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Conserved domains on  [gi|446466061|ref|WP_000543915|]
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MULTISPECIES: homoprotocatechuate degradation operon regulator HpaR [Enterobacteriaceae]

Protein Classification

MarR family transcriptional regulator( domain architecture ID 10020714)

MarR family transcriptional regulator similar to homoprotocatechuate degradation operon regulator HpaR, a repressor for the homoprotocatechuate catabolic pathway hpc operon

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HpaR TIGR02337
homoprotocatechuate degradation operon regulator, HpaR; This Helix-Turn-Helix transcriptional ...
 4-121 1.55e-64

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: 192.60  E-value: 1.55e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466061    4 SLTIALLQAREAAMSYFRPIVKRHNLTEQQWRIVRILAESPSMDFHDLAYRACILRPSLTGILTRMERDGLVLRLKPIND 83
Cdd:TIGR02337   1 SLPLALLQAREAAMSFFRPILAQHGLTEQQWRILRILAEQGSMEFTQLANQACILRPSLTGILARLERDGLVTRLKASND 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 446466061   84 QRKLYISLTKEGQALYNRAQTQIEEAYRQIEAQFTAEK 121
Cdd:TIGR02337  81 QRRVYISLTPKGQALYASLSPQIEEIYAAIEERLGEEK 118
 
Name Accession Description Interval E-value
HpaR TIGR02337
homoprotocatechuate degradation operon regulator, HpaR; This Helix-Turn-Helix transcriptional ...
 4-121 1.55e-64

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: 192.60  E-value: 1.55e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466061    4 SLTIALLQAREAAMSYFRPIVKRHNLTEQQWRIVRILAESPSMDFHDLAYRACILRPSLTGILTRMERDGLVLRLKPIND 83
Cdd:TIGR02337   1 SLPLALLQAREAAMSFFRPILAQHGLTEQQWRILRILAEQGSMEFTQLANQACILRPSLTGILARLERDGLVTRLKASND 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 446466061   84 QRKLYISLTKEGQALYNRAQTQIEEAYRQIEAQFTAEK 121
Cdd:TIGR02337  81 QRRVYISLTPKGQALYASLSPQIEEIYAAIEERLGEEK 118
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
23-122 6.37e-28

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 99.21  E-value: 6.37e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466061    23 IVKRHNLTEQQWRIVRILAESPSMDFHDLAYRACILRPSLTGILTRMERDGLVLRLKPINDQRKLYISLTKEGQALYNRA 102
Cdd:smart00347   2 ELKPLGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQL 81

                           90       100
                   ....*....|....*....|
gi 446466061   103 QTQIEEAYRQIEAQFTAEKM 122
Cdd:smart00347  82 LEARSETLAELLAGLTAEEQ 101
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
2-134 1.85e-23

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 88.87  E-value: 1.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466061   2 HDSLTIALLQAREAAMSYFRPIVKRHNLTEQQWRIVRILAESPSMDFHDLAYRACILRPSLTGILTRMERDGLVLRLKPI 81
Cdd:COG1846    9 EERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDP 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446466061  82 NDQRKLYISLTKEGQALYNRAQTQIEEAYRQIEAQFTAEKMQQLTHLLEEFIA 134
Cdd:COG1846   89 EDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRLAE 141
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 29-86 1.20e-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: 56.40  E-value: 1.20e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446466061   29 LTEQQWRIVRILAESPSMDFHDLAYRACILRPSLTGILTRMERDGLVLRLKPINDQRK 86
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRRE 58
PRK11512 PRK11512
multiple antibiotic resistance transcriptional regulator MarR;
61-133 7.47e-03

multiple antibiotic resistance transcriptional regulator MarR;


Pssm-ID: 183170  Cd Length: 144  Bit Score: 34.87  E-value: 7.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446466061  61 SLTGILTRMERDGLVLRLKPINDQRKLYISLTKEGQALYNRAQTQI-EEAYRQIEAQFTAEKMQQLTHLLEEFI 133
Cdd:PRK11512  70 ALTRMLDRLVCKGWVERLPNPNDKRGVLVKLTTSGAAICEQCHQLVgQDLHQELTKNLTADEVATLEHLLKKVL 143
 
Name Accession Description Interval E-value
HpaR TIGR02337
homoprotocatechuate degradation operon regulator, HpaR; This Helix-Turn-Helix transcriptional ...
 4-121 1.55e-64

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: 192.60  E-value: 1.55e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466061    4 SLTIALLQAREAAMSYFRPIVKRHNLTEQQWRIVRILAESPSMDFHDLAYRACILRPSLTGILTRMERDGLVLRLKPIND 83
Cdd:TIGR02337   1 SLPLALLQAREAAMSFFRPILAQHGLTEQQWRILRILAEQGSMEFTQLANQACILRPSLTGILARLERDGLVTRLKASND 80

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 446466061   84 QRKLYISLTKEGQALYNRAQTQIEEAYRQIEAQFTAEK 121
Cdd:TIGR02337  81 QRRVYISLTPKGQALYASLSPQIEEIYAAIEERLGEEK 118
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
23-122 6.37e-28

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 99.21  E-value: 6.37e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466061    23 IVKRHNLTEQQWRIVRILAESPSMDFHDLAYRACILRPSLTGILTRMERDGLVLRLKPINDQRKLYISLTKEGQALYNRA 102
Cdd:smart00347   2 ELKPLGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQL 81

                           90       100
                   ....*....|....*....|
gi 446466061   103 QTQIEEAYRQIEAQFTAEKM 122
Cdd:smart00347  82 LEARSETLAELLAGLTAEEQ 101
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
2-134 1.85e-23

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 88.87  E-value: 1.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446466061   2 HDSLTIALLQAREAAMSYFRPIVKRHNLTEQQWRIVRILAESPSMDFHDLAYRACILRPSLTGILTRMERDGLVLRLKPI 81
Cdd:COG1846    9 EERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDP 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446466061  82 NDQRKLYISLTKEGQALYNRAQTQIEEAYRQIEAQFTAEKMQQLTHLLEEFIA 134
Cdd:COG1846   89 EDRRAVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRLAE 141
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 29-86 1.20e-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: 56.40  E-value: 1.20e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446466061   29 LTEQQWRIVRILAESPSMDFHDLAYRACILRPSLTGILTRMERDGLVLRLKPINDQRK 86
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRRE 58
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 27-85 2.55e-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: 432797 [Multi-domain]  Cd Length: 60  Bit Score: 39.88  E-value: 2.55e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446466061   27 HNLTEQQWRIVRILAESPSMDFHDLAYRACILRPSLTGILTRMERDGLVLRLKPINDQR 85
Cdd:pfam12802   1 LGLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRR 59
PRK11512 PRK11512
multiple antibiotic resistance transcriptional regulator MarR;
61-133 7.47e-03

multiple antibiotic resistance transcriptional regulator MarR;


Pssm-ID: 183170  Cd Length: 144  Bit Score: 34.87  E-value: 7.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446466061  61 SLTGILTRMERDGLVLRLKPINDQRKLYISLTKEGQALYNRAQTQI-EEAYRQIEAQFTAEKMQQLTHLLEEFI 133
Cdd:PRK11512  70 ALTRMLDRLVCKGWVERLPNPNDKRGVLVKLTTSGAAICEQCHQLVgQDLHQELTKNLTADEVATLEHLLKKVL 143
 
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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