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Conserved domains on  [gi|554790358|ref|NP_001273067|]
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cyclic GMP-AMP phosphodiesterase SMPDL3A isoform b [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 177-319 3.69e-99

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: 288.11  E-value: 3.69e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790358  177 SPVNSLFVAPAVTPVKSVLEKQTNNPGIRLFQYDPRDYKLLDMLQYYLNLTEANLKGESIWKLEYILTQTYDIEDLQPES 256
Cdd:pfam19272   1 NPVNSLFVAPAVTPVKSVLEKESNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPQS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 554790358  257 LYGLAKQFTILDSKQFIKYYNYFFVSYDSSVTCDKTCKAFQICAIMNLDNISYADCLKQLYIK 319
Cdd:pfam19272  81 LYGLAKQFAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQICAIMYLDYSSYTDCIKQYAMK 143
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 1-205 1.49e-77

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: 238.74  E-value: 1.49e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790358   1 MTTTIQSLFPNLQVFPALGNHDYWPQDQLPVVT---SKVYNAVANLWKPWLDEEAISTLRKGGFYSQKVttNPNLRIISL 77
Cdd:cd00842   99 LTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHSnspSWLYDALAELWKPWLPTEAKETFKKGGYYSVDV--KDGLRVISL 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790358  78 NTNLYYGPNIMTL-NKTDPANQFEWLESTLNNSQQNKEKVYIIAHVPVGYLPSSQNitamreyYNEKLIDIFQKYSDVIA 156
Cdd:cd00842  177 NTNLYYKKNFWLYsNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDAD-------WSERFYQIINRYSDTIA 249

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 554790358 157 GQFYGHTHRDSIMVLSDKK--GSPVNSLFVAPAVTPVksvlekQTNNPGIR 205
Cdd:cd00842  250 GQFFGHTHRDEFRVFYDDKdtGSPINVAYIAPSVTPY------TGNNPSFR 294
 
Name Accession Description Interval E-value
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 177-319 3.69e-99

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: 288.11  E-value: 3.69e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790358  177 SPVNSLFVAPAVTPVKSVLEKQTNNPGIRLFQYDPRDYKLLDMLQYYLNLTEANLKGESIWKLEYILTQTYDIEDLQPES 256
Cdd:pfam19272   1 NPVNSLFVAPAVTPVKSVLEKESNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPQS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 554790358  257 LYGLAKQFTILDSKQFIKYYNYFFVSYDSSVTCDKTCKAFQICAIMNLDNISYADCLKQLYIK 319
Cdd:pfam19272  81 LYGLAKQFAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQICAIMYLDYSSYTDCIKQYAMK 143
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 1-205 1.49e-77

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: 238.74  E-value: 1.49e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790358   1 MTTTIQSLFPNLQVFPALGNHDYWPQDQLPVVT---SKVYNAVANLWKPWLDEEAISTLRKGGFYSQKVttNPNLRIISL 77
Cdd:cd00842   99 LTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHSnspSWLYDALAELWKPWLPTEAKETFKKGGYYSVDV--KDGLRVISL 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790358  78 NTNLYYGPNIMTL-NKTDPANQFEWLESTLNNSQQNKEKVYIIAHVPVGYLPSSQNitamreyYNEKLIDIFQKYSDVIA 156
Cdd:cd00842  177 NTNLYYKKNFWLYsNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDAD-------WSERFYQIINRYSDTIA 249

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 554790358 157 GQFYGHTHRDSIMVLSDKK--GSPVNSLFVAPAVTPVksvlekQTNNPGIR 205
Cdd:cd00842  250 GQFFGHTHRDEFRVFYDDKdtGSPINVAYIAPSVTPY------TGNNPSFR 294
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
11-211 5.15e-08

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 52.77  E-value: 5.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790358  11 NLQVFPALGNHDYWpqdqlpvvtskvyNAVANLWkpwldEEAISTLRKGGFYSqkVTTNPNLRIISLNTNLYYGPNimtl 90
Cdd:COG1409   64 GVPVYVVPGNHDIR-------------AAMAEAY-----REYFGDLPPGGLYY--SFDYGGVRFIGLDSNVPGRSS---- 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790358  91 NKTDPAnQFEWLESTLnnSQQNKEKVYIIAHVPVgyLPSSQNITAMREYYNEKLIDIFQKYS-DVIagqFYGHTHRDSIm 169
Cdd:COG1409  120 GELGPE-QLAWLEEEL--AAAPAKPVIVFLHHPP--YSTGSGSDRIGLRNAEELLALLARYGvDLV---LSGHVHRYER- 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 554790358 170 vlSDKKGSPVnslFVAPAVTPvksvleKQTNNPGIRLFQYDP 211
Cdd:COG1409  191 --TRRDGVPY---IVAGSTGG------QVRLPPGYRVIEVDG 221
 
Name Accession Description Interval E-value
ASMase_C pfam19272
Acid sphingomyelin phosphodiesterase C-terminal region; This entry corresponds to the ...
 177-319 3.69e-99

