDF------ 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 313 HLIEKQFRWLENDLQKANKNRVarPWIITMGHRPMYCSNadlddcTRHESrvRKGLHGKLFGLEDLFHKYGVDLEFWAHE 392
Cdd:PLN02533 262 EPGSEQYQWLENNLKKIDRKTT--PWVVAVVHAPWYNSN------EAHQG--EKESVGMKESMETLLYKARVDLVFAGHV 331

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 393 HSYERLWPIYNYQvfngslespyTNPRGPVHIITGSAGCEELLTPFVRKPRP-WSAVRVKEYGYTRMHILNGTHMHIQ-Q 470
Cdd:PLN02533 332 HAYERFDRVYQGK----------TDKCGPVYITIGDGGNREGLATKYIDPKPdISLFREASFGHGQLNVVDANTMEWTwH 401

                        410
                 ....*....|....*
gi 568944670 471 VSDDQDGKIVDDVWV 485
Cdd:PLN02533 402 RNDDDQSVASDSVWL 416
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
193-420 5.19e-24

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 100.15  E-value: 5.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 193 RLAVFGDM------GADNPKALPRLRRDTQQGMFDAVLHVGDFAYNMDQDNARVGDRFMRLIEpvaasLPYMTCPGNHEQ 266
Cdd:COG1409    2 RFAHISDLhlgapdGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG-----VPVYVVPGNHDI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 267 RYNFS-NYKARFSMPgDNEGLWYSWDLGPAHIISFSTEVYffLHYGRHLIEKQFRWLENDLQKAnknrvARPWIITMGHR 345
Cdd:COG1409   77 RAAMAeAYREYFGDL-PPGGLYYSFDYGGVRFIGLDSNVP--GRSSGELGPEQLAWLEEELAAA-----PAKPVIVFLHH 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568944670 346 PMYCSNADLDdctrhesrvRKGLHGKlFGLEDLFHKYGVDLEFWAHEHSYERLWPIYNYQVFNGSLESPYTNPRG 420
Cdd:COG1409  149 PPYSTGSGSD---------RIGLRNA-EELLALLARYGVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRLPPG 213
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 90-182 7.16e-20

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: 84.38  E-value: 7.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670   90 PEQIHLSYLGEPGTMTVTWTTW-APARSEVQFGSQlSGPLPFRAHGTARAFVDGGvlRRKLYIHRVTLRKLQPGAQYVYR 168
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSWVTPsAVTSPVVQYGTS-SSALTSTATATSSTYTTGD--GGTGYIHRATLTGLEPGTTYYYR 77

                          90
                  ....*....|....*
gi 568944670  169 CGS-SQGWSRRFRFT 182
Cdd:pfam16656  78 VGDdNGGWSEVYSFT 92
Metallophos_C pfam14008
Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of ...
 420-481 4.84e-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: 77.95  E-value: 4.84e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568944670  420 GPVHIITGSAGCEEllTPFVRKPRPWSAVRVKEYGYTRMHILNGTHMHIQQVSDDqDGKIVD 481
Cdd:pfam14008   1 APVHIVIGAAGNIE--GLFVPPQPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSD-DGTVLD 59
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 189-487 6.14e-129

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: 376.25  E-value: 6.14e-129
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 189 HWSPRLAVFGDMGA---DNPKALPRLRRDTqqGMFDAVLHVGDFAYNMDQDNARVGDRFMRLIEPVAASLPYMTCPGNHE 265
Cdd:cd00839    2 DTPLKFAVFGDMGQntnNSTNTLDHLEKEL--GNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 266 QRYNFSNYKARFSMP---------GDNEGLWYSWDLGPAHIISFSTEVYFFLHYgrhLIEKQFRWLENDLQKANKNRvaR 336
Cdd:cd00839   80 ADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLAKVDRSR--T 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 337 PWIITMGHRPMYCSNADLDDCTRHEsrvrkglhGKLFGLEDLFHKYGVDLEFWAHEHSYERLWPIYNYQVFNGSlESPYT 416
Cdd:cd00839  155 PWIIVMGHRPMYCSNDDDADCIEGE--------KMREALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVANSK-DNIYT 225

