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Conserved domains on  [gi|1965535638|ref|XP_039106861|]
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tartrate-resistant acid phosphatase type 5 [Hyaena hyaena]

Protein Classification

tartrate-resistant acid phosphatase type 5 family protein( domain architecture ID 10164501)

tartrate-resistant acid phosphatase type 5 family protein which is a metallophosphatase; similar to human tartrate-resistant acid phosphatase type 5 (ACP5) which is involved in osteopontin/bone sialoprotein dephosphorylation in bone matrix, and to Arabidopsis thaliana purple acid phosphatase 17 (PAP17) which is involved in phosphate metabolism and has a peroxidase activity

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 ...
 26-311 1.70e-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: 452.16  E-value: 1.70e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638  26 LRFVAVGDWGGVPNaPFYTARETANAKEIARTTQTLGTDFILSLGDNFYFSGVQDANDKRFRETFEDVFSASSLrNVPWY 105
Cdd:cd07378     1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 106 VLAGNHDHLGNVSAQIEYS--RVSQRWNFPSPYYRLRFKVPRSNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDAALART 183
Cdd:cd07378    79 LVLGNHDHRGNVSAQIAYTqrPNSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 184 QLSWLKKQLAAAKEDYVLVAGHYPVWSIAEHGPTRCLVKQLMPLLATYKVTAYLCGHDHNLQYLQDENGVGYVLSGAGNF 263
Cdd:cd07378   159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1965535638 264 MDPSRKHMRKVPNGYLRFHYGAEDSLGGFAYVEISPKEMSVTYIEASG 311
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 ...
 26-311 1.70e-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: 452.16  E-value: 1.70e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638  26 LRFVAVGDWGGVPNaPFYTARETANAKEIARTTQTLGTDFILSLGDNFYFSGVQDANDKRFRETFEDVFSASSLrNVPWY 105
Cdd:cd07378     1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 106 VLAGNHDHLGNVSAQIEYS--RVSQRWNFPSPYYRLRFKVPRSNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDAALART 183
Cdd:cd07378    79 LVLGNHDHRGNVSAQIAYTqrPNSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 184 QLSWLKKQLAAAKEDYVLVAGHYPVWSIAEHGPTRCLVKQLMPLLATYKVTAYLCGHDHNLQYLQDENGVGYVLSGAGNF 263
Cdd:cd07378   159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1965535638 264 MDPSRKHMRKVPNGYLRFHYGAEDSLGGFAYVEISPKEMSVTYIEASG 311
Cdd:cd07378   239 ADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
26-312 8.13e-26

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 102.85  E-value: 8.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638  26 LRFVAVGDwggvPNAPFYTARET-ANAKEIARTTQTLGTDFILSLGDNfyfsgVQDANDKRFREtFEDVFSAsslRNVPW 104
Cdd:COG1409     1 FRFAHISD----LHLGAPDGSDTaEVLAAALADINAPRPDFVVVTGDL-----TDDGEPEEYAA-AREILAR---LGVPV 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 105 YVLAGNHDHLGNVSAQIEysrvsQRWNFPSP---YYRLRFKvprsnvSVAIFMLDTVTLCGNSDdflsqqperprdaALA 181
Cdd:COG1409    68 YVVPGNHDIRAAMAEAYR-----EYFGDLPPgglYYSFDYG------GVRFIGLDSNVPGRSSG-------------ELG 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 182 RTQLSWLKKQLAAAKEDYVLVAGHYPVWSIAEHGPTRCLV--KQLMPLLATYKVTAYLCGHDHNlQYLQDENGVGYVLSG 259
Cdd:COG1409   124 PEQLAWLEEELAAAPAKPVIVFLHHPPYSTGSGSDRIGLRnaEELLALLARYGVDLVLSGHVHR-YERTRRDGVPYIVAG 202

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1965535638 260 AGnfmdpsrkhmrkvpngylrfhYGAEDSLGGFAYVEISPKEMSVTYIEASGK 312
Cdd:COG1409   203 ST---------------------GGQVRLPPGYRVIEVDGDGLTVEVRRVDGG 234
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 26-326 9.60e-18

