NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1486941900]
View 

Chain B, PapGII adhesin protein

Protein Classification

PapG_CBD and PapG_C domain-containing protein( domain architecture ID 11975394)

PapG_CBD and PapG_C domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PapG_CBD super family cl28665
PapG carbohydrate / receptor binding domain (CBD); PapG, the adhesin of the P-pili, is ...
 1-206 8.94e-129

PapG carbohydrate / receptor binding domain (CBD); PapG, the adhesin of the P-pili, is situated at the tip, mediating the attachment of uropathogenic Escherichia coli to the uroepithelium of the human kidney; PapG has a two-domain architecture: a carbohydrate binding N-terminus (this domain) and chaperone binding C-terminus (C-terminal pilin region). The carbohydrate-binding domain interacts with the receptor glycan. There are 3 PapG alleles, class I-III, which bind to different receptor isotypes, GbO3, GbO4, and GbO5, respectively.


The actual alignment was detected with superfamily member pfam03627:

Pssm-ID: 475053  Cd Length: 226  Bit Score: 366.48  E-value: 8.94e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486941900   1 WNNIVFYSLGDVNSYQGGNVVITQRPQFITSWRPGIATVTWNQCNGPEFADGfwAYYREYIAWVVFPKKVMTQNGYPLFI 80
Cdd:pfam03627  23 WHNVMFYSFNDYNSYQGGNVKITDRPQFIIPWNTGSATATYNSCNGPEFASG--VYFQEYIAWVVVPKHVMTQNGYNIFL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486941900  81 EVHNKGSWSEENTGDNDSYFFLKGYKWDERAFDAGNLCQKPGEITRLTEKFDDIIFKVALPADLPLGDYSVKIPYTSGMQ 160
Cdd:pfam03627 101 EVQSKGGWSEENTGDNDSYFFLKGYEWDEWTNDGGRVCFKPGEKKQLTNKFNDLIFKVALPADLPKGDYSVPIKYIRGIQ 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1486941900 161 RHFASYLGARFKIPYNVAKTLPRENEMLFLFKNIGGCRPSAQSLEI 206
Cdd:pfam03627 181 RHYYDYWGARYKIPYSQAKTLPATNTLLFSFKNTGGCRPSAQSLEI 226
PapG_C pfam03628
PapG chaperone-binding domain; PapG, the adhesin of the P-pili, is situated at the tip and is ...
 208-316 1.66e-67

PapG chaperone-binding domain; PapG, the adhesin of the P-pili, is situated at the tip and is only a minor component of the whole pilus structure. A two-domain structure has been postulated for PapG; a carbohydrate binding N-terminus and chaperone binding C-terminus (this domain). The chaperone-binding domain is highly conserved, and is essential for the correct assembly of the pili structure when aided by the chaperone molecule PapD.


:

Pssm-ID: 397609  Cd Length: 108  Bit Score: 206.29  E-value: 1.66e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486941900 208 HGDLSINSANNHYAAQTLSVSCDVPANIRFMLLRNTTPTYSHgKKFSVGLGHGWDSIVSVNGVDTGETTMRWYKAGTQNL 287
Cdd:pfam03628   1 HGNLSIDSANGNYASQTLSIYCDVPVNVKISLLRNTLPAYNN-QKFSVGLGNGWDSIISLDGVDTGEETLRWYTAGSQTV 79

                          90       100
                  ....*....|....*....|....*....
gi 1486941900 288 TIGSRLYGESSKIQPGVLSGSATLLMILP 316
Cdd:pfam03628  80 TIGSRLYGESGKIQPGVLSGSMTMLMILP 108
 
Name Accession Description Interval E-value
PapG_N pfam03627
PapG carbohydrate binding domain; PapG, the adhesin of the P-pili, is situated at the tip and ...
 1-206 8.94e-129

PapG carbohydrate binding domain; PapG, the adhesin of the P-pili, is situated at the tip and is only a minor component of the whole pilus structure. A two-domain structure has been postulated for PapG; a carbohydrate binding N-terminus (this domain) and chaperone binding C-terminus. The carbohydrate-binding domain interacts with the receptor glycan.


