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Conserved domains on  [gi|528481587|ref|XP_005165782|]
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tartrate-resistant acid phosphatase type 5a isoform X1 [Danio rerio]

Protein Classification

purple acid phosphatase family protein( domain architecture ID 10164501)

purple acid phosphatase (PAP) family protein is a metallophosphatase containing an active site consisting of two metal ions (usually manganese, iron, or zinc); similar to human tartrate-resistant acid phosphatase type 5 (ACP5) which is involved in osteopontin/bone sialoprotein dephosphorylation in bone matrix

CATH:  3.60.21.10
EC:  3.1.3.2
Gene Ontology:  GO:0046872|GO:0016311|GO:0003993
PubMed:  25837850|8683579|8003970

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 36-319 1.02e-163

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: 457.94  E-value: 1.02e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587  36 IRFLVLGDWGGLPNPpYVTPIETATARMMAKTASQMGADFILAVGDNFYYKGVTDVNDPRFQETFEDVYTQDSLNIPWYV 115
Cdd:cd07378    1 LRFLVLGDWGGKPNP-YTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSLQVPWYL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 116 IAGNHDHVGNVKAQIEYSQR--SKRWNFPYYYYEMNFRIPRTDSTLTIIMLDTVLLCGNSDDFLDQQPRAPRSGVLANRQ 193
Cdd:cd07378   80 VLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAETQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 194 LLWLQERLAKSKADYLLVAGHYPVWSISEHGPTDCLLKNLRPLLKKYKATAYLCGHDHNLQYIK-ESGIGYVVSGAGNFM 272
Cdd:cd07378  160 LAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVdESGTYYVISGAGSKA 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 528481587 273 DPDVRHRNRVPKGYLKFFNGDASTLGGFAHIEVDKKQMTVTFIQARG 319
Cdd:cd07378  240 DPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
 
Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 36-319 1.02e-163

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: 457.94  E-value: 1.02e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587  36 IRFLVLGDWGGLPNPpYVTPIETATARMMAKTASQMGADFILAVGDNFYYKGVTDVNDPRFQETFEDVYTQDSLNIPWYV 115
Cdd:cd07378    1 LRFLVLGDWGGKPNP-YTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSLQVPWYL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 116 IAGNHDHVGNVKAQIEYSQR--SKRWNFPYYYYEMNFRIPRTDSTLTIIMLDTVLLCGNSDDFLDQQPRAPRSGVLANRQ 193
Cdd:cd07378   80 VLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAETQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 194 LLWLQERLAKSKADYLLVAGHYPVWSISEHGPTDCLLKNLRPLLKKYKATAYLCGHDHNLQYIK-ESGIGYVVSGAGNFM 272
Cdd:cd07378  160 LAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVdESGTYYVISGAGSKA 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 528481587 273 DPDVRHRNRVPKGYLKFFNGDASTLGGFAHIEVDKKQMTVTFIQARG 319
Cdd:cd07378  240 DPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
36-319 9.72e-27

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 105.54  E-value: 9.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587  36 IRFLVLGDWGGLPNPPYVTPietATARMMAKTASQMGADFILAVGDNFYYKGVTDVNdpRFQETFEDvytqdsLNIPWYV 115
Cdd:COG1409    1 FRFAHISDLHLGAPDGSDTA---EVLAAALADINAPRPDFVVVTGDLTDDGEPEEYA--AAREILAR------LGVPVYV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 116 IAGNHDHvgnvkaqieysqrskRWNFPYYYYEmNFRIPRTDST--------LTIIMLDTVLLCGNSddfldqqpraprsG 187
Cdd:COG1409   70 VPGNHDI---------------RAAMAEAYRE-YFGDLPPGGLyysfdyggVRFIGLDSNVPGRSS-------------G 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 188 VLANRQLLWLQERLAKSKADYLLVAGHYPVWSISEHGPTDCLL--KNLRPLLKKYKATAYLCGHDHNLQYIKESGIGYVV 265
Cdd:COG1409  121 ELGPEQLAWLEEELAAAPAKPVIVFLHHPPYSTGSGSDRIGLRnaEELLALLARYGVDLVLSGHVHRYERTRRDGVPYIV 200

