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Conserved domains on  [gi|20138465|sp|O95711|]
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RecName: Full=Lymphocyte antigen 86; Short=Ly-86; AltName: Full=Protein MD-1; Flags: Precursor

Protein Classification

MD-1_MD-2 domain-containing protein (domain architecture ID 10097043)

MD-1_MD-2 domain-containing protein

Graphical summary

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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 1.03e-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: 1.03e-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 1.03e-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: 1.03e-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 3.17e-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: 3.17e-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 1.03e-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: 1.03e-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 6.20e-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: 6.20e-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 3.17e-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: 3.17e-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.3.19
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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