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Conserved domains on  [gi|66826923|ref|XP_646816|]
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hypothetical protein DDB_G0270454 [Dictyostelium discoideum AX4]

Protein Classification

ML domain-containing protein( domain architecture ID 10654303)

ML (MD-2-related lipid-recognition) domain-containing protein similar to Dictyostelium discoideum phosphatidylglycerol/phosphatidylinositol transfer protein that catalyzes the intermembrane transfer of phosphatidylglycerol and phosphatidylinositol

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
 29-144 1.15e-30

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: 106.68  E-value: 1.15e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826923     29 WNDCsDPNDSFKIEKLEFSPEQPIAGQDLIISISGYLNKEITNGEAYLSITFD--RIPIIKLKGNLCNGMGVTCPIQQGN 106
Cdd:smart00737   1 FKDC-GSNDPGQISSVSISPCPPVRGKTLTISISFTLNEDISKLKVVVHVKIGgiEVPIPGETYDLCKLTGSKCPIEKGE 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 66826923    107 YSTTTINQEIPENAPQGYYYVNFVLYDQDDLQITCIDV 144
Cdd:smart00737  80 TVNYTNSLTVPGIFPPGKYTVKWELTDEDGEELACINF 117
 
Name Accession Description Interval E-value
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
 29-144 1.15e-30

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: 106.68  E-value: 1.15e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826923     29 WNDCsDPNDSFKIEKLEFSPEQPIAGQDLIISISGYLNKEITNGEAYLSITFD--RIPIIKLKGNLCNGMGVTCPIQQGN 106
Cdd:smart00737   1 FKDC-GSNDPGQISSVSISPCPPVRGKTLTISISFTLNEDISKLKVVVHVKIGgiEVPIPGETYDLCKLTGSKCPIEKGE 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 66826923    107 YSTTTINQEIPENAPQGYYYVNFVLYDQDDLQITCIDV 144
Cdd:smart00737  80 TVNYTNSLTVPGIFPPGKYTVKWELTDEDGEELACINF 117
E1_DerP2_DerF2 pfam02221
ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins ...
 26-148 1.34e-26

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: 97.06  E-value: 1.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826923    26 SVEWNDCSDP-NDSFKIEKLEFSPEQPI-AGQDLIISISGYLNKEITNGE-AYLSITFDRIPII---KLKGNLCN----G 95
Cdd:pfam02221   1 SVPFRDCGRNkDDAPTPKSVDISPPCPLvRGQNLTISASGTTSDEISQGLkVDVEVRLGGITLPfplPETRDLCDelevG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 66826923    96 MGVTCPIQQGNYSTTTINQEIPENAPQGYYYVNFVLYDQDDLQITCIDVQMNI 148
Cdd:pfam02221  81 SGLSCPIKAGEYVTYTLTLPLPSEYPPGKYTVEAELYDQDGKPLTCFKIDVSI 133
PG-PI_TP cd00917
The phosphatidylinositol/phosphatidylglycerol transfer protein (PG/PI-TP) has been shown to ...
 40-143 1.09e-14

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: 65.81  E-value: 1.09e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826923  40 KIEKLEFSPEQPIAGQDLIISISGYLNKEITNGeAYLSIT--FDRIPIIKLKGNLCNGM---GVTCPIQQGNYSTTTiNQ 114
Cdd:cd00917  13 KVTSVEISPNPPAAGQNLTIEASGSVGKEIEDG-AYVVVEvkYGFIRLLSETYDLCDETknvDLSCPIEPGDKFLTK-LV 90

                        90       100
                ....*....|....*....|....*....
gi 66826923 115 EIPENAPQGYYYVNFVLYDQDDLQITCID 143
Cdd:cd00917  91 DLPGEIPPGKYTVSARAYTKDDEEITCLS 119
 
Name Accession Description Interval E-value
ML smart00737
Domain involved in innate immunity and lipid metabolism; ML (MD-2-related lipid-recognition) ...
 29-144 1.15e-30

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: 106.68  E-value: 1.15e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826923     29 WNDCsDPNDSFKIEKLEFSPEQPIAGQDLIISISGYLNKEITNGEAYLSITFD--RIPIIKLKGNLCNGMGVTCPIQQGN 106
Cdd:smart00737   1 FKDC-GSNDPGQISSVSISPCPPVRGKTLTISISFTLNEDISKLKVVVHVKIGgiEVPIPGETYDLCKLTGSKCPIEKGE 79

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 66826923    107 YSTTTINQEIPENAPQGYYYVNFVLYDQDDLQITCIDV 144
Cdd:smart00737  80 TVNYTNSLTVPGIFPPGKYTVKWELTDEDGEELACINF 117
E1_DerP2_DerF2 pfam02221
ML domain; ML domain - MD-2-related lipid recognition domain. This family consists of proteins ...
 26-148 1.34e-26

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: 97.06  E-value: 1.34e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826923    26 SVEWNDCSDP-NDSFKIEKLEFSPEQPI-AGQDLIISISGYLNKEITNGE-AYLSITFDRIPII---KLKGNLCN----G 95
Cdd:pfam02221   1 SVPFRDCGRNkDDAPTPKSVDISPPCPLvRGQNLTISASGTTSDEISQGLkVDVEVRLGGITLPfplPETRDLCDelevG 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 66826923    96 MGVTCPIQQGNYSTTTINQEIPENAPQGYYYVNFVLYDQDDLQITCIDVQMNI 148
Cdd:pfam02221  81 SGLSCPIKAGEYVTYTLTLPLPSEYPPGKYTVEAELYDQDGKPLTCFKIDVSI 133
PG-PI_TP cd00917
The phosphatidylinositol/phosphatidylglycerol transfer protein (PG/PI-TP) has been shown to ...
 40-143 1.09e-14

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: 65.81  E-value: 1.09e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826923  40 KIEKLEFSPEQPIAGQDLIISISGYLNKEITNGeAYLSIT--FDRIPIIKLKGNLCNGM---GVTCPIQQGNYSTTTiNQ 114
Cdd:cd00917  13 KVTSVEISPNPPAAGQNLTIEASGSVGKEIEDG-AYVVVEvkYGFIRLLSETYDLCDETknvDLSCPIEPGDKFLTK-LV 90

                        90       100
                ....*....|....*....|....*....
gi 66826923 115 EIPENAPQGYYYVNFVLYDQDDLQITCID 143
Cdd:cd00917  91 DLPGEIPPGKYTVSARAYTKDDEEITCLS 119
ML cd00912
The ML (MD-2-related lipid-recognition) domain is present in MD-1, MD-2, GM2 activator protein, ...
 29-145 7.08e-04

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: 37.50  E-value: 7.08e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66826923  29 WNDCSDPndSFKIEKLEFSPEQPIA-----GQDLIISISGYLNKEITNGEAYLSITFDRIPIIKLKG--NLCNGMG---V 98
Cdd:cd00912   1 LVDCSDN--SANIKEVLLSPCDPLPcpdhrGGNYNLSVTGTLREDIKSLYVDLALMSQGIKVLNPDNsyDFCEAGLpkpS 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 66826923  99 TCPIQQGNYSTTTINQEIPEN-APQGYYYVNFVLYDQDDLQITCIDVQ 145
Cdd:cd00912  79 FCPLRKGQQYSYAKTVNVPEFtIPTIEYQVVLEDVTDKGEVLACAQAT 126
 
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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