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Conserved domains on  [gi|1396648834|gb|PXM48366|]
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fimbrial protein [Klebsiella variicola]

Protein Classification

fimbrial protein( domain architecture ID 11182034)

fimbrial protein such as fimbrial adhesive protein FimH, which mediates shear-dependent binding of type 1 fimbriae to mannosylated surfaces via force-enhanced allosteric catch bonds and requires FimF and FimG

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FimH_man-bind pfam09160
FimH, mannose binding; Members of this family adopt a secondary structure consisting of a beta ...
26-169 4.07e-70

FimH, mannose binding; Members of this family adopt a secondary structure consisting of a beta sandwich, with nine strands arranged in two sheets in a Greek key topology. They are predominantly found in bacterial mannose-specific adhesins, since they are capable of binding to D-mannose.


:

Pssm-ID: 430438  Cd Length: 145  Bit Score: 213.91  E-value: 4.07e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648834  26 KTATGATIPIGGGSANVYVNLTPAVNVGQNLVVDLSTQIFCHNDYPETITDYVTLQRGSAYGGVLSSFSGTVKYNGTSYP 105
Cdd:pfam09160   1 KTANGSSIPIGGGTANVYVNLDPSIGVGQNLVVDLSTSISCKNDYPGTITDHVNLQQGSAYGGVLANFKGSVYYNGSSYP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1396648834 106 FPTTTETARVVYDSRTDKPWPTVLYLTPVSTAGGVAITAGSLIAVLILHQTNNYNSDS-FQFIWN 169
Cdd:pfam09160  81 FPLTSNTSVLDITSTTYTPWPLKLYLTPVSAAGGVVIKSGSLIARLNMHQTASLGSGNpRNFTWN 145
FimA COG3539
Pilin (type 1 fimbrial protein) [Cell motility];
169-301 2.89e-10

Pilin (type 1 fimbrial protein) [Cell motility];


:

Pssm-ID: 442760 [Multi-domain]  Cd Length: 172  Bit Score: 58.13  E-value: 2.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648834 169 NIYANNDVVVPTggCDVSA--RDVTVTLPDYP---------GSMAVPLTVH---C--AQSQQLGYYLSGTTADSANAIFT 232
Cdd:COG3539    25 TVNFTGTVVAPT--CTINTgsKDQTVDLGTVStsdlngvgsTSGPKPFSIKltnCdaGTSNSVKVTFTGTADSANPGLLA 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1396648834 233 NTASaSPAQGIGVQLT-RNGSAVPANSTVSLGTVSTS-PVNLGLTATYARTTGQVTAGNVQSIIGITFVYQ 301
Cdd:COG3539   103 NTGS-GGASGVGIQLLdSDGTPIPLGTPSSAVTLTSNgSATLPFYARYVATGATVTAGSFNATATFTIDYQ 172
 
Name Accession Description Interval E-value
FimH_man-bind pfam09160
FimH, mannose binding; Members of this family adopt a secondary structure consisting of a beta ...
26-169 4.07e-70

FimH, mannose binding; Members of this family adopt a secondary structure consisting of a beta sandwich, with nine strands arranged in two sheets in a Greek key topology. They are predominantly found in bacterial mannose-specific adhesins, since they are capable of binding to D-mannose.


Pssm-ID: 430438  Cd Length: 145  Bit Score: 213.91  E-value: 4.07e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648834  26 KTATGATIPIGGGSANVYVNLTPAVNVGQNLVVDLSTQIFCHNDYPETITDYVTLQRGSAYGGVLSSFSGTVKYNGTSYP 105
Cdd:pfam09160   1 KTANGSSIPIGGGTANVYVNLDPSIGVGQNLVVDLSTSISCKNDYPGTITDHVNLQQGSAYGGVLANFKGSVYYNGSSYP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1396648834 106 FPTTTETARVVYDSRTDKPWPTVLYLTPVSTAGGVAITAGSLIAVLILHQTNNYNSDS-FQFIWN 169
Cdd:pfam09160  81 FPLTSNTSVLDITSTTYTPWPLKLYLTPVSAAGGVVIKSGSLIARLNMHQTASLGSGNpRNFTWN 145
FimH_man-bind cd10466
Mannose binding domain of FimH and related proteins; This family, restricted to ...
23-180 5.50e-62

Mannose binding domain of FimH and related proteins; This family, restricted to gammaproteobacteria, includes FimH, a mannose-specific adhesin of uropathogenic Escherichia coli strains. The domain appears to bind specifically to D-mannose and mediates cellular adhesion to mannosylated proteins, a prerequisite to colonization and subsequent invasion of epithelial tissues.


