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Conserved domains on  [gi|488473531|ref|WP_002517201|]
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MULTISPECIES: Crp/Fnr family transcriptional regulator [Cutibacterium]

Protein Classification

Crp/Fnr family transcriptional regulator( domain architecture ID 11429533)

Crp/Fnr family transcriptional regulator containing a DNA-binding Crp-like helix-turn-helix (HTH) domain, may bind cyclic nucleotides

CATH:  2.60.120.10|1.10.10.10
Gene Ontology:  GO:0003677|GO:0030552
PubMed:  11407111|14638413

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 24-242 6.61e-42

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


:

Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 141.66  E-value: 6.61e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531  24 FATLGAASAARIMAMCEASVCPRNTVIFEAGDSADNLYLVVEGKVKLTRsTTADDltpRDSLLWLMGPSDMFGELSLVDG 103
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYR-ISEDG---REQILGFLGPGDFFGELSLLGG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531 104 GTRSTTATTVTRCSLLKTPGAQMRELVKGRHDVALAMLGRLSERLRRADDNTAHFVSGDVPSRLAYTLLDLARRFGTanp 183
Cdd:COG0664   77 EPSPATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLDG--- 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488473531 184 stghiVVRHDLTQHELAQAVGSSRETVNKALTDFAARGWIAARPKVVTIMEPEKLASRA 242
Cdd:COG0664  154 -----RIDLPLTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDREALERLA 207
 
Name Accession Description Interval E-value
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 24-242 6.61e-42

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 141.66  E-value: 6.61e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531  24 FATLGAASAARIMAMCEASVCPRNTVIFEAGDSADNLYLVVEGKVKLTRsTTADDltpRDSLLWLMGPSDMFGELSLVDG 103
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYR-ISEDG---REQILGFLGPGDFFGELSLLGG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531 104 GTRSTTATTVTRCSLLKTPGAQMRELVKGRHDVALAMLGRLSERLRRADDNTAHFVSGDVPSRLAYTLLDLARRFGTanp 183
Cdd:COG0664   77 EPSPATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLDG--- 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488473531 184 stghiVVRHDLTQHELAQAVGSSRETVNKALTDFAARGWIAARPKVVTIMEPEKLASRA 242
Cdd:COG0664  154 -----RIDLPLTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDREALERLA 207
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
34-232 1.11e-20

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 86.57  E-value: 1.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531  34 RIMAMCEASVCPRNTVIFEAGDSADNLYLVVEGKVkltrSTTADDLTPRDSLLWLMGPSDMFGELSLVD-GGTRSTTATT 112
Cdd:PRK11753  15 WFLSHCHIHKYPAKSTLIHAGEKAETLYYIVKGSV----AVLIKDEEGKEMILSYLNQGDFIGELGLFEeGQERSAWVRA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531 113 VTRCSLLKTPGAQMRELVKGRHDVALAMLGRLSERLRRADDNTAHFVSGDVPSRLAYTLLDLARR-FGTANPSTGHIVVr 191
Cdd:PRK11753  91 KTACEVAEISYKKFRQLIQVNPDILMALSAQMARRLQNTSRKVGDLAFLDVTGRIAQTLLDLAKQpDAMTHPDGMQIKI- 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 488473531 192 hdlTQHELAQAVGSSRETVNKALTDFAARGWIAARPKVVTI 232
Cdd:PRK11753 170 ---TRQEIGRIVGCSREMVGRVLKMLEDQGLISAHGKTIVV 207
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 45-131 7.08e-14

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 64.94  E-value: 7.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531   45 PRNTVIFEAGDSADNLYLVVEGKVKLTRsTTADDltpRDSLLWLMGPSDMFGELSLVDGGTRSTTATTVTRCSLLKTPGA 124
Cdd:pfam00027   5 KAGEVIFREGDPADSLYIVLSGKVKVYR-TLEDG---REQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRE 80


                  ....*..
gi 488473531  125 QMRELVK 131
Cdd:pfam00027  81 DFLELLE 87
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 23-141 2.42e-12

