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Conserved domains on  [gi|492476588|ref|WP_005857644|]
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MULTISPECIES: MarR family winged helix-turn-helix transcriptional regulator [Parabacteroides]

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];
7-139 1.91e-25

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


:

Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 93.88  E-value: 1.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492476588   7 FRELMLQVVRTRMAFRRSMQRTLKKnnAGITFEMLQILSCLWHEQGITQQVLAERTAKDKACLTNLMNNLEKKGYVHRKE 86
Cdd:COG1846    9 EERLGLLLRRLARALRRALDRALAE--LGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREP 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 492476588  87 DPEDRRNKLVFLTPEGEEFKKQIRPILDQVYVHAEHIIGIENVETMLSELKAV 139
Cdd:COG1846   87 DPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRL 139
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
7-139 1.91e-25

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 93.88  E-value: 1.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492476588   7 FRELMLQVVRTRMAFRRSMQRTLKKnnAGITFEMLQILSCLWHEQGITQQVLAERTAKDKACLTNLMNNLEKKGYVHRKE 86
Cdd:COG1846    9 EERLGLLLRRLARALRRALDRALAE--LGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREP 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 492476588  87 DPEDRRNKLVFLTPEGEEFKKQIRPILDQVYVHAEHIIGIENVETMLSELKAV 139
Cdd:COG1846   87 DPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRL 139
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
35-117 7.06e-20

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 78.40  E-value: 7.06e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492476588    35 GITFEMLQILSCLWHEQGITQQVLAERTAKDKACLTNLMNNLEKKGYVHRKEDPEDRRNKLVFLTPEGEEFKKQIRPILD 114
Cdd:smart00347   7 GLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLLEARS 86

                   ...
gi 492476588   115 QVY 117
Cdd:smart00347  87 ETL 89
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
43-94 4.55e-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: 426012 [Multi-domain]  Cd Length: 59  Bit Score: 49.47  E-value: 4.55e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 492476588   43 ILSCLWHEQGITQQVLAERTAKDKACLTNLMNNLEKKGYVHRKEDPEDRRNK 94
Cdd:pfam01047   8 ILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
PRK11512 PRK11512
multiple antibiotic resistance transcriptional regulator MarR;
36-115 2.10e-04

multiple antibiotic resistance transcriptional regulator MarR;


Pssm-ID: 183170  Cd Length: 144  Bit Score: 39.11  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492476588  36 ITFEMLQILSCLWHEQGITQQVLAERTAKDKACLTNLMNNLEKKGYVHRKEDPEDRRNKLVFLTPEGEEFKKQIRPILDQ 115
Cdd:PRK11512  38 ITAAQFKVLCSIRCAACITPVELKKVLSVDLGALTRMLDRLVCKGWVERLPNPNDKRGVLVKLTTSGAAICEQCHQLVGQ 117
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
7-139 1.91e-25

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 93.88  E-value: 1.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492476588   7 FRELMLQVVRTRMAFRRSMQRTLKKnnAGITFEMLQILSCLWHEQGITQQVLAERTAKDKACLTNLMNNLEKKGYVHRKE 86
Cdd:COG1846    9 EERLGLLLRRLARALRRALDRALAE--LGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREP 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 492476588  87 DPEDRRNKLVFLTPEGEEFKKQIRPILDQVYVHAEHIIGIENVETMLSELKAV 139
Cdd:COG1846   87 DPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRL 139
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
35-117 7.06e-20

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 78.40  E-value: 7.06e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492476588    35 GITFEMLQILSCLWHEQGITQQVLAERTAKDKACLTNLMNNLEKKGYVHRKEDPEDRRNKLVFLTPEGEEFKKQIRPILD 114
Cdd:smart00347   7 GLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLLEARS 86

