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Conserved domains on  [gi|446574570|ref|WP_000651916|]
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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 1.45e-17

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


:

Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 73.47  E-value: 1.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574570  20 EDNLSHQAIRILQIVSREKEITIGKVATELTLSHNTASEHVKRLIQKGFIIKERNKQDERVVNLTLTKEGIEVLEKHTLL 99
Cdd:COG1846   33 ELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGRALLEEARPA 112

                         90       100
                 ....*....|....*....|....*....
gi 446574570 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 1.45e-17

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 73.47  E-value: 1.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574570  20 EDNLSHQAIRILQIVSREKEITIGKVATELTLSHNTASEHVKRLIQKGFIIKERNKQDERVVNLTLTKEGIEVLEKHTLL 99
Cdd:COG1846   33 ELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGRALLEEARPA 112

                         90       100
                 ....*....|....*....|....*....
gi 446574570 100 DKEKIKILESQLSKEEQQLIEKAFSLLAK 128
Cdd:COG1846  113 LEALLAELLAGLSEEELEALLRLLRRLAE 141
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
22-116 1.81e-15

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 66.85  E-value: 1.81e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574570    22 NLSHQAIRILQIVSREKEITIGKVATELTLSHNTASEHVKRLIQKGFIIKERNKQDERVVNLTLTKEGIEVLEKHTLLDK 101
Cdd:smart00347   7 GLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLLEARS 86

                           90
                   ....*....|....*
gi 446574570   102 EKIKILESQLSKEEQ 116
Cdd:smart00347  87 ETLAELLAGLTAEEQ 101
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 22-79 6.88e-08

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: 46.04  E-value: 6.88e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446574570   22 NLSHQAIRILQIVSREKEITIGKVATELTLSHNTASEHVKRLIQKGFIIKERNKQDER 79
Cdd:pfam12802   2 GLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRR 59
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 28-95 4.40e-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: 36.51  E-value: 4.40e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446574570  28 IRILQIVsREKEITIGKVATELTLSHNTASEHVKRLIQKGFIIKERNKQdERVVNLTLTKEGIEVLEK 95
Cdd:cd00090   10 LRILRLL-LEGPLTVSELAERLGLSQSTVSRHLKKLEEAGLVESRREGR-RVYYSLTDAERLLALLES 75
Staph_reg_Sar TIGR01889
staphylococcal accessory regulator family; This model represents a family of transcriptional ...
 18-95 3.12e-03

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: 34.92  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574570   18 EYEDNLSHQAIRILQIVSR----EKEITIGKVATELTLSHNTASEHVKRLIQKGFIIKERNKQDERVVNLTLTKEGIEVL 93
Cdd:TIGR01889  18 KKEFNLSLEELLILYYLGKlennEGKLTLKEIIKEILIKQSALVKIIKKLSKKGYLSKERSEDDERKVIISINKEQRSKI 97


                  ..
gi 446574570   94 EK 95
Cdd:TIGR01889  98 ES 99
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
20-128 1.45e-17

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 73.47  E-value: 1.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574570  20 EDNLSHQAIRILQIVSREKEITIGKVATELTLSHNTASEHVKRLIQKGFIIKERNKQDERVVNLTLTKEGIEVLEKHTLL 99
Cdd:COG1846   33 ELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGRALLEEARPA 112

                         90       100
                 ....*....|....*....|....*....
gi 446574570 100 DKEKIKILESQLSKEEQQLIEKAFSLLAK 128
Cdd:COG1846  113 LEALLAELLAGLSEEELEALLRLLRRLAE 141
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
22-116 1.81e-15

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 66.85  E-value: 1.81e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574570    22 NLSHQAIRILQIVSREKEITIGKVATELTLSHNTASEHVKRLIQKGFIIKERNKQDERVVNLTLTKEGIEVLEKHTLLDK 101
Cdd:smart00347   7 GLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLLEARS 86

                           90
                   ....*....|....*
gi 446574570   102 EKIKILESQLSKEEQ 116
Cdd:smart00347  87 ETLAELLAGLTAEEQ 101
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 22-79 6.88e-08

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: 46.04  E-value: 6.88e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446574570   22 NLSHQAIRILQIVSREKEITIGKVATELTLSHNTASEHVKRLIQKGFIIKERNKQDER 79
Cdd:pfam12802   2 GLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRR 59
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 23-81 1.54e-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: 45.23  E-value: 1.54e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446574570   23 LSHQAIRILQIVSREKEITIGKVATELTLSHNTASEHVKRLIQKGFIIKERNKQDERVV 81
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
MntR COG1321
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];
30-99 7.51e-06

