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Conserved domains on  [gi|446367967|ref|WP_000445822|]
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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];
36-139 3.74e-23

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


:

Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 88.10  E-value: 3.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367967  36 MPPSHTQVLLLLHENGTLAVSEIGKRLAISRPNMTPLLNKLIQEELIERHYSEKDRRVILISLTAEGKLLVNQYQQFILD 115
Cdd:COG1846   36 LTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGRALLEEARPALEA 115

                         90       100
                 ....*....|....*....|....
gi 446367967 116 KLKESFQTLSEEEREKLIHSLQTI 139
Cdd:COG1846  116 LLAELLAGLSEEELEALLRLLRRL 139
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
36-139 3.74e-23

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 88.10  E-value: 3.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367967  36 MPPSHTQVLLLLHENGTLAVSEIGKRLAISRPNMTPLLNKLIQEELIERHYSEKDRRVILISLTAEGKLLVNQYQQFILD 115
Cdd:COG1846   36 LTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGRALLEEARPALEA 115

                         90       100
                 ....*....|....*....|....
gi 446367967 116 KLKESFQTLSEEEREKLIHSLQTI 139
Cdd:COG1846  116 LLAELLAGLSEEELEALLRLLRRL 139
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
39-129 7.92e-20

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 78.40  E-value: 7.92e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367967    39 SHTQ--VLLLLHENGTLAVSEIGKRLAISRPNMTPLLNKLIQEELIERHYSEKDRRVILISLTAEGKLLVNQYQQFILDK 116
Cdd:smart00347   9 TPTQflVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLLEARSET 88

                           90
                   ....*....|...
gi 446367967   117 LKESFQTLSEEER 129
Cdd:smart00347  89 LAELLAGLTAEEQ 101
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 36-92 3.16e-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: 52.59  E-value: 3.16e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446367967   36 MPPSHTQVLLLLHENGTLAVSEIGKRLAISRPNMTPLLNKLIQEELIERHYSEKDRR 92
Cdd:pfam12802   3 LTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRR 59
PRK03573 PRK03573
transcriptional regulator SlyA; Provisional
 35-144 3.16e-05

transcriptional regulator SlyA; Provisional


Pssm-ID: 179596  Cd Length: 144  Bit Score: 41.14  E-value: 3.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367967  35 HMPPSHTQVLLllhengtlavseiGKRLAISRPNMTPLLNKLIQEELIERHYSEKDRRVILISLTAEGKLLVNQYQQFIL 114
Cdd:PRK03573  42 QLPPEQSQIQL-------------AKAIGIEQPSLVRTLDQLEEKGLISRQTCASDRRAKRIKLTEKAEPLISEVEAVIN 108

                         90       100       110
                 ....*....|....*....|....*....|
gi 446367967 115 DKLKESFQTLSEEEREKLIHSLQTIQNLIL 144
Cdd:PRK03573 109 KTRAEILHGISAEEIEQLITLIAKLEKNII 138
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 38-106 2.80e-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: 37.28  E-value: 2.80e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446367967  38 PSHTQVLLLLHENGtLAVSEIGKRLAISRPNMTPLLNKLIQEELIERhysEKDRRVILISLTAEGKLLV 106
Cdd:cd00090    7 PTRLRILRLLLEGP-LTVSELAERLGLSQSTVSRHLKKLEEAGLVES---RREGRRVYYSLTDAERLLA 71
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
36-139 3.74e-23

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 88.10  E-value: 3.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367967  36 MPPSHTQVLLLLHENGTLAVSEIGKRLAISRPNMTPLLNKLIQEELIERHYSEKDRRVILISLTAEGKLLVNQYQQFILD 115
Cdd:COG1846   36 LTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGRALLEEARPALEA 115

                         90       100
                 ....*....|....*....|....
gi 446367967 116 KLKESFQTLSEEEREKLIHSLQTI 139
Cdd:COG1846  116 LLAELLAGLSEEELEALLRLLRRL 139
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
39-129 7.92e-20

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 78.40  E-value: 7.92e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367967    39 SHTQ--VLLLLHENGTLAVSEIGKRLAISRPNMTPLLNKLIQEELIERHYSEKDRRVILISLTAEGKLLVNQYQQFILDK 116
Cdd:smart00347   9 TPTQflVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLLEARSET 88

                           90
                   ....*....|...
gi 446367967   117 LKESFQTLSEEER 129
Cdd:smart00347  89 LAELLAGLTAEEQ 101
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 36-92 3.16e-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: 52.59  E-value: 3.16e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446367967   36 MPPSHTQVLLLLHENGTLAVSEIGKRLAISRPNMTPLLNKLIQEELIERHYSEKDRR 92
Cdd:pfam12802   3 LTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRR 59
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 39-94 2.21e-09

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: 50.24  E-value: 2.21e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446367967   39 SHTQ--VLLLLHENGTLAVSEIGKRLAISRPNMTPLLNKLIQEELIERHYSEKDRRVI 94
Cdd:pfam01047   2 TLTQfhILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
HTH_27 pfam13463
Winged helix DNA-binding domain;
38-102 1.52e-05

Winged helix DNA-binding domain;


Pssm-ID: 433228 [Multi-domain]  Cd Length: 68  Bit Score: 40.74  E-value: 1.52e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446367967   38 PSHTQVL-LLLHENGTLAVSEIGKRLAISRPNMTPLLNKLIQEELIERHYSEKDRRVILISLTAEG 102
Cdd:pfam13463   3 RLEALILhNIGHRGDPKTLADICFRLNVEDSHVSYSLKKLTEAGLVEREGSEEDGRETRVRLTAKG 68
PRK03573 PRK03573
transcriptional regulator SlyA; Provisional
 35-144 3.16e-05

transcriptional regulator SlyA; Provisional


Pssm-ID: 179596  Cd Length: 144  Bit Score: 41.14  E-value: 3.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367967  35 HMPPSHTQVLLllhengtlavseiGKRLAISRPNMTPLLNKLIQEELIERHYSEKDRRVILISLTAEGKLLVNQYQQFIL 114
Cdd:PRK03573  42 QLPPEQSQIQL-------------AKAIGIEQPSLVRTLDQLEEKGLISRQTCASDRRAKRIKLTEKAEPLISEVEAVIN 108

                         90       100       110
                 ....*....|....*....|....*....|
gi 446367967 115 DKLKESFQTLSEEEREKLIHSLQTIQNLIL 144
Cdd:PRK03573 109 KTRAEILHGISAEEIEQLITLIAKLEKNII 138
GbsR COG1510
DNA-binding transcriptional regulator GbsR, MarR family [Transcription];
28-92 4.55e-05

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


Pssm-ID: 441119  Cd Length: 164  Bit Score: 41.07  E-value: 4.55e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446367967  28 GEFSSQRHMPPSHTQV--LLLLHENGtLAVSEIGKRLAISRPNMTPLLNKLIQEELIERHYSEKDRR 92
Cdd:COG1510   17 GEMGERWGLPRSAGRIyaLLYLSDEP-LTADELAEELGVSKSSVSTALRELEDWGLVRRVRKPGDRK 82
COG4742 COG4742
Predicted transcriptional regulator, contains HTH domain [Transcription];
38-123 6.88e-05

Predicted transcriptional regulator, contains HTH domain [Transcription];


Pssm-ID: 443776 [Multi-domain]  Cd Length: 267  Bit Score: 41.03  E-value: 6.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367967  38 PSHTQVLLLLHEnGTLAVSEIGKRLAISRPNMTPLLNKLIQEELIERHysekDRRViliSLTAEGKLLVNQYQQFI---- 113
Cdd:COG4742   16 EKRKNILLLLAE-GPKTRSELAESLDVSRSTILRQLKELEERGLIERD----DGEY---ELTTLGRLVVEEMEPLLdtle 87

                         90
                 ....*....|.
gi 446367967 114 -LDKLKESFQT 123
Cdd:COG4742   88 vLEENRDYWET 98
PRK11512 PRK11512
multiple antibiotic resistance transcriptional regulator MarR;
22-139 1.35e-04

multiple antibiotic resistance transcriptional regulator MarR;


Pssm-ID: 183170  Cd Length: 144  Bit Score: 39.50  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367967  22 RKFMLPGEFSSQRHMPPSHTQVLLLLHENGTLAVSEIGKRLAISRPNMTPLLNKLIQEELIERHYSEKDRRVILISLTAE 101
Cdd:PRK11512  24 KKDRLLNEYLSPLDITAAQFKVLCSIRCAACITPVELKKVLSVDLGALTRMLDRLVCKGWVERLPNPNDKRGVLVKLTTS 103

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 446367967 102 GKLLVNQYQQFILDKL-KESFQTLSEEEREKLIHSLQTI 139
Cdd:PRK11512 104 GAAICEQCHQLVGQDLhQELTKNLTADEVATLEHLLKKV 142
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 38-106 2.80e-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: 37.28  E-value: 2.80e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446367967  38 PSHTQVLLLLHENGtLAVSEIGKRLAISRPNMTPLLNKLIQEELIERhysEKDRRVILISLTAEGKLLV 106
Cdd:cd00090    7 PTRLRILRLLLEGP-LTVSELAERLGLSQSTVSRHLKKLEEAGLVES---RREGRRVYYSLTDAERLLA 71
MntR COG1321
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];
43-103 4.51e-04

Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];


Pssm-ID: 440932 [Multi-domain]  Cd Length: 135  Bit Score: 37.88  E-value: 4.51e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446367967  43 VLLLLHENGTLAVSEIGKRLAISRPNMTPLLNKLIQEELIERhysEKDRRvilISLTAEGK 103
Cdd:COG1321   15 IYELSEEGGPVRTSDIAERLGVSPPSVTEMLKKLEEKGLVEY---EPYGG---ITLTEEGR 69
PRK10870 PRK10870
transcriptional repressor MprA; Provisional
 49-132 7.76e-04

transcriptional repressor MprA; Provisional


Pssm-ID: 182795  Cd Length: 176  Bit Score: 37.81  E-value: 7.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446367967  49 ENGTLAVSEIGKRLAISRPNMTPLLNKLIQEELIERHYSEKDRRVILISLTAEGKLLVNQYQQFILDKLKESFQTLSEEE 128
Cdd:PRK10870  68 ENHSIQPSELSCALGSSRTNATRIADELEKRGWIERRESDNDRRCLHLQLTEKGHEFLREVLPPQHNCLHQLWSALSTTE 147


                 ....
gi 446367967 129 REKL 132
Cdd:PRK10870 148 KDQL 151
COG3398 COG3398
Predicted transcriptional regulator, contains two HTH domains [Transcription];
43-101 2.81e-03

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


Pssm-ID: 442625 [Multi-domain]  Cd Length: 159  Bit Score: 36.01  E-value: 2.81e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446367967  43 VLLLLHENGTLAVSEIGKRLAISRPNMTPLLNKLIQEELIERhysEKDRRVILISLTAE 101
Cdd:COG3398  102 ILLYLLENPGATNKELAEELGISRSTVSWHLKRLEEDGLVER---ERDGRNVRYYLNPP 157
 
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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