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Conserved domains on  [gi|612661263|gb|EZS77512|]
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hypothetical protein W490_01839 [Staphylococcus aureus VET0191R]

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];
24-141 1.33e-21

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


:

Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 84.64  E-value: 1.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612661263  24 RRQYKKENEELDLSLTQFHIIELIDNNDKVNNKFLSEMLNVSKPAITKSIKKLLAKGLVVESHNEFNKREVNYSLTQEGK 103
Cdd:COG1846   24 RRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGR 103

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 612661263 104 KLsyiHDELHEKAVKKYEEVLKVFDNDEMAVIVEFLNR 141
Cdd:COG1846  104 AL---LEEARPALEALLAELLAGLSEEELEALLRLLRR 138
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
24-141 1.33e-21

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 84.64  E-value: 1.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612661263  24 RRQYKKENEELDLSLTQFHIIELIDNNDKVNNKFLSEMLNVSKPAITKSIKKLLAKGLVVESHNEFNKREVNYSLTQEGK 103
Cdd:COG1846   24 RRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGR 103

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 612661263 104 KLsyiHDELHEKAVKKYEEVLKVFDNDEMAVIVEFLNR 141
Cdd:COG1846  104 AL---LEEARPALEALLAELLAGLSEEELEALLRLLRR 138
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
32-132 8.79e-20

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 78.79  E-value: 8.79e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612661263    32 EELDLSLTQFHIIELIDNNDKVNNKFLSEMLNVSKPAITKSIKKLLAKGLVVESHNEFNKREVNYSLTQEGKKLsyiHDE 111
Cdd:smart00347   4 KPLGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGREL---IEQ 80

                           90       100
                   ....*....|....*....|.
gi 612661263   112 LHEKAVKKYEEVLKVFDNDEM 132
Cdd:smart00347  81 LLEARSETLAELLAGLTAEEQ 101
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 36-94 4.02e-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: 55.25  E-value: 4.02e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 612661263   36 LSLTQFHIIELIDNNDKVNNKFLSEMLNVSKPAITKSIKKLLAKGLVVESHNEFNKREV 94
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
WH_MUS81 cd21036
winged helix domain found in crossover junction endonuclease MUS81 and similar proteins; MUS81 ...
 72-105 1.37e-04

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: 38.67  E-value: 1.37e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 612661263  72 SIKKLLAKGLVVESHNefNKRevnYSLTQEGKKL 105
Cdd:cd21036   59 SMKTLIKKGLVYKEGR--PAR---YSLTEEGREL 87
PRK11512 PRK11512
multiple antibiotic resistance transcriptional regulator MarR;
15-141 7.69e-04

multiple antibiotic resistance transcriptional regulator MarR;


Pssm-ID: 183170  Cd Length: 144  Bit Score: 37.57  E-value: 7.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612661263  15 IIERENADKRRQYKKENEELDLSLTQFHIIELIDNNDKVNNKFLSEMLNVSKPAITKSIKKLLAKGLVVESHNEFNKREV 94
Cdd:PRK11512  17 LIHMVNQKKDRLLNEYLSPLDITAAQFKVLCSIRCAACITPVELKKVLSVDLGALTRMLDRLVCKGWVERLPNPNDKRGV 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 612661263  95 NYSLTQEGkklSYIHDELHEKAVKK-YEEVLKVFDNDEMAVIVEFLNR 141
Cdd:PRK11512  97 LVKLTTSG---AAICEQCHQLVGQDlHQELTKNLTADEVATLEHLLKK 141
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
24-141 1.33e-21

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 84.64  E-value: 1.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612661263  24 RRQYKKENEELDLSLTQFHIIELIDNNDKVNNKFLSEMLNVSKPAITKSIKKLLAKGLVVESHNEFNKREVNYSLTQEGK 103
Cdd:COG1846   24 RRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRAVLVRLTEKGR 103

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 612661263 104 KLsyiHDELHEKAVKKYEEVLKVFDNDEMAVIVEFLNR 141
Cdd:COG1846  104 AL---LEEARPALEALLAELLAGLSEEELEALLRLLRR 138
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
32-132 8.79e-20

