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Conserved domains on  [gi|446114037|ref|WP_000191892|]
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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];
1-126 4.55e-23

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


:

Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 88.49  E-value: 4.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446114037   1 MTQHKEEQMNEALALFYFAYKTFTEKPDEIIKEYGIQRVHHRILFFIARFPGISVNELLSLLEISKQALHGPLRQLVEKG 80
Cdd:COG1846    1 MSDEPDPAEERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446114037  81 LIESNEATHDRRVKQLSLTEEGTDLEKKLSDVQRKQMGAIFSKFGE 126
Cdd:COG1846   81 LVEREPDPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSE 126
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
1-126 4.55e-23

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 88.49  E-value: 4.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446114037   1 MTQHKEEQMNEALALFYFAYKTFTEKPDEIIKEYGIQRVHHRILFFIARFPGISVNELLSLLEISKQALHGPLRQLVEKG 80
Cdd:COG1846    1 MSDEPDPAEERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446114037  81 LIESNEATHDRRVKQLSLTEEGTDLEKKLSDVQRKQMGAIFSKFGE 126
Cdd:COG1846   81 LVEREPDPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSE 126
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
29-126 1.01e-16

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 71.09  E-value: 1.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446114037    29 EIIKEYGIQRVHHRILFFIARFPGISVNELLSLLEISKQALHGPLRQLVEKGLIESNEATHDRRVKQLSLTEEGTDLEKK 108
Cdd:smart00347   1 EELKPLGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQ 80

                           90
                   ....*....|....*...
gi 446114037   109 LSDVQRKQMGAIFSKFGE 126
Cdd:smart00347  81 LLEARSETLAELLAGLTA 98
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 34-92 1.93e-16

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: 69.15  E-value: 1.93e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446114037   34 YGIQRVHHRILFFIARFPGISVNELLSLLEISKQALHGPLRQLVEKGLIESNEATHDRR 92
Cdd:pfam12802   1 LGLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRR 59
PRK03573 PRK03573
transcriptional regulator SlyA; Provisional
 73-130 3.34e-06

transcriptional regulator SlyA; Provisional


Pssm-ID: 179596  Cd Length: 144  Bit Score: 44.22  E-value: 3.34e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446114037  73 LRQLVEKGLIESNEATHDRRVKQLSLTEEGTDLEKKLSDVQRKQMGAIFSkfGESCEE 130
Cdd:PRK03573  67 LDQLEEKGLISRQTCASDRRAKRIKLTEKAEPLISEVEAVINKTRAEILH--GISAEE 122
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 42-100 2.64e-04

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: 37.66  E-value: 2.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446114037  42 RILFFIARFPgISVNELLSLLEISKQALHGPLRQLVEKGLIESneaTHDRRVKQLSLTE 100
Cdd:cd00090   11 RILRLLLEGP-LTVSELAERLGLSQSTVSRHLKKLEEAGLVES---RREGRRVYYSLTD 65
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
1-126 4.55e-23

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 88.49  E-value: 4.55e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446114037   1 MTQHKEEQMNEALALFYFAYKTFTEKPDEIIKEYGIQRVHHRILFFIARFPGISVNELLSLLEISKQALHGPLRQLVEKG 80
Cdd:COG1846    1 MSDEPDPAEERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKG 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 446114037  81 LIESNEATHDRRVKQLSLTEEGTDLEKKLSDVQRKQMGAIFSKFGE 126
Cdd:COG1846   81 LVEREPDPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSE 126
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
29-126 1.01e-16

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 71.09  E-value: 1.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446114037    29 EIIKEYGIQRVHHRILFFIARFPGISVNELLSLLEISKQALHGPLRQLVEKGLIESNEATHDRRVKQLSLTEEGTDLEKK 108
Cdd:smart00347   1 EELKPLGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQ 80

                           90
                   ....*....|....*...
gi 446114037   109 LSDVQRKQMGAIFSKFGE 126
Cdd:smart00347  81 LLEARSETLAELLAGLTA 98
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 34-92 1.93e-16

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: 69.15  E-value: 1.93e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446114037   34 YGIQRVHHRILFFIARFPGISVNELLSLLEISKQALHGPLRQLVEKGLIESNEATHDRR 92
Cdd:pfam12802   1 LGLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRR 59
PRK03573 PRK03573
transcriptional regulator SlyA; Provisional
 73-130 3.34e-06

transcriptional regulator SlyA; Provisional


Pssm-ID: 179596  Cd Length: 144  Bit Score: 44.22  E-value: 3.34e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446114037  73 LRQLVEKGLIESNEATHDRRVKQLSLTEEGTDLEKKLSDVQRKQMGAIFSkfGESCEE 130
Cdd:PRK03573  67 LDQLEEKGLISRQTCASDRRAKRIKLTEKAEPLISEVEAVINKTRAEILH--GISAEE 122
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 36-94 2.86e-05

