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Conserved domains on  [gi|21465855|pdb|1KIU|J]
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Chain J, FimH PROTEIN

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 ...
4-147 1.47e-72

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: 219.30  E-value: 1.47e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIU_J          4 KTANGTAIPIGGGSANVYVNLAPVVNVGQNLVVDLSTQIFCHNDYPETITDYVTLQRGSAYGGVLSNFSGTVKYSGSSYP 83
Cdd:pfam09160   1 KTANGSSIPIGGGTANVYVNLDPSIGVGQNLVVDLSTSISCKNDYPGTITDHVNLQQGSAYGGVLANFKGSVYYNGSSYP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
1KIU_J         84 FPTTSETPRVVYNSRTDKPWPVALYLTPVSSAGGVAIKAGSLIAVLILRNTNNYNSDD-FQFVWN 147
Cdd:pfam09160  81 FPLTSNTSVLDITSTTYTPWPLKLYLTPVSAAGGVVIKSGSLIARLNMHQTASLGSGNpRNFTWN 145
FimA COG3539
Pilin (type 1 fimbrial protein) [Cell motility];
147-279 5.39e-12

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


:

Pssm-ID: 442760 [Multi-domain]  Cd Length: 172  Bit Score: 62.75  E-value: 5.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIU_J      147 NIYANNDVVVPTggCDVSA--RDVTVTLPDYP-----------GSVPIPLTV-YC--AKSQNLGYYLSGTTADAGNSIFT 210
Cdd:COG3539  25 TVNFTGTVVAPT--CTINTgsKDQTVDLGTVStsdlngvgstsGPKPFSIKLtNCdaGTSNSVKVTFTGTADSANPGLLA 102
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1KIU_J      211 NTASfSPAQGVGVQLT-RNGTIIPANNTVSLGAV-GTSAVSLGLTANYARTGGQVTAGNVQSIIGVTFVYQ 279
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 ...
4-147 1.47e-72

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: 219.30  E-value: 1.47e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIU_J          4 KTANGTAIPIGGGSANVYVNLAPVVNVGQNLVVDLSTQIFCHNDYPETITDYVTLQRGSAYGGVLSNFSGTVKYSGSSYP 83
Cdd:pfam09160   1 KTANGSSIPIGGGTANVYVNLDPSIGVGQNLVVDLSTSISCKNDYPGTITDHVNLQQGSAYGGVLANFKGSVYYNGSSYP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
1KIU_J         84 FPTTSETPRVVYNSRTDKPWPVALYLTPVSSAGGVAIKAGSLIAVLILRNTNNYNSDD-FQFVWN 147
Cdd:pfam09160  81 FPLTSNTSVLDITSTTYTPWPLKLYLTPVSAAGGVVIKSGSLIARLNMHQTASLGSGNpRNFTWN 145
FimH_man-bind cd10466
Mannose binding domain of FimH and related proteins; This family, restricted to ...
1-158 1.27e-63

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: 196.80  E-value: 1.27e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIU_J        1 FACKTANGTAIpIGGGSANVYVNLAPVVNVGQNLVVDLSTQIFCHNDYPE-TITDYVTLQRGSAYGGVLSNFSGTVKYSG 79
Cdd:cd10466   1 FTCRVADTGQI-FGSGSANVYVNLSPTVNVGQNLVVDLSQLIQCMNDDPSgTITDYVNLLRGSGFGGPLLNFSGSLDFYG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIU_J       80 SSYPFPTTSETPRVVYNSRTDKPWPVALYLTPVSSAGGVAIKAGSLIAVLILRNTNNYN--SDDFQFVWNIYANNDVVVP 157
Cdd:cd10466  80 STYPFPLQSDTKVIVYSSGTWKPLPLKLYLTPVSAAGGVVIKAGDLIATLTMNKKSTYGgrADPFNFTWRFYAKNDVVIP 159

                .
1KIU_J      158 T 158
Cdd:cd10466 160 T 160
FimA COG3539
Pilin (type 1 fimbrial protein) [Cell motility];
147-279 5.39e-12

