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Conserved domains on  [gi|496663373|ref|WP_009305866|]
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MULTISPECIES: MarR family winged helix-turn-helix transcriptional regulator [Eggerthella]

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];
8-139 3.61e-25

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


:

Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 93.50  E-value: 3.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663373   8 RELFAITYDLQKILHDTMTPICQEHGLTLQQMHVLVELMRTPGLTAGQLSDRAGILRTNFSPVCRKLENRGLIERQRSQT 87
Cdd:COG1846   10 ERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPE 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496663373  88 DRRSLRLHVTDEGRALLASVDGEVQRRYGRAFSAEPQETFDAILEGFQALSA 139
Cdd:COG1846   90 DRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRLAE 141
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
8-139 3.61e-25

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 93.50  E-value: 3.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663373   8 RELFAITYDLQKILHDTMTPICQEHGLTLQQMHVLVELMRTPGLTAGQLSDRAGILRTNFSPVCRKLENRGLIERQRSQT 87
Cdd:COG1846   10 ERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPE 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496663373  88 DRRSLRLHVTDEGRALLASVDGEVQRRYGRAFSAEPQETFDAILEGFQALSA 139
Cdd:COG1846   90 DRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRLAE 141
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
28-120 9.62e-21

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 80.72  E-value: 9.62e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663373    28 ICQEHGLTLQQMHVLVELMRTPGLTAGQLSDRAGILRTNFSPVCRKLENRGLIERQRSQTDRRSLRLHVTDEGRALLASV 107
Cdd:smart00347   2 ELKPLGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQL 81

                           90
                   ....*....|...
gi 496663373   108 DGEVQRRYGRAFS 120
Cdd:smart00347  82 LEARSETLAELLA 94
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 32-91 5.57e-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: 59.52  E-value: 5.57e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663373   32 HGLTLQQMHVLVELMRTPGLTAGQLSDRAGILRTNFSPVCRKLENRGLIERQRSQTDRRS 91
Cdd:pfam12802   1 LGLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRRA 60
PRK10870 PRK10870
transcriptional repressor MprA; Provisional
 55-107 2.92e-08

transcriptional repressor MprA; Provisional


Pssm-ID: 182795  Cd Length: 176  Bit Score: 50.13  E-value: 2.92e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496663373  55 QLSDRAGILRTNFSPVCRKLENRGLIERQRSQTDRRSLRLHVTDEGRALLASV 107
Cdd:PRK10870  76 ELSCALGSSRTNATRIADELEKRGWIERRESDNDRRCLHLQLTEKGHEFLREV 128
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 42-108 8.61e-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: 36.12  E-value: 8.61e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496663373  42 LVELMRTPGLTAGQLSDRAGILRTNFSPVCRKLENRGLIERQRsQTDRRSLRLHVTDEGRALLASVD 108
Cdd:cd00090   12 ILRLLLEGPLTVSELAERLGLSQSTVSRHLKKLEEAGLVESRR-EGRRVYYSLTDAERLLALLESLL 77
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
8-139 3.61e-25

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 93.50  E-value: 3.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663373   8 RELFAITYDLQKILHDTMTPICQEHGLTLQQMHVLVELMRTPGLTAGQLSDRAGILRTNFSPVCRKLENRGLIERQRSQT 87
Cdd:COG1846   10 ERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPE 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 496663373  88 DRRSLRLHVTDEGRALLASVDGEVQRRYGRAFSAEPQETFDAILEGFQALSA 139
Cdd:COG1846   90 DRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRLAE 141
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
28-120 9.62e-21

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 80.72  E-value: 9.62e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663373    28 ICQEHGLTLQQMHVLVELMRTPGLTAGQLSDRAGILRTNFSPVCRKLENRGLIERQRSQTDRRSLRLHVTDEGRALLASV 107
Cdd:smart00347   2 ELKPLGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQL 81

