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Conserved domains on  [gi|545222149|ref|XP_005611965|]
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tartrate-resistant acid phosphatase type 5 isoform X1 [Equus caballus]

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 1.45e-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: 447.54  E-value: 1.45e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149  26 LRFVAVGDWGGVPNaPFYTARETATAKEIAKTVQILGTDFILSLGDNFYFNGVQNANDKRFQETFEDVFSASSLrNVPWY 105
Cdd:cd07378    1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 106 VLAGNHDHLGNVSAQIAYSSI--SKRWNFPSPFYRLRFKVPRSNVSVAIFMLDTVTLCGNSNDFTSQQPERPRDLALART 183
Cdd:cd07378   79 LVLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 184 QLSWLKKQLAAAKEDYVLVAGHYPIWSIAEHGPTHCLVKQLLPLLAMHKVTAYLCGHDHNLQYLQDENGIGFVLSGAGNF 263
Cdd:cd07378  159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 545222149 264 MDPSTKHARKVPNGYLRFHHGTNTSMGGFAYVEISPKEMTVTYIEASG 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 1.45e-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: 447.54  E-value: 1.45e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149  26 LRFVAVGDWGGVPNaPFYTARETATAKEIAKTVQILGTDFILSLGDNFYFNGVQNANDKRFQETFEDVFSASSLrNVPWY 105
Cdd:cd07378    1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 106 VLAGNHDHLGNVSAQIAYSSI--SKRWNFPSPFYRLRFKVPRSNVSVAIFMLDTVTLCGNSNDFTSQQPERPRDLALART 183
Cdd:cd07378   79 LVLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 184 QLSWLKKQLAAAKEDYVLVAGHYPIWSIAEHGPTHCLVKQLLPLLAMHKVTAYLCGHDHNLQYLQDENGIGFVLSGAGNF 263
Cdd:cd07378  159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 545222149 264 MDPSTKHARKVPNGYLRFHHGTNTSMGGFAYVEISPKEMTVTYIEASG 311
Cdd:cd07378  239 ADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
26-312 6.53e-28

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 108.63  E-value: 6.53e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149  26 LRFVAVGDwggvPNAPFYTARET-ATAKEIAKTVQILGTDFILSLGDNfyfngVQNANDKRFQEtFEDVFSAsslRNVPW 104
Cdd:COG1409    1 FRFAHISD----LHLGAPDGSDTaEVLAAALADINAPRPDFVVVTGDL-----TDDGEPEEYAA-AREILAR---LGVPV 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 105 YVLAGNHDHlgnvsaqiayssiskrWNFPSPFYRLRFKVPRSNVSVAIFMLDTVTLCG-NSNDFTSQqperprDLALART 183
Cdd:COG1409   68 YVVPGNHDI----------------RAAMAEAYREYFGDLPPGGLYYSFDYGGVRFIGlDSNVPGRS------SGELGPE 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 184 QLSWLKKQLAAAKEDYVLVAGHYPIWSIAEHGPTHCLV--KQLLPLLAMHKVTAYLCGHDHNlQYLQDENGIGFVLSgag 261
Cdd:COG1409  126 QLAWLEEELAAAPAKPVIVFLHHPPYSTGSGSDRIGLRnaEELLALLARYGVDLVLSGHVHR-YERTRRDGVPYIVA--- 201

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 545222149 262 nfmdPSTKHARKVPNGYlrfhhgtntsmggfAYVEISPKEMTVTYIEASGK 312
Cdd:COG1409  202 ----GSTGGQVRLPPGY--------------RVIEVDGDGLTVEVRRVDGG 234
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 5-261 7.45e-22

