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Conserved domains on  [gi|480339780|gb|ENX59971|]
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hypothetical protein F885_02163 [Acinetobacter higginsii]

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];
22-151 4.11e-23

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


:

Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 88.49  E-value: 4.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339780  22 FYWISQVNAQYVQNIDNVLKKYGLDNSRRRILIALHVKPHASVSELSDMVISKMSTTTKIVYRLKDEGYIDTYSCKEDGR 101
Cdd:COG1846   13 GLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRR 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 480339780 102 ITRVYLTDKGQEMITKINDLTSVILEQSFDGLTPLQIEKTMEILRHMFKN 151
Cdd:COG1846   93 AVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRLAEN 142
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
22-151 4.11e-23

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 88.49  E-value: 4.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339780  22 FYWISQVNAQYVQNIDNVLKKYGLDNSRRRILIALHVKPHASVSELSDMVISKMSTTTKIVYRLKDEGYIDTYSCKEDGR 101
Cdd:COG1846   13 GLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRR 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 480339780 102 ITRVYLTDKGQEMITKINDLTSVILEQSFDGLTPLQIEKTMEILRHMFKN 151
Cdd:COG1846   93 AVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRLAEN 142
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
38-138 3.74e-16

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 69.16  E-value: 3.74e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339780    38 NVLKKYGLDNSRRRILIALHVKPHASVSELSDMVISKMSTTTKIVYRLKDEGYIDTYSCKEDGRITRVYLTDKGQEMITK 117
Cdd:smart00347   1 EELKPLGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQ 80

                           90       100
                   ....*....|....*....|.
gi 480339780   118 INDLTSVILEQSFDGLTPLQI 138
Cdd:smart00347  81 LLEARSETLAELLAGLTAEEQ 101
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 43-102 5.23e-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: 46.81  E-value: 5.23e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480339780   43 YGLDNSRRRILIALHVKPHASVSELSD-MVISKmSTTTKIVYRLKDEGYIDTYSCKEDGRI 102
Cdd:pfam12802   1 LGLTPAQFRVLLALARNPGLTVAELARrLGISK-QTVSRLVKRLEAKGLVEREPSPADRRA 60
PRK03573 PRK03573
transcriptional regulator SlyA; Provisional
 85-154 5.84e-06

transcriptional regulator SlyA; Provisional


Pssm-ID: 179596  Cd Length: 144  Bit Score: 43.45  E-value: 5.84e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339780  85 LKDEGYIDTYSCKEDGRITRVYLTDKGQEMITKINDLTSVILEQSFDGLTPLQIEKTMEILRHMFKNLAR 154
Cdd:PRK03573  70 LEEKGLISRQTCASDRRAKRIKLTEKAEPLISEVEAVINKTRAEILHGISAEEIEQLITLIAKLEKNIIE 139
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 46-110 2.63e-05

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: 40.36  E-value: 2.63e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480339780  46 DNSRRRILIALHVKPhASVSELSDMV-ISKmSTTTKIVYRLKDEGYIDTYsckEDGRITRVYLTDK 110
Cdd:cd00090    6 DPTRLRILRLLLEGP-LTVSELAERLgLSQ-STVSRHLKKLEEAGLVESR---REGRRVYYSLTDA 66
 
Name Accession Description Interval E-value
MarR COG1846
DNA-binding transcriptional regulator, MarR family [Transcription];
22-151 4.11e-23

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


Pssm-ID: 441451 [Multi-domain]  Cd Length: 142  Bit Score: 88.49  E-value: 4.11e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339780  22 FYWISQVNAQYVQNIDNVLKKYGLDNSRRRILIALHVKPHASVSELSDMVISKMSTTTKIVYRLKDEGYIDTYSCKEDGR 101
Cdd:COG1846   13 GLLLRRLARALRRALDRALAELGLTPAQFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVEREPDPEDRR 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 480339780 102 ITRVYLTDKGQEMITKINDLTSVILEQSFDGLTPLQIEKTMEILRHMFKN 151
Cdd:COG1846   93 AVLVRLTEKGRALLEEARPALEALLAELLAGLSEEELEALLRLLRRLAEN 142
HTH_MARR smart00347
helix_turn_helix multiple antibiotic resistance protein;
38-138 3.74e-16

helix_turn_helix multiple antibiotic resistance protein;