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: 39.84  E-value: 2.86e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446114037   36 IQRVHHRILFFIARFPGISVNELLSLLEISKQALHGPLRQLVEKGLIESNEATHDRRVK 94
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 42-100 2.64e-04

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: 37.66  E-value: 2.64e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446114037  42 RILFFIARFPgISVNELLSLLEISKQALHGPLRQLVEKGLIESneaTHDRRVKQLSLTE 100
Cdd:cd00090   11 RILRLLLEGP-LTVSELAERLGLSQSTVSRHLKKLEEAGLVES---RREGRRVYYSLTD 65
HTH_24 pfam13412
Winged helix-turn-helix DNA-binding;
38-82 5.97e-04

Winged helix-turn-helix DNA-binding;


Pssm-ID: 404317 [Multi-domain]  Cd Length: 45  Bit Score: 35.87  E-value: 5.97e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 446114037   38 RVHHRILFFIARFPGISVNELLSLLEISKQALHGPLRQLVEKGLI 82
Cdd:pfam13412   1 ETDRKILNLLQENPRISQRELAERLGLSPSTVNRRLKRLEEEGVI 45
COG3398 COG3398
Predicted transcriptional regulator, contains two HTH domains [Transcription];
42-101 6.03e-04

Predicted transcriptional regulator, contains two HTH domains [Transcription];


Pssm-ID: 442625 [Multi-domain]  Cd Length: 159  Bit Score: 38.32  E-value: 6.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446114037  42 RILFFIARFPGISVNELLSLLEISKQALHGPLRQLVEKGLIESneaTHDRRVKQLSLTEE 101
Cdd:COG3398  101 RILLYLLENPGATNKELAEELGISRSTVSWHLKRLEEDGLVER---ERDGRNVRYYLNPP 157
HTH_27 pfam13463
Winged helix DNA-binding domain;
38-102 1.28e-03

Winged helix DNA-binding domain;


Pssm-ID: 433228 [Multi-domain]  Cd Length: 68  Bit Score: 35.73  E-value: 1.28e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446114037   38 RVHHRILFFI-ARFPGISVNELLSLLEISKQALHGPLRQLVEKGLIESNEATHDRRVKQLSLTEEG 102
Cdd:pfam13463   3 RLEALILHNIgHRGDPKTLADICFRLNVEDSHVSYSLKKLTEAGLVEREGSEEDGRETRVRLTAKG 68
PriA COG1198
Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, ...
 42-120 4.09e-03

Primosomal protein N' (replication factor Y) - superfamily II helicase [Replication, recombination and repair];


Pssm-ID: 440811 [Multi-domain]  Cd Length: 728  Bit Score: 36.63  E-value: 4.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446114037  42 RIL-FFIARFPGISVNELLSLLEISKQALhgplRQLVEKGLIESNEATHDRRVKQLSLTEEGtdlEKKLSDVQRKQMGAI 120
Cdd:COG1198  135 RVLeALREHGGPLTLSELAKEAGVSRSVL----KALVKKGLLEIEEREVDRDPFAPDVPAEP---PPTLNEEQQAAVEAI 207
COG2345 COG2345
Predicted transcriptional regulator, ArsR family [Transcription];
41-105 5.06e-03

Predicted transcriptional regulator, ArsR family [Transcription];


Pssm-ID: 441914 [Multi-domain]  Cd Length: 217  Bit Score: 36.05  E-value: 5.06e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446114037  41 HRILFFIARFPGISVNELLSLLEISKQALHGPLRQLVEKGLIESNEATHDR-RVKQL-SLTEEGTDL 105
Cdd:COG2345   16 RRILELLKRAGPVTAAELAEALGLTPNAVRRHLDALEEEGLVERETERRGRgRPAKLyRLTEAGRAR 82
HTH_20 pfam12840
Helix-turn-helix domain; This domain represents a DNA-binding Helix-turn-helix domain found in ...
 42-84 6.51e-03

Helix-turn-helix domain; This domain represents a DNA-binding Helix-turn-helix domain found in transcriptional regulatory proteins.


Pssm-ID: 432824 [Multi-domain]  Cd Length: 61  Bit Score: 33.67  E-value: 6.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 446114037   42 RILFFIARFPGISVNELLSLLEISKQALHGPLRQLVEKGLIES 84
Cdd:pfam12840  14 RILRALVGDEPLTASELARRLDISRNTLSYHLRKLEEAGLVEV 56
 
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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