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Conserved domains on  [gi|42573457|ref|NP_974825|]
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MD-2-related lipid recognition domain-containing protein [Arabidopsis thaliana]

Protein Classification

ML domain-containing protein( domain architecture ID 5313)

ML (MD-2-related lipid-recognition) domain-containing protein; the ML 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; it is predicted to mediate diverse biological functions through interaction with specific lipids

Gene Ontology:  GO:0008289
PubMed:  12076526

Graphical summary

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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, ...
 28-120 1.93e-23

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 cd00917:

Pssm-ID: 469700  Cd Length: 122  Bit Score: 88.15  E-value: 1.93e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573457  28 FEYCTKNGHDYGSISQIWVSPsDGPQENPTITIHLFGSASKDISAGTLVYVTYRSGDFTGLLKTYDLCDVS-ACNPEYVI 106
Cdd:cd00917   1 FEYCDKGGEDIVKVTSVEISP-NPPAAGQNLTIEASGSVGKEIEDGAYVVVEVKYGFIRLLSETYDLCDETkNVDLSCPI 79

                        90
                ....*....|....
gi 42573457 107 EAGTDFELTLSDVL 120
Cdd:cd00917  80 EPGDKFLTKLVDLP 93
 
Name Accession Description Interval E-value
PG-PI_TP cd00917
The phosphatidylinositol/phosphatidylglycerol transfer protein (PG/PI-TP) has been shown to ...
 28-120 1.93e-23

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: 88.15  E-value: 1.93e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573457  28 FEYCTKNGHDYGSISQIWVSPsDGPQENPTITIHLFGSASKDISAGTLVYVTYRSGDFTGLLKTYDLCDVS-ACNPEYVI 106
Cdd:cd00917   1 FEYCDKGGEDIVKVTSVEISP-NPPAAGQNLTIEASGSVGKEIEDGAYVVVEVKYGFIRLLSETYDLCDETkNVDLSCPI 79

                        90
                ....*....|....
gi 42573457 107 EAGTDFELTLSDVL 120
Cdd:cd00917  80 EPGDKFLTKLVDLP 93
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
 28-127 6.78e-15

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: 66.24  E-value: 6.78e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573457     28 FEYCTKNghDYGSISQIWVSPsDGPQENPTITIHLFGSASKDISAGTlVYVTYRSGD--FTGLLKTYDLCDVSA--CNpe 103
Cdd:smart00737   1 FKDCGSN--DPGQISSVSISP-CPPVRGKTLTISISFTLNEDISKLK-VVVHVKIGGieVPIPGETYDLCKLTGskCP-- 74

                           90       100
                   ....*....|....*....|....
gi 42573457    104 yvIEAGTDFELTLSDVLYVGFDEV 127
Cdd:smart00737  75 --IEKGETVNYTNSLTVPGIFPPG 96
E1_DerP2_DerF2 pfam02221
ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins ...
 25-117 3.81e-12

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: 59.31  E-value: 3.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573457    25 AIDFEYCTKNGHDYGSISQIWVSPSDGPQENPTITIHLFGSASKDISAGTLVYVTYRSGDFTGLLK---TYDLCDV---- 97
Cdd:pfam02221   1 SVPFRDCGRNKDDAPTPKSVDISPPCPLVRGQNLTISASGTTSDEISQGLKVDVEVRLGGITLPFPlpeTRDLCDElevg 80

                          90       100
                  ....*....|....*....|..
gi 42573457    98 --SACNpeyvIEAGTDFELTLS 117
Cdd:pfam02221  81 sgLSCP----IKAGEYVTYTLT 98
 
Name Accession Description Interval E-value
PG-PI_TP cd00917
The phosphatidylinositol/phosphatidylglycerol transfer protein (PG/PI-TP) has been shown to ...
 28-120 1.93e-23

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: 88.15  E-value: 1.93e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573457  28 FEYCTKNGHDYGSISQIWVSPsDGPQENPTITIHLFGSASKDISAGTLVYVTYRSGDFTGLLKTYDLCDVS-ACNPEYVI 106
Cdd:cd00917   1 FEYCDKGGEDIVKVTSVEISP-NPPAAGQNLTIEASGSVGKEIEDGAYVVVEVKYGFIRLLSETYDLCDETkNVDLSCPI 79

                        90
                ....*....|....
gi 42573457 107 EAGTDFELTLSDVL 120
Cdd:cd00917  80 EPGDKFLTKLVDLP 93
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
 28-127 6.78e-15

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: 66.24  E-value: 6.78e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573457     28 FEYCTKNghDYGSISQIWVSPsDGPQENPTITIHLFGSASKDISAGTlVYVTYRSGD--FTGLLKTYDLCDVSA--CNpe 103
Cdd:smart00737   1 FKDCGSN--DPGQISSVSISP-CPPVRGKTLTISISFTLNEDISKLK-VVVHVKIGGieVPIPGETYDLCKLTGskCP-- 74

                           90       100
                   ....*....|....*....|....
gi 42573457    104 yvIEAGTDFELTLSDVLYVGFDEV 127
Cdd:smart00737  75 --IEKGETVNYTNSLTVPGIFPPG 96
E1_DerP2_DerF2 pfam02221
ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins ...
 25-117 3.81e-12

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: 59.31  E-value: 3.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42573457    25 AIDFEYCTKNGHDYGSISQIWVSPSDGPQENPTITIHLFGSASKDISAGTLVYVTYRSGDFTGLLK---TYDLCDV---- 97
Cdd:pfam02221   1 SVPFRDCGRNKDDAPTPKSVDISPPCPLVRGQNLTISASGTTSDEISQGLKVDVEVRLGGITLPFPlpeTRDLCDElevg 80

                          90       100
                  ....*....|....*....|..
gi 42573457    98 --SACNpeyvIEAGTDFELTLS 117
Cdd:pfam02221  81 sgLSCP----IKAGEYVTYTLT 98
 
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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