NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|446757668|ref|WP_000834924|]
View 

MULTISPECIES: HTH-type transcriptional regulator Hpr [Bacillus]

Protein Classification

HTH-type transcriptional regulator Hpr( domain architecture ID 10014408)

HTH-type transcriptional regulator Hpr is a negative regulator of protease production and sporulation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PRK13777 PRK13777
HTH-type transcriptional regulator Hpr;
2-185 1.80e-120

HTH-type transcriptional regulator Hpr;


:

Pssm-ID: 237501  Cd Length: 185  Bit Score: 338.17  E-value: 1.80e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446757668   2 KSGEKDYSVKEAMIFSQRIAQLSKALWKCVEKDWQQWIKPYDLNINEHHILTIAYHLKGASISEIAKFGVMHVSTAFNFS 81
Cdd:PRK13777   1 KSGEKDYSIKEAMLFSQKIAQLSKALWKSVEKDWQQWIKPYDLNINEHHILWIAYHLKGASISEIAKFGVMHVSTAFNFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446757668  82 KKLEERGYLVFSKKEDDKRNTYIEITDKGEELLLRLMEEYDPENNSVFNGALALRNFYGKFPENIELIAILRNIYGQDFI 161
Cdd:PRK13777  81 KKLEERGYLTFSKKEDDKRNTYIELTEKGEELLLETMEEYDPENNSVFNGALPLRELYGKFPEFIELMAIVRNIYGDDFI 160
                        170       180
                 ....*....|....*....|....
gi 446757668 162 DIFEKSLEDIEENFTESDQKLVKK 185
Cdd:PRK13777 161 DIFEKSLENIEENFTEEDGKLVKK 184
 
Name Accession Description Interval E-value
PRK13777 PRK13777
HTH-type transcriptional regulator Hpr;
2-185 1.80e-120

HTH-type transcriptional regulator Hpr;


Pssm-ID: 237501  Cd Length: 185  Bit Score: 338.17  E-value: 1.80e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446757668   2 KSGEKDYSVKEAMIFSQRIAQLSKALWKCVEKDWQQWIKPYDLNINEHHILTIAYHLKGASISEIAKFGVMHVSTAFNFS 81
Cdd:PRK13777   1 KSGEKDYSIKEAMLFSQKIAQLSKALWKSVEKDWQQWIKPYDLNINEHHILWIAYHLKGASISEIAKFGVMHVSTAFNFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446757668  82 KKLEERGYLVFSKKEDDKRNTYIEITDKGEELLLRLMEEYDPENNSVFNGALALRNFYGKFPENIELIAILRNIYGQDFI 161
Cdd:PRK13777  81 KKLEERGYLTFSKKEDDKRNTYIELTEKGEELLLETMEEYDPENNSVFNGALPLRELYGKFPEFIELMAIVRNIYGDDFI 160
                        170       180
                 ....*....|....*....|....
gi 446757668 162 DIFEKSLEDIEENFTESDQKLVKK 185
Cdd:PRK13777 161 DIFEKSLENIEENFTEEDGKLVKK 184
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
37-110 1.60e-18

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 76.48  E-value: 1.60e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446757668    37 QWIKPYDLNINEHHILTIAYHLKGASISEIAKFGVMHVSTAFNFSKKLEERGYLVFSKKEDDKRNTYIEITDKG 110
Cdd:smart00347   1 EELKPLGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEG 74
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
44-102 8.65e-13

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: 60.25  E-value: 8.65e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446757668   44 LNINEHHILTIAYHLKGASISEIAKFGVMHVSTAFNFSKKLEERGYLVFSKKEDDKRNT 102
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
18-110 2.39e-12

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 61.14  E-value: 2.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446757668  18 QRIAQLSKALWKCVEKDWQQWIKPYDLNINEHHILTIAYHLKGASISEIAKFGVMHVSTAFNFSKKLEERGYLVFSKKED 97
Cdd:COG1846   10 ERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPE 89
                         90
                 ....*....|...
gi 446757668  98 DKRNTYIEITDKG 110
Cdd:COG1846   90 DRRAVLVRLTEKG 102
 
Name Accession Description Interval E-value
PRK13777 PRK13777
HTH-type transcriptional regulator Hpr;
2-185 1.80e-120

HTH-type transcriptional regulator Hpr;


Pssm-ID: 237501  Cd Length: 185  Bit Score: 338.17  E-value: 1.80e-120
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446757668   2 KSGEKDYSVKEAMIFSQRIAQLSKALWKCVEKDWQQWIKPYDLNINEHHILTIAYHLKGASISEIAKFGVMHVSTAFNFS 81
Cdd:PRK13777   1 KSGEKDYSIKEAMLFSQKIAQLSKALWKSVEKDWQQWIKPYDLNINEHHILWIAYHLKGASISEIAKFGVMHVSTAFNFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446757668  82 KKLEERGYLVFSKKEDDKRNTYIEITDKGEELLLRLMEEYDPENNSVFNGALALRNFYGKFPENIELIAILRNIYGQDFI 161
Cdd:PRK13777  81 KKLEERGYLTFSKKEDDKRNTYIELTEKGEELLLETMEEYDPENNSVFNGALPLRELYGKFPEFIELMAIVRNIYGDDFI 160
                        170       180
                 ....*....|....*....|....
gi 446757668 162 DIFEKSLEDIEENFTESDQKLVKK 185
Cdd:PRK13777 161 DIFEKSLENIEENFTEEDGKLVKK 184
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
37-110 1.60e-18

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 76.48  E-value: 1.60e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446757668    37 QWIKPYDLNINEHHILTIAYHLKGASISEIAKFGVMHVSTAFNFSKKLEERGYLVFSKKEDDKRNTYIEITDKG 110
Cdd:smart00347   1 EELKPLGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEG 74
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
44-102 8.65e-13

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: 60.25  E-value: 8.65e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446757668   44 LNINEHHILTIAYHLKGASISEIAKFGVMHVSTAFNFSKKLEERGYLVFSKKEDDKRNT 102
Cdd:pfam01047   1 LTLTQFHILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
18-110 2.39e-12

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 61.14  E-value: 2.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446757668  18 QRIAQLSKALWKCVEKDWQQWIKPYDLNINEHHILTIAYHLKGASISEIAKFGVMHVSTAFNFSKKLEERGYLVFSKKED 97
Cdd:COG1846   10 ERLGLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPE 89
                         90
                 ....*....|...
gi 446757668  98 DKRNTYIEITDKG 110
Cdd:COG1846   90 DRRAVLVRLTEKG 102
HTH_27 pfam13463
Winged helix DNA-binding domain;
51-110 1.59e-06

Winged helix DNA-binding domain;


Pssm-ID: 433228 [Multi-domain]  Cd Length: 68  Bit Score: 43.82  E-value: 1.59e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446757668   51 ILTIAYH-LKGASISEIAKFGVMHVSTAFNFSKKLEERGYLVFSKKEDDKRNTYIEITDKG 110
Cdd:pfam13463   8 ILHNIGHrGDPKTLADICFRLNVEDSHVSYSLKKLTEAGLVEREGSEEDGRETRVRLTAKG 68
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
42-100 8.65e-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: 38.72  E-value: 8.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 446757668   42 YDLNINEHHILTIAYHLKGASISEIAKFGVMHVSTAFNFSKKLEERGYLVFSKKEDDKR 100
Cdd:pfam12802   1 LGLTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVEREPSPADRR 59
 
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