Pssm-ID: 198456  Cd Length: 160  Bit Score: 193.71  E-value: 5.50e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648834  23 FACKTATGATIpIGGGSANVYVNLTPAVNVGQNLVVDLSTQIFCHNDYPE-TITDYVTLQRGSAYGGVLSSFSGTVKYNG 101
Cdd:cd10466     1 FTCRVADTGQI-FGSGSANVYVNLSPTVNVGQNLVVDLSQLIQCMNDDPSgTITDYVNLLRGSGFGGPLLNFSGSLDFYG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648834 102 TSYPFPTTTETARVVYDSRTDKPWPTVLYLTPVSTAGGVAITAGSLIAVLILHQTNNYN--SDSFQFIWNIYANNDVVVP 179
Cdd:cd10466    80 STYPFPLQSDTKVIVYSSGTWKPLPLKLYLTPVSAAGGVVIKAGDLIATLTMNKKSTYGgrADPFNFTWRFYAKNDVVIP 159

                  .
gi 1396648834 180 T 180
Cdd:cd10466   160 T 160
FimA COG3539
Pilin (type 1 fimbrial protein) [Cell motility];
169-301 2.89e-10

Pilin (type 1 fimbrial protein) [Cell motility];


Pssm-ID: 442760 [Multi-domain]  Cd Length: 172  Bit Score: 58.13  E-value: 2.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648834 169 NIYANNDVVVPTggCDVSA--RDVTVTLPDYP---------GSMAVPLTVH---C--AQSQQLGYYLSGTTADSANAIFT 232
Cdd:COG3539    25 TVNFTGTVVAPT--CTINTgsKDQTVDLGTVStsdlngvgsTSGPKPFSIKltnCdaGTSNSVKVTFTGTADSANPGLLA 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1396648834 233 NTASaSPAQGIGVQLT-RNGSAVPANSTVSLGTVSTS-PVNLGLTATYARTTGQVTAGNVQSIIGITFVYQ 301
Cdd:COG3539   103 NTGS-GGASGVGIQLLdSDGTPIPLGTPSSAVTLTSNgSATLPFYARYVATGATVTAGSFNATATFTIDYQ 172
PRK15220 PRK15220
fimbrial protein YehD;
197-299 1.04e-04

fimbrial protein YehD;


Pssm-ID: 237928  Cd Length: 178  Bit Score: 42.11  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648834 197 YPGSMAVPLTVHCAQSQQLGYYLSGTTADSANAIFTNTASASPAqGIGVQLTRNGSAVPANSTVSL--GTVSTSPVNLGL 274
Cdd:PRK15220   73 YTNPTAMPLKVKCTQGAAPRISFSRSQFVDNMDITKNNGSANGA-GFAVYYDGTDVKPDPETGVTLnpNKFENGVYTLNF 151
                          90       100
                  ....*....|....*....|....*
gi 1396648834 275 TATYARTTGQVTAGNVQSIIGITFV 299
Cdd:PRK15220  152 SARYARVDNDVTSGDVESTLTLTVV 176
Fimbrial pfam00419
Fimbrial protein;
176-301 1.50e-04

Fimbrial protein;


Pssm-ID: 425671  Cd Length: 152  Bit Score: 41.27  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648834 176 VVVPTGGCDVSARDV-TVTLPDYPG-----------SMAVPLTVHC---AQSQQLGYYLSGTTADSANAIFTNTASASPA 240
Cdd:pfam00419   7 VTRVPATCKITAGTPiEVDFGQIPVnelnaggegsrQKPFSITLECssgSSAVKVTVGLFGTADASSPNLLLTGNGAGAA 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1396648834 241 QGIGVQL-TRNGSAVPANSTVSLGTVSTSPV---NLGLTATYARTTGQ-VTAGNVQSIIGITFVYQ 301
Cdd:pfam00419  87 TGVGIRLyDANGGALPPNNGTSSIPVSATAAvatGITFTASLVATTGGtPTAGDFNATATIVVDYQ 152
 
Name Accession Description Interval E-value
FimH_man-bind pfam09160
FimH, mannose binding; Members of this family adopt a secondary structure consisting of a beta ...
26-169 4.07e-70

FimH, mannose binding; Members of this family adopt a secondary structure consisting of a beta sandwich, with nine strands arranged in two sheets in a Greek key topology. They are predominantly found in bacterial mannose-specific adhesins, since they are capable of binding to D-mannose.


Pssm-ID: 430438  Cd Length: 145  Bit Score: 213.91  E-value: 4.07e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648834  26 KTATGATIPIGGGSANVYVNLTPAVNVGQNLVVDLSTQIFCHNDYPETITDYVTLQRGSAYGGVLSSFSGTVKYNGTSYP 105
Cdd:pfam09160   1 KTANGSSIPIGGGTANVYVNLDPSIGVGQNLVVDLSTSISCKNDYPGTITDHVNLQQGSAYGGVLANFKGSVYYNGSSYP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1396648834 106 FPTTTETARVVYDSRTDKPWPTVLYLTPVSTAGGVAITAGSLIAVLILHQTNNYNSDS-FQFIWN 169
Cdd:pfam09160  81 FPLTSNTSVLDITSTTYTPWPLKLYLTPVSAAGGVVIKSGSLIARLNMHQTASLGSGNpRNFTWN 145
FimH_man-bind cd10466
Mannose binding domain of FimH and related proteins; This family, restricted to ...
23-180 5.50e-62

Mannose binding domain of FimH and related proteins; This family, restricted to gammaproteobacteria, includes FimH, a mannose-specific adhesin of uropathogenic Escherichia coli strains. The domain appears to bind specifically to D-mannose and mediates cellular adhesion to mannosylated proteins, a prerequisite to colonization and subsequent invasion of epithelial tissues.


Pssm-ID: 198456  Cd Length: 160  Bit Score: 193.71  E-value: 5.50e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648834  23 FACKTATGATIpIGGGSANVYVNLTPAVNVGQNLVVDLSTQIFCHNDYPE-TITDYVTLQRGSAYGGVLSSFSGTVKYNG 101
Cdd:cd10466     1 FTCRVADTGQI-FGSGSANVYVNLSPTVNVGQNLVVDLSQLIQCMNDDPSgTITDYVNLLRGSGFGGPLLNFSGSLDFYG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648834 102 TSYPFPTTTETARVVYDSRTDKPWPTVLYLTPVSTAGGVAITAGSLIAVLILHQTNNYN--SDSFQFIWNIYANNDVVVP 179
Cdd:cd10466    80 STYPFPLQSDTKVIVYSSGTWKPLPLKLYLTPVSAAGGVVIKAGDLIATLTMNKKSTYGgrADPFNFTWRFYAKNDVVIP 159

                  .
gi 1396648834 180 T 180
Cdd:cd10466   160 T 160
FimA COG3539
Pilin (type 1 fimbrial protein) [Cell motility];
169-301 2.89e-10

Pilin (type 1 fimbrial protein) [Cell motility];


Pssm-ID: 442760 [Multi-domain]  Cd Length: 172  Bit Score: 58.13  E-value: 2.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648834 169 NIYANNDVVVPTggCDVSA--RDVTVTLPDYP---------GSMAVPLTVH---C--AQSQQLGYYLSGTTADSANAIFT 232
Cdd:COG3539    25 TVNFTGTVVAPT--CTINTgsKDQTVDLGTVStsdlngvgsTSGPKPFSIKltnCdaGTSNSVKVTFTGTADSANPGLLA 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1396648834 233 NTASaSPAQGIGVQLT-RNGSAVPANSTVSLGTVSTS-PVNLGLTATYARTTGQVTAGNVQSIIGITFVYQ 301
Cdd:COG3539   103 NTGS-GGASGVGIQLLdSDGTPIPLGTPSSAVTLTSNgSATLPFYARYVATGATVTAGSFNATATFTIDYQ 172
PRK15220 PRK15220
fimbrial protein YehD;
197-299 1.04e-04

fimbrial protein YehD;


Pssm-ID: 237928  Cd Length: 178  Bit Score: 42.11  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648834 197 YPGSMAVPLTVHCAQSQQLGYYLSGTTADSANAIFTNTASASPAqGIGVQLTRNGSAVPANSTVSL--GTVSTSPVNLGL 274
Cdd:PRK15220   73 YTNPTAMPLKVKCTQGAAPRISFSRSQFVDNMDITKNNGSANGA-GFAVYYDGTDVKPDPETGVTLnpNKFENGVYTLNF 151
                          90       100
                  ....*....|....*....|....*
gi 1396648834 275 TATYARTTGQVTAGNVQSIIGITFV 299
Cdd:PRK15220  152 SARYARVDNDVTSGDVESTLTLTVV 176
Fimbrial pfam00419
Fimbrial protein;
176-301 1.50e-04

Fimbrial protein;


Pssm-ID: 425671  Cd Length: 152  Bit Score: 41.27  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1396648834 176 VVVPTGGCDVSARDV-TVTLPDYPG-----------SMAVPLTVHC---AQSQQLGYYLSGTTADSANAIFTNTASASPA 240
Cdd:pfam00419   7 VTRVPATCKITAGTPiEVDFGQIPVnelnaggegsrQKPFSITLECssgSSAVKVTVGLFGTADASSPNLLLTGNGAGAA 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1396648834 241 QGIGVQL-TRNGSAVPANSTVSLGTVSTSPV---NLGLTATYARTTGQ-VTAGNVQSIIGITFVYQ 301
Cdd:pfam00419  87 TGVGIRLyDANGGALPPNNGTSSIPVSATAAvatGITFTASLVATTGGtPTAGDFNATATIVVDYQ 152
 
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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