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Conserved domains on  [gi|755140978|ref|WP_042491036|]
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MULTISPECIES: TIR domain-containing protein [Bacteria]

Protein Classification

TIR domain-containing protein( domain architecture ID 10556460)

TIR domain-containing protein adopts a flavodoxin fold and may play a role in signal transduction as a phosphorylation-independent conformational switch protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DUF1863 pfam08937
MTH538 TIR-like domain (DUF1863); This domain adopts the flavodoxin fold, that is, five ...
 3-119 3.66e-29

MTH538 TIR-like domain (DUF1863); This domain adopts the flavodoxin fold, that is, five parallel beta-strands and four helical segments. The structure is a three-layer sandwich with alpha-1 and alpha-4 on one side of the beta-sheet, and alpha-2 and alpha-3 on the other side. Probable role in signal transduction as a phosphorylation-independent conformational switch protein. This domain is similar to the TIR domain.


:

Pssm-ID: 430330  Cd Length: 127  Bit Score: 103.64  E-value: 3.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755140978    3 RRVFFSFHFARDAWRVSQVRNAWMLPGS--RDSNTIVDHAS---WEEIMRKG--PQAIQNWIDTQMNGSSVVAVLIGRDT 75
Cdd:pfam08937   1 RKVFISFHHEDDVWRYDKLRNLFANSNDiiGDPNINWGFPDgndHEPIKRRNddSEYIKRWIRDQLNGSSVTIVLVGPET 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 755140978   76 HTRPWVEYEIRKAHREGRGILGVHLAGMK--DSNGTVDPAGADPIA 119
Cdd:pfam08937  81 WSRRWVDWEIAISLKKGKGLLGVRIPGLKrsDLPRGPSALGANAFA 126
 
Name Accession Description Interval E-value
DUF1863 pfam08937
MTH538 TIR-like domain (DUF1863); This domain adopts the flavodoxin fold, that is, five ...
 3-119 3.66e-29

MTH538 TIR-like domain (DUF1863); This domain adopts the flavodoxin fold, that is, five parallel beta-strands and four helical segments. The structure is a three-layer sandwich with alpha-1 and alpha-4 on one side of the beta-sheet, and alpha-2 and alpha-3 on the other side. Probable role in signal transduction as a phosphorylation-independent conformational switch protein. This domain is similar to the TIR domain.


Pssm-ID: 430330  Cd Length: 127  Bit Score: 103.64  E-value: 3.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755140978    3 RRVFFSFHFARDAWRVSQVRNAWMLPGS--RDSNTIVDHAS---WEEIMRKG--PQAIQNWIDTQMNGSSVVAVLIGRDT 75
Cdd:pfam08937   1 RKVFISFHHEDDVWRYDKLRNLFANSNDiiGDPNINWGFPDgndHEPIKRRNddSEYIKRWIRDQLNGSSVTIVLVGPET 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 755140978   76 HTRPWVEYEIRKAHREGRGILGVHLAGMK--DSNGTVDPAGADPIA 119
Cdd:pfam08937  81 WSRRWVDWEIAISLKKGKGLLGVRIPGLKrsDLPRGPSALGANAFA 126
 
Name Accession Description Interval E-value
DUF1863 pfam08937
MTH538 TIR-like domain (DUF1863); This domain adopts the flavodoxin fold, that is, five ...
 3-119 3.66e-29

MTH538 TIR-like domain (DUF1863); This domain adopts the flavodoxin fold, that is, five parallel beta-strands and four helical segments. The structure is a three-layer sandwich with alpha-1 and alpha-4 on one side of the beta-sheet, and alpha-2 and alpha-3 on the other side. Probable role in signal transduction as a phosphorylation-independent conformational switch protein. This domain is similar to the TIR domain.


Pssm-ID: 430330  Cd Length: 127  Bit Score: 103.64  E-value: 3.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755140978    3 RRVFFSFHFARDAWRVSQVRNAWMLPGS--RDSNTIVDHAS---WEEIMRKG--PQAIQNWIDTQMNGSSVVAVLIGRDT 75
Cdd:pfam08937   1 RKVFISFHHEDDVWRYDKLRNLFANSNDiiGDPNINWGFPDgndHEPIKRRNddSEYIKRWIRDQLNGSSVTIVLVGPET 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 755140978   76 HTRPWVEYEIRKAHREGRGILGVHLAGMK--DSNGTVDPAGADPIA 119
Cdd:pfam08937  81 WSRRWVDWEIAISLKKGKGLLGVRIPGLKrsDLPRGPSALGANAFA 126
 
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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