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Conserved domains on  [gi|78042502|ref|NP_001030191|]
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acid sphingomyelinase-like phosphodiesterase 3a precursor [Bos taurus]

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 ...
 37-333 1.35e-112

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: 333.11  E-value: 1.35e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502  37 FWHVTDFHLDPTYHITGDHTkVCASS--------KGAEASDPGPFGDVMCDSPYRLIFSALDFIKNSGQKVSFMIWTGDS 108
Cdd:cd00842   1 FLHISDIHYDPLYKVGSEYA-NCRSPlccrdesgPGDVKPPAGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502 109 PPHVPVLELSTDKVINvTANITTTIQRLFPNLQVFPALGNHDYWPQDQLPVVN---SKVYNAVANLWKPWLTEDAITTLR 185
Cdd:cd00842  80 VRHDVDEQTPEETVES-ESNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHSnspSWLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502 186 KGGFYTQKVSnnPKLRIISLNTNLYYGPNSVTL-NQTDPANQFEWLENTLNISQQNKEKVYIIAHVPVGYLPYArgisam 264
Cdd:cd00842 159 KGGYYSVDVK--DGLRVISLNTNLYYKKNFWLYsNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYD------ 230

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78042502 265 rKYHNEKLIDIFRKYSDIIAGQFYGHTHRDSIMVLSDKK--GKPVNSLFVAPAVTPVRsvlerlTNNPGVR 333
Cdd:cd00842 231 -ADWSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKdtGSPINVAYIAPSVTPYT------GNNPSFR 294
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 305-447 8.80e-100

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: 294.66  E-value: 8.80e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502   305 KPVNSLFVAPAVTPVRSVLERLTNNPGVRLFQYDPRDYKLLDMLQYYLNLTDANLKGESNWKLEYNLTQAYDIQDLQPKS 384
Cdd:pfam19272   1 NPVNSLFVAPAVTPVKSVLEKESNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPQS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78042502   385 LYKLAKQFAIQESKQFIKYYKYFFVSYDSSVICQGKCKIFQICAIMNLDVISYTDCFRQYHMK 447
Cdd:pfam19272  81 LYGLAKQFAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQICAIMYLDYSSYTDCIKQYAMK 143
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 37-333 1.35e-112

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: 333.11  E-value: 1.35e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502  37 FWHVTDFHLDPTYHITGDHTkVCASS--------KGAEASDPGPFGDVMCDSPYRLIFSALDFIKNSGQKVSFMIWTGDS 108
Cdd:cd00842   1 FLHISDIHYDPLYKVGSEYA-NCRSPlccrdesgPGDVKPPAGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502 109 PPHVPVLELSTDKVINvTANITTTIQRLFPNLQVFPALGNHDYWPQDQLPVVN---SKVYNAVANLWKPWLTEDAITTLR 185
Cdd:cd00842  80 VRHDVDEQTPEETVES-ESNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHSnspSWLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502 186 KGGFYTQKVSnnPKLRIISLNTNLYYGPNSVTL-NQTDPANQFEWLENTLNISQQNKEKVYIIAHVPVGYLPYArgisam 264
Cdd:cd00842 159 KGGYYSVDVK--DGLRVISLNTNLYYKKNFWLYsNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYD------ 230

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78042502 265 rKYHNEKLIDIFRKYSDIIAGQFYGHTHRDSIMVLSDKK--GKPVNSLFVAPAVTPVRsvlerlTNNPGVR 333
Cdd:cd00842 231 -ADWSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKdtGSPINVAYIAPSVTPYT------GNNPSFR 294
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 305-447 8.80e-100

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: 294.66  E-value: 8.80e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502   305 KPVNSLFVAPAVTPVRSVLERLTNNPGVRLFQYDPRDYKLLDMLQYYLNLTDANLKGESNWKLEYNLTQAYDIQDLQPKS 384
Cdd:pfam19272   1 NPVNSLFVAPAVTPVKSVLEKESNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPQS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78042502   385 LYKLAKQFAIQESKQFIKYYKYFFVSYDSSVICQGKCKIFQICAIMNLDVISYTDCFRQYHMK 447
Cdd:pfam19272  81 LYGLAKQFAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQICAIMYLDYSSYTDCIKQYAMK 143
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
37-339 1.44e-08

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 55.08  E-value: 1.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502  37 FWHVTDFHLDPTyhiTGDHTkvcasskgaeasdpgpfgdvmcdspYRLIFSALDFIKNsgQKVSFMIWTGDspphvpvle 116
Cdd:COG1409   3 FAHISDLHLGAP---DGSDT-------------------------AEVLAAALADINA--PRPDFVVVTGD--------- 43

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502 117 LSTDKVINVTANITTTIQRLfpNLQVFPALGNHDYWpqdqlpVVNSKVYNAVANLWKPwltedaittlrKGGFYTQKVSN 196
Cdd:COG1409  44 LTDDGEPEEYAAAREILARL--GVPVYVVPGNHDIR------AAMAEAYREYFGDLPP-----------GGLYYSFDYGG 104

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502 197 npkLRIISLNTNLYYGPNSVTlnqtdPANQFEWLENTLniSQQNKEKVYIIAHVPVgyLPYARGISAMRKYHNEKLIDIF 276
Cdd:COG1409 105 ---VRFIGLDSNVPGRSSGEL-----GPEQLAWLEEEL--AAAPAKPVIVFLHHPP--YSTGSGSDRIGLRNAEELLALL 172

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78042502 277 RKYS-DIIagqFYGHTHRDSImvlSDKKGKPVnslFVAPAVTPvrsvleRLTNNPGVRLFQYDP 339
Cdd:COG1409 173 ARYGvDLV---LSGHVHRYER---TRRDGVPY---IVAGSTGG------QVRLPPGYRVIEVDG 221
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 37-333 1.35e-112

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: 333.11  E-value: 1.35e-112
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502  37 FWHVTDFHLDPTYHITGDHTkVCASS--------KGAEASDPGPFGDVMCDSPYRLIFSALDFIKNSGQKVSFMIWTGDS 108
Cdd:cd00842   1 FLHISDIHYDPLYKVGSEYA-NCRSPlccrdesgPGDVKPPAGYWGTYGCDSPWSLVESALEAIKKNHPKPDFILWTGDL 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502 109 PPHVPVLELSTDKVINvTANITTTIQRLFPNLQVFPALGNHDYWPQDQLPVVN---SKVYNAVANLWKPWLTEDAITTLR 185
Cdd:cd00842  80 VRHDVDEQTPEETVES-ESNLTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHSnspSWLYDALAELWKPWLPTEAKETFK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502 186 KGGFYTQKVSnnPKLRIISLNTNLYYGPNSVTL-NQTDPANQFEWLENTLNISQQNKEKVYIIAHVPVGYLPYArgisam 264
Cdd:cd00842 159 KGGYYSVDVK--DGLRVISLNTNLYYKKNFWLYsNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYD------ 230

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 78042502 265 rKYHNEKLIDIFRKYSDIIAGQFYGHTHRDSIMVLSDKK--GKPVNSLFVAPAVTPVRsvlerlTNNPGVR 333
Cdd:cd00842 231 -ADWSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKdtGSPINVAYIAPSVTPYT------GNNPSFR 294
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 305-447 8.80e-100

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: 294.66  E-value: 8.80e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502   305 KPVNSLFVAPAVTPVRSVLERLTNNPGVRLFQYDPRDYKLLDMLQYYLNLTDANLKGESNWKLEYNLTQAYDIQDLQPKS 384
Cdd:pfam19272   1 NPVNSLFVAPAVTPVKSVLEKESNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPQS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78042502   385 LYKLAKQFAIQESKQFIKYYKYFFVSYDSSVICQGKCKIFQICAIMNLDVISYTDCFRQYHMK 447
Cdd:pfam19272  81 LYGLAKQFAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQICAIMYLDYSSYTDCIKQYAMK 143
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
37-339 1.44e-08

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 55.08  E-value: 1.44e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502  37 FWHVTDFHLDPTyhiTGDHTkvcasskgaeasdpgpfgdvmcdspYRLIFSALDFIKNsgQKVSFMIWTGDspphvpvle 116
Cdd:COG1409   3 FAHISDLHLGAP---DGSDT-------------------------AEVLAAALADINA--PRPDFVVVTGD--------- 43

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502 117 LSTDKVINVTANITTTIQRLfpNLQVFPALGNHDYWpqdqlpVVNSKVYNAVANLWKPwltedaittlrKGGFYTQKVSN 196
Cdd:COG1409  44 LTDDGEPEEYAAAREILARL--GVPVYVVPGNHDIR------AAMAEAYREYFGDLPP-----------GGLYYSFDYGG 104

