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Conserved domains on  [gi|489212222|ref|WP_003120996|]
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MULTISPECIES: type 4 pilus major pilin [Pseudomonas]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PilS super family cl27040
PilS N terminal; Type IV pili are bacterial virulence-associated adhesins that promote ...
44-173 1.02e-11

PilS N terminal; Type IV pili are bacterial virulence-associated adhesins that promote bacterial attachment to host cells. In Salmonella typhi, the structural pilin protein PilS interacts with the cystic fibrosis transmembrane conductance regulator. Mutagenesis studies suggest that residues on an alpha-beta loop and the C terminal disulphide-bonded region of PilS might be involved in binding specificity of the pilus.


The actual alignment was detected with superfamily member pfam08805:

Pssm-ID: 474887  Cd Length: 138  Bit Score: 59.48  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212222   44 SSNANEEQRNISVIAANARALKTSSGYGSSGTNLIpsLIAINGVPKNMSVSSGVVYNVYGGSVTVSS-----TGMGFSIT 118
Cdd:pfam08805   1 LYQASAEQTNITTIQAGTKKLYKGRAGYDGLSNAT--LIAAKVVPTSMTRTGDIYYNRWGGNVSVSPargsgFNNSFTIT 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489212222  119 TSKLPKDACITLGTKIAKNTFEQTKINSGTAITGE--VTTAAATQACS-SDSNSITWT 173
Cdd:pfam08805  79 YTNVPEGACGDLSTMLSNAGWYSVTIGGTAMVDANvtVTLATATTACDrGDANTVIFT 136
 
Name Accession Description Interval E-value
PilS pfam08805
PilS N terminal; Type IV pili are bacterial virulence-associated adhesins that promote ...
44-173 1.02e-11

PilS N terminal; Type IV pili are bacterial virulence-associated adhesins that promote bacterial attachment to host cells. In Salmonella typhi, the structural pilin protein PilS interacts with the cystic fibrosis transmembrane conductance regulator. Mutagenesis studies suggest that residues on an alpha-beta loop and the C terminal disulphide-bonded region of PilS might be involved in binding specificity of the pilus.


Pssm-ID: 430227  Cd Length: 138  Bit Score: 59.48  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212222   44 SSNANEEQRNISVIAANARALKTSSGYGSSGTNLIpsLIAINGVPKNMSVSSGVVYNVYGGSVTVSS-----TGMGFSIT 118
Cdd:pfam08805   1 LYQASAEQTNITTIQAGTKKLYKGRAGYDGLSNAT--LIAAKVVPTSMTRTGDIYYNRWGGNVSVSPargsgFNNSFTIT 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489212222  119 TSKLPKDACITLGTKIAKNTFEQTKINSGTAITGE--VTTAAATQACS-SDSNSITWT 173
Cdd:pfam08805  79 YTNVPEGACGDLSTMLSNAGWYSVTIGGTAMVDANvtVTLATATTACDrGDANTVIFT 136
 
Name Accession Description Interval E-value
PilS pfam08805
PilS N terminal; Type IV pili are bacterial virulence-associated adhesins that promote ...
44-173 1.02e-11

PilS N terminal; Type IV pili are bacterial virulence-associated adhesins that promote bacterial attachment to host cells. In Salmonella typhi, the structural pilin protein PilS interacts with the cystic fibrosis transmembrane conductance regulator. Mutagenesis studies suggest that residues on an alpha-beta loop and the C terminal disulphide-bonded region of PilS might be involved in binding specificity of the pilus.


Pssm-ID: 430227  Cd Length: 138  Bit Score: 59.48  E-value: 1.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489212222   44 SSNANEEQRNISVIAANARALKTSSGYGSSGTNLIpsLIAINGVPKNMSVSSGVVYNVYGGSVTVSS-----TGMGFSIT 118
Cdd:pfam08805   1 LYQASAEQTNITTIQAGTKKLYKGRAGYDGLSNAT--LIAAKVVPTSMTRTGDIYYNRWGGNVSVSPargsgFNNSFTIT 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 489212222  119 TSKLPKDACITLGTKIAKNTFEQTKINSGTAITGE--VTTAAATQACS-SDSNSITWT 173
Cdd:pfam08805  79 YTNVPEGACGDLSTMLSNAGWYSVTIGGTAMVDANvtVTLATATTACDrGDANTVIFT 136
 
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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