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: 288.11  E-value: 3.69e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790358  177 SPVNSLFVAPAVTPVKSVLEKQTNNPGIRLFQYDPRDYKLLDMLQYYLNLTEANLKGESIWKLEYILTQTYDIEDLQPES 256
Cdd:pfam19272   1 NPVNSLFVAPAVTPVKSVLEKESNNPGVRLYQYDPKDYKLLDMLQYYLNLTEANLKGESNWKLEYILTKAYGIEDLQPQS 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 554790358  257 LYGLAKQFTILDSKQFIKYYNYFFVSYDSSVTCDKTCKAFQICAIMNLDNISYADCLKQLYIK 319
Cdd:pfam19272  81 LYGLAKQFAVPHSKQFEKYYNYFFVSYDSSIVCEGGCKALQICAIMYLDYSSYTDCIKQYAMK 143
MPP_ASMase cd00842
acid sphingomyelinase and related proteins, metallophosphatase domain; Acid sphingomyelinase ...
 1-205 1.49e-77

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: 238.74  E-value: 1.49e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790358   1 MTTTIQSLFPNLQVFPALGNHDYWPQDQLPVVT---SKVYNAVANLWKPWLDEEAISTLRKGGFYSQKVttNPNLRIISL 77
Cdd:cd00842   99 LTNLLKKYFPNVPVYPALGNHDSYPVNQFPPHSnspSWLYDALAELWKPWLPTEAKETFKKGGYYSVDV--KDGLRVISL 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790358  78 NTNLYYGPNIMTL-NKTDPANQFEWLESTLNNSQQNKEKVYIIAHVPVGYLPSSQNitamreyYNEKLIDIFQKYSDVIA 156
Cdd:cd00842  177 NTNLYYKKNFWLYsNNTDPCGQLQWLEDELEDAEQKGEKVWIIGHIPPGLNSYDAD-------WSERFYQIINRYSDTIA 249

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 554790358 157 GQFYGHTHRDSIMVLSDKK--GSPVNSLFVAPAVTPVksvlekQTNNPGIR 205
Cdd:cd00842  250 GQFFGHTHRDEFRVFYDDKdtGSPINVAYIAPSVTPY------TGNNPSFR 294
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
11-211 5.15e-08

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


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 52.77  E-value: 5.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790358  11 NLQVFPALGNHDYWpqdqlpvvtskvyNAVANLWkpwldEEAISTLRKGGFYSqkVTTNPNLRIISLNTNLYYGPNimtl 90
Cdd:COG1409   64 GVPVYVVPGNHDIR-------------AAMAEAY-----REYFGDLPPGGLYY--SFDYGGVRFIGLDSNVPGRSS---- 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790358  91 NKTDPAnQFEWLESTLnnSQQNKEKVYIIAHVPVgyLPSSQNITAMREYYNEKLIDIFQKYS-DVIagqFYGHTHRDSIm 169
Cdd:COG1409  120 GELGPE-QLAWLEEEL--AAAPAKPVIVFLHHPP--YSTGSGSDRIGLRNAEELLALLARYGvDLV---LSGHVHRYER- 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 554790358 170 vlSDKKGSPVnslFVAPAVTPvksvleKQTNNPGIRLFQYDP 211
Cdd:COG1409  191 --TRRDGVPY---IVAGSTGG------QVRLPPGYRVIEVDG 221
MPP_Nbla03831 cd07396
Homo sapiens Nbla03831 and related proteins, metallophosphatase domain; Nbla03831 (also known ...
 11-165 2.88e-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: 50.79  E-value: 2.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790358  11 NLQVFPALGNHDYwpqdqlpvvtskvynavANLWKPWLDEEAISTLRKGGFYSQKvtTNPNLRIISLNTNLYYGpnimTL 90
Cdd:cd07396   81 KGPVHHVLGNHEF-----------------YNFPREYLNHLKTLNGEDAYYYSFS--PGPGFRFLVLDFVKFNG----GI 137

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 554790358  91 NKTdpanQFEWLESTLNNSQQNKEKVYIIAHVPVgYLPSSQNITAMREYynEKLIDIFQKYSDVIAgQFYGHTHR 165
Cdd:cd07396  138 GEE----QLAWLRNELTSADANGEKVIVLSHLPI-YPEAADPQCLLWNY--EEVLAILESYPCVKA-CFSGHNHE 204
MPP_PAPs cd00839
purple acid phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 5-164 6.21e-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: 43.83  E-value: 6.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790358   5 IQSLFPNLQVFPALGNHDYWPQDQlpvvTSKVYNAVANLWKPWLDeeaiSTLRKGGFYSqkvTTNPNLRIISLNTNLYYG 84
Cdd:cd00839   62 IEPLASYVPYMVAPGNHEADYNGS----TSKIKFFMPGRGMPPSP----SGSTENLWYS---FDVGPVHFISLSTETDFL 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 554790358  85 PnimtlnKTDPANQFEWLESTLnnSQQNKEKV-YIIA--HVPVGYlpSSQNITAMREYYN--EKLIDIFQKYS-DVIagq 158
Cdd:cd00839  131 K------GDNISPQYDWLEADL--AKVDRSRTpWIIVmgHRPMYC--SNDDDADCIEGEKmrEALEDLFYKYGvDLV--- 197


                 ....*.
gi 554790358 159 FYGHTH 164
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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