NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|20138465|sp|O95711|]
View 

RecName: Full=Lymphocyte antigen 86; Short=Ly-86; AltName: Full=Protein MD-1; Flags: Precursor

Protein Classification

ML domain-containing protein( domain architecture ID 10097043)

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 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 ...
 30-159 1.09e-76

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: 224.36  E-value: 1.09e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138465  30 HVVCSDSGLEVLYQSCDPLQDFGFSVEKCSKQLKSNINIRFGIILREDIKELFLDLALMSQGSSVLNFSYPICEAALPKF 109
Cdd:cd00915   1 HWVCNSSDLEFSYSSCDPMQDFSFSAEPCSTLKGTNGFIRIKFILRRDIKELYFNLSLNVNGIEVLTRSEIICHGYLDKY 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 20138465 110 SFCGRRKGEQIYYAGPVNNPEFTIPQGEYQVLLELYTEKRSTVACANATI 159
Cdd:cd00915  81 SFCGALKGETVYYVGPFSFKGILIPQGQYRCVAELIVENRETVACANFTI 130
 
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 ...
 30-159 1.09e-76

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: 224.36  E-value: 1.09e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138465  30 HVVCSDSGLEVLYQSCDPLQDFGFSVEKCSKQLKSNINIRFGIILREDIKELFLDLALMSQGSSVLNFSYPICEAALPKF 109
Cdd:cd00915   1 HWVCNSSDLEFSYSSCDPMQDFSFSAEPCSTLKGTNGFIRIKFILRRDIKELYFNLSLNVNGIEVLTRSEIICHGYLDKY 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 20138465 110 SFCGRRKGEQIYYAGPVNNPEFTIPQGEYQVLLELYTEKRSTVACANATI 159
Cdd:cd00915  81 SFCGALKGETVYYVGPFSFKGILIPQGQYRCVAELIVENRETVACANFTI 130
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
 42-159 3.35e-26

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: 95.90  E-value: 3.35e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138465     42 YQSCD---PLQDFGFSVEKCSKQLKSNINIRFGIILREDIKELFLDLALMSQGSSV--LNFSYPICEAALpkfSFCGRRK 116
Cdd:smart00737   1 FKDCGsndPGQISSVSISPCPPVRGKTLTISISFTLNEDISKLKVVVHVKIGGIEVpiPGETYDLCKLTG---SKCPIEK 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 20138465    117 GEQIYYAGPVNNPEfTIPQGEYQVLLELYTEKRSTVACANATI 159
Cdd:smart00737  78 GETVNYTNSLTVPG-IFPPGKYTVKWELTDEDGEELACINFTV 119
 
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 ...
 30-159 1.09e-76

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: 224.36  E-value: 1.09e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138465  30 HVVCSDSGLEVLYQSCDPLQDFGFSVEKCSKQLKSNINIRFGIILREDIKELFLDLALMSQGSSVLNFSYPICEAALPKF 109
Cdd:cd00915   1 HWVCNSSDLEFSYSSCDPMQDFSFSAEPCSTLKGTNGFIRIKFILRRDIKELYFNLSLNVNGIEVLTRSEIICHGYLDKY 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 20138465 110 SFCGRRKGEQIYYAGPVNNPEFTIPQGEYQVLLELYTEKRSTVACANATI 159
Cdd:cd00915  81 SFCGALKGETVYYVGPFSFKGILIPQGQYRCVAELIVENRETVACANFTI 130
ML cd00912
The ML (MD-2-related lipid-recognition) domain is present in MD-1, MD-2, GM2 activator protein, ...
 30-159 6.55e-42

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: 136.11  E-value: 6.55e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138465  30 HVVCSDSG---LEVLYQSCDPLqdfgfsveKCSKQLKSNINIRFGIILREDIKELFLDLALMSQGSSVLNF--SYPICEA 104
Cdd:cd00912   1 LVDCSDNSaniKEVLLSPCDPL--------PCPDHRGGNYNLSVTGTLREDIKSLYVDLALMSQGIKVLNPdnSYDFCEA 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20138465 105 ALPKFSFCGRRKGEQIYYAGPVNNPEFTIPQGEYQVLLELYTEKRSTVACANATI 159
Cdd:cd00912  73 GLPKPSFCPLRKGQQYSYAKTVNVPEFTIPTIEYQVVLEDVTDKGEVLACAQATI 127
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
 42-159 3.35e-26

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: 95.90  E-value: 3.35e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20138465     42 YQSCD---PLQDFGFSVEKCSKQLKSNINIRFGIILREDIKELFLDLALMSQGSSV--LNFSYPICEAALpkfSFCGRRK 116
Cdd:smart00737   1 FKDCGsndPGQISSVSISPCPPVRGKTLTISISFTLNEDISKLKVVVHVKIGGIEVpiPGETYDLCKLTG---SKCPIEK 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 20138465    117 GEQIYYAGPVNNPEfTIPQGEYQVLLELYTEKRSTVACANATI 159
Cdd:smart00737  78 GETVNYTNSLTVPG-IFPPGKYTVKWELTDEDGEELACINFTV 119
 
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