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Conserved domains on  [gi|1046899426|ref|XP_017450976|]
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tartrate-resistant acid phosphatase type 5 isoform X1 [Rattus norvegicus]

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 ...
 36-321 4.61e-161

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: 451.01  E-value: 4.61e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426  36 LRFVAVGDWGGVPNaPFHTAREMANAKEIARTVQIMGADFIMSLGDNFYFTGVHDANDKRFQETFEDVFSDRALrNIPWY 115
Cdd:cd07378     1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 116 VLAGNHDHLGNVSAQIAYSKI--SKRWNFPSPYYRLRFKVPRSNITVAIFMLDTVMLCGNSDDFVSQQPEMPRDLGVART 193
Cdd:cd07378    79 LVLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 194 QLSWLKKQLAAAKEDYVLVAGHYPIWSIAEHGPTRCLVKNLRPLLAAYGVTAYLCGHDHNLQYLQDENGVGYVLSGAGNF 273
Cdd:cd07378   159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1046899426 274 MDPSVRHQRKVPNGYLRFHYGSEDSLGGFTYVEIGSKEMSITYVEASG 321
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 ...
 36-321 4.61e-161

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: 451.01  E-value: 4.61e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426  36 LRFVAVGDWGGVPNaPFHTAREMANAKEIARTVQIMGADFIMSLGDNFYFTGVHDANDKRFQETFEDVFSDRALrNIPWY 115
Cdd:cd07378     1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 116 VLAGNHDHLGNVSAQIAYSKI--SKRWNFPSPYYRLRFKVPRSNITVAIFMLDTVMLCGNSDDFVSQQPEMPRDLGVART 193
Cdd:cd07378    79 LVLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 194 QLSWLKKQLAAAKEDYVLVAGHYPIWSIAEHGPTRCLVKNLRPLLAAYGVTAYLCGHDHNLQYLQDENGVGYVLSGAGNF 273
Cdd:cd07378   159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1046899426 274 MDPSVRHQRKVPNGYLRFHYGSEDSLGGFTYVEIGSKEMSITYVEASG 321
Cdd:cd07378   239 ADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
36-292 1.56e-27

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 107.47  E-value: 1.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426  36 LRFVAVGD------WGGVPNAPFHTAREMANAKEIartvqimgaDFIMSLGDNfyftgVHDANDKRFQEtFEDVFSDRal 109
Cdd:COG1409     1 FRFAHISDlhlgapDGSDTAEVLAAALADINAPRP---------DFVVVTGDL-----TDDGEPEEYAA-AREILARL-- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 110 rNIPWYVLAGNHDHLGNVSAQIAyskisKRWNFPSP---YYRLRFKvprsniTVAIFMLDTVMLCGNSDDfvsqqpempr 186
Cdd:COG1409    64 -GVPVYVVPGNHDIRAAMAEAYR-----EYFGDLPPgglYYSFDYG------GVRFIGLDSNVPGRSSGE---------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 187 dlgVARTQLSWLKKQLAAAKEDYVLVAGHYPIWSIAEHGPTRCLV--KNLRPLLAAYGVTAYLCGHDHNlQYLQDENGVG 264
Cdd:COG1409   122 ---LGPEQLAWLEEELAAAPAKPVIVFLHHPPYSTGSGSDRIGLRnaEELLALLARYGVDLVLSGHVHR-YERTRRDGVP 197

                         250       260
                  ....*....|....*....|....*...
gi 1046899426 265 YVLSgagnfmdPSVRHQRKVPNGYLRFH 292
Cdd:COG1409   198 YIVA-------GSTGGQVRLPPGYRVIE 218
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 36-333 6.63e-18

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 83.72  E-value: 6.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426  36 LRFVAVGDWGGVPNApfhtarEMANAKEIARTVQIMGADFIMSLGDNFyFTGVHDANDKRFQETFEDVFSDRA-LRNIPW 114
Cdd:PTZ00422   27 LRFASLGNWGTGSKQ------QKLVASYLKQYAKNERVTFLVSPGSNF-PGGVDGLNDPKWKHCFENVYSEESgDMQIPF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 115 YVLAGNHDHLGNVSAQ----------------IAYSKISK---RWNFPSPYYRL-----------RFKVPRSNITVAIFM 164
Cdd:PTZ00422  100 FTVLGQADWDGNYNAEllkgqnvylnghgqtdIEYDSNNDiypKWIMPNYWYHYfthftdtsgpsLLKSGHKDMSVAFIF 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 165 LDTVMLCGN-SDDFVSQQpemprdlgvartqlSW--LKKQLAAAKE--DYVLVAGHYPIWSiaeHGPTRC---LVKNLRP 236
Cdd:PTZ00422  180 IDTWILSSSfPYKKVSER--------------AWqdLKATLEYAPKiaDYIIVVGDKPIYS---SGSSKGdsyLSYYLLP 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 237 LLAAYGVTAYLCGHDHNLqYLQDENGVGYVLSGAGNfmdpsvRHQRKVPNGYLRFHYGSEDSlgGFTYVEIGSKEMsITY 316
Cdd:PTZ00422  243 LLKDAQVDLYISGYDRNM-EVLTDEGTAHINCGSGG------NSGRKSIMKNSKSLFYSEDI--GFCIHELNAEGM-VTK 312

                         330       340
                  ....*....|....*....|.
gi 1046899426 317 VEASGK----SLFKTSLPRRP 333
Cdd:PTZ00422  313 FVSGNTgevlYTHKQPLKKRK 333
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 36-147 8.80e-05

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: 41.43  E-value: 8.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426  36 LRFVAVGDWGGVPNAPfhtaremANAKEIARTVQIMGADFIMSLGDNFYftgvHDANDKRFQETFEdvfsdRALRNIPWY 115
Cdd:pfam00149   1 MRILVIGDLHLPGQLD-------DLLELLKKLLEEGKPDLVLHAGDLVD----RGPPSEEVLELLE-----RLIKYVPVY 64

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1046899426 116 VLAGNHD--HLGNVSAQIAYSKISKRWNFPSPYY 147
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 ...
 36-321 4.61e-161

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: 451.01  E-value: 4.61e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426  36 LRFVAVGDWGGVPNaPFHTAREMANAKEIARTVQIMGADFIMSLGDNFYFTGVHDANDKRFQETFEDVFSDRALrNIPWY 115
Cdd:cd07378     1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 116 VLAGNHDHLGNVSAQIAYSKI--SKRWNFPSPYYRLRFKVPRSNITVAIFMLDTVMLCGNSDDFVSQQPEMPRDLGVART 193
Cdd:cd07378    79 LVLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 194 QLSWLKKQLAAAKEDYVLVAGHYPIWSIAEHGPTRCLVKNLRPLLAAYGVTAYLCGHDHNLQYLQDENGVGYVLSGAGNF 273
Cdd:cd07378   159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1046899426 274 MDPSVRHQRKVPNGYLRFHYGSEDSLGGFTYVEIGSKEMSITYVEASG 321
Cdd:cd07378   239 ADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
36-292 1.56e-27

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 107.47  E-value: 1.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426  36 LRFVAVGD------WGGVPNAPFHTAREMANAKEIartvqimgaDFIMSLGDNfyftgVHDANDKRFQEtFEDVFSDRal 109
Cdd:COG1409     1 FRFAHISDlhlgapDGSDTAEVLAAALADINAPRP---------DFVVVTGDL-----TDDGEPEEYAA-AREILARL-- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 110 rNIPWYVLAGNHDHLGNVSAQIAyskisKRWNFPSP---YYRLRFKvprsniTVAIFMLDTVMLCGNSDDfvsqqpempr 186
Cdd:COG1409    64 -GVPVYVVPGNHDIRAAMAEAYR-----EYFGDLPPgglYYSFDYG------GVRFIGLDSNVPGRSSGE---------- 121

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 187 dlgVARTQLSWLKKQLAAAKEDYVLVAGHYPIWSIAEHGPTRCLV--KNLRPLLAAYGVTAYLCGHDHNlQYLQDENGVG 264
Cdd:COG1409   122 ---LGPEQLAWLEEELAAAPAKPVIVFLHHPPYSTGSGSDRIGLRnaEELLALLARYGVDLVLSGHVHR-YERTRRDGVP 197

                         250       260
                  ....*....|....*....|....*...
gi 1046899426 265 YVLSgagnfmdPSVRHQRKVPNGYLRFH 292
Cdd:COG1409   198 YIVA-------GSTGGQVRLPPGYRVIE 218
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 36-333 6.63e-18

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 83.72  E-value: 6.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426  36 LRFVAVGDWGGVPNApfhtarEMANAKEIARTVQIMGADFIMSLGDNFyFTGVHDANDKRFQETFEDVFSDRA-LRNIPW 114
Cdd:PTZ00422   27 LRFASLGNWGTGSKQ------QKLVASYLKQYAKNERVTFLVSPGSNF-PGGVDGLNDPKWKHCFENVYSEESgDMQIPF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 115 YVLAGNHDHLGNVSAQ----------------IAYSKISK---RWNFPSPYYRL-----------RFKVPRSNITVAIFM 164
Cdd:PTZ00422  100 FTVLGQADWDGNYNAEllkgqnvylnghgqtdIEYDSNNDiypKWIMPNYWYHYfthftdtsgpsLLKSGHKDMSVAFIF 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 165 LDTVMLCGN-SDDFVSQQpemprdlgvartqlSW--LKKQLAAAKE--DYVLVAGHYPIWSiaeHGPTRC---LVKNLRP 236
Cdd:PTZ00422  180 IDTWILSSSfPYKKVSER--------------AWqdLKATLEYAPKiaDYIIVVGDKPIYS---SGSSKGdsyLSYYLLP 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 237 LLAAYGVTAYLCGHDHNLqYLQDENGVGYVLSGAGNfmdpsvRHQRKVPNGYLRFHYGSEDSlgGFTYVEIGSKEMsITY 316
Cdd:PTZ00422  243 LLKDAQVDLYISGYDRNM-EVLTDEGTAHINCGSGG------NSGRKSIMKNSKSLFYSEDI--GFCIHELNAEGM-VTK 312

                         330       340
                  ....*....|....*....|.
gi 1046899426 317 VEASGK----SLFKTSLPRRP 333
Cdd:PTZ00422  313 FVSGNTgevlYTHKQPLKKRK 333
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 73-266 5.62e-12

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: 64.66  E-value: 5.62e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426  73 ADFIMSLGDnfyfTGVHDANDKRFQETFEDVFSDRALRNIPWYVLAGNHDhLGNVSAQiaYSKISKRWN-FPSPYYRL-- 149
Cdd:cd07396    47 LAFVVQLGD----IIDGYNAKDRSKEALDAVLSILDRLKGPVHHVLGNHE-FYNFPRE--YLNHLKTLNgEDAYYYSFsp 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 150 ----RFKVprsnitvaifmLDTVMLCGnsddfvsqqpemprdlGVARTQLSWLKKQL--AAAKEDYVLVAGHYPIWSIAE 223
Cdd:cd07396   120 gpgfRFLV-----------LDFVKFNG----------------GIGEEQLAWLRNELtsADANGEKVIVLSHLPIYPEAA 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1046899426 224 HGptRCLVKNLRPLLA---AYG-VTAYLCGHDHNLQYLQDENGVGYV 266
Cdd:cd07396   173 DP--QCLLWNYEEVLAileSYPcVKACFSGHNHEGGYEQDSHGVHHV 217
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 36-253 6.13e-09

