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Conserved domains on  [gi|109079384|ref|XP_001109570|]
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Protein Classification

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List of domain hits

Name Accession Description Interval E-value
ML super family cl00274
The ML (MD-2-related lipid-recognition) domain is present in MD-1, MD-2, GM2 activator protein, ...
30-189 5.05e-100

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.


The actual alignment was detected with superfamily member cd00258:

Pssm-ID: 412276  Cd Length: 162  Bit Score: 285.62  E-value: 5.05e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109079384  30 SFSWDNCDEGKDPAVIRSLTLEPDPILIPGNVTVGVVGSTSVPLSSPLKVELVLEKEVAGLWIKIPCTDYIGSCTFEDFC 109
Cdd:cd00258    2 GFSWSNCDGESLPAVIKSLTVNPDPINIPGDLTVSTVGSTSVPLSSPLKVILTLEKEVAGLWMKIPCLDNIGSCTYDNAC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109079384 110 DVLDMLIPTGEPCPEPLRTYGLPCHCPFKEGTYSLPKSEFVVPHLELPSWLTTGNYRIESILSNRGKRLGCIKIAASLKG 189
Cdd:cd00258   82 DLLDTLIPPGQQCPEPLRTYGLPCHCPFKEGVYSLPDSTFTLPNVDLPSWLTNGNYRITGILMADGKELGCGKFTFSLES 161
 
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 ...
30-189 5.05e-100

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: 285.62  E-value: 5.05e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109079384  30 SFSWDNCDEGKDPAVIRSLTLEPDPILIPGNVTVGVVGSTSVPLSSPLKVELVLEKEVAGLWIKIPCTDYIGSCTFEDFC 109
Cdd:cd00258    2 GFSWSNCDGESLPAVIKSLTVNPDPINIPGDLTVSTVGSTSVPLSSPLKVILTLEKEVAGLWMKIPCLDNIGSCTYDNAC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109079384 110 DVLDMLIPTGEPCPEPLRTYGLPCHCPFKEGTYSLPKSEFVVPHLELPSWLTTGNYRIESILSNRGKRLGCIKIAASLKG 189
Cdd:cd00258   82 DLLDTLIPPGQQCPEPLRTYGLPCHCPFKEGVYSLPDSTFTLPNVDLPSWLTNGNYRITGILMADGKELGCGKFTFSLES 161
E1_DerP2_DerF2 pfam02221
ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins ...
30-187 8.45e-21

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: 83.15  E-value: 8.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109079384   30 SFSWDNCDEGKDPAVIRSLTLE--PDPILIPGNVTVGVVGsTSVPLSSPLKVelVLEKEVAGlwIKIPCTdyigSCTFED 107
Cdd:pfam02221   1 GVPFRDCGGKDDIPTPTSVDISgpPCPLVRGQNLTISADF-TSDEISQGLKV--VVEVRLGG--ITLPFP----LPETLD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109079384  108 FCDVLdmliptgepcpeplrtyGLPCHCPFKEGTYSlpkseFVVPHLELPSWLTTGNYRIE-SILSNRGKRLGCIKIAAS 186
Cdd:pfam02221  72 ACEWL-----------------GLGLSCPIKAGEYV-----TYTLTLPVPSEYPPGKYTVEaELYDDDGKVLTCFKFDAS 129

                  .
gi 109079384  187 L 187
Cdd:pfam02221 130 I 130
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
33-185 2.57e-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: 65.85  E-value: 2.57e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109079384    33 WDNCDEGkDPAVIRSLTLEPDPILIPGNVTVGVVGSTSVPLSSpLKVELVLEKEvaGLWIKIPCTDYigsctfeDFCDVL 112
Cdd:smart00737   1 FKDCGSN-DPGQISSVSISPCPPVRGKTLTISISFTLNEDISK-LKVVVHVKIG--GIEVPIPGETY-------DLCKLT 69
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109079384   113 DMliptgepcpeplrtyglpcHCPFKEGTYSLPKSEFVVphlelPSWLTTGNYRIE-SILSNRGKRLGCIKIAA 185
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 ...
30-189 5.05e-100

