Splunc6 precursor [Mus musculus]
LBP/BPI/CETP family protein( domain architecture ID 1919)
LBP (lipopolysaccharide-binding protein)/BPI (bactericidal permeability-increasing protein)/CETP (cholesteryl ester transfer protein) family protein similar to Mesocricetus auratus cholesteryl ester transfer protein and Equus burchellii antiquorum latherin
List of domain hits
Name | Accession | Description | Interval | E-value | |||
BPI super family | cl00188 | BPI/LBP/CETP domain; Bactericidal permeability-increasing protein (BPI) / ... |
204-349 | 5.03e-03 | |||
BPI/LBP/CETP domain; Bactericidal permeability-increasing protein (BPI) / Lipopolysaccharide-binding protein (LBP) / Cholesteryl ester transfer protein (CETP) domain; binds to and neutralizes lipopolysaccharides from the outer membrane of Gram-negative bacteria.; Apolar pockets on the concave surface bind a molecule of phosphatidylcholine, primarily by interacting with their acyl chains; this suggests that the pockets may also bind the acyl chains of lipopolysaccharide. The actual alignment was detected with superfamily member cd00264: Pssm-ID: 412206 Cd Length: 208 Bit Score: 37.75 E-value: 5.03e-03
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Name | Accession | Description | Interval | E-value | |||
BPI | cd00264 | BPI/LBP/CETP domain; Bactericidal permeability-increasing protein (BPI) / ... |
204-349 | 5.03e-03 | |||
BPI/LBP/CETP domain; Bactericidal permeability-increasing protein (BPI) / Lipopolysaccharide-binding protein (LBP) / Cholesteryl ester transfer protein (CETP) domain; binds to and neutralizes lipopolysaccharides from the outer membrane of Gram-negative bacteria.; Apolar pockets on the concave surface bind a molecule of phosphatidylcholine, primarily by interacting with their acyl chains; this suggests that the pockets may also bind the acyl chains of lipopolysaccharide. Pssm-ID: 238164 Cd Length: 208 Bit Score: 37.75 E-value: 5.03e-03
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Name | Accession | Description | Interval | E-value | |||
BPI | cd00264 | BPI/LBP/CETP domain; Bactericidal permeability-increasing protein (BPI) / ... |
204-349 | 5.03e-03 | |||
BPI/LBP/CETP domain; Bactericidal permeability-increasing protein (BPI) / Lipopolysaccharide-binding protein (LBP) / Cholesteryl ester transfer protein (CETP) domain; binds to and neutralizes lipopolysaccharides from the outer membrane of Gram-negative bacteria.; Apolar pockets on the concave surface bind a molecule of phosphatidylcholine, primarily by interacting with their acyl chains; this suggests that the pockets may also bind the acyl chains of lipopolysaccharide. Pssm-ID: 238164 Cd Length: 208 Bit Score: 37.75 E-value: 5.03e-03
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Blast search parameters | ||||
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