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Conserved domains on  [gi|499594376|ref|WP_011275110|]
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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];
4-138 1.30e-17

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


:

Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 73.85  E-value: 1.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594376   4 NEFFNSFIGLYRPYMKRTQSILDQFDLHPGQWLILRDIASTSPTTLVHISKRRFIEKPTTRKIIKVLSDRELLIVEPSKE 83
Cdd:COG1846   10 ERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPE 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499594376  84 DKREKLLSLSDKGQTLYVDVYRKILPVQRELIknARLSDVELENVISVMNKLHHA 138
Cdd:COG1846   90 DRRAVLVRLTEKGRALLEEARPALEALLAELL--AGLSEEELEALLRLLRRLAEN 142
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
4-138 1.30e-17

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 73.85  E-value: 1.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594376   4 NEFFNSFIGLYRPYMKRTQSILDQFDLHPGQWLILRDIASTSPTTLVHISKRRFIEKPTTRKIIKVLSDRELLIVEPSKE 83
Cdd:COG1846   10 ERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPE 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499594376  84 DKREKLLSLSDKGQTLYVDVYRKILPVQRELIknARLSDVELENVISVMNKLHHA 138
Cdd:COG1846   90 DRRAVLVRLTEKGRALLEEARPALEALLAELL--AGLSEEELEALLRLLRRLAEN 142
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
24-125 4.06e-12

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 58.37  E-value: 4.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594376    24 ILDQFDLHPGQWLILRDIASTSPTTLVHISKRRFIEKPTTRKIIKVLSDRELLIVEPSKEDKREKLLSLSDKGQTLYVDV 103
Cdd:smart00347   2 ELKPLGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQL 81

                           90       100
                   ....*....|....*....|..
gi 499594376   104 YRKILPVQRELIknARLSDVEL 125
Cdd:smart00347  82 LEARSETLAELL--AGLTAEEQ 101
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 28-87 5.65e-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: 49.12  E-value: 5.65e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594376   28 FDLHPGQWLILRDIASTSPTTLVHISKRRFIEKPTTRKIIKVLSDRELLIVEPSKEDKRE 87
Cdd:pfam12802   1 LGLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRRA 60
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
4-138 1.30e-17

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 73.85  E-value: 1.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594376   4 NEFFNSFIGLYRPYMKRTQSILDQFDLHPGQWLILRDIASTSPTTLVHISKRRFIEKPTTRKIIKVLSDRELLIVEPSKE 83
Cdd:COG1846   10 ERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPE 89

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499594376  84 DKREKLLSLSDKGQTLYVDVYRKILPVQRELIknARLSDVELENVISVMNKLHHA 138
Cdd:COG1846   90 DRRAVLVRLTEKGRALLEEARPALEALLAELL--AGLSEEELEALLRLLRRLAEN 142
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
24-125 4.06e-12

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 58.37  E-value: 4.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594376    24 ILDQFDLHPGQWLILRDIASTSPTTLVHISKRRFIEKPTTRKIIKVLSDRELLIVEPSKEDKREKLLSLSDKGQTLYVDV 103
Cdd:smart00347   2 ELKPLGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQL 81

                           90       100
                   ....*....|....*....|..
gi 499594376   104 YRKILPVQRELIknARLSDVEL 125
Cdd:smart00347  82 LEARSETLAELL--AGLTAEEQ 101
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 28-87 5.65e-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: 49.12  E-value: 5.65e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594376   28 FDLHPGQWLILRDIASTSPTTLVHISKRRFIEKPTTRKIIKVLSDRELLIVEPSKEDKRE 87
Cdd:pfam12802   1 LGLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRRA 60
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 30-88 3.30e-05

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: 39.45  E-value: 3.30e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 499594376   30 LHPGQWLILRDIASTSPTTLVHISKRRFIEKPTTRKIIKVLSDRELLIVEPSKEDKREK 88
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
HTH_27 pfam13463
Winged helix DNA-binding domain;
34-96 1.10e-04

Winged helix DNA-binding domain;


Pssm-ID: 433228 [Multi-domain]  Cd Length: 68  Bit Score: 38.04  E-value: 1.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 499594376   34 QWLILRDIASTS-PTTLVHISKRRFIEKPTTRKIIKVLSDRELLIVEPSKEDKREKLLSLSDKG 96
Cdd:pfam13463   5 EALILHNIGHRGdPKTLADICFRLNVEDSHVSYSLKKLTEAGLVEREGSEEDGRETRVRLTAKG 68
MntR COG1321
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];
37-106 4.16e-03

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


Pssm-ID: 440932 [Multi-domain]  Cd Length: 135  Bit Score: 35.18  E-value: 4.16e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499594376  37 ILRDIASTSPTTLVHISKRRFIEKPTTRKIIKVLSDRELLIVEPSKEdkreklLSLSDKGQTLYVDVYRK 106
Cdd:COG1321   15 IYELSEEGGPVRTSDIAERLGVSPPSVTEMLKKLEEKGLVEYEPYGG------ITLTEEGRELALRIVRR 78
 
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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