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: 285.62  E-value: 5.05e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109079384  30 SFSWDNCDEGKDPAVIRSLTLEPDPILIPGNVTVGVVGSTSVPLSSPLKVELVLEKEVAGLWIKIPCTDYIGSCTFEDFC 109
Cdd:cd00258    2 GFSWSNCDGESLPAVIKSLTVNPDPINIPGDLTVSTVGSTSVPLSSPLKVILTLEKEVAGLWMKIPCLDNIGSCTYDNAC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109079384 110 DVLDMLIPTGEPCPEPLRTYGLPCHCPFKEGTYSLPKSEFVVPHLELPSWLTTGNYRIESILSNRGKRLGCIKIAASLKG 189
Cdd:cd00258   82 DLLDTLIPPGQQCPEPLRTYGLPCHCPFKEGVYSLPDSTFTLPNVDLPSWLTNGNYRITGILMADGKELGCGKFTFSLES 161
ML cd00912
The ML (MD-2-related lipid-recognition) domain is present in MD-1, MD-2, GM2 activator protein, ...
33-185 2.51e-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: 97.20  E-value: 2.51e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109079384  33 WDNCDEGkdPAVIRSLTLEPD-----PILIPGNVTVGVVGSTSVPLSSPlKVELVLEKEvaglWIKIPCTDyigscTFED 107
Cdd:cd00912    1 LVDCSDN--SANIKEVLLSPCdplpcPDHRGGNYNLSVTGTLREDIKSL-YVDLALMSQ----GIKVLNPD-----NSYD 68
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 109079384 108 FCDVLDmliptgepcpeplrtyGLPCHCPFKEG-TYSLPKSEFVVPhlelPSWLTTGNYRIESILSNRGKRLGCIKIAA 185
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 ...
30-187 8.45e-21

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: 83.15  E-value: 8.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109079384   30 SFSWDNCDEGKDPAVIRSLTLE--PDPILIPGNVTVGVVGsTSVPLSSPLKVelVLEKEVAGlwIKIPCTdyigSCTFED 107
Cdd:pfam02221   1 GVPFRDCGGKDDIPTPTSVDISgpPCPLVRGQNLTISADF-TSDEISQGLKV--VVEVRLGG--ITLPFP----LPETLD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109079384  108 FCDVLdmliptgepcpeplrtyGLPCHCPFKEGTYSlpkseFVVPHLELPSWLTTGNYRIE-SILSNRGKRLGCIKIAAS 186
Cdd:pfam02221  72 ACEWL-----------------GLGLSCPIKAGEYV-----TYTLTLPVPSEYPPGKYTVEaELYDDDGKVLTCFKFDAS 129

                  .
gi 109079384  187 L 187
Cdd:pfam02221 130 I 130
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
33-185 2.57e-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: 65.85  E-value: 2.57e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109079384    33 WDNCDEGkDPAVIRSLTLEPDPILIPGNVTVGVVGSTSVPLSSpLKVELVLEKEvaGLWIKIPCTDYigsctfeDFCDVL 112
Cdd:smart00737   1 FKDCGSN-DPGQISSVSISPCPPVRGKTLTISISFTLNEDISK-LKVVVHVKIG--GIEVPIPGETY-------DLCKLT 69
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 109079384   113 DMliptgepcpeplrtyglpcHCPFKEGTYSLPKSEFVVphlelPSWLTTGNYRIE-SILSNRGKRLGCIKIAA 185
Cdd:smart00737  70 GS-------------------KCPIEKGETVNYTNSLTV-----PGIFPPGKYTVKwELTDEDGEELACINFTV 119
DUF1091 pfam06477
Protein of unknown function (DUF1091); This is a family of uncharacterized proteins. Based on ...
107-167 1.66e-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: 38.83  E-value: 1.66e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109079384  107 DFCDVL--------DMLIPTgepcpepLRTYG-LPCHCPFKEGTYSLPKseFVVPHLELPSWLTTGNYRI 167
Cdd:pfam06477  23 DFCKFLknpnnplfKIFYKS-------LKKFSnLNHTCPYPKGNYYVRN--FRLDEKLLPSFLPEGDYKL 83
PG-PI_TP cd00917
The phosphatidylinositol/phosphatidylglycerol transfer protein (PG/PI-TP) has been shown to ...
33-182 5.95e-03

The phosphatidylinositol/phosphatidylglycerol transfer protein (PG/PI-TP) has been shown to bind phosphatidylglycerol and phosphatidylinositol, but the biological significance of this is still obscure. These proteins belong to the ML domain family.


Pssm-ID: 238459  Cd Length: 122  Bit Score: 35.38  E-value: 5.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 109079384  33 WDNCDEG-KDPAVIRSLTLEPDPILIPGNVTVGVVGSTSVPLSSPLKVELvlekEVAGLWIKIPCTDYigsctfeDFCDV 111
Cdd:cd00917    1 FEYCDKGgEDIVKVTSVEISPNPPAAGQNLTIEASGSVGKEIEDGAYVVV----EVKYGFIRLLSETY-------DLCDE 69
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 109079384 112 ldmliptgepcpeplrTYGLPCHCPFKEGTYSLPKSefvvphLELPSWLTTGNYRIE-SILSNRGKRLGCIK 182
Cdd:cd00917   70 ----------------TKNVDLSCPIEPGDKFLTKL------VDLPGEIPPGKYTVSaRAYTKDDEEITCLS 119
 
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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