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Conserved domains on  [gi|114602919|ref|XP_527083|]
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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 3.32e-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: 288.70  E-value: 3.32e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114602919  32 SSFSWDNCDEGKDPAVIRSLTLEPDPIIVPGNVTLSVVGSTSVPLSSPLKVDLVLEKEVAGLWIKIPCTDYIGSCTFEHF 111
Cdd:cd00258    1 NGFSWSNCDGESLPAVIKSLTVNPDPINIPGDLTVSTVGSTSVPLSSPLKVILTLEKEVAGLWMKIPCLDNIGSCTYDNA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114602919 112 CDVLDMLIPTGEPCPEPLRTYGLPCHCPFKEGTYSLPKSEFVVPDLELPSWLTTGNYRIESVLSSGGKRLGCIKIAASLK 191
Cdd:cd00258   81 CDLLDTLIPPGQQCPEPLRTYGLPCHCPFKEGVYSLPDSTFTLPNVDLPSWLTNGNYRITGILMADGKELGCGKFTFSLE 160

                 ..
gi 114602919 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 3.32e-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: 288.70  E-value: 3.32e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114602919  32 SSFSWDNCDEGKDPAVIRSLTLEPDPIIVPGNVTLSVVGSTSVPLSSPLKVDLVLEKEVAGLWIKIPCTDYIGSCTFEHF 111
Cdd:cd00258    1 NGFSWSNCDGESLPAVIKSLTVNPDPINIPGDLTVSTVGSTSVPLSSPLKVILTLEKEVAGLWMKIPCLDNIGSCTYDNA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114602919 112 CDVLDMLIPTGEPCPEPLRTYGLPCHCPFKEGTYSLPKSEFVVPDLELPSWLTTGNYRIESVLSSGGKRLGCIKIAASLK 191
Cdd:cd00258   81 CDLLDTLIPPGQQCPEPLRTYGLPCHCPFKEGVYSLPDSTFTLPNVDLPSWLTNGNYRITGILMADGKELGCGKFTFSLE 160

                 ..
gi 114602919 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 3.33e-20

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: 396688  Cd Length: 130  Bit Score: 81.61  E-value: 3.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114602919   33 SFSWDNCDEGKDPAVIRSLTLE--PDPIIVPGNVTLSVVGsTSVPLSSPLKVDlvLEKEVAGlwIKIPCTdyigSCTFEH 110
Cdd:pfam02221   1 GVPFRDCGGKDDIPTPTSVDISgpPCPLVRGQNLTISADF-TSDEISQGLKVV--VEVRLGG--ITLPFP----LPETLD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114602919  111 FCDVLdmliptgepcpeplrtyGLPCHCPFKEGTYSlpkseFVVPDLELPSWLTTGNYRIE-SVLSSGGKRLGCIKIAAS 189
Cdd:pfam02221  72 ACEWL-----------------GLGLSCPIKAGEYV-----TYTLTLPVPSEYPPGKYTVEaELYDDDGKVLTCFKFDAS 129

                  .
gi 114602919  190 L 190
Cdd:pfam02221 130 I 130
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
36-188 6.58e-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: 65.08  E-value: 6.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114602919    36 WDNCDEGkDPAVIRSLTLEPDPIIVPGNVTLSVVGSTSVPLSSpLKVDLVLEKEvaGLWIKIPCTDYigsctfeHFCDVL 115
Cdd:smart00737   1 FKDCGSN-DPGQISSVSISPCPPVRGKTLTISISFTLNEDISK-LKVVVHVKIG--GIEVPIPGETY-------DLCKLT 69
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114602919   116 DMliptgepcpeplrtyglpcHCPFKEGTYSLPKSEFVVpdlelPSWLTTGNYRIESVL-SSGGKRLGCIKIAA 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 3.32e-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: 288.70  E-value: 3.32e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114602919  32 SSFSWDNCDEGKDPAVIRSLTLEPDPIIVPGNVTLSVVGSTSVPLSSPLKVDLVLEKEVAGLWIKIPCTDYIGSCTFEHF 111
Cdd:cd00258    1 NGFSWSNCDGESLPAVIKSLTVNPDPINIPGDLTVSTVGSTSVPLSSPLKVILTLEKEVAGLWMKIPCLDNIGSCTYDNA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114602919 112 CDVLDMLIPTGEPCPEPLRTYGLPCHCPFKEGTYSLPKSEFVVPDLELPSWLTTGNYRIESVLSSGGKRLGCIKIAASLK 191
Cdd:cd00258   81 CDLLDTLIPPGQQCPEPLRTYGLPCHCPFKEGVYSLPDSTFTLPNVDLPSWLTNGNYRITGILMADGKELGCGKFTFSLE 160

