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Conserved domains on  [gi|1196723647|ref|XP_021114017|]
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BPI fold-containing family C protein isoform X5 [Heterocephalus glaber]

Protein Classification

LBP/BPI/CETP family protein( domain architecture ID 10472645)

LBP (lipopolysaccharide-binding protein)/BPI (bactericidal permeability-increasing protein)/CETP (cholesteryl ester transfer protein) family protein similar to bactericidal/permeability-increasing protein-like

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LBP_BPI_CETP pfam01273
LBP / BPI / CETP family, N-terminal domain; The N and C terminal domains of the LBP/BPI/CETP ...
45-212 9.01e-36

LBP / BPI / CETP family, N-terminal domain; The N and C terminal domains of the LBP/BPI/CETP family are structurally similar.


:

Pssm-ID: 396022  Cd Length: 164  Bit Score: 128.96  E-value: 9.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647  45 ALDYGVRAGMEMMEQMVKEKHISDLKGSETLEFLkiDYVNYNFSNIKINAFSFPNTSLAFVPGVGIRVLTNHGTANISTN 124
Cdd:pfam01273   1 GLDYANQLGLKALQKELQKITLPDILGEEGIKLL--GKVLYNITNLKISNLQLPNLQLEFSPGGGLLLLIIPLTLKVSGK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647 125 WEVRATLFHdaggadlFLSGVYFTGVIILTQNALGHPALKLQDCYAQVSHAHVSFVGDLSTLYNTFAEPMEKPILRNLNA 204
Cdd:pfam01273  79 WPLRGSFLE-------LVVGVDITASLRLERDPQGRPTLVLSDCSSSPGSISISLLGGLGWLLDLLTNLLESTLPKVLQS 151

                  ....*...
gi 1196723647 205 MLCPIISE 212
Cdd:pfam01273 152 QLCPVIQS 159
BPI super family cl00188
BPI/LBP/CETP domain; Bactericidal permeability-increasing protein (BPI) / ...
249-415 6.09e-19

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: 85.49  E-value: 6.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647 249 HYLDLNLKGVFYPLEDLTDPLFSPEPFELPERSDSMLYIGISEHFFRSASFAHFTAGAFSVTLS--TKEISNHLIQNSQV 326
Cdd:pfam02886   1 NTLDVMFKGEFFPLNHRSPVRFPPPVMALPEEHDRMVYFAISDYFFNSALYVYHRAGFLKVTLTddMIPKDSDLRLTTKC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647 327 IGNVLSRIMDLYIlFQPLMLRIMATEPPVVRLQPGNFSLDIPASAVLFTQPQNATEmEPIVSMDFVASTSVGLAILGQRL 406
Cdd:pfam02886  81 FGPFLPLLAEQYP-NMTLELEGSALSPPLLNFSPGGLTISPNASLNAFVVLPNSVR-EQVFRLDVDTNASATLTINGSRV 158

                  ....*....
gi 1196723647 407 ICSLSLNRA 415
Cdd:pfam02886 159 TGELKLRKL 167
 
Name Accession Description Interval E-value
LBP_BPI_CETP pfam01273
LBP / BPI / CETP family, N-terminal domain; The N and C terminal domains of the LBP/BPI/CETP ...
45-212 9.01e-36

LBP / BPI / CETP family, N-terminal domain; The N and C terminal domains of the LBP/BPI/CETP family are structurally similar.


Pssm-ID: 396022  Cd Length: 164  Bit Score: 128.96  E-value: 9.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647  45 ALDYGVRAGMEMMEQMVKEKHISDLKGSETLEFLkiDYVNYNFSNIKINAFSFPNTSLAFVPGVGIRVLTNHGTANISTN 124
Cdd:pfam01273   1 GLDYANQLGLKALQKELQKITLPDILGEEGIKLL--GKVLYNITNLKISNLQLPNLQLEFSPGGGLLLLIIPLTLKVSGK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647 125 WEVRATLFHdaggadlFLSGVYFTGVIILTQNALGHPALKLQDCYAQVSHAHVSFVGDLSTLYNTFAEPMEKPILRNLNA 204
Cdd:pfam01273  79 WPLRGSFLE-------LVVGVDITASLRLERDPQGRPTLVLSDCSSSPGSISISLLGGLGWLLDLLTNLLESTLPKVLQS 151

                  ....*...
gi 1196723647 205 MLCPIISE 212
Cdd:pfam01273 152 QLCPVIQS 159
BPI1 cd00025
BPI/LBP/CETP N-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
36-260 5.22e-29

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: 5.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647  36 GIKARVTQRALDYGVRAGMEMMEQMVKEKHISDLKGSETLEFlkIDYVNYNFSNIKINAFSFPNTSLAFVPGVGIRVLTN 115
Cdd:cd00025     1 GAVARLSPKGLKFAKQQGLKVLQAELEKLQIPDILGAMKIKL--LGKGRVGLSNKEIQELKLPSSSIKLVEVKGLDLSIS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647 116 HGTANISTNWEVRATLFHDAGGADLFLSGVYFTGVIILTQNALGHPALKLQDCYAQVSHAHVSFVGDLSTLYNTFAEPME 195
Cdd:cd00025    79 NVSIGLSGVWKYNYRFILDGGNVELSVEGMNIQADLRLGRDPSGRPKLSLSDCSSTVGSLRVHLGGSLGWLAKLFMNFIE 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196723647 196 KPILRNLNAMLCPIISEEAEVLNANLSSLEVLTKIDNFTLLDYSLISPPEITEHYLDLNLKGVFY 260
Cdd:cd00025   159 SLLKKVLKGQLCPVIDASLVSMLESLLQLPKLPPVDSNAGVDYSLTSPPVLTASYLDSDIKGTFQ 223
BPI1 smart00328
BPI/LBP/CETP N-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
40-264 3.74e-27

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: 107.86  E-value: 3.74e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647   40 RVTQRALDYGVRAGMEMMEQMVKEKHISDLKGSETLEFLkiDYVNYNFSNIKINAFSFPNTSLAFVPGVGIRVLTNHGTA 119
Cdd:smart00328   1 RITQKGLDYAAQEGALALQKELPKITIPDIRGDFAIKLL--GIGHYSIYSLSISRLELPSSLLRFQPSKGLRLSISNLSL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647  120 NISTNWEVRATLFHDAGGADLFLSGVYFTGVIILTQNALGHPALKLQDCYAQVSHAHVSFVG-DLSTLYNTFAEPMEKPI 198
Cdd:smart00328  79 RVSGDLKGSLNFIKLEGNFQLSVEGLSISADLRIESNASGRPTVTLSSCSSSIGDVRLHFSGsVLGWLINLFRKFIENTL 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196723647  199 LRNLNAMLCPIISEE-AEVLNANLSSLEVLTKIDNFTLLDYSLISPPEITEHYLDLNLKGVFYPLED 264
Cdd:smart00328 159 RNVLEDQICPVIDSAvSNKMNDYLQTLPLSISLDSLIGVDYSLVSPPRVTASFLDVRLKGKFFWKNH 225
LBP_BPI_CETP_C pfam02886
LBP / BPI / CETP family, C-terminal domain; The N and C terminal domains of the LBP/BPI/CETP ...
249-415 6.09e-19

LBP / BPI / CETP family, C-terminal domain; The N and C terminal domains of the LBP/BPI/CETP family are structurally similar.