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502 197 npkLRIISLNTNLYYGPNSVTlnqtdPANQFEWLENTLniSQQNKEKVYIIAHVPVgyLPYARGISAMRKYHNEKLIDIF 276
Cdd:COG1409 105 ---VRFIGLDSNVPGRSSGEL-----GPEQLAWLEEEL--AAAPAKPVIVFLHHPP--YSTGSGSDRIGLRNAEELLALL 172

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78042502 277 RKYS-DIIagqFYGHTHRDSImvlSDKKGKPVnslFVAPAVTPvrsvleRLTNNPGVRLFQYDP 339
Cdd:COG1409 173 ARYGvDLV---LSGHVHRYER---TRRDGVPY---IVAGSTGG------QVRLPPGYRVIEVDG 221
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 139-293 9.96e-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: 49.64  E-value: 9.96e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502 139 NLQVFPALGNHDYwpqdqlpvvnskvynavANLWKPWLTEdAITTLRKGGFYTQkVSNNPKLRIISLNTNLYYGPNSvtl 218
Cdd:cd07396  81 KGPVHHVLGNHEF-----------------YNFPREYLNH-LKTLNGEDAYYYS-FSPGPGFRFLVLDFVKFNGGIG--- 138

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78042502 219 nqtdpANQFEWLENTLNISQQNKEKVYIIAHVPVgyLPYargisAMRKYHN----EKLIDIFRKYSDIIAgQFYGHTHR 293
Cdd:cd07396 139 -----EEQLAWLRNELTSADANGEKVIVLSHLPI--YPE-----AADPQCLlwnyEEVLAILESYPCVKA-CFSGHNHE 204
CE4_PelA_like_C cd10922
C-terminal Putative NodB-like catalytic domain of PelA-like uncharacterized hypothetical ...
 80-173 1.44e-03

C-terminal Putative NodB-like catalytic domain of PelA-like uncharacterized hypothetical proteins found in bacteria; This family is represented by a protein PelA of unknown function that is encoded by a gene in the pelA-G gene cluster for pellicle production and biofilm formation in Pseudomonas aeruginosa. PelA and most of the family members contain a domain of unknown function, DUF297, in the N-terminus and a C-terminal domain that shows high sequence similarity to the catalytic domain of the six-stranded barrel rhizobial NodB-like proteins, which remove N-linked or O-linked acetyl groups from cell wall polysaccharides and belong to the larger carbohydrate esterase 4 (CE4) superfamily.


Pssm-ID: 200548  Cd Length: 266  Bit Score: 40.38  E-value: 1.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502  80 SPYRLIFSALDFIKNS----GQKVSFMIWTGDSPPHVPVLELSTD-KVINVTANiTTTIQRLFPNL-QVFPALGNHDYWP 153
Cdd:cd10922 118 DLHREIVGSTDYINERlappGKPVRVLLWSGDCLPPAAAVALAYEaGLLNMNGG-DTRISRTNPSLtAVSPLGRPVGGYL 196

                        90       100
                ....*....|....*....|
gi 78042502 154 QDQLPVVNSKVYnavANLWK 173
Cdd:cd10922 197 QVYAPLSNENVY---TNLWT 213
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 133-292 3.37e-03

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: 39.20  E-value: 3.37e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502 133 IQRLFPNLQVFPALGNHDYWPQDQLPVVNSKVYNavanlwkPWLTEDAITTLRKGgFYtqkvS-NNPKLRIISLNTNLYY 211
Cdd:cd00839  62 IEPLASYVPYMVAPGNHEADYNGSTSKIKFFMPG-------RGMPPSPSGSTENL-WY----SfDVGPVHFISLSTETDF 129

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78042502 212 GPNsvtlnqTDPANQFEWLENTLniSQQNKEKV-YIIA--HVPVG--YLPYARGISAMRKYhnEKLIDIFRKYS-DIIag 285
Cdd:cd00839 130 LKG------DNISPQYDWLEADL--AKVDRSRTpWIIVmgHRPMYcsNDDDADCIEGEKMR--EALEDLFYKYGvDLV-- 197


                ....*..
gi 78042502 286 qFYGHTH 292
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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