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Conserved domains on  [gi|2753918731|dbj|GAB0346057|]
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MarR family transcriptional regulator [Staphylococcus pseudintermedius]

Protein Classification

MarR family transcriptional regulator( domain architecture ID 12204203)

MarR family transcriptional regulator is a winged helix-turn-helix domain-containing protein, named for an Escherichia coli regulator of an operon that encodes a drug efflux pump

Gene Ontology:  GO:0003677|GO:0003700
PubMed:  10498949

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
34-132 8.02e-19

helix_turn_helix multiple antibiotic resistance protein;


:

Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 76.09  E-value: 8.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753918731   34 LNLSLTQFHIIELIANNDKVNNKFLADKLNISNPAVTKSIKKLLSKDLVLELQNAQNKREVHYKLTKKGKKLssiHDELH 113
Cdd:smart00347   6 LGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGREL---IEQLL 82

                           90
                   ....*....|....*....
gi 2753918731  114 NQAVKKYEEVLKVFNEKEL 132
Cdd:smart00347  83 EARSETLAELLAGLTAEEQ 101
 
Name Accession Description Interval E-value
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
34-132 8.02e-19

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 76.09  E-value: 8.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753918731   34 LNLSLTQFHIIELIANNDKVNNKFLADKLNISNPAVTKSIKKLLSKDLVLELQNAQNKREVHYKLTKKGKKLssiHDELH 113
Cdd:smart00347   6 LGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGREL---IEQLL 82

                           90
                   ....*....|....*....
gi 2753918731  114 NQAVKKYEEVLKVFNEKEL 132
Cdd:smart00347  83 EARSETLAELLAGLTAEEQ 101
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
32-141 5.66e-18

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 75.39  E-value: 5.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753918731  32 EGLNLSLTQFHIIELIANNDKVNNKFLADKLNISNPAVTKSIKKLLSKDLVLELQNAQNKREVHYKLTKKGKKLssiHDE 111
Cdd:COG1846    32 AELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGRAL---LEE 108

                          90       100       110
                  ....*....|....*....|....*....|
gi 2753918731 112 LHNQAVKKYEEVLKVFNEKELDVIVEFLSR 141
Cdd:COG1846   109 ARPALEALLAELLAGLSEEELEALLRLLRR 138
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 36-94 7.67e-11

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: 54.48  E-value: 7.67e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2753918731  36 LSLTQFHIIELIANNDKVNNKFLADKLNISNPAVTKSIKKLLSKDLVLELQNAQNKREV 94
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 43-113 7.81e-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: 33.81  E-value: 7.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753918731  43 IIELIANNDKvNNKFLADKLNISNPAVTKSIKKLLSKDLVLElqnAQNKREVHYKLTKKGKKLSSIHDELH 113
Cdd:cd00090    12 ILRLLLEGPL-TVSELAERLGLSQSTVSRHLKKLEEAGLVES---RREGRRVYYSLTDAERLLALLESLLE 78
 
Name Accession Description Interval E-value
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
34-132 8.02e-19

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 76.09  E-value: 8.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753918731   34 LNLSLTQFHIIELIANNDKVNNKFLADKLNISNPAVTKSIKKLLSKDLVLELQNAQNKREVHYKLTKKGKKLssiHDELH 113
Cdd:smart00347   6 LGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGREL---IEQLL 82

                           90
                   ....*....|....*....
gi 2753918731  114 NQAVKKYEEVLKVFNEKEL 132
Cdd:smart00347  83 EARSETLAELLAGLTAEEQ 101
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
32-141 5.66e-18

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 75.39  E-value: 5.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753918731  32 EGLNLSLTQFHIIELIANNDKVNNKFLADKLNISNPAVTKSIKKLLSKDLVLELQNAQNKREVHYKLTKKGKKLssiHDE 111
Cdd:COG1846    32 AELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGRAL---LEE 108

                          90       100       110
                  ....*....|....*....|....*....|
gi 2753918731 112 LHNQAVKKYEEVLKVFNEKELDVIVEFLSR 141
Cdd:COG1846   109 ARPALEALLAELLAGLSEEELEALLRLLRR 138
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 36-94 7.67e-11