                           90
                   ....*....|...
gi 496663373   108 DGEVQRRYGRAFS 120
Cdd:smart00347  82 LEARSETLAELLA 94
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 32-91 5.57e-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: 59.52  E-value: 5.57e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663373   32 HGLTLQQMHVLVELMRTPGLTAGQLSDRAGILRTNFSPVCRKLENRGLIERQRSQTDRRS 91
Cdd:pfam12802   1 LGLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRRA 60
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 34-91 4.54e-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: 52.16  E-value: 4.54e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 496663373   34 LTLQQMHVLVELMRTPGLTAGQLSDRAGILRTNFSPVCRKLENRGLIERQRSQTDRRS 91
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRRE 58
PRK10870 PRK10870
transcriptional repressor MprA; Provisional
 55-107 2.92e-08

transcriptional repressor MprA; Provisional


Pssm-ID: 182795  Cd Length: 176  Bit Score: 50.13  E-value: 2.92e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496663373  55 QLSDRAGILRTNFSPVCRKLENRGLIERQRSQTDRRSLRLHVTDEGRALLASV 107
Cdd:PRK10870  76 ELSCALGSSRTNATRIADELEKRGWIERRESDNDRRCLHLQLTEKGHEFLREV 128
TrmB pfam01978
Sugar-specific transcriptional regulator TrmB; One member of this family, TrmB, has been shown ...
 30-85 8.50e-06

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: 40.97  E-value: 8.50e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 496663373   30 QEHGLTLQQMHVLVELMRTPGLTAGQLSDRAGILRTNFSPVCRKLENRGLIERQRS 85
Cdd:pfam01978   2 QKLGLSEYEAKVYLALLKLGPATADEIAEESGVPRSKVYEVLRSLEDKGLVEREKG 57
HTH_27 pfam13463
Winged helix DNA-binding domain;
46-100 1.88e-05

Winged helix DNA-binding domain;


Pssm-ID: 433228 [Multi-domain]  Cd Length: 68  Bit Score: 40.35  E-value: 1.88e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 496663373   46 MRTPGLTAGQLSDRAGILRTNFSPVCRKLENRGLIERQRSQTDRRSLRLHVTDEG 100
Cdd:pfam13463  14 HRGDPKTLADICFRLNVEDSHVSYSLKKLTEAGLVEREGSEEDGRETRVRLTAKG 68
YrhO COG1378
Sugar-specific transcriptional regulator TrmB [Transcription];
33-85 8.45e-05

Sugar-specific transcriptional regulator TrmB [Transcription];


Pssm-ID: 440988 [Multi-domain]  Cd Length: 238  Bit Score: 40.77  E-value: 8.45e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 496663373  33 GLTLQQMHVLVELMRTPGLTAGQLSDRAGILRTNFSPVCRKLENRGLIERQRS 85
Cdd:COG1378   10 GLSEYEAKVYLALLELGPATASELAKASGVPRSRVYDVLESLEEKGLVEVSEG 62
PRK13777 PRK13777
HTH-type transcriptional regulator Hpr;
66-144 1.68e-04

HTH-type transcriptional regulator Hpr;


Pssm-ID: 237501  Cd Length: 185  Bit Score: 39.64  E-value: 1.68e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 496663373  66 NFSpvcRKLENRGLIERQRSQTDRRSLRLHVTDEGRALLAsvdgEVQRRYgrafsaEPQEtfDAILEGFQALSAFSGKL 144
Cdd:PRK13777  78 NFS---KKLEERGYLTFSKKEDDKRNTYIELTEKGEELLL----ETMEEY------DPEN--NSVFNGALPLRELYGKF 141
PRK03573 PRK03573
transcriptional regulator SlyA; Provisional
 30-109 8.39e-04

transcriptional regulator SlyA; Provisional


Pssm-ID: 179596  Cd Length: 144  Bit Score: 37.29  E-value: 8.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496663373  30 QEHGLTLQQMHVLvelmrTPGLTAGQLSDRAGILRTNFSPVCRKLENRGLIERQRSQTDRRSLRLHVTDEGRALLASVDG 109
Cdd:PRK03573  31 QTHWVTLHNIHQL-----PPEQSQIQLAKAIGIEQPSLVRTLDQLEEKGLISRQTCASDRRAKRIKLTEKAEPLISEVEA 105
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 42-108 8.61e-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: 36.12  E-value: 8.61e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496663373  42 LVELMRTPGLTAGQLSDRAGILRTNFSPVCRKLENRGLIERQRsQTDRRSLRLHVTDEGRALLASVD 108
Cdd:cd00090   12 ILRLLLEGPLTVSELAERLGLSQSTVSRHLKKLEEAGLVESRR-EGRRVYYSLTDAERLLALLESLL 77
 
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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