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Conserved domains on  [gi|937432790|gb|ALI30470|]
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uncharacterized protein Dmel_CG32052, isoform D [Drosophila melanogaster]

Protein Classification

acid sphingomyelinase family protein( domain architecture ID 17655516)

acid sphingomyelinase family protein such as human acid sphingomyelinase-like phosphodiesterase 3b, a lipid-modulating phosphodiesterase active on the surface of macrophages and dendritic cells

CATH:  3.60.21.10
EC:  3.1.4.-
Gene Ontology:  GO:0004767|GO:0046872|GO:0006685
PubMed:  15052326|19536191|23579450|8003970|25837850

Graphical summary

 Zoom to residue level

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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 ...
 28-351 4.44e-70

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: 225.64  E-value: 4.44e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790  28 FWHISDLHLDTLYSTqGDIYRSCwelaRSVSGSNANSAA---SEPPGPFGHYNCDSPWRLIESAVKTMKaKQGDNVEFVL 104
Cdd:cd00842    1 FLHISDIHYDPLYKV-GSEYANC----RSPLCCRDESGPgdvKPPAGYWGTYGCDSPWSLVESALEAIK-KNHPKPDFIL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790 105 WTGDALSHSAQPLSEQKQHEILRNITELLGRSFSSQFIFPVLG-HE---------DGSGS---YRRLGELWRHWLPSEAL 171
Cdd:cd00842   75 WTGDLVRHDVDEQTPEETVESESNLTNLLKKYFPNVPVYPALGnHDsypvnqfppHSNSPswlYDALAELWKPWLPTEAK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790 172 VTFDQGGYYSIEqTKSRLRIVALNTNF--------MRLDPDPDpraslslrwpaeyfaepkasvssisaedellaeQQWL 243
Cdd:cd00842  155 ETFKKGGYYSVD-VKDGLRVISLNTNLyykknfwlYSNNTDPC---------------------------------GQLQ 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790 244 WLEEVLTKSKEKQETVYIVGHMPPGVDErhlgtqhnqltFTERNNQRYLDMVRRFAPVIQGQFFGHLHSDTFRLIYDAK- 322
Cdd:cd00842  201 WLEDELEDAEQKGEKVWIIGHIPPGLNS-----------YDADWSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKd 269

                        330       340       350
                 ....*....|....*....|....*....|
gi 937432790 323 -GNPISWLMIAPSIVPRkagigSSNNPALR 351
Cdd:cd00842  270 tGSPINVAYIAPSVTPY-----TGNNPSFR 294
ASMase_C super family cl44707
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 324-462 7.55e-25

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.


The actual alignment was detected with superfamily member pfam19272:

Pssm-ID: 466022  Cd Length: 143  Bit Score: 100.14  E-value: 7.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790  324 NPISWLMIAPSIVPRKAGIG-SSNNPALRLYKFDTGSGQVLDYTQFWLDLPLANRANEPTWQPEYNLTHYYALPEISAVA 402
Cdd:pfam19272   1 NPVNSLFVAPAVTPVKSVLEkESNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPQS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790  403 LHNFAERFTGTDLSWFTRYHRANAVRYHSGSACPGLCMLNHYCAITRLDYDEFRICLEKE 462
Cdd:pfam19272  81 LYGLAKQFAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQICAIMYLDYSSYTDCIKQY 140
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 28-351 4.44e-70

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: 225.64  E-value: 4.44e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790  28 FWHISDLHLDTLYSTqGDIYRSCwelaRSVSGSNANSAA---SEPPGPFGHYNCDSPWRLIESAVKTMKaKQGDNVEFVL 104
Cdd:cd00842    1 FLHISDIHYDPLYKV-GSEYANC----RSPLCCRDESGPgdvKPPAGYWGTYGCDSPWSLVESALEAIK-KNHPKPDFIL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790 105 WTGDALSHSAQPLSEQKQHEILRNITELLGRSFSSQFIFPVLG-HE---------DGSGS---YRRLGELWRHWLPSEAL 171
Cdd:cd00842   75 WTGDLVRHDVDEQTPEETVESESNLTNLLKKYFPNVPVYPALGnHDsypvnqfppHSNSPswlYDALAELWKPWLPTEAK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790 172 VTFDQGGYYSIEqTKSRLRIVALNTNF--------MRLDPDPDpraslslrwpaeyfaepkasvssisaedellaeQQWL 243
Cdd:cd00842  155 ETFKKGGYYSVD-VKDGLRVISLNTNLyykknfwlYSNNTDPC---------------------------------GQLQ 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790 244 WLEEVLTKSKEKQETVYIVGHMPPGVDErhlgtqhnqltFTERNNQRYLDMVRRFAPVIQGQFFGHLHSDTFRLIYDAK- 322
Cdd:cd00842  201 WLEDELEDAEQKGEKVWIIGHIPPGLNS-----------YDADWSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKd 269

                        330       340       350
                 ....*....|....*....|....*....|
gi 937432790 323 -GNPISWLMIAPSIVPRkagigSSNNPALR 351
Cdd:cd00842  270 tGSPINVAYIAPSVTPY-----TGNNPSFR 294
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 324-462 7.55e-25

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: 100.14  E-value: 7.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790  324 NPISWLMIAPSIVPRKAGIG-SSNNPALRLYKFDTGSGQVLDYTQFWLDLPLANRANEPTWQPEYNLTHYYALPEISAVA 402
Cdd:pfam19272   1 NPVNSLFVAPAVTPVKSVLEkESNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPQS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790  403 LHNFAERFTGTDLSWFTRYHRANAVRYHSGSACPGLCMLNHYCAITRLDYDEFRICLEKE 462
Cdd:pfam19272  81 LYGLAKQFAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQICAIMYLDYSSYTDCIKQY 140
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
28-311 3.65e-07

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 51.23  E-value: 3.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790  28 FWHISDLHldtlystqgdiyrscwelarsvsgsnansaaseppgpFGHYNCDSPWRLIESAVKTMKAKQGDnveFVLWTG 107
Cdd:COG1409    3 FAHISDLH-------------------------------------LGAPDGSDTAEVLAAALADINAPRPD---FVVVTG 42

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790 108 DaLSHSAQPlseqKQHEILRNITELLGRSFssqfiFPVLG-HEDGSGSYRRLGELWRHWLPSEALVTFDQGGYysieqtk 186
Cdd:COG1409   43 D-LTDDGEP----EEYAAAREILARLGVPV-----YVVPGnHDIRAAMAEAYREYFGDLPPGGLYYSFDYGGV------- 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790 187 srlRIVALNTNfmrldpdpdpraslslrWPAEYFAEpkasvssisaedelLAEQQWLWLEEVLTKSKEKqeTVYIVGHMP 266
Cdd:COG1409  106 ---RFIGLDSN-----------------VPGRSSGE--------------LGPEQLAWLEEELAAAPAK--PVIVFLHHP 149

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 937432790 267 PgVDERHLGTQHNQltfteRNNQRYLDMVRRFApvIQGQFFGHLH 311
Cdd:COG1409  150 P-YSTGSGSDRIGL-----RNAEELLALLARYG--VDLVLSGHVH 186
 
Name Accession Description Interval E-value
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 28-351 4.44e-70