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


Pssm-ID: 442760 [Multi-domain]  Cd Length: 172  Bit Score: 62.75  E-value: 5.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIU_J      147 NIYANNDVVVPTggCDVSA--RDVTVTLPDYP-----------GSVPIPLTV-YC--AKSQNLGYYLSGTTADAGNSIFT 210
Cdd:COG3539  25 TVNFTGTVVAPT--CTINTgsKDQTVDLGTVStsdlngvgstsGPKPFSIKLtNCdaGTSNSVKVTFTGTADSANPGLLA 102
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1KIU_J      211 NTASfSPAQGVGVQLT-RNGTIIPANNTVSLGAV-GTSAVSLGLTANYARTGGQVTAGNVQSIIGVTFVYQ 279
Cdd:COG3539 103 NTGS-GGASGVGIQLLdSDGTPIPLGTPSSAVTLtSNGSATLPFYARYVATGATVTAGSFNATATFTIDYQ 172
Fimbrial pfam00419
Fimbrial protein;
154-279 7.06e-06

Fimbrial protein;


Pssm-ID: 425671  Cd Length: 152  Bit Score: 45.12  E-value: 7.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIU_J        154 VVVPTGGCDVSARDV-TVTLPDYPG-----------SVPIPLTVYC---AKSQNLGYYLSGTTADAGNSIFTNTASFSPA 218
Cdd:pfam00419   7 VTRVPATCKITAGTPiEVDFGQIPVnelnaggegsrQKPFSITLECssgSSAVKVTVGLFGTADASSPNLLLTGNGAGAA 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
1KIU_J        219 QGVGVQL-TRNGTIIPANNTVS---LGAVGTSAVSLGLTANYARTGGQ-VTAGNVQSIIGVTFVYQ 279
Cdd:pfam00419  87 TGVGIRLyDANGGALPPNNGTSsipVSATAAVATGITFTASLVATTGGtPTAGDFNATATIVVDYQ 152
PRK15220 PRK15220
fimbrial protein YehD;
175-277 1.26e-04

fimbrial protein YehD;


Pssm-ID: 237928  Cd Length: 178  Bit Score: 41.72  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIU_J       175 YPGSVPIPLTVYCAKSQNLGYYLSGTTADAGNSIFTNTASfSPAQGVGVQLTRNGTIIPANNTVSL-GAVGTSAV-SLGL 252
Cdd:PRK15220  73 YTNPTAMPLKVKCTQGAAPRISFSRSQFVDNMDITKNNGS-ANGAGFAVYYDGTDVKPDPETGVTLnPNKFENGVyTLNF 151
                         90       100
                 ....*....|....*....|....*
1KIU_J       253 TANYARTGGQVTAGNVQSIIGVTFV 277
Cdd:PRK15220 152 SARYARVDNDVTSGDVESTLTLTVV 176
 
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 ...
4-147 1.47e-72

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: 219.30  E-value: 1.47e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIU_J          4 KTANGTAIPIGGGSANVYVNLAPVVNVGQNLVVDLSTQIFCHNDYPETITDYVTLQRGSAYGGVLSNFSGTVKYSGSSYP 83
Cdd:pfam09160   1 KTANGSSIPIGGGTANVYVNLDPSIGVGQNLVVDLSTSISCKNDYPGTITDHVNLQQGSAYGGVLANFKGSVYYNGSSYP 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
1KIU_J         84 FPTTSETPRVVYNSRTDKPWPVALYLTPVSSAGGVAIKAGSLIAVLILRNTNNYNSDD-FQFVWN 147
Cdd:pfam09160  81 FPLTSNTSVLDITSTTYTPWPLKLYLTPVSAAGGVVIKSGSLIARLNMHQTASLGSGNpRNFTWN 145
FimH_man-bind cd10466
Mannose binding domain of FimH and related proteins; This family, restricted to ...
1-158 1.27e-63

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: 196.80  E-value: 1.27e-63
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIU_J        1 FACKTANGTAIpIGGGSANVYVNLAPVVNVGQNLVVDLSTQIFCHNDYPE-TITDYVTLQRGSAYGGVLSNFSGTVKYSG 79
Cdd:cd10466   1 FTCRVADTGQI-FGSGSANVYVNLSPTVNVGQNLVVDLSQLIQCMNDDPSgTITDYVNLLRGSGFGGPLLNFSGSLDFYG 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIU_J       80 SSYPFPTTSETPRVVYNSRTDKPWPVALYLTPVSSAGGVAIKAGSLIAVLILRNTNNYN--SDDFQFVWNIYANNDVVVP 157
Cdd:cd10466  80 STYPFPLQSDTKVIVYSSGTWKPLPLKLYLTPVSAAGGVVIKAGDLIATLTMNKKSTYGgrADPFNFTWRFYAKNDVVIP 159