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568944670 417 NPRGPVHIITGSAGCEELL-TPFVRKPRPWSAVRVKEYGYTRMHILNGTHMHIQQVSdDQDGKIVDDVWVVR 487
Cdd:cd00839  226 NPKGPVHIVIGAAGNDEGLdDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVR-NQDGQVADSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 90-485 1.73e-46

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 167.17  E-value: 1.73e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670  90 PEQIHLSYLGePGTMTVTWTTWAPARSEVQFGSqLSGPLPFRAHGTARAFvDGGVLRRKLYIHRVTLRKLQPGAQYVYRC 169
Cdd:PLN02533  44 PDQVHISLVG-PDKMRISWITQDSIPPSVVYGT-VSGKYEGSANGTSSSY-HYLLIYRSGQINDVVIGPLKPNTVYYYKC 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 170 G---SSQGWSrrFRFTALKNGVhwspRLAVFGDMGAD--NPKALPRLRRDTqqgmFDAVLHVGDFAY-NMDQDnarVGDR 243
Cdd:PLN02533 121 GgpsSTQEFS--FRTPPSKFPI----KFAVSGDLGTSewTKSTLEHVSKWD----YDVFILPGDLSYaNFYQP---LWDT 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 244 FMRLIEPVAASLPYMTCPGNHE-------QRYNFSNYKARFSMP----GDNEGLWYSWDLGPAHIISFSTEVYFflhygr 312
Cdd:PLN02533 188 FGRLVQPLASQRPWMVTHGNHElekipilHPEKFTAYNARWRMPfeesGSTSNLYYSFNVYGVHIIMLGSYTDF------ 261

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 313 HLIEKQFRWLENDLQKANKNRVarPWIITMGHRPMYCSNadlddcTRHESrvRKGLHGKLFGLEDLFHKYGVDLEFWAHE 392
Cdd:PLN02533 262 EPGSEQYQWLENNLKKIDRKTT--PWVVAVVHAPWYNSN------EAHQG--EKESVGMKESMETLLYKARVDLVFAGHV 331

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 393 HSYERLWPIYNYQvfngslespyTNPRGPVHIITGSAGCEELLTPFVRKPRP-WSAVRVKEYGYTRMHILNGTHMHIQ-Q 470
Cdd:PLN02533 332 HAYERFDRVYQGK----------TDKCGPVYITIGDGGNREGLATKYIDPKPdISLFREASFGHGQLNVVDANTMEWTwH 401

                        410
                 ....*....|....*
gi 568944670 471 VSDDQDGKIVDDVWV 485
Cdd:PLN02533 402 RNDDDQSVASDSVWL 416
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
193-420 5.19e-24

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 100.15  E-value: 5.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 193 RLAVFGDM------GADNPKALPRLRRDTQQGMFDAVLHVGDFAYNMDQDNARVGDRFMRLIEpvaasLPYMTCPGNHEQ 266
Cdd:COG1409    2 RFAHISDLhlgapdGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG-----VPVYVVPGNHDI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 267 RYNFS-NYKARFSMPgDNEGLWYSWDLGPAHIISFSTEVYffLHYGRHLIEKQFRWLENDLQKAnknrvARPWIITMGHR 345
Cdd:COG1409   77 RAAMAeAYREYFGDL-PPGGLYYSFDYGGVRFIGLDSNVP--GRSSGELGPEQLAWLEEELAAA-----PAKPVIVFLHH 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568944670 346 PMYCSNADLDdctrhesrvRKGLHGKlFGLEDLFHKYGVDLEFWAHEHSYERLWPIYNYQVFNGSLESPYTNPRG 420
Cdd:COG1409  149 PPYSTGSGSD---------RIGLRNA-EELLALLARYGVDLVLSGHVHRYERTRRDGVPYIVAGSTGGQVRLPPG 213
Pur_ac_phosph_N pfam16656
Purple acid Phosphatase, N-terminal domain; This domain is found at the N-terminus of Purple ...
 90-182 7.16e-20

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: 84.38  E-value: 7.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670   90 PEQIHLSYLGEPGTMTVTWTTW-APARSEVQFGSQlSGPLPFRAHGTARAFVDGGvlRRKLYIHRVTLRKLQPGAQYVYR 168
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSWVTPsAVTSPVVQYGTS-SSALTSTATATSSTYTTGD--GGTGYIHRATLTGLEPGTTYYYR 77

