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Conserved domains on  [gi|446121079|ref|WP_000198934|]
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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];
1-138 2.81e-19

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


:

Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 78.47  E-value: 2.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446121079   1 MTRTYK----EIINEMNRAYNEFYILLFQELKdEYGLTGQQESMLFHIHLNENTTANHIATTFNISKSAVSQVLSKLEKQ 76
Cdd:COG1846    1 MSDEPDpaeeRLGLLLRRLARALRRALDRALA-ELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEK 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446121079  77 KMISKQVNPNNKREYFLTLGPNGSKYMEQLSKLDDVLIEKYFSKIDINALEQMTDTLKKINK 138
Cdd:COG1846   80 GLVEREPDPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRLAE 141
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
1-138 2.81e-19

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 78.47  E-value: 2.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446121079   1 MTRTYK----EIINEMNRAYNEFYILLFQELKdEYGLTGQQESMLFHIHLNENTTANHIATTFNISKSAVSQVLSKLEKQ 76
Cdd:COG1846    1 MSDEPDpaeeRLGLLLRRLARALRRALDRALA-ELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEK 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446121079  77 KMISKQVNPNNKREYFLTLGPNGSKYMEQLSKLDDVLIEKYFSKIDINALEQMTDTLKKINK 138
Cdd:COG1846   80 GLVEREPDPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRLAE 141
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 31-90 4.42e-13

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: 60.30  E-value: 4.42e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446121079   31 YGLTGQQESMLFHIHLNENTTANHIATTFNISKSAVSQVLSKLEKQKMISKQVNPNNKRE 90
Cdd:pfam12802   1 LGLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRRA 60
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
29-124 3.87e-11

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 56.06  E-value: 3.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446121079    29 DEYGLTGQQESMLFHIHLNENTTANHIATTFNISKSAVSQVLSKLEKQKMISKQVNPNNKREYFLTLGPNGSKYMEQLSK 108
Cdd:smart00347   4 KPLGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLLE 83

                           90
                   ....*....|....*.
gi 446121079   109 LDDVLIEKYFSKIDIN 124
Cdd:smart00347  84 ARSETLAELLAGLTAE 99
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 40-97 1.96e-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: 35.35  E-value: 1.96e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446121079  40 MLFHIHLNEnTTANHIATTFNISKSAVSQVLSKLEKQKMISKQVNPnNKREYFLTLGP 97
Cdd:cd00090   12 ILRLLLEGP-LTVSELAERLGLSQSTVSRHLKKLEEAGLVESRREG-RRVYYSLTDAE 67
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
1-138 2.81e-19

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 78.47  E-value: 2.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446121079   1 MTRTYK----EIINEMNRAYNEFYILLFQELKdEYGLTGQQESMLFHIHLNENTTANHIATTFNISKSAVSQVLSKLEKQ 76
Cdd:COG1846    1 MSDEPDpaeeRLGLLLRRLARALRRALDRALA-ELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEK 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446121079  77 KMISKQVNPNNKREYFLTLGPNGSKYMEQLSKLDDVLIEKYFSKIDINALEQMTDTLKKINK 138
Cdd:COG1846   80 GLVEREPDPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRLAE 141
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 31-90 4.42e-13

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: 60.30  E-value: 4.42e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446121079   31 YGLTGQQESMLFHIHLNENTTANHIATTFNISKSAVSQVLSKLEKQKMISKQVNPNNKRE 90
Cdd:pfam12802   1 LGLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRRA 60
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
29-124 3.87e-11

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 56.06  E-value: 3.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446121079    29 DEYGLTGQQESMLFHIHLNENTTANHIATTFNISKSAVSQVLSKLEKQKMISKQVNPNNKREYFLTLGPNGSKYMEQLSK 108
Cdd:smart00347   4 KPLGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLLE 83

                           90
                   ....*....|....*.
gi 446121079   109 LDDVLIEKYFSKIDIN 124
Cdd:smart00347  84 ARSETLAELLAGLTAE 99
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 33-90 1.93e-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: 40.22  E-value: 1.93e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446121079   33 LTGQQESMLFHIHLNENTTANHIATTFNISKSAVSQVLSKLEKQKMISKQVNPNNKRE 90
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRRE 58
GbsR COG1510
DNA-binding transcriptional regulator GbsR, MarR family [Transcription];
1-92 2.95e-05

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


Pssm-ID: 441119  Cd Length: 164  Bit Score: 41.84  E-value: 2.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446121079   1 MTRTYKEIINEMnraynefyILLFQELKDEYGLT---GQQESMLFhIHlNENTTANHIATTFNISKSAVSQVLSKLEKQK 77
Cdd:COG1510    1 MSEKLEEAKERF--------IEAFGEMGERWGLPrsaGRIYALLY-LS-DEPLTADELAEELGVSKSSVSTALRELEDWG 70

                         90
                 ....*....|....*
gi 446121079  78 MISKQVNPNNKREYF 92
Cdd:COG1510   71 LVRRVRKPGDRKDYF 85
HTH_27 pfam13463
Winged helix DNA-binding domain;
33-99 1.39e-03

Winged helix DNA-binding domain;


Pssm-ID: 433228 [Multi-domain]  Cd Length: 68  Bit Score: 35.34  E-value: 1.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446121079   33 LTGQQESMLFHI-HLNENTTANHIATTFNISKSAVSQVLSKLEKQKMISKQVNPNNKREYFLTLGPNG 99
Cdd:pfam13463   1 LTRLEALILHNIgHRGDPKTLADICFRLNVEDSHVSYSLKKLTEAGLVEREGSEEDGRETRVRLTAKG 68
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 40-97 1.96e-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: 35.35  E-value: 1.96e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446121079  40 MLFHIHLNEnTTANHIATTFNISKSAVSQVLSKLEKQKMISKQVNPnNKREYFLTLGP 97
Cdd:cd00090   12 ILRLLLEGP-LTVSELAERLGLSQSTVSRHLKKLEEAGLVESRREG-RRVYYSLTDAE 67
HTH_ARSR smart00418
helix_turn_helix, Arsenical Resistance Operon Repressor;
51-94 7.00e-03

helix_turn_helix, Arsenical Resistance Operon Repressor;


Pssm-ID: 197713 [Multi-domain]  Cd Length: 66  Bit Score: 33.34  E-value: 7.00e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 446121079    51 TANHIATTFNISKSAVSQVLSKLEKQKMISKQVNPNNKReYFLT 94
Cdd:smart00418  12 CVCELAEILGLSQSTVSHHLKKLREAGLVESRREGKRVY-YSLT 54
 
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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