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Conserved domains on  [gi|489056483|ref|WP_002966619|]
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MULTISPECIES: homoprotocatechuate degradation operon regulator HpaR [Brucella]

Protein Classification

helix-turn-helix domain-containing protein( domain architecture ID 229396)

helix-turn-helix domain-containing protein may bind DNA and be involved in the regulation of gene expression

Gene Ontology:  GO:0003677|GO:0006355

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HTH_CRP super family cl46859
helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic ...
 30-147 5.51e-48

helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic regulatory proteins belonging to the catabolite activator protein family.


The actual alignment was detected with superfamily member TIGR02337:

Pssm-ID: 481199 [Multi-domain]  Cd Length: 118  Bit Score: 151.38  E-value: 5.51e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056483   30 SVPIALLRAREAVMSHFRPMLAQHDITEQQWRVIRILAETDIVDASEMAERAFILAPSLTRIIRSLEERGIITKTRDEND 109
Cdd:TIGR02337   1 SLPLALLQAREAAMSFFRPILAQHGLTEQQWRILRILAEQGSMEFTQLANQACILRPSLTGILARLERDGLVTRLKASND 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 489056483  110 GRRVLLQITPAGLAIIKEVAPESRLIYQMIEERFGRER 147
Cdd:TIGR02337  81 QRRVYISLTPKGQALYASLSPQIEEIYAAIEERLGEEK 118
 
Name Accession Description Interval E-value
HpaR TIGR02337
homoprotocatechuate degradation operon regulator, HpaR; This Helix-Turn-Helix transcriptional ...
 30-147 5.51e-48

homoprotocatechuate degradation operon regulator, HpaR; This Helix-Turn-Helix transcriptional regulator is a member of the MarR family (pfam01047) and is found in association with operons for the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate.


Pssm-ID: 188209 [Multi-domain]  Cd Length: 118  Bit Score: 151.38  E-value: 5.51e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056483   30 SVPIALLRAREAVMSHFRPMLAQHDITEQQWRVIRILAETDIVDASEMAERAFILAPSLTRIIRSLEERGIITKTRDEND 109
Cdd:TIGR02337   1 SLPLALLQAREAAMSFFRPILAQHGLTEQQWRILRILAEQGSMEFTQLANQACILRPSLTGILARLERDGLVTRLKASND 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 489056483  110 GRRVLLQITPAGLAIIKEVAPESRLIYQMIEERFGRER 147
Cdd:TIGR02337  81 QRRVYISLTPKGQALYASLSPQIEEIYAAIEERLGEEK 118
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
24-148 6.07e-22

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 85.79  E-value: 6.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056483  24 PRNTRRSVPIALLRAREAVMSHFRPMLAQHDITEQQWRVIRILAETDIVDASEMAERAFILAPSLTRIIRSLEERGIITK 103
Cdd:COG1846    5 PDPAEERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVER 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489056483 104 TRDENDGRRVLLQITPAGLAIIKEVAPESRLIYQMIEERFGRERI 148
Cdd:COG1846   85 EPDPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEEL 129
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
50-148 9.81e-19

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 76.09  E-value: 9.81e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056483    50 LAQHDITEQQWRVIRILAETDIVDASEMAERAFILAPSLTRIIRSLEERGIITKTRDENDGRRVLLQITPAGLAIIKEVA 129
Cdd:smart00347   3 LKPLGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLL 82

                           90
                   ....*....|....*....
gi 489056483   130 PESRLIYQMIEERFGRERI 148
Cdd:smart00347  83 EARSETLAELLAGLTAEEQ 101
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 55-113 1.65e-10

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: 53.71  E-value: 1.65e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489056483   55 ITEQQWRVIRILAETDIVDASEMAERAFILAPSLTRIIRSLEERGIITKTRDENDGRRV 113
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
 
Name Accession Description Interval E-value
HpaR TIGR02337
homoprotocatechuate degradation operon regulator, HpaR; This Helix-Turn-Helix transcriptional ...
 30-147 5.51e-48

homoprotocatechuate degradation operon regulator, HpaR; This Helix-Turn-Helix transcriptional regulator is a member of the MarR family (pfam01047) and is found in association with operons for the degradation of 4-hydroxyphenylacetic acid via homoprotocatechuate.


Pssm-ID: 188209 [Multi-domain]  Cd Length: 118  Bit Score: 151.38  E-value: 5.51e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056483   30 SVPIALLRAREAVMSHFRPMLAQHDITEQQWRVIRILAETDIVDASEMAERAFILAPSLTRIIRSLEERGIITKTRDEND 109
Cdd:TIGR02337   1 SLPLALLQAREAAMSFFRPILAQHGLTEQQWRILRILAEQGSMEFTQLANQACILRPSLTGILARLERDGLVTRLKASND 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 489056483  110 GRRVLLQITPAGLAIIKEVAPESRLIYQMIEERFGRER 147
Cdd:TIGR02337  81 QRRVYISLTPKGQALYASLSPQIEEIYAAIEERLGEEK 118
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
24-148 6.07e-22

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 85.79  E-value: 6.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056483  24 PRNTRRSVPIALLRAREAVMSHFRPMLAQHDITEQQWRVIRILAETDIVDASEMAERAFILAPSLTRIIRSLEERGIITK 103
Cdd:COG1846    5 PDPAEERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVER 84

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 489056483 104 TRDENDGRRVLLQITPAGLAIIKEVAPESRLIYQMIEERFGRERI 148
Cdd:COG1846   85 EPDPEDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEEL 129
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
50-148 9.81e-19

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 76.09  E-value: 9.81e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056483    50 LAQHDITEQQWRVIRILAETDIVDASEMAERAFILAPSLTRIIRSLEERGIITKTRDENDGRRVLLQITPAGLAIIKEVA 129
Cdd:smart00347   3 LKPLGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQLL 82

                           90
                   ....*....|....*....
gi 489056483   130 PESRLIYQMIEERFGRERI 148
Cdd:smart00347  83 EARSETLAELLAGLTAEEQ 101
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 55-113 1.65e-10

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: 53.71  E-value: 1.65e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 489056483   55 ITEQQWRVIRILAETDIVDASEMAERAFILAPSLTRIIRSLEERGIITKTRDENDGRRV 113
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 53-112 4.38e-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: 49.89  E-value: 4.38e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 489056483   53 HDITEQQWRVIRILAETDIVDASEMAERAFILAPSLTRIIRSLEERGIITKTRDENDGRR 112
Cdd:pfam12802   1 LGLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRRA 60
HTH_27 pfam13463
Winged helix DNA-binding domain;
55-121 7.41e-04

Winged helix DNA-binding domain;


Pssm-ID: 433228 [Multi-domain]  Cd Length: 68  Bit Score: 36.11  E-value: 7.41e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489056483   55 ITEQQWRVIRILAET-DIVDASEMAERAFILAPSLTRIIRSLEERGIITKTRDENDGRRVLLQITPAG 121
Cdd:pfam13463   1 LTRLEALILHNIGHRgDPKTLADICFRLNVEDSHVSYSLKKLTEAGLVEREGSEEDGRETRVRLTAKG 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.
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