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


Pssm-ID: 440932 [Multi-domain]  Cd Length: 135  Bit Score: 42.50  E-value: 7.51e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446574570  30 ILQIVSREKEITIGKVATELTLSHNTASEHVKRLIQKGFIIKERNKqdervvNLTLTKEGIE----VLEKHTLL 99
Cdd:COG1321   15 IYELSEEGGPVRTSDIAERLGVSPPSVTEMLKKLEEKGLVEYEPYG------GITLTEEGRElalrIVRRHRLL 82
HTH_24 pfam13412
Winged helix-turn-helix DNA-binding;
28-69 3.96e-04

Winged helix-turn-helix DNA-binding;


Pssm-ID: 404317 [Multi-domain]  Cd Length: 45  Bit Score: 35.87  E-value: 3.96e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 446574570   28 IRILQIVSREKEITIGKVATELTLSHNTASEHVKRLIQKGFI 69
Cdd:pfam13412   4 RKILNLLQENPRISQRELAERLGLSPSTVNRRLKRLEEEGVI 45
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 28-95 4.40e-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: 36.51  E-value: 4.40e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446574570  28 IRILQIVsREKEITIGKVATELTLSHNTASEHVKRLIQKGFIIKERNKQdERVVNLTLTKEGIEVLEK 95
Cdd:cd00090   10 LRILRLL-LEGPLTVSELAERLGLSQSTVSRHLKKLEEAGLVESRREGR-RVYYSLTDAERLLALLES 75
HTH_20 pfam12840
Helix-turn-helix domain; This domain represents a DNA-binding Helix-turn-helix domain found in ...
 29-73 1.01e-03

Helix-turn-helix domain; This domain represents a DNA-binding Helix-turn-helix domain found in transcriptional regulatory proteins.


Pssm-ID: 432824 [Multi-domain]  Cd Length: 61  Bit Score: 35.21  E-value: 1.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 446574570   29 RILQIVSREKEITIGKVATELTLSHNTASEHVKRLIQKGFIIKER 73
Cdd:pfam12840  14 RILRALVGDEPLTASELARRLDISRNTLSYHLRKLEEAGLVEVVR 58
COG2345 COG2345
Predicted transcriptional regulator, ArsR family [Transcription];
29-69 1.64e-03

Predicted transcriptional regulator, ArsR family [Transcription];


Pssm-ID: 441914 [Multi-domain]  Cd Length: 217  Bit Score: 36.82  E-value: 1.64e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 446574570  29 RILQIVSREKEITIGKVATELTLSHNTASEHVKRLIQKGFI 69
Cdd:COG2345   17 RILELLKRAGPVTAAELAEALGLTPNAVRRHLDALEEEGLV 57
COG4189 COG4189
Predicted transcriptional regulator, ArsR family [Transcription];
23-93 1.70e-03

Predicted transcriptional regulator, ArsR family [Transcription];


Pssm-ID: 443343 [Multi-domain]  Cd Length: 97  Bit Score: 35.32  E-value: 1.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446574570  23 LSHQA-IRILQIVSREkEITIGKVATELTLSHNTASEHVKRLIQKGFI-IKERNKQDERVVNLTLTKEGIEVL 93
Cdd:COG4189   16 LASETrLRILRLLAEE-PLNVNELAEALGLPKSTVSYHIRKLEEAGLIrTEYKPGKRGRQKICYLRVDKILIV 87
COG3398 COG3398
Predicted transcriptional regulator, contains two HTH domains [Transcription];
29-86 2.75e-03

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


Pssm-ID: 442625 [Multi-domain]  Cd Length: 159  Bit Score: 35.62  E-value: 2.75e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446574570  29 RILQIVSREKEITIGKVATELTLSHNTASEHVKRLIQKGFIIKERnkqDERVVNLTLT 86
Cdd:COG3398  101 RILLYLLENPGATNKELAEELGISRSTVSWHLKRLEEDGLVERER---DGRNVRYYLN 155
Staph_reg_Sar TIGR01889
staphylococcal accessory regulator family; This model represents a family of transcriptional ...
 18-95 3.12e-03

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: 34.92  E-value: 3.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446574570   18 EYEDNLSHQAIRILQIVSR----EKEITIGKVATELTLSHNTASEHVKRLIQKGFIIKERNKQDERVVNLTLTKEGIEVL 93
Cdd:TIGR01889  18 KKEFNLSLEELLILYYLGKlennEGKLTLKEIIKEILIKQSALVKIIKKLSKKGYLSKERSEDDERKVIISINKEQRSKI 97


                  ..
gi 446574570   94 EK 95
Cdd:TIGR01889  98 ES 99
Rfk COG1339
Archaeal CTP-dependent riboflavin kinase [Coenzyme transport and metabolism]; Archaeal ...
 34-95 3.59e-03

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: 35.98  E-value: 3.59e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446574570  34 VSREKEITIGKVATELTLSHNTASEHVKRLIQKGFIIKERNKQDERVvnlTLTKEGIEVLEK 95
Cdd:COG1339   17 LKGPVKISSSELAKRLGISQQTASRRLQELEDAGLIERDLVGDGQWV---KITEKGEELLRR 75
 
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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