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Conserved domains on  [gi|829895215|ref|XP_012646012|]
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tartrate-resistant acid phosphatase type 5 [Microcebus murinus]

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 ...
 26-311 3.36e-163

Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


:

Pssm-ID: 277324 [Multi-domain]  Cd Length: 286  Bit Score: 456.02  E-value: 3.36e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215  26 LRFVAVGDWGGVPNaPFHTAREMANAKEIARTVQTLGADFILSLGDNFYFTGVQDANDKRFQETFEDVFSDRSLrNVPWY 105
Cdd:cd07378    1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 106 VLAGNHDHLGNVSAQIAYSK--VSKRWNFPSPYYRLRFKIPRTNVSVAIFMLDTVTICGNSDDFLSQQPERPRDLDLART 183
Cdd:cd07378   79 LVLGNHDHRGNVSAQIAYTQrpNSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 184 QLSWLKKQLAAAKEDYVLVAGHYPVWSIAEHGPTRCLVKQLQPLLATYGVTAYLCGHDHNLQYLQDENGVGYVLSGAGNF 263
Cdd:cd07378  159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 829895215 264 MDPSKRHQRKVPNGYLRFHYGAEDSLGGFAYVEMSPKEMSVTYIEASG 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 3.36e-163

Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277324 [Multi-domain]  Cd Length: 286  Bit Score: 456.02  E-value: 3.36e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215  26 LRFVAVGDWGGVPNaPFHTAREMANAKEIARTVQTLGADFILSLGDNFYFTGVQDANDKRFQETFEDVFSDRSLrNVPWY 105
Cdd:cd07378    1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 106 VLAGNHDHLGNVSAQIAYSK--VSKRWNFPSPYYRLRFKIPRTNVSVAIFMLDTVTICGNSDDFLSQQPERPRDLDLART 183
Cdd:cd07378   79 LVLGNHDHRGNVSAQIAYTQrpNSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 184 QLSWLKKQLAAAKEDYVLVAGHYPVWSIAEHGPTRCLVKQLQPLLATYGVTAYLCGHDHNLQYLQDENGVGYVLSGAGNF 263
Cdd:cd07378  159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 829895215 264 MDPSKRHQRKVPNGYLRFHYGAEDSLGGFAYVEMSPKEMSVTYIEASG 311
Cdd:cd07378  239 ADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
26-286 2.52e-29

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 112.09  E-value: 2.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215  26 LRFVAVGDWGGVPNAPFHTAREMANAkeiARTVQTLGADFILSLGDNfyftgVQDANDKRFQEtFEDVFSDRslrNVPWY 105
Cdd:COG1409    1 FRFAHISDLHLGAPDGSDTAEVLAAA---LADINAPRPDFVVVTGDL-----TDDGEPEEYAA-AREILARL---GVPVY 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 106 VLAGNHDHLGNVSAQIAyskvsKRWNFPSP---YYRLRFKiprtnvSVAIFMLDTVTICGNSDDflsqqperprdldLAR 182
Cdd:COG1409   69 VVPGNHDIRAAMAEAYR-----EYFGDLPPgglYYSFDYG------GVRFIGLDSNVPGRSSGE-------------LGP 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 183 TQLSWLKKQLAAAKEDYVLVAGHYPVWSIAEHGPTRCLV--KQLQPLLATYGVTAYLCGHDHNlQYLQDENGVGYVLSGA 260
Cdd:COG1409  125 EQLAWLEEELAAAPAKPVIVFLHHPPYSTGSGSDRIGLRnaEELLALLARYGVDLVLSGHVHR-YERTRRDGVPYIVAGS 203

                        250       260
                 ....*....|....*....|....*.
gi 829895215 261 GNfmdpskrHQRKVPNGYLRFHYGAE 286
Cdd:COG1409  204 TG-------GQVRLPPGYRVIEVDGD 222
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 26-323 3.76e-18

