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Conserved domains on  [gi|446013715|ref|WP_000091570|]
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MULTISPECIES: GntR family transcriptional regulator [Enterobacteriaceae]

Protein Classification

GntR family transcriptional regulator( domain architecture ID 11706244)

GntR family transcriptional regulator binds a specific ligand that modulates DNA binding and the expression of genes encoding fatty acid biosynthetic and degrading enzymes

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GntR COG1802
DNA-binding transcriptional regulator, GntR family [Transcription];
93-301 2.22e-28

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


:

Pssm-ID: 441407 [Multi-domain]  Cd Length: 222  Bit Score: 108.86  E-value: 2.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715  93 QAFFTMINQRQLRPGETFSELQLARAAGVSPVVVREYLLKFGRYNLIHSEKRGQWSMKQFDQSYAEQLFELREMLETHSL 172
Cdd:COG1802   18 EALREAILSGELPPGERLSEAELAERLGVSRTPVREALRRLEAEGLVEIRPNRGARVAPLSPEEIRELYEVRAALEGLAA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715 173 QHFLNLpdHDPRWLQAktMLERHRLLRDNI-GNSFRMFSQLDRDFHSLLLSAADNIFFDQSLEIISVIFHFhYQWDESDL 251
Cdd:COG1802   98 RLAAER--ATPADLAR--LRALLEELEAAAaAGDVAAYLELDREFHRALVEAAGNPRLAELLRRLRARLRR-YRRLSLRS 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446013715 252 KQRNIIAVDEHMTILSALICRSDLDATLALRNHLNSAKQSMIRSINENTR 301
Cdd:COG1802  173 PGRLEESLAEHRAILDALEAGDAEAAAAALRAHLERARERLLEALAAAAA 222
HTH_ARSR super family cl46857
Arsenical Resistance Operon Repressor and similar prokaryotic, metal regulated homodimeric ...
 7-59 1.65e-07

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.


The actual alignment was detected with superfamily member cd07377:

Pssm-ID: 481197 [Multi-domain]  Cd Length: 66  Bit Score: 47.44  E-value: 1.65e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446013715   7 LRHNVINQVIDDMARGHIP--SPLPSQSALAEMYNISRTTVRHILSHLRECGVLT 59
Cdd:cd07377    2 LYEQIADQLREAILSGELKpgDRLPSERELAEELGVSRTTVREALRELEAEGLVE 56
 
Name Accession Description Interval E-value
GntR COG1802
DNA-binding transcriptional regulator, GntR family [Transcription];
93-301 2.22e-28

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


Pssm-ID: 441407 [Multi-domain]  Cd Length: 222  Bit Score: 108.86  E-value: 2.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715  93 QAFFTMINQRQLRPGETFSELQLARAAGVSPVVVREYLLKFGRYNLIHSEKRGQWSMKQFDQSYAEQLFELREMLETHSL 172
Cdd:COG1802   18 EALREAILSGELPPGERLSEAELAERLGVSRTPVREALRRLEAEGLVEIRPNRGARVAPLSPEEIRELYEVRAALEGLAA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715 173 QHFLNLpdHDPRWLQAktMLERHRLLRDNI-GNSFRMFSQLDRDFHSLLLSAADNIFFDQSLEIISVIFHFhYQWDESDL 251
Cdd:COG1802   98 RLAAER--ATPADLAR--LRALLEELEAAAaAGDVAAYLELDREFHRALVEAAGNPRLAELLRRLRARLRR-YRRLSLRS 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446013715 252 KQRNIIAVDEHMTILSALICRSDLDATLALRNHLNSAKQSMIRSINENTR 301
Cdd:COG1802  173 PGRLEESLAEHRAILDALEAGDAEAAAAALRAHLERARERLLEALAAAAA 222
FCD smart00895
This entry represents the C-terminal ligand binding domain of many members of the GntR family; ...
 159-287 3.87e-10

This entry represents the C-terminal ligand binding domain of many members of the GntR family; This domain probably binds to a range of effector molecules that regulate the transcription of genes through the action of the N-terminal DNA-binding domain. This domain is found in and that are regulators of sugar biosynthesis operons. Many bacterial transcription regulation proteins bind DNA through a helix-turn-helix (HTH) motif, which can be classified into subfamilies on the basis of sequence similarities. The HTH GntR family has many members distributed among diverse bacterial groups that regulate various biological processes. It was named GntR after the Bacillus subtilis repressor of the gluconate operon. In general, these proteins contain a DNA-binding HTH domain at the N terminus, and an effector binding or oligomerisation domain at the C terminus. The winged-helix DNA-binding domain is well conserved in structure for the whole of the GntR family, and is similar in structure to other transcriptional regulator families. The C-terminal effector-binding and oligomerisation domains are more variable and are consequently used to define the subfamilies. Based on the sequence and structure of the C-terminal domains, the GtnR family can be divided into four major groups, as represented by FadR, HutC, MocR and YtrA, as well as some minor groups such as those represented by AraR and PlmA.


Pssm-ID: 214892 [Multi-domain]  Cd Length: 123  Bit Score: 56.60  E-value: 3.87e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715   159 QLFELREMLETHSLQHF-LNLPDHDPRWLQAktMLERHRLLRDNiGNSFRMFSQLDRDFHSLLLSAADNIFFDQSLEIIS 237
Cdd:smart00895   1 ELYEVRRALEPLAARLAaERATDEDLAALEA--LLDAMEAAAAA-GDDLEEFAELDREFHRALAEAAGNPVLLELLESLR 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 446013715   238 VIFHFHYQWDESDLKqrniIAVDEHMTILSALICRSDLDATLALRNHLNS 287
Cdd:smart00895  78 ARLRRLRRLSLEAAR----RALDEHRAILDAIRARDAEAARAAMREHLEA 123
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
 7-59 1.65e-07

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: 47.44  E-value: 1.65e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446013715   7 LRHNVINQVIDDMARGHIP--SPLPSQSALAEMYNISRTTVRHILSHLRECGVLT 59
Cdd:cd07377    2 LYEQIADQLREAILSGELKpgDRLPSERELAEELGVSRTTVREALRELEAEGLVE 56
FCD pfam07729
FCD domain; This domain is the C-terminal ligand binding domain of many members of the GntR ...
 159-283 8.10e-07

FCD domain; This domain is the C-terminal ligand binding domain of many members of the GntR family. This domain binds to a range of effector molecules, including Lactate, Zn(II), Ni(II), Ca(II), Mg(II), citrate, sugar acids, sialic acid and N-acetylglucosamine-6-P, that regulate the transcription of genes through the action of the N-terminal DNA-binding domain pfam00392 (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). This domain is found in Swiss:P45427 and Swiss:P31460 that are regulators of sugar biosynthesis operons. It is also in the known structure of FadR where it binds to acyl-coA, the domain is alpha helical. This family has been named as FCD for (FadR C-terminal Domain).


Pssm-ID: 429623 [Multi-domain]  Cd Length: 121  Bit Score: 47.36  E-value: 8.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715  159 QLFELREMLETHSL-QHFLNLPDHDPRWLQAktMLERHRLLRDNigNSFRMFSQLDRDFHSLLLSAADNIFFDQSLEIIS 237
Cdd:pfam07729   1 ELYELRAALEPLAArLAAERATDEDLAELEA--LLEALEAAADA--GDLEAFAEADREFHLALAEAAGNPVLARMLESLW 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 446013715  238 VIFHfHYQWDESDLKQRNIIAVDEHMTILSALICRSDLDATLALRN 283
Cdd:pfam07729  77 DRLR-RLRRLLLSSPGRLRASLEEHRAILDAIRARDPEAARAAMRR 121
GntR pfam00392
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ...
 10-59 5.32e-05

Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the N-terminal HTH region of GntR-like bacterial transcription factors. At the C-terminus there is usually an effector-binding/oligomerization domain. The GntR-like proteins include the following sub-families: MocR, YtrR, FadR, AraR, HutC and PlmA, DevA, DasR. Many of these proteins have been shown experimentally to be autoregulatory, enabling the prediction of operator sites and the discovery of cis/trans relationships. The DasR regulator has been shown to be a global regulator of primary metabolism and development in Streptomyces coelicolor.


