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Conserved domains on  [gi|697053878|ref|WP_033146484|]
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MULTISPECIES: MarR family winged helix-turn-helix transcriptional regulator [Enterobacter]

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];
15-122 1.39e-28

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


:

Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 102.36  E-value: 1.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053878  15 DNQLCFALYSANLALNKLYRQLLAPLNLTYPQYLVMLVLWEQDDVTVSDIGERLFLDSATLTPLLKRLESGGLINRHRSR 94
Cdd:COG1846    9 EERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDP 88

                         90       100
                 ....*....|....*....|....*...
gi 697053878  95 KDERQVAVTLSEAGRELQQQALGIPHAV 122
Cdd:COG1846   89 EDRRAVLVRLTEKGRALLEEARPALEAL 116
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
15-122 1.39e-28

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 102.36  E-value: 1.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053878  15 DNQLCFALYSANLALNKLYRQLLAPLNLTYPQYLVMLVLWEQDDVTVSDIGERLFLDSATLTPLLKRLESGGLINRHRSR 94
Cdd:COG1846    9 EERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDP 88

                         90       100
                 ....*....|....*....|....*...
gi 697053878  95 KDERQVAVTLSEAGRELQQQALGIPHAV 122
Cdd:COG1846   89 EDRRAVLVRLTEKGRALLEEARPALEAL 116
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
37-116 3.07e-24

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 89.96  E-value: 3.07e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053878    37 LAPLNLTYPQYLVMLVLWEQDDVTVSDIGERLFLDSATLTPLLKRLESGGLINRHRSRKDERQVAVTLSEAGRELQQQAL 116
Cdd:smart00347   3 LKPLGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLL 82
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 42-100 4.44e-15

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: 65.26  E-value: 4.44e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 697053878   42 LTYPQYLVMLVLWEQDDVTVSDIGERLFLDSATLTPLLKRLESGGLINRHRSRKDERQV 100
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
PRK11512 PRK11512
multiple antibiotic resistance transcriptional regulator MarR;
22-114 1.21e-05

multiple antibiotic resistance transcriptional regulator MarR;


Pssm-ID: 183170  Cd Length: 144  Bit Score: 42.58  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053878  22 LYSANLALNKLYRQLLAPLNLTYPQYLVMLVLWEQDDVTVSDIGERLFLDSATLTPLLKRLESGGLINRHRSRKDERQVA 101
Cdd:PRK11512  18 IHMVNQKKDRLLNEYLSPLDITAAQFKVLCSIRCAACITPVELKKVLSVDLGALTRMLDRLVCKGWVERLPNPNDKRGVL 97

                         90
                 ....*....|...
gi 697053878 102 VTLSEAGRELQQQ 114
Cdd:PRK11512  98 VKLTTSGAAICEQ 110
Staph_reg_Sar TIGR01889
staphylococcal accessory regulator family; This model represents a family of transcriptional ...
 40-117 6.61e-05

staphylococcal accessory regulator family; This model represents a family of transcriptional regulatory proteins in Staphylococcus aureus and Staphylococcus epidermidis. Some members contain two tandem copies of this region. This family is related to the MarR transcriptional regulator family described by pfam01047. [Regulatory functions, DNA interactions]


Pssm-ID: 130944  Cd Length: 109  Bit Score: 39.93  E-value: 6.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053878   40 LNLTYPQYLVM--LVLWEQDD--VTVSDIGERLFLDSATLTPLLKRLESGGLINRHRSRKDERQVAVTLSEAGRELQQQA 115
Cdd:TIGR01889  21 FNLSLEELLILyyLGKLENNEgkLTLKEIIKEILIKQSALVKIIKKLSKKGYLSKERSEDDERKVIISINKEQRSKIESL 100


                  ..
gi 697053878  116 LG 117
Cdd:TIGR01889 101 IS 102
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 56-109 7.66e-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: 7.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 697053878  56 QDDVTVSDIGERLFLDSATLTPLLKRLESGGLInrhRSRKDERQVAVTLSEAGR 109
Cdd:cd00090   18 EGPLTVSELAERLGLSQSTVSRHLKKLEEAGLV---ESRREGRRVYYSLTDAER 68
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
15-122 1.39e-28

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 102.36  E-value: 1.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053878  15 DNQLCFALYSANLALNKLYRQLLAPLNLTYPQYLVMLVLWEQDDVTVSDIGERLFLDSATLTPLLKRLESGGLINRHRSR 94
Cdd:COG1846    9 EERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDP 88

                         90       100
                 ....*....|....*....|....*...
gi 697053878  95 KDERQVAVTLSEAGRELQQQALGIPHAV 122
Cdd:COG1846   89 EDRRAVLVRLTEKGRALLEEARPALEAL 116
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
37-116 3.07e-24

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 89.96  E-value: 3.07e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053878    37 LAPLNLTYPQYLVMLVLWEQDDVTVSDIGERLFLDSATLTPLLKRLESGGLINRHRSRKDERQVAVTLSEAGRELQQQAL 116
Cdd:smart00347   3 LKPLGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLL 82
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 42-100 4.44e-15

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: 65.26  E-value: 4.44e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 697053878   42 LTYPQYLVMLVLWEQDDVTVSDIGERLFLDSATLTPLLKRLESGGLINRHRSRKDERQV 100
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 40-99 4.64e-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: 432797 [Multi-domain]  Cd Length: 60  Bit Score: 49.51  E-value: 4.64e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053878   40 LNLTYPQYLVMLVLWEQDDVTVSDIGERLFLDSATLTPLLKRLESGGLINRHRSRKDERQ 99
Cdd:pfam12802   1 LGLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRRA 60
PRK11512 PRK11512
multiple antibiotic resistance transcriptional regulator MarR;
22-114 1.21e-05

multiple antibiotic resistance transcriptional regulator MarR;


Pssm-ID: 183170  Cd Length: 144  Bit Score: 42.58  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053878  22 LYSANLALNKLYRQLLAPLNLTYPQYLVMLVLWEQDDVTVSDIGERLFLDSATLTPLLKRLESGGLINRHRSRKDERQVA 101
Cdd:PRK11512  18 IHMVNQKKDRLLNEYLSPLDITAAQFKVLCSIRCAACITPVELKKVLSVDLGALTRMLDRLVCKGWVERLPNPNDKRGVL 97

                         90
                 ....*....|...
gi 697053878 102 VTLSEAGRELQQQ 114
Cdd:PRK11512  98 VKLTTSGAAICEQ 110
HTH_27 pfam13463
Winged helix DNA-binding domain;
42-108 1.59e-05

Winged helix DNA-binding domain;


Pssm-ID: 433228 [Multi-domain]  Cd Length: 68  Bit Score: 40.74  E-value: 1.59e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697053878   42 LTYPQYLVM-LVLWEQDDVTVSDIGERLFLDSATLTPLLKRLESGGLINRHRSRKDERQVAVTLSEAG 108
Cdd:pfam13463   1 LTRLEALILhNIGHRGDPKTLADICFRLNVEDSHVSYSLKKLTEAGLVEREGSEEDGRETRVRLTAKG 68
MntR COG1321
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];
46-111 1.80e-05

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


Pssm-ID: 440932 [Multi-domain]  Cd Length: 135  Bit Score: 41.73  E-value: 1.80e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 697053878  46 QYLVMLVLWEQDD--VTVSDIGERLFLDSATLTPLLKRLESGGLINRHRSRKderqvaVTLSEAGREL 111
Cdd:COG1321   10 DYLKAIYELSEEGgpVRTSDIAERLGVSPPSVTEMLKKLEEKGLVEYEPYGG------ITLTEEGREL 71
Staph_reg_Sar TIGR01889
staphylococcal accessory regulator family; This model represents a family of transcriptional ...
 40-117 6.61e-05

staphylococcal accessory regulator family; This model represents a family of transcriptional regulatory proteins in Staphylococcus aureus and Staphylococcus epidermidis. Some members contain two tandem copies of this region. This family is related to the MarR transcriptional regulator family described by pfam01047. [Regulatory functions, DNA interactions]


Pssm-ID: 130944  Cd Length: 109  Bit Score: 39.93  E-value: 6.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 697053878   40 LNLTYPQYLVM--LVLWEQDD--VTVSDIGERLFLDSATLTPLLKRLESGGLINRHRSRKDERQVAVTLSEAGRELQQQA 115
Cdd:TIGR01889  21 FNLSLEELLILyyLGKLENNEgkLTLKEIIKEILIKQSALVKIIKKLSKKGYLSKERSEDDERKVIISINKEQRSKIESL 100


                  ..
gi 697053878  116 LG 117
Cdd:TIGR01889 101 IS 102
TFIIE_alpha pfam02002
TFIIE alpha subunit; The general transcription factor TFIIE has an essential role in ...
 48-100 5.97e-04

TFIIE alpha subunit; The general transcription factor TFIIE has an essential role in eukaryotic transcription initiation together with RNA polymerase II and other general factors. Human TFIIE consists of two subunits TFIIE-alpha and TFIIE-beta and joins the pre-initiation complex after RNA polymerase II and TFIIF. This family consists of the conserved amino terminal region of eukaryotic TFIIE-alpha and proteins from archaebacteria that are presumed to be TFIIE-alpha subunits also Swiss:O29501.


Pssm-ID: 280224  Cd Length: 105  Bit Score: 36.99  E-value: 5.97e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 697053878   48 LVMLVLWEQDDVTVSDIGERLFLDSATLTPLLKRLESGGLINRHRSRKDERQV 100
Cdd:pfam02002  17 LVLDVLLFNGEVTEEDLAELLKIDLNELRKLLNRLYEARLISYRRRRDDETGW 69
Penicillinase_R pfam03965
Penicillinase repressor; The penicillinase repressor negatively regulates expression of the ...
 49-92 9.53e-04

Penicillinase repressor; The penicillinase repressor negatively regulates expression of the penicillinase gene. The N-terminal region of this protein is involved in operator recognition, while the C-terminal is responsible for dimerization of the protein.


Pssm-ID: 427620  Cd Length: 115  Bit Score: 36.81  E-value: 9.53e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 697053878   49 VMLVLWEQDDVTVSDI----GERLFLDSATLTPLLKRLESGGLINRHR 92
Cdd:pfam03965   8 VMEILWALGPATVKEVveelPEPKDWAYSTVKTLLTRLVKKGLLSREK 55
Rfk COG1339
Archaeal CTP-dependent riboflavin kinase [Coenzyme transport and metabolism]; Archaeal ...
 59-111 9.68e-04

Archaeal CTP-dependent riboflavin kinase [Coenzyme transport and metabolism]; Archaeal CTP-dependent riboflavin kinase is part of the Pathway/BioSystem: Riboflavin/FAD biosynthesis


Pssm-ID: 440950 [Multi-domain]  Cd Length: 219  Bit Score: 37.90  E-value: 9.68e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 697053878  59 VTVSDIGERLFLDSATLTPLLKRLESGGLINRHRSRKDERqvaVTLSEAGREL 111
Cdd:COG1339   23 ISSSELAKRLGISQQTASRRLQELEDAGLIERDLVGDGQW---VKITEKGEEL 72
COG2512 COG2512
Predicted transcriptional regulator, contains CW (cell wall-binding) repeats and an HTH domain ...
 59-110 1.51e-03

Predicted transcriptional regulator, contains CW (cell wall-binding) repeats and an HTH domain [General function prediction only];


Pssm-ID: 442002 [Multi-domain]  Cd Length: 80  Bit Score: 35.66  E-value: 1.51e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 697053878  59 VTVSDIGERLFLDSATLTPLLKRLESGGLINRHRsrkDERQVAVTLSEAGRE 110
Cdd:COG2512   31 MTQSEIVKETGWSKSKVSRLLSRLEERGLIEKER---VGRENVVELPEDEPE 79
COG3398 COG3398
Predicted transcriptional regulator, contains two HTH domains [Transcription];
49-106 3.33e-03

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


Pssm-ID: 442625 [Multi-domain]  Cd Length: 159  Bit Score: 36.01  E-value: 3.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 697053878  49 VMLVLWEQDDVTVSDIGERLFLDSATLTPLLKRLESGGLINRhrsRKDERQVAVTLSE 106
Cdd:COG3398  102 ILLYLLENPGATNKELAEELGISRSTVSWHLKRLEEDGLVER---ERDGRNVRYYLNP 156
HTH_DTXR smart00529
Helix-turn-helix diphteria tox regulatory element; iron dependent repressor
 61-111 4.46e-03

Helix-turn-helix diphteria tox regulatory element; iron dependent repressor


Pssm-ID: 197774 [Multi-domain]  Cd Length: 95  Bit Score: 34.50  E-value: 4.46e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 697053878    61 VSDIGERLFLDSATLTPLLKRLESGGLINRHRSRKderqvaVTLSEAGREL 111
Cdd:smart00529   1 TSEIAERLNVSPPTVTEMLKKLEKMGLVEYEPYRG------ITLTEKGRRL 45
PRK11050 PRK11050
manganese-binding transcriptional regulator MntR;
63-115 6.79e-03

manganese-binding transcriptional regulator MntR;


Pssm-ID: 182927 [Multi-domain]  Cd Length: 152  Bit Score: 34.99  E-value: 6.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 697053878  63 DIGERLFLDSATLTPLLKRLESGGLINRHRSRkderqvAVTLSEAGRELQQQA 115
Cdd:PRK11050  56 DIAARLGVSQPTVAKMLKRLARDGLVEMRPYR------GVFLTPEGEKLAQES 102
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 56-109 7.66e-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: 7.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 697053878  56 QDDVTVSDIGERLFLDSATLTPLLKRLESGGLInrhRSRKDERQVAVTLSEAGR 109
Cdd:cd00090   18 EGPLTVSELAERLGLSQSTVSRHLKKLEEAGLV---ESRREGRRVYYSLTDAER 68
 
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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