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 84.11  E-value: 3.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215  26 LRFVAVGDWGGVPNApfhtarEMANAKEIARTVQTLGADFILSLGDNFyFTGVQDANDKRFQETFEDVFSDRS-LRNVPW 104
Cdd:PTZ00422  27 LRFASLGNWGTGSKQ------QKLVASYLKQYAKNERVTFLVSPGSNF-PGGVDGLNDPKWKHCFENVYSEESgDMQIPF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 105 YVLAGNHDHLGNVSAQ----------------IAYSKVSK---RWNFPSPYYRL-----------RFKIPRTNVSVAIFM 154
Cdd:PTZ00422 100 FTVLGQADWDGNYNAEllkgqnvylnghgqtdIEYDSNNDiypKWIMPNYWYHYfthftdtsgpsLLKSGHKDMSVAFIF 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 155 LDTVTICgnsddflSQQPerprdlDLARTQLSW--LKKQLAAAKE--DYVLVAGHYPVWSiaeHGPTRC---LVKQLQPL 227
Cdd:PTZ00422 180 IDTWILS-------SSFP------YKKVSERAWqdLKATLEYAPKiaDYIIVVGDKPIYS---SGSSKGdsyLSYYLLPL 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 228 LATYGVTAYLCGHDHNLqYLQDENGVGYVLSGAGNfmdpskRHQRKVPNGYLRFHYGAEDSlgGFAYVEMSPKEMsVTYI 307
Cdd:PTZ00422 244 LKDAQVDLYISGYDRNM-EVLTDEGTAHINCGSGG------NSGRKSIMKNSKSLFYSEDI--GFCIHELNAEGM-VTKF 313

                        330       340
                 ....*....|....*....|
gi 829895215 308 EASGK----SLFKTSLPRRP 323
Cdd:PTZ00422 314 VSGNTgevlYTHKQPLKKRK 333
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 26-137 3.19e-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: 42.59  E-value: 3.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215   26 LRFVAVGDWGGVPNAPfhtaremANAKEIARTVQTLGADFILSLGDNFyftgvqdaNDKRFQETFEDVFsDRSLRNVPWY 105
Cdd:pfam00149   1 MRILVIGDLHLPGQLD-------DLLELLKKLLEEGKPDLVLHAGDLV--------DRGPPSEEVLELL-ERLIKYVPVY 64

                          90       100       110
                  ....*....|....*....|....*....|....
gi 829895215  106 VLAGNHD--HLGNVSAQIAYSKVSKRWNFPSPYY 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 3.36e-163

Homo sapiens acid phosphatase 5 and related proteins, metallophosphatase domain; Acid phosphatase 5 (ACP5) removes the mannose 6-phosphate recognition marker from lysosomal proteins. The exact site of dephosphorylation is not clear. Evidence suggests dephosphorylation may take place in a prelysosomal compartment as well as in the lysosome. ACP5 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277324 [Multi-domain]  Cd Length: 286  Bit Score: 456.02  E-value: 3.36e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215  26 LRFVAVGDWGGVPNaPFHTAREMANAKEIARTVQTLGADFILSLGDNFYFTGVQDANDKRFQETFEDVFSDRSLrNVPWY 105
Cdd:cd07378    1 LRFLVLGDWGGKPN-PYTTAAQSLVAKQMAKVASKLGIDFILSLGDNFYDDGVKDVDDPRFQETFEDVYSAPSL-QVPWY 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 106 VLAGNHDHLGNVSAQIAYSK--VSKRWNFPSPYYRLRFKIPRTNVSVAIFMLDTVTICGNSDDFLSQQPERPRDLDLART 183
Cdd:cd07378   79 LVLGNHDHRGNVSAQIAYTQrpNSKRWNFPNYYYDISFKFPSSDVTVAFIMIDTVLLCGNTDDEASGQPRGPPNKKLAET 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 184 QLSWLKKQLAAAKEDYVLVAGHYPVWSIAEHGPTRCLVKQLQPLLATYGVTAYLCGHDHNLQYLQDENGVGYVLSGAGNF 263
Cdd:cd07378  159 QLAWLEKQLAASKADYKIVVGHYPIYSSGEHGPTKCLVDILLPLLKKYKVDAYLSGHDHNLQHIVDESGTYYVISGAGSK 238

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 829895215 264 MDPSKRHQRKVPNGYLRFHYGAEDSLGGFAYVEMSPKEMSVTYIEASG 311
Cdd:cd07378  239 ADPSDIHRDKVPQGYLLFFSGFYSSGGGFAYLEITSSELVIRFVDSDG 286
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
26-286 2.52e-29