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 95.28  E-value: 7.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149   5 MVLLFLQASLVLSLANRATPV---LRFVAVGDWGGVPNapfYTARETATAKEIAKTVQIlgtDFILSLGDNFyFNGVQNA 81
Cdd:PTZ00422   3 SFCKLVLFSLFVLIFISSYSVkaqLRFASLGNWGTGSK---QQKLVASYLKQYAKNERV---TFLVSPGSNF-PGGVDGL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149  82 NDKRFQETFEDVFS-ASSLRNVPWYVLAGNHDHLGNVSAQ----------------IAYSSISK---RWNFPSPFYRL-- 139
Cdd:PTZ00422  76 NDPKWKHCFENVYSeESGDMQIPFFTVLGQADWDGNYNAEllkgqnvylnghgqtdIEYDSNNDiypKWIMPNYWYHYft 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 140 ---------RFKVPRSNVSVAIFMLDTVTLcgnSNDFTSQQPerprdlalarTQLSW--LKKQLAAAKE--DYVLVAGHY 206
Cdd:PTZ00422 156 hftdtsgpsLLKSGHKDMSVAFIFIDTWIL---SSSFPYKKV----------SERAWqdLKATLEYAPKiaDYIIVVGDK 222

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 545222149 207 PIWSIAEHGPTHCLVKQLLPLLAMHKVTAYLCGHDHNLqYLQDENGIGFVLSGAG 261
Cdd:PTZ00422 223 PIYSSGSSKGDSYLSYYLLPLLKDAQVDLYISGYDRNM-EVLTDEGTAHINCGSG 276
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 26-137 6.09e-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: 41.82  E-value: 6.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149   26 LRFVAVGDWGGVPNAPfytaretATAKEIAKTVQILGTDFILSLGDNFyfngvqnaNDKRFQETFEDVFsASSLRNVPWY 105
Cdd:pfam00149   1 MRILVIGDLHLPGQLD-------DLLELLKKLLEEGKPDLVLHAGDLV--------DRGPPSEEVLELL-ERLIKYVPVY 64

                          90       100       110
                  ....*....|....*....|....*....|....
gi 545222149  106 VLAGNHD--HLGNVSAQIAYSSISKRWNFPSPFY 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 1.45e-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: 447.54  E-value: 1.45e-159
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149  26 LRFVAVGDWGGVPNaPFYTARETATAKEIAKTVQILGTDFILSLGDNFYFNGVQNANDKRFQETFEDVFSASSLrNVPWY 105
Cdd:cd07378    1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 106 VLAGNHDHLGNVSAQIAYSSI--SKRWNFPSPFYRLRFKVPRSNVSVAIFMLDTVTLCGNSNDFTSQQPERPRDLALART 183
Cdd:cd07378   79 LVLGNHDHRGNVSAQIAYTQRpnSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 184 QLSWLKKQLAAAKEDYVLVAGHYPIWSIAEHGPTHCLVKQLLPLLAMHKVTAYLCGHDHNLQYLQDENGIGFVLSGAGNF 263
Cdd:cd07378  159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 545222149 264 MDPSTKHARKVPNGYLRFHHGTNTSMGGFAYVEISPKEMTVTYIEASG 311
Cdd:cd07378  239 ADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
26-312 6.53e-28

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 108.63  E-value: 6.53e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149  26 LRFVAVGDwggvPNAPFYTARET-ATAKEIAKTVQILGTDFILSLGDNfyfngVQNANDKRFQEtFEDVFSAsslRNVPW 104
Cdd:COG1409    1 FRFAHISD----LHLGAPDGSDTaEVLAAALADINAPRPDFVVVTGDL-----TDDGEPEEYAA-AREILAR---LGVPV 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 105 YVLAGNHDHlgnvsaqiayssiskrWNFPSPFYRLRFKVPRSNVSVAIFMLDTVTLCG-NSNDFTSQqperprDLALART 183
Cdd:COG1409   68 YVVPGNHDI----------------RAAMAEAYREYFGDLPPGGLYYSFDYGGVRFIGlDSNVPGRS------SGELGPE 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 184 QLSWLKKQLAAAKEDYVLVAGHYPIWSIAEHGPTHCLV--KQLLPLLAMHKVTAYLCGHDHNlQYLQDENGIGFVLSgag 261
Cdd:COG1409  126 QLAWLEEELAAAPAKPVIVFLHHPPYSTGSGSDRIGLRnaEELLALLARYGVDLVLSGHVHR-YERTRRDGVPYIVA--- 201

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 545222149 262 nfmdPSTKHARKVPNGYlrfhhgtntsmggfAYVEISPKEMTVTYIEASGK 312
Cdd:COG1409  202 ----GSTGGQVRLPPGY--------------RVIEVDGDGLTVEVRRVDGG 234
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 5-261 7.45e-22

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 95.28  E-value: 7.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149   5 MVLLFLQASLVLSLANRATPV---LRFVAVGDWGGVPNapfYTARETATAKEIAKTVQIlgtDFILSLGDNFyFNGVQNA 81
Cdd:PTZ00422   3 SFCKLVLFSLFVLIFISSYSVkaqLRFASLGNWGTGSK---QQKLVASYLKQYAKNERV---TFLVSPGSNF-PGGVDGL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149  82 NDKRFQETFEDVFS-ASSLRNVPWYVLAGNHDHLGNVSAQ----------------IAYSSISK---RWNFPSPFYRL-- 139
Cdd:PTZ00422  76 NDPKWKHCFENVYSeESGDMQIPFFTVLGQADWDGNYNAEllkgqnvylnghgqtdIEYDSNNDiypKWIMPNYWYHYft 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 140 ---------RFKVPRSNVSVAIFMLDTVTLcgnSNDFTSQQPerprdlalarTQLSW--LKKQLAAAKE--DYVLVAGHY 206
Cdd:PTZ00422 156 hftdtsgpsLLKSGHKDMSVAFIFIDTWIL---SSSFPYKKV----------SERAWqdLKATLEYAPKiaDYIIVVGDK 222

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 545222149 207 PIWSIAEHGPTHCLVKQLLPLLAMHKVTAYLCGHDHNLqYLQDENGIGFVLSGAG 261
Cdd:PTZ00422 223 PIYSSGSSKGDSYLSYYLLPLLKDAQVDLYISGYDRNM-EVLTDEGTAHINCGSG 276
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 64-256 6.24e-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: 6.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149  64 DFILSLGDnfYFNGvQNAnDKRFQETFEDVFSASSLRNVPWYVLAGNHD-------HLGNVSAQIAYSSiskRWNFPSPF 136
Cdd:cd07396   48 AFVVQLGD--IIDG-YNA-KDRSKEALDAVLSILDRLKGPVHHVLGNHEfynfpreYLNHLKTLNGEDA---YYYSFSPG 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 137 YRLRFKVprsnvsvaifmLDTVTLCGnsndftsqqperprdlALARTQLSWLKKQL--AAAKEDYVLVAGHYPIWSIAEH 214
Cdd:cd07396  121 PGFRFLV-----------LDFVKFNG----------------GIGEEQLAWLRNELtsADANGEKVIVLSHLPIYPEAAD 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 545222149 215 GptHCLV---KQLLPLLAMHK-VTAYLCGHDHNLQYLQDENGIGFV 256
Cdd:cd07396  174 P--QCLLwnyEEVLAILESYPcVKACFSGHNHEGGYEQDSHGVHHV 217
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 26-243 2.80e-10

