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Conserved domains on  [gi|488216402|ref|WP_002287610|]
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MULTISPECIES: MarR family winged helix-turn-helix transcriptional regulator [Enterococcus]

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];
34-140 3.31e-25

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


:

Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 93.50  E-value: 3.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216402  34 DLSITEMHTIEAIGMYKKKTTSEVAKELSITVGTLTTAINKLVKKGYVERIRSEDDRRVVKLGLTKKGKLLFRVHQHFHR 113
Cdd:COG1846   35 GLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGRALLEEARPALE 114
                         90       100
                 ....*....|....*....|....*..
gi 488216402 114 EMVKNILDGMATEEQHALLDALKNLHD 140
Cdd:COG1846  115 ALLAELLAGLSEEELEALLRLLRRLAE 141
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
34-140 3.31e-25

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 93.50  E-value: 3.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216402  34 DLSITEMHTIEAIGMYKKKTTSEVAKELSITVGTLTTAINKLVKKGYVERIRSEDDRRVVKLGLTKKGKLLFRVHQHFHR 113
Cdd:COG1846   35 GLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGRALLEEARPALE 114
                         90       100
                 ....*....|....*....|....*..
gi 488216402 114 EMVKNILDGMATEEQHALLDALKNLHD 140
Cdd:COG1846  115 ALLAELLAGLSEEELEALLRLLRRLAE 141
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
33-128 1.79e-19

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 77.63  E-value: 1.79e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216402    33 KDLSITEMHTIEAIGMYKKKTTSEVAKELSITVGTLTTAINKLVKKGYVERIRSEDDRRVVKLGLTKKGKLLFRVHQHFH 112
Cdd:smart00347   6 LGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLLEAR 85
                           90
                   ....*....|....*.
gi 488216402   113 REMVKNILDGMATEEQ 128
Cdd:smart00347  86 SETLAELLAGLTAEEQ 101
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
34-91 6.46e-11

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: 54.52  E-value: 6.46e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 488216402   34 DLSITEMHTIEAIGMYKKKTTSEVAKELSITVGTLTTAINKLVKKGYVERIRSEDDRR 91
Cdd:pfam12802   2 GLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRR 59
PRK11512 PRK11512
multiple antibiotic resistance transcriptional regulator MarR;
34-128 2.70e-08

multiple antibiotic resistance transcriptional regulator MarR;


Pssm-ID: 183170  Cd Length: 144  Bit Score: 49.51  E-value: 2.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216402  34 DLSITEMHTIEAIGMYKKKTTSEVAKELSITVGTLTTAINKLVKKGYVERIRSEDDRRVVKLGLTKKGKLLF-----RVH 108
Cdd:PRK11512  37 DITAAQFKVLCSIRCAACITPVELKKVLSVDLGALTRMLDRLVCKGWVERLPNPNDKRGVLVKLTTSGAAICeqchqLVG 116
                         90       100
                 ....*....|....*....|.
gi 488216402 109 QHFHREMVKNIL-DGMATEEQ 128
Cdd:PRK11512 117 QDLHQELTKNLTaDEVATLEH 137
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
52-104 7.34e-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: 33.43  E-value: 7.34e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488216402  52 KTTSEVAKELSITVGTLTTAINKLVKKGYVERIRsedDRRVVKLGLTKKGKLL 104
Cdd:cd00090   21 LTVSELAERLGLSQSTVSRHLKKLEEAGLVESRR---EGRRVYYSLTDAERLL 70
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
34-140 3.31e-25

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 93.50  E-value: 3.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216402  34 DLSITEMHTIEAIGMYKKKTTSEVAKELSITVGTLTTAINKLVKKGYVERIRSEDDRRVVKLGLTKKGKLLFRVHQHFHR 113
Cdd:COG1846   35 GLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGRALLEEARPALE 114
                         90       100
                 ....*....|....*....|....*..
gi 488216402 114 EMVKNILDGMATEEQHALLDALKNLHD 140
Cdd:COG1846  115 ALLAELLAGLSEEELEALLRLLRRLAE 141
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
33-128 1.79e-19

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 77.63  E-value: 1.79e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216402    33 KDLSITEMHTIEAIGMYKKKTTSEVAKELSITVGTLTTAINKLVKKGYVERIRSEDDRRVVKLGLTKKGKLLFRVHQHFH 112
Cdd:smart00347   6 LGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLLEAR 85
                           90
                   ....*....|....*.
gi 488216402   113 REMVKNILDGMATEEQ 128
Cdd:smart00347  86 SETLAELLAGLTAEEQ 101
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
34-91 6.46e-11

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: 54.52  E-value: 6.46e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 488216402   34 DLSITEMHTIEAIGMYKKKTTSEVAKELSITVGTLTTAINKLVKKGYVERIRSEDDRR 91
Cdd:pfam12802   2 GLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRR 59
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
35-93 6.19e-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: 426012 [Multi-domain]  Cd Length: 59  Bit Score: 51.78  E-value: 6.19e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488216402   35 LSITEMHTIEAIGMYKKKTTSEVAKELSITVGTLTTAINKLVKKGYVERIRSEDDRRVV 93
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
PRK11512 PRK11512
multiple antibiotic resistance transcriptional regulator MarR;
34-128 2.70e-08

multiple antibiotic resistance transcriptional regulator MarR;


Pssm-ID: 183170  Cd Length: 144  Bit Score: 49.51  E-value: 2.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216402  34 DLSITEMHTIEAIGMYKKKTTSEVAKELSITVGTLTTAINKLVKKGYVERIRSEDDRRVVKLGLTKKGKLLF-----RVH 108
Cdd:PRK11512  37 DITAAQFKVLCSIRCAACITPVELKKVLSVDLGALTRMLDRLVCKGWVERLPNPNDKRGVLVKLTTSGAAICeqchqLVG 116
                         90       100
                 ....*....|....*....|.
gi 488216402 109 QHFHREMVKNIL-DGMATEEQ 128
Cdd:PRK11512 117 QDLHQELTKNLTaDEVATLEH 137
HTH_27 pfam13463
Winged helix DNA-binding domain;
47-101 1.94e-05