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 83.34  E-value: 9.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638  26 LRFVAVGDWGGVPNapfYTARETANAKEIARTTQTlgtDFILSLGDNFyFSGVQDANDKRFRETFEDVFS-ASSLRNVPW 104
Cdd:PTZ00422   27 LRFASLGNWGTGSK---QQKLVASYLKQYAKNERV---TFLVSPGSNF-PGGVDGLNDPKWKHCFENVYSeESGDMQIPF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 105 YVLAGNHDHLGNVSAQ----------------IEYSRVSQ---RWNFPSPYYRL-----------RFKVPRSNVSVAIFM 154
Cdd:PTZ00422  100 FTVLGQADWDGNYNAEllkgqnvylnghgqtdIEYDSNNDiypKWIMPNYWYHYfthftdtsgpsLLKSGHKDMSVAFIF 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 155 LDTVTLCgnsddflSQQPERprdaalARTQLSW--LKKQLAAAKE--DYVLVAGHYPVWSiaeHGPTRC---LVKQLMPL 227
Cdd:PTZ00422  180 IDTWILS-------SSFPYK------KVSERAWqdLKATLEYAPKiaDYIIVVGDKPIYS---SGSSKGdsyLSYYLLPL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 228 LATYKVTAYLCGHDHNLqYLQDENGVGYVLSGAGNfmDPSRKHMRKVPNGYlrfhYGAEDSlgGFAYVEISPKEMsVTYI 307
Cdd:PTZ00422  244 LKDAQVDLYISGYDRNM-EVLTDEGTAHINCGSGG--NSGRKSIMKNSKSL----FYSEDI--GFCIHELNAEGM-VTKF 313

                         330       340
                  ....*....|....*....|.
gi 1965535638 308 --EASGKSLFKTRLPRRARPE 326
Cdd:PTZ00422  314 vsGNTGEVLYTHKQPLKKRKL 334
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 26-137 8.07e-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: 8.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638  26 LRFVAVGDWGGVPNAPfytaretANAKEIARTTQTLGTDFILSLGDNFyfsgvqdaNDKRFRETFEDVFsASSLRNVPWY 105
Cdd:pfam00149   1 MRILVIGDLHLPGQLD-------DLLELLKKLLEEGKPDLVLHAGDLV--------DRGPPSEEVLELL-ERLIKYVPVY 64

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1965535638 106 VLAGNHD--HLGNVSAQIEYSRVSQRWNFPSPYY 137
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 ...
 26-311 1.70e-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: 452.16  E-value: 1.70e-161
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638  26 LRFVAVGDWGGVPNaPFYTARETANAKEIARTTQTLGTDFILSLGDNFYFSGVQDANDKRFRETFEDVFSASSLrNVPWY 105
Cdd:cd07378     1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 106 VLAGNHDHLGNVSAQIEYS--RVSQRWNFPSPYYRLRFKVPRSNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDAALART 183
Cdd:cd07378    79 LVLGNHDHRGNVSAQIAYTqrPNSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 184 QLSWLKKQLAAAKEDYVLVAGHYPVWSIAEHGPTRCLVKQLMPLLATYKVTAYLCGHDHNLQYLQDENGVGYVLSGAGNF 263
Cdd:cd07378   159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1965535638 264 MDPSRKHMRKVPNGYLRFHYGAEDSLGGFAYVEISPKEMSVTYIEASG 311
Cdd:cd07378   239 ADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
26-312 8.13e-26

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 102.85  E-value: 8.13e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638  26 LRFVAVGDwggvPNAPFYTARET-ANAKEIARTTQTLGTDFILSLGDNfyfsgVQDANDKRFREtFEDVFSAsslRNVPW 104
Cdd:COG1409     1 FRFAHISD----LHLGAPDGSDTaEVLAAALADINAPRPDFVVVTGDL-----TDDGEPEEYAA-AREILAR---LGVPV 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 105 YVLAGNHDHLGNVSAQIEysrvsQRWNFPSP---YYRLRFKvprsnvSVAIFMLDTVTLCGNSDdflsqqperprdaALA 181
Cdd:COG1409    68 YVVPGNHDIRAAMAEAYR-----EYFGDLPPgglYYSFDYG------GVRFIGLDSNVPGRSSG-------------ELG 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 182 RTQLSWLKKQLAAAKEDYVLVAGHYPVWSIAEHGPTRCLV--KQLMPLLATYKVTAYLCGHDHNlQYLQDENGVGYVLSG 259
Cdd:COG1409   124 PEQLAWLEEELAAAPAKPVIVFLHHPPYSTGSGSDRIGLRnaEELLALLARYGVDLVLSGHVHR-YERTRRDGVPYIVAG 202

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1965535638 260 AGnfmdpsrkhmrkvpngylrfhYGAEDSLGGFAYVEISPKEMSVTYIEASGK 312
Cdd:COG1409   203 ST---------------------GGQVRLPPGYRVIEVDGDGLTVEVRRVDGG 234
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 26-326 9.60e-18

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 83.34  E-value: 9.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638  26 LRFVAVGDWGGVPNapfYTARETANAKEIARTTQTlgtDFILSLGDNFyFSGVQDANDKRFRETFEDVFS-ASSLRNVPW 104
Cdd:PTZ00422   27 LRFASLGNWGTGSK---QQKLVASYLKQYAKNERV---TFLVSPGSNF-PGGVDGLNDPKWKHCFENVYSeESGDMQIPF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 105 YVLAGNHDHLGNVSAQ----------------IEYSRVSQ---RWNFPSPYYRL-----------RFKVPRSNVSVAIFM 154
Cdd:PTZ00422  100 FTVLGQADWDGNYNAEllkgqnvylnghgqtdIEYDSNNDiypKWIMPNYWYHYfthftdtsgpsLLKSGHKDMSVAFIF 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 155 LDTVTLCgnsddflSQQPERprdaalARTQLSW--LKKQLAAAKE--DYVLVAGHYPVWSiaeHGPTRC---LVKQLMPL 227
Cdd:PTZ00422  180 IDTWILS-------SSFPYK------KVSERAWqdLKATLEYAPKiaDYIIVVGDKPIYS---SGSSKGdsyLSYYLLPL 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 228 LATYKVTAYLCGHDHNLqYLQDENGVGYVLSGAGNfmDPSRKHMRKVPNGYlrfhYGAEDSlgGFAYVEISPKEMsVTYI 307
Cdd:PTZ00422  244 LKDAQVDLYISGYDRNM-EVLTDEGTAHINCGSGG--NSGRKSIMKNSKSL----FYSEDI--GFCIHELNAEGM-VTKF 313

                         330       340
                  ....*....|....*....|.
gi 1965535638 308 --EASGKSLFKTRLPRRARPE 326
Cdd:PTZ00422  314 vsGNTGEVLYTHKQPLKKRKL 334
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 64-256 4.45e-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: 61.96  E-value: 4.45e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638  64 DFILSLGDnfYFSGvqDANDKRFRETFEDVFSASSLRNVPWYVLAGNHDhLGNVSAqiEYSRVSQRWN-FPSPYYRL--- 139
Cdd:cd07396    48 AFVVQLGD--IIDG--YNAKDRSKEALDAVLSILDRLKGPVHHVLGNHE-FYNFPR--EYLNHLKTLNgEDAYYYSFspg 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 140 ---RFKVprsnvsvaifmLDTVTLCGnsddflsqqperprdaALARTQLSWLKKQL--AAAKEDYVLVAGHYPVWSIAEH 214
Cdd:cd07396   121 pgfRFLV-----------LDFVKFNG----------------GIGEEQLAWLRNELtsADANGEKVIVLSHLPIYPEAAD 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1965535638 215 GptRCLV---KQLMPLLATYK-VTAYLCGHDHNLQYLQDENGVGYV 256
Cdd:cd07396   174 P--QCLLwnyEEVLAILESYPcVKACFSGHNHEGGYEQDSHGVHHV 217
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 23-243 1.57e-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: 58.08  E-value: 1.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638  23 NPVLRFVAVGDWGgvpnAPFYTARETANAKEiartTQTLGTDFILSLGD---NFYFSGVQDANDkrFRETFEDVFSassl 99
Cdd:cd00839     2 DTPLKFAVFGDMG----QNTNNSTNTLDHLE----KELGNYDAIIHVGDiayADGYNNGSRWDT--FMRQIEPLAS---- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 100 rNVPWYVLAGNHDhlgnvsaqIEY--SRVSQRWNFPSPYYRLRFKVPRSNV--SVAIFMLDTVTLCGNSDDFLSQQPERp 175
Cdd:cd00839    68 -YVPYMVAPGNHE--------ADYngSTSKIKFFMPGRGMPPSPSGSTENLwySFDVGPVHFISLSTETDFLKGDNISP- 137

