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MULTISPECIES: GntR family transcriptional regulator [Bacillus]

Protein Classification

GntR family transcriptional regulator( domain architecture ID 10164222)

GntR family transcriptional regulator similar to the arabinose metabolism transcriptional repressor AraR, which negatively controls the expression of arabinose utilization genes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
83-357 7.48e-111

ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of AraR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


:

Pssm-ID: 380483 [Multi-domain]  Cd Length: 274  Bit Score: 324.51  E-value: 7.48e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYNPNISYYLSFK 162
Cdd:cd01541    1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEPTKSALPNPNLDLYEELQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQGKYRMKGYIQALGEAKLNFLPEHVLF 242
Cdd:cd01541   81 KKGIPVVFINSYYPELDAPSVSLDDEKGGYLATKHLIDLGHRRIAGIFKSDDLQGVERYQGFIKALREAGLPIDDDRILW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 243 FDTESKQH--LGEQISTFLMAHRhELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQkNAHVKLTTLTHP 320
Cdd:cd01541  161 YSTEDLEDrfFAEELREFLRRLS-RCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLAS-LSEPPLTSVVHP 238
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 640667755 321 QEQMGRDAADWMIKKVQGkKNLPDQTFYEPELVPGET 357
Cdd:cd01541  239 KEELGRKAAELLLRMIEE-GRKPESVIFPPELIERES 274
MngR super family cl34419
DNA-binding transcriptional regulator, GntR family [Transcription];
17-70 2.45e-18

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


The actual alignment was detected with superfamily member COG2188:

Pssm-ID: 441791 [Multi-domain]  Cd Length: 238  Bit Score: 82.99  E-value: 2.45e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 640667755  17 LTGDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFVTNQ 70
Cdd:COG2188   19 ESGELPPGDRLPSERELAEEFGVSRMTVRKALDELVEEGLLERRQGRGTFVAEP 72
 
Name Accession Description Interval E-value
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
83-357 7.48e-111

ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of AraR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380483 [Multi-domain]  Cd Length: 274  Bit Score: 324.51  E-value: 7.48e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYNPNISYYLSFK 162
Cdd:cd01541    1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEPTKSALPNPNLDLYEELQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQGKYRMKGYIQALGEAKLNFLPEHVLF 242
Cdd:cd01541   81 KKGIPVVFINSYYPELDAPSVSLDDEKGGYLATKHLIDLGHRRIAGIFKSDDLQGVERYQGFIKALREAGLPIDDDRILW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 243 FDTESKQH--LGEQISTFLMAHRhELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQkNAHVKLTTLTHP 320
Cdd:cd01541  161 YSTEDLEDrfFAEELREFLRRLS-RCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLAS-LSEPPLTSVVHP 238
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 640667755 321 QEQMGRDAADWMIKKVQGkKNLPDQTFYEPELVPGET 357
Cdd:cd01541  239 KEELGRKAAELLLRMIEE-GRKPESVIFPPELIERES 274
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
82-362 1.33e-70

DNA-binding transcriptional regulator, LacI/PurR family [Transcription];


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 223.92  E-value: 1.33e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  82 KTIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTksnlyNPNISYYLSF 161
Cdd:COG1609   62 RTIGVVVPDLSNPFFAELLRGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGS-----RLDDARLERL 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 162 KEQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLIS-KTDDLQGKYRMKGYIQALGEAKLNFLPEHV 240
Cdd:COG1609  137 AEAGIPVVLIDRPLPDPGVPSVGVDNRAGARLATEHLIELGHRRIAFIGgPADSSSARERLAGYREALAEAGLPPDPELV 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 241 LF--FDTESkqhlGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQkNAHVKLTTLT 318
Cdd:COG1609  217 VEgdFSAES----GYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLAR-YLTPPLTTVR 291
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 640667755 319 HPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELVPGETIKRIK 362
Cdd:COG1609  292 QPIEEMGRRAAELLLDRIEGPDAPPERVLLPPELVVRESTAPAP 335
PRK11041 PRK11041
DNA-binding transcriptional regulator CytR; Provisional
82-353 2.58e-35

DNA-binding transcriptional regulator CytR; Provisional


Pssm-ID: 182923 [Multi-domain]  Cd Length: 309  Bit Score: 130.89  E-value: 2.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  82 KTIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIveptksnLYNPNISYYLSF 161
Cdd:PRK11041  36 RTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTFVNLIITKQIDGML-------LLGSRLPFDASK 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 162 KEQDV--PLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQ-GKYRMKGYIQALGEAKLNFLPE 238
Cdd:PRK11041 109 EEQRNlpPMVMANEFAPELELPTVHIDNLTAAFEAVNYLHELGHKRIACIAGPEEMPlCHYRLQGYVQALRRCGITVDPQ 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 239 HVLF--FDTESKQHLGEQistfLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQkNAHVKLTT 316
Cdd:PRK11041 189 YIARgdFTFEAGAKALKQ----LLDLPQPPTAVFCHSDVMALGALSQAKRMGLRVPQDLSIIGFDDIDLAQ-YCDPPLTT 263
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 640667755 317 LTHPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELV 353
Cdd:PRK11041 264 VAQPRYEIGREAMLLLLEQLQGHHVSSGSRLLDCELI 300
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
198-357 3.45e-25

Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional regulatory proteins. It is related to bacterial periplasmic binding proteins, although this domain is unlikely to be found in the periplasm. This domain acts as a sensor binding small molecule ligands that the DNA-binding domain responds to. This domain recognizes Sugars, sugar phosphates, sugar acids and purines (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433159 [Multi-domain]  Cd Length: 160  Bit Score: 99.72  E-value: 3.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  198 LITSGHQQIGLISKTDDLQGKY---RMKGYIQALGEAKLnfLPEHVLFFDTESKQHLGEQIStfLMAHRHELTALVCYND 274
Cdd:pfam13377   2 LAELGHRRIALIGPEGDRDDPYsdlRERGFREAARELGL--DVEPTLYAGDDEAEAAAARER--LRWLGALPTAVFVAND 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  275 EVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQKnAHVKLTTLTHPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELVP 354
Cdd:pfam13377  78 EVALGVLQALREAGLRVPEDLSVIGFDDSPLAAL-VSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVE 156

                  ...
gi 640667755  355 GET 357
Cdd:pfam13377 157 RES 159
MngR COG2188
DNA-binding transcriptional regulator, GntR family [Transcription];
17-70 2.45e-18

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


Pssm-ID: 441791 [Multi-domain]  Cd Length: 238  Bit Score: 82.99  E-value: 2.45e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 640667755  17 LTGDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFVTNQ 70
Cdd:COG2188   19 ESGELPPGDRLPSERELAEEFGVSRMTVRKALDELVEEGLLERRQGRGTFVAEP 72
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
17-68 1.60e-17

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: 75.95  E-value: 1.60e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 640667755  17 LTGDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFVT 68
Cdd:cd07377   15 LSGELKPGDRLPSERELAEELGVSRTTVREALRELEAEGLVERRPGRGTFVA 66
GntR pfam00392
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ...
17-67 1.48e-14

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: 67.64  E-value: 1.48e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 640667755   17 LTGDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFV 67
Cdd:pfam00392  14 LSGRLRPGDKLPSERELAAEFGVSRTTVREALRRLEAEGLVERRQGRGTFV 64
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
17-67 1.18e-13

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 64.90  E-value: 1.18e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 640667755    17 LTGDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFV 67
Cdd:smart00345  10 VSGELRPGDKLPSERELAAQLGVSRTTVREALSRLEAEGLVQRRPGSGTFV 60
C_P_lyase_phnF TIGR02325
phosphonates metabolism transcriptional regulator PhnF; All members of the seed alignment for ...
19-78 3.07e-12

phosphonates metabolism transcriptional regulator PhnF; All members of the seed alignment for this family are predicted helix-turn-helix transcriptional regulatory proteins of the broader gntR and are found associated with genes for the import and degradation of phosphonates and/or related compounds (e.g. phosphonites) with a direct C-P bond. [Transport and binding proteins, Anions, Regulatory functions, DNA interactions]


Pssm-ID: 131378 [Multi-domain]  Cd Length: 238  Bit Score: 65.58  E-value: 3.07e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755   19 GDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFVTNQYQTKPAGH 78
Cdd:TIGR02325  24 GHLRAGDYLPAEMQLAERFGVNRHTVRRAIAALVERGLLRAEQGRGTFVAARRIDYPLSA 83
his_ut_repres TIGR02018
histidine utilization repressor, proteobacterial; This model represents a proteobacterial ...
18-133 1.03e-11

histidine utilization repressor, proteobacterial; This model represents a proteobacterial histidine utilization repressor. It is usually found clustered with the enzymes HutUHIG so that it can regulate its own expression as well. A number of species have several paralogs and may fine-tune the regulation according to levels of degradation intermediates such as urocanate. This family belongs to the larger GntR family of transcriptional regulators. [Energy metabolism, Amino acids and amines, Regulatory functions, DNA interactions]


Pssm-ID: 188194 [Multi-domain]  Cd Length: 230  Bit Score: 63.88  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755   18 TGDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFVtnqyqTKPAGHAHMKTIgvittyisdyifP 97
Cdd:TIGR02018  16 SGEWPPGHRIPSEHELVAQYGCSRMTVNRALRELTDAGLLERRQGVGTFV-----AEPKAQSALLEI------------R 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 640667755   98 SIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMM 133
Cdd:TIGR02018  79 NIADEIVARGHRYRYELLELETRRATAEDAAALALP 114
PRK11402 PRK11402
transcriptional regulator PhoB;
19-70 1.36e-11

transcriptional regulator PhoB;


Pssm-ID: 183118 [Multi-domain]  Cd Length: 241  Bit Score: 63.70  E-value: 1.36e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 640667755  19 GDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFVTNQ 70
Cdd:PRK11402  25 GVYQAGQQIPTENELCTQYNVSRITIRKAISDLVADGVLIRWQGKGTFVQSQ 76
 
Name Accession Description Interval E-value
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
83-357 7.48e-111

ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of AraR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380483 [Multi-domain]  Cd Length: 274  Bit Score: 324.51  E-value: 7.48e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYNPNISYYLSFK 162
Cdd:cd01541    1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEPTKSALPNPNLDLYEELQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQGKYRMKGYIQALGEAKLNFLPEHVLF 242
Cdd:cd01541   81 KKGIPVVFINSYYPELDAPSVSLDDEKGGYLATKHLIDLGHRRIAGIFKSDDLQGVERYQGFIKALREAGLPIDDDRILW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 243 FDTESKQH--LGEQISTFLMAHRhELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQkNAHVKLTTLTHP 320
Cdd:cd01541  161 YSTEDLEDrfFAEELREFLRRLS-RCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLAS-LSEPPLTSVVHP 238
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 640667755 321 QEQMGRDAADWMIKKVQGkKNLPDQTFYEPELVPGET 357
Cdd:cd01541  239 KEELGRKAAELLLRMIEE-GRKPESVIFPPELIERES 274
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
83-353 1.17e-71

ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily; Ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily. In most cases, ligands are monosaccharide including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the domain sugar binding changes the DNA binding activity of the repressor domain.


Pssm-ID: 380491 [Multi-domain]  Cd Length: 264  Bit Score: 223.93  E-value: 1.17e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTksnlyNPNISYYLSFK 162
Cdd:cd06267    1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPS-----SLDDELLEELL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQ-GKYRMKGYIQALGEAKLNFLPEHVL 241
Cdd:cd06267   76 AAGIPVVLIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLStSRERLEGYRDALAEAGLPVDPELVV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 242 F--FDTESkqhlGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQkNAHVKLTTLTH 319
Cdd:cd06267  156 EgdFSEES----GYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAA-LLTPPLTTVRQ 230
                        250       260       270
                 ....*....|....*....|....*....|....
gi 640667755 320 PQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELV 353
Cdd:cd06267  231 PAYEMGRAAAELLLERIEGEEEPPRRIVLPTELV 264
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
82-362 1.33e-70

DNA-binding transcriptional regulator, LacI/PurR family [Transcription];


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 223.92  E-value: 1.33e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  82 KTIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTksnlyNPNISYYLSF 161
Cdd:COG1609   62 RTIGVVVPDLSNPFFAELLRGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGS-----RLDDARLERL 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 162 KEQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLIS-KTDDLQGKYRMKGYIQALGEAKLNFLPEHV 240
Cdd:COG1609  137 AEAGIPVVLIDRPLPDPGVPSVGVDNRAGARLATEHLIELGHRRIAFIGgPADSSSARERLAGYREALAEAGLPPDPELV 216
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 241 LF--FDTESkqhlGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQkNAHVKLTTLT 318
Cdd:COG1609  217 VEgdFSAES----GYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLAR-YLTPPLTTVR 291
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 640667755 319 HPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELVPGETIKRIK 362
Cdd:COG1609  292 QPIEEMGRRAAELLLDRIEGPDAPPERVLLPPELVVRESTAPAP 335
PBP1_DegA_Like cd19976
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
83-353 3.36e-62

