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Conserved domains on  [gi|1431010741|ref|WP_113996097|]
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MULTISPECIES: IrmA family protein [Aeromonas]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IrmA super family cl39990
interleukin receptor mimic protein A; The E. coli interleukin [IL] receptor mimic protein A ...
 28-132 3.82e-29

interleukin receptor mimic protein A; The E. coli interleukin [IL] receptor mimic protein A (IrmA), is a small (13 kDa) Uropathogenic E. coli (UPEC) protein that was originally identified in a large reverse genetic screen as a broadly protective vaccine antigen. It has a fibronectin III (FNIII)-like fold that forms a domain-swapped dimer with structural mimicry to the binding domain of the IL-2 receptor (IL-2R), the IL-4 receptor (IL-4R) and, to a lesser extent, the IL-10 receptor (IL-10R). IrmA binds to all three cytokines, with the greatest affinity observed for IL-4. It is suggested that IrmA may contribute to manipulation of the innate immune response during UPEC infection.


The actual alignment was detected with superfamily member pfam18673:

Pssm-ID: 436657  Cd Length: 109  Bit Score: 102.47  E-value: 3.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431010741  28 LSIQHTDTVYANQGVCAYHFSLDSGGADE-FGRLYITLQFNDKKG-KALAESTLEVEPFGGSSATRYGGGFTEVDCGQVE 105
Cdd:pfam18673   1 IQIRHSDTVFANGGICAANFRFDNGGSGEgFGPLAVHIQLKDKAGnKLLAEDTIDVADFGNSDADRTAEAFLEHECACDE 80

                          90       100
                  ....*....|....*....|....*..
gi 1431010741 106 QAKSIAIIQATEVFAHNQVTrLPISTF 132
Cdd:pfam18673  81 NLSAVEIIGATAEMNGEQSD-LLAKDF 106
 
Name Accession Description Interval E-value
IrmA pfam18673
interleukin receptor mimic protein A; The E. coli interleukin [IL] receptor mimic protein A ...
 28-132 3.82e-29

interleukin receptor mimic protein A; The E. coli interleukin [IL] receptor mimic protein A (IrmA), is a small (13 kDa) Uropathogenic E. coli (UPEC) protein that was originally identified in a large reverse genetic screen as a broadly protective vaccine antigen. It has a fibronectin III (FNIII)-like fold that forms a domain-swapped dimer with structural mimicry to the binding domain of the IL-2 receptor (IL-2R), the IL-4 receptor (IL-4R) and, to a lesser extent, the IL-10 receptor (IL-10R). IrmA binds to all three cytokines, with the greatest affinity observed for IL-4. It is suggested that IrmA may contribute to manipulation of the innate immune response during UPEC infection.


Pssm-ID: 436657  Cd Length: 109  Bit Score: 102.47  E-value: 3.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431010741  28 LSIQHTDTVYANQGVCAYHFSLDSGGADE-FGRLYITLQFNDKKG-KALAESTLEVEPFGGSSATRYGGGFTEVDCGQVE 105
Cdd:pfam18673   1 IQIRHSDTVFANGGICAANFRFDNGGSGEgFGPLAVHIQLKDKAGnKLLAEDTIDVADFGNSDADRTAEAFLEHECACDE 80

                          90       100
                  ....*....|....*....|....*..
gi 1431010741 106 QAKSIAIIQATEVFAHNQVTrLPISTF 132
Cdd:pfam18673  81 NLSAVEIIGATAEMNGEQSD-LLAKDF 106
 
Name Accession Description Interval E-value
IrmA pfam18673
interleukin receptor mimic protein A; The E. coli interleukin [IL] receptor mimic protein A ...
 28-132 3.82e-29

interleukin receptor mimic protein A; The E. coli interleukin [IL] receptor mimic protein A (IrmA), is a small (13 kDa) Uropathogenic E. coli (UPEC) protein that was originally identified in a large reverse genetic screen as a broadly protective vaccine antigen. It has a fibronectin III (FNIII)-like fold that forms a domain-swapped dimer with structural mimicry to the binding domain of the IL-2 receptor (IL-2R), the IL-4 receptor (IL-4R) and, to a lesser extent, the IL-10 receptor (IL-10R). IrmA binds to all three cytokines, with the greatest affinity observed for IL-4. It is suggested that IrmA may contribute to manipulation of the innate immune response during UPEC infection.


Pssm-ID: 436657  Cd Length: 109  Bit Score: 102.47  E-value: 3.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1431010741  28 LSIQHTDTVYANQGVCAYHFSLDSGGADE-FGRLYITLQFNDKKG-KALAESTLEVEPFGGSSATRYGGGFTEVDCGQVE 105
Cdd:pfam18673   1 IQIRHSDTVFANGGICAANFRFDNGGSGEgFGPLAVHIQLKDKAGnKLLAEDTIDVADFGNSDADRTAEAFLEHECACDE 80

                          90       100
                  ....*....|....*....|....*..
gi 1431010741 106 QAKSIAIIQATEVFAHNQVTrLPISTF 132
Cdd:pfam18673  81 NLSAVEIIGATAEMNGEQSD-LLAKDF 106
 
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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