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 112.09  E-value: 2.52e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215  26 LRFVAVGDWGGVPNAPFHTAREMANAkeiARTVQTLGADFILSLGDNfyftgVQDANDKRFQEtFEDVFSDRslrNVPWY 105
Cdd:COG1409    1 FRFAHISDLHLGAPDGSDTAEVLAAA---LADINAPRPDFVVVTGDL-----TDDGEPEEYAA-AREILARL---GVPVY 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 106 VLAGNHDHLGNVSAQIAyskvsKRWNFPSP---YYRLRFKiprtnvSVAIFMLDTVTICGNSDDflsqqperprdldLAR 182
Cdd:COG1409   69 VVPGNHDIRAAMAEAYR-----EYFGDLPPgglYYSFDYG------GVRFIGLDSNVPGRSSGE-------------LGP 124

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 183 TQLSWLKKQLAAAKEDYVLVAGHYPVWSIAEHGPTRCLV--KQLQPLLATYGVTAYLCGHDHNlQYLQDENGVGYVLSGA 260
Cdd:COG1409  125 EQLAWLEEELAAAPAKPVIVFLHHPPYSTGSGSDRIGLRnaEELLALLARYGVDLVLSGHVHR-YERTRRDGVPYIVAGS 203

                        250       260
                 ....*....|....*....|....*.
gi 829895215 261 GNfmdpskrHQRKVPNGYLRFHYGAE 286
Cdd:COG1409  204 TG-------GQVRLPPGYRVIEVDGD 222
PTZ00422 PTZ00422
glideosome-associated protein 50; Provisional
 26-323 3.76e-18

glideosome-associated protein 50; Provisional


Pssm-ID: 185607 [Multi-domain]  Cd Length: 394  Bit Score: 84.11  E-value: 3.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215  26 LRFVAVGDWGGVPNApfhtarEMANAKEIARTVQTLGADFILSLGDNFyFTGVQDANDKRFQETFEDVFSDRS-LRNVPW 104
Cdd:PTZ00422  27 LRFASLGNWGTGSKQ------QKLVASYLKQYAKNERVTFLVSPGSNF-PGGVDGLNDPKWKHCFENVYSEESgDMQIPF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 105 YVLAGNHDHLGNVSAQ----------------IAYSKVSK---RWNFPSPYYRL-----------RFKIPRTNVSVAIFM 154
Cdd:PTZ00422 100 FTVLGQADWDGNYNAEllkgqnvylnghgqtdIEYDSNNDiypKWIMPNYWYHYfthftdtsgpsLLKSGHKDMSVAFIF 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 155 LDTVTICgnsddflSQQPerprdlDLARTQLSW--LKKQLAAAKE--DYVLVAGHYPVWSiaeHGPTRC---LVKQLQPL 227
Cdd:PTZ00422 180 IDTWILS-------SSFP------YKKVSERAWqdLKATLEYAPKiaDYIIVVGDKPIYS---SGSSKGdsyLSYYLLPL 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 228 LATYGVTAYLCGHDHNLqYLQDENGVGYVLSGAGNfmdpskRHQRKVPNGYLRFHYGAEDSlgGFAYVEMSPKEMsVTYI 307
Cdd:PTZ00422 244 LKDAQVDLYISGYDRNM-EVLTDEGTAHINCGSGG------NSGRKSIMKNSKSLFYSEDI--GFCIHELNAEGM-VTKF 313

                        330       340
                 ....*....|....*....|
gi 829895215 308 EASGK----SLFKTSLPRRP 323
Cdd:PTZ00422 314 VSGNTgevlYTHKQPLKKRK 333
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 26-243 4.35e-11

purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; Purple acid phosphatases (PAPs) belong to a diverse family of binuclear metallohydrolases that have been identified and characterized in plants, animals, and fungi. PAPs contain a binuclear metal center and their characteristic pink or purple color derives from a charge-transfer transition between a tyrosine residue and a chromophoric ferric ion within the binuclear center. PAPs catalyze the hydrolysis of a wide range of activated phosphoric acid mono- and di-esters and anhydrides. PAPs are distinguished from the other phosphatases by their insensitivity to L-(+) tartrate inhibition and are therefore also known as tartrate resistant acid phosphatases (TRAPs). While only a few copies of PAP-like genes are present in mammalian and fungal genomes, multiple copies are present in plant genomes. PAPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277318 [Multi-domain]  Cd Length: 296  Bit Score: 62.70  E-value: 4.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215  26 LRFVAVGDWGGVPNAPFHTAREMANAKEiartvqtlGADFILSLGDNFYFTGvqDANDKR---FQETFEDVFSdrslrNV 102
Cdd:cd00839    5 LKFAVFGDMGQNTNNSTNTLDHLEKELG--------NYDAIIHVGDIAYADG--YNNGSRwdtFMRQIEPLAS-----YV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 103 PWYVLAGNHDHLGNVSAQIAYSKVSKRWNFPSP-------YYrlrfkiprtnvSVAIFMLDTVTICGNSDDFLSQQPERp 175
Cdd:cd00839   70 PYMVAPGNHEADYNGSTSKIKFFMPGRGMPPSPsgstenlWY-----------SFDVGPVHFISLSTETDFLKGDNISP- 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 829895215 176 rdldlartQLSWLKKQLAAA---KEDYVLVAGHYPvWSIAEHGPTRCLVK-----QLQPLLATYGVTAYLCGHDHN 243
Cdd:cd00839  138 --------QYDWLEADLAKVdrsRTPWIIVMGHRP-MYCSNDDDADCIEGekmreALEDLFYKYGVDLVLSGHVHA 204
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 63-256 2.68e-09

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: 56.96  E-value: 2.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215  63 ADFILSLGD--NFYFTgvqdanDKRFQETFEDVFSDRSLRNVPWYVLAGNHDhLGNVSAQiaYSKVSKRWN-FPSPYYRL 139
Cdd:cd07396   47 LAFVVQLGDiiDGYNA------KDRSKEALDAVLSILDRLKGPVHHVLGNHE-FYNFPRE--YLNHLKTLNgEDAYYYSF 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 140 RFKIPRTNVsvaifMLDTVTICGNsddflsqqperprdldLARTQLSWLKKQL--AAAKEDYVLVAGHYPVWSIAEHGpt 217
Cdd:cd07396  118 SPGPGFRFL-----VLDFVKFNGG----------------IGEEQLAWLRNELtsADANGEKVIVLSHLPIYPEAADP-- 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 829895215 218 RCLV---KQLQPLLATYG-VTAYLCGHDHNLQYLQDENGVGYV 256
Cdd:cd07396  175 QCLLwnyEEVLAILESYPcVKACFSGHNHEGGYEQDSHGVHHV 217
MPP_TMEM62_N cd07401
Homo sapiens TMEM62, N-terminal metallophosphatase domain; TMEM62 (transmembrane protein 62) ...
 104-245 3.08e-07

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: 50.83  E-value: 3.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 104 WYVLAGNHDHLGNVSAQIA---YSKVSKRwnFPSPYYRLRFKIPRTNVSvaifmldtvTICGNSDDFLSqqPERPRD--L 178
Cdd:cd07401   80 LFDIRGNHDLFGIVSFDSQnnyYRKYSNT--GRDHSHSFSSTTRFGNYS---------FIGFDPTIFPG--PKRPFNffG 146

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 829895215 179 DLARTQLSWLKKQLAAAKE-DYVLVAGHYPVWSIAEHGPtRCLVKQLQPLLATYGVTAYLCGHDHNLQ 245
Cdd:cd07401  147 SLDKKLLDRLEKELEKSKNsKYTIWFGHYPHSLIISPSA-KSSSKTFKDLLKKYNVTAYLCGHLHPLG 213
MPP_GpdQ cd07402
Enterobacter aerogenes GpdQ and related proteins, metallophosphatase domain; GpdQ ...
 101-243 9.91e-07

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: 49.20  E-value: 9.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 101 NVPWYVLAGNHDHlgnvsaQIAYSKVskrwnFPSPYYRLRFKIPRTnVSVA---IFMLDTV---TICGnsddFLSQQper 174
Cdd:cd07402   69 PAPVYWIPGNHDD------RAAMREA-----LPEPPYDDNGPVQYV-VDFGgwrLILLDTSvpgVHHG----ELSDE--- 129

