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Conserved domains on  [gi|616687512|gb|KAE85158|]
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UPF0403 protein [Staphylococcus aureus VET0402R]

Protein Classification

BrxA/BrxB family bacilliredoxin( domain architecture ID 10534661)

BrxA/BrxB family bacilliredoxin which may catalyze the removal of bacillithiol that becomes linked to protein thiols under oxidative stress; may participate in a complex catalyzing the removal of S-thioallylations from proteins caused by allicin stress

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Disulph_isomer pfam06491
Disulphide isomerase; This family of proteins has disulphide isomerase activity, EC:5.3.4.1. ...
 7-144 2.49e-74

Disulphide isomerase; This family of proteins has disulphide isomerase activity, EC:5.3.4.1. It has a similar fold to thioredoxin, with an alpha-beta-alpha-beta-alpha-beta-beta-alpha topology. It has a conserved CGC motif in the loop immediately downstream of the first beta strand. This motif is essential for activity.


:

Pssm-ID: 428976  Cd Length: 136  Bit Score: 217.78  E-value: 2.49e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687512    7 YMKEIAQQMRGELTQNGFTSLETSEAVSEYMNQvnADDTTFVVINSTCGCAAGLARPAAVAvATQNEHRPTNTVTVFAGQ 86
Cdd:pfam06491   1 YPEELVQPMREELTRAGFEELTTAEEVDEALAK--AKGTTLVVVNSVCGCAAGIARPAVAM-ALEHDKKPDHLVTVFAGQ 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 616687512   87 DKEATATMRE-FIQQVPSSPSYALFKGRDLVYFMPREFIEGRDINDIAMDLKDAFDENC 144
Cdd:pfam06491  78 DKEATAKAREyFLGYPPSSPSIALFKDGELVHFIERHHIEGRPAEEIAENLKAAFDEYC 136
 
Name Accession Description Interval E-value
Disulph_isomer pfam06491
Disulphide isomerase; This family of proteins has disulphide isomerase activity, EC:5.3.4.1. ...
 7-144 2.49e-74

Disulphide isomerase; This family of proteins has disulphide isomerase activity, EC:5.3.4.1. It has a similar fold to thioredoxin, with an alpha-beta-alpha-beta-alpha-beta-beta-alpha topology. It has a conserved CGC motif in the loop immediately downstream of the first beta strand. This motif is essential for activity.


Pssm-ID: 428976  Cd Length: 136  Bit Score: 217.78  E-value: 2.49e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687512    7 YMKEIAQQMRGELTQNGFTSLETSEAVSEYMNQvnADDTTFVVINSTCGCAAGLARPAAVAvATQNEHRPTNTVTVFAGQ 86
Cdd:pfam06491   1 YPEELVQPMREELTRAGFEELTTAEEVDEALAK--AKGTTLVVVNSVCGCAAGIARPAVAM-ALEHDKKPDHLVTVFAGQ 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 616687512   87 DKEATATMRE-FIQQVPSSPSYALFKGRDLVYFMPREFIEGRDINDIAMDLKDAFDENC 144
Cdd:pfam06491  78 DKEATAKAREyFLGYPPSSPSIALFKDGELVHFIERHHIEGRPAEEIAENLKAAFDEYC 136
YphP_YqiW TIGR04191
putative bacilliredoxin, YphP/YqiW family; This protein family is one of several observed in ...
 7-144 3.35e-74

putative bacilliredoxin, YphP/YqiW family; This protein family is one of several observed in species that express bacillithiol, an analog of glutathione and mycothiol. Rather than being involved in bacillithiol biosynthesis, members are likely to act in bacillithiol-dependent processes. A suggested term is bacilliredoxin (a glutaredoxin-like thiol-dependent oxidoreductase), and a suggested role of YphP is de-bacillithiolation - removing bacillithiol that became linked to protein thiols under oxidative stress. An older description of YphP as a disulphide isomerase therefore may be wrong.


Pssm-ID: 275043  Cd Length: 136  Bit Score: 217.48  E-value: 3.35e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687512    7 YMKEIAQQMRGELTQNGFTSLETSEAVSEYMNqvNADDTTFVVINSTCGCAAGLARPAaVAVATQNEHRPTNTVTVFAGQ 86
Cdd:TIGR04191   1 YPEELVQPMREELTRAGFEELTTAEDVDEAME--NAEGTTLVVVNSVCGCAAGLARPA-VAQALQNDKKPDHLVTVFAGQ 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 616687512   87 DKEATATMRE-FIQQVPSSPSYALFKGRDLVYFMPREFIEGRDINDIAMDLKDAFDENC 144
Cdd:TIGR04191  78 DKEATAKAREyFLGYPPSSPSIALFKDGELVHFIERHHIEGRSAEEIAADLQAAFDEYC 136
 
Name Accession Description Interval E-value
Disulph_isomer pfam06491
Disulphide isomerase; This family of proteins has disulphide isomerase activity, EC:5.3.4.1. ...
 7-144 2.49e-74

Disulphide isomerase; This family of proteins has disulphide isomerase activity, EC:5.3.4.1. It has a similar fold to thioredoxin, with an alpha-beta-alpha-beta-alpha-beta-beta-alpha topology. It has a conserved CGC motif in the loop immediately downstream of the first beta strand. This motif is essential for activity.


Pssm-ID: 428976  Cd Length: 136  Bit Score: 217.78  E-value: 2.49e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687512    7 YMKEIAQQMRGELTQNGFTSLETSEAVSEYMNQvnADDTTFVVINSTCGCAAGLARPAAVAvATQNEHRPTNTVTVFAGQ 86
Cdd:pfam06491   1 YPEELVQPMREELTRAGFEELTTAEEVDEALAK--AKGTTLVVVNSVCGCAAGIARPAVAM-ALEHDKKPDHLVTVFAGQ 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 616687512   87 DKEATATMRE-FIQQVPSSPSYALFKGRDLVYFMPREFIEGRDINDIAMDLKDAFDENC 144
Cdd:pfam06491  78 DKEATAKAREyFLGYPPSSPSIALFKDGELVHFIERHHIEGRPAEEIAENLKAAFDEYC 136
YphP_YqiW TIGR04191
putative bacilliredoxin, YphP/YqiW family; This protein family is one of several observed in ...
 7-144 3.35e-74

putative bacilliredoxin, YphP/YqiW family; This protein family is one of several observed in species that express bacillithiol, an analog of glutathione and mycothiol. Rather than being involved in bacillithiol biosynthesis, members are likely to act in bacillithiol-dependent processes. A suggested term is bacilliredoxin (a glutaredoxin-like thiol-dependent oxidoreductase), and a suggested role of YphP is de-bacillithiolation - removing bacillithiol that became linked to protein thiols under oxidative stress. An older description of YphP as a disulphide isomerase therefore may be wrong.


Pssm-ID: 275043  Cd Length: 136  Bit Score: 217.48  E-value: 3.35e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 616687512    7 YMKEIAQQMRGELTQNGFTSLETSEAVSEYMNqvNADDTTFVVINSTCGCAAGLARPAaVAVATQNEHRPTNTVTVFAGQ 86
Cdd:TIGR04191   1 YPEELVQPMREELTRAGFEELTTAEDVDEAME--NAEGTTLVVVNSVCGCAAGLARPA-VAQALQNDKKPDHLVTVFAGQ 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 616687512   87 DKEATATMRE-FIQQVPSSPSYALFKGRDLVYFMPREFIEGRDINDIAMDLKDAFDENC 144
Cdd:TIGR04191  78 DKEATAKAREyFLGYPPSSPSIALFKDGELVHFIERHHIEGRSAEEIAADLQAAFDEYC 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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