                .
1KIU_J      158 T 158
Cdd:cd10466 160 T 160
FimA COG3539
Pilin (type 1 fimbrial protein) [Cell motility];
147-279 5.39e-12

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


Pssm-ID: 442760 [Multi-domain]  Cd Length: 172  Bit Score: 62.75  E-value: 5.39e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIU_J      147 NIYANNDVVVPTggCDVSA--RDVTVTLPDYP-----------GSVPIPLTV-YC--AKSQNLGYYLSGTTADAGNSIFT 210
Cdd:COG3539  25 TVNFTGTVVAPT--CTINTgsKDQTVDLGTVStsdlngvgstsGPKPFSIKLtNCdaGTSNSVKVTFTGTADSANPGLLA 102
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1KIU_J      211 NTASfSPAQGVGVQLT-RNGTIIPANNTVSLGAV-GTSAVSLGLTANYARTGGQVTAGNVQSIIGVTFVYQ 279
Cdd:COG3539 103 NTGS-GGASGVGIQLLdSDGTPIPLGTPSSAVTLtSNGSATLPFYARYVATGATVTAGSFNATATFTIDYQ 172
Fimbrial pfam00419
Fimbrial protein;
154-279 7.06e-06

Fimbrial protein;


Pssm-ID: 425671  Cd Length: 152  Bit Score: 45.12  E-value: 7.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIU_J        154 VVVPTGGCDVSARDV-TVTLPDYPG-----------SVPIPLTVYC---AKSQNLGYYLSGTTADAGNSIFTNTASFSPA 218
Cdd:pfam00419   7 VTRVPATCKITAGTPiEVDFGQIPVnelnaggegsrQKPFSITLECssgSSAVKVTVGLFGTADASSPNLLLTGNGAGAA 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
1KIU_J        219 QGVGVQL-TRNGTIIPANNTVS---LGAVGTSAVSLGLTANYARTGGQ-VTAGNVQSIIGVTFVYQ 279
Cdd:pfam00419  87 TGVGIRLyDANGGALPPNNGTSsipVSATAAVATGITFTASLVATTGGtPTAGDFNATATIVVDYQ 152
PRK15220 PRK15220
fimbrial protein YehD;
175-277 1.26e-04

fimbrial protein YehD;


Pssm-ID: 237928  Cd Length: 178  Bit Score: 41.72  E-value: 1.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIU_J       175 YPGSVPIPLTVYCAKSQNLGYYLSGTTADAGNSIFTNTASfSPAQGVGVQLTRNGTIIPANNTVSL-GAVGTSAV-SLGL 252
Cdd:PRK15220  73 YTNPTAMPLKVKCTQGAAPRISFSRSQFVDNMDITKNNGS-ANGAGFAVYYDGTDVKPDPETGVTLnPNKFENGVyTLNF 151
                         90       100
                 ....*....|....*....|....*
1KIU_J       253 TANYARTGGQVTAGNVQSIIGVTFV 277
Cdd:PRK15220 152 SARYARVDNDVTSGDVESTLTLTVV 176
PRK15305 PRK15305
fimbrial protein StkG;
169-279 9.81e-04

fimbrial protein StkG;


Pssm-ID: 185205  Cd Length: 353  Bit Score: 40.01  E-value: 9.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1KIU_J       169 TVTLPDYPGS---------VPIPLTVYCAKSQNLGYYLSGTTADAGNSIFTNTAS----FSPAQGVGVQLTR-NGTIIPA 234
Cdd:PRK15305 222 TVNLGDWYRSdvekdqtteVPFQITGTCTGTIKVSFVAKSSYTNADKNLFTNSITsnssVTAAGGVGVKISSpAYSQIHA 301
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
1KIU_J       235 NNTVSLGAVGT------SAVSLGLTANYARTGGQ-VTAGNVQSIIGVTFVYQ 279
Cdd:PRK15305 302 DSSPEYIAVGNiigmpvTSVNANFKAKLVKTGTEaVTPGIFGSSVTFQVTYE 353
 
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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