Pssm-ID: 306822 [Multi-domain]  Cd Length: 64  Bit Score: 40.29  E-value: 5.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446013715   10 NVINQVIDDMARGHIP--SPLPSQSALAEMYNISRTTVRHILSHLRECGVLT 59
Cdd:pfam00392   4 QVYARLREDILSGRLRpgDKLPSERELAAEFGVSRTTVREALRRLEAEGLVE 55
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
11-59 4.33e-04

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 37.94  E-value: 4.33e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 446013715    11 VINQVIDDMARGHIPS--PLPSQSALAEMYNISRTTVRHILSHLRECGVLT 59
Cdd:smart00345   1 VAERLREDIVSGELRPgdKLPSERELAAQLGVSRTTVREALSRLEAEGLVQ 51
PRK11402 PRK11402
transcriptional regulator PhoB;
4-58 7.66e-04

transcriptional regulator PhoB;


Pssm-ID: 183118 [Multi-domain]  Cd Length: 241  Bit Score: 40.20  E-value: 7.66e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446013715   4 SQNLRHNVINQVIDDMARGhIPSP---LPSQSALAEMYNISRTTVRHILSHLRECGVL 58
Cdd:PRK11402   7 HQLLYATVRQRLLDDIAQG-VYQAgqqIPTENELCTQYNVSRITIRKAISDLVADGVL 63
PRK10225 PRK10225
Uxu operon transcriptional regulator;
98-297 1.69e-03

Uxu operon transcriptional regulator;


Pssm-ID: 182318 [Multi-domain]  Cd Length: 257  Bit Score: 39.23  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715  98 MINQRQLRPGETFS-ELQLARAAGVSPVVVREYLLKFGRYNLIHS---------EKRGQWSMKQFDQSYAE-----QLFE 162
Cdd:PRK10225  21 LIIKTPYNPGERLPpEREIAEMLDVTRTVVREALIMLEIKGLVEVrrgagiyvlDSSGSHNTDSPDANVCNdagpfELLQ 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715 163 LREMLEThSLQHF--LNLPDHDPRWLQAKTMLERHRLLRDNIGNSfrmfSQLDRDFHSLLLSAADNiffdqslEIISVIF 240
Cdd:PRK10225 101 ARQLLES-NIAEFaaLQATREDIVKMRQALQLEERELASSAPGSS----ESGDMQFHLAIAEATHN-------SMLVELF 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446013715 241 HFHYQWDES------------DLKQRNIIAVDeHMTILSALICRSDLDATLALRNHLNSAKQSMIRSIN 297
Cdd:PRK10225 169 RQSWQWRENnpmwiqlhshldDSLYRKEWLGD-HKQILAALIKKDARAAKLAMWQHLENVKQRLLEFSN 236
IscR COG1959
DNA-binding transcriptional regulator, IscR family [Transcription];
18-72 2.47e-03

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


Pssm-ID: 441562  Cd Length: 141  Bit Score: 37.51  E-value: 2.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715  18 DMARGHIPSPLPSqSALAEMYNISRTTVRHILSHLRECGVLTQV-----GndYVIARKPD 72
Cdd:COG1959   15 YLALHPGGEPVTS-KEIAERQGISPSYLEKILQKLRKAGLVESVrgpggG--YRLARPPE 71
 
Name Accession Description Interval E-value
GntR COG1802
DNA-binding transcriptional regulator, GntR family [Transcription];
93-301 2.22e-28

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


Pssm-ID: 441407 [Multi-domain]  Cd Length: 222  Bit Score: 108.86  E-value: 2.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715  93 QAFFTMINQRQLRPGETFSELQLARAAGVSPVVVREYLLKFGRYNLIHSEKRGQWSMKQFDQSYAEQLFELREMLETHSL 172
Cdd:COG1802   18 EALREAILSGELPPGERLSEAELAERLGVSRTPVREALRRLEAEGLVEIRPNRGARVAPLSPEEIRELYEVRAALEGLAA 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715 173 QHFLNLpdHDPRWLQAktMLERHRLLRDNI-GNSFRMFSQLDRDFHSLLLSAADNIFFDQSLEIISVIFHFhYQWDESDL 251
Cdd:COG1802   98 RLAAER--ATPADLAR--LRALLEELEAAAaAGDVAAYLELDREFHRALVEAAGNPRLAELLRRLRARLRR-YRRLSLRS 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 446013715 252 KQRNIIAVDEHMTILSALICRSDLDATLALRNHLNSAKQSMIRSINENTR 301
Cdd:COG1802  173 PGRLEESLAEHRAILDALEAGDAEAAAAALRAHLERARERLLEALAAAAA 222
FadR COG2186
DNA-binding transcriptional regulator, FadR family [Transcription];
97-301 6.98e-13