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528481587 266 SGAGNfmdpdvrHRNRVPKGYlkffngdastlggfAHIEVDKKQMTVTFIQARG 319
Cdd:COG1409  201 AGSTG-------GQVRLPPGY--------------RVIEVDGDGLTVEVRRVDG 233
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 6-336 6.51e-25

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 103.75  E-value: 6.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587   6 MLVFLSALPGVLCYYSSFVdleaqgsnQSSIRFLVLGDWGglpnppyvtpIETATARMMAKTASQMGAD----FILAVGD 81
Cdd:PTZ00422   5 CKLVLFSLFVLIFISSYSV--------KAQLRFASLGNWG----------TGSKQQKLVASYLKQYAKNervtFLVSPGS 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587  82 NFYYkGVTDVNDPRFQETFEDVYTQDS--LNIPWYVIAGNHDHVGNVKAQ----------------IEYSQRSK---RWN 140
Cdd:PTZ00422  67 NFPG-GVDGLNDPKWKHCFENVYSEESgdMQIPFFTVLGQADWDGNYNAEllkgqnvylnghgqtdIEYDSNNDiypKWI 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 141 FP--YYYYEMNF---------RIPRTDSTLTIIMLDTVLLcgnSDDFLDQQPRAPRSGVLaNRQLlwlqeRLAKSKADYL 209
Cdd:PTZ00422 146 MPnyWYHYFTHFtdtsgpsllKSGHKDMSVAFIFIDTWIL---SSSFPYKKVSERAWQDL-KATL-----EYAPKIADYI 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 210 LVAGHYPVWSiseHGPTDCLLK---NLRPLLKKYKATAYLCGHDHNLQYIKESGIGYVVSGAGNfmdpDVRHRNRVPKGY 286
Cdd:PTZ00422 217 IVVGDKPIYS---SGSSKGDSYlsyYLLPLLKDAQVDLYISGYDRNMEVLTDEGTAHINCGSGG----NSGRKSIMKNSK 289

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528481587 287 LKFFNGDAstlgGFAHIEVDKKQMTVTFIQA-RGTSLYRAVLKKRDDVLED 336
Cdd:PTZ00422 290 SLFYSEDI----GFCIHELNAEGMVTKFVSGnTGEVLYTHKQPLKKRKLRF 336
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 36-153 9.07e-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: 47.21  E-value: 9.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587   36 IRFLVLGDWGGLPNPPyvtpietATARMMAKTASQMGADFILAVGDNFYYkgvtDVNDPRFQETFEDVYTqdslNIPWYV 115
Cdd:pfam00149   1 MRILVIGDLHLPGQLD-------DLLELLKKLLEEGKPDLVLHAGDLVDR----GPPSEEVLELLERLIK----YVPVYL 65

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 528481587  116 IAGNHDHvgNVKAQIEYSQRSKRWNFPYYYYEMNFRIP 153
Cdd:pfam00149  66 VRGNHDF--DYGECLRLYPYLGLLARPWKRFLEVFNFL 101
 
Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 36-319 1.02e-163

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: 457.94  E-value: 1.02e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587  36 IRFLVLGDWGGLPNPpYVTPIETATARMMAKTASQMGADFILAVGDNFYYKGVTDVNDPRFQETFEDVYTQDSLNIPWYV 115
Cdd:cd07378    1 LRFLVLGDWGGKPNP-YTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSLQVPWYL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 116 IAGNHDHVGNVKAQIEYSQR--SKRWNFPYYYYEMNFRIPRTDSTLTIIMLDTVLLCGNSDDFLDQQPRAPRSGVLANRQ 193
Cdd:cd07378   80 VLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAETQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 194 LLWLQERLAKSKADYLLVAGHYPVWSISEHGPTDCLLKNLRPLLKKYKATAYLCGHDHNLQYIK-ESGIGYVVSGAGNFM 272
Cdd:cd07378  160 LAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVdESGTYYVISGAGSKA 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 528481587 273 DPDVRHRNRVPKGYLKFFNGDASTLGGFAHIEVDKKQMTVTFIQARG 319
Cdd:cd07378  240 DPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
36-319 9.72e-27