Winged helix DNA-binding domain;


Pssm-ID: 433228 [Multi-domain]  Cd Length: 68  Bit Score: 40.35  E-value: 1.94e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 488216402   47 GMYKKKTTSEVAKELSITVGTLTTAINKLVKKGYVERIRSEDDRRVVKLGLTKKG 101
Cdd:pfam13463  14 HRGDPKTLADICFRLNVEDSHVSYSLKKLTEAGLVEREGSEEDGRETRVRLTAKG 68
MntR COG1321
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];
33-102 1.42e-04

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


Pssm-ID: 440932 [Multi-domain]  Cd Length: 135  Bit Score: 39.42  E-value: 1.42e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488216402  33 KDLSITEMHTIEAIGMYKKK----TTSEVAKELSITVGTLTTAINKLVKKGYVERirsEDDRRVVklgLTKKGK 102
Cdd:COG1321    2 MMLSESEEDYLKAIYELSEEggpvRTSDIAERLGVSPPSVTEMLKKLEEKGLVEY---EPYGGIT---LTEEGR 69
PRK13777 PRK13777
HTH-type transcriptional regulator Hpr;
34-105 4.47e-04

HTH-type transcriptional regulator Hpr;


Pssm-ID: 237501  Cd Length: 185  Bit Score: 38.49  E-value: 4.47e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488216402  34 DLSITEMHTIEAIGMYKKKTTSEVAKelsITVGTLTTAIN---KLVKKGYVERIRSEDDRRVVKLGLTKKGKLLF 105
Cdd:PRK13777  42 DLNINEHHILWIAYHLKGASISEIAK---FGVMHVSTAFNfskKLEERGYLTFSKKEDDKRNTYIELTEKGEELL 113
pheS PRK04172
phenylalanine--tRNA ligase subunit alpha;
33-102 2.56e-03

phenylalanine--tRNA ligase subunit alpha;


Pssm-ID: 235239 [Multi-domain]  Cd Length: 489  Bit Score: 36.73  E-value: 2.56e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216402  33 KDLSITEMHTIEAIGMYKKKTTSEVAKELSITVGTLTTAINKLVKKGYVErirsEDDRRVVKLGLTKKGK 102
Cdd:PRK04172   2 MELHPNEKKVLKALKELKEATLEELAEKLGLPPEAVMRAAEWLEEKGLVK----VEERVEEVYVLTEEGK 67
GbsR COG1510
DNA-binding transcriptional regulator GbsR, MarR family [Transcription];
53-144 3.72e-03

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


Pssm-ID: 441119  Cd Length: 164  Bit Score: 35.68  E-value: 3.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488216402  53 TTSEVAKELSITVGTLTTAINKLVKKGYVERIRSEDDRRVvklgltkkgklLFRVHQHFhREMVKNILDGMATEEQHALL 132
Cdd:COG1510   44 TADELAEELGVSKSSVSTALRELEDWGLVRRVRKPGDRKD-----------YFRAEKDV-WELFRRVFRERLRREIDPTL 111
                         90
                 ....*....|..
gi 488216402 133 DALKNLHDFLQD 144
Cdd:COG1510  112 ELLREALEELED 123
PRK10870 PRK10870
transcriptional repressor MprA; Provisional
60-106 4.50e-03

transcriptional repressor MprA; Provisional


Pssm-ID: 182795  Cd Length: 176  Bit Score: 35.49  E-value: 4.50e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488216402  60 ELSITVG---TLTTAI-NKLVKKGYVERIRSEDDRRVVKLGLTKKGKLLFR 106
Cdd:PRK10870  76 ELSCALGssrTNATRIaDELEKRGWIERRESDNDRRCLHLQLTEKGHEFLR 126
TrmB pfam01978
Sugar-specific transcriptional regulator TrmB; One member of this family, TrmB, has been shown ...
34-87 5.56e-03

Sugar-specific transcriptional regulator TrmB; One member of this family, TrmB, has been shown to be a sugar-specific transcriptional regulator of the trehalose/maltose ABC transporter in Thermococcus litoralis.


Pssm-ID: 396525 [Multi-domain]  Cd Length: 67  Bit Score: 33.65  E-value: 5.56e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 488216402   34 DLSITEMHTIEAIGMYKKKTTSEVAKELSITVGTLTTAINKLVKKGYVERIRSE 87
Cdd:pfam01978   5 GLSEYEAKVYLALLKLGPATADEIAEESGVPRSKVYEVLRSLEDKGLVEREKGR 58
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
52-104 7.34e-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: 33.43  E-value: 7.34e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488216402  52 KTTSEVAKELSITVGTLTTAINKLVKKGYVERIRsedDRRVVKLGLTKKGKLL 104
Cdd:cd00090   21 LTVSELAERLGLSQSTVSRHLKKLEEAGLVESRR---EGRRVYYSLTDAERLL 70
HTH_24 pfam13412
Winged helix-turn-helix DNA-binding;
53-81 9.24e-03

Winged helix-turn-helix DNA-binding;


Pssm-ID: 404317 [Multi-domain]  Cd Length: 45  Bit Score: 32.41  E-value: 9.24e-03
                          10        20
                  ....*....|....*....|....*....
gi 488216402   53 TTSEVAKELSITVGTLTTAINKLVKKGYV 81
Cdd:pfam13412  17 SQRELAERLGLSPSTVNRRLKRLEEEGVI 45
 
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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