                 ..
gi 114602919 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 1.50e-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: 97.97  E-value: 1.50e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114602919  36 WDNCDEGkdPAVIRSLTLEPD-----PIIVPGNVTLSVVGSTSVPLSSPlKVDLVLEKEvaglWIKIPCTDyigscTFEH 110
Cdd:cd00912    1 LVDCSDN--SANIKEVLLSPCdplpcPDHRGGNYNLSVTGTLREDIKSL-YVDLALMSQ----GIKVLNPD-----NSYD 68
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 114602919 111 FCDVLDmliptgepcpeplrtyGLPCHCPFKEG-TYSLPKSEFVVPdlelPSWLTTGNYRIESVLSSGGKRLGCIKIAA 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 3.33e-20

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: 396688  Cd Length: 130  Bit Score: 81.61  E-value: 3.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114602919   33 SFSWDNCDEGKDPAVIRSLTLE--PDPIIVPGNVTLSVVGsTSVPLSSPLKVDlvLEKEVAGlwIKIPCTdyigSCTFEH 110
Cdd:pfam02221   1 GVPFRDCGGKDDIPTPTSVDISgpPCPLVRGQNLTISADF-TSDEISQGLKVV--VEVRLGG--ITLPFP----LPETLD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114602919  111 FCDVLdmliptgepcpeplrtyGLPCHCPFKEGTYSlpkseFVVPDLELPSWLTTGNYRIE-SVLSSGGKRLGCIKIAAS 189
Cdd:pfam02221  72 ACEWL-----------------GLGLSCPIKAGEYV-----TYTLTLPVPSEYPPGKYTVEaELYDDDGKVLTCFKFDAS 129

                  .
gi 114602919  190 L 190
Cdd:pfam02221 130 I 130
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
36-188 6.58e-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: 65.08  E-value: 6.58e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 114602919    36 WDNCDEGkDPAVIRSLTLEPDPIIVPGNVTLSVVGSTSVPLSSpLKVDLVLEKEvaGLWIKIPCTDYigsctfeHFCDVL 115
Cdd:smart00737   1 FKDCGSN-DPGQISSVSISPCPPVRGKTLTISISFTLNEDISK-LKVVVHVKIG--GIEVPIPGETY-------DLCKLT 69
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 114602919   116 DMliptgepcpeplrtyglpcHCPFKEGTYSLPKSEFVVpdlelPSWLTTGNYRIESVL-SSGGKRLGCIKIAA 188
Cdd:smart00737  70 GS-------------------KCPIEKGETVNYTNSLTV-----PGIFPPGKYTVKWELtDEDGEELACINFTV 119
DUF1091 pfam06477
Protein of unknown function (DUF1091); This is a family of uncharacterized proteins. Based on ...
134-170 6.16e-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: 399471  Cd Length: 83  Bit Score: 37.29  E-value: 6.16e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 114602919  134 LPCHCPFKEGTYSLPKseFVVPDLELPSWLTTGNYRI 170
Cdd:pfam06477  49 LNHTCPYPKGNYYVRN--FRLDEKLLPSFLPEGDYKL 83
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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