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Conserved domains on  [gi|6680624|ref|NP_031414|]
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tartrate-resistant acid phosphatase type 5 precursor [Mus musculus]

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

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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 ...
 28-313 2.70e-159

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: 446.39  E-value: 2.70e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624   28 LRFVAVGDWGGVPNaPFHTAREMANAKEIARTVQTMGADFIMSLGDNFYFTGVHDASDKRFQETFEDVFSDRALrNIPWY 107
Cdd:cd07378   1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWY 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624  108 VLAGNHDHLGNVSAQIAYSKI--SKRWNFPSPYYRLRFKIPRTNITVAIFMLDTVMLCGNSDDFASQQPKMPRDLGVART 185
Cdd:cd07378  79 LVLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624  186 QLSWLKKQLAAAKEDYVLVAGHYPIWSIAEHGPTRCLVKNLRPLLATYGVTAYLCGHDHNLQYLQDENGVGYVLSGAGNF 265
Cdd:cd07378 159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 6680624  266 MDPSVRHQRKVPNGYLRFHYGSEDSLGGFTHVEISPKEMTIIYVEASG 313
Cdd:cd07378 239 ADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
 
Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 28-313 2.70e-159

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: 446.39  E-value: 2.70e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624   28 LRFVAVGDWGGVPNaPFHTAREMANAKEIARTVQTMGADFIMSLGDNFYFTGVHDASDKRFQETFEDVFSDRALrNIPWY 107
Cdd:cd07378   1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWY 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624  108 VLAGNHDHLGNVSAQIAYSKI--SKRWNFPSPYYRLRFKIPRTNITVAIFMLDTVMLCGNSDDFASQQPKMPRDLGVART 185
Cdd:cd07378  79 LVLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624  186 QLSWLKKQLAAAKEDYVLVAGHYPIWSIAEHGPTRCLVKNLRPLLATYGVTAYLCGHDHNLQYLQDENGVGYVLSGAGNF 265
Cdd:cd07378 159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 6680624  266 MDPSVRHQRKVPNGYLRFHYGSEDSLGGFTHVEISPKEMTIIYVEASG 313
Cdd:cd07378 239 ADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
28-284 3.54e-27

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 106.31  E-value: 3.54e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624   28 LRFVAVGDWGGVPNAPFHTAREMANAkeiARTVQTMGADFIMSLGDNfyftgVHDASDKRFQEtFEDVFSDRalrNIPWY 107
Cdd:COG1409   1 FRFAHISDLHLGAPDGSDTAEVLAAA---LADINAPRPDFVVVTGDL-----TDDGEPEEYAA-AREILARL---GVPVY 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624  108 VLAGNHDHLGNVSAqiAYSKISKRWNFPSPYYRLRFKiprtniTVAIFMLDTVMLCGNSDDfasqqpkmprdlgVARTQL 187
Cdd:COG1409  69 VVPGNHDIRAAMAE--AYREYFGDLPPGGLYYSFDYG------GVRFIGLDSNVPGRSSGE-------------LGPEQL 127

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624  188 SWLKKQLAAAKEDYVLVAGHYPIWSIAEHGPTRCLV--KNLRPLLATYGVTAYLCGHDHNlQYLQDENGVGYVLSgagnf 265
Cdd:COG1409 128 AWLEEELAAAPAKPVIVFLHHPPYSTGSGSDRIGLRnaEELLALLARYGVDLVLSGHVHR-YERTRRDGVPYIVA----- 201

                       250
                ....*....|....*....
gi 6680624  266 mdPSVRHQRKVPNGYLRFH 284
Cdd:COG1409 202 --GSTGGQVRLPPGYRVIE 218
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 28-263 1.87e-17

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 82.18  E-value: 1.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624    28 LRFVAVGDWGGVPNApfhtarEMANAKEIARTVQTMGADFIMSLGDNFyFTGVHDASDKRFQETFEDVFSDRA-LRNIPW 106
Cdd:PTZ00422  27 LRFASLGNWGTGSKQ------QKLVASYLKQYAKNERVTFLVSPGSNF-PGGVDGLNDPKWKHCFENVYSEESgDMQIPF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624   107 YVLAGNHDHLGNVSAQ----------------IAYSKISK---RWNFPSPYYRL-----------RFKIPRTNITVAIFM 156
Cdd:PTZ00422 100 FTVLGQADWDGNYNAEllkgqnvylnghgqtdIEYDSNNDiypKWIMPNYWYHYfthftdtsgpsLLKSGHKDMSVAFIF 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624   157 LDTVMLcgnsddfASQQPkmprDLGVARTQLSWLKKQLAAAKE--DYVLVAGHYPIWSiaeHGPTRC---LVKNLRPLLA 231
Cdd:PTZ00422 180 IDTWIL-------SSSFP----YKKVSERAWQDLKATLEYAPKiaDYIIVVGDKPIYS---SGSSKGdsyLSYYLLPLLK 245