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


Pssm-ID: 441789 [Multi-domain]  Cd Length: 232  Bit Score: 66.88  E-value: 6.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715  97 TMINQRQLRPGETF-SELQLARAAGVSPVVVREYLLKFGRYNLIHSEKRG--------QWSM-------KQFDQSYAEQL 160
Cdd:COG2186   18 ELILSGELKPGDRLpSERELAEQLGVSRTTVREALRALEALGLVEVRQGGgtfvrepsPWALldplallLALDDASLRDL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715 161 FELREMLETHSLQH-FLNLPDHDprwlqAKTMLERHRLLRDNIGNSfRMFSQLDRDFHSLLLSAADNIFFDQSLEIISVI 239
Cdd:COG2186   98 LEARLALEPEAARLaAERATDED-----LARLEAALAEMEAAADDG-EAFAEADLAFHRAIAEASGNPLLALLLESLREL 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446013715 240 FHfHYQWDESDLKQRNIIAVDEHMTILSALICRSDLDATLALRNHLNSAKQSMIRSINENTR 301
Cdd:COG2186  172 LR-RSVRLTLRSPEARERSLAEHRAILDAIRAGDPEAARAAMRAHLEAVRERLREALAERAR 232
FCD smart00895
This entry represents the C-terminal ligand binding domain of many members of the GntR family; ...
 159-287 3.87e-10

This entry represents the C-terminal ligand binding domain of many members of the GntR family; This domain probably binds to a range of effector molecules that regulate the transcription of genes through the action of the N-terminal DNA-binding domain. This domain is found in and that are regulators of sugar biosynthesis operons. Many bacterial transcription regulation proteins bind DNA through a helix-turn-helix (HTH) motif, which can be classified into subfamilies on the basis of sequence similarities. The HTH GntR family has many members distributed among diverse bacterial groups that regulate various biological processes. It was named GntR after the Bacillus subtilis repressor of the gluconate operon. In general, these proteins contain a DNA-binding HTH domain at the N terminus, and an effector binding or oligomerisation domain at the C terminus. The winged-helix DNA-binding domain is well conserved in structure for the whole of the GntR family, and is similar in structure to other transcriptional regulator families. The C-terminal effector-binding and oligomerisation domains are more variable and are consequently used to define the subfamilies. Based on the sequence and structure of the C-terminal domains, the GtnR family can be divided into four major groups, as represented by FadR, HutC, MocR and YtrA, as well as some minor groups such as those represented by AraR and PlmA.


Pssm-ID: 214892 [Multi-domain]  Cd Length: 123  Bit Score: 56.60  E-value: 3.87e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715   159 QLFELREMLETHSLQHF-LNLPDHDPRWLQAktMLERHRLLRDNiGNSFRMFSQLDRDFHSLLLSAADNIFFDQSLEIIS 237
Cdd:smart00895   1 ELYEVRRALEPLAARLAaERATDEDLAALEA--LLDAMEAAAAA-GDDLEEFAELDREFHRALAEAAGNPVLLELLESLR 77

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 446013715   238 VIFHFHYQWDESDLKqrniIAVDEHMTILSALICRSDLDATLALRNHLNS 287
Cdd:smart00895  78 ARLRRLRRLSLEAAR----RALDEHRAILDAIRARDAEAARAAMREHLEA 123
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
 7-59 1.65e-07

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: 47.44  E-value: 1.65e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446013715   7 LRHNVINQVIDDMARGHIP--SPLPSQSALAEMYNISRTTVRHILSHLRECGVLT 59
Cdd:cd07377    2 LYEQIADQLREAILSGELKpgDRLPSERELAEELGVSRTTVREALRELEAEGLVE 56
FCD pfam07729
FCD domain; This domain is the C-terminal ligand binding domain of many members of the GntR ...
 159-283 8.10e-07

FCD domain; This domain is the C-terminal ligand binding domain of many members of the GntR family. This domain binds to a range of effector molecules, including Lactate, Zn(II), Ni(II), Ca(II), Mg(II), citrate, sugar acids, sialic acid and N-acetylglucosamine-6-P, that regulate the transcription of genes through the action of the N-terminal DNA-binding domain pfam00392 (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043). This domain is found in Swiss:P45427 and Swiss:P31460 that are regulators of sugar biosynthesis operons. It is also in the known structure of FadR where it binds to acyl-coA, the domain is alpha helical. This family has been named as FCD for (FadR C-terminal Domain).