Pssm-ID: 460994  Cd Length: 226  Bit Score: 366.48  E-value: 8.94e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486941900   1 WNNIVFYSLGDVNSYQGGNVVITQRPQFITSWRPGIATVTWNQCNGPEFADGfwAYYREYIAWVVFPKKVMTQNGYPLFI 80
Cdd:pfam03627  23 WHNVMFYSFNDYNSYQGGNVKITDRPQFIIPWNTGSATATYNSCNGPEFASG--VYFQEYIAWVVVPKHVMTQNGYNIFL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486941900  81 EVHNKGSWSEENTGDNDSYFFLKGYKWDERAFDAGNLCQKPGEITRLTEKFDDIIFKVALPADLPLGDYSVKIPYTSGMQ 160
Cdd:pfam03627 101 EVQSKGGWSEENTGDNDSYFFLKGYEWDEWTNDGGRVCFKPGEKKQLTNKFNDLIFKVALPADLPKGDYSVPIKYIRGIQ 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1486941900 161 RHFASYLGARFKIPYNVAKTLPRENEMLFLFKNIGGCRPSAQSLEI 206
Cdd:pfam03627 181 RHYYDYWGARYKIPYSQAKTLPATNTLLFSFKNTGGCRPSAQSLEI 226
PapG_CBD cd00239
PapG carbohydrate / receptor binding domain (CBD); PapG, the adhesin of the P-pili, is ...
 1-196 2.76e-117

PapG carbohydrate / receptor binding domain (CBD); PapG, the adhesin of the P-pili, is situated at the tip, mediating the attachment of uropathogenic Escherichia coli to the uroepithelium of the human kidney; PapG has a two-domain architecture: a carbohydrate binding N-terminus (this domain) and chaperone binding C-terminus (C-terminal pilin region). The carbohydrate-binding domain interacts with the receptor glycan. There are 3 PapG alleles, class I-III, which bind to different receptor isotypes, GbO3, GbO4, and GbO5, respectively.


Pssm-ID: 119414  Cd Length: 194  Bit Score: 336.02  E-value: 2.76e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486941900   1 WNNIVFYSLGDVNSYQGGNVVITQRPQFITSWRPGIATVTWNQCNGPEFADGfwAYYREYIAWVVFPKKVMTQNGYPLFI 80
Cdd:cd00239     1 WHNVMFYSFNDYIYYPGGNVKVTDRPQFIIPWNTGTATATYVSCNGPEFASG--VYFQEYIAWVVVPKHVSTQNGYNIFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486941900  81 EVHNKGSWSEENTGDNDSYFFLKGYKWDERAFDAGNLCQKPGEITRLTEKFDDIIFKVALPADLPLGDYSVKIPYTSGMQ 160
Cdd:cd00239    79 EVQSKGSWSLENTGDNDNYYFLKGYEWDEWTFDGGRTCFNPGEKKQLANKFNDLTFNVLLPVDLPKGDYTFPVKYIRGIQ 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1486941900 161 RHFASYLGARFKIPYNVAKTLPRENEMLFLFKNIGG 196
Cdd:cd00239   159 RHYYDYWGGRYKIPYSQMKTLPATNTLMFSFKNTGG 194
PapG_C pfam03628
PapG chaperone-binding domain; PapG, the adhesin of the P-pili, is situated at the tip and is ...
 208-316 1.66e-67

PapG chaperone-binding domain; PapG, the adhesin of the P-pili, is situated at the tip and is only a minor component of the whole pilus structure. A two-domain structure has been postulated for PapG; a carbohydrate binding N-terminus and chaperone binding C-terminus (this domain). The chaperone-binding domain is highly conserved, and is essential for the correct assembly of the pili structure when aided by the chaperone molecule PapD.


Pssm-ID: 397609  Cd Length: 108  Bit Score: 206.29  E-value: 1.66e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486941900 208 HGDLSINSANNHYAAQTLSVSCDVPANIRFMLLRNTTPTYSHgKKFSVGLGHGWDSIVSVNGVDTGETTMRWYKAGTQNL 287
Cdd:pfam03628   1 HGNLSIDSANGNYASQTLSIYCDVPVNVKISLLRNTLPAYNN-QKFSVGLGNGWDSIISLDGVDTGEETLRWYTAGSQTV 79

                          90       100
                  ....*....|....*....|....*....
gi 1486941900 288 TIGSRLYGESSKIQPGVLSGSATLLMILP 316
Cdd:pfam03628  80 TIGSRLYGESGKIQPGVLSGSMTMLMILP 108
 
Name Accession Description Interval E-value
PapG_N pfam03627
PapG carbohydrate binding domain; PapG, the adhesin of the P-pili, is situated at the tip and ...
 1-206 8.94e-129

PapG carbohydrate binding domain; PapG, the adhesin of the P-pili, is situated at the tip and is only a minor component of the whole pilus structure. A two-domain structure has been postulated for PapG; a carbohydrate binding N-terminus (this domain) and chaperone binding C-terminus. The carbohydrate-binding domain interacts with the receptor glycan.