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 78.79  E-value: 8.79e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612661263    32 EELDLSLTQFHIIELIDNNDKVNNKFLSEMLNVSKPAITKSIKKLLAKGLVVESHNEFNKREVNYSLTQEGKKLsyiHDE 111
Cdd:smart00347   4 KPLGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGREL---IEQ 80

                           90       100
                   ....*....|....*....|.
gi 612661263   112 LHEKAVKKYEEVLKVFDNDEM 132
Cdd:smart00347  81 LLEARSETLAELLAGLTAEEQ 101
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 36-94 4.02e-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: 55.25  E-value: 4.02e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 612661263   36 LSLTQFHIIELIDNNDKVNNKFLSEMLNVSKPAITKSIKKLLAKGLVVESHNEFNKREV 94
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 34-93 1.43e-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: 51.05  E-value: 1.43e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 612661263   34 LDLSLTQFHIIELIDNNDKVNNKFLSEMLNVSKPAITKSIKKLLAKGLVVESHNEFNKRE 93
Cdd:pfam12802   1 LGLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRRA 60
MntR COG1321
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];
43-105 6.80e-07

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


Pssm-ID: 440932 [Multi-domain]  Cd Length: 135  Bit Score: 45.96  E-value: 6.80e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612661263  43 IIELIDNNDKVNNKFLSEMLNVSKPAITKSIKKLLAKGLVVESHNEFnkrevnYSLTQEGKKL 105
Cdd:COG1321   15 IYELSEEGGPVRTSDIAERLGVSPPSVTEMLKKLEEKGLVEYEPYGG------ITLTEEGREL 71
HTH_27 pfam13463
Winged helix DNA-binding domain;
58-102 7.12e-06

Winged helix DNA-binding domain;


Pssm-ID: 433228 [Multi-domain]  Cd Length: 68  Bit Score: 41.51  E-value: 7.12e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 612661263   58 LSEMLNVSKPAITKSIKKLLAKGLVVESHNEFNKREVNYSLTQEG 102
Cdd:pfam13463  24 ICFRLNVEDSHVSYSLKKLTEAGLVEREGSEEDGRETRVRLTAKG 68
HTH_24 pfam13412
Winged helix-turn-helix DNA-binding;
39-82 7.47e-05

Winged helix-turn-helix DNA-binding;


Pssm-ID: 404317 [Multi-domain]  Cd Length: 45  Bit Score: 38.18  E-value: 7.47e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 612661263   39 TQFHIIELIDNNDKVNNKFLSEMLNVSKPAITKSIKKLLAKGLV 82
Cdd:pfam13412   2 TDRKILNLLQENPRISQRELAERLGLSPSTVNRRLKRLEEEGVI 45
WH_MUS81 cd21036
winged helix domain found in crossover junction endonuclease MUS81 and similar proteins; MUS81 ...
 72-105 1.37e-04

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: 38.67  E-value: 1.37e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 612661263  72 SIKKLLAKGLVVESHNefNKRevnYSLTQEGKKL 105
Cdd:cd21036   59 SMKTLIKKGLVYKEGR--PAR---YSLTEEGREL 87
COG3398 COG3398
Predicted transcriptional regulator, contains two HTH domains [Transcription];
8-101 1.77e-04

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


Pssm-ID: 442625 [Multi-domain]  Cd Length: 159  Bit Score: 39.48  E-value: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612661263   8 ILKLQQFIIERENADKRRQYKK-----ENEELDLSL----TQFHIIELIDNNDKVNNKFLSEMLNVSKPAITKSIKKLLA 78
Cdd:COG3398   58 RLEREGKITSEKDGGRTRYFPNsgtysEEEKKILAYlrreTPRRILLYLLENPGATNKELAEELGISRSTVSWHLKRLEE 137

                         90       100
                 ....*....|....*....|...
gi 612661263  79 KGLVVESHNEfnkREVNYSLTQE 101
Cdd:COG3398  138 DGLVERERDG---RNVRYYLNPP 157
BirA COG1654
Biotin operon repressor [Transcription];
39-130 6.70e-04

Biotin operon repressor [Transcription];


Pssm-ID: 441260 [Multi-domain]  Cd Length: 324  Bit Score: 38.81  E-value: 6.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612661263  39 TQFHIIELIDNNDKVNNKFLSEMLNVSKPAITKSIKKLLAKGLVVESHnefnkREVNYSLTQEGKKLSY--IHDELHEKA 116
Cdd:COG1654    5 TRLKLLRLLADGEFHSGEELAEELGVSRAAVWKHIKALRELGYEIESV-----PGKGYRLAEPPDLLDPeeIRAGLSTKR 79

                         90
                 ....*....|....
gi 612661263 117 VKKYEEVLKVFDND 130
Cdd:COG1654   80 LGREILYVISSTST 93
PRK11512 PRK11512
multiple antibiotic resistance transcriptional regulator MarR;
15-141 7.69e-04

multiple antibiotic resistance transcriptional regulator MarR;


Pssm-ID: 183170  Cd Length: 144  Bit Score: 37.57  E-value: 7.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612661263  15 IIERENADKRRQYKKENEELDLSLTQFHIIELIDNNDKVNNKFLSEMLNVSKPAITKSIKKLLAKGLVVESHNEFNKREV 94
Cdd:PRK11512  17 LIHMVNQKKDRLLNEYLSPLDITAAQFKVLCSIRCAACITPVELKKVLSVDLGALTRMLDRLVCKGWVERLPNPNDKRGV 96

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 612661263  95 NYSLTQEGkklSYIHDELHEKAVKK-YEEVLKVFDNDEMAVIVEFLNR 141
Cdd:PRK11512  97 LVKLTTSG---AAICEQCHQLVGQDlHQELTKNLTADEVATLEHLLKK 141
HTH_ASNC smart00344
helix_turn_helix ASNC type; AsnC: an autogenously regulated activator of asparagine synthetase ...
 42-128 2.19e-03

helix_turn_helix ASNC type; AsnC: an autogenously regulated activator of asparagine synthetase A transcription in Escherichia coli)


Pssm-ID: 214628 [Multi-domain]  Cd Length: 108  Bit Score: 35.57  E-value: 2.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612661263    42 HIIELIDNNDKVNNKFLSEMLNVSKPAITKSIKKLLAKGLVVESHNEFNKREVNYSLTqegkklSYIHDELH-------- 113
Cdd:smart00344   7 KILEELQKDARISLAELAKKVGLSPSTVHNRVKRLEEEGVIKGYTAVLNPKKLGLSVT------AFVGVTLEnpdkleef 80

                           90
                   ....*....|....*
gi 612661263   114 EKAVKKYEEVLKVFD 128
Cdd:smart00344  81 LEKLEKLPEVEEVYL 95
PRK10411 PRK10411
L-fucose operon activator;
40-86 2.40e-03

L-fucose operon activator;


Pssm-ID: 236684 [Multi-domain]  Cd Length: 240  Bit Score: 36.71  E-value: 2.40e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 612661263  40 QFHIIELIDNNDKVNNKFLSEMLNVSKPAITKSIKKLLAKGLVVESH 86
Cdd:PRK10411   6 QQAIVDLLLNHTSLTTEALAEQLNVSKETIRRDLNELQTQGKILRNH 52
Fe_dep_repress pfam01325
Iron dependent repressor, N-terminal DNA binding domain; This family includes the Diphtheria ...
 43-86 5.72e-03

Iron dependent repressor, N-terminal DNA binding domain; This family includes the Diphtheria toxin repressor. DNA binding is through a helix-turn-helix motif.


Pssm-ID: 396062 [Multi-domain]  Cd Length: 57  Bit Score: 33.50  E-value: 5.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 612661263   43 IIELIDNNDKVNNKFLSEMLNVSKPAITKSIKKLLAKGLVVESH 86
Cdd:pfam01325  10 IYTLSEEKGVVKTKDLAERLNVSPSTVSEMLKKLEKMGYVDYEP 53
HTH_11 pfam08279
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.
 43-85 6.85e-03

HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.


Pssm-ID: 429896 [Multi-domain]  Cd Length: 52  Bit Score: 33.17  E-value: 6.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 612661263   43 IIELIDNNDKVNNKFLSEMLNVSKPAITKSIKKLLAKGLVVES 85
Cdd:pfam08279   4 LQLLLEARGPISGQELAEKLGVSRRTIRRDIKILEELGVPIEA 46
 
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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