Pssm-ID: 429623 [Multi-domain]  Cd Length: 121  Bit Score: 47.36  E-value: 8.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715  159 QLFELREMLETHSL-QHFLNLPDHDPRWLQAktMLERHRLLRDNigNSFRMFSQLDRDFHSLLLSAADNIFFDQSLEIIS 237
Cdd:pfam07729   1 ELYELRAALEPLAArLAAERATDEDLAELEA--LLEALEAAADA--GDLEAFAEADREFHLALAEAAGNPVLARMLESLW 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 446013715  238 VIFHfHYQWDESDLKQRNIIAVDEHMTILSALICRSDLDATLALRN 283
Cdd:pfam07729  77 DRLR-RLRRLLLSSPGRLRASLEEHRAILDAIRARDPEAARAAMRR 121
MngR COG2188
DNA-binding transcriptional regulator, GntR family [Transcription];
7-130 1.86e-06

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


Pssm-ID: 441791 [Multi-domain]  Cd Length: 238  Bit Score: 47.93  E-value: 1.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715   7 LRHNVINQVIDDMARGHIP--SPLPSQSALAEMYNISRTTVRHILSHLRECGVLTQ---VGNdYVIARKPDHD-DGFACT 80
Cdd:COG2188    6 LYLQIADALRERIESGELPpgDRLPSERELAEEFGVSRMTVRKALDELVEEGLLERrqgRGT-FVAEPKIEYPlSRLTSF 84

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446013715  81 TASMSEQNKVFEqafFTMINQRQLRPGETFSE-LQLARAAgvsPVVVREYL 130
Cdd:COG2188   85 TEELRARGREPS---TRVLSAERVPADEEVAEaLGLPPGA---PVLRIERL 129
GntR pfam00392
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ...
 10-59 5.32e-05

Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the N-terminal HTH region of GntR-like bacterial transcription factors. At the C-terminus there is usually an effector-binding/oligomerization domain. The GntR-like proteins include the following sub-families: MocR, YtrR, FadR, AraR, HutC and PlmA, DevA, DasR. Many of these proteins have been shown experimentally to be autoregulatory, enabling the prediction of operator sites and the discovery of cis/trans relationships. The DasR regulator has been shown to be a global regulator of primary metabolism and development in Streptomyces coelicolor.


Pssm-ID: 306822 [Multi-domain]  Cd Length: 64  Bit Score: 40.29  E-value: 5.32e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 446013715   10 NVINQVIDDMARGHIP--SPLPSQSALAEMYNISRTTVRHILSHLRECGVLT 59
Cdd:pfam00392   4 QVYARLREDILSGRLRpgDKLPSERELAAEFGVSRTTVREALRRLEAEGLVE 55
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
11-59 4.33e-04

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 37.94  E-value: 4.33e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 446013715    11 VINQVIDDMARGHIPS--PLPSQSALAEMYNISRTTVRHILSHLRECGVLT 59
Cdd:smart00345   1 VAERLREDIVSGELRPgdKLPSERELAAQLGVSRTTVREALSRLEAEGLVQ 51
PRK11402 PRK11402
transcriptional regulator PhoB;
4-58 7.66e-04

transcriptional regulator PhoB;