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 829895215 175 prdldlartQLSWLKKQLAAAKEDYVLVAGHYPVWS--IAEHGPTRCLVKQ-LQPLLATY-GVTAYLCGHDHN 243
Cdd:cd07402  130 ---------QLDWLEAALAEAPDRPTLIFLHHPPFPlgIPWMDAIRLRNSQaLFAVLARHpQVKAILCGHIHR 193
MPP_1 cd07400
Uncharacterized subfamily, metallophosphatase domain; Uncharacterized subfamily of the MPP ...
 200-259 1.17e-06

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: 47.29  E-value: 1.17e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 829895215 200 VLVAGHYPVWSIAEHGPTRCLV---KQLQPLLATYGVTAYLCGHDH--NLQYLQDENGVGYVLSG 259
Cdd:cd07400   73 AIVALHHPLLPPPDTGRERNVLldaGDALKLLKELGVDLVLHGHKHvpAVWNLGLLNGIVVVNAG 137
SbcD COG0420
DNA repair exonuclease SbcCD nuclease subunit [Replication, recombination and repair];
27-259 2.70e-05

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


Pssm-ID: 440189 [Multi-domain]  Cd Length: 250  Bit Score: 44.90  E-value: 2.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215  27 RFVAVGDW--GgvpnAPFHtAREMANA-----KEIARTVQTLGADFILSLGDNFyftgvqDAN--DKRFQETFEDVFSDR 97
Cdd:COG0420    2 RFLHTADWhlG----KPLH-GASRREDqlaalDRLVDLAIEEKVDAVLIAGDLF------DSAnpSPEAVRLLAEALRRL 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215  98 SLRNVPWYVLAGNHDHLGnvsaqiayskvskRWNFPSPYYRlrfkipRTNVSV-AIFMLDTVTICGNSD------DFLsq 170
Cdd:COG0420   71 SEAGIPVVLIAGNHDSPS-------------RLSAGSPLLE------NLGVHVfGSVEPEPVELEDGLGvavyglPYL-- 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 171 qpeRPRDLDLARTQLSWLKKQLAAAKedYVLVAGHYPVWSIAEHGPTRCLVKQLQPLLATyGVTAYLCGHDHNLQYLQDE 250
Cdd:COG0420  130 ---RPSDEEALRDLLERLPRALDPGG--PNILLLHGFVAGASGSRDIYVAPVPLSALPAA-GFDYVALGHIHRPQVLGGD 203


                 ....*....
gi 829895215 251 NGVGYvlSG 259
Cdd:COG0420  204 PRIRY--SG 210
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 26-137 3.19e-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: 42.59  E-value: 3.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215   26 LRFVAVGDWGGVPNAPfhtaremANAKEIARTVQTLGADFILSLGDNFyftgvqdaNDKRFQETFEDVFsDRSLRNVPWY 105
Cdd:pfam00149   1 MRILVIGDLHLPGQLD-------DLLELLKKLLEEGKPDLVLHAGDLV--------DRGPPSEEVLELL-ERLIKYVPVY 64

                          90       100       110
                  ....*....|....*....|....*....|....
gi 829895215  106 VLAGNHD--HLGNVSAQIAYSKVSKRWNFPSPYY 137
Cdd:pfam00149  65 LVRGNHDfdYGECLRLYPYLGLLARPWKRFLEVF 98
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 187-257 3.86e-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: 42.64  E-value: 3.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 187 WLKKQLAAAKEDYVLVAG-------HYPVWSIAEHG--PTRCLVKQLQPLLATYGVTAYLCGHDHNLQYLQDENGVGYVL 257
Cdd:cd00838   48 LKALRLLLAGIPVYVVPGnhdilvtHGPPYDPLDEGspGEDPGSEALLELLDKYGPDLVLSGHTHVPGRREVDKGGTLVV 127
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 43-114 1.29e-04

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


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 41.10  E-value: 1.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 829895215  43 HTAREMANAKEIARTVQTLGADFILSLGDNFYFTGVQDANDKRFQEtfedvfsdRSLRNVPWYVLAGNHDHL 114
Cdd:cd00838    7 HGNLEALEAVLEAALAKAEKPDLVICLGDLVDYGPDPEEVELKALR--------LLLAGIPVYVVPGNHDIL 70
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 39-242 1.82e-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: 42.67  E-value: 1.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215  39 NAPFHTARE-MANAKEIArtvqtLGADFILSLGDNfyftgVQDANDKRFQETFEDVFS------DRSLRNVPWYVLAGNH 111
Cdd:cd00842   50 DSPWSLVESaLEAIKKNH-----PKPDFILWTGDL-----VRHDVDEQTPEETVESESnltnllKKYFPNVPVYPALGNH 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 112 DhlGNVSAQIAYSKVSKRWNF------PSP--------------YYrlrFKIPRTNVSVaIFmLDTVtICGNSDDFLSQQ 171
Cdd:cd00842  120 D--SYPVNQFPPHSNSPSWLYdalaelWKPwlpteaketfkkggYY---SVDVKDGLRV-IS-LNTN-LYYKKNFWLYSN 191

