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Conserved domains on  [gi|1194424426|gb|ARR86680|]
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hypothetical protein BSR25_0852 [Lactococcus lactis subsp. lactis bv. diacetylactis]

Protein Classification

glutathione S-transferase; glutathione S-transferase omega family protein( domain architecture ID 10512386)

glutathione S-transferase catalyzes the conjugation of reduced glutathione to a wide range of endogenous and xenobiotic alkylating agents, including carcinogens, therapeutic drugs, environmental toxins and products of oxidative stress| glutathione S-transferase (GST) omega family protein such as class-omega GSTs, which catalyze the GSH dependent reduction of protein disulfides, dehydroascorbate and monomethylarsonate, activities which are more characteristic of glutaredoxins than GSTs

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ArsC pfam03960
ArsC family; This family is related to glutaredoxins pfam00462.
8-117 1.01e-32

ArsC family; This family is related to glutaredoxins pfam00462.


:

Pssm-ID: 427617  Cd Length: 109  Bit Score: 110.77  E-value: 1.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194424426   8 SSSNQSAECVTSWFKKRNIPYVVIS--KTSLCKEDIVRVLELSNKGFEEIIvseSKAPKLYSELrsSCDMDQISTEQMIQ 85
Cdd:pfam03960   3 SPNCSTCRKALAWLEEHGIEYQEIDylETPPSKEELKDILAKLGDGVEALL---NTRGTTYREL--NLDKEDLSEDELLE 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1194424426  86 FILKNQQLLRSPITFDDRRLLIGYNNEDIRTF 117
Cdd:pfam03960  78 LILEHPSLIRRPIVVDGGKLLVGFNEEEIRAF 109
 
Name Accession Description Interval E-value
ArsC pfam03960
ArsC family; This family is related to glutaredoxins pfam00462.
8-117 1.01e-32

ArsC family; This family is related to glutaredoxins pfam00462.


Pssm-ID: 427617  Cd Length: 109  Bit Score: 110.77  E-value: 1.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194424426   8 SSSNQSAECVTSWFKKRNIPYVVIS--KTSLCKEDIVRVLELSNKGFEEIIvseSKAPKLYSELrsSCDMDQISTEQMIQ 85
Cdd:pfam03960   3 SPNCSTCRKALAWLEEHGIEYQEIDylETPPSKEELKDILAKLGDGVEALL---NTRGTTYREL--NLDKEDLSEDELLE 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1194424426  86 FILKNQQLLRSPITFDDRRLLIGYNNEDIRTF 117
Cdd:pfam03960  78 LILEHPSLIRRPIVVDGGKLLVGFNEEEIRAF 109
ArsC_Spx cd03032
Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding ...
1-119 8.82e-27

Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding protein present in bacilli and some mollicutes. It inhibits transcription by binding to the C-terminal domain of the alpha subunit of RNAP, disrupting complex formation between RNAP and certain transcriptional activator proteins like ResD and ComA. In response to oxidative stress, Spx can also activate transcription, making it a general regulator that exerts both positive and negative control over transcription initiation. Spx has been shown to exert redox-sensitive transcriptional control over genes like trxA (TRX) and trxB (TRX reductase), genes that function in thiol homeostasis. This redox-sensitive activity is dependent on the presence of a CXXC motif, present in some members of the Spx subfamily, that acts as a thiol/disulfide switch. Spx has also been shown to repress genes in a sulfate-dependent manner independent of the presence of the CXXC motif.


Pssm-ID: 239330  Cd Length: 115  Bit Score: 95.77  E-value: 8.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194424426   1 MIKIYQKSSSNQSAEcVTSWFKKRNIPYVV--ISKTSLCKEDIVRVLELSNKGFEEIIVSESKAPKlyselRSSCDMDQI 78
Cdd:cd03032     1 MIKLYTSPSCSSCRK-AKQWLEEHQIPFEErnLFKQPLTKEELKEILSLTENGVEDIISTRSKAFK-----NLNIDIDEL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1194424426  79 STEQMIQFILKNQQLLRSPITFDDRRLLIGYNNEDIRTFIP 119
Cdd:cd03032    75 SLSELIRLISEHPSLLRRPIIIDEKRLQIGYNEDEIRQFLP 115
spxA PRK13344
transcriptional regulator Spx; Reviewed
1-123 2.75e-20

transcriptional regulator Spx; Reviewed


Pssm-ID: 183988  Cd Length: 132  Bit Score: 79.62  E-value: 2.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194424426   1 MIKIYQKSSSNqSAECVTSWFKKRNIPYVV--ISKTSLCKEDIVRVLELSNKGFEEIIVSESKAPKLYSelrssCDMDQI 78
Cdd:PRK13344    1 MIKIYTISSCT-SCKKAKTWLNAHQLSYKEqnLGKEPLTKEEILAILTKTENGIESIVSSKNRYAKALD-----CDIEEL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1194424426  79 STEQMIQFILKNQQLLRSPITFDDRRLLIGYNNEDIRTFIPWRLR 123
Cdd:PRK13344   75 SVNEVIDLIQENPRILKSPILIDDKRLQVGYKEDDIRAFLPRSIR 119
ArsC COG1393
Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and ...
1-119 6.87e-14

Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and metabolism];


Pssm-ID: 441003  Cd Length: 115  Bit Score: 62.80  E-value: 6.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194424426   1 MIKIYQKSSsnqsaeCVTS-----WFKKRNIPYVVIS--KTSLCKEDIVRVLELSNKGFEEIIvseSKAPKLYSELrsSC 73
Cdd:COG1393     1 MITIYGNPN------CSTSrkalaWLEEAGIEYEFIDylKTPPTAEELKELLAKLGLGVEELL---NTRGTTYREL--GL 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1194424426  74 DMDQISTEQMIQFILKNQQLLRSPITFDDRRLLIGYNNEDIRTFIP 119
Cdd:COG1393    70 KDKALSEEEALALMLEHPSLIKRPIVVTGDKALVGFPPEEVLALLG 115
 
Name Accession Description Interval E-value
ArsC pfam03960
ArsC family; This family is related to glutaredoxins pfam00462.
8-117 1.01e-32

ArsC family; This family is related to glutaredoxins pfam00462.


Pssm-ID: 427617  Cd Length: 109  Bit Score: 110.77  E-value: 1.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194424426   8 SSSNQSAECVTSWFKKRNIPYVVIS--KTSLCKEDIVRVLELSNKGFEEIIvseSKAPKLYSELrsSCDMDQISTEQMIQ 85
Cdd:pfam03960   3 SPNCSTCRKALAWLEEHGIEYQEIDylETPPSKEELKDILAKLGDGVEALL---NTRGTTYREL--NLDKEDLSEDELLE 77
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1194424426  86 FILKNQQLLRSPITFDDRRLLIGYNNEDIRTF 117
Cdd:pfam03960  78 LILEHPSLIRRPIVVDGGKLLVGFNEEEIRAF 109
ArsC_Spx cd03032
Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding ...
1-119 8.82e-27

Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding protein present in bacilli and some mollicutes. It inhibits transcription by binding to the C-terminal domain of the alpha subunit of RNAP, disrupting complex formation between RNAP and certain transcriptional activator proteins like ResD and ComA. In response to oxidative stress, Spx can also activate transcription, making it a general regulator that exerts both positive and negative control over transcription initiation. Spx has been shown to exert redox-sensitive transcriptional control over genes like trxA (TRX) and trxB (TRX reductase), genes that function in thiol homeostasis. This redox-sensitive activity is dependent on the presence of a CXXC motif, present in some members of the Spx subfamily, that acts as a thiol/disulfide switch. Spx has also been shown to repress genes in a sulfate-dependent manner independent of the presence of the CXXC motif.


Pssm-ID: 239330  Cd Length: 115  Bit Score: 95.77  E-value: 8.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194424426   1 MIKIYQKSSSNQSAEcVTSWFKKRNIPYVV--ISKTSLCKEDIVRVLELSNKGFEEIIVSESKAPKlyselRSSCDMDQI 78
Cdd:cd03032     1 MIKLYTSPSCSSCRK-AKQWLEEHQIPFEErnLFKQPLTKEELKEILSLTENGVEDIISTRSKAFK-----NLNIDIDEL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1194424426  79 STEQMIQFILKNQQLLRSPITFDDRRLLIGYNNEDIRTFIP 119
Cdd:cd03032    75 SLSELIRLISEHPSLLRRPIIIDEKRLQIGYNEDEIRQFLP 115
spxA PRK13344
transcriptional regulator Spx; Reviewed
1-123 2.75e-20

transcriptional regulator Spx; Reviewed


Pssm-ID: 183988  Cd Length: 132  Bit Score: 79.62  E-value: 2.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194424426   1 MIKIYQKSSSNqSAECVTSWFKKRNIPYVV--ISKTSLCKEDIVRVLELSNKGFEEIIVSESKAPKLYSelrssCDMDQI 78
Cdd:PRK13344    1 MIKIYTISSCT-SCKKAKTWLNAHQLSYKEqnLGKEPLTKEEILAILTKTENGIESIVSSKNRYAKALD-----CDIEEL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1194424426  79 STEQMIQFILKNQQLLRSPITFDDRRLLIGYNNEDIRTFIPWRLR 123
Cdd:PRK13344   75 SVNEVIDLIQENPRILKSPILIDDKRLQVGYKEDDIRAFLPRSIR 119
spxA PRK01655
transcriptional regulator Spx; Reviewed
1-123 1.24e-18

transcriptional regulator Spx; Reviewed


Pssm-ID: 179316  Cd Length: 131  Bit Score: 75.49  E-value: 1.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194424426   1 MIKIYQkSSSNQSAECVTSWFKKRNIPYVV--ISKTSLCKEDIVRVLELSNKGFEEIIVSESKapkLYSELrsSCDMDQI 78
Cdd:PRK01655    1 MVTLFT-SPSCTSCRKAKAWLEEHDIPFTErnIFSSPLTIDEIKQILRMTEDGTDEIISTRSK---VFQKL--NVDVESL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1194424426  79 STEQMIQFILKNQQLLRSPITFDDRRLLIGYNNEDIRTFIPWRLR 123
Cdd:PRK01655   75 SLQDLIKLISDNPGLLRRPIIIDEKRLQVGYNEDEIRAFLPRKVR 119
ArsC COG1393
Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and ...
1-119 6.87e-14

Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and metabolism];


Pssm-ID: 441003  Cd Length: 115  Bit Score: 62.80  E-value: 6.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194424426   1 MIKIYQKSSsnqsaeCVTS-----WFKKRNIPYVVIS--KTSLCKEDIVRVLELSNKGFEEIIvseSKAPKLYSELrsSC 73
Cdd:COG1393     1 MITIYGNPN------CSTSrkalaWLEEAGIEYEFIDylKTPPTAEELKELLAKLGLGVEELL---NTRGTTYREL--GL 69
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1194424426  74 DMDQISTEQMIQFILKNQQLLRSPITFDDRRLLIGYNNEDIRTFIP 119
Cdd:COG1393    70 KDKALSEEEALALMLEHPSLIKRPIVVTGDKALVGFPPEEVLALLG 115
ArsC_family cd02977
Arsenate Reductase (ArsC) family; composed of TRX-fold arsenic reductases and similar proteins ...
2-109 1.21e-12

Arsenate Reductase (ArsC) family; composed of TRX-fold arsenic reductases and similar proteins including the transcriptional regulator, Spx. ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from glutathione (GSH) via glutaredoxin (GRX), through a single catalytic cysteine. This family of predominantly bacterial enzymes is unrelated to two other families of arsenate reductases which show similarity to low-molecular-weight acid phosphatases and phosphotyrosyl phosphatases. Spx is a general regulator that exerts negative and positive control over transcription initiation by binding to the C-terminal domain of the alpha subunit of RNA polymerase.


Pssm-ID: 239275  Cd Length: 105  Bit Score: 59.43  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194424426   2 IKIYQKSSsnqsaeCVTS-----WFKKRNIPYVVI--SKTSLCKEDIVRVLELSNKGFEEIIvseSKAPKLYSELrSSCD 74
Cdd:cd02977     1 ITIYGNPN------CSTSrkalaWLEEHGIEYEFIdyLKEPPTKEELKELLAKLGLGVEDLF---NTRGTPYRKL-GLAD 70
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1194424426  75 MDQISTEQMIQFILKNQQLLRSPITFDDRRLLIGY 109
Cdd:cd02977    71 KDELSDEEALELMAEHPKLIKRPIVVDGDRLLVGF 105
PRK12559 PRK12559
transcriptional regulator Spx; Provisional
1-123 4.96e-11

transcriptional regulator Spx; Provisional


Pssm-ID: 79035  Cd Length: 131  Bit Score: 55.88  E-value: 4.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1194424426   1 MIKIYQKSSSNqSAECVTSWFKKRNIPYVV--ISKTSLCKEDIVRVLELSNKGFEEIIVSESKApklYSELrsSCDMDQI 78
Cdd:PRK12559    1 MVVLYTTASCA-SCRKAKAWLEENQIDYTEknIVSNSMTVDELKSILRLTEEGATEIISTRSKT---FQDL--NINIEEL 74
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1194424426  79 STEQMIQFILKNQQLLRSPITFDDRRLLIGYNNEDIRTFIPWRLR 123
Cdd:PRK12559   75 SLNEFYKLIIEHPLMLRRPIMLDEKRLQIGFNDEEIRKFLPRSVR 119
 
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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