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Conserved domains on  [gi|24307911|ref|NP_006705|]
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cyclic GMP-AMP phosphodiesterase SMPDL3A isoform a precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 40-336 9.77e-113

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: 333.50  E-value: 9.77e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911  40 FWHVTDLHLDPTYHITDDHTkVCASSKGANASNP--------GPFGDVLCDSPYQLILSAFDFIKNSGQEASFMIWTGDS 111
Cdd:cd00842   1 FLHISDIHYDPLYKVGSEYA-NCRSPLCCRDESGpgdvkppaGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911 112 PPHVpVPELSTDTVINVITNMTTTIQSLFPNLQVFPALGNHDYWPQDQLPVVT---SKVYNAVANLWKPWLDEEAISTLR 188
Cdd:cd00842  80 VRHD-VDEQTPEETVESESNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHSnspSWLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911 189 KGGFYSQKVttNPNLRIISLNTNLYYGPNIMTL-NKTDPANQFEWLESTLNNSQQNKEKVYIIAHVPVGYLPSSQNitam 267
Cdd:cd00842 159 KGGYYSVDV--KDGLRVISLNTNLYYKKNFWLYsNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDAD---- 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24307911 268 reyYNEKLIDIFQKYSDVIAGQFYGHTHRDSIMVLSDKK--GSPVNSLFVAPAVTPVksvlekQTNNPGIR 336
Cdd:cd00842 233 ---WSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKdtGSPINVAYIAPSVTPY------TGNNPSFR 294
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 308-450 2.65e-101

Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the C-terminal region of the phosphodiesterase domain found in acid sphingomyelin phosphodiesterases. It contains two disulphide bridges.


:

Pssm-ID: 466022  Cd Length: 143  Bit Score: 298.52  E-value: 2.65e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911   308 SPVNSLFVAPAVTPVKSVLEKQTNNPGIRLFQYDPRDYKLLDMLQYYLNLTEANLKGESIWKLEYILTQTYDIEDLQPES 387
Cdd:pfam19272   1 NPVNSLFVAPAVTPVKSVLEKESNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPQS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24307911   388 LYGLAKQFTILDSKQFIKYYNYFFVSYDSSVTCDKTCKAFQICAIMNLDNISYADCLKQLYIK 450
Cdd:pfam19272  81 LYGLAKQFAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQICAIMYLDYSSYTDCIKQYAMK 143
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 40-336 9.77e-113

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: 333.50  E-value: 9.77e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911  40 FWHVTDLHLDPTYHITDDHTkVCASSKGANASNP--------GPFGDVLCDSPYQLILSAFDFIKNSGQEASFMIWTGDS 111
Cdd:cd00842   1 FLHISDIHYDPLYKVGSEYA-NCRSPLCCRDESGpgdvkppaGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911 112 PPHVpVPELSTDTVINVITNMTTTIQSLFPNLQVFPALGNHDYWPQDQLPVVT---SKVYNAVANLWKPWLDEEAISTLR 188
Cdd:cd00842  80 VRHD-VDEQTPEETVESESNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHSnspSWLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911 189 KGGFYSQKVttNPNLRIISLNTNLYYGPNIMTL-NKTDPANQFEWLESTLNNSQQNKEKVYIIAHVPVGYLPSSQNitam 267
Cdd:cd00842 159 KGGYYSVDV--KDGLRVISLNTNLYYKKNFWLYsNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDAD---- 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24307911 268 reyYNEKLIDIFQKYSDVIAGQFYGHTHRDSIMVLSDKK--GSPVNSLFVAPAVTPVksvlekQTNNPGIR 336
Cdd:cd00842 233 ---WSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKdtGSPINVAYIAPSVTPY------TGNNPSFR 294
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 308-450 2.65e-101

Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the C-terminal region of the phosphodiesterase domain found in acid sphingomyelin phosphodiesterases. It contains two disulphide bridges.


Pssm-ID: 466022  Cd Length: 143  Bit Score: 298.52  E-value: 2.65e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911   308 SPVNSLFVAPAVTPVKSVLEKQTNNPGIRLFQYDPRDYKLLDMLQYYLNLTEANLKGESIWKLEYILTQTYDIEDLQPES 387
Cdd:pfam19272   1 NPVNSLFVAPAVTPVKSVLEKESNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPQS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24307911   388 LYGLAKQFTILDSKQFIKYYNYFFVSYDSSVTCDKTCKAFQICAIMNLDNISYADCLKQLYIK 450
Cdd:pfam19272  81 LYGLAKQFAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQICAIMYLDYSSYTDCIKQYAMK 143
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
40-342 1.02e-08

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 55.47  E-value: 1.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911  40 FWHVTDLHLDPTyhitddhtkvcassKGANAsnpgpfgdvlcdspYQLILSAFDFIKNsgQEASFMIWTGDspphvpvpe 119
Cdd:COG1409   3 FAHISDLHLGAP--------------DGSDT--------------AEVLAAALADINA--PRPDFVVVTGD--------- 43

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911 120 lstdtvinvITNMTTTIQ-----SLFPNLQ--VFPALGNHDYWpqdqlpvvtskvyNAVANLWkpwldEEAISTLRKGGF 192
Cdd:COG1409  44 ---------LTDDGEPEEyaaarEILARLGvpVYVVPGNHDIR-------------AAMAEAY-----REYFGDLPPGGL 96

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911 193 YSqkVTTNPNLRIISLNTNLYYGPNimtlNKTDPAnQFEWLESTLnnSQQNKEKVYIIAHVPVgyLPSSQNITAMREYYN 272
Cdd:COG1409  97 YY--SFDYGGVRFIGLDSNVPGRSS----GELGPE-QLAWLEEEL--AAAPAKPVIVFLHHPP--YSTGSGSDRIGLRNA 165

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24307911 273 EKLIDIFQKYS-DVIagqFYGHTHRDSImvlSDKKGSPVnslFVAPAVTPvksvleKQTNNPGIRLFQYDP 342
Cdd:COG1409 166 EELLALLARYGvDLV---LSGHVHRYER---TRRDGVPY---IVAGSTGG------QVRLPPGYRVIEVDG 221
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 40-336 9.77e-113

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: 333.50  E-value: 9.77e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911  40 FWHVTDLHLDPTYHITDDHTkVCASSKGANASNP--------GPFGDVLCDSPYQLILSAFDFIKNSGQEASFMIWTGDS 111
Cdd:cd00842   1 FLHISDIHYDPLYKVGSEYA-NCRSPLCCRDESGpgdvkppaGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911 112 PPHVpVPELSTDTVINVITNMTTTIQSLFPNLQVFPALGNHDYWPQDQLPVVT---SKVYNAVANLWKPWLDEEAISTLR 188
Cdd:cd00842  80 VRHD-VDEQTPEETVESESNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHSnspSWLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911 189 KGGFYSQKVttNPNLRIISLNTNLYYGPNIMTL-NKTDPANQFEWLESTLNNSQQNKEKVYIIAHVPVGYLPSSQNitam 267
Cdd:cd00842 159 KGGYYSVDV--KDGLRVISLNTNLYYKKNFWLYsNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDAD---- 232

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24307911 268 reyYNEKLIDIFQKYSDVIAGQFYGHTHRDSIMVLSDKK--GSPVNSLFVAPAVTPVksvlekQTNNPGIR 336
Cdd:cd00842 233 ---WSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKdtGSPINVAYIAPSVTPY------TGNNPSFR 294
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 308-450 2.65e-101

Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the C-terminal region of the phosphodiesterase domain found in acid sphingomyelin phosphodiesterases. It contains two disulphide bridges.