                          90
                  ....*....|....*
gi 568944670  169 CGS-SQGWSRRFRFT 182
Cdd:pfam16656  78 VGDdNGGWSEVYSFT 92
Metallophos_C pfam14008
Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of ...
 420-481 4.84e-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: 77.95  E-value: 4.84e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568944670  420 GPVHIITGSAGCEEllTPFVRKPRPWSAVRVKEYGYTRMHILNGTHMHIQQVSDDqDGKIVD 481
Cdd:pfam14008   1 APVHIVIGAAGNIE--GLFVPPQPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSD-DGTVLD 59
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 193-299 1.06e-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: 50.29  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670  193 RLAVFGDMG-----ADNPKALPRLRRDTQqgmFDAVLHVGDFAYNMDQDnarvgDRFMRLIEPVAASLPYMTCPGNHEQR 267
Cdd:pfam00149   2 RILVIGDLHlpgqlDDLLELLKKLLEEGK---PDLVLHAGDLVDRGPPS-----EEVLELLERLIKYVPVYLVRGNHDFD 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568944670  268 Y----NFSNYKARFSMPGDNEGLWYSWdLGPAHIIS 299
Cdd:pfam00149  74 YgeclRLYPYLGLLARPWKRFLEVFNF-LPLAGILS 108
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 217-355 4.17e-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: 51.12  E-value: 4.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 217 QGMFDAVLHVGDFAynmdqDNARVG--DRFMRLIEPVAAslPYMTCPGNHEQRYNFsnYKARFSMP-GDNEGLWYSWDLG 293
Cdd:cd07402   37 HPRPDLVVVTGDLS-----DDGSPEsyERLRELLAPLPA--PVYWIPGNHDDRAAM--REALPEPPyDDNGPVQYVVDFG 107

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568944670 294 PAHIISFSTEVYFFLHYgrHLIEKQFRWLENDLQKANKnrvaRPWIITMGHRPMYCSNADLD 355
Cdd:cd07402  108 GWRLILLDTSVPGVHHG--ELSDEQLDWLEAALAEAPD----RPTLIFLHHPPFPLGIPWMD 163
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 215-353 5.04e-06

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: 47.71  E-value: 5.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 215 TQQGMFDAVLHVGDFaynMDQDNARvgDRFMRLIEPV-----AASLPYMTCPGNHEqRYNFS-NYKARFSMPGDNEGLWY 288
Cdd:cd07396   42 NRESNLAFVVQLGDI---IDGYNAK--DRSKEALDAVlsildRLKGPVHHVLGNHE-FYNFPrEYLNHLKTLNGEDAYYY 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568944670 289 SWDLGPahiiSFSTEVYFFLHYGRHLIEKQFRWLENDLQ--KANKNRVarpwiITMGHRPMYCSNAD 353
Cdd:cd07396  116 SFSPGP----GFRFLVLDFVKFNGGIGEEQLAWLRNELTsaDANGEKV-----IVLSHLPIYPEAAD 173
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 193-396 5.85e-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: 5.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 193 RLAVFGDMGA-DNPKALPRLRrDTQQGM--------FDAVLHVGD-FAYNMDQDnarVGD-RFMRLIEPV--AASL--PY 257
Cdd:cd07378    2 RFLVLGDWGGkPNPYTTAAQS-LVAKQMakvasklgIDFILSLGDnFYDDGVKD---VDDpRFQETFEDVysAPSLqvPW 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 258 MTCPGNHEQRYNFS---------NYKaRFSMPgdneGLWY--SWdlgpaHIISFSTEVYFFL--------HYGRH----- 313
Cdd:cd07378   78 YLVLGNHDHRGNVSaqiaytqrpNSK-RWNFP----NYYYdiSF-----KFPSSDVTVAFIMidtvllcgNTDDEasgqp 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568944670 314 -------LIEKQFRWLENDLQKANKNrvarpWIITMGHRPMYCSnadlddctrhesrvrkGLHGKLFGLED----LFHKY 382
Cdd:cd07378  148 rgppnkkLAETQLAWLEKQLAASKAD-----YKIVVGHYPIYSS----------------GEHGPTKCLVDillpLLKKY 206

                        250
                 ....*....|....
gi 568944670 383 GVDLEFWAHEHSYE 396
Cdd:cd07378  207 KVDAYLSGHDHNLQ 220
 
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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