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Conserved domains on  [gi|446574577|ref|WP_000651923|]
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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];
20-128 3.43e-16

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


:

Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 70.00  E-value: 3.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574577  20 EDNLSHQAIRILQIVSREKNITIGKVASELSLSHNTASEHVKRLIQKDFLLKERNKQDERVVNLTLTTEGMEVLEKHTLL 99
Cdd:COG1846   33 ELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGRALLEEARPA 112

                         90       100
                 ....*....|....*....|....*....
gi 446574577 100 DKEKIKILESQLSKEEQQLIEKAFSLLAK 128
Cdd:COG1846  113 LEALLAELLAGLSEEELEALLRLLRRLAE 141
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
20-128 3.43e-16

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 70.00  E-value: 3.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574577  20 EDNLSHQAIRILQIVSREKNITIGKVASELSLSHNTASEHVKRLIQKDFLLKERNKQDERVVNLTLTTEGMEVLEKHTLL 99
Cdd:COG1846   33 ELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGRALLEEARPA 112

                         90       100
                 ....*....|....*....|....*....
gi 446574577 100 DKEKIKILESQLSKEEQQLIEKAFSLLAK 128
Cdd:COG1846  113 LEALLAELLAGLSEEELEALLRLLRRLAE 141
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
22-116 8.47e-15

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 65.31  E-value: 8.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574577    22 NLSHQAIRILQIVSREKNITIGKVASELSLSHNTASEHVKRLIQKDFLLKERNKQDERVVNLTLTTEGMEVLEKHTLLDK 101
Cdd:smart00347   7 GLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLLEARS 86

                           90
                   ....*....|....*
gi 446574577   102 EKIKILESQLSKEEQ 116
Cdd:smart00347  87 ETLAELLAGLTAEEQ 101
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 23-81 5.86e-07

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: 43.69  E-value: 5.86e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446574577   23 LSHQAIRILQIVSREKNITIGKVASELSLSHNTASEHVKRLIQKDFLLKERNKQDERVV 81
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
20-128 3.43e-16

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 70.00  E-value: 3.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574577  20 EDNLSHQAIRILQIVSREKNITIGKVASELSLSHNTASEHVKRLIQKDFLLKERNKQDERVVNLTLTTEGMEVLEKHTLL 99
Cdd:COG1846   33 ELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGRALLEEARPA 112

                         90       100
                 ....*....|....*....|....*....
gi 446574577 100 DKEKIKILESQLSKEEQQLIEKAFSLLAK 128
Cdd:COG1846  113 LEALLAELLAGLSEEELEALLRLLRRLAE 141
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
22-116 8.47e-15

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 65.31  E-value: 8.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574577    22 NLSHQAIRILQIVSREKNITIGKVASELSLSHNTASEHVKRLIQKDFLLKERNKQDERVVNLTLTTEGMEVLEKHTLLDK 101
Cdd:smart00347   7 GLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLLEARS 86

                           90
                   ....*....|....*
gi 446574577   102 EKIKILESQLSKEEQ 116
Cdd:smart00347  87 ETLAELLAGLTAEEQ 101
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 23-81 5.86e-07

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: 43.69  E-value: 5.86e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446574577   23 LSHQAIRILQIVSREKNITIGKVASELSLSHNTASEHVKRLIQKDFLLKERNKQDERVV 81
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 22-79 9.09e-07

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: 43.35  E-value: 9.09e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446574577   22 NLSHQAIRILQIVSREKNITIGKVASELSLSHNTASEHVKRLIQKDFLLKERNKQDER 79
Cdd:pfam12802   2 GLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRR 59
HTH_24 pfam13412
Winged helix-turn-helix DNA-binding;
28-69 2.86e-03

Winged helix-turn-helix DNA-binding;


Pssm-ID: 404317 [Multi-domain]  Cd Length: 45  Bit Score: 33.56  E-value: 2.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 446574577   28 IRILQIVSREKNITIGKVASELSLSHNTASEHVKRLIQKDFL 69
Cdd:pfam13412   4 RKILNLLQENPRISQRELAERLGLSPSTVNRRLKRLEEEGVI 45
COG3398 COG3398
Predicted transcriptional regulator, contains two HTH domains [Transcription];
29-88 6.61e-03

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


Pssm-ID: 442625 [Multi-domain]  Cd Length: 159  Bit Score: 34.85  E-value: 6.61e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574577  29 RILQIVSREKNITIGKVASELSLSHNTASEHVKRLIQKDFLLKERnkqDERVVNLTLTTE 88
Cdd:COG3398  101 RILLYLLENPGATNKELAEELGISRSTVSWHLKRLEEDGLVERER---DGRNVRYYLNPP 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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