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: 54.48  E-value: 7.67e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2753918731  36 LSLTQFHIIELIANNDKVNNKFLADKLNISNPAVTKSIKKLLSKDLVLELQNAQNKREV 94
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 34-93 7.79e-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: 44.12  E-value: 7.79e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2753918731  34 LNLSLTQFHIIELIANNDKVNNKFLADKLNISNPAVTKSIKKLLSKDLVLELQNAQNKRE 93
Cdd:pfam12802   1 LGLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRRA 60
MntR COG1321
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];
43-105 2.45e-06

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


Pssm-ID: 440932 [Multi-domain]  Cd Length: 135  Bit Score: 44.42  E-value: 2.45e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2753918731  43 IIELIANNDKVNNKFLADKLNISNPAVTKSIKKLLSKDLVLelqnaQNKREvHYKLTKKGKKL 105
Cdd:COG1321    15 IYELSEEGGPVRTSDIAERLGVSPPSVTEMLKKLEEKGLVE-----YEPYG-GITLTEEGREL 71
HTH_27 pfam13463
Winged helix DNA-binding domain;
58-102 6.97e-05

Winged helix DNA-binding domain;


Pssm-ID: 433228 [Multi-domain]  Cd Length: 68  Bit Score: 38.81  E-value: 6.97e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2753918731  58 LADKLNISNPAVTKSIKKLLSKDLVLELQNAQNKREVHYKLTKKG 102
Cdd:pfam13463  24 ICFRLNVEDSHVSYSLKKLTEAGLVEREGSEEDGRETRVRLTAKG 68
HTH_24 pfam13412
Winged helix-turn-helix DNA-binding;
39-82 1.11e-04

Winged helix-turn-helix DNA-binding;


Pssm-ID: 404317 [Multi-domain]  Cd Length: 45  Bit Score: 37.80  E-value: 1.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2753918731  39 TQFHIIELIANNDKVNNKFLADKLNISNPAVTKSIKKLLSKDLV 82
Cdd:pfam13412   2 TDRKILNLLQENPRISQRELAERLGLSPSTVNRRLKRLEEEGVI 45
COG3398 COG3398
Predicted transcriptional regulator, contains two HTH domains [Transcription];
43-82 1.70e-03

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


Pssm-ID: 442625 [Multi-domain]  Cd Length: 159  Bit Score: 36.78  E-value: 1.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2753918731  43 IIELIANNDKVNNKFLADKLNISNPAVTKSIKKLLSKDLV 82
Cdd:COG3398   102 ILLYLLENPGATNKELAEELGISRSTVSWHLKRLEEDGLV 141
HTH_DTXR smart00529
Helix-turn-helix diphteria tox regulatory element; iron dependent repressor
 55-107 5.44e-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: 5.44e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2753918731   55 NKFLADKLNISNPAVTKSIKKLLSKDLVlelqnaQNKREVHYKLTKKGKKLSS 107
Cdd:smart00529   1 TSEIAERLNVSPPTVTEMLKKLEKMGLV------EYEPYRGITLTEKGRRLAR 47
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 43-113 7.81e-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: 33.81  E-value: 7.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2753918731  43 IIELIANNDKvNNKFLADKLNISNPAVTKSIKKLLSKDLVLElqnAQNKREVHYKLTKKGKKLSSIHDELH 113
Cdd:cd00090    12 ILRLLLEGPL-TVSELAERLGLSQSTVSRHLKKLEEAGLVES---RREGRRVYYSLTDAERLLALLESLLE 78
WH_MUS81 cd21036
winged helix domain found in crossover junction endonuclease MUS81 and similar proteins; MUS81 ...
 72-105 7.98e-03

winged helix domain found in crossover junction endonuclease MUS81 and similar proteins; MUS81 is a crossover junction endonuclease that interacts with EME1 (essential meiotic structure-specific endonuclease 1) and EME2, to form a DNA structure-specific endonuclease with substrate preference for branched DNA structures with a 5'-end at the branch nick. The MUS80-EME1 endonuclease maintains genomic integrity in metazoans by cleaving branched DNA structures that can form during mitosis and fission yeast meiosis, and during processing of damaged replication folks. This model corresponds to the winged helix (WH) domain of MUS81, which is responsible for DNA binding. It comprises four helices and two beta strands.


Pssm-ID: 411029  Cd Length: 94  Bit Score: 34.05  E-value: 7.98e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2753918731  72 SIKKLLSKDLVLElqnaqNKREVHYKLTKKGKKL 105
Cdd:cd21036    59 SMKTLIKKGLVYK-----EGRPARYSLTEEGREL 87
 
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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