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Conserved domains on  [gi|446442841|ref|WP_000520696|]
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MULTISPECIES: fimbrial protein [Enterobacteriaceae]

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 ...
28-171 1.00e-76

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: 230.86  E-value: 1.00e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446442841   28 NVDGGSS--IGAGTTSVYVNLDPVIQPGQNLVVDLSQHISCWNDYGGWYdTDHINLVQGSAFAGSLQSYKGSLYWNNVTY 105
Cdd:pfam09160   1 KTANGSSipIGGGTANVYVNLDPSIGVGQNLVVDLSTSISCKNDYPGTI-TDHVNLQQGSAYGGVLANFKGSVYYNGSSY 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446442841  106 PFPLTTNTNVLDIGDKTPMPLPLKLYITPVGAAGGVVIKAGEVIARIHMYKIATLGSGNPRNFTWN 171
Cdd:pfam09160  80 PFPLTSNTSVLDITSTTYTPWPLKLYLTPVSAAGGVVIKSGSLIARLNMHQTASLGSGNPRNFTWN 145
FimA COG3539
Pilin (type 1 fimbrial protein) [Cell motility];
171-304 1.87e-09

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


:

Pssm-ID: 442760 [Multi-domain]  Cd Length: 172  Bit Score: 55.82  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446442841 171 NIISNNSVVMPTggCTVD--SRNVNVNLPDFPGSA-------------EIPLgVYCSSE--QKLSFYLSGATTDSARQVF 233
Cdd:COG3539   25 TVNFTGTVVAPT--CTINtgSKDQTVDLGTVSTSDlngvgstsgpkpfSIKL-TNCDAGtsNSVKVTFTGTADSANPGLL 101
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446442841 234 ANTAPDAtkASGVGVSLM-RNGKILATGENVSLGTVNKS-KVPLGLSATYGQTGNKVAAGTVQSVIGVTFIYE 304
Cdd:COG3539  102 ANTGSGG--ASGVGIQLLdSDGTPIPLGTPSSAVTLTSNgSATLPFYARYVATGATVTAGSFNATATFTIDYQ 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 ...
28-171 1.00e-76

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: 230.86  E-value: 1.00e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446442841   28 NVDGGSS--IGAGTTSVYVNLDPVIQPGQNLVVDLSQHISCWNDYGGWYdTDHINLVQGSAFAGSLQSYKGSLYWNNVTY 105
Cdd:pfam09160   1 KTANGSSipIGGGTANVYVNLDPSIGVGQNLVVDLSTSISCKNDYPGTI-TDHVNLQQGSAYGGVLANFKGSVYYNGSSY 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446442841  106 PFPLTTNTNVLDIGDKTPMPLPLKLYITPVGAAGGVVIKAGEVIARIHMYKIATLGSGNPRNFTWN 171
Cdd:pfam09160  80 PFPLTSNTSVLDITSTTYTPWPLKLYLTPVSAAGGVVIKSGSLIARLNMHQTASLGSGNPRNFTWN 145
FimH_man-bind cd10466
Mannose binding domain of FimH and related proteins; This family, restricted to ...
25-182 8.99e-76

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: 228.77  E-value: 8.99e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446442841  25 FSCNV-DGGSSIGAGTTSVYVNLDPVIQPGQNLVVDLSQHISCWNDYGGWYDTDHINLVQGSAFAGSLQSYKGSLYWNNV 103
Cdd:cd10466    1 FTCRVaDTGQIFGSGSANVYVNLSPTVNVGQNLVVDLSQLIQCMNDDPSGTITDYVNLLRGSGFGGPLLNFSGSLDFYGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446442841 104 TYPFPLTTNTNVLDIGDKTPMPLPLKLYITPVGAAGGVVIKAGEVIARIHMYKIATLGS-GNPRNFTWNIISNNSVVMPT 182
Cdd:cd10466   81 TYPFPLQSDTKVIVYSSGTWKPLPLKLYLTPVSAAGGVVIKAGDLIATLTMNKKSTYGGrADPFNFTWRFYAKNDVVIPT 160
FimA COG3539
Pilin (type 1 fimbrial protein) [Cell motility];
171-304 1.87e-09

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


Pssm-ID: 442760 [Multi-domain]  Cd Length: 172  Bit Score: 55.82  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446442841 171 NIISNNSVVMPTggCTVD--SRNVNVNLPDFPGSA-------------EIPLgVYCSSE--QKLSFYLSGATTDSARQVF 233
Cdd:COG3539   25 TVNFTGTVVAPT--CTINtgSKDQTVDLGTVSTSDlngvgstsgpkpfSIKL-TNCDAGtsNSVKVTFTGTADSANPGLL 101
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446442841 234 ANTAPDAtkASGVGVSLM-RNGKILATGENVSLGTVNKS-KVPLGLSATYGQTGNKVAAGTVQSVIGVTFIYE 304
Cdd:COG3539  102 ANTGSGG--ASGVGIQLLdSDGTPIPLGTPSSAVTLTSNgSATLPFYARYVATGATVTAGSFNATATFTIDYQ 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 ...
28-171 1.00e-76

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: 230.86  E-value: 1.00e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446442841   28 NVDGGSS--IGAGTTSVYVNLDPVIQPGQNLVVDLSQHISCWNDYGGWYdTDHINLVQGSAFAGSLQSYKGSLYWNNVTY 105
Cdd:pfam09160   1 KTANGSSipIGGGTANVYVNLDPSIGVGQNLVVDLSTSISCKNDYPGTI-TDHVNLQQGSAYGGVLANFKGSVYYNGSSY 79
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446442841  106 PFPLTTNTNVLDIGDKTPMPLPLKLYITPVGAAGGVVIKAGEVIARIHMYKIATLGSGNPRNFTWN 171
Cdd:pfam09160  80 PFPLTSNTSVLDITSTTYTPWPLKLYLTPVSAAGGVVIKSGSLIARLNMHQTASLGSGNPRNFTWN 145
FimH_man-bind cd10466
Mannose binding domain of FimH and related proteins; This family, restricted to ...
25-182 8.99e-76

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: 228.77  E-value: 8.99e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446442841  25 FSCNV-DGGSSIGAGTTSVYVNLDPVIQPGQNLVVDLSQHISCWNDYGGWYDTDHINLVQGSAFAGSLQSYKGSLYWNNV 103
Cdd:cd10466    1 FTCRVaDTGQIFGSGSANVYVNLSPTVNVGQNLVVDLSQLIQCMNDDPSGTITDYVNLLRGSGFGGPLLNFSGSLDFYGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446442841 104 TYPFPLTTNTNVLDIGDKTPMPLPLKLYITPVGAAGGVVIKAGEVIARIHMYKIATLGS-GNPRNFTWNIISNNSVVMPT 182
Cdd:cd10466   81 TYPFPLQSDTKVIVYSSGTWKPLPLKLYLTPVSAAGGVVIKAGDLIATLTMNKKSTYGGrADPFNFTWRFYAKNDVVIPT 160
FimA COG3539
Pilin (type 1 fimbrial protein) [Cell motility];
171-304 1.87e-09

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


Pssm-ID: 442760 [Multi-domain]  Cd Length: 172  Bit Score: 55.82  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446442841 171 NIISNNSVVMPTggCTVD--SRNVNVNLPDFPGSA-------------EIPLgVYCSSE--QKLSFYLSGATTDSARQVF 233
Cdd:COG3539   25 TVNFTGTVVAPT--CTINtgSKDQTVDLGTVSTSDlngvgstsgpkpfSIKL-TNCDAGtsNSVKVTFTGTADSANPGLL 101
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446442841 234 ANTAPDAtkASGVGVSLM-RNGKILATGENVSLGTVNKS-KVPLGLSATYGQTGNKVAAGTVQSVIGVTFIYE 304
Cdd:COG3539  102 ANTGSGG--ASGVGIQLLdSDGTPIPLGTPSSAVTLTSNgSATLPFYARYVATGATVTAGSFNATATFTIDYQ 172
 
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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