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Conserved domains on  [gi|488377842|ref|WP_002447227|]
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MULTISPECIES: MarR family winged helix-turn-helix transcriptional regulator [Staphylococcus]

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];
1-140 2.38e-15

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


:

Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 68.07  E-value: 2.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377842   1 MVRRIEDHISFLEKFINDVNTLTAKLLKDLQTEYGISAEQSHVLNMLSI-EALTVGQITEKQGVNKAAVSRRVKKLLNAE 79
Cdd:COG1846    1 MSDEPDPAEERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEaGGLTQSELAERLGLTKSTVSRLLDRLEEKG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488377842  80 LVklEKPHSNTDQRLKIIKLSNKGKKYIKERKAIMSHIASDMTSDFDSKEIEKVRQVLEII 140
Cdd:COG1846   81 LV--EREPDPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRL 139
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
1-140 2.38e-15

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 68.07  E-value: 2.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377842   1 MVRRIEDHISFLEKFINDVNTLTAKLLKDLQTEYGISAEQSHVLNMLSI-EALTVGQITEKQGVNKAAVSRRVKKLLNAE 79
Cdd:COG1846    1 MSDEPDPAEERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEaGGLTQSELAERLGLTKSTVSRLLDRLEEKG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488377842  80 LVklEKPHSNTDQRLKIIKLSNKGKKYIKERKAIMSHIASDMTSDFDSKEIEKVRQVLEII 140
Cdd:COG1846   81 LV--EREPDPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRL 139
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
33-130 3.62e-13

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 61.46  E-value: 3.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377842    33 EYGISAEQSHVLNMLS-IEALTVGQITEKQGVNKAAVSRRVKKLLNAELVklEKPHSNTDQRLKIIKLSNKGKKYIKERK 111
Cdd:smart00347   5 PLGLTPTQFLVLRILYeEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLV--RREPSPEDRRSVLVSLTEEGRELIEQLL 82

                           90
                   ....*....|....*....
gi 488377842   112 AIMSHIASDMTSDFDSKEI 130
Cdd:smart00347  83 EARSETLAELLAGLTAEEQ 101
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 34-93 1.61e-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: 45.66  E-value: 1.61e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488377842   34 YGISAEQSHVLNMLSI-EALTVGQITEKQGVNKAAVSRRVKKLLNAELVKLEKphSNTDQR 93
Cdd:pfam12802   1 LGLTPAQFRVLLALARnPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREP--SPADRR 59
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 43-85 1.96e-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: 38.05  E-value: 1.96e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 488377842  43 VLNMLSIEALTVGQITEKQGVNKAAVSRRVKKLLNAELVKLEK 85
Cdd:cd00090   12 ILRLLLEGPLTVSELAERLGLSQSTVSRHLKKLEEAGLVESRR 54
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
1-140 2.38e-15

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 68.07  E-value: 2.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377842   1 MVRRIEDHISFLEKFINDVNTLTAKLLKDLQTEYGISAEQSHVLNMLSI-EALTVGQITEKQGVNKAAVSRRVKKLLNAE 79
Cdd:COG1846    1 MSDEPDPAEERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEaGGLTQSELAERLGLTKSTVSRLLDRLEEKG 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488377842  80 LVklEKPHSNTDQRLKIIKLSNKGKKYIKERKAIMSHIASDMTSDFDSKEIEKVRQVLEII 140
Cdd:COG1846   81 LV--EREPDPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRL 139
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
33-130 3.62e-13

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 61.46  E-value: 3.62e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377842    33 EYGISAEQSHVLNMLS-IEALTVGQITEKQGVNKAAVSRRVKKLLNAELVklEKPHSNTDQRLKIIKLSNKGKKYIKERK 111
Cdd:smart00347   5 PLGLTPTQFLVLRILYeEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLV--RREPSPEDRRSVLVSLTEEGRELIEQLL 82