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 829895215 172 PERPRDldlartQLSWLKKQLAAAKE--DYVLVAGH-YPVWSIAEHGPTRCLVKqlqpLLATYG--VTAYLCGHDH 242
Cdd:cd00842  192 NTDPCG------QLQWLEDELEDAEQkgEKVWIIGHiPPGLNSYDADWSERFYQ----IINRYSdtIAGQFFGHTH 257
PhoD COG3540
Phosphodiesterase/alkaline phosphatase D [Inorganic ion transport and metabolism];
20-196 4.25e-04

Phosphodiesterase/alkaline phosphatase D [Inorganic ion transport and metabolism];


Pssm-ID: 442761 [Multi-domain]  Cd Length: 482  Bit Score: 41.83  E-value: 4.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215  20 GSAAPALRFVAVGDWGGvPNAPFHTAREMANAKeiartvqtlgADFILSLGDNFYFTGVQDANDKRFQ--------ETFE 91
Cdd:COG3540  129 PGAPDRLRFAFASCQNY-EGGYFTAYRAMAEED----------PDFVLHLGDYIYEDGPGPYGLPGLWrpepskeaETLA 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215  92 D-------VFSDRSLR----NVPWYVLAGNHDHLGNvsaqiAYSKVSKRWNFPSPYYRLRFK-----------IPRTNVS 149
Cdd:COG3540  198 DyrgryaqYRSDPDLQalhaAVPWIATWDDHEVANN-----WAGGGAEHDRYTEGDFAARRAaalqafyeympIRRPGPD 272

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 829895215 150 ---------------VAIFMLDTVTICGNSDDFLSQQPERP-RDLdLARTQLSWLKKQLAAAK 196
Cdd:COG3540  273 gddgriyrrfrygdlADLFMLDTRSYRDPQPCLQCPEADDPdRTL-LGAEQLAWLKDGLAAST 334
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
27-243 7.36e-04

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 40.00  E-value: 7.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215  27 RFVAVGDWGGvpnapfhtarEMANAKEIARTVQTLGADFILSLGDnfyFTgvqdanDKRFQETFEDVFSDRSLRNVPWYV 106
Cdd:COG2129    1 KILAVSDLHG----------NFDLLEKLLELARAEDADLVILAGD---LT------DFGTAEEAREVLEELAALGVPVLA 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215 107 LAGNHDhlgnvsaqiayskvskrwnfpspYYRLRFKIPRTNVSVA---IFMLDTVTICGnsddfLSQQPERPRDLDLART 183
Cdd:COG2129   62 VPGNHD-----------------------DPEVLDALEESGVHNLhgrVVEIGGLRIAG-----LGGSRPTPFGTPYEYT 113

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 829895215 184 QlSWLKKQLAAAKEDY--VLVAgHYP--------VWSIAEHGPTRC--LVKQLQPLLAtygvtayLCGHDHN 243
Cdd:COG2129  114 E-EEIEERLAKLREKDvdILLT-HAPpygttldrVEDGPHVGSKALreLIEEFQPKLV-------LHGHIHE 176
MPP_Mre11_N cd00840
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ...
 27-114 9.84e-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: 36.48  E-value: 9.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 829895215  27 RFVAVGDW--GgvpnAPFHTAREMANA-----KEIARTVQTLGADFILSLGDNFyftgvqDANDKRF--QETFEDVFSDR 97
Cdd:cd00840    1 RFLHTADWhlG----YPLYGLSRREEDffkafEEIVDLAIEEKVDFVLIAGDLF------DSNNPSPeaLKLAIEGLRRL 70

                         90
                 ....*....|....*..
gi 829895215  98 SLRNVPWYVLAGNHDHL 114
Cdd:cd00840   71 CEAGIPVFVIAGNHDSP 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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