NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|15607877|ref|NP_215251|]
View 

transcriptional regulator [Mycobacterium tuberculosis H37Rv]

Protein Classification

MarR family transcriptional regulator( domain architecture ID 12204203)

MarR family transcriptional regulator is a winged helix-turn-helix domain-containing protein, named for an Escherichia coli regulator of an operon that encodes a drug efflux pump

Gene Ontology:  GO:0003677|GO:0003700
PubMed:  10498949

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
47-147 2.02e-22

helix_turn_helix multiple antibiotic resistance protein;


:

Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 85.72  E-value: 2.02e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607877     47 TALRPYDLSFSRFELLRLLAFSriGALPITKASDRLQVHVTSVTHAIRRLEADGLVRRVPHPTDGRTTLVQITELGRSTV 126
Cdd:smart00347   1 EELKPLGLTPTQFLVLRILYEE--GPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELI 78

                           90       100
                   ....*....|....*....|....
gi 15607877    127 EDATVTLNE---QVFAnvGMGAEE 147
Cdd:smart00347  79 EQLLEARSEtlaELLA--GLTAEE 100
 
Name Accession Description Interval E-value
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
47-147 2.02e-22

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 85.72  E-value: 2.02e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607877     47 TALRPYDLSFSRFELLRLLAFSriGALPITKASDRLQVHVTSVTHAIRRLEADGLVRRVPHPTDGRTTLVQITELGRSTV 126
Cdd:smart00347   1 EELKPLGLTPTQFLVLRILYEE--GPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELI 78

                           90       100
                   ....*....|....*....|....
gi 15607877    127 EDATVTLNE---QVFAnvGMGAEE 147
Cdd:smart00347  79 EQLLEARSEtlaELLA--GLTAEE 100
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
34-161 1.61e-21

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 84.64  E-value: 1.61e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607877  34 VMRAHQILLARVETALRPYDLSFSRFELLRLLAfsRIGALPITKASDRLQVHVTSVTHAIRRLEADGLVRRVPHPTDGRT 113
Cdd:COG1846  16 LRRLARALRRALDRALAELGLTPAQFRVLAALA--EAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRA 93

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15607877 114 TLVQITELGRSTVEDAT---VTLNEQVFAnvGMGAEESQALVSAVETLRRN 161
Cdd:COG1846  94 VLVRLTEKGRALLEEARpalEALLAELLA--GLSEEELEALLRLLRRLAEN 142
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 54-112 2.17e-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: 426012 [Multi-domain]  Cd Length: 59  Bit Score: 48.31  E-value: 2.17e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15607877    54 LSFSRFELLRLLafSRIGALPITKASDRLQVHVTSVTHAIRRLEADGLVRRVPHPTDGR 112
Cdd:pfam01047   1 LTLTQFHILRIL--YEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRR 57
PRK11512 PRK11512
multiple antibiotic resistance transcriptional regulator MarR;
49-127 4.33e-04

multiple antibiotic resistance transcriptional regulator MarR;


Pssm-ID: 183170  Cd Length: 144  Bit Score: 38.34  E-value: 4.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607877   49 LRPYDLSFSRFELL-RLLAFSRIGALPITKAsdrLQVHVTSVTHAIRRLEADGLVRRVPHPTDGRTTLVQITELGRSTVE 127
Cdd:PRK11512  33 LSPLDITAAQFKVLcSIRCAACITPVELKKV---LSVDLGALTRMLDRLVCKGWVERLPNPNDKRGVLVKLTTSGAAICE 109
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
 79-107 4.89e-03

Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional regulators; This CD represents the winged HTH DNA-binding domain of the GntR (named after the gluconate operon repressor in Bacillus subtilis) family of bacterial transcriptional regulators and their putative homologs found in eukaryota and archaea. The GntR family has over 6000 members distributed among almost all bacterial species, which is comprised of FadR, HutC, MocR, YtrA, AraR, PlmA, and other subfamilies for the regulation of the most varied biological process. The monomeric proteins of the GntR family are characterized by two function domains: a small highly conserved winged helix-turn-helix prokaryotic DNA binding domain in the N-terminus, and a very diverse regulatory ligand-binding domain in the C-terminus for effector-binding/oligomerization, which provides the basis for the subfamily classifications. Binding of the effector to GntR-like transcriptional regulators is presumed to result in a conformational change that regulates the DNA-binding affinity of the repressor. The GntR-like proteins bind as dimers, where each monomer recognizes a half-site of 2-fold symmetric DNA sequences.


