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Conserved domains on  [gi|1820917471|ref|XP_032698087|]
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acid phosphatase type 7 isoform X2 [Lontra canadensis]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 10096029)

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.-.-.-
Gene Ontology:  GO:0016787|GO:0046872
PubMed:  25837850|8003970
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; ...
 63-362 8.15e-133

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: 381.26  E-value: 8.15e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471  63 PHWSPRLAVFGDLGAENPKA---FPRLRRDTQKgmYDAVLHVGDFAYNMDQDNARVGDKFMRLIEPVAASLPYMTCPGNH 139
Cdd:cd00839     1 PDTPLKFAVFGDMGQNTNNStntLDHLEKELGN--YDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471 140 EERYNFSNYKARFSMP---------GNNEGLWYSWDLGPAHIISFSTEVYFFLSYgrhLVERQFHWLESDLQKANKNRaa 210
Cdd:cd00839    79 EADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLAKVDRSR-- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471 211 RPWIITMGHRPMYCSNADLDDCTWHEskvrkglrGKFYGLEDLFYKYGVDLQLWAHEHSYERLWPIYNYQVFNgSQEMPY 290
Cdd:cd00839   154 TPWIIVMGHRPMYCSNDDDADCIEGE--------KMREALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVAN-SKDNIY 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820917471 291 TNPRGPVHIITGSAGCEERL-TPFSLFPRPWSAVRVKEYGYTRLHILNGTHLHIQQVSdDQDGKIVDDIWVVR 362
Cdd:cd00839   225 TNPKGPVHIVIGAAGNDEGLdDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVR-NQDGQVADSFWIVK 296
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 63-362 8.15e-133

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: 381.26  E-value: 8.15e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471  63 PHWSPRLAVFGDLGAENPKA---FPRLRRDTQKgmYDAVLHVGDFAYNMDQDNARVGDKFMRLIEPVAASLPYMTCPGNH 139
Cdd:cd00839     1 PDTPLKFAVFGDMGQNTNNStntLDHLEKELGN--YDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471 140 EERYNFSNYKARFSMP---------GNNEGLWYSWDLGPAHIISFSTEVYFFLSYgrhLVERQFHWLESDLQKANKNRaa 210
Cdd:cd00839    79 EADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLAKVDRSR-- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471 211 RPWIITMGHRPMYCSNADLDDCTWHEskvrkglrGKFYGLEDLFYKYGVDLQLWAHEHSYERLWPIYNYQVFNgSQEMPY 290
Cdd:cd00839   154 TPWIIVMGHRPMYCSNDDDADCIEGE--------KMREALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVAN-SKDNIY 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820917471 291 TNPRGPVHIITGSAGCEERL-TPFSLFPRPWSAVRVKEYGYTRLHILNGTHLHIQQVSdDQDGKIVDDIWVVR 362
Cdd:cd00839   225 TNPKGPVHIVIGAAGNDEGLdDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVR-NQDGQVADSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 42-368 1.92e-35

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 134.42  E-value: 1.92e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471  42 YRCGSSQGwSRRFRFRAlknGPHWSP-RLAVFGDLG-AENPKAfprLRRDTQKGMYDAVLHVGDFAY-NMDQDnarVGDK 118
Cdd:PLN02533  118 YKCGGPSS-TQEFSFRT---PPSKFPiKFAVSGDLGtSEWTKS---TLEHVSKWDYDVFILPGDLSYaNFYQP---LWDT 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471 119 FMRLIEPVAASLPYMTCPGNHE-------ERYNFSNYKARFSMP----GNNEGLWYSWDLGPAHIISFSTEVYFFLSygr 187
Cdd:PLN02533  188 FGRLVQPLASQRPWMVTHGNHElekipilHPEKFTAYNARWRMPfeesGSTSNLYYSFNVYGVHIIMLGSYTDFEPG--- 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471 188 hlvERQFHWLESDLQKANKNRAarPWIITMGHRPMYCSNADlddctwHE-SKVRKGLRGKfygLEDLFYKYGVDLQLWAH 266
Cdd:PLN02533  265 ---SEQYQWLENNLKKIDRKTT--PWVVAVVHAPWYNSNEA------HQgEKESVGMKES---METLLYKARVDLVFAGH 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471 267 EHSYERLWPIYNYQvfngsqempyTNPRGPVHIITGSAGCEERLTPFSLFPRP-WSAVRVKEYGYTRLHILNGTHLHIQ- 344
Cdd:PLN02533  331 VHAYERFDRVYQGK----------TDKCGPVYITIGDGGNREGLATKYIDPKPdISLFREASFGHGQLNVVDANTMEWTw 400

                         330       340
                  ....*....|....*....|....
gi 1820917471 345 QVSDDQDGKIVDDIWVVRPLVDRM 368
Cdd:PLN02533  401 HRNDDDQSVASDSVWLKSLLTEPG 424
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
68-312 4.24e-26

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 104.39  E-value: 4.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471  68 RLAVFGDL------GAENPKAFPRLRRDTQKGMYDAVLHVGDFAYNMDQDNARVGDKFMRLIEpvaasLPYMTCPGNHEE 141
Cdd:COG1409     2 RFAHISDLhlgapdGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG-----VPVYVVPGNHDI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471 142 RYNFS-NYKARFSMPgNNEGLWYSWDLGPAHIISFSTEVYffLSYGRHLVERQFHWLESDLQkanknRAARPWIITMGHR 220
Cdd:COG1409    77 RAAMAeAYREYFGDL-PPGGLYYSFDYGGVRFIGLDSNVP--GRSSGELGPEQLAWLEEELA-----AAPAKPVIVFLHH 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471 221 PMYCSNADLDDCTWHESKvrkglrgkfyGLEDLFYKYGVDLQLWAHEHSYERlwpiynyqvfngsqempyTNPRGPVHII 300
Cdd:COG1409   149 PPYSTGSGSDRIGLRNAE----------ELLALLARYGVDLVLSGHVHRYER------------------TRRDGVPYIV 200

                         250
                  ....*....|..
gi 1820917471 301 TGSAGCEERLTP 312
Cdd:COG1409   201 AGSTGGQVRLPP 212
Metallophos_C pfam14008
Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of ...
 295-356 7.38e-19

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


Pssm-ID: 464064 [Multi-domain]  Cd Length: 60  Bit Score: 79.49  E-value: 7.38e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820917471 295 GPVHIITGSAGCEERLTPFSlfPRPWSAVRVKEYGYTRLHILNGTHLHIQQVSDDqDGKIVD 356
Cdd:pfam14008   1 APVHIVIGAAGNIEGLFVPP--QPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSD-DGTVLD 59
 
Name Accession Description Interval E-value
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 63-362 8.15e-133

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: 381.26  E-value: 8.15e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471  63 PHWSPRLAVFGDLGAENPKA---FPRLRRDTQKgmYDAVLHVGDFAYNMDQDNARVGDKFMRLIEPVAASLPYMTCPGNH 139
Cdd:cd00839     1 PDTPLKFAVFGDMGQNTNNStntLDHLEKELGN--YDAIIHVGDIAYADGYNNGSRWDTFMRQIEPLASYVPYMVAPGNH 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471 140 EERYNFSNYKARFSMP---------GNNEGLWYSWDLGPAHIISFSTEVYFFLSYgrhLVERQFHWLESDLQKANKNRaa 210
Cdd:cd00839    79 EADYNGSTSKIKFFMPgrgmppspsGSTENLWYSFDVGPVHFISLSTETDFLKGD---NISPQYDWLEADLAKVDRSR-- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471 211 RPWIITMGHRPMYCSNADLDDCTWHEskvrkglrGKFYGLEDLFYKYGVDLQLWAHEHSYERLWPIYNYQVFNgSQEMPY 290
Cdd:cd00839   154 TPWIIVMGHRPMYCSNDDDADCIEGE--------KMREALEDLFYKYGVDLVLSGHVHAYERTCPVYNNTVAN-SKDNIY 224

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820917471 291 TNPRGPVHIITGSAGCEERL-TPFSLFPRPWSAVRVKEYGYTRLHILNGTHLHIQQVSdDQDGKIVDDIWVVR 362
Cdd:cd00839   225 TNPKGPVHIVIGAAGNDEGLdDAFSYPQPEWSAFRSSDFGFGRLTVHNETHLYFEWVR-NQDGQVADSFWIVK 296
PLN02533 PLN02533
probable purple acid phosphatase
 42-368 1.92e-35

probable purple acid phosphatase


Pssm-ID: 215292 [Multi-domain]  Cd Length: 427  Bit Score: 134.42  E-value: 1.92e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471  42 YRCGSSQGwSRRFRFRAlknGPHWSP-RLAVFGDLG-AENPKAfprLRRDTQKGMYDAVLHVGDFAY-NMDQDnarVGDK 118
Cdd:PLN02533  118 YKCGGPSS-TQEFSFRT---PPSKFPiKFAVSGDLGtSEWTKS---TLEHVSKWDYDVFILPGDLSYaNFYQP---LWDT 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471 119 FMRLIEPVAASLPYMTCPGNHE-------ERYNFSNYKARFSMP----GNNEGLWYSWDLGPAHIISFSTEVYFFLSygr 187
Cdd:PLN02533  188 FGRLVQPLASQRPWMVTHGNHElekipilHPEKFTAYNARWRMPfeesGSTSNLYYSFNVYGVHIIMLGSYTDFEPG--- 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471 188 hlvERQFHWLESDLQKANKNRAarPWIITMGHRPMYCSNADlddctwHE-SKVRKGLRGKfygLEDLFYKYGVDLQLWAH 266
Cdd:PLN02533  265 ---SEQYQWLENNLKKIDRKTT--PWVVAVVHAPWYNSNEA------HQgEKESVGMKES---METLLYKARVDLVFAGH 330

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471 267 EHSYERLWPIYNYQvfngsqempyTNPRGPVHIITGSAGCEERLTPFSLFPRP-WSAVRVKEYGYTRLHILNGTHLHIQ- 344
Cdd:PLN02533  331 VHAYERFDRVYQGK----------TDKCGPVYITIGDGGNREGLATKYIDPKPdISLFREASFGHGQLNVVDANTMEWTw 400

                         330       340
                  ....*....|....*....|....
gi 1820917471 345 QVSDDQDGKIVDDIWVVRPLVDRM 368
Cdd:PLN02533  401 HRNDDDQSVASDSVWLKSLLTEPG 424
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
68-312 4.24e-26

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 104.39  E-value: 4.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471  68 RLAVFGDL------GAENPKAFPRLRRDTQKGMYDAVLHVGDFAYNMDQDNARVGDKFMRLIEpvaasLPYMTCPGNHEE 141
Cdd:COG1409     2 RFAHISDLhlgapdGSDTAEVLAAALADINAPRPDFVVVTGDLTDDGEPEEYAAAREILARLG-----VPVYVVPGNHDI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471 142 RYNFS-NYKARFSMPgNNEGLWYSWDLGPAHIISFSTEVYffLSYGRHLVERQFHWLESDLQkanknRAARPWIITMGHR 220
Cdd:COG1409    77 RAAMAeAYREYFGDL-PPGGLYYSFDYGGVRFIGLDSNVP--GRSSGELGPEQLAWLEEELA-----AAPAKPVIVFLHH 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471 221 PMYCSNADLDDCTWHESKvrkglrgkfyGLEDLFYKYGVDLQLWAHEHSYERlwpiynyqvfngsqempyTNPRGPVHII 300
Cdd:COG1409   149 PPYSTGSGSDRIGLRNAE----------ELLALLARYGVDLVLSGHVHRYER------------------TRRDGVPYIV 200

                         250
                  ....*....|..
gi 1820917471 301 TGSAGCEERLTP 312
Cdd:COG1409   201 AGSTGGQVRLPP 212
Metallophos_C pfam14008
Iron/zinc purple acid phosphatase-like protein C; This domain is found at the C-terminus of ...
 295-356 7.38e-19

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


Pssm-ID: 464064 [Multi-domain]  Cd Length: 60  Bit Score: 79.49  E-value: 7.38e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820917471 295 GPVHIITGSAGCEERLTPFSlfPRPWSAVRVKEYGYTRLHILNGTHLHIQQVSDDqDGKIVD 356
Cdd:pfam14008   1 APVHIVIGAAGNIEGLFVPP--QPPWSAFRDTDYGYGRLTVHNRTHLTWEFVRSD-DGTVLD 59
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 68-174 4.89e-08

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: 50.67  E-value: 4.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471  68 RLAVFGDLG-----AENPKAFPRLRRDTQKgmyDAVLHVGDFAYNMDQDnarvgDKFMRLIEPVAASLPYMTCPGNHE-- 140
Cdd:pfam00149   2 RILVIGDLHlpgqlDDLLELLKKLLEEGKP---DLVLHAGDLVDRGPPS-----EEVLELLERLIKYVPVYLVRGNHDfd 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1820917471 141 --ERYNFSNYKARFSMPGNNEGLWYSWdLGPAHIIS 174
Cdd:pfam00149  74 ygECLRLYPYLGLLARPWKRFLEVFNF-LPLAGILS 108
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 96-230 6.93e-07

Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ (glycerophosphodiesterase Q, also known as Rv0805 in Mycobacterium tuberculosis) is a binuclear metallophosphoesterase from Enterobacter aerogenes that catalyzes the hydrolysis of mono-, di-, and triester substrates, including some organophosphate pesticides and products of the degradation of nerve agents. The GpdQ homolog, Rv0805, has 2',3'-cyclic nucleotide phosphodiesterase activity. GpdQ and Rv0805 belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 49.97  E-value: 6.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471  96 DAVLHVGDFAynmdqDNARVG--DKFMRLIEPVAAslPYMTCPGNHEERYNFsnYKARFSMP-GNNEGLWYSWDLGPAHI 172
Cdd:cd07402    41 DLVVVTGDLS-----DDGSPEsyERLRELLAPLPA--PVYWIPGNHDDRAAM--REALPEPPyDDNGPVQYVVDFGGWRL 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1820917471 173 ISFSTEVYFFlSYGRhLVERQFHWLESDLqkanKNRAARPWIITMGHRPMYCSNADLD 230
Cdd:cd07402   112 ILLDTSVPGV-HHGE-LSDEQLDWLEAAL----AEAPDRPTLIFLHHPPFPLGIPWMD 163
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 90-228 1.97e-04

Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known as LOC56985) is an uncharacterized Homo sapiens protein with a domain that belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277341 [Multi-domain]  Cd Length: 245  Bit Score: 42.32  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471  90 TQKGMYDAVLHVGDF--AYNMDQDNARVGDKFMRLIEpvAASLPYMTCPGNHEeRYNFS-NYKARFSMPGNNEGLWYSWD 166
Cdd:cd07396    42 NRESNLAFVVQLGDIidGYNAKDRSKEALDAVLSILD--RLKGPVHHVLGNHE-FYNFPrEYLNHLKTLNGEDAYYYSFS 118

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1820917471 167 LGPahiiSFSTEVYFFLSYGRHLVERQFHWLESDLQKANKNRAArpwIITMGHRPMYCSNAD 228
Cdd:cd07396   119 PGP----GFRFLVLDFVKFNGGIGEEQLAWLRNELTSADANGEK---VIVLSHLPIYPEAAD 173
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 68-309 1.13e-03

Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277324 [Multi-domain]  Cd Length: 286  Bit Score: 40.39  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471  68 RLAVFGDLGAENPKAFPRLRRDTQKGM--------YDAVLHVGD-FAYNMDQDnarVGDK-FMRLIEPV--AASL--PYM 133
Cdd:cd07378     2 RFLVLGDWGGKPNPYTTAAQSLVAKQMakvasklgIDFILSLGDnFYDDGVKD---VDDPrFQETFEDVysAPSLqvPWY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471 134 TCPGNHEERYNFS---------NYKaRFSMPGnnegLWY--SWdlgpaHIISFSTEVYFFL--------SYGRH------ 188
Cdd:cd07378    79 LVLGNHDHRGNVSaqiaytqrpNSK-RWNFPN----YYYdiSF-----KFPSSDVTVAFIMidtvllcgNTDDEasgqpr 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1820917471 189 ------LVERQFHWLESDLQKANKNraarpWIITMGHRPMYcSNAdlddctwhESKVRKGLRgkfYGLEDLFYKYGVDLQ 262
Cdd:cd07378   149 gppnkkLAETQLAWLEKQLAASKAD-----YKIVVGHYPIY-SSG--------EHGPTKCLV---DILLPLLKKYKVDAY 211

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1820917471 263 LWAHEHsyerlwpiyNYQVFNGSQEMPYtnprgpvhIITGSAGCEER 309
Cdd:cd07378   212 LSGHDH---------NLQHIVDESGTYY--------VISGAGSKADP 241
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
68-140 4.29e-03

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 38.07  E-value: 4.29e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820917471  68 RLAVFGDLgAENPKAFPRLRRDTQKGMYDAVLHVGDFAYNMDQDNARvgdKFMRLIEpvAASLPYMTCPGNHE 140
Cdd:COG2129     1 KILAVSDL-HGNFDLLEKLLELARAEDADLVILAGDLTDFGTAEEAR---EVLEELA--ALGVPVLAVPGNHD 67
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 70-140 5.99e-03

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 36.48  E-value: 5.99e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1820917471  70 AVFGDL--GAENPKAFPRLRRDTQKGmYDAVLHVGDFAYNMDQDNARVGdkfmRLIEPVAASLPYMTCPGNHE 140
Cdd:cd00838     1 LVISDIhgNLEALEAVLEAALAKAEK-PDLVICLGDLVDYGPDPEEVEL----KALRLLLAGIPVYVVPGNHD 68
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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