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Conserved domains on  [gi|66730493|ref|NP_001019450|]
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lymphocyte antigen 96 precursor [Rattus norvegicus]

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, ...
 23-153 5.16e-54

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: 166.97  E-value: 5.16e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730493  23 WICNSSDAIISYSYCDHMKIpISISSEPCIRLKGTNGFVHVEFIPRGNLKNLYFNLFININSIELPKRKEIVCHGYDDDY 102
Cdd:cd00915   2 WVCNSSDLEFSYSSCDPMQD-FSFSAEPCSTLKGTNGFIRIKFILRRDIKELYFNLSLNVNGIEVLTRSEIICHGYLDKY 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 66730493 103 SFCRALKGEAVNTAIPFSFDGILFPKGHHRCVAEAIAGDtEEKLFCLNFTI 153
Cdd:cd00915  81 SFCGALKGETVYYVGPFSFKGILIPQGQYRCVAELIVEN-RETVACANFTI 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 ...
 23-153 5.16e-54

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: 166.97  E-value: 5.16e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730493  23 WICNSSDAIISYSYCDHMKIpISISSEPCIRLKGTNGFVHVEFIPRGNLKNLYFNLFININSIELPKRKEIVCHGYDDDY 102
Cdd:cd00915   2 WVCNSSDLEFSYSSCDPMQD-FSFSAEPCSTLKGTNGFIRIKFILRRDIKELYFNLSLNVNGIEVLTRSEIICHGYLDKY 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 66730493 103 SFCRALKGEAVNTAIPFSFDGILFPKGHHRCVAEAIAGDtEEKLFCLNFTI 153
Cdd:cd00915  81 SFCGALKGETVYYVGPFSFKGILIPQGQYRCVAELIVEN-RETVACANFTI 130
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
 34-153 3.77e-24

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: 90.50  E-value: 3.77e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730493     34 YSYCDHMKI--PISISSEPCIRLKGTNGFVHVEFIPRGNLKNLYFNLFININSIELPKRKEI--VCHGyddDYSFCRALK 109
Cdd:smart00737   1 FKDCGSNDPgqISSVSISPCPPVRGKTLTISISFTLNEDISKLKVVVHVKIGGIEVPIPGETydLCKL---TGSKCPIEK 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 66730493    110 GEAVNTAIPFSFDGIlFPKGHHRCVAEAIAGDtEEKLFCLNFTI 153
Cdd:smart00737  78 GETVNYTNSLTVPGI-FPPGKYTVKWELTDED-GEELACINFTV 119
E1_DerP2_DerF2 pfam02221
ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins ...
 32-155 2.77e-07

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: 46.98  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730493    32 ISYSYC----DHMKIPISIS-SEPCIRLKGTNGFVHVEF-IPRGNLKNLYFNLFININSIELPKRKEI---VC-HGYDDD 101
Cdd:pfam02221   2 VPFRDCgrnkDDAPTPKSVDiSPPCPLVRGQNLTISASGtTSDEISQGLKVDVEVRLGGITLPFPLPEtrdLCdELEVGS 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 66730493   102 YSFCRALKGEAVNTAIPFSFDGILfPKGHHRCVAEAIAGDtEEKLFCLNFTIIH 155
Cdd:pfam02221  82 GLSCPIKAGEYVTYTLTLPLPSEY-PPGKYTVEAELYDQD-GKPLTCFKIDVSI 133
 
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 ...
 23-153 5.16e-54

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: 166.97  E-value: 5.16e-54
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730493  23 WICNSSDAIISYSYCDHMKIpISISSEPCIRLKGTNGFVHVEFIPRGNLKNLYFNLFININSIELPKRKEIVCHGYDDDY 102
Cdd:cd00915   2 WVCNSSDLEFSYSSCDPMQD-FSFSAEPCSTLKGTNGFIRIKFILRRDIKELYFNLSLNVNGIEVLTRSEIICHGYLDKY 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 66730493 103 SFCRALKGEAVNTAIPFSFDGILFPKGHHRCVAEAIAGDtEEKLFCLNFTI 153
Cdd:cd00915  81 SFCGALKGETVYYVGPFSFKGILIPQGQYRCVAELIVEN-RETVACANFTI 130
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
 34-153 3.77e-24

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: 90.50  E-value: 3.77e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730493     34 YSYCDHMKI--PISISSEPCIRLKGTNGFVHVEFIPRGNLKNLYFNLFININSIELPKRKEI--VCHGyddDYSFCRALK 109
Cdd:smart00737   1 FKDCGSNDPgqISSVSISPCPPVRGKTLTISISFTLNEDISKLKVVVHVKIGGIEVPIPGETydLCKL---TGSKCPIEK 77

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 66730493    110 GEAVNTAIPFSFDGIlFPKGHHRCVAEAIAGDtEEKLFCLNFTI 153
Cdd:smart00737  78 GETVNYTNSLTVPGI-FPPGKYTVKWELTDED-GEELACINFTV 119
E1_DerP2_DerF2 pfam02221
ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins ...
 32-155 2.77e-07

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: 46.98  E-value: 2.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730493    32 ISYSYC----DHMKIPISIS-SEPCIRLKGTNGFVHVEF-IPRGNLKNLYFNLFININSIELPKRKEI---VC-HGYDDD 101
Cdd:pfam02221   2 VPFRDCgrnkDDAPTPKSVDiSPPCPLVRGQNLTISASGtTSDEISQGLKVDVEVRLGGITLPFPLPEtrdLCdELEVGS 81

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 66730493   102 YSFCRALKGEAVNTAIPFSFDGILfPKGHHRCVAEAIAGDtEEKLFCLNFTIIH 155
Cdd:pfam02221  82 GLSCPIKAGEYVTYTLTLPLPSEY-PPGKYTVEAELYDQD-GKPLTCFKIDVSI 133
 
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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