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Conserved domains on  [gi|2077967308|ref|WP_220186090|]
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MULTISPECIES: molecular chaperone [Citrobacter]

Protein Classification

molecular chaperone( domain architecture ID 1001023)

molecular chaperone belonging to the periplasmic pilus chaperone family may be involved in fimbrial biogenesis, similar to Escherichia coli protein FasC and Yersinia pestis chaperone protein caf1M

Gene Ontology:  GO:0061077
SCOP:  4002248|4007561

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FimC super family cl34557
P pilus assembly protein, chaperone PapD [Extracellular structures];
1-183 1.54e-06

P pilus assembly protein, chaperone PapD [Extracellular structures];


The actual alignment was detected with superfamily member COG3121:

Pssm-ID: 442355 [Multi-domain]  Cd Length: 237  Bit Score: 47.29  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077967308   1 MLMVFPVHA-VYLESTIYEMPADKSFISKRIYNDSDKQNVYSISAVKIDKPGPGGEKRSPiadgeLLFTPLNFSLAPESG 79
Cdd:COG3121    15 LLASAAAAAgISISPTRVIYPAGDKEASLTLTNTGDTPYLVQSWVDDWDQDAGPDKATAP-----FVVTPPLFRLEPGKS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077967308  80 EFFKIFYRG---PADeTERYYRILFRELPvtlltDREHGKKSEAIPAVAIDTI--LVVRPRKI---------NFQYHLDE 145
Cdd:COG3121    90 QTVRIIRTGpplPQD-RESLFRLNVDEIP-----PKDASEEGKNTLQIALRTRikLFYRPAGLkgspedaaeKLTWSLVG 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2077967308 146 QRGILRNTGN---TFFKIILHQGCHSTDDEAEMryLLPGET 183
Cdd:COG3121   164 NGLTVTNPGPyyvTLSDLSLGAGGKKLKKGLGM--VLPGST 202
 
Name Accession Description Interval E-value
FimC COG3121
P pilus assembly protein, chaperone PapD [Extracellular structures];
1-183 1.54e-06

P pilus assembly protein, chaperone PapD [Extracellular structures];


Pssm-ID: 442355 [Multi-domain]  Cd Length: 237  Bit Score: 47.29  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077967308   1 MLMVFPVHA-VYLESTIYEMPADKSFISKRIYNDSDKQNVYSISAVKIDKPGPGGEKRSPiadgeLLFTPLNFSLAPESG 79
Cdd:COG3121    15 LLASAAAAAgISISPTRVIYPAGDKEASLTLTNTGDTPYLVQSWVDDWDQDAGPDKATAP-----FVVTPPLFRLEPGKS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077967308  80 EFFKIFYRG---PADeTERYYRILFRELPvtlltDREHGKKSEAIPAVAIDTI--LVVRPRKI---------NFQYHLDE 145
Cdd:COG3121    90 QTVRIIRTGpplPQD-RESLFRLNVDEIP-----PKDASEEGKNTLQIALRTRikLFYRPAGLkgspedaaeKLTWSLVG 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2077967308 146 QRGILRNTGN---TFFKIILHQGCHSTDDEAEMryLLPGET 183
Cdd:COG3121   164 NGLTVTNPGPyyvTLSDLSLGAGGKKLKKGLGM--VLPGST 202
 
Name Accession Description Interval E-value
FimC COG3121
P pilus assembly protein, chaperone PapD [Extracellular structures];
1-183 1.54e-06

P pilus assembly protein, chaperone PapD [Extracellular structures];


Pssm-ID: 442355 [Multi-domain]  Cd Length: 237  Bit Score: 47.29  E-value: 1.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077967308   1 MLMVFPVHA-VYLESTIYEMPADKSFISKRIYNDSDKQNVYSISAVKIDKPGPGGEKRSPiadgeLLFTPLNFSLAPESG 79
Cdd:COG3121    15 LLASAAAAAgISISPTRVIYPAGDKEASLTLTNTGDTPYLVQSWVDDWDQDAGPDKATAP-----FVVTPPLFRLEPGKS 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2077967308  80 EFFKIFYRG---PADeTERYYRILFRELPvtlltDREHGKKSEAIPAVAIDTI--LVVRPRKI---------NFQYHLDE 145
Cdd:COG3121    90 QTVRIIRTGpplPQD-RESLFRLNVDEIP-----PKDASEEGKNTLQIALRTRikLFYRPAGLkgspedaaeKLTWSLVG 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2077967308 146 QRGILRNTGN---TFFKIILHQGCHSTDDEAEMryLLPGET 183
Cdd:COG3121   164 NGLTVTNPGPyyvTLSDLSLGAGGKKLKKGLGM--VLPGST 202
 
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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