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1965535638 176 rdaalartQLSWLKKQLAAA---KEDYVLVAGHYPvWSIAEHGPTRCLVKQLM-----PLLATYKVTAYLCGHDHN 243
Cdd:cd00839   138 --------QYDWLEADLAKVdrsRTPWIIVMGHRP-MYCSNDDDADCIEGEKMrealeDLFYKYGVDLVLSGHVHA 204
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 104-245 1.42e-08

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: 54.68  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 104 WYVLAGNHDHLGNVSAQIE--YSRVSQRwNFPSPYYRLRFKVPRSNVSVAIFmldtvtlcgnsDDFLSQQPERPRD--AA 179
Cdd:cd07401    80 LFDIRGNHDLFGIVSFDSQnnYYRKYSN-TGRDHSHSFSSTTRFGNYSFIGF-----------DPTIFPGPKRPFNffGS 147

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1965535638 180 LARTQLSWLKKQLAAAKE-DYVLVAGHYPVWSIAEHGPtRCLVKQLMPLLATYKVTAYLCGHDHNLQ 245
Cdd:cd07401   148 LDKKLLDRLEKELEKSKNsKYTIWFGHYPHSLIISPSA-KSSSKTFKDLLKKYNVTAYLCGHLHPLG 213
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 200-259 4.32e-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: 48.44  E-value: 4.32e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1965535638 200 VLVAGHYPVWSIAEHGPTRCLV---KQLMPLLATYKVTAYLCGHDH--NLQYLQDENGVGYVLSG 259
Cdd:cd07400    73 AIVALHHPLLPPPDTGRERNVLldaGDALKLLKELGVDLVLHGHKHvpAVWNLGLLNGIVVVNAG 137
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 101-243 2.40e-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: 48.04  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 101 NVPWYVLAGNHDHlgnvsaqieysRVSQRWNFPSPYYrlrfkvprsnvsVAIFMLDTVTLCGNSDD-FLSQQPERPRDAA 179
Cdd:cd07402    69 PAPVYWIPGNHDD-----------RAAMREALPEPPY------------DDNGPVQYVVDFGGWRLiLLDTSVPGVHHGE 125

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1965535638 180 LARTQLSWLKKQLAAAKEDYVLVAGHYPVWS--IAEHGPTRCLVKQ-LMPLLATY-KVTAYLCGHDHN 243
Cdd:cd07402   126 LSDEQLDWLEAALAEAPDRPTLIFLHHPPFPlgIPWMDAIRLRNSQaLFAVLARHpQVKAILCGHIHR 193
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 64-242 6.05e-05

acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase (ASMase) is a ubiquitously expressed phosphodiesterase which hydrolyzes sphingomyelin in acid pH conditions to form ceramide, a bioactive second messenger, as part of the sphingomyelin signaling pathway. ASMase is localized at the noncytosolic leaflet of biomembranes (for example the luminal leaflet of endosomes, lysosomes and phagosomes, and the extracellular leaflet of plasma membranes). ASMase-deficient humans develop Niemann-Pick disease. This disease is characterized by lysosomal storage of sphingomyelin in all tissues. Although ASMase-deficient mice are resistant to stress-induced apoptosis, they have greater susceptibility to bacterial infection. The latter correlates with defective phagolysosomal fusion and antibacterial killing activity in ASMase-deficient macrophages. ASMase 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: 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: 277321 [Multi-domain]  Cd Length: 294  Bit Score: 44.21  E-value: 6.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638  64 DFILSLGDNfyfsgVQDANDKRFRETFEDVFSASS------LRNVPWYVLAGNHDhlGNVSAQIEYSRVSQRWNF----- 132
Cdd:cd00842    71 DFILWTGDL-----VRHDVDEQTPEETVESESNLTnllkkyFPNVPVYPALGNHD--SYPVNQFPPHSNSPSWLYdalae 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 133 -PSP--------------YYrlrFKVPRSNVSVaIFmLDTVtLCGNSDDFLSQQPERPRDaalartQLSWLKKQLAAAKE 197
Cdd:cd00842   144 lWKPwlpteaketfkkggYY---SVDVKDGLRV-IS-LNTN-LYYKKNFWLYSNNTDPCG------QLQWLEDELEDAEQ 211

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1965535638 198 --DYVLVAGH-YPVWSIAEHGPTRCLVKqlmpLLATYK--VTAYLCGHDH 242
Cdd:cd00842   212 kgEKVWIIGHiPPGLNSYDADWSERFYQ----IINRYSdtIAGQFFGHTH 257
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 187-257 7.01e-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: 41.87  E-value: 7.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 187 WLKKQLAAAKEDYVLVAG-------HYPVWSIAEHG--PTRCLVKQLMPLLATYKVTAYLCGHDHNLQYLQDENGVGYVL 257
Cdd:cd00838    48 LKALRLLLAGIPVYVVPGnhdilvtHGPPYDPLDEGspGEDPGSEALLELLDKYGPDLVLSGHTHVPGRREVDKGGTLVV 127
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 26-137 8.07e-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: 8.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638  26 LRFVAVGDWGGVPNAPfytaretANAKEIARTTQTLGTDFILSLGDNFyfsgvqdaNDKRFRETFEDVFsASSLRNVPWY 105
Cdd:pfam00149   1 MRILVIGDLHLPGQLD-------DLLELLKKLLEEGKPDLVLHAGDLV--------DRGPPSEEVLELL-ERLIKYVPVY 64

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1965535638 106 VLAGNHD--HLGNVSAQIEYSRVSQRWNFPSPYY 137
Cdd:pfam00149  65 LVRGNHDfdYGECLRLYPYLGLLARPWKRFLEVF 98
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 29-114 5.54e-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: 39.56  E-value: 5.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638  29 VAVGDW-GGVPNAPFYTARETANAKEIarttqtlgtDFILSLGDNFYFSGVQDANDKRFREtfedvfsaSSLRNVPWYVL 107
Cdd:cd00838     1 LVISDIhGNLEALEAVLEAALAKAEKP---------DLVICLGDLVDYGPDPEEVELKALR--------LLLAGIPVYVV 63


                  ....*..
gi 1965535638 108 AGNHDHL 114
Cdd:cd00838    64 PGNHDIL 70
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
 64-242 1.11e-03

cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional


Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 39.92  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638  64 DFILSLGDNfyfsgVQDANDK---RFREtfedvfSASSLrNVPWYVLAGNHD---HLGNV--SAQIEYSR---VSQRWNf 132
Cdd:PRK11148   57 DLIVATGDL-----AQDHSSEayqHFAE------GIAPL-RKPCVWLPGNHDfqpAMYSAlqDAGISPAKhvlIGEHWQ- 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1965535638 133 pspyyrlrfkvprsnvsvaIFMLDtvtlcgnsddflSQQPERPRdAALARTQLSWLKKQLAAAKEDYVLVA-GHYPVwsi 211
Cdd:PRK11148  124 -------------------ILLLD------------SQVFGVPH-GELSEYQLEWLERKLADAPERHTLVLlHHHPL--- 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1965535638 212 aehgPTRCL---------VKQLMPLLATY-KVTAYLCGHDH 242
Cdd:PRK11148  169 ----PAGCAwldqhslrnAHELAEVLAKFpNVKAILCGHIH 205
 
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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