NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|767951741|ref|XP_011515810|]
View 

lymphocyte antigen 96 isoform X4 [Homo sapiens]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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, ...
 22-130 5.30e-35

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 cd00915:

Pssm-ID: 469700  Cd Length: 130  Bit Score: 117.66  E-value: 5.30e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951741  22 YWVCNSSDASISYTYCDKMQYpISINVNPCIELKRSKGLLHIFYIPRRDLKQLYFNLYITVNTMNLPKRKEVICRGSDDD 101
Cdd:cd00915    1 HWVCNSSDLEFSYSSCDPMQD-FSFSAEPCSTLKGTNGFIRIKFILRRDIKELYFNLSLNVNGIEVLTRSEIICHGYLDK 79

                         90       100
                 ....*....|....*....|....*....
gi 767951741 102 YSFCRALKGETVNTTISFSFKGIKFSKEE 130
Cdd:cd00915   80 YSFCGALKGETVYYVGPFSFKGILIPQGQ 108
 
Name Accession Description Interval E-value
MD-1_MD-2 cd00915
MD-1 and MD-2 are cofactors required for LPS signaling through cell surface receptors. MD-2 ...
 22-130 5.30e-35

MD-1 and MD-2 are cofactors required for LPS signaling through cell surface receptors. MD-2 and its binding partner, Toll-like receptor 4 (TLR4), are essential for the innate immune responses of mammalian cells to bacterial lipopolysaccharide (LPS); MD-2 directly binds the lipid A moiety of LPS. The TLR4-like receptor, RP105, which mediates LPS-induced lymphocyte proliferation, interacts with MD-1; MD-1 enhances RP105-mediated LPS-induced growth of B cells. These proteins belong to the ML domain family.


Pssm-ID: 238457  Cd Length: 130  Bit Score: 117.66  E-value: 5.30e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951741  22 YWVCNSSDASISYTYCDKMQYpISINVNPCIELKRSKGLLHIFYIPRRDLKQLYFNLYITVNTMNLPKRKEVICRGSDDD 101
Cdd:cd00915    1 HWVCNSSDLEFSYSSCDPMQD-FSFSAEPCSTLKGTNGFIRIKFILRRDIKELYFNLSLNVNGIEVLTRSEIICHGYLDK 79

                         90       100
                 ....*....|....*....|....*....
gi 767951741 102 YSFCRALKGETVNTTISFSFKGIKFSKEE 130
Cdd:cd00915   80 YSFCGALKGETVYYVGPFSFKGILIPQGQ 108
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
 34-124 5.47e-16

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: 68.93  E-value: 5.47e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951741    34 YTYCDKMQY--PISINVNPCIELKRSKGLLHIFYIPRRDLKQLYFNLYITVN--TMNLPKRKEVICrgsDDDYSFCRALK 109
Cdd:smart00737   1 FKDCGSNDPgqISSVSISPCPPVRGKTLTISISFTLNEDISKLKVVVHVKIGgiEVPIPGETYDLC---KLTGSKCPIEK 77

                           90
                   ....*....|....*
gi 767951741   110 GETVNTTISFSFKGI 124
Cdd:smart00737  78 GETVNYTNSLTVPGI 92
E1_DerP2_DerF2 pfam02221
ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins ...
 31-124 2.68e-03

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: 35.42  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951741   31 SISYTYCDKMQYPI----SINVNPCIELKRSKGL-LHI-FYIPRRDLKQLYFNLYITVNTMNLPKRKEV---ICRGSDDD 101
Cdd:pfam02221   1 SVPFRDCGRNKDDAptpkSVDISPPCPLVRGQNLtISAsGTTSDEISQGLKVDVEVRLGGITLPFPLPEtrdLCDELEVG 80

                          90       100
                  ....*....|....*....|....
gi 767951741  102 YSF-CRALKGETVNTTISFSFKGI 124
Cdd:pfam02221  81 SGLsCPIKAGEYVTYTLTLPLPSE 104
 
Name Accession Description Interval E-value
MD-1_MD-2 cd00915
MD-1 and MD-2 are cofactors required for LPS signaling through cell surface receptors. MD-2 ...
 22-130 5.30e-35

MD-1 and MD-2 are cofactors required for LPS signaling through cell surface receptors. MD-2 and its binding partner, Toll-like receptor 4 (TLR4), are essential for the innate immune responses of mammalian cells to bacterial lipopolysaccharide (LPS); MD-2 directly binds the lipid A moiety of LPS. The TLR4-like receptor, RP105, which mediates LPS-induced lymphocyte proliferation, interacts with MD-1; MD-1 enhances RP105-mediated LPS-induced growth of B cells. These proteins belong to the ML domain family.


Pssm-ID: 238457  Cd Length: 130  Bit Score: 117.66  E-value: 5.30e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951741  22 YWVCNSSDASISYTYCDKMQYpISINVNPCIELKRSKGLLHIFYIPRRDLKQLYFNLYITVNTMNLPKRKEVICRGSDDD 101
Cdd:cd00915    1 HWVCNSSDLEFSYSSCDPMQD-FSFSAEPCSTLKGTNGFIRIKFILRRDIKELYFNLSLNVNGIEVLTRSEIICHGYLDK 79

                         90       100
                 ....*....|....*....|....*....
gi 767951741 102 YSFCRALKGETVNTTISFSFKGIKFSKEE 130
Cdd:cd00915   80 YSFCGALKGETVYYVGPFSFKGILIPQGQ 108
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
 34-124 5.47e-16

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: 68.93  E-value: 5.47e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951741    34 YTYCDKMQY--PISINVNPCIELKRSKGLLHIFYIPRRDLKQLYFNLYITVN--TMNLPKRKEVICrgsDDDYSFCRALK 109
Cdd:smart00737   1 FKDCGSNDPgqISSVSISPCPPVRGKTLTISISFTLNEDISKLKVVVHVKIGgiEVPIPGETYDLC---KLTGSKCPIEK 77

                           90
                   ....*....|....*
gi 767951741   110 GETVNTTISFSFKGI 124
Cdd:smart00737  78 GETVNYTNSLTVPGI 92
E1_DerP2_DerF2 pfam02221
ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins ...
 31-124 2.68e-03

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: 35.42  E-value: 2.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767951741   31 SISYTYCDKMQYPI----SINVNPCIELKRSKGL-LHI-FYIPRRDLKQLYFNLYITVNTMNLPKRKEV---ICRGSDDD 101
Cdd:pfam02221   1 SVPFRDCGRNKDDAptpkSVDISPPCPLVRGQNLtISAsGTTSDEISQGLKVDVEVRLGGITLPFPLPEtrdLCDELEVG 80

                          90       100
                  ....*....|....*....|....
gi 767951741  102 YSF-CRALKGETVNTTISFSFKGI 124
Cdd:pfam02221  81 SGLsCPIKAGEYVTYTLTLPLPSE 104
 
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