Pssm-ID: 466022  Cd Length: 143  Bit Score: 298.52  E-value: 2.65e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911   308 SPVNSLFVAPAVTPVKSVLEKQTNNPGIRLFQYDPRDYKLLDMLQYYLNLTEANLKGESIWKLEYILTQTYDIEDLQPES 387
Cdd:pfam19272   1 NPVNSLFVAPAVTPVKSVLEKESNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPQS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24307911   388 LYGLAKQFTILDSKQFIKYYNYFFVSYDSSVTCDKTCKAFQICAIMNLDNISYADCLKQLYIK 450
Cdd:pfam19272  81 LYGLAKQFAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQICAIMYLDYSSYTDCIKQYAMK 143
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
40-342 1.02e-08

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 55.47  E-value: 1.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911  40 FWHVTDLHLDPTyhitddhtkvcassKGANAsnpgpfgdvlcdspYQLILSAFDFIKNsgQEASFMIWTGDspphvpvpe 119
Cdd:COG1409   3 FAHISDLHLGAP--------------DGSDT--------------AEVLAAALADINA--PRPDFVVVTGD--------- 43

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911 120 lstdtvinvITNMTTTIQ-----SLFPNLQ--VFPALGNHDYWpqdqlpvvtskvyNAVANLWkpwldEEAISTLRKGGF 192
Cdd:COG1409  44 ---------LTDDGEPEEyaaarEILARLGvpVYVVPGNHDIR-------------AAMAEAY-----REYFGDLPPGGL 96

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911 193 YSqkVTTNPNLRIISLNTNLYYGPNimtlNKTDPAnQFEWLESTLnnSQQNKEKVYIIAHVPVgyLPSSQNITAMREYYN 272
Cdd:COG1409  97 YY--SFDYGGVRFIGLDSNVPGRSS----GELGPE-QLAWLEEEL--AAAPAKPVIVFLHHPP--YSTGSGSDRIGLRNA 165

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24307911 273 EKLIDIFQKYS-DVIagqFYGHTHRDSImvlSDKKGSPVnslFVAPAVTPvksvleKQTNNPGIRLFQYDP 342
Cdd:COG1409 166 EELLALLARYGvDLV---LSGHVHRYER---TRRDGVPY---IVAGSTGG------QVRLPPGYRVIEVDG 221
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 142-296 6.02e-07

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: 50.41  E-value: 6.02e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911 142 NLQVFPALGNHDYwpqdqlpvvtskvynavANLWKPWLDEEAISTLRKGGFYSQKvtTNPNLRIISLNTNLYYGpnimTL 221
Cdd:cd07396  81 KGPVHHVLGNHEF-----------------YNFPREYLNHLKTLNGEDAYYYSFS--PGPGFRFLVLDFVKFNG----GI 137

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24307911 222 NKTdpanQFEWLESTLNNSQQNKEKVYIIAHVPVgYLPSSQNITAMREYynEKLIDIFQKYSDVIAgQFYGHTHR 296
Cdd:cd07396 138 GEE----QLAWLRNELTSADANGEKVIVLSHLPI-YPEAADPQCLLWNY--EEVLAILESYPCVKA-CFSGHNHE 204
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 136-295 3.82e-05

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: 45.37  E-value: 3.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911 136 IQSLFPNLQVFPALGNHDYWPQDQlpvvTSKVYNAVANLWKPWLDeeaiSTLRKGGFYSqkvTTNPNLRIISLNTNLYYG 215
Cdd:cd00839  62 IEPLASYVPYMVAPGNHEADYNGS----TSKIKFFMPGRGMPPSP----SGSTENLWYS---FDVGPVHFISLSTETDFL 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24307911 216 PnimtlnKTDPANQFEWLESTLnnSQQNKEKV-YIIA--HVPVGYlpSSQNITAMREYYN--EKLIDIFQKYS-DVIagq 289
Cdd:cd00839 131 K------GDNISPQYDWLEADL--AKVDRSRTpWIIVmgHRPMYC--SNDDDADCIEGEKmrEALEDLFYKYGvDLV--- 197


                ....*.
gi 24307911 290 FYGHTH 295
Cdd:cd00839 198 LSGHVH 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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