                        250       260       270
                 ....*....|....*....|....*....|..
gi 6680624   232 TYGVTAYLCGHDHNLqYLQDENGVGYVLSGAG 263
Cdd:PTZ00422 246 DAQVDLYISGYDRNM-EVLTDEGTAHINCGSG 276
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 28-139 6.05e-04

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: 39.12  E-value: 6.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624     28 LRFVAVGDWGGVPNAPfhtaremANAKEIARTVQTMGADFIMSLGDNFYftgvHDASDKRFQETFEdvfsdRALRNIPWY 107
Cdd:pfam00149   1 MRILVIGDLHLPGQLD-------DLLELLKKLLEEGKPDLVLHAGDLVD----RGPPSEEVLELLE-----RLIKYVPVY 64

                          90       100       110
                  ....*....|....*....|....*....|....
gi 6680624    108 VLAGNHD--HLGNVSAQIAYSKISKRWNFPSPYY 139
Cdd:pfam00149  65 LVRGNHDfdYGECLRLYPYLGLLARPWKRFLEVF 98
 
Name Accession Description Interval E-value
MPP_ACP5 cd07378
Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid ...
 28-313 2.70e-159

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: 446.39  E-value: 2.70e-159
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624   28 LRFVAVGDWGGVPNaPFHTAREMANAKEIARTVQTMGADFIMSLGDNFYFTGVHDASDKRFQETFEDVFSDRALrNIPWY 107
Cdd:cd07378   1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWY 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624  108 VLAGNHDHLGNVSAQIAYSKI--SKRWNFPSPYYRLRFKIPRTNITVAIFMLDTVMLCGNSDDFASQQPKMPRDLGVART 185
Cdd:cd07378  79 LVLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624  186 QLSWLKKQLAAAKEDYVLVAGHYPIWSIAEHGPTRCLVKNLRPLLATYGVTAYLCGHDHNLQYLQDENGVGYVLSGAGNF 265
Cdd:cd07378 159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 6680624  266 MDPSVRHQRKVPNGYLRFHYGSEDSLGGFTHVEISPKEMTIIYVEASG 313
Cdd:cd07378 239 ADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
28-284 3.54e-27

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 106.31  E-value: 3.54e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624   28 LRFVAVGDWGGVPNAPFHTAREMANAkeiARTVQTMGADFIMSLGDNfyftgVHDASDKRFQEtFEDVFSDRalrNIPWY 107
Cdd:COG1409   1 FRFAHISDLHLGAPDGSDTAEVLAAA---LADINAPRPDFVVVTGDL-----TDDGEPEEYAA-AREILARL---GVPVY 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624  108 VLAGNHDHLGNVSAqiAYSKISKRWNFPSPYYRLRFKiprtniTVAIFMLDTVMLCGNSDDfasqqpkmprdlgVARTQL 187
Cdd:COG1409  69 VVPGNHDIRAAMAE--AYREYFGDLPPGGLYYSFDYG------GVRFIGLDSNVPGRSSGE-------------LGPEQL 127

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624  188 SWLKKQLAAAKEDYVLVAGHYPIWSIAEHGPTRCLV--KNLRPLLATYGVTAYLCGHDHNlQYLQDENGVGYVLSgagnf 265
Cdd:COG1409 128 AWLEEELAAAPAKPVIVFLHHPPYSTGSGSDRIGLRnaEELLALLARYGVDLVLSGHVHR-YERTRRDGVPYIVA----- 201

                       250
                ....*....|....*....
gi 6680624  266 mdPSVRHQRKVPNGYLRFH 284
Cdd:COG1409 202 --GSTGGQVRLPPGYRVIE 218
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 28-263 1.87e-17

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 82.18  E-value: 1.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624    28 LRFVAVGDWGGVPNApfhtarEMANAKEIARTVQTMGADFIMSLGDNFyFTGVHDASDKRFQETFEDVFSDRA-LRNIPW 106
Cdd:PTZ00422  27 LRFASLGNWGTGSKQ------QKLVASYLKQYAKNERVTFLVSPGSNF-PGGVDGLNDPKWKHCFENVYSEESgDMQIPF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624   107 YVLAGNHDHLGNVSAQ----------------IAYSKISK---RWNFPSPYYRL-----------RFKIPRTNITVAIFM 156
Cdd:PTZ00422 100 FTVLGQADWDGNYNAEllkgqnvylnghgqtdIEYDSNNDiypKWIMPNYWYHYfthftdtsgpsLLKSGHKDMSVAFIF 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624   157 LDTVMLcgnsddfASQQPkmprDLGVARTQLSWLKKQLAAAKE--DYVLVAGHYPIWSiaeHGPTRC---LVKNLRPLLA 231
Cdd:PTZ00422 180 IDTWIL-------SSSFP----YKKVSERAWQDLKATLEYAPKiaDYIIVVGDKPIYS---SGSSKGdsyLSYYLLPLLK 245

                        250       260       270
                 ....*....|....*....|....*....|..
gi 6680624   232 TYGVTAYLCGHDHNLqYLQDENGVGYVLSGAG 263
Cdd:PTZ00422 246 DAQVDLYISGYDRNM-EVLTDEGTAHINCGSG 276
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 65-258 1.41e-11

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: 63.50  E-value: 1.41e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624   65 ADFIMSLGDnfyfTGVHDASDKRFQETFEDVFSDRALRNIPWYVLAGNHDhLGNVSAQiaYSKISKRWN-FPSPYYRLRf 143
Cdd:cd07396  47 LAFVVQLGD----IIDGYNAKDRSKEALDAVLSILDRLKGPVHHVLGNHE-FYNFPRE--YLNHLKTLNgEDAYYYSFS- 118

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624  144 kiPRTNITVaiFMLDTVMLCGnsddfasqqpkmprdlGVARTQLSWLKKQL--AAAKEDYVLVAGHYPIWSIAEHGptRC 221
Cdd:cd07396 119 --PGPGFRF--LVLDFVKFNG----------------GIGEEQLAWLRNELtsADANGEKVIVLSHLPIYPEAADP--QC 176

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 6680624  222 LVKNLRPLLA---TYG-VTAYLCGHDHNLQYLQDENGVGYV 258
Cdd:cd07396 177 LLWNYEEVLAileSYPcVKACFSGHNHEGGYEQDSHGVHHV 217
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 24-245 6.36e-08

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: 53.07  E-value: 6.36e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624   24 PTPTLRFVAVGDWGGVPNAPFHTAREMANAKEiartvqtmGADFIMSLGDNFYFTGvhDASDKR---FQETFEDVFSdra 100
Cdd:cd00839   1 PDTPLKFAVFGDMGQNTNNSTNTLDHLEKELG--------NYDAIIHVGDIAYADG--YNNGSRwdtFMRQIEPLAS--- 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624  101 lrNIPWYVLAGNHDhlgnvsaqIAYSkiSKRWNFPSPYYRLRFKIPRTNIT------VAIFMLDTVMLCGNSDDFASQQP 174
Cdd:cd00839  68 --YVPYMVAPGNHE--------ADYN--GSTSKIKFFMPGRGMPPSPSGSTenlwysFDVGPVHFISLSTETDFLKGDNI 135

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6680624  175 KmprdlgvarTQLSWLKKQLAAA---KEDYVLVAGHYPIWSIAEHGPTRCLVKNLR----PLLATYGVTAYLCGHDHN 245
Cdd:cd00839 136 S---------PQYDWLEADLAKVdrsRTPWIIVMGHRPMYCSNDDDADCIEGEKMRealeDLFYKYGVDLVLSGHVHA 204
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 202-261 3.72e-07

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: 48.83  E-value: 3.72e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6680624  202 VLVAGHYPIWSIAEHGPTRCLVKN---LRPLLATYGVTAYLCGHDH--NLQYLQDENGVGYVLSG 261
Cdd:cd07400  73 AIVALHHPLLPPPDTGRERNVLLDagdALKLLKELGVDLVLHGHKHvpAVWNLGLLNGIVVVNAG 137
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 71-247 2.39e-05

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: 45.05  E-value: 2.39e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624   71 LGDNFYFTGVHDASDK-RFQETFEDVFSD-RALRNIPWYVLAGNHDHLGNVSAQIA---YSKISKRwnFPSPYYRLRFKI 145
Cdd:cd07401  43 LTDNKTGNKLPSYQYQeEWQWKYYNILKEsSVINKEYLFDIRGNHDLFGIVSFDSQnnyYRKYSNT--GRDHSHSFSSTT 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624  146 PRTNITVaifmldtvmLCGNSDDFASqqPKMPRD--LGVARTQLSWLKKQLAAAKE-DYVLVAGHYPIWSIAEHGPtRCL 222
Cdd:cd07401 121 RFGNYSF---------IGFDPTIFPG--PKRPFNffGSLDKKLLDRLEKELEKSKNsKYTIWFGHYPHSLIISPSA-KSS 188

                       170       180
                ....*....|....*....|....*
gi 6680624  223 VKNLRPLLATYGVTAYLCGHDHNLQ 247
Cdd:cd07401 189 SKTFKDLLKKYNVTAYLCGHLHPLG 213
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
29-303 8.96e-05

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 43.36  E-value: 8.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624   29 RFVAVGDW--GgvpnAPFHtAREMANA-----KEIARTVQTMGADFIMSLGDNFyftgvHDAS-DKRFQETFEDVFSDRA 100
Cdd:COG0420   2 RFLHTADWhlG----KPLH-GASRREDqlaalDRLVDLAIEEKVDAVLIAGDLF-----DSANpSPEAVRLLAEALRRLS 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624  101 LRNIPWYVLAGNHDHLGnvsaqiayskiskRWNFPSPYYRlrfkipRTNITV-AIFMLDTVMLCGNSD------DFASqq 173
Cdd:COG0420  72 EAGIPVVLIAGNHDSPS-------------RLSAGSPLLE------NLGVHVfGSVEPEPVELEDGLGvavyglPYLR-- 130

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624  174 pkmPRDLGVARTQLSWLKKQLAAAKedYVLVAGHYPIWSIAEHGPTRCLVKNLRPLLATyGVTAYLCGHDHNLQYLQDEN 253
Cdd:COG0420 131 ---PSDEEALRDLLERLPRALDPGG--PNILLLHGFVAGASGSRDIYVAPVPLSALPAA-GFDYVALGHIHRPQVLGGDP 204

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 6680624  254 GVGYvlSGAgnfmdpsvrhqrkvPNGYlRFhygSEDSLGGFTHVEISPKE 303
Cdd:COG0420 205 RIRY--SGS--------------PEPR-SF---SEAGGKGVLLVELDAGG 234
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 189-259 1.14e-04

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: 41.48  E-value: 1.14e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624  189 WLKKQLAAAKEDYVLVAG-------HYPIWSIAEHG--PTRCLVKNLRPLLATYGVTAYLCGHDHNLQYLQDENGVGYVL 259
Cdd:cd00838  48 LKALRLLLAGIPVYVVPGnhdilvtHGPPYDPLDEGspGEDPGSEALLELLDKYGPDLVLSGHTHVPGRREVDKGGTLVV 127
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 100-245 1.54e-04

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


Pssm-ID: 277347 [Multi-domain]  Cd Length: 240  Bit Score: 42.65  E-value: 1.54e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624  100 ALRNIPWYVLAGNHDHlgnvsaQIAYSKIskrwnFPSPYYRLRFKIPRTNI--TVAIFMLDTVM-------LCGnsddfa 170
Cdd:cd07402  66 APLPAPVYWIPGNHDD------RAAMREA-----LPEPPYDDNGPVQYVVDfgGWRLILLDTSVpgvhhgeLSD------ 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624  171 sqqpkmprdlgvarTQLSWLKKQLAAAKEDYVLVAGHYP--IWSIAEHGPTRClvKN---LRPLLATY-GVTAYLCGHDH 244
Cdd:cd07402 129 --------------EQLDWLEAALAEAPDRPTLIFLHHPpfPLGIPWMDAIRL--RNsqaLFAVLARHpQVKAILCGHIH 192


                .
gi 6680624  245 N 245
Cdd:cd07402 193 R 193
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 64-116 2.83e-04

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: 40.33  E-value: 2.83e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 6680624   64 GADFIMSLGDNFYFTGVHDASDKRFQEtfedvfsdRALRNIPWYVLAGNHDHL 116
Cdd:cd00838  26 KPDLVICLGDLVDYGPDPEEVELKALR--------LLLAGIPVYVVPGNHDIL 70
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 28-139 6.05e-04

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: 39.12  E-value: 6.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6680624     28 LRFVAVGDWGGVPNAPfhtaremANAKEIARTVQTMGADFIMSLGDNFYftgvHDASDKRFQETFEdvfsdRALRNIPWY 107
Cdd:pfam00149   1 MRILVIGDLHLPGQLD-------DLLELLKKLLEEGKPDLVLHAGDLVD----RGPPSEEVLELLE-----RLIKYVPVY 64

                          90       100       110
                  ....*....|....*....|....*....|....
gi 6680624    108 VLAGNHD--HLGNVSAQIAYSKISKRWNFPSPYY 139
Cdd:pfam00149  65 LVRGNHDfdYGECLRLYPYLGLLARPWKRFLEVF 98
 
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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