Pssm-ID: 183118 [Multi-domain]  Cd Length: 241  Bit Score: 40.20  E-value: 7.66e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 446013715   4 SQNLRHNVINQVIDDMARGhIPSP---LPSQSALAEMYNISRTTVRHILSHLRECGVL 58
Cdd:PRK11402   7 HQLLYATVRQRLLDDIAQG-VYQAgqqIPTENELCTQYNVSRITIRKAISDLVADGVL 63
Rrf2 pfam02082
Iron-dependent Transcriptional regulator; Several proteins in this family form iron-sulfur ...
 18-72 1.00e-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: 1.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 446013715   18 DMARGHIPSPLPSqSALAEMYNISRTTVRHILSHLRECGVLTQV---GNDYVIARKPD 72
Cdd:pfam02082  14 YLALHPGGEPVTS-EEIAERQNISPVYLEKILAKLRKAGLVESVrgaGGGYRLARPPE 70
PRK10225 PRK10225
Uxu operon transcriptional regulator;
98-297 1.69e-03

Uxu operon transcriptional regulator;


Pssm-ID: 182318 [Multi-domain]  Cd Length: 257  Bit Score: 39.23  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715  98 MINQRQLRPGETFS-ELQLARAAGVSPVVVREYLLKFGRYNLIHS---------EKRGQWSMKQFDQSYAE-----QLFE 162
Cdd:PRK10225  21 LIIKTPYNPGERLPpEREIAEMLDVTRTVVREALIMLEIKGLVEVrrgagiyvlDSSGSHNTDSPDANVCNdagpfELLQ 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715 163 LREMLEThSLQHF--LNLPDHDPRWLQAKTMLERHRLLRDNIGNSfrmfSQLDRDFHSLLLSAADNiffdqslEIISVIF 240
Cdd:PRK10225 101 ARQLLES-NIAEFaaLQATREDIVKMRQALQLEERELASSAPGSS----ESGDMQFHLAIAEATHN-------SMLVELF 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446013715 241 HFHYQWDES------------DLKQRNIIAVDeHMTILSALICRSDLDATLALRNHLNSAKQSMIRSIN 297
Cdd:PRK10225 169 RQSWQWRENnpmwiqlhshldDSLYRKEWLGD-HKQILAALIKKDARAAKLAMWQHLENVKQRLLEFSN 236
IscR COG1959
DNA-binding transcriptional regulator, IscR family [Transcription];
18-72 2.47e-03

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


Pssm-ID: 441562  Cd Length: 141  Bit Score: 37.51  E-value: 2.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715  18 DMARGHIPSPLPSqSALAEMYNISRTTVRHILSHLRECGVLTQV-----GndYVIARKPD 72
Cdd:COG1959   15 YLALHPGGEPVTS-KEIAERQGISPSYLEKILQKLRKAGLVESVrgpggG--YRLARPPE 71
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
 2-69 2.70e-03

DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440781 [Multi-domain]  Cd Length: 471  Bit Score: 39.04  E-value: 2.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715   2 SRSQNLRHNVINQVIDDMARGHIP--SPLPSQSALAEMYNISRTTVRHILSHLRECGvltqvgndYVIAR 69
Cdd:COG1167    8 DSSGPLYLQLADALREAILSGRLPpgDRLPSSRELAAQLGVSRSTVVRAYEELEAEG--------LIESR 69
PRK03837 PRK03837
transcriptional regulator NanR; Provisional
 98-288 7.18e-03

transcriptional regulator NanR; Provisional


Pssm-ID: 235166 [Multi-domain]  Cd Length: 241  Bit Score: 37.31  E-value: 7.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715  98 MINQRQLRPGETF-SELQLARAAGVSPVVVREYLLKFGRYNLI---HSEkRGQWSMKQFDQSYAEQLFELREMLETH--S 171
Cdd:PRK03837  25 MIRSGEFGPGDQLpSERELMAFFGVGRPAVREALQALKRKGLVqisHGE-RARVSRPSADTIIGQLSGMAKDFLSQSpdG 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446013715 172 LQHFLNL-----------------PDHDPRWLQAktmLERHrllRDNIGNSfRMFSQLDRDFHSLLLSAADN-IFFDQSL 233
Cdd:PRK03837 104 LAHLKQArlffesslaryaaehatDEQIALLRKA---LERN---SQSLGDN-AAFIRSDMEFHRVIAEIPGNpIFMAIHE 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446013715 234 EIISVIFHFHYQwdESDLKQRNIIAVDEHMTILSAlICRSDLD-ATLALRNHLNSA 288
Cdd:PRK03837 177 ALLDWLIEARPE--VVILHGHENVTLQEHIAIVDA-IRAHDPDeADRALQSHLNRV 229
 
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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