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Conserved domains on  [gi|446740407|ref|WP_000817663|]
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MULTISPECIES: MarR family winged helix-turn-helix transcriptional regulator [Bacillus]

Protein Classification

MarR family winged helix-turn-helix transcriptional regulator( domain architecture ID 11448790)

MarR family winged helix-turn-helix (wHTH) transcriptional regulator similar to Bacillus thuringiensis DNA-binding transcriptional repressor TubR, a DNA-binding protein that is part of the type III plasmid partition system used to ensure correct segregation of the pBtoxis plasmid

Gene Ontology:  GO:0006355|GO:0003700
PubMed:  10498949|28670937
SCOP:  4000246

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
37-142 6.15e-20

DNA-binding transcriptional regulator, MarR family [Transcription];


:

Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 80.01  E-value: 6.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446740407  37 LPTSQMMALEEL-EVEKLTVWQLSNKLRLETSTVSRLVDKLVKKGLIYREVNEKNRRELFLHLTEKGHITVNCLREQSIT 115
Cdd:COG1846   36 LTPAQFRVLAALaEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGRALLEEARPALEA 115

                         90       100
                 ....*....|....*....|....*..
gi 446740407 116 FYQSILNNLSESEQKIVVDGFELFINS 142
Cdd:COG1846  116 LLAELLAGLSEEELEALLRLLRRLAEN 142
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
37-142 6.15e-20

DNA-binding transcriptional regulator, MarR family [Transcription];


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 80.01  E-value: 6.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446740407  37 LPTSQMMALEEL-EVEKLTVWQLSNKLRLETSTVSRLVDKLVKKGLIYREVNEKNRRELFLHLTEKGHITVNCLREQSIT 115
Cdd:COG1846   36 LTPAQFRVLAALaEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGRALLEEARPALEA 115

                         90       100
                 ....*....|....*....|....*..
gi 446740407 116 FYQSILNNLSESEQKIVVDGFELFINS 142
Cdd:COG1846  116 LLAELLAGLSEEELEALLRLLRRLAEN 142
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
34-129 2.13e-17

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 72.24  E-value: 2.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446740407    34 EKPLPTSQMMALEELEVEK-LTVWQLSNKLRLETSTVSRLVDKLVKKGLIYREVNEKNRRELFLHLTEKGHITVNCLREQ 112
Cdd:smart00347   5 PLGLTPTQFLVLRILYEEGpLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLLEA 84

                           90
                   ....*....|....*..
gi 446740407   113 SITFYQSILNNLSESEQ 129
Cdd:smart00347  85 RSETLAELLAGLTAEEQ 101
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 37-93 2.06e-10

MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.


Pssm-ID: 432797 [Multi-domain]  Cd Length: 60  Bit Score: 52.98  E-value: 2.06e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446740407   37 LPTSQMMALEEL-EVEKLTVWQLSNKLRLETSTVSRLVDKLVKKGLIYREVNEKNRRE 93
Cdd:pfam12802   3 LTPAQFRVLLALaRNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRRA 60
PRK10870 PRK10870
transcriptional repressor MprA; Provisional
 42-130 5.83e-05

transcriptional repressor MprA; Provisional


Pssm-ID: 182795  Cd Length: 176  Bit Score: 40.89  E-value: 5.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446740407  42 MMALEELEVEKLTVWQLSNKLRLETSTVSRLVDKLVKKGLIYREVNEKNRRELFLHLTEKGHITVNCLREQSITFYQSIL 121
Cdd:PRK10870  61 LITLESQENHSIQPSELSCALGSSRTNATRIADELEKRGWIERRESDNDRRCLHLQLTEKGHEFLREVLPPQHNCLHQLW 140


                 ....*....
gi 446740407 122 NNLSESEQK 130
Cdd:PRK10870 141 SALSTTEKD 149
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 45-104 1.04e-03

Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions.


Pssm-ID: 238042 [Multi-domain]  Cd Length: 78  Bit Score: 35.74  E-value: 1.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446740407  45 LEELEVEKLTVWQLSNKLRLETSTVSRLVDKLVKKGLIYRevnEKNRRELFLHLTEKGHI 104
Cdd:cd00090   13 LRLLLEGPLTVSELAERLGLSQSTVSRHLKKLEEAGLVES---RREGRRVYYSLTDAERL 69
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
37-142 6.15e-20

DNA-binding transcriptional regulator, MarR family [Transcription];


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 80.01  E-value: 6.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446740407  37 LPTSQMMALEEL-EVEKLTVWQLSNKLRLETSTVSRLVDKLVKKGLIYREVNEKNRRELFLHLTEKGHITVNCLREQSIT 115
Cdd:COG1846   36 LTPAQFRVLAALaEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGRALLEEARPALEA 115

                         90       100
                 ....*....|....*....|....*..
gi 446740407 116 FYQSILNNLSESEQKIVVDGFELFINS 142
Cdd:COG1846  116 LLAELLAGLSEEELEALLRLLRRLAEN 142
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
34-129 2.13e-17

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 72.24  E-value: 2.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446740407    34 EKPLPTSQMMALEELEVEK-LTVWQLSNKLRLETSTVSRLVDKLVKKGLIYREVNEKNRRELFLHLTEKGHITVNCLREQ 112
Cdd:smart00347   5 PLGLTPTQFLVLRILYEEGpLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLLEA 84

                           90
                   ....*....|....*..
gi 446740407   113 SITFYQSILNNLSESEQ 129
Cdd:smart00347  85 RSETLAELLAGLTAEEQ 101
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 37-93 2.06e-10

MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.


Pssm-ID: 432797 [Multi-domain]  Cd Length: 60  Bit Score: 52.98  E-value: 2.06e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446740407   37 LPTSQMMALEEL-EVEKLTVWQLSNKLRLETSTVSRLVDKLVKKGLIYREVNEKNRRE 93
Cdd:pfam12802   3 LTPAQFRVLLALaRNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRRA 60
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 40-93 1.34e-07

MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.


Pssm-ID: 426012 [Multi-domain]  Cd Length: 59  Bit Score: 45.62  E-value: 1.34e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446740407   40 SQMMALEEL-EVEKLTVWQLSNKLRLETSTVSRLVDKLVKKGLIYREVNEKNRRE 93
Cdd:pfam01047   4 TQFHILRILyEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRRE 58
HTH_27 pfam13463
Winged helix DNA-binding domain;
57-102 2.58e-05

Winged helix DNA-binding domain;


Pssm-ID: 433228 [Multi-domain]  Cd Length: 68  Bit Score: 39.96  E-value: 2.58e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 446740407   57 QLSNKLRLETSTVSRLVDKLVKKGLIYREVNEKNRRELFLHLTEKG 102
Cdd:pfam13463  23 DICFRLNVEDSHVSYSLKKLTEAGLVEREGSEEDGRETRVRLTAKG 68
PRK10870 PRK10870
transcriptional repressor MprA; Provisional
 42-130 5.83e-05

transcriptional repressor MprA; Provisional


Pssm-ID: 182795  Cd Length: 176  Bit Score: 40.89  E-value: 5.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446740407  42 MMALEELEVEKLTVWQLSNKLRLETSTVSRLVDKLVKKGLIYREVNEKNRRELFLHLTEKGHITVNCLREQSITFYQSIL 121
Cdd:PRK10870  61 LITLESQENHSIQPSELSCALGSSRTNATRIADELEKRGWIERRESDNDRRCLHLQLTEKGHEFLREVLPPQHNCLHQLW 140


                 ....*....
gi 446740407 122 NNLSESEQK 130
Cdd:PRK10870 141 SALSTTEKD 149
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 45-104 1.04e-03

Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric repressors. ARSR subfamily of helix-turn-helix bacterial transcription regulatory proteins (winged helix topology). Includes several proteins that appear to dissociate from DNA in the presence of metal ions.


Pssm-ID: 238042 [Multi-domain]  Cd Length: 78  Bit Score: 35.74  E-value: 1.04e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446740407  45 LEELEVEKLTVWQLSNKLRLETSTVSRLVDKLVKKGLIYRevnEKNRRELFLHLTEKGHI 104
Cdd:cd00090   13 LRLLLEGPLTVSELAERLGLSQSTVSRHLKKLEEAGLVES---RREGRRVYYSLTDAERL 69
COG3355 COG3355
Predicted transcriptional regulator [Transcription];
51-88 1.11e-03

Predicted transcriptional regulator [Transcription];


Pssm-ID: 442583 [Multi-domain]  Cd Length: 131  Bit Score: 36.87  E-value: 1.11e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 446740407  51 EKLTVWQLSNKLRLETSTVSRLVDKLVKKGLIYREVNE 88
Cdd:COG3355   41 EPLTVEELAEALDRSRSTVYRSLQKLLEAGLVEREKRN 78
PRK11512 PRK11512
multiple antibiotic resistance transcriptional regulator MarR;
53-128 3.78e-03

multiple antibiotic resistance transcriptional regulator MarR;


Pssm-ID: 183170  Cd Length: 144  Bit Score: 35.64  E-value: 3.78e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446740407  53 LTVWQLSNKLRLETSTVSRLVDKLVKKGLIYREVNEKNRRELFLHLTEKGH-ITVNCLREQSITFYQSILNNLSESE 128
Cdd:PRK11512  55 ITPVELKKVLSVDLGALTRMLDRLVCKGWVERLPNPNDKRGVLVKLTTSGAaICEQCHQLVGQDLHQELTKNLTADE 131
 
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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