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 105.54  E-value: 9.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587  36 IRFLVLGDWGGLPNPPYVTPietATARMMAKTASQMGADFILAVGDNFYYKGVTDVNdpRFQETFEDvytqdsLNIPWYV 115
Cdd:COG1409    1 FRFAHISDLHLGAPDGSDTA---EVLAAALADINAPRPDFVVVTGDLTDDGEPEEYA--AAREILAR------LGVPVYV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 116 IAGNHDHvgnvkaqieysqrskRWNFPYYYYEmNFRIPRTDST--------LTIIMLDTVLLCGNSddfldqqpraprsG 187
Cdd:COG1409   70 VPGNHDI---------------RAAMAEAYRE-YFGDLPPGGLyysfdyggVRFIGLDSNVPGRSS-------------G 120

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 188 VLANRQLLWLQERLAKSKADYLLVAGHYPVWSISEHGPTDCLL--KNLRPLLKKYKATAYLCGHDHNLQYIKESGIGYVV 265
Cdd:COG1409  121 ELGPEQLAWLEEELAAAPAKPVIVFLHHPPYSTGSGSDRIGLRnaEELLALLARYGVDLVLSGHVHRYERTRRDGVPYIV 200

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 528481587 266 SGAGNfmdpdvrHRNRVPKGYlkffngdastlggfAHIEVDKKQMTVTFIQARG 319
Cdd:COG1409  201 AGSTG-------GQVRLPPGY--------------RVIEVDGDGLTVEVRRVDG 233
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 6-336 6.51e-25

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 103.75  E-value: 6.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587   6 MLVFLSALPGVLCYYSSFVdleaqgsnQSSIRFLVLGDWGglpnppyvtpIETATARMMAKTASQMGAD----FILAVGD 81
Cdd:PTZ00422   5 CKLVLFSLFVLIFISSYSV--------KAQLRFASLGNWG----------TGSKQQKLVASYLKQYAKNervtFLVSPGS 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587  82 NFYYkGVTDVNDPRFQETFEDVYTQDS--LNIPWYVIAGNHDHVGNVKAQ----------------IEYSQRSK---RWN 140
Cdd:PTZ00422  67 NFPG-GVDGLNDPKWKHCFENVYSEESgdMQIPFFTVLGQADWDGNYNAEllkgqnvylnghgqtdIEYDSNNDiypKWI 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 141 FP--YYYYEMNF---------RIPRTDSTLTIIMLDTVLLcgnSDDFLDQQPRAPRSGVLaNRQLlwlqeRLAKSKADYL 209
Cdd:PTZ00422 146 MPnyWYHYFTHFtdtsgpsllKSGHKDMSVAFIFIDTWIL---SSSFPYKKVSERAWQDL-KATL-----EYAPKIADYI 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 210 LVAGHYPVWSiseHGPTDCLLK---NLRPLLKKYKATAYLCGHDHNLQYIKESGIGYVVSGAGNfmdpDVRHRNRVPKGY 286
Cdd:PTZ00422 217 IVVGDKPIYS---SGSSKGDSYlsyYLLPLLKDAQVDLYISGYDRNMEVLTDEGTAHINCGSGG----NSGRKSIMKNSK 289

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 528481587 287 LKFFNGDAstlgGFAHIEVDKKQMTVTFIQA-RGTSLYRAVLKKRDDVLED 336
Cdd:PTZ00422 290 SLFYSEDI----GFCIHELNAEGMVTKFVSGnTGEVLYTHKQPLKKRKLRF 336
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 33-275 2.00e-11

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: 63.86  E-value: 2.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587  33 QSSIRFLVLGDWGGLPNppyvtpieTATARMMAKTASQMGADFILAVGD---NFYYKgvtdvNDPR---FQETFEDVYTq 106
Cdd:cd00839    2 DTPLKFAVFGDMGQNTN--------NSTNTLDHLEKELGNYDAIIHVGDiayADGYN-----NGSRwdtFMRQIEPLAS- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 107 dslNIPWYVIAGNHDhvgnvkaqIEYsqrskrWNFPYYYYE--MNFRIPRTDSTLT-------------IIMLDTVLlcg 171
Cdd:cd00839   68 ---YVPYMVAPGNHE--------ADY------NGSTSKIKFfmPGRGMPPSPSGSTenlwysfdvgpvhFISLSTET--- 127

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 172 nsdDFLDqqpraprsGVLANRQLLWLQERLAK---SKADYLLVAGHYPvWSISEHGPTDC-LLKNLR----PLLKKYKAT 243
Cdd:cd00839  128 ---DFLK--------GDNISPQYDWLEADLAKvdrSRTPWIIVMGHRP-MYCSNDDDADCiEGEKMRealeDLFYKYGVD 195

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 528481587 244 AYLCGHDHNLQ-----------------YIKESGIGYVVSG-AGNFMDPD 275
Cdd:cd00839  196 LVLSGHVHAYErtcpvynntvanskdniYTNPKGPVHIVIGaAGNDEGLD 245
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 74-254 6.91e-09

Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) is an uncharacterized Homo sapiens transmembrane protein with an N-terminal metallophosphatase domain. TMEM62 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: 277346 [Multi-domain]  Cd Length: 254  Bit Score: 55.83  E-value: 6.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587  74 DFILAVGD---NFYYKGVtdvndPRFQETFEDVYTQ-----DSLNIP---WYVIAGNHDHVGNVKAQIE------YSqRS 136
Cdd:cd07401   35 TLVLITGDltdNKTGNKL-----PSYQYQEEWQWKYynilkESSVINkeyLFDIRGNHDLFGIVSFDSQnnyyrkYS-NT 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 137 KRWNFPYYYYEMNFRiprtdsTLTIIMLDTvllcgnsddFLDQQPRAPRS--GVLANRQLLWLQERLAKSK-ADYLLVAG 213
Cdd:cd07401  109 GRDHSHSFSSTTRFG------NYSFIGFDP---------TIFPGPKRPFNffGSLDKKLLDRLEKELEKSKnSKYTIWFG 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 528481587 214 HYPVWSISEHGPTDcLLKNLRPLLKKYKATAYLCGHDHNLQ 254
Cdd:cd07401  174 HYPHSLIISPSAKS-SSKTFKDLLKKYNVTAYLCGHLHPLG 213
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 68-252 5.35e-08

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: 53.05  E-value: 5.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587  68 ASQMGADFILAVGDnfyykgVTDVNDP----RFQETFedvytqDSLNIPWYVIAGNHDHVGNVKAQIEYSQRSKRwNFPY 143
Cdd:cd07402   35 ALHPRPDLVVVTGD------LSDDGSPesyeRLRELL------APLPAPVYWIPGNHDDRAAMREALPEPPYDDN-GPVQ 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 144 YYYEmnfriprtDSTLTIIMLDTVLlcgnsddfldqqPRAPRsGVLANRQLLWLQERLAKSKADYLLVAGHYPVWSISEH 223
Cdd:cd07402  102 YVVD--------FGGWRLILLDTSV------------PGVHH-GELSDEQLDWLEAALAEAPDRPTLIFLHHPPFPLGIP 160

                        170       180       190
                 ....*....|....*....|....*....|...
gi 528481587 224 GPTDCLLKN---LRPLLKKYKATAY-LCGHDHN 252
Cdd:cd07402  161 WMDAIRLRNsqaLFAVLARHPQVKAiLCGHIHR 193
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 36-153 9.07e-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: 47.21  E-value: 9.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587   36 IRFLVLGDWGGLPNPPyvtpietATARMMAKTASQMGADFILAVGDNFYYkgvtDVNDPRFQETFEDVYTqdslNIPWYV 115
Cdd:pfam00149   1 MRILVIGDLHLPGQLD-------DLLELLKKLLEEGKPDLVLHAGDLVDR----GPPSEEVLELLERLIK----YVPVYL 65

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 528481587  116 IAGNHDHvgNVKAQIEYSQRSKRWNFPYYYYEMNFRIP 153
Cdd:pfam00149  66 VRGNHDF--DYGECLRLYPYLGLLARPWKRFLEVFNFL 101
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 165-269 4.07e-06

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: 45.72  E-value: 4.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 165 DTVLLCGnsdDFLDqqprapRSGVLANRQLLWlqERLAKSKADYLLVAG-------HYPVWSISEHG--PTDCLLKNLRP 235
Cdd:cd00838   28 DLVICLG---DLVD------YGPDPEEVELKA--LRLLLAGIPVYVVPGnhdilvtHGPPYDPLDEGspGEDPGSEALLE 96

                         90       100       110
                 ....*....|....*....|....*....|....
gi 528481587 236 LLKKYKATAYLCGHDHNLQYIKESGIGYVVSGAG 269
Cdd:cd00838   97 LLDKYGPDLVLSGHTHVPGRREVDKGGTLVVNPG 130
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 107-268 3.59e-05

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: 44.63  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 107 DSLNIPWYVIAGNHDHVGNVKAQIEYSQRSKRWNFPYYYYEMN--FRiprtdstltIIMLDTVLLCGNsddfldqqprap 184
Cdd:cd07396   78 DRLKGPVHHVLGNHEFYNFPREYLNHLKTLNGEDAYYYSFSPGpgFR---------FLVLDFVKFNGG------------ 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 185 rsgvLANRQLLWLQE--RLAKSKADYLLVAGHYPVWSISEHGptDCLLKN---LRPLLKKYKAT-AYLCGHDHNLQYIK- 257
Cdd:cd07396  137 ----IGEEQLAWLRNelTSADANGEKVIVLSHLPIYPEAADP--QCLLWNyeeVLAILESYPCVkACFSGHNHEGGYEQd 210

                        170
                 ....*....|.
gi 528481587 258 ESGIGYVVSGA 268
Cdd:cd07396  211 SHGVHHVTLEG 221
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 37-122 2.13e-04

Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 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: 277319 [Multi-domain]  Cd Length: 186  Bit Score: 41.49  E-value: 2.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587  37 RFLVLGDW--GGLPNPPyvTPIETATARM---MAKTASQMGADFILAVGDNFyykgvtDVNDP------RFQETFEDVyt 105
Cdd:cd00840    1 RFLHTADWhlGYPLYGL--SRREEDFFKAfeeIVDLAIEEKVDFVLIAGDLF------DSNNPspealkLAIEGLRRL-- 70

                         90
                 ....*....|....*..
gi 528481587 106 qDSLNIPWYVIAGNHDH 122
Cdd:cd00840   71 -CEAGIPVFVIAGNHDS 86
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 210-269 2.80e-04

Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the 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: 277345 [Multi-domain]  Cd Length: 138  Bit Score: 40.35  E-value: 2.80e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481587 210 LVAGHYPVWSISEHGPTDCLLKN---LRPLLKKYKATAYLCGHDHnLQYIKESGI--GYVVSGAG 269
Cdd:cd07400   74 IVALHHPLLPPPDTGRERNVLLDagdALKLLKELGVDLVLHGHKH-VPAVWNLGLlnGIVVVNAG 137
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
64-287 5.02e-04

DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 41.05  E-value: 5.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587  64 MAKTASQMGADFILAVGDnfyykgVTDVNDP------RFQETFEDVytqDSLNIPWYVIAGNHDHVGnvkaqieysqrsk 137
Cdd:COG0420   31 LVDLAIEEKVDAVLIAGD------LFDSANPspeavrLLAEALRRL---SEAGIPVVLIAGNHDSPS------------- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528481587 138 RWNFPYYYYE-MNFRI--PRTDSTLTIIMLDTVLLCGNSddFLDQQPRAPRSGVLAnrqllWLQERLAKSKadYLLVAGH 214
Cdd:COG0420   89 RLSAGSPLLEnLGVHVfgSVEPEPVELEDGLGVAVYGLP--YLRPSDEEALRDLLE-----RLPRALDPGG--PNILLLH 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 528481587 215 YPVWSISEHGPTDCLLKNLRPLLKKyKATAYLCGHDHNLQYIKESG-IGYvvSGAgnfmdPDVRHRN-RVPKGYL 287
Cdd:COG0420  160 GFVAGASGSRDIYVAPVPLSALPAA-GFDYVALGHIHRPQVLGGDPrIRY--SGS-----PEPRSFSeAGGKGVL 226
 
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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