                   ...
gi 492476588   115 QVY 117
Cdd:smart00347  87 ETL 89
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
43-94 4.55e-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: 426012 [Multi-domain]  Cd Length: 59  Bit Score: 49.47  E-value: 4.55e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 492476588   43 ILSCLWHEQGITQQVLAERTAKDKACLTNLMNNLEKKGYVHRKEDPEDRRNK 94
Cdd:pfam01047   8 ILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
35-92 8.65e-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: 48.74  E-value: 8.65e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 492476588   35 GITFEMLQILSCLWHEQGITQQVLAERTAKDKACLTNLMNNLEKKGYVHRKEDPEDRR 92
Cdd:pfam12802   2 GLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRR 59
HTH_27 pfam13463
Winged helix DNA-binding domain;
42-102 2.27e-05

Winged helix DNA-binding domain;


Pssm-ID: 433228 [Multi-domain]  Cd Length: 68  Bit Score: 39.96  E-value: 2.27e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492476588   42 QILSCLWHEQGI-TQQVLAERTAKDKACLTNLMNNLEKKGYVHRKEDPEDRRNKLVFLTPEG 102
Cdd:pfam13463   7 LILHNIGHRGDPkTLADICFRLNVEDSHVSYSLKKLTEAGLVEREGSEEDGRETRVRLTAKG 68
PRK11512 PRK11512
multiple antibiotic resistance transcriptional regulator MarR;
36-115 2.10e-04

multiple antibiotic resistance transcriptional regulator MarR;


Pssm-ID: 183170  Cd Length: 144  Bit Score: 39.11  E-value: 2.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492476588  36 ITFEMLQILSCLWHEQGITQQVLAERTAKDKACLTNLMNNLEKKGYVHRKEDPEDRRNKLVFLTPEGEEFKKQIRPILDQ 115
Cdd:PRK11512  38 ITAAQFKVLCSIRCAACITPVELKKVLSVDLGALTRMLDRLVCKGWVERLPNPNDKRGVLVKLTTSGAAICEQCHQLVGQ 117
PRK10870 PRK10870
transcriptional repressor MprA; Provisional
70-111 5.98e-04

transcriptional repressor MprA; Provisional


Pssm-ID: 182795  Cd Length: 176  Bit Score: 38.19  E-value: 5.98e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 492476588  70 TNLMNNLEKKGYVHRKEDPEDRRNKLVFLTPEGEEFKKQIRP 111
Cdd:PRK10870  89 TRIADELEKRGWIERRESDNDRRCLHLQLTEKGHEFLREVLP 130
HTH_24 pfam13412
Winged helix-turn-helix DNA-binding;
41-82 3.63e-03

Winged helix-turn-helix DNA-binding;


Pssm-ID: 404317 [Multi-domain]  Cd Length: 45  Bit Score: 33.56  E-value: 3.63e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 492476588   41 LQILSCLWHEQGITQQVLAERTAKDKACLTNLMNNLEKKGYV 82
Cdd:pfam13412   4 RKILNLLQENPRISQRELAERLGLSPSTVNRRLKRLEEEGVI 45
COG3398 COG3398
Predicted transcriptional regulator, contains two HTH domains [Transcription];
43-101 3.91e-03

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


Pssm-ID: 442625 [Multi-domain]  Cd Length: 159  Bit Score: 35.62  E-value: 3.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492476588  43 ILSCLWHEQGITQQVLAERTAKDKACLTNLMNNLEKKGYVHRKedpEDRRNKLVFLTPE 101
Cdd:COG3398  102 ILLYLLENPGATNKELAEELGISRSTVSWHLKRLEEDGLVERE---RDGRNVRYYLNPP 157
PRK13777 PRK13777
HTH-type transcriptional regulator Hpr;
71-104 7.99e-03

HTH-type transcriptional regulator Hpr;


Pssm-ID: 237501  Cd Length: 185  Bit Score: 35.02  E-value: 7.99e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 492476588  71 NLMNNLEKKGYVH--RKEDpeDRRNKLVFLTPEGEE 104
Cdd:PRK13777  78 NFSKKLEERGYLTfsKKED--DKRNTYIELTEKGEE 111
 
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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