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: 225.64  E-value: 4.44e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790  28 FWHISDLHLDTLYSTqGDIYRSCwelaRSVSGSNANSAA---SEPPGPFGHYNCDSPWRLIESAVKTMKaKQGDNVEFVL 104
Cdd:cd00842    1 FLHISDIHYDPLYKV-GSEYANC----RSPLCCRDESGPgdvKPPAGYWGTYGCDSPWSLVESALEAIK-KNHPKPDFIL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790 105 WTGDALSHSAQPLSEQKQHEILRNITELLGRSFSSQFIFPVLG-HE---------DGSGS---YRRLGELWRHWLPSEAL 171
Cdd:cd00842   75 WTGDLVRHDVDEQTPEETVESESNLTNLLKKYFPNVPVYPALGnHDsypvnqfppHSNSPswlYDALAELWKPWLPTEAK 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790 172 VTFDQGGYYSIEqTKSRLRIVALNTNF--------MRLDPDPDpraslslrwpaeyfaepkasvssisaedellaeQQWL 243
Cdd:cd00842  155 ETFKKGGYYSVD-VKDGLRVISLNTNLyykknfwlYSNNTDPC---------------------------------GQLQ 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790 244 WLEEVLTKSKEKQETVYIVGHMPPGVDErhlgtqhnqltFTERNNQRYLDMVRRFAPVIQGQFFGHLHSDTFRLIYDAK- 322
Cdd:cd00842  201 WLEDELEDAEQKGEKVWIIGHIPPGLNS-----------YDADWSERFYQIINRYSDTIAGQFFGHTHRDEFRVFYDDKd 269

                        330       340       350
                 ....*....|....*....|....*....|
gi 937432790 323 -GNPISWLMIAPSIVPRkagigSSNNPALR 351
Cdd:cd00842  270 tGSPINVAYIAPSVTPY-----TGNNPSFR 294
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 324-462 7.55e-25

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: 100.14  E-value: 7.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790  324 NPISWLMIAPSIVPRKAGIG-SSNNPALRLYKFDTGSGQVLDYTQFWLDLPLANRANEPTWQPEYNLTHYYALPEISAVA 402
Cdd:pfam19272   1 NPVNSLFVAPAVTPVKSVLEkESNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPQS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790  403 LHNFAERFTGTDLSWFTRYHRANAVRYHSGSACPGLCMLNHYCAITRLDYDEFRICLEKE 462
Cdd:pfam19272  81 LYGLAKQFAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQICAIMYLDYSSYTDCIKQY 140
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
28-311 3.65e-07

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 51.23  E-value: 3.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790  28 FWHISDLHldtlystqgdiyrscwelarsvsgsnansaaseppgpFGHYNCDSPWRLIESAVKTMKAKQGDnveFVLWTG 107
Cdd:COG1409    3 FAHISDLH-------------------------------------LGAPDGSDTAEVLAAALADINAPRPD---FVVVTG 42

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790 108 DaLSHSAQPlseqKQHEILRNITELLGRSFssqfiFPVLG-HEDGSGSYRRLGELWRHWLPSEALVTFDQGGYysieqtk 186
Cdd:COG1409   43 D-LTDDGEP----EEYAAAREILARLGVPV-----YVVPGnHDIRAAMAEAYREYFGDLPPGGLYYSFDYGGV------- 105

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 937432790 187 srlRIVALNTNfmrldpdpdpraslslrWPAEYFAEpkasvssisaedelLAEQQWLWLEEVLTKSKEKqeTVYIVGHMP 266
Cdd:COG1409  106 ---RFIGLDSN-----------------VPGRSSGE--------------LGPEQLAWLEEELAAAPAK--PVIVFLHHP 149

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 937432790 267 PgVDERHLGTQHNQltfteRNNQRYLDMVRRFApvIQGQFFGHLH 311
Cdd:COG1409  150 P-YSTGSGSDRIGL-----RNAEELLALLARYG--VDLVLSGHVH 186
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 237-312 4.82e-03

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: 38.85  E-value: 4.82e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 937432790 237 LAEQQWLWLEEVLTKSKEKQETVYIVGHMPpgVDERHLGTQHNQLtfterNNQRYLDMVRRFaPVIQGQFFGHLHS 312
Cdd:cd07396  137 IGEEQLAWLRNELTSADANGEKVIVLSHLP--IYPEAADPQCLLW-----NYEEVLAILESY-PCVKACFSGHNHE 204
 
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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