NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568990912|ref|XP_006520290|]
View 

sphingomyelin phosphodiesterase 5 isoform X1 [Mus musculus]

Protein Classification

sphingomyelin phosphodiesterase( domain architecture ID 10173353)

sphingomyelin phosphodiesterase (sphingomyelinase or SMase) catalyzes the hydrolysis of membrane sphingomyelin to phosphorylcholine and ceramide

CATH:  3.60.10.10
EC:  3.1.4.12
Gene Ontology:  GO:0005543|GO:0004767|GO:0005515|GO:0046872
SCOP:  4002213

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
nSMase cd09078
Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological ...
 201-389 5.62e-45

Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological membranes to ceramide and phosphorylcholine; Sphingomyelinases (SMase) are phosphodiesterases that catalyze the hydrolysis of sphingomyelin to ceramide and phosphorylcholine. Eukaryotic SMases have been classified according to their pH optima and are known as acid SMase, alkaline SMase, and neutral SMase (nSMase). Eukaryotic proteins in this family are nSMases, and are activated by a variety of stress-inducing agents such as cytokines or UV radiation. Ceramides and other metabolic derivatives, including sphingosine, are lipid "second messenger" molecules that participate in the regulation of stress-induced cellular responses, including cell death, adhesion, differentiation, and proliferation. Bacterial neutral SMases, which also belong to this domain family, are secreted proteins that act as membrane-damaging virulence factors. They promote colonization of the host tissue. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


:

Pssm-ID: 197312 [Multi-domain]  Cd Length: 280  Bit Score: 159.43  E-value: 5.62e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990912 201 GLDFVCLQEVFDLRAARRLVRVLVPnLGPVIYDVGTFGLMaGPYIKVLGSGLLLASRYPLLRATFRCFPNARREDAMASK 280
Cdd:cd09078   36 QYDVVVLQEVFDARARKRLLNGLKK-EYPYQTDVVGRSPS-GWSSKLVDGGVVILSRYPIVEKDQYIFPNGCGADCLAAK 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990912 281 GLLSVQAQLGIVdghpIVGYLHCTHLHA---PVEDGHIRCKQLTLLLEWVEEFeaeNRQSDEAVafsVLLGDLNFDNCSQ 357
Cdd:cd09078  114 GVLYAKINKGGT----KVYHVFGTHLQAsdgSCLDRAVRQKQLDELRAFIEEK---NIPDNEPV---IIAGDFNVDKRSS 183

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568990912 358 DhaKEQGHKL--FSCFQDPCRLGVC-QEQPWALGT 389
Cdd:cd09078  184 R--DEYDDMLeqLHDYNAPEPITAGeTPLTWDPGT 216
 
Name Accession Description Interval E-value
nSMase cd09078
Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological ...
 201-389 5.62e-45

Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological membranes to ceramide and phosphorylcholine; Sphingomyelinases (SMase) are phosphodiesterases that catalyze the hydrolysis of sphingomyelin to ceramide and phosphorylcholine. Eukaryotic SMases have been classified according to their pH optima and are known as acid SMase, alkaline SMase, and neutral SMase (nSMase). Eukaryotic proteins in this family are nSMases, and are activated by a variety of stress-inducing agents such as cytokines or UV radiation. Ceramides and other metabolic derivatives, including sphingosine, are lipid "second messenger" molecules that participate in the regulation of stress-induced cellular responses, including cell death, adhesion, differentiation, and proliferation. Bacterial neutral SMases, which also belong to this domain family, are secreted proteins that act as membrane-damaging virulence factors. They promote colonization of the host tissue. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197312 [Multi-domain]  Cd Length: 280  Bit Score: 159.43  E-value: 5.62e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990912 201 GLDFVCLQEVFDLRAARRLVRVLVPnLGPVIYDVGTFGLMaGPYIKVLGSGLLLASRYPLLRATFRCFPNARREDAMASK 280
Cdd:cd09078   36 QYDVVVLQEVFDARARKRLLNGLKK-EYPYQTDVVGRSPS-GWSSKLVDGGVVILSRYPIVEKDQYIFPNGCGADCLAAK 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990912 281 GLLSVQAQLGIVdghpIVGYLHCTHLHA---PVEDGHIRCKQLTLLLEWVEEFeaeNRQSDEAVafsVLLGDLNFDNCSQ 357
Cdd:cd09078  114 GVLYAKINKGGT----KVYHVFGTHLQAsdgSCLDRAVRQKQLDELRAFIEEK---NIPDNEPV---IIAGDFNVDKRSS 183

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568990912 358 DhaKEQGHKL--FSCFQDPCRLGVC-QEQPWALGT 389
Cdd:cd09078  184 R--DEYDDMLeqLHDYNAPEPITAGeTPLTWDPGT 216
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
 252-351 3.48e-06

Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function prediction only];


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 47.21  E-value: 3.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990912 252 LLLASRYPLLRATFRCFPNARREdamaSKGLLSVQAQlgiVDGHPIvgYLHCTHLHAPveDGHIRCKQLTLLLEWVEEfe 331
Cdd:COG3568   47 NAILSRYPIVSSGTFDLPDPGGE----PRGALWADVD---VPGKPL--RVVNTHLDLR--SAAARRRQARALAELLAE-- 113

                         90       100
                 ....*....|....*....|
gi 568990912 332 aenRQSDEAVafsVLLGDLN 351
Cdd:COG3568  114 ---LPAGAPV---ILAGDFN 127
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 203-353 9.36e-05

Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 43.37  E-value: 9.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990912  203 DFVCLQEVFDLRAARRLVRVLVPNLGPVIYDVGTFGlmagpyikvLGSGLLLASRYPLLRATFRCFPNarredamasKGL 282
Cdd:pfam03372  32 DVVALQETDDDDASRLLLALLAYGGFLSYGGPGGGG---------GGGGVAILSRYPLSSVILVDLGE---------FGD 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568990912  283 LSVQAQLGIVDGHPIVGYLHCTHLHAPVEDGHIRCKQLTLLLewveeFEAENRQSDEAVafsVLLGDLNFD 353
Cdd:pfam03372  94 PALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLL-----LLALLAPRSEPV---ILAGDFNAD 156
 
Name Accession Description Interval E-value
nSMase cd09078
Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological ...
 201-389 5.62e-45

Neutral sphingomyelinases (nSMase) catalyze the hydrolysis of sphingomyelin in biological membranes to ceramide and phosphorylcholine; Sphingomyelinases (SMase) are phosphodiesterases that catalyze the hydrolysis of sphingomyelin to ceramide and phosphorylcholine. Eukaryotic SMases have been classified according to their pH optima and are known as acid SMase, alkaline SMase, and neutral SMase (nSMase). Eukaryotic proteins in this family are nSMases, and are activated by a variety of stress-inducing agents such as cytokines or UV radiation. Ceramides and other metabolic derivatives, including sphingosine, are lipid "second messenger" molecules that participate in the regulation of stress-induced cellular responses, including cell death, adhesion, differentiation, and proliferation. Bacterial neutral SMases, which also belong to this domain family, are secreted proteins that act as membrane-damaging virulence factors. They promote colonization of the host tissue. This family belongs to the large EEP (exonuclease/endonuclease/phosphatase) superfamily that contains functionally diverse enzymes that share a common catalytic mechanism of cleaving phosphodiester bonds.


Pssm-ID: 197312 [Multi-domain]  Cd Length: 280  Bit Score: 159.43  E-value: 5.62e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990912 201 GLDFVCLQEVFDLRAARRLVRVLVPnLGPVIYDVGTFGLMaGPYIKVLGSGLLLASRYPLLRATFRCFPNARREDAMASK 280
Cdd:cd09078   36 QYDVVVLQEVFDARARKRLLNGLKK-EYPYQTDVVGRSPS-GWSSKLVDGGVVILSRYPIVEKDQYIFPNGCGADCLAAK 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990912 281 GLLSVQAQLGIVdghpIVGYLHCTHLHA---PVEDGHIRCKQLTLLLEWVEEFeaeNRQSDEAVafsVLLGDLNFDNCSQ 357
Cdd:cd09078  114 GVLYAKINKGGT----KVYHVFGTHLQAsdgSCLDRAVRQKQLDELRAFIEEK---NIPDNEPV---IIAGDFNVDKRSS 183

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568990912 358 DhaKEQGHKL--FSCFQDPCRLGVC-QEQPWALGT 389
Cdd:cd09078  184 R--DEYDDMLeqLHDYNAPEPITAGeTPLTWDPGT 216
ElsH COG3568
Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function ...
 252-351 3.48e-06

Metal-dependent hydrolase, endonuclease/exonuclease/phosphatase family [General function prediction only];


Pssm-ID: 442789 [Multi-domain]  Cd Length: 167  Bit Score: 47.21  E-value: 3.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990912 252 LLLASRYPLLRATFRCFPNARREdamaSKGLLSVQAQlgiVDGHPIvgYLHCTHLHAPveDGHIRCKQLTLLLEWVEEfe 331
Cdd:COG3568   47 NAILSRYPIVSSGTFDLPDPGGE----PRGALWADVD---VPGKPL--RVVNTHLDLR--SAAARRRQARALAELLAE-- 113

                         90       100
                 ....*....|....*....|
gi 568990912 332 aenRQSDEAVafsVLLGDLN 351
Cdd:COG3568  114 ---LPAGAPV---ILAGDFN 127
Exo_endo_phos pfam03372
Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium ...
 203-353 9.36e-05

Endonuclease/Exonuclease/phosphatase family; This large family of proteins includes magnesium dependent endonucleases and a large number of phosphatases involved in intracellular signalling. This family includes: AP endonuclease proteins EC:4.2.99.18, DNase I proteins EC:3.1.21.1, Synaptojanin an inositol-1,4,5-trisphosphate phosphatase EC:3.1.3.56, Sphingomyelinase EC:3.1.4.12 and Nocturnin.


Pssm-ID: 460902 [Multi-domain]  Cd Length: 183  Bit Score: 43.37  E-value: 9.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568990912  203 DFVCLQEVFDLRAARRLVRVLVPNLGPVIYDVGTFGlmagpyikvLGSGLLLASRYPLLRATFRCFPNarredamasKGL 282
Cdd:pfam03372  32 DVVALQETDDDDASRLLLALLAYGGFLSYGGPGGGG---------GGGGVAILSRYPLSSVILVDLGE---------FGD 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568990912  283 LSVQAQLGIVDGHPIVGYLHCTHLHAPVEDGHIRCKQLTLLLewveeFEAENRQSDEAVafsVLLGDLNFD 353
Cdd:pfam03372  94 PALRGAIAPFAGVLVVPLVLTLAPHASPRLARDEQRADLLLL-----LLALLAPRSEPV---ILAGDFNAD 156
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH