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Conserved domains on  [gi|39995109|ref|NP_000396|]
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ganglioside GM2 activator isoform 1 precursor [Homo sapiens]

Protein Classification

GM2-AP domain-containing protein( domain architecture ID 10083577)

GM2-AP domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GM2-AP cd00258
GM2 activator protein (GM2-AP) is a non-enzymatic lysosomal protein that acts as cofactor in ...
 32-193 2.55e-101

GM2 activator protein (GM2-AP) is a non-enzymatic lysosomal protein that acts as cofactor in the sequential degradation of gangliosides. GM2A is an essential cofactor for beta-hexosaminidase A (Hex A) in the enzymatic hydrolysis of GM2 ganglioside to GM3. Mutation of the gene results in the AB variant of Tay-Sachs disease. GM2-AP and similar proteins belong to the ML domain family.


:

Pssm-ID: 238161  Cd Length: 162  Bit Score: 289.09  E-value: 2.55e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995109  32 SSFSWDNCDEGKDPAVIRSLTLEPDPIIVPGNVTLSVMGSTSVPLSSPLKVDLVLEKEVAGLWIKIPCTDYIGSCTFEHF 111
Cdd:cd00258   1 NGFSWSNCDGESLPAVIKSLTVNPDPINIPGDLTVSTVGSTSVPLSSPLKVILTLEKEVAGLWMKIPCLDNIGSCTYDNA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995109 112 CDVLDMLIPTGEPCPEPLRTYGLPCHCPFKEGTYSLPKSEFVVPDLELPSWLTTGNYRIESVLSSSGKRLGCIKIAASLK 191
Cdd:cd00258  81 CDLLDTLIPPGQQCPEPLRTYGLPCHCPFKEGVYSLPDSTFTLPNVDLPSWLTNGNYRITGILMADGKELGCGKFTFSLE 160


                ..
gi 39995109 192 GI 193
Cdd:cd00258 161 SS 162
 
Name Accession Description Interval E-value
GM2-AP cd00258
GM2 activator protein (GM2-AP) is a non-enzymatic lysosomal protein that acts as cofactor in ...
 32-193 2.55e-101

GM2 activator protein (GM2-AP) is a non-enzymatic lysosomal protein that acts as cofactor in the sequential degradation of gangliosides. GM2A is an essential cofactor for beta-hexosaminidase A (Hex A) in the enzymatic hydrolysis of GM2 ganglioside to GM3. Mutation of the gene results in the AB variant of Tay-Sachs disease. GM2-AP and similar proteins belong to the ML domain family.


Pssm-ID: 238161  Cd Length: 162  Bit Score: 289.09  E-value: 2.55e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995109  32 SSFSWDNCDEGKDPAVIRSLTLEPDPIIVPGNVTLSVMGSTSVPLSSPLKVDLVLEKEVAGLWIKIPCTDYIGSCTFEHF 111
Cdd:cd00258   1 NGFSWSNCDGESLPAVIKSLTVNPDPINIPGDLTVSTVGSTSVPLSSPLKVILTLEKEVAGLWMKIPCLDNIGSCTYDNA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995109 112 CDVLDMLIPTGEPCPEPLRTYGLPCHCPFKEGTYSLPKSEFVVPDLELPSWLTTGNYRIESVLSSSGKRLGCIKIAASLK 191
Cdd:cd00258  81 CDLLDTLIPPGQQCPEPLRTYGLPCHCPFKEGVYSLPDSTFTLPNVDLPSWLTNGNYRITGILMADGKELGCGKFTFSLE 160


                ..
gi 39995109 192 GI 193
Cdd:cd00258 161 SS 162
E1_DerP2_DerF2 pfam02221
ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins ...
 33-190 2.23e-25

ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins from plants, animals and fungi, including dust mite allergen Der P 2. It has been implicate in lipid recognition, particularly in the recognition of pathogen related products. A mutation in Npc2 causes a rare form of Niemann-Pick type C2 disease. This domain has a similar topology to immunoglobulin domains.


Pssm-ID: 460498  Cd Length: 133  Bit Score: 95.13  E-value: 2.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995109    33 SFSWDNCDEGKDPAV-IRSLTLEPD-PIIVPGNVTLSVMGSTSVPLSSPLKVDLvlekEVAGLWIKIPCTDYigscTFEH 110
Cdd:pfam02221   1 SVPFRDCGRNKDDAPtPKSVDISPPcPLVRGQNLTISASGTTSDEISQGLKVDV----EVRLGGITLPFPLP----ETRD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995109   111 FCDVLDmliptgepcpeplrtYGLPCHCPFKEGTYSlpkseFVVPDLELPSWLTTGNYRIE-SVLSSSGKRLGCIKIAAS 189
Cdd:pfam02221  73 LCDELE---------------VGSGLSCPIKAGEYV-----TYTLTLPLPSEYPPGKYTVEaELYDQDGKPLTCFKIDVS 132


                  .
gi 39995109   190 L 190
Cdd:pfam02221 133 I 133
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
 36-188 4.32e-14

Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) is a novel domain identified in MD-1, MD-2, GM2A, Npc2 and multiple proteins of unknown function in plants, animals and fungi. These single-domain proteins were predicted to form a beta-rich fold containing multiple strands, and to mediate diverse biological functions through interacting with specific lipids.


Pssm-ID: 214796  Cd Length: 119  Bit Score: 65.47  E-value: 4.32e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995109     36 WDNCDEGkDPAVIRSLTLEPDPIIVPGNVTLSVMGSTSVPLSSpLKVDLVLEKEvaGLWIKIPCTDYigsctfeHFCDVL 115
Cdd:smart00737   1 FKDCGSN-DPGQISSVSISPCPPVRGKTLTISISFTLNEDISK-LKVVVHVKIG--GIEVPIPGETY-------DLCKLT 69

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 39995109    116 DMliptgepcpeplrtyglpcHCPFKEGTYSLPKSEFVVpdlelPSWLTTGNYRIESVL-SSSGKRLGCIKIAA 188
Cdd:smart00737  70 GS-------------------KCPIEKGETVNYTNSLTV-----PGIFPPGKYTVKWELtDEDGEELACINFTV 119
 
Name Accession Description Interval E-value
GM2-AP cd00258
GM2 activator protein (GM2-AP) is a non-enzymatic lysosomal protein that acts as cofactor in ...
 32-193 2.55e-101

GM2 activator protein (GM2-AP) is a non-enzymatic lysosomal protein that acts as cofactor in the sequential degradation of gangliosides. GM2A is an essential cofactor for beta-hexosaminidase A (Hex A) in the enzymatic hydrolysis of GM2 ganglioside to GM3. Mutation of the gene results in the AB variant of Tay-Sachs disease. GM2-AP and similar proteins belong to the ML domain family.


Pssm-ID: 238161  Cd Length: 162  Bit Score: 289.09  E-value: 2.55e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995109  32 SSFSWDNCDEGKDPAVIRSLTLEPDPIIVPGNVTLSVMGSTSVPLSSPLKVDLVLEKEVAGLWIKIPCTDYIGSCTFEHF 111
Cdd:cd00258   1 NGFSWSNCDGESLPAVIKSLTVNPDPINIPGDLTVSTVGSTSVPLSSPLKVILTLEKEVAGLWMKIPCLDNIGSCTYDNA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995109 112 CDVLDMLIPTGEPCPEPLRTYGLPCHCPFKEGTYSLPKSEFVVPDLELPSWLTTGNYRIESVLSSSGKRLGCIKIAASLK 191
Cdd:cd00258  81 CDLLDTLIPPGQQCPEPLRTYGLPCHCPFKEGVYSLPDSTFTLPNVDLPSWLTNGNYRITGILMADGKELGCGKFTFSLE 160


                ..
gi 39995109 192 GI 193
Cdd:cd00258 161 SS 162
ML cd00912
The ML (MD-2-related lipid-recognition) domain is present in MD-1, MD-2, GM2 activator protein, ...
 36-188 1.12e-26

The ML (MD-2-related lipid-recognition) domain is present in MD-1, MD-2, GM2 activator protein, Niemann-Pick type C2 (Npc2) protein, phosphatidylinositol/phosphatidylglycerol transfer protein (PG/PI-TP), mite allergen Der p 2 and several proteins of unknown function in plants, animals and fungi. These single-domain proteins form two anti-parallel beta-pleated sheets stabilized by three disulfide bonds and with an accessible central hydrophobic cavity, and are predicted to mediate diverse biological functions through interaction with specific lipids.


Pssm-ID: 238454  Cd Length: 127  Bit Score: 98.36  E-value: 1.12e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995109  36 WDNCDEGkdPAVIRSLTLEPD-----PIIVPGNVTLSVMGSTSVPLSSPlKVDLVLEKEvaglWIKIPCTDyigscTFEH 110
Cdd:cd00912   1 LVDCSDN--SANIKEVLLSPCdplpcPDHRGGNYNLSVTGTLREDIKSL-YVDLALMSQ----GIKVLNPD-----NSYD 68

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39995109 111 FCDVLDmliptgepcpeplrtyGLPCHCPFKEG-TYSLPKSEFVVPdlelPSWLTTGNYRIESVLSSSGKRLGCIKIAA 188
Cdd:cd00912  69 FCEAGL----------------PKPSFCPLRKGqQYSYAKTVNVPE----FTIPTIEYQVVLEDVTDKGEVLACAQATI 127
E1_DerP2_DerF2 pfam02221
ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins ...
 33-190 2.23e-25

ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins from plants, animals and fungi, including dust mite allergen Der P 2. It has been implicate in lipid recognition, particularly in the recognition of pathogen related products. A mutation in Npc2 causes a rare form of Niemann-Pick type C2 disease. This domain has a similar topology to immunoglobulin domains.


Pssm-ID: 460498  Cd Length: 133  Bit Score: 95.13  E-value: 2.23e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995109    33 SFSWDNCDEGKDPAV-IRSLTLEPD-PIIVPGNVTLSVMGSTSVPLSSPLKVDLvlekEVAGLWIKIPCTDYigscTFEH 110
Cdd:pfam02221   1 SVPFRDCGRNKDDAPtPKSVDISPPcPLVRGQNLTISASGTTSDEISQGLKVDV----EVRLGGITLPFPLP----ETRD 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995109   111 FCDVLDmliptgepcpeplrtYGLPCHCPFKEGTYSlpkseFVVPDLELPSWLTTGNYRIE-SVLSSSGKRLGCIKIAAS 189
Cdd:pfam02221  73 LCDELE---------------VGSGLSCPIKAGEYV-----TYTLTLPLPSEYPPGKYTVEaELYDQDGKPLTCFKIDVS 132


                  .
gi 39995109   190 L 190
Cdd:pfam02221 133 I 133
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
 36-188 4.32e-14

Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) is a novel domain identified in MD-1, MD-2, GM2A, Npc2 and multiple proteins of unknown function in plants, animals and fungi. These single-domain proteins were predicted to form a beta-rich fold containing multiple strands, and to mediate diverse biological functions through interacting with specific lipids.


Pssm-ID: 214796  Cd Length: 119  Bit Score: 65.47  E-value: 4.32e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39995109     36 WDNCDEGkDPAVIRSLTLEPDPIIVPGNVTLSVMGSTSVPLSSpLKVDLVLEKEvaGLWIKIPCTDYigsctfeHFCDVL 115
Cdd:smart00737   1 FKDCGSN-DPGQISSVSISPCPPVRGKTLTISISFTLNEDISK-LKVVVHVKIG--GIEVPIPGETY-------DLCKLT 69

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 39995109    116 DMliptgepcpeplrtyglpcHCPFKEGTYSLPKSEFVVpdlelPSWLTTGNYRIESVL-SSSGKRLGCIKIAA 188
Cdd:smart00737  70 GS-------------------KCPIEKGETVNYTNSLTV-----PGIFPPGKYTVKWELtDEDGEELACINFTV 119
DUF1091 pfam06477
Protein of unknown function (DUF1091); This is a family of uncharacterized proteins. Based on ...
 129-170 9.79e-04

Protein of unknown function (DUF1091); This is a family of uncharacterized proteins. Based on its distant similarity to pfam02221 and conserved pattern of cysteine residues it is possible that these domains are also lipid binding.


Pssm-ID: 461928  Cd Length: 83  Bit Score: 36.52  E-value: 9.79e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 39995109   129 LRTYG-LPCHCPFKEGTYSLPKseFVVPDLELPSWLTTGNYRI 170
Cdd:pfam06477  43 LKKFSnLNHTCPYPKGNYYLRN--FVLDEDLLPSFLPEGDYKI 83
 
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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