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Conserved domains on  [gi|951089233|ref|WP_057581437|]
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MULTISPECIES: MarR family winged helix-turn-helix transcriptional regulator [unclassified Streptomyces]

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];
9-149 1.32e-23

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


:

Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 90.03  E-value: 1.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951089233   9 NADERRAWLAYIEFSTLLSDHLNRQLRrDAGMTHADYSLLTYLSMAPENTlgMSDLAQRLKITRSRLTHAVSRLRDVGLV 88
Cdd:COG1846    6 DPAEERLGLLLRRLARALRRALDRALA-ELGLTPAQFRVLAALAEAGGLT--QSELAERLGLTKSTVSRLLDRLEEKGLV 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951089233  89 DRREDPADGRGQLAFLTDAGRALLEEVAPGHVEAVRRaVFDALTPEQVRQFAEIGEAISEA 149
Cdd:COG1846   83 EREPDPEDRRAVLVRLTEKGRALLEEARPALEALLAE-LLAGLSEEELEALLRLLRRLAEN 142
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
9-149 1.32e-23

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 90.03  E-value: 1.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951089233   9 NADERRAWLAYIEFSTLLSDHLNRQLRrDAGMTHADYSLLTYLSMAPENTlgMSDLAQRLKITRSRLTHAVSRLRDVGLV 88
Cdd:COG1846    6 DPAEERLGLLLRRLARALRRALDRALA-ELGLTPAQFRVLAALAEAGGLT--QSELAERLGLTKSTVSRLLDRLEEKGLV 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951089233  89 DRREDPADGRGQLAFLTDAGRALLEEVAPGHVEAVRRaVFDALTPEQVRQFAEIGEAISEA 149
Cdd:COG1846   83 EREPDPEDRRAVLVRLTEKGRALLEEARPALEALLAE-LLAGLSEEELEALLRLLRRLAEN 142
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
39-136 9.27e-15

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 66.08  E-value: 9.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951089233    39 GMTHADYSLLTYLSMAPenTLGMSDLAQRLKITRSRLTHAVSRLRDVGLVDRREDPADGRGQLAFLTDAGRALLEEVAPG 118
Cdd:smart00347   7 GLTPTQFLVLRILYEEG--PLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLLEA 84

                           90
                   ....*....|....*...
gi 951089233   119 HVEAvRRAVFDALTPEQV 136
Cdd:smart00347  85 RSET-LAELLAGLTAEEQ 101
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 39-99 1.51e-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: 51.44  E-value: 1.51e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951089233   39 GMTHADYSLLTYLSMAPENTlgMSDLAQRLKITRSRLTHAVSRLRDVGLVDRREDPADGRG 99
Cdd:pfam12802   2 GLTPAQFRVLLALARNPGLT--VAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRRA 60
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 62-111 1.25e-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: 36.12  E-value: 1.25e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 951089233  62 SDLAQRLKITRSRLTHAVSRLRDVGLVDRREdpaDGRGQLAFLTDAGRAL 111
Cdd:cd00090   24 SELAERLGLSQSTVSRHLKKLEEAGLVESRR---EGRRVYYSLTDAERLL 70
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
9-149 1.32e-23

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 90.03  E-value: 1.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951089233   9 NADERRAWLAYIEFSTLLSDHLNRQLRrDAGMTHADYSLLTYLSMAPENTlgMSDLAQRLKITRSRLTHAVSRLRDVGLV 88
Cdd:COG1846    6 DPAEERLGLLLRRLARALRRALDRALA-ELGLTPAQFRVLAALAEAGGLT--QSELAERLGLTKSTVSRLLDRLEEKGLV 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951089233  89 DRREDPADGRGQLAFLTDAGRALLEEVAPGHVEAVRRaVFDALTPEQVRQFAEIGEAISEA 149
Cdd:COG1846   83 EREPDPEDRRAVLVRLTEKGRALLEEARPALEALLAE-LLAGLSEEELEALLRLLRRLAEN 142
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
39-136 9.27e-15

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 66.08  E-value: 9.27e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951089233    39 GMTHADYSLLTYLSMAPenTLGMSDLAQRLKITRSRLTHAVSRLRDVGLVDRREDPADGRGQLAFLTDAGRALLEEVAPG 118
Cdd:smart00347   7 GLTPTQFLVLRILYEEG--PLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLLEA 84

                           90
                   ....*....|....*...
gi 951089233   119 HVEAvRRAVFDALTPEQV 136
Cdd:smart00347  85 RSET-LAELLAGLTAEEQ 101
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 39-99 1.51e-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: 51.44  E-value: 1.51e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951089233   39 GMTHADYSLLTYLSMAPENTlgMSDLAQRLKITRSRLTHAVSRLRDVGLVDRREDPADGRG 99
Cdd:pfam12802   2 GLTPAQFRVLLALARNPGLT--VAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRRA 60
MntR COG1321
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];
62-115 3.28e-05

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


Pssm-ID: 440932 [Multi-domain]  Cd Length: 135  Bit Score: 41.34  E-value: 3.28e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 951089233  62 SDLAQRLKITRSRLTHAVSRLRDVGLVDRREDpadgrgQLAFLTDAGRALLEEV 115
Cdd:COG1321   28 SDIAERLGVSPPSVTEMLKKLEEKGLVEYEPY------GGITLTEEGRELALRI 75
HTH_ARSR smart00418
helix_turn_helix, Arsenical Resistance Operon Repressor;
46-115 7.05e-05

helix_turn_helix, Arsenical Resistance Operon Repressor;


Pssm-ID: 197713 [Multi-domain]  Cd Length: 66  Bit Score: 39.12  E-value: 7.05e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951089233    46 SLLTYLSmapENTLGMSDLAQRLKITRSRLTHAVSRLRDVGLVDRREdpaDGRGQLAFLTD-AGRALLEEV 115
Cdd:smart00418   1 KILKLLA---EGELCVCELAEILGLSQSTVSHHLKKLREAGLVESRR---EGKRVYYSLTDeKVADLLEEL 65
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 40-98 5.71e-04

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: 36.37  E-value: 5.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 951089233   40 MTHADYSLLTYLSMAPEntLGMSDLAQRLKITRSRLTHAVSRLRDVGLVDRREDPADGR 98
Cdd:pfam01047   1 LTLTQFHILRILYEHGP--LTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRR 57
COG3355 COG3355
Predicted transcriptional regulator [Transcription];
39-99 9.71e-04

Predicted transcriptional regulator [Transcription];


Pssm-ID: 442583 [Multi-domain]  Cd Length: 131  Bit Score: 37.25  E-value: 9.71e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951089233  39 GMTHADYSLLTYLSMAPENtLGMSDLAQRLKITRSRLTHAVSRLRDVGLVDRREDPADGRG 99
Cdd:COG3355   24 GLSETDAEVYLILLENGEP-LTVEELAEALDRSRSTVYRSLQKLLEAGLVEREKRNLEGGG 83
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 62-111 1.25e-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: 36.12  E-value: 1.25e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 951089233  62 SDLAQRLKITRSRLTHAVSRLRDVGLVDRREdpaDGRGQLAFLTDAGRAL 111
Cdd:cd00090   24 SELAERLGLSQSTVSRHLKKLEEAGLVESRR---EGRRVYYSLTDAERLL 70
COG3398 COG3398
Predicted transcriptional regulator, contains two HTH domains [Transcription];
46-106 3.70e-03

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


Pssm-ID: 442625 [Multi-domain]  Cd Length: 159  Bit Score: 36.01  E-value: 3.70e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 951089233  46 SLLTYLSMAPENTLgmSDLAQRLKITRSRLTHAVSRLRDVGLVDRREdpaDGRGQLAFLTD 106
Cdd:COG3398  101 RILLYLLENPGATN--KELAEELGISRSTVSWHLKRLEEDGLVERER---DGRNVRYYLNP 156
COG4742 COG4742
Predicted transcriptional regulator, contains HTH domain [Transcription];
40-117 7.28e-03

Predicted transcriptional regulator, contains HTH domain [Transcription];


Pssm-ID: 443776 [Multi-domain]  Cd Length: 267  Bit Score: 35.64  E-value: 7.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 951089233  40 MTHADYSLLTYLSMAP----------ENTLGMSDLAQRLKITRSRLTHAVSRLRDVGLVDRREDpadgrgqlAF-LTDAG 108
Cdd:COG4742    1 MGSMKLDLLDFLFLSEkrknillllaEGPKTRSELAESLDVSRSTILRQLKELEERGLIERDDG--------EYeLTTLG 72


                 ....*....
gi 951089233 109 RALLEEVAP 117
Cdd:COG4742   73 RLVVEEMEP 81
 
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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