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: 60.39  E-value: 2.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149  26 LRFVAVGDWGgvpnAPFYTARETAtaKEIAKtvQILGTDFILSLGD---NFYFNGVQNANDkrFQETFEDVFSasslrNV 102
Cdd:cd00839    5 LKFAVFGDMG----QNTNNSTNTL--DHLEK--ELGNYDAIIHVGDiayADGYNNGSRWDT--FMRQIEPLAS-----YV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 103 PWYVLAGNHDhlgnvsAQIAYSSISKRWNFPSPFYRLRFKVPRSNV--SVAIFMLDTVTLCGNSNDFTSQQPERprdlal 180
Cdd:cd00839   70 PYMVAPGNHE------ADYNGSTSKIKFFMPGRGMPPSPSGSTENLwySFDVGPVHFISLSTETDFLKGDNISP------ 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545222149 181 artQLSWLKKQLAAA---KEDYVLVAGHYPiWSIAEHGPTHCLVK-----QLLPLLAMHKVTAYLCGHDHN 243
Cdd:cd00839  138 ---QYDWLEADLAKVdrsRTPWIIVMGHRP-MYCSNDDDADCIEGekmreALEDLFYKYGVDLVLSGHVHA 204
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 56-245 1.03e-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: 55.06  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149  56 KTVQILGTDFILSLGD---NFYFNGVQNAN-DKRFQETFEDVF-SASSLRNVPWYVLAGNHDHLGNVSAQI-----AYSS 125
Cdd:cd07401   27 NFIDVIKPTLVLITGDltdNKTGNKLPSYQyQEEWQWKYYNILkESSVINKEYLFDIRGNHDLFGIVSFDSqnnyyRKYS 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 126 ISKRWNFPSPFYRLRFkvprSNVSvaifmldtvTLCGNSNDFTSqqPERPRD--LALARTQLSWLKKQLAAAKE-DYVLV 202
Cdd:cd07401  107 NTGRDHSHSFSSTTRF----GNYS---------FIGFDPTIFPG--PKRPFNffGSLDKKLLDRLEKELEKSKNsKYTIW 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 545222149 203 AGHYPIWSIAEHGPTHCLvKQLLPLLAMHKVTAYLCGHDHNLQ 245
Cdd:cd07401  172 FGHYPHSLIISPSAKSSS-KTFKDLLKKYNVTAYLCGHLHPLG 213
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 139-259 3.88e-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: 3.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 139 LRFKVPRSNVSVAIFMLDTVtlcgN---------SNDFTsqQPERPRDLALARTQLSWLkkqlaaAKEDYVLVAG----- 204
Cdd:cd07400    7 LHFGEERKPEVLELNLLDEI----NalkpdlvvvTGDLT--QRARPAEFEEAREFLDAL------EPEPVVVVPGnhdai 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545222149 205 ---HYPIWSIAEHG---PTHCLVKQLLPLLAMHKVTAYLCGHDH--NLQYLQDENGIGFVLSG 259
Cdd:cd07400   75 valHHPLLPPPDTGrerNVLLDAGDALKLLKELGVDLVLHGHKHvpAVWNLGLLNGIVVVNAG 137
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 26-137 6.09e-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: 41.82  E-value: 6.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149   26 LRFVAVGDWGGVPNAPfytaretATAKEIAKTVQILGTDFILSLGDNFyfngvqnaNDKRFQETFEDVFsASSLRNVPWY 105
Cdd:pfam00149   1 MRILVIGDLHLPGQLD-------DLLELLKKLLEEGKPDLVLHAGDLV--------DRGPPSEEVLELL-ERLIKYVPVY 64

                          90       100       110
                  ....*....|....*....|....*....|....
gi 545222149  106 VLAGNHD--HLGNVSAQIAYSSISKRWNFPSPFY 137
Cdd:pfam00149  65 LVRGNHDfdYGECLRLYPYLGLLARPWKRFLEVF 98
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 64-242 1.22e-04

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: 43.06  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149  64 DFILSLGDNfyfngVQNANDKRFQETFEDVFSASS------LRNVPWYVLAGNHDhlGNVSAQIAYSSISKRWNFPSpFY 137
Cdd:cd00842   71 DFILWTGDL-----VRHDVDEQTPEETVESESNLTnllkkyFPNVPVYPALGNHD--SYPVNQFPPHSNSPSWLYDA-LA 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 138 RL-----------RFK-------VPRSNVSVaIFmLDTVtLCGNSNDFTSQQPERPRDlalartQLSWLKKQLAAAKE-- 197
Cdd:cd00842  143 ELwkpwlpteakeTFKkggyysvDVKDGLRV-IS-LNTN-LYYKKNFWLYSNNTDPCG------QLQWLEDELEDAEQkg 213

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 545222149 198 DYVLVAGH-YPIWSIAEHGPTHCLVKqllpllAMHK----VTAYLCGHDH 242
Cdd:cd00842  214 EKVWIIGHiPPGLNSYDADWSERFYQ------IINRysdtIAGQFFGHTH 257
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 101-243 1.45e-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: 1.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 101 NVPWYVLAGNHDHlgnvsaQIAYSSIskrwnFPSPFYRLRFKVPRSnVSVA---IFMLDTVTlcgnsndftsqqPERPRD 177
Cdd:cd07402   69 PAPVYWIPGNHDD------RAAMREA-----LPEPPYDDNGPVQYV-VDFGgwrLILLDTSV------------PGVHHG 124

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 178 lALARTQLSWLKKQLAAAKEDYVLVAGHYPIWSIAEHGP-THCLVKQ--LLPLLAMH-KVTAYLCGHDHN 243
Cdd:cd07402  125 -ELSDEQLDWLEAALAEAPDRPTLIFLHHPPFPLGIPWMdAIRLRNSqaLFAVLARHpQVKAILCGHIHR 193
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 187-257 7.91e-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: 39.17  E-value: 7.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 187 WLKKQLAAAKEDYVLVAG-------HYPIWSIAEHG--PTHCLVKQLLPLLAMHKVTAYLCGHDHNLQYLQDENGIGFVL 257
Cdd:cd00838   48 LKALRLLLAGIPVYVVPGnhdilvtHGPPYDPLDEGspGEDPGSEALLELLDKYGPDLVLSGHTHVPGRREVDKGGTLVV 127
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 51-114 1.77e-03

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


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 38.02  E-value: 1.77e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545222149  51 AKEIAKTVQILGTDFILSLGDNFYFNGVQNANDKRFQEtfedvfsaSSLRNVPWYVLAGNHDHL 114
Cdd:cd00838   15 AVLEAALAKAEKPDLVICLGDLVDYGPDPEEVELKALR--------LLLAGIPVYVVPGNHDIL 70
PRK11148 PRK11148
cyclic 3',5'-adenosine monophosphate phosphodiesterase; Provisional
 184-242 3.47e-03

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


Pssm-ID: 182997 [Multi-domain]  Cd Length: 275  Bit Score: 38.76  E-value: 3.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 184 QLSWLKKQLAAAKEDYVLVA-GHYPIwsiaehgPTHCL---------VKQLLPLLAMH-KVTAYLCGHDH 242
Cdd:PRK11148 143 QLEWLERKLADAPERHTLVLlHHHPL-------PAGCAwldqhslrnAHELAEVLAKFpNVKAILCGHIH 205
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
27-250 8.22e-03

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 37.20  E-value: 8.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149  27 RFVAVGDW--GgvpnAPFYTA-RETATAK------EIAKTVQIlgtDFILSLGDNFyfngvQNAN-DKRFQETFEDVFSA 96
Cdd:COG0420    2 RFLHTADWhlG----KPLHGAsRREDQLAaldrlvDLAIEEKV---DAVLIAGDLF-----DSANpSPEAVRLLAEALRR 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149  97 SSLRNVPWYVLAGNHDHLGnvsaqiayssiskRWNFPSPFYRlrfkvpRSNVSV-AIFMLDTVTLCGNSN------DFTs 169
Cdd:COG0420   70 LSEAGIPVVLIAGNHDSPS-------------RLSAGSPLLE------NLGVHVfGSVEPEPVELEDGLGvavyglPYL- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545222149 170 qqpeRPRDLALARTQLSWLKKQLAAAKedYVLVAGHYPIWSIAEHGPTH--CLVKQLLPLLAMHkvtAYLCGHDHNLQYL 247
Cdd:COG0420  130 ----RPSDEEALRDLLERLPRALDPGG--PNILLLHGFVAGASGSRDIYvaPVPLSALPAAGFD---YVALGHIHRPQVL 200


                 ...
gi 545222149 248 QDE 250
Cdd:COG0420  201 GGD 203
 
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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