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 61.57  E-value: 2.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531  23 FFATLGAASAARIMAMCEASVCPRNTVIFEAGDSADNLYLVVEGKVKLTRSTTADdltpRDSLLWLMGPSDMFGELSLVD 102
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDG----REQIVGFLGPGDLFGELALLG 76

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488473531 103 GGTRSTTATTVTRCSLLKTPGAQMRELVKGRHDVALAML 141
Cdd:cd00038   77 NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 23-103 5.01e-10

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 55.48  E-value: 5.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531    23 FFATLGAASAARIMAMCEASVCPRNTVIFEAGDSADNLYLVVEGKVKLTRSTTADdltpRDSLLWLMGPSDMFGELSLVD 102
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDG----EEQIVGTLGPGDFFGELALLT 76


                   .
gi 488473531   103 G 103
Cdd:smart00100  77 N 77
 
Name Accession Description Interval E-value
Crp COG0664
cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal ...
 24-242 6.61e-42

cAMP-binding domain of CRP or a regulatory subunit of cAMP-dependent protein kinases [Signal transduction mechanisms];


Pssm-ID: 440428 [Multi-domain]  Cd Length: 207  Bit Score: 141.66  E-value: 6.61e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531  24 FATLGAASAARIMAMCEASVCPRNTVIFEAGDSADNLYLVVEGKVKLTRsTTADDltpRDSLLWLMGPSDMFGELSLVDG 103
Cdd:COG0664    1 FAGLSDEELEALLAHLELRTLKKGEVLFREGDPADHLYFVLSGLVKLYR-ISEDG---REQILGFLGPGDFFGELSLLGG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531 104 GTRSTTATTVTRCSLLKTPGAQMRELVKGRHDVALAMLGRLSERLRRADDNTAHFVSGDVPSRLAYTLLDLARRFGTanp 183
Cdd:COG0664   77 EPSPATAEALEDSELLRIPREDLEELLERNPELARALLRLLARRLRQLQERLVSLAFLSAEERLARFLLELADRLDG--- 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488473531 184 stghiVVRHDLTQHELAQAVGSSRETVNKALTDFAARGWIAARPKVVTIMEPEKLASRA 242
Cdd:COG0664  154 -----RIDLPLTQEEIASYLGLTRETVSRILKKLEKEGLIELERGRITILDREALERLA 207
PRK11753 PRK11753
cAMP-activated global transcriptional regulator CRP;
34-232 1.11e-20

cAMP-activated global transcriptional regulator CRP;


Pssm-ID: 236969 [Multi-domain]  Cd Length: 211  Bit Score: 86.57  E-value: 1.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531  34 RIMAMCEASVCPRNTVIFEAGDSADNLYLVVEGKVkltrSTTADDLTPRDSLLWLMGPSDMFGELSLVD-GGTRSTTATT 112
Cdd:PRK11753  15 WFLSHCHIHKYPAKSTLIHAGEKAETLYYIVKGSV----AVLIKDEEGKEMILSYLNQGDFIGELGLFEeGQERSAWVRA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531 113 VTRCSLLKTPGAQMRELVKGRHDVALAMLGRLSERLRRADDNTAHFVSGDVPSRLAYTLLDLARR-FGTANPSTGHIVVr 191
Cdd:PRK11753  91 KTACEVAEISYKKFRQLIQVNPDILMALSAQMARRLQNTSRKVGDLAFLDVTGRIAQTLLDLAKQpDAMTHPDGMQIKI- 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 488473531 192 hdlTQHELAQAVGSSRETVNKALTDFAARGWIAARPKVVTI 232
Cdd:PRK11753 170 ---TRQEIGRIVGCSREMVGRVLKMLEDQGLISAHGKTIVV 207
cNMP_binding pfam00027
Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, ...
 45-131 7.08e-14

Cyclic nucleotide-binding domain; This domain sensor domain can bind cAMP, cGMP, c-di-GMP, oxygen and 2-oxoglutarate (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 459637 [Multi-domain]  Cd Length: 89  Bit Score: 64.94  E-value: 7.08e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531   45 PRNTVIFEAGDSADNLYLVVEGKVKLTRsTTADDltpRDSLLWLMGPSDMFGELSLVDGGTRSTTATTVTRCSLLKTPGA 124
Cdd:pfam00027   5 KAGEVIFREGDPADSLYIVLSGKVKVYR-TLEDG---REQILAVLGPGDFFGELALLGGEPRSATVVALTDSELLVIPRE 80


                  ....*..
gi 488473531  125 QMRELVK 131
Cdd:pfam00027  81 DFLELLE 87
HTH_Crp_2 pfam13545
Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain ...
 166-241 7.80e-13

Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain that is likely to bind DNA.


Pssm-ID: 463917 [Multi-domain]  Cd Length: 68  Bit Score: 61.70  E-value: 7.80e-13
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488473531  166 RLAYTLLDLARRfgtanpsTGHIVVRHDLTQHELAQAVGSSRETVNKALTDFAARGWIAARPkvVTIMEPEKLASR 241
Cdd:pfam13545   2 RLARFLLELAAR-------DGGGRIDLPLTQEDLADLLGTTRETVSRVLSELRREGLIERGR--ITILDPEALEAL 68
CAP_ED cd00038
effector domain of the CAP family of transcription factors; members include CAP (or cAMP ...
 23-141 2.42e-12

effector domain of the CAP family of transcription factors; members include CAP (or cAMP receptor protein (CRP)), which binds cAMP, FNR (fumarate and nitrate reduction), which uses an iron-sulfur cluster to sense oxygen) and CooA, a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. Cyclic nucleotide-binding domain similar to CAP are also present in cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) and vertebrate cyclic nucleotide-gated ion-channels. Cyclic nucleotide-monophosphate binding domain; proteins that bind cyclic nucleotides (cAMP or cGMP) share a structural domain of about 120 residues; the best studied is the prokaryotic catabolite gene activator, CAP, where such a domain is known to be composed of three alpha-helices and a distinctive eight-stranded, antiparallel beta-barrel structure; three conserved glycine residues are thought to be essential for maintenance of the structural integrity of the beta-barrel; CooA is a homodimeric transcription factor that belongs to CAP family; cAMP- and cGMP-dependent protein kinases (cAPK and cGPK) contain two tandem copies of the cyclic nucleotide-binding domain; cAPK's are composed of two different subunits, a catalytic chain and a regulatory chain, which contains both copies of the domain; cGPK's are single chain enzymes that include the two copies of the domain in their N-terminal section; also found in vertebrate cyclic nucleotide-gated ion-channels


Pssm-ID: 237999 [Multi-domain]  Cd Length: 115  Bit Score: 61.57  E-value: 2.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531  23 FFATLGAASAARIMAMCEASVCPRNTVIFEAGDSADNLYLVVEGKVKLTRSTTADdltpRDSLLWLMGPSDMFGELSLVD 102
Cdd:cd00038    1 LFSGLDDEELEELADALEERRFPAGEVIIRQGDPADSLYIVLSGSVEVYKLDEDG----REQIVGFLGPGDLFGELALLG 76

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488473531 103 GGTRSTTATTVTRCSLLKTPGAQMRELVKGRHDVALAML 141
Cdd:cd00038   77 NGPRSATVRALTDSELLVLPRSDFRRLLQEYPELARRLL 115
cNMP smart00100
Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a ...
 23-103 5.01e-10

Cyclic nucleotide-monophosphate binding domain; Catabolite gene activator protein (CAP) is a prokaryotic homologue of eukaryotic cNMP-binding domains, present in ion channels, and cNMP-dependent kinases.


Pssm-ID: 197516 [Multi-domain]  Cd Length: 120  Bit Score: 55.48  E-value: 5.01e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531    23 FFATLGAASAARIMAMCEASVCPRNTVIFEAGDSADNLYLVVEGKVKLTRSTTADdltpRDSLLWLMGPSDMFGELSLVD 102
Cdd:smart00100   1 LFKNLDAEELRELADALEPVRYPAGEVIIRQGDVGDSFYIIVSGEVEVYKVLEDG----EEQIVGTLGPGDFFGELALLT 76


                   .
gi 488473531   103 G 103
Cdd:smart00100  77 N 77
HTH_CRP smart00419
helix_turn_helix, cAMP Regulatory protein;
186-232 5.73e-09

helix_turn_helix, cAMP Regulatory protein;