Pssm-ID: 197670 [Multi-domain]  Cd Length: 101  Bit Score: 69.16  E-value: 3.74e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339780    38 NVLKKYGLDNSRRRILIALHVKPHASVSELSDMVISKMSTTTKIVYRLKDEGYIDTYSCKEDGRITRVYLTDKGQEMITK 117
Cdd:smart00347   1 EELKPLGLTPTQFLVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLVRREPSPEDRRSVLVSLTEEGRELIEQ 80

                           90       100
                   ....*....|....*....|.
gi 480339780   118 INDLTSVILEQSFDGLTPLQI 138
Cdd:smart00347  81 LLEARSETLAELLAGLTAEEQ 101
MarR_2 pfam12802
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 43-102 5.23e-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: 46.81  E-value: 5.23e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480339780   43 YGLDNSRRRILIALHVKPHASVSELSD-MVISKmSTTTKIVYRLKDEGYIDTYSCKEDGRI 102
Cdd:pfam12802   1 LGLTPAQFRVLLALARNPGLTVAELARrLGISK-QTVSRLVKRLEAKGLVEREPSPADRRA 60
PRK03573 PRK03573
transcriptional regulator SlyA; Provisional
 85-154 5.84e-06

transcriptional regulator SlyA; Provisional


Pssm-ID: 179596  Cd Length: 144  Bit Score: 43.45  E-value: 5.84e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339780  85 LKDEGYIDTYSCKEDGRITRVYLTDKGQEMITKINDLTSVILEQSFDGLTPLQIEKTMEILRHMFKNLAR 154
Cdd:PRK03573  70 LEEKGLISRQTCASDRRAKRIKLTEKAEPLISEVEAVINKTRAEILHGISAEEIEQLITLIAKLEKNIIE 139
HTH_ARSR cd00090
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 46-110 2.63e-05

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: 40.36  E-value: 2.63e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480339780  46 DNSRRRILIALHVKPhASVSELSDMV-ISKmSTTTKIVYRLKDEGYIDTYsckEDGRITRVYLTDK 110
Cdd:cd00090    6 DPTRLRILRLLLEGP-LTVSELAERLgLSQ-STVSRHLKKLEEAGLVESR---REGRRVYYSLTDA 66
PRK13777 PRK13777
HTH-type transcriptional regulator Hpr;
40-149 3.03e-05

HTH-type transcriptional regulator Hpr;


Pssm-ID: 237501  Cd Length: 185  Bit Score: 41.95  E-value: 3.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339780  40 LKKYGLDNSRRRIL-IALHVKpHASVSELSDMVISKMSTTTKIVYRLKDEGYIdTYSCKE-DGRITRVYLTDKGQEMITK 117
Cdd:PRK13777  38 IKPYDLNINEHHILwIAYHLK-GASISEIAKFGVMHVSTAFNFSKKLEERGYL-TFSKKEdDKRNTYIELTEKGEELLLE 115

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 480339780 118 I----NDLTSVIleqsFDGLTPLQ--------IEKTMEILRHMF 149
Cdd:PRK13777 116 TmeeyDPENNSV----FNGALPLRelygkfpeFIELMAIVRNIY 155
MntR COG1321
Mn-dependent transcriptional regulator MntR, DtxR family [Transcription];
52-118 3.78e-05

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


Pssm-ID: 440932 [Multi-domain]  Cd Length: 135  Bit Score: 40.96  E-value: 3.78e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480339780  52 ILIALHVKPHASVSELSDMVISKMSTTTKIVYRLKDEGYIDtyscKEDGRItrVYLTDKGQEMITKI 118
Cdd:COG1321   15 IYELSEEGGPVRTSDIAERLGVSPPSVTEMLKKLEEKGLVE----YEPYGG--ITLTEEGRELALRI 75
PRK10870 PRK10870
transcriptional repressor MprA; Provisional
 8-113 2.61e-04

transcriptional repressor MprA; Provisional


Pssm-ID: 182795  Cd Length: 176  Bit Score: 39.35  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339780   8 FLPTADSFNL-----EDFPFYWI------SQVNAQYVQNIDNVLKKYGLDNSRRRILIALHVKPHASV--SELSDMVISK 74
Cdd:PRK10870   5 FTPIEQMLKFrasrhEDFPYQEIlltrlcMHMQSKLLENRNKMLKAQGINETLFMALITLESQENHSIqpSELSCALGSS 84

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 480339780  75 MSTTTKIVYRLKDEGYIDTYSCKEDGRITRVYLTDKGQE 113
Cdd:PRK10870  85 RTNATRIADELEKRGWIERRESDNDRRCLHLQLTEKGHE 123
CRABP1 cd19460
cellular retinoic acid-binding protein 1; Cellular retinoic acid-binding proteins (CRABPs) ...
 34-97 2.69e-04

cellular retinoic acid-binding protein 1; Cellular retinoic acid-binding proteins (CRABPs) play a role in the metabolism of vitamin A and retinoic acid. They bind all trans retinoic acid, but not retinol. Retinol, the alcohol form of vitamin A, is an essential dietary nutrient. Within the cell, it gets oxidized into its biologically active acid form, retinoic acid, which interacts with the nuclear receptors (RARs and RXRs). The two CRABPs (CRABP1 AND CRABP2) differ in their pattern of expression across cells and developmental stages. Like other lipid binding proteins, CRABPs serve to solubilize and protect their ligand in the aqueous cytosol and transport retinoic acid between cellular compartments. This subgroup includes CRABP1 (also known as CRABP, CRABP-I, CRABPI, RBP5), which is thought to play an important role in retinoic acid-mediated differentiation and proliferation processes. CRABP1 has been shown to modulate stem cell proliferation to affect learning and memory. It has also been shown to regulate CaMKII, excessive and/or persistent activation of which is detrimental in acute and chronic cardiac injury. CRABPs belong to the intracellular fatty acid-binding protein (FABP) family, members of which are small proteins that bind hydrophobic ligands in a non-covalent, reversible manner, and besides CRABPS include the cellular retinol-binding protein (CRBPs) and the fatty acid-binding proteins (FABPs).


Pssm-ID: 381235  Cd Length: 136  Bit Score: 38.86  E-value: 2.69e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480339780  34 QNIDNVLKKYGLDNSRRRILIALHVKPHASVSELSDMVISKMST---TTKIVYRLK---DEGYIDTYSCK 97
Cdd:cd19460   13 ENFDELLKALGVNAMLRKVAVAAASKPHVEIRQDGDQFYIKTSTtvrTTEINFKVGeefEEETVDGRKCR 82
MarR pfam01047
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ...
 51-103 7.30e-04

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: 35.99  E-value: 7.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 480339780   51 RILIALHVKPHASVSELSDMVISKMSTTTKIVYRLKDEGYIDTYSCKEDGRIT 103
Cdd:pfam01047   7 HILRILYEHGPLTVSELAEKLGVSKSTVTRVLDRLEKKGLIERSRSPEDRREV 59
HTH_24 pfam13412
Winged helix-turn-helix DNA-binding;
49-91 9.94e-04

Winged helix-turn-helix DNA-binding;


Pssm-ID: 404317 [Multi-domain]  Cd Length: 45  Bit Score: 35.10  E-value: 9.94e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 480339780   49 RRRILIALHVKPHASVSELSDMV-ISKmSTTTKIVYRLKDEGYI 91
Cdd:pfam13412   3 DRKILNLLQENPRISQRELAERLgLSP-STVNRRLKRLEEEGVI 45
 
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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