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Conserved domains on  [gi|1569289680|ref|NP_780528|]
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acid phosphatase type 7 precursor [Mus musculus]

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; ...
 131-429 1.86e-128

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: 373.17  E-value: 1.86e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 131 HWSPRLAVFGDMGA---DNPKALPRLRRDTqqGMFDAVLHVGDFAYNMDQDNARVGDRFMRLIEPVAASLPYMTCPGNHE 207
Cdd:cd00839     2 DTPLKFAVFGDMGQntnNSTNTLDHLEKEL--GNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 208 QRYNFSNYKARFSMP---------GDNEGLWYSWDLGPAHIISFSTEVYFFLHYgrhLIEKQFRWLENDLQKANKNRvaR 278
Cdd:cd00839    80 ADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLAKVDRSR--T 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 279 PWIITMGHRPMYCSNADLDDCTRHEsrvrkglhGKLFGLEDLFHKYGVDLEFWAHEHSYERLWPIYNYQVFNGSlESPYT 358
Cdd:cd00839   155 PWIIVMGHRPMYCSNDDDADCIEGE--------KMREALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVANSK-DNIYT 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1569289680 359 NPRGPVHIITGSAGCEELL-TPFVRKPRPWSAVRVKEYGYTRMHILNGTHMHIQQVSdDQDGKIVDDVWVVR 429
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 ...
 32-124 5.24e-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: 5.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680  32 PEQIHLSYLGEPGTMTVTWTTW-APARSEVQFGSQlSGPLPFRAHGTARAFVDGGvlRRKLYIHRVTLRKLQPGAQYVYR 110
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSWVTPsAVTSPVVQYGTS-SSALTSTATATSSTYTTGD--GGTGYIHRATLTGLEPGTTYYYR 77

                          90
                  ....*....|....*
gi 1569289680 111 CGS-SQGWSRRFRFT 124
Cdd:pfam16656  78 VGDdNGGWSEVYSFT 92
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 131-429 1.86e-128

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: 373.17  E-value: 1.86e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 131 HWSPRLAVFGDMGA---DNPKALPRLRRDTqqGMFDAVLHVGDFAYNMDQDNARVGDRFMRLIEPVAASLPYMTCPGNHE 207
Cdd:cd00839     2 DTPLKFAVFGDMGQntnNSTNTLDHLEKEL--GNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 208 QRYNFSNYKARFSMP---------GDNEGLWYSWDLGPAHIISFSTEVYFFLHYgrhLIEKQFRWLENDLQKANKNRvaR 278
Cdd:cd00839    80 ADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLAKVDRSR--T 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 279 PWIITMGHRPMYCSNADLDDCTRHEsrvrkglhGKLFGLEDLFHKYGVDLEFWAHEHSYERLWPIYNYQVFNGSlESPYT 358
Cdd:cd00839   155 PWIIVMGHRPMYCSNDDDADCIEGE--------KMREALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVANSK-DNIYT 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1569289680 359 NPRGPVHIITGSAGCEELL-TPFVRKPRPWSAVRVKEYGYTRMHILNGTHMHIQQVSdDQDGKIVDDVWVVR 429
Cdd:cd00839   226 NPKGPVHIVIGAAGNDEGLdDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVR-NQDGQVADSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 32-427 1.39e-46

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 166.01  E-value: 1.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680  32 PEQIHLSYLGePGTMTVTWTTWAPARSEVQFGSqLSGPLPFRAHGTARAFvDGGVLRRKLYIHRVTLRKLQPGAQYVYRC 111
Cdd:PLN02533   44 PDQVHISLVG-PDKMRISWITQDSIPPSVVYGT-VSGKYEGSANGTSSSY-HYLLIYRSGQINDVVIGPLKPNTVYYYKC 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 112 G---SSQGWSrrFRFTALKNGVhwspRLAVFGDMGAD--NPKALPRLRRDTqqgmFDAVLHVGDFAY-NMDQDnarVGDR 185
Cdd:PLN02533  121 GgpsSTQEFS--FRTPPSKFPI----KFAVSGDLGTSewTKSTLEHVSKWD----YDVFILPGDLSYaNFYQP---LWDT 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 186 FMRLIEPVAASLPYMTCPGNHE-------QRYNFSNYKARFSMP----GDNEGLWYSWDLGPAHIISFSTEVYFflhygr 254
Cdd:PLN02533  188 FGRLVQPLASQRPWMVTHGNHElekipilHPEKFTAYNARWRMPfeesGSTSNLYYSFNVYGVHIIMLGSYTDF------ 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 255 HLIEKQFRWLENDLQKANKNRVarPWIITMGHRPMYCSNadlddcTRHESrvRKGLHGKLFGLEDLFHKYGVDLEFWAHE 334
Cdd:PLN02533  262 EPGSEQYQWLENNLKKIDRKTT--PWVVAVVHAPWYNSN------EAHQG--EKESVGMKESMETLLYKARVDLVFAGHV 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 335 HSYERLWPIYNYQvfngslespyTNPRGPVHIITGSAGCEELLTPFVRKPRP-WSAVRVKEYGYTRMHILNGTHMHIQ-Q 412
Cdd:PLN02533  332 HAYERFDRVYQGK----------TDKCGPVYITIGDGGNREGLATKYIDPKPdISLFREASFGHGQLNVVDANTMEWTwH 401

                         410
                  ....*....|....*
gi 1569289680 413 VSDDQDGKIVDDVWV 427
Cdd:PLN02533  402 RNDDDQSVASDSVWL 416
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
135-362 3.48e-24

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 100.15  E-value: 3.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 135 RLAVFGDM------GADNPKALPRLRRDTQQGMFDAVLHVGDFAYNMDQDNARVGDRFMRLIEpvaasLPYMTCPGNHEQ 208
Cdd:COG1409     2 RFAHISDLhlgapdGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG-----VPVYVVPGNHDI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 209 RYNFS-NYKARFSMPgDNEGLWYSWDLGPAHIISFSTEVYffLHYGRHLIEKQFRWLENDLQKAnknrvARPWIITMGHR 287
Cdd:COG1409    77 RAAMAeAYREYFGDL-PPGGLYYSFDYGGVRFIGLDSNVP--GRSSGELGPEQLAWLEEELAAA-----PAKPVIVFLHH 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1569289680 288 PMYCSNADLDdctrhesrvRKGLHGKlFGLEDLFHKYGVDLEFWAHEHSYERLWPIYNYQVFNGSLESPYTNPRG 362
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 ...
 32-124 5.24e-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: 5.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680  32 PEQIHLSYLGEPGTMTVTWTTW-APARSEVQFGSQlSGPLPFRAHGTARAFVDGGvlRRKLYIHRVTLRKLQPGAQYVYR 110
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSWVTPsAVTSPVVQYGTS-SSALTSTATATSSTYTTGD--GGTGYIHRATLTGLEPGTTYYYR 77

                          90
                  ....*....|....*
gi 1569289680 111 CGS-SQGWSRRFRFT 124
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 ...
 362-423 4.44e-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: 4.44e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1569289680 362 GPVHIITGSAGCEEllTPFVRKPRPWSAVRVKEYGYTRMHILNGTHMHIQQVSDDqDGKIVD 423
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; ...
 131-429 1.86e-128

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: 373.17  E-value: 1.86e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 131 HWSPRLAVFGDMGA---DNPKALPRLRRDTqqGMFDAVLHVGDFAYNMDQDNARVGDRFMRLIEPVAASLPYMTCPGNHE 207
Cdd:cd00839     2 DTPLKFAVFGDMGQntnNSTNTLDHLEKEL--GNYDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNHE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 208 QRYNFSNYKARFSMP---------GDNEGLWYSWDLGPAHIISFSTEVYFFLHYgrhLIEKQFRWLENDLQKANKNRvaR 278
Cdd:cd00839    80 ADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLAKVDRSR--T 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 279 PWIITMGHRPMYCSNADLDDCTRHEsrvrkglhGKLFGLEDLFHKYGVDLEFWAHEHSYERLWPIYNYQVFNGSlESPYT 358
Cdd:cd00839   155 PWIIVMGHRPMYCSNDDDADCIEGE--------KMREALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVANSK-DNIYT 225

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1569289680 359 NPRGPVHIITGSAGCEELL-TPFVRKPRPWSAVRVKEYGYTRMHILNGTHMHIQQVSdDQDGKIVDDVWVVR 429
Cdd:cd00839   226 NPKGPVHIVIGAAGNDEGLdDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVR-NQDGQVADSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 32-427 1.39e-46

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 166.01  E-value: 1.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680  32 PEQIHLSYLGePGTMTVTWTTWAPARSEVQFGSqLSGPLPFRAHGTARAFvDGGVLRRKLYIHRVTLRKLQPGAQYVYRC 111
Cdd:PLN02533   44 PDQVHISLVG-PDKMRISWITQDSIPPSVVYGT-VSGKYEGSANGTSSSY-HYLLIYRSGQINDVVIGPLKPNTVYYYKC 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 112 G---SSQGWSrrFRFTALKNGVhwspRLAVFGDMGAD--NPKALPRLRRDTqqgmFDAVLHVGDFAY-NMDQDnarVGDR 185
Cdd:PLN02533  121 GgpsSTQEFS--FRTPPSKFPI----KFAVSGDLGTSewTKSTLEHVSKWD----YDVFILPGDLSYaNFYQP---LWDT 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 186 FMRLIEPVAASLPYMTCPGNHE-------QRYNFSNYKARFSMP----GDNEGLWYSWDLGPAHIISFSTEVYFflhygr 254
Cdd:PLN02533  188 FGRLVQPLASQRPWMVTHGNHElekipilHPEKFTAYNARWRMPfeesGSTSNLYYSFNVYGVHIIMLGSYTDF------ 261

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 255 HLIEKQFRWLENDLQKANKNRVarPWIITMGHRPMYCSNadlddcTRHESrvRKGLHGKLFGLEDLFHKYGVDLEFWAHE 334
Cdd:PLN02533  262 EPGSEQYQWLENNLKKIDRKTT--PWVVAVVHAPWYNSN------EAHQG--EKESVGMKESMETLLYKARVDLVFAGHV 331

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 335 HSYERLWPIYNYQvfngslespyTNPRGPVHIITGSAGCEELLTPFVRKPRP-WSAVRVKEYGYTRMHILNGTHMHIQ-Q 412
Cdd:PLN02533  332 HAYERFDRVYQGK----------TDKCGPVYITIGDGGNREGLATKYIDPKPdISLFREASFGHGQLNVVDANTMEWTwH 401

                         410
                  ....*....|....*
gi 1569289680 413 VSDDQDGKIVDDVWV 427
Cdd:PLN02533  402 RNDDDQSVASDSVWL 416
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
135-362 3.48e-24

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 100.15  E-value: 3.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 135 RLAVFGDM------GADNPKALPRLRRDTQQGMFDAVLHVGDFAYNMDQDNARVGDRFMRLIEpvaasLPYMTCPGNHEQ 208
Cdd:COG1409     2 RFAHISDLhlgapdGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG-----VPVYVVPGNHDI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 209 RYNFS-NYKARFSMPgDNEGLWYSWDLGPAHIISFSTEVYffLHYGRHLIEKQFRWLENDLQKAnknrvARPWIITMGHR 287
Cdd:COG1409    77 RAAMAeAYREYFGDL-PPGGLYYSFDYGGVRFIGLDSNVP--GRSSGELGPEQLAWLEEELAAA-----PAKPVIVFLHH 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1569289680 288 PMYCSNADLDdctrhesrvRKGLHGKlFGLEDLFHKYGVDLEFWAHEHSYERLWPIYNYQVFNGSLESPYTNPRG 362
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 ...
 32-124 5.24e-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: 5.24e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680  32 PEQIHLSYLGEPGTMTVTWTTW-APARSEVQFGSQlSGPLPFRAHGTARAFVDGGvlRRKLYIHRVTLRKLQPGAQYVYR 110
Cdd:pfam16656   1 PEQVHLSLTGDSTSMTVSWVTPsAVTSPVVQYGTS-SSALTSTATATSSTYTTGD--GGTGYIHRATLTGLEPGTTYYYR 77

                          90
                  ....*....|....*
gi 1569289680 111 CGS-SQGWSRRFRFT 124
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 ...
 362-423 4.44e-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: 4.44e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1569289680 362 GPVHIITGSAGCEEllTPFVRKPRPWSAVRVKEYGYTRMHILNGTHMHIQQVSDDqDGKIVD 423
Cdd:pfam14008   1 APVHIVIGAAGNIE--GLFVPPQPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSD-DGTVLD 59
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 135-241 1.04e-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: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 135 RLAVFGDMG-----ADNPKALPRLRRDTQqgmFDAVLHVGDFAYNMDQDnarvgDRFMRLIEPVAASLPYMTCPGNHEQR 209
Cdd:pfam00149   2 RILVIGDLHlpgqlDDLLELLKKLLEEGK---PDLVLHAGDLVDRGPPS-----EEVLELLERLIKYVPVYLVRGNHDFD 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1569289680 210 Y----NFSNYKARFSMPGDNEGLWYSWdLGPAHIIS 241
Cdd:pfam00149  74 YgeclRLYPYLGLLARPWKRFLEVFNF-LPLAGILS 108
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 159-297 2.62e-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: 51.51  E-value: 2.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 159 QGMFDAVLHVGDFAynmdqDNARVG--DRFMRLIEPVAAslPYMTCPGNHEQRYNFsnYKARFSMP-GDNEGLWYSWDLG 235
Cdd:cd07402    37 HPRPDLVVVTGDLS-----DDGSPEsyERLRELLAPLPA--PVYWIPGNHDDRAAM--REALPEPPyDDNGPVQYVVDFG 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1569289680 236 PAHIISFSTEVYFFLHYgrHLIEKQFRWLENDLQKANKnrvaRPWIITMGHRPMYCSNADLD 297
Cdd:cd07402   108 GWRLILLDTSVPGVHHG--ELSDEQLDWLEAALAEAPD----RPTLIFLHHPPFPLGIPWMD 163
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 157-295 6.62e-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: 47.33  E-value: 6.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 157 TQQGMFDAVLHVGDFaynMDQDNARvgDRFMRLIEPV-----AASLPYMTCPGNHEqRYNFS-NYKARFSMPGDNEGLWY 230
Cdd:cd07396    42 NRESNLAFVVQLGDI---IDGYNAK--DRSKEALDAVlsildRLKGPVHHVLGNHE-FYNFPrEYLNHLKTLNGEDAYYY 115

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1569289680 231 SWDLGPahiiSFSTEVYFFLHYGRHLIEKQFRWLENDLQ--KANKNRVarpwiITMGHRPMYCSNAD 295
Cdd:cd07396   116 SFSPGP----GFRFLVLDFVKFNGGIGEEQLAWLRNELTsaDANGEKV-----IVLSHLPIYPEAAD 173
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 135-338 9.58e-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: 43.85  E-value: 9.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 135 RLAVFGDMGA-DNPKALPRLRrDTQQGM--------FDAVLHVGD-FAYNMDQDnarVGD-RFMRLIEPV--AASL--PY 199
Cdd:cd07378     2 RFLVLGDWGGkPNPYTTAAQS-LVAKQMakvasklgIDFILSLGDnFYDDGVKD---VDDpRFQETFEDVysAPSLqvPW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 200 MTCPGNHEQRYNFS---------NYKaRFSMPgdneGLWY--SWdlgpaHIISFSTEVYFFL--------HYGRH----- 255
Cdd:cd07378    78 YLVLGNHDHRGNVSaqiaytqrpNSK-RWNFP----NYYYdiSF-----KFPSSDVTVAFIMidtvllcgNTDDEasgqp 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1569289680 256 -------LIEKQFRWLENDLQKANKNrvarpWIITMGHRPMYCSnadlddctrhesrvrkGLHGKLFGLED----LFHKY 324
Cdd:cd07378   148 rgppnkkLAETQLAWLEKQLAASKAD-----YKIVVGHYPIYSS----------------GEHGPTKCLVDillpLLKKY 206

                         250
                  ....*....|....
gi 1569289680 325 GVDLEFWAHEHSYE 338
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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