                           90
                   ....*....|....*....
gi 488377842   112 AIMSHIASDMTSDFDSKEI 130
Cdd:smart00347  83 EARSETLAELLAGLTAEEQ 101
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 34-93 1.61e-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: 45.66  E-value: 1.61e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488377842   34 YGISAEQSHVLNMLSI-EALTVGQITEKQGVNKAAVSRRVKKLLNAELVKLEKphSNTDQR 93
Cdd:pfam12802   1 LGLTPAQFRVLLALARnPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREP--SPADRR 59
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 43-85 1.96e-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: 38.05  E-value: 1.96e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 488377842  43 VLNMLSIEALTVGQITEKQGVNKAAVSRRVKKLLNAELVKLEK 85
Cdd:cd00090   12 ILRLLLEGPLTVSELAERLGLSQSTVSRHLKKLEEAGLVESRR 54
ArsR COG0640
DNA-binding transcriptional regulator, ArsR family [Transcription];
43-85 2.04e-04

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


Pssm-ID: 440405 [Multi-domain]  Cd Length: 92  Bit Score: 38.33  E-value: 2.04e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 488377842  43 VLNMLSIEALTVGQITEKQGVNKAAVSRRVKKLLNAELVKLEK 85
Cdd:COG0640   25 ILRLLAEGELCVGELAEALGLSQSTVSHHLKVLREAGLVTSRR 67
HTH_ARSR smart00418
helix_turn_helix, Arsenical Resistance Operon Repressor;
43-85 2.61e-04

helix_turn_helix, Arsenical Resistance Operon Repressor;


Pssm-ID: 197713 [Multi-domain]  Cd Length: 66  Bit Score: 37.19  E-value: 2.61e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 488377842    43 VLNMLSIEALTVGQITEKQGVNKAAVSRRVKKLLNAELVKLEK 85
Cdd:smart00418   2 ILKLLAEGELCVCELAEILGLSQSTVSHHLKKLREAGLVESRR 44
HTH_5 pfam01022
Bacterial regulatory protein, arsR family; Members of this family contains a DNA binding ...
 43-81 3.86e-04

Bacterial regulatory protein, arsR family; Members of this family contains a DNA binding 'helix-turn-helix' motif. This family includes other proteins which are not included in the Prosite definition.


Pssm-ID: 425993 [Multi-domain]  Cd Length: 45  Bit Score: 36.27  E-value: 3.86e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 488377842   43 VLNMLSIEALTVGQITEKQGVNKAAVSRRVKKLLNAELV 81
Cdd:pfam01022   7 ILKLLAEGELCVCELAEELGLSQSTVSHHLKKLREAGLV 45
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 36-93 4.83e-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: 4.83e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488377842   36 ISAEQSHVLNMLS-IEALTVGQITEKQGVNKAAVSRRVKKLLNAELVklEKPHSNTDQR 93
Cdd:pfam01047   1 LTLTQFHILRILYeHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLI--ERSRSPEDRR 57
COG3355 COG3355
Predicted transcriptional regulator [Transcription];
13-151 2.08e-03

Predicted transcriptional regulator [Transcription];


Pssm-ID: 442583 [Multi-domain]  Cd Length: 131  Bit Score: 36.10  E-value: 2.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488377842  13 EKFINDVNTLTAKLLKDLQTEYGISAEQSHVLNML--SIEALTVGQITEKQGVNKAAVSRRVKKLLNAELVklekphsnt 90
Cdd:COG3355    2 SDSIEMLVRLEPDLEDVLECVYGLSETDAEVYLILleNGEPLTVEELAEALDRSRSTVYRSLQKLLEAGLV--------- 72

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488377842  91 dQRLKIIkLSNKGKKYIkeRKAI-MSHIASDMTSDFDskeiEKVRQVLEIIDYRIQSYTSKL 151
Cdd:COG3355   73 -EREKRN-LEGGGYPYV--YYAIdPEELKEKLVDDLD----EWYEKVGELIEEFEEEKADPL 126
 
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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