LBP (lipopolysaccharide-binding protein)/BPI (bactericidal permeability-increasing protein)/CETP (cholesteryl ester transfer protein) family protein similar to Homo sapiens BPI fold-containing family B member 6 and Gallus gallus cholesteryl ester transfer protein
BPI/LBP/CETP N-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
27-252
1.50e-69
BPI/LBP/CETP N-terminal domain; Bactericidal permeability-increasing protein (BPI) / Lipopolysaccharide-binding protein (LBP) / Cholesteryl ester transfer protein (CETP) N-terminal 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: 237992 Cd Length: 223 Bit Score: 219.55 E-value: 1.50e-69
BPI/LBP/CETP domain; Bactericidal permeability-increasing protein (BPI) / ...
250-416
4.78e-34
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 smart00329:
Pssm-ID: 412206 Cd Length: 202 Bit Score: 126.27 E-value: 4.78e-34
BPI/LBP/CETP N-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
27-252
1.50e-69
BPI/LBP/CETP N-terminal domain; Bactericidal permeability-increasing protein (BPI) / Lipopolysaccharide-binding protein (LBP) / Cholesteryl ester transfer protein (CETP) N-terminal 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: 237992 Cd Length: 223 Bit Score: 219.55 E-value: 1.50e-69
BPI/LBP/CETP N-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
31-251
5.87e-69
BPI/LBP/CETP N-terminal domain; Bactericidal permeability-increasing protein (BPI) / Lipopolysaccharide-binding protein (LBP) / Cholesteryl ester transfer protein (CETP) N-terminal domain
Pssm-ID: 214622 [Multi-domain] Cd Length: 225 Bit Score: 218.03 E-value: 5.87e-69
BPI/LBP/CETP C-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
250-416
4.78e-34
BPI/LBP/CETP C-terminal domain; Bactericidal permeability-increasing protein (BPI) / Lipopolysaccharide-binding protein (LBP) / Cholesteryl ester transfer protein (CETP) C-terminal domain
Pssm-ID: 128624 Cd Length: 202 Bit Score: 126.27 E-value: 4.78e-34
BPI/LBP/CETP C-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
213-419
1.24e-29
BPI/LBP/CETP C-terminal domain; Bactericidal permeability-increasing protein (BPI) / Lipopolysaccharide-binding protein (LBP) / Cholesteryl ester transfer protein (CETP) C-terminal 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: 237993 Cd Length: 200 Bit Score: 114.32 E-value: 1.24e-29
BPI/LBP/CETP N-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
27-252
1.50e-69
BPI/LBP/CETP N-terminal domain; Bactericidal permeability-increasing protein (BPI) / Lipopolysaccharide-binding protein (LBP) / Cholesteryl ester transfer protein (CETP) N-terminal 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: 237992 Cd Length: 223 Bit Score: 219.55 E-value: 1.50e-69
BPI/LBP/CETP N-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
31-251
5.87e-69
BPI/LBP/CETP N-terminal domain; Bactericidal permeability-increasing protein (BPI) / Lipopolysaccharide-binding protein (LBP) / Cholesteryl ester transfer protein (CETP) N-terminal domain
Pssm-ID: 214622 [Multi-domain] Cd Length: 225 Bit Score: 218.03 E-value: 5.87e-69
BPI/LBP/CETP C-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
250-416
4.78e-34
BPI/LBP/CETP C-terminal domain; Bactericidal permeability-increasing protein (BPI) / Lipopolysaccharide-binding protein (LBP) / Cholesteryl ester transfer protein (CETP) C-terminal domain
Pssm-ID: 128624 Cd Length: 202 Bit Score: 126.27 E-value: 4.78e-34
BPI/LBP/CETP C-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
213-419
1.24e-29
BPI/LBP/CETP C-terminal domain; Bactericidal permeability-increasing protein (BPI) / Lipopolysaccharide-binding protein (LBP) / Cholesteryl ester transfer protein (CETP) C-terminal 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: 237993 Cd Length: 200 Bit Score: 114.32 E-value: 1.24e-29
BPI/LBP/CETP domain; Bactericidal permeability-increasing protein (BPI) / ...
27-250
3.18e-29
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: 113.25 E-value: 3.18e-29
BPI/LBP/CETP domain; Bactericidal permeability-increasing protein (BPI) / ...
264-419
2.23e-14
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: 71.65 E-value: 2.23e-14
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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Functional characterization of the conserved domain architecture found on the query.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
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