LBP (lipopolysaccharide-binding protein)/BPI (bactericidal permeability-increasing protein)/CETP (cholesteryl ester transfer protein) family protein similar to bactericidal/permeability-increasing protein-like
BPI/LBP/CETP domain; Bactericidal permeability-increasing protein (BPI) / ...
238-475
6.50e-35
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 pfam02886:
Pssm-ID: 412206 Cd Length: 238 Bit Score: 130.94 E-value: 6.50e-35
BPI/LBP/CETP C-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
273-474
1.15e-32
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: 123.57 E-value: 1.15e-32
BPI/LBP/CETP N-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
25-249
1.62e-28
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: 112.85 E-value: 1.62e-28
BPI/LBP/CETP C-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
270-471
1.74e-28
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: 112.02 E-value: 1.74e-28
BPI/LBP/CETP N-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
29-253
2.09e-26
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: 106.71 E-value: 2.09e-26
BPI/LBP/CETP C-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
273-474
1.15e-32
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: 123.57 E-value: 1.15e-32
BPI/LBP/CETP N-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
25-249
1.62e-28
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: 112.85 E-value: 1.62e-28
BPI/LBP/CETP C-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
270-471
1.74e-28
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: 112.02 E-value: 1.74e-28
BPI/LBP/CETP N-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
29-253
2.09e-26
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: 106.71 E-value: 2.09e-26
BPI/LBP/CETP domain; Bactericidal permeability-increasing protein (BPI) / ...
273-473
1.03e-16
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: 78.58 E-value: 1.03e-16
BPI/LBP/CETP domain; Bactericidal permeability-increasing protein (BPI) / ...
25-246
8.98e-09
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: 55.47 E-value: 8.98e-09
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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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
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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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(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.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
(illustrated example)
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
non-specific hits
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the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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