Pssm-ID: 128696 [Multi-domain]  Cd Length: 48  Bit Score: 50.52  E-value: 5.73e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 488473531   186 GHIVVRHDLTQHELAQAVGSSRETVNKALTDFAARGWIAARPKVVTI 232
Cdd:smart00419   1 EGIRVRLPLTRQEIAELLGLTRETVSRTLKRLEKEGLISREGGRIVI 47
HTH_CRP cd00092
helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic ...
 165-233 3.76e-08

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


Pssm-ID: 238044 [Multi-domain]  Cd Length: 67  Bit Score: 48.82  E-value: 3.76e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531 165 SRLAYTLLDLARRFGTANPSTGHivvrhdLTQHELAQAVGSSRETVNKALTDFAARGWIAARP-KVVTIM 233
Cdd:cd00092    3 ERLASFLLNLSLRYGAGDLVQLP------LTRQEIADYLGLTRETVSRTLKELEEEGLISRRGrGKYRVN 66
ftrB PRK09392
transcriptional activator FtrB; Provisional
 21-239 7.16e-08

transcriptional activator FtrB; Provisional


Pssm-ID: 181817 [Multi-domain]  Cd Length: 236  Bit Score: 51.56  E-value: 7.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531  21 QPFFATLGAASAARIMAMCEASVCPRNTVIFEAGDSADNLYLVVEGKVKLtrSTTADDltpRDSLLWLMGPSDMFGELSL 100
Cdd:PRK09392  12 LPLFADMADATFERLMRGAFLQRFPPGTMLITEGEPADFLFVVLDGLVEL--SASSQD---RETTLAILRPVSTFILAAV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531 101 VDGGTRSTTATTVTRCSLLKTPGAQMRELVKGRHDVALAMLGRLSERLRRADDNTAHFVSGDVPSRLAYTLLDLARRFGT 180
Cdd:PRK09392  87 VLDAPYLMSARTLTRSRVLMIPAELVREAMSEDPGFMRAVVFELAGCYRGLVKSLKNQKLRSSAERLANYLLKQSLRQGG 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488473531 181 ANpstghiVVRHDLTQHELAQAVGSSRETVNKALTDFAARGwIAARPKVVTIMEPEKLA 239
Cdd:PRK09392 167 AD------VVTLPYEKRVLASYLGMTPENLSRAFAALASHG-VHVDGSAVTITDPAGLA 218
PRK13918 PRK13918
CRP/FNR family transcriptional regulator; Provisional
 46-242 1.80e-06

CRP/FNR family transcriptional regulator; Provisional


Pssm-ID: 237557 [Multi-domain]  Cd Length: 202  Bit Score: 47.12  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531  46 RNTVIFEAGD---------SADNLYLVVEGkvkLTRSTTADD----LTPRdsllwLMGPSDMFGELSLvdGGTRSTTATT 112
Cdd:PRK13918   6 VDTVTYRPGAvilypgvpgPSDMLYRVRSG---LVRLHTVDDegnaLTLR-----YVRPGEYFGEEAL--AGAERAYFAE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488473531 113 VTRCSLLKT--PGAQMRELVkgrHDVALamlgRLSERLRRADDNTAHFVSGDVPSRLAYTLLDLARRFGTANPSTGHIVV 190
Cdd:PRK13918  76 AVTDSRIDVlnPALMSAEDN---LVLTQ----HLVRTLARAYESIYRLVGQRLKNRIAAALLELSDTPLATQEDSGETMI 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488473531 191 RhdLTQHELAQAVGSSRETVNKALTDFAARGWIAARPKVVTIMEPEKLASRA 242
Cdd:PRK13918 149 Y--ATHDELAAAVGSVRETVTKVIGELSREGYIRSGYGKIQLLDLKGLEELA 198
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
 195-228 2.42e-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: 35.50  E-value: 2.42e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 488473531 195 TQHELAQAVGSSRETVNKALTDFAARGWIAARPK 228
Cdd:cd07377   27 SERELAEELGVSRTTVREALRELEAEGLVERRPG 60
 
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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