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: 56.15  E-value: 6.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426  36 LRFVAVGDWGGVPNAPFHTAREMANAKEiartvqimGADFIMSLGDNFYFTGvhDANDKR---FQETFEDVFSdralrNI 112
Cdd:cd00839     5 LKFAVFGDMGQNTNNSTNTLDHLEKELG--------NYDAIIHVGDIAYADG--YNNGSRwdtFMRQIEPLAS-----YV 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 113 PWYVLAGNHDhlgnvsaqiayskiskrWNFPSPYYRLRFKVPRSNITVA-------------IFMLDTVMLCGNSDDFVS 179
Cdd:cd00839    70 PYMVAPGNHE-----------------ADYNGSTSKIKFFMPGRGMPPSpsgstenlwysfdVGPVHFISLSTETDFLKG 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 180 QQPEmprdlgvarTQLSWLKKQLAAA---KEDYVLVAGHYPIWSIAEHGPTRCLVKNLR----PLLAAYGVTAYLCGHDH 252
Cdd:cd00839   133 DNIS---------PQYDWLEADLAKVdrsRTPWIIVMGHRPMYCSNDDDADCIEGEKMRealeDLFYKYGVDLVLSGHVH 203


                  .
gi 1046899426 253 N 253
Cdd:cd00839   204 A 204
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 210-269 2.07e-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: 49.60  E-value: 2.07e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046899426 210 VLVAGHYPIWSIAEHGPTRCLVKN---LRPLLAAYGVTAYLCGHDH--NLQYLQDENGVGYVLSG 269
Cdd:cd07400    73 AIVALHHPLLPPPDTGRERNVLLDagdALKLLKELGVDLVLHGHKHvpAVWNLGLLNGIVVVNAG 137
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 108-281 2.83e-06

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: 47.66  E-value: 2.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 108 ALRNIPWYVLAGNHDHlgnvsaQIAYSKIskrwnFPSPYYRLRFKV--PRSNITVAIFMLDTVmlcgnsddfVSQQPEmp 185
Cdd:cd07402    66 APLPAPVYWIPGNHDD------RAAMREA-----LPEPPYDDNGPVqyVVDFGGWRLILLDTS---------VPGVHH-- 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 186 rdlGVAR-TQLSWLKKQLAAAKEDYVLVAGHYP--IWSIAEHGPTRClvKN---LRPLLAAY-GVTAYLCGHDHnlqylQ 258
Cdd:cd07402   124 ---GELSdEQLDWLEAALAEAPDRPTLIFLHHPpfPLGIPWMDAIRL--RNsqaLFAVLARHpQVKAILCGHIH-----R 193

                         170       180
                  ....*....|....*....|....*
gi 1046899426 259 DENGV--GYVLSGAgnfmdPSVRHQ 281
Cdd:cd07402   194 PISGSfrGIPFSTA-----PSTCHQ 213
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
37-269 1.00e-05

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 46.06  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426  37 RFVAVGDW--GgvpnAPFHtAREMANA-----KEIARTVQIMGADFIMSLGDNFyftgvHDAN-DKRFQETFEDVFSDRA 108
Cdd:COG0420     2 RFLHTADWhlG----KPLH-GASRREDqlaalDRLVDLAIEEKVDAVLIAGDLF-----DSANpSPEAVRLLAEALRRLS 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 109 LRNIPWYVLAGNHDHLGnvsaqiayskiskRWNFPSPYYRlrfkvpRSNITV-AIFMLDTVMLCGNSD------DFVSqq 181
Cdd:COG0420    72 EAGIPVVLIAGNHDSPS-------------RLSAGSPLLE------NLGVHVfGSVEPEPVELEDGLGvavyglPYLR-- 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 182 pemPRDLGVARTQLSWLKKQLAAAKedYVLVAGHYPIWSIAEHGPTRCLVKNLRPLLAAyGVTAYLCGHDHNLQYLQDEN 261
Cdd:COG0420   131 ---PSDEEALRDLLERLPRALDPGG--PNILLLHGFVAGASGSRDIYVAPVPLSALPAA-GFDYVALGHIHRPQVLGGDP 204


                  ....*...
gi 1046899426 262 GVGYvlSG 269
Cdd:COG0420   205 RIRY--SG 210
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 166-267 2.86e-05

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: 43.02  E-value: 2.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 166 DTVMLCGnsdDFVsqqpemprDLGVARTQLSWLKKQLAAAKEDYVLVAG-------HYPIWSIAEHG--PTRCLVKNLRP 236
Cdd:cd00838    28 DLVICLG---DLV--------DYGPDPEEVELKALRLLLAGIPVYVVPGnhdilvtHGPPYDPLDEGspGEDPGSEALLE 96

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1046899426 237 LLAAYGVTAYLCGHDHNLQYLQDENGVGYVL 267
Cdd:cd00838    97 LLDKYGPDLVLSGHTHVPGRREVDKGGTLVV 127
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 79-255 5.03e-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: 44.28  E-value: 5.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426  79 LGDNFYFTGVHDAN-DKRFQETFEDVFSD-RALRNIPWYVLAGNHDHLGNVSAQIA---YSKISKRwnFPSPYYRLRFKV 153
Cdd:cd07401    43 LTDNKTGNKLPSYQyQEEWQWKYYNILKEsSVINKEYLFDIRGNHDLFGIVSFDSQnnyYRKYSNT--GRDHSHSFSSTT 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426 154 PRSNITVAIFmldtvmlcgnsDDFVSQQPEMPRD--LGVARTQLSWLKKQLAAAKE-DYVLVAGHYPIWSIAEHGPtRCL 230
Cdd:cd07401   121 RFGNYSFIGF-----------DPTIFPGPKRPFNffGSLDKKLLDRLEKELEKSKNsKYTIWFGHYPHSLIISPSA-KSS 188

                         170       180
                  ....*....|....*....|....*
gi 1046899426 231 VKNLRPLLAAYGVTAYLCGHDHNLQ 255
Cdd:cd07401   189 SKTFKDLLKKYNVTAYLCGHLHPLG 213
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 36-147 8.80e-05

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: 41.43  E-value: 8.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426  36 LRFVAVGDWGGVPNAPfhtaremANAKEIARTVQIMGADFIMSLGDNFYftgvHDANDKRFQETFEdvfsdRALRNIPWY 115
Cdd:pfam00149   1 MRILVIGDLHLPGQLD-------DLLELLKKLLEEGKPDLVLHAGDLVD----RGPPSEEVLELLE-----RLIKYVPVY 64

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1046899426 116 VLAGNHD--HLGNVSAQIAYSKISKRWNFPSPYY 147
Cdd:pfam00149  65 LVRGNHDfdYGECLRLYPYLGLLARPWKRFLEVF 98
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 53-124 9.82e-05

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: 9.82e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046899426  53 HTAREMANAKEIARTVQIMGADFIMSLGDNFYFTGVHDANDKRFQEtfedvfsdRALRNIPWYVLAGNHDHL 124
Cdd:cd00838     7 HGNLEALEAVLEAALAKAEKPDLVICLGDLVDYGPDPEEVELKALR--------LLLAGIPVYVVPGNHDIL 70
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 37-124 5.27e-03

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: 37.25  E-value: 5.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046899426  37 RFVAVGDW--GgvpnAPFHTAREMANA-----KEIARTVQIMGADFIMSLGDNFyftgvHDAN-DKRFQETFEDVFSDRA 108
Cdd:cd00840     1 RFLHTADWhlG----YPLYGLSRREEDffkafEEIVDLAIEEKVDFVLIAGDLF-----DSNNpSPEALKLAIEGLRRLC 71

                          90
                  ....*....|....*.
gi 1046899426 109 LRNIPWYVLAGNHDHL 124
Cdd:cd00840    72 EAGIPVFVIAGNHDSP 87
 
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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