Pssm-ID: 397154  Cd Length: 238  Bit Score: 85.49  E-value: 6.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647 249 HYLDLNLKGVFYPLEDLTDPLFSPEPFELPERSDSMLYIGISEHFFRSASFAHFTAGAFSVTLS--TKEISNHLIQNSQV 326
Cdd:pfam02886   1 NTLDVMFKGEFFPLNHRSPVRFPPPVMALPEEHDRMVYFAISDYFFNSALYVYHRAGFLKVTLTddMIPKDSDLRLTTKC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647 327 IGNVLSRIMDLYIlFQPLMLRIMATEPPVVRLQPGNFSLDIPASAVLFTQPQNATEmEPIVSMDFVASTSVGLAILGQRL 406
Cdd:pfam02886  81 FGPFLPLLAEQYP-NMTLELEGSALSPPLLNFSPGGLTISPNASLNAFVVLPNSVR-EQVFRLDVDTNASATLTINGSRV 158

                  ....*....
gi 1196723647 407 ICSLSLNRA 415
Cdd:pfam02886 159 TGELKLRKL 167
BPI2 cd00026
BPI/LBP/CETP C-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
284-415 4.61e-13

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: 67.71  E-value: 4.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647 284 MLYIGISEHFFRSASFAHFTAGAFSVTL-STKEISNHLIqNSQVIGNVLSRIMDLYILfQPLMLRIMATEPPVVRLQPGN 362
Cdd:cd00026     1 MVYLAVSEHVFNSAALVYFQAGALNLLLtDDMPPSKSRL-TTSIFGIFIPELAKKYPN-MPQQLKISVSSPPHLVLSEGG 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1196723647 363 FSLDIPASAVLFTQPQNATEmEPIVSMDFVASTSVGLAILGQRLICSLSLNRA 415
Cdd:cd00026    79 ATLAQQLDVEIFATLPDSQL-RPLFRLGVDTSSSAQLSVSKKKLIGSLNLDRF 130
BPI2 smart00329
BPI/LBP/CETP C-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
281-415 1.99e-12

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: 65.80  E-value: 1.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647  281 SDSMLYIGISEHFFRSASFAHFTAGAFSVTLSTKEISNHL--IQNSQVIGNVLSRIMDLYIlFQPLMLRIMATEPPVVRL 358
Cdd:smart00329   1 SDRMVYLALSEYFFNSLLFVYQQAGALKLTITDDMLPKESkfLLTTCCFGTLVPEVAEQYP-DSTLQLEISVLSPPRVTL 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1196723647  359 QPGNFSLDIPASAVLFTQPQNATEmEPIVSMDFVASTSVGLAILGQRLICSLSLNRA 415
Cdd:smart00329  80 QPGGATVYIHASVKVFAILPDSSR-ASLFLMSVDTNVSAKSSFKTKKLLGELKLDKL 135
 
Name Accession Description Interval E-value
LBP_BPI_CETP pfam01273
LBP / BPI / CETP family, N-terminal domain; The N and C terminal domains of the LBP/BPI/CETP ...
45-212 9.01e-36

LBP / BPI / CETP family, N-terminal domain; The N and C terminal domains of the LBP/BPI/CETP family are structurally similar.


Pssm-ID: 396022  Cd Length: 164  Bit Score: 128.96  E-value: 9.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647  45 ALDYGVRAGMEMMEQMVKEKHISDLKGSETLEFLkiDYVNYNFSNIKINAFSFPNTSLAFVPGVGIRVLTNHGTANISTN 124
Cdd:pfam01273   1 GLDYANQLGLKALQKELQKITLPDILGEEGIKLL--GKVLYNITNLKISNLQLPNLQLEFSPGGGLLLLIIPLTLKVSGK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647 125 WEVRATLFHdaggadlFLSGVYFTGVIILTQNALGHPALKLQDCYAQVSHAHVSFVGDLSTLYNTFAEPMEKPILRNLNA 204
Cdd:pfam01273  79 WPLRGSFLE-------LVVGVDITASLRLERDPQGRPTLVLSDCSSSPGSISISLLGGLGWLLDLLTNLLESTLPKVLQS 151

                  ....*...
gi 1196723647 205 MLCPIISE 212
Cdd:pfam01273 152 QLCPVIQS 159
BPI1 cd00025
BPI/LBP/CETP N-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
36-260 5.22e-29

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: 5.22e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647  36 GIKARVTQRALDYGVRAGMEMMEQMVKEKHISDLKGSETLEFlkIDYVNYNFSNIKINAFSFPNTSLAFVPGVGIRVLTN 115
Cdd:cd00025     1 GAVARLSPKGLKFAKQQGLKVLQAELEKLQIPDILGAMKIKL--LGKGRVGLSNKEIQELKLPSSSIKLVEVKGLDLSIS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647 116 HGTANISTNWEVRATLFHDAGGADLFLSGVYFTGVIILTQNALGHPALKLQDCYAQVSHAHVSFVGDLSTLYNTFAEPME 195
Cdd:cd00025    79 NVSIGLSGVWKYNYRFILDGGNVELSVEGMNIQADLRLGRDPSGRPKLSLSDCSSTVGSLRVHLGGSLGWLAKLFMNFIE 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1196723647 196 KPILRNLNAMLCPIISEEAEVLNANLSSLEVLTKIDNFTLLDYSLISPPEITEHYLDLNLKGVFY 260
Cdd:cd00025   159 SLLKKVLKGQLCPVIDASLVSMLESLLQLPKLPPVDSNAGVDYSLTSPPVLTASYLDSDIKGTFQ 223
BPI1 smart00328
BPI/LBP/CETP N-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
40-264 3.74e-27

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: 107.86  E-value: 3.74e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647   40 RVTQRALDYGVRAGMEMMEQMVKEKHISDLKGSETLEFLkiDYVNYNFSNIKINAFSFPNTSLAFVPGVGIRVLTNHGTA 119
Cdd:smart00328   1 RITQKGLDYAAQEGALALQKELPKITIPDIRGDFAIKLL--GIGHYSIYSLSISRLELPSSLLRFQPSKGLRLSISNLSL 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647  120 NISTNWEVRATLFHDAGGADLFLSGVYFTGVIILTQNALGHPALKLQDCYAQVSHAHVSFVG-DLSTLYNTFAEPMEKPI 198
Cdd:smart00328  79 RVSGDLKGSLNFIKLEGNFQLSVEGLSISADLRIESNASGRPTVTLSSCSSSIGDVRLHFSGsVLGWLINLFRKFIENTL 158
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196723647  199 LRNLNAMLCPIISEE-AEVLNANLSSLEVLTKIDNFTLLDYSLISPPEITEHYLDLNLKGVFYPLED 264
Cdd:smart00328 159 RNVLEDQICPVIDSAvSNKMNDYLQTLPLSISLDSLIGVDYSLVSPPRVTASFLDVRLKGKFFWKNH 225
LBP_BPI_CETP_C pfam02886
LBP / BPI / CETP family, C-terminal domain; The N and C terminal domains of the LBP/BPI/CETP ...
249-415 6.09e-19

LBP / BPI / CETP family, C-terminal domain; The N and C terminal domains of the LBP/BPI/CETP family are structurally similar.


Pssm-ID: 397154  Cd Length: 238  Bit Score: 85.49  E-value: 6.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647 249 HYLDLNLKGVFYPLEDLTDPLFSPEPFELPERSDSMLYIGISEHFFRSASFAHFTAGAFSVTLS--TKEISNHLIQNSQV 326
Cdd:pfam02886   1 NTLDVMFKGEFFPLNHRSPVRFPPPVMALPEEHDRMVYFAISDYFFNSALYVYHRAGFLKVTLTddMIPKDSDLRLTTKC 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647 327 IGNVLSRIMDLYIlFQPLMLRIMATEPPVVRLQPGNFSLDIPASAVLFTQPQNATEmEPIVSMDFVASTSVGLAILGQRL 406
Cdd:pfam02886  81 FGPFLPLLAEQYP-NMTLELEGSALSPPLLNFSPGGLTISPNASLNAFVVLPNSVR-EQVFRLDVDTNASATLTINGSRV 158

                  ....*....
gi 1196723647 407 ICSLSLNRA 415
Cdd:pfam02886 159 TGELKLRKL 167
BPI2 cd00026
BPI/LBP/CETP C-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
284-415 4.61e-13

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: 67.71  E-value: 4.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647 284 MLYIGISEHFFRSASFAHFTAGAFSVTL-STKEISNHLIqNSQVIGNVLSRIMDLYILfQPLMLRIMATEPPVVRLQPGN 362
Cdd:cd00026     1 MVYLAVSEHVFNSAALVYFQAGALNLLLtDDMPPSKSRL-TTSIFGIFIPELAKKYPN-MPQQLKISVSSPPHLVLSEGG 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1196723647 363 FSLDIPASAVLFTQPQNATEmEPIVSMDFVASTSVGLAILGQRLICSLSLNRA 415
Cdd:cd00026    79 ATLAQQLDVEIFATLPDSQL-RPLFRLGVDTSSSAQLSVSKKKLIGSLNLDRF 130
BPI2 smart00329
BPI/LBP/CETP C-terminal domain; Bactericidal permeability-increasing protein (BPI) / ...
281-415 1.99e-12

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: 65.80  E-value: 1.99e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647  281 SDSMLYIGISEHFFRSASFAHFTAGAFSVTLSTKEISNHL--IQNSQVIGNVLSRIMDLYIlFQPLMLRIMATEPPVVRL 358
Cdd:smart00329   1 SDRMVYLALSEYFFNSLLFVYQQAGALKLTITDDMLPKESkfLLTTCCFGTLVPEVAEQYP-DSTLQLEISVLSPPRVTL 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1196723647  359 QPGNFSLDIPASAVLFTQPQNATEmEPIVSMDFVASTSVGLAILGQRLICSLSLNRA 415
Cdd:smart00329  80 QPGGATVYIHASVKVFAILPDSSR-ASLFLMSVDTNVSAKSSFKTKKLLGELKLDKL 135
BPI cd00264
BPI/LBP/CETP domain; Bactericidal permeability-increasing protein (BPI) / ...
36-257 5.49e-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: 55.86  E-value: 5.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647  36 GIKARVTQ----RALDYGVRAGmEMMEQMVKEKhISDLKGSETLEFLKIDYVNYNFSNIKINAFSFPNTSLAFVPGvGIr 111
Cdd:cd00264     1 MVVLRLSEdvlnSALQVYLKAG-ALLLTLTIPD-IPKALKLKLSGIIPLGAKKYPDMNLQLKILSLSSPTLKLSPK-GL- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647 112 vltnhgTANISTNWEVRATLFHDAGGADLFLSGVYFTGVIILTQNAlGHPALKLQDCYAQVSHAHVSFVGdlstlYNTFA 191
Cdd:cd00264    77 ------DLSQSVSIELFVTWPASDGGNPLFSLEVEISASLQLSVDP-GRLTLSLSLCSSTVELLSSNIGG-----FGNFI 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1196723647 192 EPMEKPILrnlNAMLCPIISEEAEVLNANLSSLEVLTKIDNFTLLDYSLISPPEITEHYLDLNLKG 257
Cdd:cd00264   145 VSLLQKVL---NTILCPVVLPALNSKLRSGLPLLPVPPVPSPAGVDYSLTAEPVLSASFLLLDADV 207
BPI cd00264
BPI/LBP/CETP domain; Bactericidal permeability-increasing protein (BPI) / ...
284-415 1.93e-08

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: 54.31  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196723647 284 MLYIGISEHFFRSASFAHFTAGAFSVTLSTKEISNHLIQNSQVIGNVLSRIMDlyilFQPLMLRIMATEPPVVRLQPGNF 363
Cdd:cd00264     1 MVVLRLSEDVLNSALQVYLKAGALLLTLTIPDIPKALKLKLSGIIPLGAKKYP----DMNLQLKILSLSSPTLKLSPKGL 76
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1196723647 364 SLDIPASAVLFTQPQNATEMEPIVSMDFVASTSVGLAILGQRLICSLSLNRA 415
Cdd:cd00264    77 DLSQSVSIELFVTWPASDGGNPLFSLEVEISASLQLSVDPGRLTLSLSLCSS 128
 
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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