Pssm-ID: 153418 [Multi-domain]  Cd Length: 66  Bit Score: 33.96  E-value: 4.89e-03
                        10        20
                ....*....|....*....|....*....
gi 15607877  79 SDRLQVHVTSVTHAIRRLEADGLVRRVPH 107
Cdd:cd07377  32 AEELGVSRTTVREALRELEAEGLVERRPG 60
 
Name Accession Description Interval E-value
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
47-147 2.02e-22

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 85.72  E-value: 2.02e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607877     47 TALRPYDLSFSRFELLRLLAFSriGALPITKASDRLQVHVTSVTHAIRRLEADGLVRRVPHPTDGRTTLVQITELGRSTV 126
Cdd:smart00347   1 EELKPLGLTPTQFLVLRILYEE--GPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELI 78

                           90       100
                   ....*....|....*....|....
gi 15607877    127 EDATVTLNE---QVFAnvGMGAEE 147
Cdd:smart00347  79 EQLLEARSEtlaELLA--GLTAEE 100
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
34-161 1.61e-21

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 84.64  E-value: 1.61e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607877  34 VMRAHQILLARVETALRPYDLSFSRFELLRLLAfsRIGALPITKASDRLQVHVTSVTHAIRRLEADGLVRRVPHPTDGRT 113
Cdd:COG1846  16 LRRLARALRRALDRALAELGLTPAQFRVLAALA--EAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRRA 93

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15607877 114 TLVQITELGRSTVEDAT---VTLNEQVFAnvGMGAEESQALVSAVETLRRN 161
Cdd:COG1846  94 VLVRLTEKGRALLEEARpalEALLAELLA--GLSEEELEALLRLLRRLAEN 142
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 54-112 2.17e-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: 426012 [Multi-domain]  Cd Length: 59  Bit Score: 48.31  E-value: 2.17e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15607877    54 LSFSRFELLRLLafSRIGALPITKASDRLQVHVTSVTHAIRRLEADGLVRRVPHPTDGR 112
Cdd:pfam01047   1 LTLTQFHILRIL--YEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRR 57
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 52-112 8.30e-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: 432797 [Multi-domain]  Cd Length: 60  Bit Score: 41.42  E-value: 8.30e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15607877    52 YDLSFSRFELLRLLAfsRIGALPITKASDRLQVHVTSVTHAIRRLEADGLVRRVPHPTDGR 112
Cdd:pfam12802   1 LGLTPAQFRVLLALA--RNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRR 59
HTH_27 pfam13463
Winged helix DNA-binding domain;
60-122 2.27e-04

Winged helix DNA-binding domain;


Pssm-ID: 433228 [Multi-domain]  Cd Length: 68  Bit Score: 37.65  E-value: 2.27e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15607877    60 ELLRLLaFSRIGALPITKASDRLQVHVTSVTHAIRRLEADGLVRRVPHPTDGRTTLVQITELG 122
Cdd:pfam13463   7 LILHNI-GHRGDPKTLADICFRLNVEDSHVSYSLKKLTEAGLVEREGSEEDGRETRVRLTAKG 68
PRK11512 PRK11512
multiple antibiotic resistance transcriptional regulator MarR;
49-127 4.33e-04

multiple antibiotic resistance transcriptional regulator MarR;


Pssm-ID: 183170  Cd Length: 144  Bit Score: 38.34  E-value: 4.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15607877   49 LRPYDLSFSRFELL-RLLAFSRIGALPITKAsdrLQVHVTSVTHAIRRLEADGLVRRVPHPTDGRTTLVQITELGRSTVE 127
Cdd:PRK11512  33 LSPLDITAAQFKVLcSIRCAACITPVELKKV---LSVDLGALTRMLDRLVCKGWVERLPNPNDKRGVLVKLTTSGAAICE 109
MntR COG1321
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];
79-123 2.09e-03

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


Pssm-ID: 440932 [Multi-domain]  Cd Length: 135  Bit Score: 36.33  E-value: 2.09e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 15607877  79 SDRLQVHVTSVTHAIRRLEADGLVRRVPhptDGRTTLvqiTELGR 123
Cdd:COG1321  31 AERLGVSPPSVTEMLKKLEEKGLVEYEP---YGGITL---TEEGR 69
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
 79-107 4.89e-03

Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional regulators; This CD represents the winged HTH DNA-binding domain of the GntR (named after the gluconate operon repressor in Bacillus subtilis) family of bacterial transcriptional regulators and their putative homologs found in eukaryota and archaea. The GntR family has over 6000 members distributed among almost all bacterial species, which is comprised of FadR, HutC, MocR, YtrA, AraR, PlmA, and other subfamilies for the regulation of the most varied biological process. The monomeric proteins of the GntR family are characterized by two function domains: a small highly conserved winged helix-turn-helix prokaryotic DNA binding domain in the N-terminus, and a very diverse regulatory ligand-binding domain in the C-terminus for effector-binding/oligomerization, which provides the basis for the subfamily classifications. Binding of the effector to GntR-like transcriptional regulators is presumed to result in a conformational change that regulates the DNA-binding affinity of the repressor. The GntR-like proteins bind as dimers, where each monomer recognizes a half-site of 2-fold symmetric DNA sequences.


Pssm-ID: 153418 [Multi-domain]  Cd Length: 66  Bit Score: 33.96  E-value: 4.89e-03
                        10        20
                ....*....|....*....|....*....
gi 15607877  79 SDRLQVHVTSVTHAIRRLEADGLVRRVPH 107
Cdd:cd07377  32 AEELGVSRTTVREALRELEAEGLVERRPG 60
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 57-123 9.23e-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: 33.43  E-value: 9.23e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15607877  57 SRFELLRLLafsRIGALPITKASDRLQVHVTSVTHAIRRLEADGLVRRVPhptDGRTTLVQITELGR 123
Cdd:cd00090   8 TRLRILRLL---LEGPLTVSELAERLGLSQSTVSRHLKKLEEAGLVESRR---EGRRVYYSLTDAER 68
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH