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Conserved domains on  [gi|510996607|ref|WP_016264467|]
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MarR family winged helix-turn-helix transcriptional regulator [Latilactobacillus sakei]

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];
1-146 4.32e-17

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


:

Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 73.47  E-value: 4.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996607   1 MSSKITgkySEDWEVITHLSLIYRWVISNLSDFVSGESLNYKvsfdQFLIMYEIATNDDLTGSKLAKTMSVSRSAISRQC 80
Cdd:COG1846    1 MSDEPD---PAEERLGLLLRRLARALRRALDRALAELGLTPA----QFRVLAALAEAGGLTQSELAERLGLTKSTVSRLL 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510996607  81 RLLKENGYVVEEHLQSDQRVKFLSLTKQGQDVLDRLVSRYVQKYQEIETQMGREKIDGLIQFIDQF 146
Cdd:COG1846   74 DRLEEKGLVEREPDPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRL 139
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
1-146 4.32e-17

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 73.47  E-value: 4.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996607   1 MSSKITgkySEDWEVITHLSLIYRWVISNLSDFVSGESLNYKvsfdQFLIMYEIATNDDLTGSKLAKTMSVSRSAISRQC 80
Cdd:COG1846    1 MSDEPD---PAEERLGLLLRRLARALRRALDRALAELGLTPA----QFRVLAALAEAGGLTQSELAERLGLTKSTVSRLL 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510996607  81 RLLKENGYVVEEHLQSDQRVKFLSLTKQGQDVLDRLVSRYVQKYQEIETQMGREKIDGLIQFIDQF 146
Cdd:COG1846   74 DRLEEKGLVEREPDPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRL 139
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
41-127 1.65e-14

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 65.69  E-value: 1.65e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996607    41 YKVSFDQFLIMYEIATNDDLTGSKLAKTMSVSRSAISRQCRLLKENGYVVEEHLQSDQRVKFLSLTKQGQDVLDRLVSRY 120
Cdd:smart00347   6 LGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLLEAR 85


                   ....*..
gi 510996607   121 VQKYQEI 127
Cdd:smart00347  86 SETLAEL 92
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 43-99 5.87e-08

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: 47.20  E-value: 5.87e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 510996607   43 VSFDQFLIMYEIATNDDLTGSKLAKTMSVSRSAISRQCRLLKENGYVVEEHLQSDQR 99
Cdd:pfam12802   3 LTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRR 59
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 50-106 2.17e-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: 35.35  E-value: 2.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 510996607  50 IMYEIAtNDDLTGSKLAKTMSVSRSAISRQCRLLKENGYVVEEHlqsDQRVKFLSLT 106
Cdd:cd00090   12 ILRLLL-EGPLTVSELAERLGLSQSTVSRHLKKLEEAGLVESRR---EGRRVYYSLT 64
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
1-146 4.32e-17

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 73.47  E-value: 4.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996607   1 MSSKITgkySEDWEVITHLSLIYRWVISNLSDFVSGESLNYKvsfdQFLIMYEIATNDDLTGSKLAKTMSVSRSAISRQC 80
Cdd:COG1846    1 MSDEPD---PAEERLGLLLRRLARALRRALDRALAELGLTPA----QFRVLAALAEAGGLTQSELAERLGLTKSTVSRLL 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 510996607  81 RLLKENGYVVEEHLQSDQRVKFLSLTKQGQDVLDRLVSRYVQKYQEIETQMGREKIDGLIQFIDQF 146
Cdd:COG1846   74 DRLEEKGLVEREPDPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRL 139
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
41-127 1.65e-14

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 65.69  E-value: 1.65e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996607    41 YKVSFDQFLIMYEIATNDDLTGSKLAKTMSVSRSAISRQCRLLKENGYVVEEHLQSDQRVKFLSLTKQGQDVLDRLVSRY 120
Cdd:smart00347   6 LGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLLEAR 85


                   ....*..
gi 510996607   121 VQKYQEI 127
Cdd:smart00347  86 SETLAEL 92
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 43-99 5.87e-08

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: 47.20  E-value: 5.87e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 510996607   43 VSFDQFLIMYEIATNDDLTGSKLAKTMSVSRSAISRQCRLLKENGYVVEEHLQSDQR 99
Cdd:pfam12802   3 LTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRR 59
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 47-101 2.84e-06

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: 42.92  E-value: 2.84e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 510996607   47 QFLIMYEIATNDDLTGSKLAKTMSVSRSAISRQCRLLKENGYVVEEHLQSDQRVK 101
Cdd:pfam01047   5 QFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
HTH_11 pfam08279
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.
 54-91 1.07e-04

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: 38.18  E-value: 1.07e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 510996607   54 IATNDDLTGSKLAKTMSVSRSAISRQCRLLKENGYVVE 91
Cdd:pfam08279   8 LEARGPISGQELAEKLGVSRRTIRRDIKILEELGVPIE 45
BirA COG1654
Biotin operon repressor [Transcription];
60-145 1.94e-03

Biotin operon repressor [Transcription];


Pssm-ID: 441260 [Multi-domain]  Cd Length: 324  Bit Score: 37.66  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 510996607  60 LTGSKLAKTMSVSRSAISRQCRLLKENGYVVEehlqsdqrvkflSLTKQG---QDVLDRLvsryvqKYQEIETQMGREKI 136
Cdd:COG1654   19 HSGEELAEELGVSRAAVWKHIKALRELGYEIE------------SVPGKGyrlAEPPDLL------DPEEIRAGLSTKRL 80


                 ....*....
gi 510996607 137 DGLIQFIDQ 145
Cdd:COG1654   81 GREILYVIS 89
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 50-106 2.17e-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: 35.35  E-value: 2.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 510996607  50 IMYEIAtNDDLTGSKLAKTMSVSRSAISRQCRLLKENGYVVEEHlqsDQRVKFLSLT 106
Cdd:cd00090   12 ILRLLL-EGPLTVSELAERLGLSQSTVSRHLKKLEEAGLVESRR---EGRRVYYSLT 64
MntR COG1321
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];
51-120 8.40e-03

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


Pssm-ID: 440932 [Multi-domain]  Cd Length: 135  Bit Score: 34.79  E-value: 8.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 510996607  51 MYEI-ATNDDLTGSKLAKTMSVSRSAISRQCRLLKENGYVVEEhlqsdqRVKFLSLTKQGQDVLDRLVSRY 120
Cdd:COG1321   15 IYELsEEGGPVRTSDIAERLGVSPPSVTEMLKKLEEKGLVEYE------PYGGITLTEEGRELALRIVRRH 79
 
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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