Pssm-ID: 460994  Cd Length: 226  Bit Score: 366.48  E-value: 8.94e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486941900   1 WNNIVFYSLGDVNSYQGGNVVITQRPQFITSWRPGIATVTWNQCNGPEFADGfwAYYREYIAWVVFPKKVMTQNGYPLFI 80
Cdd:pfam03627  23 WHNVMFYSFNDYNSYQGGNVKITDRPQFIIPWNTGSATATYNSCNGPEFASG--VYFQEYIAWVVVPKHVMTQNGYNIFL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486941900  81 EVHNKGSWSEENTGDNDSYFFLKGYKWDERAFDAGNLCQKPGEITRLTEKFDDIIFKVALPADLPLGDYSVKIPYTSGMQ 160
Cdd:pfam03627 101 EVQSKGGWSEENTGDNDSYFFLKGYEWDEWTNDGGRVCFKPGEKKQLTNKFNDLIFKVALPADLPKGDYSVPIKYIRGIQ 180

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1486941900 161 RHFASYLGARFKIPYNVAKTLPRENEMLFLFKNIGGCRPSAQSLEI 206
Cdd:pfam03627 181 RHYYDYWGARYKIPYSQAKTLPATNTLLFSFKNTGGCRPSAQSLEI 226
PapG_CBD cd00239
PapG carbohydrate / receptor binding domain (CBD); PapG, the adhesin of the P-pili, is ...
 1-196 2.76e-117

PapG carbohydrate / receptor binding domain (CBD); PapG, the adhesin of the P-pili, is situated at the tip, mediating the attachment of uropathogenic Escherichia coli to the uroepithelium of the human kidney; PapG has a two-domain architecture: a carbohydrate binding N-terminus (this domain) and chaperone binding C-terminus (C-terminal pilin region). The carbohydrate-binding domain interacts with the receptor glycan. There are 3 PapG alleles, class I-III, which bind to different receptor isotypes, GbO3, GbO4, and GbO5, respectively.


Pssm-ID: 119414  Cd Length: 194  Bit Score: 336.02  E-value: 2.76e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486941900   1 WNNIVFYSLGDVNSYQGGNVVITQRPQFITSWRPGIATVTWNQCNGPEFADGfwAYYREYIAWVVFPKKVMTQNGYPLFI 80
Cdd:cd00239     1 WHNVMFYSFNDYIYYPGGNVKVTDRPQFIIPWNTGTATATYVSCNGPEFASG--VYFQEYIAWVVVPKHVSTQNGYNIFL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486941900  81 EVHNKGSWSEENTGDNDSYFFLKGYKWDERAFDAGNLCQKPGEITRLTEKFDDIIFKVALPADLPLGDYSVKIPYTSGMQ 160
Cdd:cd00239    79 EVQSKGSWSLENTGDNDNYYFLKGYEWDEWTFDGGRTCFNPGEKKQLANKFNDLTFNVLLPVDLPKGDYTFPVKYIRGIQ 158

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1486941900 161 RHFASYLGARFKIPYNVAKTLPRENEMLFLFKNIGG 196
Cdd:cd00239   159 RHYYDYWGGRYKIPYSQMKTLPATNTLMFSFKNTGG 194
PapG_C pfam03628
PapG chaperone-binding domain; PapG, the adhesin of the P-pili, is situated at the tip and is ...
 208-316 1.66e-67

PapG chaperone-binding domain; PapG, the adhesin of the P-pili, is situated at the tip and is only a minor component of the whole pilus structure. A two-domain structure has been postulated for PapG; a carbohydrate binding N-terminus and chaperone binding C-terminus (this domain). The chaperone-binding domain is highly conserved, and is essential for the correct assembly of the pili structure when aided by the chaperone molecule PapD.


Pssm-ID: 397609  Cd Length: 108  Bit Score: 206.29  E-value: 1.66e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1486941900 208 HGDLSINSANNHYAAQTLSVSCDVPANIRFMLLRNTTPTYSHgKKFSVGLGHGWDSIVSVNGVDTGETTMRWYKAGTQNL 287
Cdd:pfam03628   1 HGNLSIDSANGNYASQTLSIYCDVPVNVKISLLRNTLPAYNN-QKFSVGLGNGWDSIISLDGVDTGEETLRWYTAGSQTV 79

                          90       100
                  ....*....|....*....|....*....
gi 1486941900 288 TIGSRLYGESSKIQPGVLSGSATLLMILP 316
Cdd:pfam03628  80 TIGSRLYGESGKIQPGVLSGSMTMLMILP 108
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH