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Conserved domains on  [gi|489917817|ref|WP_003821182|]
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heat-inducible transcriptional repressor HrcA [Bordetella bronchiseptica]

Protein Classification

HrcA family transcriptional regulator( domain architecture ID 11444430)

HrcA family transcriptional regulator such as heat-inducible transcription repressor HrcA, which is a negative regulator of class I heat shock genes (grpE-dnaK-dnaJ and groELS operons)

Gene Ontology:  GO:0009408|GO:0003677|GO:0006355
PubMed:  9266682
SCOP:  4000169

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HrcA COG1420
Transcriptional regulator of heat shock response [Transcription];
1-332 1.77e-148

Transcriptional regulator of heat shock response [Transcription];


:

Pssm-ID: 441030 [Multi-domain]  Cd Length: 339  Bit Score: 421.06  E-value: 1.77e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817   1 MDDRARALLKALIERYIADGQPVGSRTLSKVFDL--SPATIRNVMADLEELGLIHSPHTSAGRVPTPRGYRMFVDSLLAV 78
Cdd:COG1420    1 LDERQREILRAIVEDYIATGEPVGSRTLAKRYGLgvSPATIRNEMADLEELGLLEQPHTSAGRIPTDKGYRLYVDSLLEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817  79 RAY-QFEPAHIGELL--PVSEPSRAVNAAAALLSNLTQFAGVVLTPKRTQ-IFRQIEFIRLSDKRVLLIIVTPEGDVQNR 154
Cdd:COG1420   81 KPLsEEERRAIEAFLsqRAGDLEDLLQRAARLLSQLTNYAAVVLAPKLERaRLKHIELVPLSERRVLVVLVTDSGRVENR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817 155 ILSAQRDYTEAELLEAGNFFNVHFSGKSFDAVRRTLSTELAQLRDDISRLMQA--AVEAGAEAADDGEAVVISGERKLLD 232
Cdd:COG1420  161 VIELPEGLSEEELEELSNYLNARLAGLTLSEIRERLLEELEQELAEYDDLLRAllEALLEALSEEDEERLYVSGTSNLLR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817 233 VTDIaSDMDRLRKMFSLFEKKTDLLQLLDVSSRAQGVQIYIGGDSQLVPMEEVSVITAPYGLDGKVIGTLGVIGPTRMAY 312
Cdd:COG1420  241 QPEF-SDLEKLRELLELLEEKEVLLRLLDEAESAEGVQVFIGSENGLEGLKDCSVVTAPYRVGGKVVGTLGVIGPTRMDY 319
                        330       340
                 ....*....|....*....|
gi 489917817 313 ERVIPIVDITARLLSNALSH 332
Cdd:COG1420  320 ERVIPLVDYTARYLSRLLSK 339
 
Name Accession Description Interval E-value
HrcA COG1420
Transcriptional regulator of heat shock response [Transcription];
1-332 1.77e-148

Transcriptional regulator of heat shock response [Transcription];


Pssm-ID: 441030 [Multi-domain]  Cd Length: 339  Bit Score: 421.06  E-value: 1.77e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817   1 MDDRARALLKALIERYIADGQPVGSRTLSKVFDL--SPATIRNVMADLEELGLIHSPHTSAGRVPTPRGYRMFVDSLLAV 78
Cdd:COG1420    1 LDERQREILRAIVEDYIATGEPVGSRTLAKRYGLgvSPATIRNEMADLEELGLLEQPHTSAGRIPTDKGYRLYVDSLLEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817  79 RAY-QFEPAHIGELL--PVSEPSRAVNAAAALLSNLTQFAGVVLTPKRTQ-IFRQIEFIRLSDKRVLLIIVTPEGDVQNR 154
Cdd:COG1420   81 KPLsEEERRAIEAFLsqRAGDLEDLLQRAARLLSQLTNYAAVVLAPKLERaRLKHIELVPLSERRVLVVLVTDSGRVENR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817 155 ILSAQRDYTEAELLEAGNFFNVHFSGKSFDAVRRTLSTELAQLRDDISRLMQA--AVEAGAEAADDGEAVVISGERKLLD 232
Cdd:COG1420  161 VIELPEGLSEEELEELSNYLNARLAGLTLSEIRERLLEELEQELAEYDDLLRAllEALLEALSEEDEERLYVSGTSNLLR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817 233 VTDIaSDMDRLRKMFSLFEKKTDLLQLLDVSSRAQGVQIYIGGDSQLVPMEEVSVITAPYGLDGKVIGTLGVIGPTRMAY 312
Cdd:COG1420  241 QPEF-SDLEKLRELLELLEEKEVLLRLLDEAESAEGVQVFIGSENGLEGLKDCSVVTAPYRVGGKVVGTLGVIGPTRMDY 319
                        330       340
                 ....*....|....*....|
gi 489917817 313 ERVIPIVDITARLLSNALSH 332
Cdd:COG1420  320 ERVIPLVDYTARYLSRLLSK 339
hrcA TIGR00331
heat shock gene repressor HrcA; HrcA represses the class I heat shock operons groE and dnaK; ...
2-330 9.65e-100

heat shock gene repressor HrcA; HrcA represses the class I heat shock operons groE and dnaK; overproduction prevents induction of these operons by heat shock while deletion allows constitutive expression even at low temperatures. In Bacillus subtilis, hrcA is the first gene of the dnaK operon and so is itself a heat shock gene. [Regulatory functions, DNA interactions]


Pssm-ID: 273017 [Multi-domain]  Cd Length: 337  Bit Score: 297.27  E-value: 9.65e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817    2 DDRARALLKALIERYIADGQPVGSRTLSKVF--DLSPATIRNVMADLEELGLIHSPHTSAGRVPTPRGYRMFVDSLLAV- 78
Cdd:TIGR00331   1 TERQRKILKAIVEEYIKTGQPVGSKTLLEKYnlGLSSATIRNDMADLEDLGFIEKPHTSSGRIPTDKGYRYYVDHLLKVd 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817   79 RAYQFEPAHIGELL--PVSEPSRAVNAAAALLSNLTQFAGVVLTPKRTQ-IFRQIEFIRLSDKRVLLIIVTPEGDVQNRI 155
Cdd:TIGR00331  81 SLTEEEKRRIQNQFlqRRFYLEKVLQLAASLLSELTNYTAVVLGPRLSQdKLKHIELIPLDPNLALAVIVTDSGRVKNKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817  156 LSAQRDYTEAELLEAGNFFNVHFSGKSFDAVRRTLSTELAQLRDDISRLMQAAVEAGAE--AADDGEAVVISGERKLLDV 233
Cdd:TIGR00331 161 IELPANISQEDLERAVNILNDRLRGRTLSEIREQIIELLSQLKIEIEEFEDELVDLIISifSEFNEEELYVDGKSNLLEQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817  234 TDIASDMDRLRKMFSLFEKKTDLLQLLDVSSRAQGVQIYIGGDSQLVPMEEVSVITAPYGLDGKVIGTLGVIGPTRMAYE 313
Cdd:TIGR00331 241 PEFFDPIERIRELLELLESKKFLELLLNEALHEPGVTVKIGDENGDKSLEDFSVISSPYKIGGNPIGAIGVIGPKRMDYQ 320
                         330
                  ....*....|....*..
gi 489917817  314 RVIPIVDITARLLSNAL 330
Cdd:TIGR00331 321 RVIPLVNYIARLLSELL 337
HrcA pfam01628
HrcA protein C terminal domain; HrcA is found to negatively regulate the transcription of heat ...
101-316 3.34e-66

HrcA protein C terminal domain; HrcA is found to negatively regulate the transcription of heat shock genes. HrcA contains an amino terminal helix-turn-helix domain, however this corresponds to the carboxy terminal domain.


Pssm-ID: 460271  Cd Length: 221  Bit Score: 207.78  E-value: 3.34e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817  101 VNAAAALLSNLTQFAGVVLTPKRTQ-IFRQIEFIRLSDKRVLLIIVTPEGDVQNRILSAQRDYTEAELLEAGNFFNVHFS 179
Cdd:pfam01628   4 LQRAAKLLSELTNYAAVVLAPSLSEaRLKHIELVPLSERRALVVLVTDSGRVENRVIRLPEDISEEELEKLSNLLNERLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817  180 GKSFDAVRRTLSTELA--QLRDDISRLMQAAVEAGAEAADDgeaVVISGERKLLDVTDiASDMDRLRKMFSLFEKKTDLL 257
Cdd:pfam01628  84 GLTLSEIRERLLEELAlgEYDELLDAVLEALLEALEESEEE---VYVSGTSNLLNQPE-FSDDEKLRELLELLEEKEVLL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917817  258 QLLD---VSSRAQGVQIYIGGDSQLVPMEEVSVITAPYGLDGKVIGTLGVIGPTRMAYERVI 316
Cdd:pfam01628 160 ELLEealDSDDRSGVQVRIGSENPLEELKDCSVVTAPYGIGGKVVGTIGVIGPTRMDYAKVI 221
PRK03911 PRK03911
HrcA family transcriptional regulator;
8-64 2.69e-08

HrcA family transcriptional regulator;


Pssm-ID: 235174  Cd Length: 260  Bit Score: 53.88  E-value: 2.69e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489917817   8 LLKALIERYIADGQPVGSRTLSKVFDL--SPATIRNVMADLEELGLIHSPHTSAGRVPT 64
Cdd:PRK03911   8 LLDSIIQTYLQDNEPIGSNELKSLMNLkiSAATIRNYFKKLSDEGLLTQLHISGGRIPT 66
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
9-52 9.47e-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: 34.35  E-value: 9.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489917817   9 LKALIERYIADGQ-PVGS-----RTLSKVFDLSPATIRNVMADLEELGLI 52
Cdd:cd07377    6 IADQLREAILSGElKPGDrlpseRELAEELGVSRTTVREALRELEAEGLV 55
 
Name Accession Description Interval E-value
HrcA COG1420
Transcriptional regulator of heat shock response [Transcription];
1-332 1.77e-148

Transcriptional regulator of heat shock response [Transcription];


Pssm-ID: 441030 [Multi-domain]  Cd Length: 339  Bit Score: 421.06  E-value: 1.77e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817   1 MDDRARALLKALIERYIADGQPVGSRTLSKVFDL--SPATIRNVMADLEELGLIHSPHTSAGRVPTPRGYRMFVDSLLAV 78
Cdd:COG1420    1 LDERQREILRAIVEDYIATGEPVGSRTLAKRYGLgvSPATIRNEMADLEELGLLEQPHTSAGRIPTDKGYRLYVDSLLEV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817  79 RAY-QFEPAHIGELL--PVSEPSRAVNAAAALLSNLTQFAGVVLTPKRTQ-IFRQIEFIRLSDKRVLLIIVTPEGDVQNR 154
Cdd:COG1420   81 KPLsEEERRAIEAFLsqRAGDLEDLLQRAARLLSQLTNYAAVVLAPKLERaRLKHIELVPLSERRVLVVLVTDSGRVENR 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817 155 ILSAQRDYTEAELLEAGNFFNVHFSGKSFDAVRRTLSTELAQLRDDISRLMQA--AVEAGAEAADDGEAVVISGERKLLD 232
Cdd:COG1420  161 VIELPEGLSEEELEELSNYLNARLAGLTLSEIRERLLEELEQELAEYDDLLRAllEALLEALSEEDEERLYVSGTSNLLR 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817 233 VTDIaSDMDRLRKMFSLFEKKTDLLQLLDVSSRAQGVQIYIGGDSQLVPMEEVSVITAPYGLDGKVIGTLGVIGPTRMAY 312
Cdd:COG1420  241 QPEF-SDLEKLRELLELLEEKEVLLRLLDEAESAEGVQVFIGSENGLEGLKDCSVVTAPYRVGGKVVGTLGVIGPTRMDY 319
                        330       340
                 ....*....|....*....|
gi 489917817 313 ERVIPIVDITARLLSNALSH 332
Cdd:COG1420  320 ERVIPLVDYTARYLSRLLSK 339
hrcA TIGR00331
heat shock gene repressor HrcA; HrcA represses the class I heat shock operons groE and dnaK; ...
2-330 9.65e-100

heat shock gene repressor HrcA; HrcA represses the class I heat shock operons groE and dnaK; overproduction prevents induction of these operons by heat shock while deletion allows constitutive expression even at low temperatures. In Bacillus subtilis, hrcA is the first gene of the dnaK operon and so is itself a heat shock gene. [Regulatory functions, DNA interactions]


Pssm-ID: 273017 [Multi-domain]  Cd Length: 337  Bit Score: 297.27  E-value: 9.65e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817    2 DDRARALLKALIERYIADGQPVGSRTLSKVF--DLSPATIRNVMADLEELGLIHSPHTSAGRVPTPRGYRMFVDSLLAV- 78
Cdd:TIGR00331   1 TERQRKILKAIVEEYIKTGQPVGSKTLLEKYnlGLSSATIRNDMADLEDLGFIEKPHTSSGRIPTDKGYRYYVDHLLKVd 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817   79 RAYQFEPAHIGELL--PVSEPSRAVNAAAALLSNLTQFAGVVLTPKRTQ-IFRQIEFIRLSDKRVLLIIVTPEGDVQNRI 155
Cdd:TIGR00331  81 SLTEEEKRRIQNQFlqRRFYLEKVLQLAASLLSELTNYTAVVLGPRLSQdKLKHIELIPLDPNLALAVIVTDSGRVKNKV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817  156 LSAQRDYTEAELLEAGNFFNVHFSGKSFDAVRRTLSTELAQLRDDISRLMQAAVEAGAE--AADDGEAVVISGERKLLDV 233
Cdd:TIGR00331 161 IELPANISQEDLERAVNILNDRLRGRTLSEIREQIIELLSQLKIEIEEFEDELVDLIISifSEFNEEELYVDGKSNLLEQ 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817  234 TDIASDMDRLRKMFSLFEKKTDLLQLLDVSSRAQGVQIYIGGDSQLVPMEEVSVITAPYGLDGKVIGTLGVIGPTRMAYE 313
Cdd:TIGR00331 241 PEFFDPIERIRELLELLESKKFLELLLNEALHEPGVTVKIGDENGDKSLEDFSVISSPYKIGGNPIGAIGVIGPKRMDYQ 320
                         330
                  ....*....|....*..
gi 489917817  314 RVIPIVDITARLLSNAL 330
Cdd:TIGR00331 321 RVIPLVNYIARLLSELL 337
HrcA pfam01628
HrcA protein C terminal domain; HrcA is found to negatively regulate the transcription of heat ...
101-316 3.34e-66

HrcA protein C terminal domain; HrcA is found to negatively regulate the transcription of heat shock genes. HrcA contains an amino terminal helix-turn-helix domain, however this corresponds to the carboxy terminal domain.


Pssm-ID: 460271  Cd Length: 221  Bit Score: 207.78  E-value: 3.34e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817  101 VNAAAALLSNLTQFAGVVLTPKRTQ-IFRQIEFIRLSDKRVLLIIVTPEGDVQNRILSAQRDYTEAELLEAGNFFNVHFS 179
Cdd:pfam01628   4 LQRAAKLLSELTNYAAVVLAPSLSEaRLKHIELVPLSERRALVVLVTDSGRVENRVIRLPEDISEEELEKLSNLLNERLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489917817  180 GKSFDAVRRTLSTELA--QLRDDISRLMQAAVEAGAEAADDgeaVVISGERKLLDVTDiASDMDRLRKMFSLFEKKTDLL 257
Cdd:pfam01628  84 GLTLSEIRERLLEELAlgEYDELLDAVLEALLEALEESEEE---VYVSGTSNLLNQPE-FSDDEKLRELLELLEEKEVLL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489917817  258 QLLD---VSSRAQGVQIYIGGDSQLVPMEEVSVITAPYGLDGKVIGTLGVIGPTRMAYERVI 316
Cdd:pfam01628 160 ELLEealDSDDRSGVQVRIGSENPLEELKDCSVVTAPYGIGGKVVGTIGVIGPTRMDYAKVI 221
PRK03911 PRK03911
HrcA family transcriptional regulator;
8-64 2.69e-08

HrcA family transcriptional regulator;


Pssm-ID: 235174  Cd Length: 260  Bit Score: 53.88  E-value: 2.69e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 489917817   8 LLKALIERYIADGQPVGSRTLSKVFDL--SPATIRNVMADLEELGLIHSPHTSAGRVPT 64
Cdd:PRK03911   8 LLDSIIQTYLQDNEPIGSNELKSLMNLkiSAATIRNYFKKLSDEGLLTQLHISGGRIPT 66
HrcA_DNA-bdg pfam03444
Winged helix-turn-helix transcription repressor, HrcA DNA-binding; This domain is always found ...
6-69 3.26e-08

Winged helix-turn-helix transcription repressor, HrcA DNA-binding; This domain is always found with a pair of CBS domains pfam00571.


Pssm-ID: 281443 [Multi-domain]  Cd Length: 79  Bit Score: 50.02  E-value: 3.26e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489917817    6 RALLKALIERYIADGQPVGSRTLSKVFDLSPATIRNVMADLEELGLIHS-PHTSAGRVPTPRGYR 69
Cdd:pfam03444   7 KEILQALINLYRKKGRAVKGEEIADIIGRNPGTVRNQMQSLKALGLVEGvPGPKGGYKPTSKAYE 71
Rrf2 pfam02082
Iron-dependent Transcriptional regulator; Several proteins in this family form iron-sulfur ...
9-54 1.13e-03

Iron-dependent Transcriptional regulator; Several proteins in this family form iron-sulfur clusters enabling iron dependent DNA transcription regulation. The iron binding is mediated by three conserved cysteine residues. Members of this family can also bind O-acetyl-L-serine, [Fe-S] and nitric oxide (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 396591 [Multi-domain]  Cd Length: 131  Bit Score: 38.69  E-value: 1.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 489917817    9 LKALIerYIA---DGQPVGSRTLSKVFDLSPATIRNVMADLEELGLIHS 54
Cdd:pfam02082   9 LHALL--YLAlhpGGEPVTSEEIAERQNISPVYLEKILAKLRKAGLVES 55
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
9-52 9.47e-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: 34.35  E-value: 9.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 489917817   9 LKALIERYIADGQ-PVGS-----RTLSKVFDLSPATIRNVMADLEELGLI 52
Cdd:cd07377    6 IADQLREAILSGElKPGDrlpseRELAEELGVSRTTVREALRELEAEGLV 55
 
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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