ligand-binding domain of putative DNA transcription regulators highly similar to that of the transcription regulator DegA; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the transcription regulator DegA, which is involved in the control of degradation of Bacillus subtilis amidophosphoribosyltransferase (purF). This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380631 [Multi-domain]  Cd Length: 268  Bit Score: 199.78  E-value: 3.36e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNlynpNISYYLSFK 162
Cdd:cd19976    1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNIS----DEAIIKLLK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQG-KYRMKGYIQALGEAKLNFLPEhvL 241
Cdd:cd19976   77 EEKIPVVVLDRYIEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPSTYNeHERIEGYKNALQDHNLPIDES--W 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 242 FFDTESKQHLGEQISTFLMAhRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQKnAHVKLTTLTHPQ 321
Cdd:cd19976  155 IYSGESSLEGGYKAAEELLK-SKNPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEY-ITPALTTIAQPI 232
                        250       260       270
                 ....*....|....*....|....*....|..
gi 640667755 322 EQMGRDAADWMIKKVQGKKNLPDQTFYEPELV 353
Cdd:cd19976  233 FEMGQEAAKLLLKIIKNPAKKKEEIVLPPELI 264
PBP1_sucrose_transcription_regulator cd06288
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ...
83-360 9.06e-56

ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380511 [Multi-domain]  Cd Length: 268  Bit Score: 183.52  E-value: 9.06e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYI--SDYiFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYNPNIsyyls 160
Cdd:cd06288    1 TIGLITDDIatTPF-AGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYASMHHREVTLPP----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 161 fKEQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLIS-KTDDLQGKYRMKGYIQALGEAKLNFLPEH 239
Cdd:cd06288   75 -ELTDIPLVLLNCFDDDPSLPSVVPDDEQGGYLATRHLIEAGHRRIAFIGgPEDSLATRLRLAGYRAALAEAGIPYDPSL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 240 VLFFDTESKQhlGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQkNAHVKLTTLTH 319
Cdd:cd06288  154 VVHGDWGRES--GYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAA-YLRPPLTTVAL 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 640667755 320 PQEQMGRDAADWMIKKVQGKKNLPDQTfyepeLVPGETIKR 360
Cdd:cd06288  231 PYYEMGRRAAELLLDGIEGEPPEPGVI-----RVPCPLIER 266
PBP1_GalS-like cd06270
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ...
83-353 1.31e-55

ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalS is a dimeric protein like GalR,and its major role is in regulating expression of the high-affinity galactose transporter encoded by the mgl operon, whereas GalR is the exclusive regulator of galactose permease, the low-affinity galactose transporter. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are homologous to the periplasmic sugar binding of ABC-type transport systems.


Pssm-ID: 380494 [Multi-domain]  Cd Length: 266  Bit Score: 182.72  E-value: 1.31e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSnlynpNISYYLSFK 162
Cdd:cd06270    1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRAL-----SDEELILIA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLIS---KTDDlqGKYRMKGYIQALGEAKLNFLPEH 239
Cdd:cd06270   76 EKIPPLVVINRYIPGLADRCVWLDNEQGGRLAAEHLLDLGHRRIACITgplDIPD--ARERLAGYRDALAEAGIPLDPSL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 240 VLF--FDTESkqhlGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQkNAHVKLTTL 317
Cdd:cd06270  154 IIEgdFTIEG----GYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLAR-YLSPKLTTV 228
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 640667755 318 THPQEQMGRDAADWMIKKVQGKKNLPDQTFYePELV 353
Cdd:cd06270  229 HYPIEEMAQAAAELALNLAYGEPLPISHEFT-PTLI 263
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
83-353 1.54e-55

periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its close homologs; This group includes the ligand-binding domain of putative repressor of the endoglucanase operon from Paenibacillus polymyxa and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380632 [Multi-domain]  Cd Length: 264  Bit Score: 182.73  E-value: 1.54e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLynpniSYYLSFK 162
Cdd:cd19977    1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNE-----DLIEKLV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLIS-KTDDLQGKYRMKGYIQALGEAKLNFLPE--H 239
Cdd:cd19977   76 KSGIPVVFVDRYIPGLDVDTVVVDNFKGAYQATEHLIELGHKRIAFITyPLELSTRQERLEGYKAALADHGLPVDEEliK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 240 VLFFDTESKQHLGEQISTflmahRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAqKNAHVKLTTLTH 319
Cdd:cd19977  156 HVDRQDDVRKAISELLKL-----EKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWA-DLFNPPLTVIAQ 229
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 640667755 320 PQEQMGRDAADWMIKKVQGKKNLPDQTF-YEPELV 353
Cdd:cd19977  230 PTYEIGRKAAELLLDRIENKPKGPPRQIvLPTELI 264
PBP1_CcpA-like cd19975
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
83-357 4.02e-54

ligand-binding domain of putative DNA transcription regulators highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.


Pssm-ID: 380630 [Multi-domain]  Cd Length: 269  Bit Score: 179.29  E-value: 4.02e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVeptKSNLYNPNISYYLsfK 162
Cdd:cd19975    1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIF---ASGTLTEENKQLL--K 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLIS-KTDDLQ-GKYRMKGYIQALGEAKLNfLPEHV 240
Cdd:cd19975   76 NMNIPVVLVSTESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISgPLDDPNaGYPRYEGYKKALKDAGLP-IKENL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 241 LFFDTESKQHlGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQknaHV--KLTTLT 318
Cdd:cd19975  155 IVEGDFSFKS-GYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAE---MSipPLTTVS 230
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 640667755 319 HPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELVPGET 357
Cdd:cd19975  231 QPFYEMGKKAVELLLDLIKNEKKEEKSIVLPHQIIERES 269
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
83-354 5.34e-49

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380508 [Multi-domain]  Cd Length: 269  Bit Score: 165.86  E-value: 5.34e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSnlynpnISYYLSFK 162
Cdd:cd06285    1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARD------DAPDLQEL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQD-VPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLI---SKTDDLQGkyRMKGYIQALGEAKLNFLPE 238
Cdd:cd06285   75 AARgVPVVLVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVagpLNASTGRD--RLRGYRRALAEAGLPVPDE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 239 HVL--FFDTESkqhlGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQKnAHVKLTT 316
Cdd:cd06285  153 RIVpgGFTIEA----GREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAF-LPPPLTT 227
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 640667755 317 LTHPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELVP 354
Cdd:cd06285  228 VRQPKYEMGRRAAELLLQLIEGGGRPPRSITLPPELVV 265
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
83-357 4.68e-48

ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus Metalliredigens (strain Qymf) and its close homologs; This group includes the ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus metalliredigens (strain Qymf) and its close homologs. Qymf is a strict anaerobe that could be grown in the presence of borax and its cells are straight rods that produce endospores. This group is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380514 [Multi-domain]  Cd Length: 264  Bit Score: 163.07  E-value: 4.68e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPtksnlYNPNISYYlsfK 162
Cdd:cd06291    1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILGS-----HSLDIEEY---K 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYEQlEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQ-GKYRMKGYIQALGEAKLNFLPEHVL 241
Cdd:cd06291   73 KLNIPIVSIDRYLSE-GIPSVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSpANERYRGFEDALKEAGIEYEIIEID 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 242 F--FDTESKQHLGEQIstflMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAqKNAHVKLTTLTH 319
Cdd:cd06291  152 EndFSEEDAYELAKEL----LEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEIS-ELLYPELTTIRQ 226
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 640667755 320 PQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELVPGET 357
Cdd:cd06291  227 PIEEMAKEAVELLLKLIEGEEIEESRIVLPVELIERET 264
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
83-353 4.27e-47

ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380507 [Multi-domain]  Cd Length: 267  Bit Score: 160.78  E-value: 4.27e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIveptksnLYNPNISYYLSFK 162
Cdd:cd06284    1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVI-------LLSGRLDAELLSE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQD-VPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDD-LQGKYRMKGYIQALGEAKLNFLPEHV 240
Cdd:cd06284   74 LSKrYPIVQCCEYIPDSGVPSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDnVYARERLEGYRRALAEAGLPVDEDLI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 241 LFFDTESKqhLGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQKnAHVKLTTLTHP 320
Cdd:cd06284  154 IEGDFSFE--AGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEM-FSPSLTTIRQP 230
                        250       260       270
                 ....*....|....*....|....*....|...
gi 640667755 321 QEQMGRDAADWMIKKVQGKKNLPDQTFYEPELV 353
Cdd:cd06284  231 RYEIGETAAELLLEKIEGEGVPPEHIILPHELI 263
PBP1_RegR_EndR_KdgR-like cd06283
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ...
83-360 2.17e-45

ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR; Ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR, all of which are members of the LacI-GalR family of bacterial transcription regulators. RegR regulates bacterial competence and the expression of virulence factors, including hyaluronidase. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380506 [Multi-domain]  Cd Length: 266  Bit Score: 156.17  E-value: 2.17e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYnpnisYYLSFK 162
Cdd:cd06283    1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPTGNNND-----AYLELA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLIskTDDLQG----KYRMKGYIQALGEAKLNflpE 238
Cdd:cd06283   76 QKGLPVVLVDRQIEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFV--TEPIKGistrRERLQGFLDALARYNIE---G 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 239 HVLFFDTESKQHLGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAqKNAHVKLTTLT 318
Cdd:cd06283  151 DVYVIEIEDTEDLQQALAAFLSQHDGGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWA-DLIGPGITTIR 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 640667755 319 HPQEQMGRDAADWMIKKVQGKKNLPDQTfyepeLVPGETIKR 360
Cdd:cd06283  230 QPTYEIGKAAAEILLERIEGDSGEPKEI-----ELPSELIIR 266
PBP1_LacI-like cd06290
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
83-357 2.55e-45

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380513 [Multi-domain]  Cd Length: 267  Bit Score: 156.24  E-value: 2.55e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKsnlynpNISYYLSFK 162
Cdd:cd06290    1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGF------GDEELLKLL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDD-LQGKYRMKGYIQALGEAKLNFLPEHVL 241
Cdd:cd06290   75 AEGIPVVLVDRELEGLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDhPDAQERYAGYRRALEDAGLEVDPRLIV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 242 F--FDTESKQHLGEQistfLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAqKNAHVKLTTLTH 319
Cdd:cd06290  155 EgdFTEESGYEAMKK----LLKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFS-KYTTPPLTTVRQ 229
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 640667755 320 PQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELVPGET 357
Cdd:cd06290  230 PLYEMGKTAAEILLELIEGKGRPPRRIILPTELVIRES 267
PBP1_LacI-like cd06273
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
83-357 9.89e-43

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380497 [Multi-domain]  Cd Length: 268  Bit Score: 149.58  E-value: 9.89e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIV--EPTKSNLYNpnisyYLs 160
Cdd:cd06273    1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILvgSDHDPELFE-----LL- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 161 fKEQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLIS---KTDDLQgKYRMKGYIQALGEAKLNFLP 237
Cdd:cd06273   75 -EQRQVPYVLTWSYDEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISgptAGNDRA-RARLAGIRDALAERGLELPE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 238 EHVLF--FDTESkqhlGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAqknAHV--K 313
Cdd:cd06273  153 ERVVEapYSIEE----GREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELA---AHLspP 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 640667755 314 LTTLTHPQEQMGRDAADWMIKKVQGKKnLPDQTFYEPELVPGET 357
Cdd:cd06273  226 LTTVRVPAREIGELAARYLLALLEGGP-PPKSVELETELIVRES 268
PBP1_MalR-like cd06294
ligand-binding domain of maltose transcription regulator MalR which is a member of the ...
83-353 8.96e-41

ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors; This group includes the ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380517 [Multi-domain]  Cd Length: 269  Bit Score: 144.26  E-value: 8.96e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYI-----FPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNlyNPNISY 157
Cdd:cd06294    1 TIGLVLPSSAEELfqnpfFSEVLRGISQVANENGYSLLLATGNTEEELLEEVKRMVRGRRVDGFILLYSKED--DPLIEY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 158 ylsFKEQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQ-GKYRMKGYIQALGEAKLNFL 236
Cdd:cd06294   79 ---LKEEGFPFVVIGKPLDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVvSIDRLQGYKQALKEAGLPLD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 237 PEHVLFfdTESKQHLGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQkNAHVKLTT 316
Cdd:cd06294  156 DDYILL--LDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAE-LASPPLTS 232
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 640667755 317 LTHPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELV 353
Cdd:cd06294  233 VDINPYELGREAAKLLINLLEGPESLPKNVIVPHELI 269
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
83-354 1.00e-40

ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria; This group includes the ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria. They are members of the LacI-GalR family of repressor proteins which are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380512 [Multi-domain]  Cd Length: 268  Bit Score: 144.25  E-value: 1.00e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEP---TKSNLYNPnisyyl 159
Cdd:cd06289    1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPaagTTAELLRR------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 160 sFKEQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQ-GKYRMKGYIQALGEAKLnfLPE 238
Cdd:cd06289   75 -LKAWGIPVVLALRDVPGSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSStRRERLAGFRAALAEAGL--PLD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 239 HVLFFDTESKQHLGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNsyiAQKNAHV--KLTT 316
Cdd:cd06289  152 ESLIVPGPATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDD---VPEAALWtpPLTT 228
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 640667755 317 LTHPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELVP 354
Cdd:cd06289  229 VSVHPREIGRRAARLLLRRIEGPDTPPERIIIEPRLVV 266
PBP1_AglR_RafR-like cd06292
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ...
83-353 1.90e-40

Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the repressors specific raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins highly similar to DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR). Members of this group belong to the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380515 [Multi-domain]  Cd Length: 273  Bit Score: 143.56  E-value: 1.90e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITT----YISDYIFPSIIRGIESRLNEENYSLLLASTNNDvEQEKKALEMML-SFGVDGLIVepTKSNLYNPNISY 157
Cdd:cd06292    1 LIGYVVPelpgGFSDPFFDEFLAALGHAAAARGYDVLLFTASGD-EDEIDYYRDLVrSRRVDGFVL--ASTRHDDPRVRY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 158 ylsFKEQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQ-GKYRMKGYIQALGEAKLNFL 236
Cdd:cd06292   78 ---LHEAGVPFVAFGRANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPEGSVpSDDRLAGYRAALEEAGLPFD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 237 PEHVLffDTESKQHLGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQkNAHVKLTT 316
Cdd:cd06292  155 PGLVV--EGENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAA-FTHPPLTT 231
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 640667755 317 LTHPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELV 353
Cdd:cd06292  232 VRQPIDEIGRAVVDLLLAAIEGNPSEPREILLQPELV 268
PBP1_PurR cd06275
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ...
83-353 4.65e-40

ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli; Ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli. This dimeric PurR belongs to the LacI-GalR family of transcription regulators and is activated to bind to DNA operator sites by initially binding either of high affinity corepressors, hypoxanthine or guanine. PurR is composed of two functional domains: aan N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the purine transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380499 [Multi-domain]  Cd Length: 269  Bit Score: 142.40  E-value: 4.65e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYNPNIsyyLSFk 162
Cdd:cd06275    1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAEL---LAA- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLIS-KTDDLQGKYRMKGYIQALGEAKLNfLPEHVL 241
Cdd:cd06275   77 LRSIPVVVLDREIAGDNADAVLDDSFQGGYLATRHLIELGHRRIGCITgPLEHSVSRERLAGFRRALAEAGIE-VPPSWI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 242 F---FDTESkqhlGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQKnAHVKLTTLT 318
Cdd:cd06275  156 VegdFEPEG----GYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARY-FSPALTTIH 230
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 640667755 319 HPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELV 353
Cdd:cd06275  231 QPKDELGELAVELLLDRIENKREEPQSIVLEPELI 265
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
83-353 2.62e-39

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380516 [Multi-domain]  Cd Length: 270  Bit Score: 140.48  E-value: 2.62e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPtksnlYNPNISYYLSFK 162
Cdd:cd06293    1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTP-----SDDDLSHLARLR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDL-QGKYRMKGYIQALGEAKLNFLPE-HV 240
Cdd:cd06293   76 ARGTAVVLLDRPAPGPAGCSVSVDDVQGGALAVDHLLELGHRRIAFVSGPLRTrQVAERLAGARAAVAEAGLDPDEVvRE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 241 LFFDTESKQhLGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQKnAHVKLTTLTHP 320
Cdd:cd06293  156 LSAPDANAE-LGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAA-ANPPLTTVRQP 233
                        250       260       270
                 ....*....|....*....|....*....|...
gi 640667755 321 QEQMGRDAADWMIKKVQGKKNLPDQTFYEPELV 353
Cdd:cd06293  234 SYELGRAAADLLLDEIEGPGHPHEHVVFQPELV 266
PBP1_LacI-like cd06299
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ...
83-333 7.17e-38

ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum produces significant amounts of L-glutamate directly from cheap sugar and ammonia; This group includes the ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum which has a unique ability to produce significant amounts of L-glutamate directly from cheap sugar and ammonia. This regulatory protein is a member of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380522 [Multi-domain]  Cd Length: 268  Bit Score: 136.64  E-value: 7.17e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTksnlyNPNISYYLSFK 162
Cdd:cd06299    1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPT-----GENSEGLQALI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYEQL-EVPFLCLDDVKSSYLATKELITSGHQQIGLIS-KTDDLQGKYRMKGYIQALGEAKLNflPEHV 240
Cdd:cd06299   76 AQGLPVVFVDREVEGLgGVPVVTSDNRPGAREAVEYLVSLGHRRIGYISgPLSTSTGRERLAAFRAALTAAGIP--IDEE 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 241 LFFDTESKQHLGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQKNAHvKLTTLTHP 320
Cdd:cd06299  154 LVAFGDFRQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSP-PLTVIAQP 232
                        250
                 ....*....|...
gi 640667755 321 QEQMGRDAADWMI 333
Cdd:cd06299  233 VERIGRRAVELLL 245
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
83-353 8.09e-38

ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380503 [Multi-domain]  Cd Length: 266  Bit Score: 136.62  E-value: 8.09e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLynpniSYYLSFK 162
Cdd:cd06280    1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGPS-----RELKRLL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQGKY-RMKGYIQALGEAKLNFLPEHVL 241
Cdd:cd06280   76 KHGIPIVLIDREVEGLELDLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEISTTReRLAGYREALAEAGIPVDESLIF 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 242 FFDT--ESKQHLGEQistfLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQKnAHVKLTTLTH 319
Cdd:cd06280  156 EGDStiEGGYEAVKA----LLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEI-VDPPLTVVAQ 230
                        250       260       270
                 ....*....|....*....|....*....|....
gi 640667755 320 PQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELV 353
Cdd:cd06280  231 PAYEIGRIAAQLLLERIEGQGEEPRRIVLPTELI 264
PBP1_LacI-like cd19974
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
83-360 1.07e-37

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380629 [Multi-domain]  Cd Length: 270  Bit Score: 136.14  E-value: 1.07e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITT--YISDYIF-PSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNlynpniSYYL 159
Cdd:cd19974    1 NIAVLIPerFFGDNSFyGKIYQGIEKELSELGYNLVLEIISDEDEEELNLPSIISEEKVDGIIILGEISK------EYLE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 160 SFKEQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLI-------SKTDdlqgkyRMKGYIQALGEAK 232
Cdd:cd19974   75 KLKELGIPVVLVDHYDEELNADSVLSDNYYGAYKLTSYLIEKGHKKIGFVgdinytsSFMD------RYLGYRKALLEAG 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 233 LNFLPEHVLFFDTESKQHLGEQISTFLmaHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNsYIAQKNAHV 312
Cdd:cd19974  149 LPPEKEEWLLEDRDDGYGLTEEIELPL--KLMLPTAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDN-IELAELSTP 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 640667755 313 KLTTLTHPQEQMGRDAADWMIKKVQGKKnlpdqTFYEPELVPGETIKR 360
Cdd:cd19974  226 PLTTVEVDKEAMGRRAVEQLLWRIENPD-----RPFEKILVSGKLIER 268
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
83-357 1.95e-37

ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators; This group represents the ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of GntR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding, which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380489 [Multi-domain]  Cd Length: 269  Bit Score: 135.70  E-value: 1.95e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIV------EPTKSNLynpnis 156
Cdd:cd01575    1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILtgtehtPATRKLL------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 157 yylsfKEQDVPLIminayyEQLEVPFLCLDDV------KSSYLATKELITSGHQQIGLISKTDDLQGKY--RMKGYIQAL 228
Cdd:cd01575   75 -----RAAGIPVV------ETWDLPDDPIDMAvgfsnfAAGRAMARHLIERGYRRIAFVGARLDGDSRArqRLEGFRDAL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 229 GEAKLNflPEHVLFFDTESKQHLGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQk 308
Cdd:cd01575  144 AEAGLP--LPLVLLVELPSSFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAA- 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 640667755 309 NAHVKLTTLTHPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELVPGET 357
Cdd:cd01575  221 ALPPALTTVRVPRYEIGRKAAELLLARLEGEEPEPRVVDLGFELVRRES 269
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
83-341 2.16e-36

ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of TreR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380484 [Multi-domain]  Cd Length: 259  Bit Score: 132.62  E-value: 2.16e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTksnlynpNIS--YYLS 160
Cdd:cd01542    1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFAT-------EITdeHRKA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 161 FKEQDVPLIMINAYYEqlEVPFLCLDDVKSSYLATKELITSGHQQIGLI--SKTDDLQGKYRMKGYIQALGEAKLnflpE 238
Cdd:cd01542   74 LKKLKIPVVVLGQEHE--GFSCVYHDDYGAGKLLGEYLLKKGHKNIAYIgvDEEDIAVGVARKQGYLDALKEHGI----D 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 239 HVLFFDTESKQHLGEQISTFLMAHrHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQkNAHVKLTTLT 318
Cdd:cd01542  148 EVEIVETDFSMESGYEAAKELLKE-NKPDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSE-FVSPSLTTVK 225
                        250       260
                 ....*....|....*....|...
gi 640667755 319 HPQEQMGRDAADWMIKKVQGKKN 341
Cdd:cd01542  226 FDYEEAGEKAAELLLDMIEGEKV 248
PRK11041 PRK11041
DNA-binding transcriptional regulator CytR; Provisional
82-353 2.58e-35

DNA-binding transcriptional regulator CytR; Provisional


Pssm-ID: 182923 [Multi-domain]  Cd Length: 309  Bit Score: 130.89  E-value: 2.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  82 KTIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIveptksnLYNPNISYYLSF 161
Cdd:PRK11041  36 RTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTFVNLIITKQIDGML-------LLGSRLPFDASK 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 162 KEQDV--PLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQ-GKYRMKGYIQALGEAKLNFLPE 238
Cdd:PRK11041 109 EEQRNlpPMVMANEFAPELELPTVHIDNLTAAFEAVNYLHELGHKRIACIAGPEEMPlCHYRLQGYVQALRRCGITVDPQ 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 239 HVLF--FDTESKQHLGEQistfLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQkNAHVKLTT 316
Cdd:PRK11041 189 YIARgdFTFEAGAKALKQ----LLDLPQPPTAVFCHSDVMALGALSQAKRMGLRVPQDLSIIGFDDIDLAQ-YCDPPLTT 263
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 640667755 317 LTHPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELV 353
Cdd:PRK11041 264 VAQPRYEIGREAMLLLLEQLQGHHVSSGSRLLDCELI 300
PBP1_CcpB-like cd06286
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ...
83-353 3.28e-35

ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species; This group includes the ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species. Catabolite control protein B (CcpB) is 30% identical in sequence to CcpA which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. Like CcpA, the DNA-binding protein CcpB exerts its catabolite-repressing effect by a mechanism dependent on the presence of HPr(Ser-P), the small phosphocarrier proteins of the phosphoenolpyruvate-sugar phosphotransferase system, but with a less significant degree.


Pssm-ID: 380509 [Multi-domain]  Cd Length: 262  Bit Score: 129.59  E-value: 3.28e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYNpnISYYLSFK 162
Cdd:cd06286    1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLIITSRENDWEV--IEPYAKYG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 eqdvPLIMINaYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQ---GKYRMKGYIQALGEAKLNFLPEH 239
Cdd:cd06286   79 ----PIVLCE-ETDSPDIPSVYIDRYEAYLEALEYLKEKGHRKIGYCLGRPESSsasTQARLKAYQDVLGEHGLSLREEW 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 240 VlFFDTESKQHlGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQKnahVKLTTLTH 319
Cdd:cd06286  154 I-FTNCHTIED-GYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISEL---LNLTTIDQ 228
                        250       260       270
                 ....*....|....*....|....*....|....
gi 640667755 320 PQEQMGRDAADWMIKKVQGKKnlPDQTFYEPELV 353
Cdd:cd06286  229 PLEEMGKEAFELLLSQLESKE--PTKKELPSKLI 260
PBP1_LacI-like cd06282
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
83-330 2.22e-34

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380505 [Multi-domain]  Cd Length: 267  Bit Score: 127.40  E-value: 2.22e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVeptksNLYNPNISYYLS-F 161
Cdd:cd06282    1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLIL-----TVGDAQGSEALElL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 162 KEQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLIS---KTDDlQGKYRMKGYIQALGEAKLNFLP- 237
Cdd:cd06282   76 EEEGVPYVLLFNQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAgdfSASD-RARLRYQGYRDALKEAGLKPIPi 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 238 EHVLFFDTESKqhlgEQISTFLMAHRHeLTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQKnAHVKLTTL 317
Cdd:cd06282  155 VEVDFPTNGLE----EALTSLLSGPNP-PTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGEL-LTPTLATV 228
                        250
                 ....*....|...
gi 640667755 318 THPQEQMGRDAAD 330
Cdd:cd06282  229 VQPSRDMGRAAAD 241
PRK10703 PRK10703
HTH-type transcriptional repressor PurR;
80-353 5.86e-34

HTH-type transcriptional repressor PurR;


Pssm-ID: 236739 [Multi-domain]  Cd Length: 341  Bit Score: 128.30  E-value: 5.86e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  80 HMKTIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKsnlYNPNisyyl 159
Cdd:PRK10703  58 HTKSIGLLATSSEAPYFAEIIEAVEKNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSE---YPEP----- 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 160 sfkeqdvPLIMINAYYEqleVPFLCLD---------DV------KSSYLATKELITSGHQQIGLIS----KTddlQGKYR 220
Cdd:PRK10703 130 -------LLAMLEEYRH---IPMVVMDwgeakadftDAiidnafEGGYLAGRYLIERGHRDIGVIPgpleRN---TGAGR 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 221 MKGYIQALGEAKLNFLPEHVL--FFDTESkqhlGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSII 298
Cdd:PRK10703 197 LAGFMKAMEEANIKVPEEWIVqgDFEPES----GYEAMQQILSQKHRPTAVFCGGDIMAMGAICAADEMGLRVPQDISVI 272
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 640667755 299 GQDNSYIAQKNAHvKLTTLTHPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELV 353
Cdd:PRK10703 273 GYDNVRNARYFTP-ALTTIHQPKDRLGETAFNMLLDRIVNKREEPQTIEVHPRLV 326
PBP1_CcpA cd06298
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ...
83-325 7.75e-34

ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; Ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.


Pssm-ID: 380521 [Multi-domain]  Cd Length: 268  Bit Score: 125.87  E-value: 7.75e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIveptksnLYNPNIS--YYLS 160
Cdd:cd06298    1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGII-------FMGDELTeeIREE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 161 FKEQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLIS--KTDDLQGKYRMKGYIQALGEAKLNFLPE 238
Cdd:cd06298   74 FKRSPVPVVLAGTVDSDHEIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSgpLKEYINNDKKLQGYKRALEEAGLEFNEP 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 239 hvLFFDTESKQHLGEQISTFLMAhRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQKnAHVKLTTLT 318
Cdd:cd06298  154 --LIFEGDYDYDSGYELYEELLE-SGEPDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATM-SRPQLTSIN 229

                 ....*..
gi 640667755 319 HPQEQMG 325
Cdd:cd06298  230 QPLYDIG 236
PBP1_LacI cd01574
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ...
83-353 4.66e-33

ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of LacI is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380488 [Multi-domain]  Cd Length: 265  Bit Score: 123.85  E-value: 4.66e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLAST-NNDVEQEKKALEMMLSFGVDGLIVeptksNLYNPNISYYLSF 161
Cdd:cd01574    1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATVdEDDPASVREALDRLLSQRVDGIIV-----IAPDEAVLEALRR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 162 KEQDVPLIMINAYyEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDD-LQGKYRMKGYIQALGEAKLnfLPEHV 240
Cdd:cd01574   76 LPPGLPVVIVGSG-PSPGVPTVSIDQEEGARLATRHLLELGHRRIAHIAGPLDwVDARARLRGWREALEEAGL--PPPPV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 241 LF--FDTESkqhlGEQIsTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAqknAHV--KLTT 316
Cdd:cd01574  153 VEgdWSAAS----GYRA-GRRLLDDGPVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEA---AYFvpPLTT 224
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 640667755 317 LTHPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELV 353
Cdd:cd01574  225 VRQDFAELGRRAVELLLALIEGPAPPPESVLLPPELV 261
PBP1_LacI-like cd06281
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
83-356 1.22e-31

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380504 [Multi-domain]  Cd Length: 270  Bit Score: 120.04  E-value: 1.22e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVepTKSNLYNPNISYYLSfk 162
Cdd:cd06281    1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLIL--TPGDEDDPELAAALA-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYeQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQ-GKYRMKGYIQALGEAKLNFlPEHVL 241
Cdd:cd06281   77 RLDIPVVLIDRDL-PGDIDSVLVDHRSGVRQATEYLLSLGHRRIALLTGGPDIRpGRERIAGFKAAFAAAGLPP-DPDLV 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 242 FFDTESKQHlGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQknAHV-KLTTLTHP 320
Cdd:cd06281  155 RLGSFSADS-GFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAE--LHDpPITAIRWD 231
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 640667755 321 QEQMGRDAADWMIKKVQGKKNLPDQTFYEP-ELVPGE 356
Cdd:cd06281  232 LDAVGRAAAELLLDRIEGPPAGPPRRIVVPtELILRD 268
PBP1_SalR cd01545
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ...
92-357 8.46e-31

ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. The SalR binds to glucose based compound Salicin which is chemically related to aspirin. The ligand-binding of SalR is structurally homologous to the periplasmic sugar-binding domain of ABC-transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380487 [Multi-domain]  Cd Length: 270  Bit Score: 118.04  E-value: 8.46e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  92 SDYIFpSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLS-FGVDGLIVEPTKSNlyNPNISYYLsfKEQDVPLIM 170
Cdd:cd01545   11 ASYVS-ALQVGALRACREAGYHLVVEPCDSDDEDLADRLRRFLSrSRPDGVILTPPLSD--DPALLDAL--DELGIPYVR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 171 INAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDD-LQGKYRMKGYIQALGEAKLNFLPEHVL--FFDTES 247
Cdd:cd01545   86 IAPGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGPPDhGASAERLEGFRDALAEAGLPLDPDLVVqgDFTFES 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 248 kqhlGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQknaHV--KLTTLTHPQEQMG 325
Cdd:cd01545  166 ----GLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIAR---LVwpPLTTVRQPIAEMA 238
                        250       260       270
                 ....*....|....*....|....*....|..
gi 640667755 326 RDAADWMIKKVQGKKNLPDQTFYEPELVPGET 357
Cdd:cd01545  239 RRAVELLIAAIRGAPAGPERETLPHELVIRES 270
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
83-360 1.17e-29

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380501 [Multi-domain]  Cd Length: 266  Bit Score: 114.55  E-value: 1.17e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDvEQEKKALEMMLSFGVDGLIVepTKSNlynPNISYYLSFK 162
Cdd:cd06278    1 LVGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDE-DDVDDALRQLLQYRVDGVIV--TSAT---LSSELAEECA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQ-GKYRMKGYIQALGEAKLNFLPEHVL 241
Cdd:cd06278   75 RRGIPVVLFNRVVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPEGTStSRERERGFRAALAELGLPPPAVEAG 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 242 FFDTESkqhlGEQISTFLMAHRHELTALVCYNDEVGLEVANVC-SEIGLSIPDDLSIIGQDNSYIAQkNAHVKLTTLTHP 320
Cdd:cd06278  155 DYSYEG----GYEAARRLLAAPDRPDAIFCANDLMALGALDAArQEGGLVVPEDISVVGFDDIPMAA-WPSYDLTTVRQP 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 640667755 321 QEQMGRDAADwMIKKVQGKKNLPDQTfyepELVPGETIKR 360
Cdd:cd06278  230 IEEMAEAAVD-LLLERIENPETPPER----RVLPGELVER 264
PBP1_AglR-like cd20010
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ...
83-353 3.96e-29

Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and similar proteins; Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380665 [Multi-domain]  Cd Length: 269  Bit Score: 113.42  E-value: 3.96e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVI----TTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDvEQEKKALEMMLSFG-VDGLIVEPTKSNlyNPNISY 157
Cdd:cd20010    1 AIGLVlpldPGDLGDPFFLEFLAGLSEALAERGLDLLLAPAPSG-EDELATYRRLVERGrVDGFILARTRVN--DPRIAY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 158 ylsFKEQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQ-GKYRMKGYIQALGEAKLNFL 236
Cdd:cd20010   78 ---LLERGIPFVVHGRSESGAPYAWVDIDNEGAFRRATRRLLALGHRRIALLNGPEELNfAHQRRDGYRAALAEAGLPVD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 237 PEHVLF--FDTESkqhlGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQKNAHVKL 314
Cdd:cd20010  155 PALVREgpLTEEG----GYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLLPALEYFSPPL 230
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 640667755 315 TTLTHPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELV 353
Cdd:cd20010  231 TTTRSSLRDAGRRLAEMLLALIDGEPAAELQELWPPELI 269
PBP1_LacI-like cd06277
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
96-353 3.32e-27

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380500 [Multi-domain]  Cd Length: 275  Bit Score: 108.48  E-value: 3.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  96 FPSIIRGIESRLNEENYSLLLASTNNDVEQEKKaLEMMLSFGVDGLIVEPTksnlyNPNISYYLSFKEQDVPLIMINAYY 175
Cdd:cd06277   21 FSELIDGIEREARKYGYNLLISSVDIGDDFDEI-LKELTDDQSSGIILLGT-----ELEEKQIKLFQDVSIPVVVVDNYF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 176 EQLEVPFLCLDDVKSSYLATKELITSGHQQIGLI-SKTDDLQGKYRMKGYIQALGEAKLNFLPEHVLFFDTeSKQHLGEQ 254
Cdd:cd06277   95 EDLNFDCVVIDNEDGAYEAVKYLVELGHTRIGYLaSSYRIKNFEERRRGFRKAMRELGLSEDPEPEFVVSV-GPEGAYKD 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 255 ISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQKnAHVKLTTLTHPQEQMGRDAADWMIK 334
Cdd:cd06277  174 MKALLDTGPKLPTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAM-VDPPLTTIHVPKEQMGKLAVRRLIE 252
                        250
                 ....*....|....*....
gi 640667755 335 KVQGKKNLPDQTFYEPELV 353
Cdd:cd06277  253 KIKDPDGGTLKILVSTKLV 271
PBP1_CcpA_TTHA0807 cd06297
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ...
83-357 5.13e-27

ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its close homologs; Ligand-binding domain of the uncharacterized transcription regulator TTHA0807 from the extremely thermophilic organism Thermus thermophilus HB8 and close homologs from other bacteria. Although its exact biological function is not known, the TTHA0807 belongs to the catabolite control protein A (CcpA)family of regulatory proteins. The CcpA functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.


Pssm-ID: 380520 [Multi-domain]  Cd Length: 268  Bit Score: 107.55  E-value: 5.13e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEptksnLYNPNISYYLSFK 162
Cdd:cd06297    1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLLSEYRLEKYLRNSTLAYQCDGLVMA-----SLDLTELFEEVIV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYEQLEvpFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQG-----KYRMKGYIQALGEAKLNFLP 237
Cdd:cd06297   76 PTEKPVVLIDANSMGYD--CVYVDNVKGGFMATEYLAGLGEREYVFFGIEEDTVFtetvfREREQGFLEALNKAGRPISS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 238 EHVlfFDTESKQHLGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAqknAHVKLTTL 317
Cdd:cd06297  154 SRM--FRIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWA---ASPGLTTV 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 640667755 318 THPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELVPGET 357
Cdd:cd06297  229 RQPVEEMGEAAAKLLLKRLNEYGGPPRSLKFEPELIVRES 268
PRK10423 PRK10423
transcriptional repressor RbsR; Provisional
82-354 1.15e-25

transcriptional repressor RbsR; Provisional


Pssm-ID: 182448 [Multi-domain]  Cd Length: 327  Bit Score: 105.17  E-value: 1.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  82 KTIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYNPNI-SYYLS 160
Cdd:PRK10423  57 RTIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTETHQPSREImQRYPS 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 161 fkeqdVPLIMINAyyeqleVPFLCLDDV--KSSYL----ATKELITSGHQQIGLIS-KTDDLQGKYRMKGYIQALGEAKL 233
Cdd:PRK10423 137 -----VPTVMMDW------APFDGDSDLiqDNSLLggdlATQYLIDKGYTRIACITgPLDKTPARLRLEGYRAAMKRAGL 205
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 234 NFLPEHVLFFDTESKQhlGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQKNAHvK 313
Cdd:PRK10423 206 NIPDGYEVTGDFEFNG--GFDAMQQLLALPLRPQAVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTP-P 282
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 640667755 314 LTTLTHPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELVP 354
Cdd:PRK10423 283 LTTIHQPKDELGELAIDVLIHRMAQPTLQQQRLQLTPELME 323
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
198-357 3.45e-25

Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional regulatory proteins. It is related to bacterial periplasmic binding proteins, although this domain is unlikely to be found in the periplasm. This domain acts as a sensor binding small molecule ligands that the DNA-binding domain responds to. This domain recognizes Sugars, sugar phosphates, sugar acids and purines (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433159 [Multi-domain]  Cd Length: 160  Bit Score: 99.72  E-value: 3.45e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  198 LITSGHQQIGLISKTDDLQGKY---RMKGYIQALGEAKLnfLPEHVLFFDTESKQHLGEQIStfLMAHRHELTALVCYND 274
Cdd:pfam13377   2 LAELGHRRIALIGPEGDRDDPYsdlRERGFREAARELGL--DVEPTLYAGDDEAEAAAARER--LRWLGALPTAVFVAND 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  275 EVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQKnAHVKLTTLTHPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELVP 354
Cdd:pfam13377  78 EVALGVLQALREAGLRVPEDLSVIGFDDSPLAAL-VSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVE 156

                  ...
gi 640667755  355 GET 357
Cdd:pfam13377 157 RES 159
PBP1_CatR-like cd06296
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ...
83-330 6.61e-25

ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation; This group includes the ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation. This group belongs to the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380519 [Multi-domain]  Cd Length: 270  Bit Score: 101.97  E-value: 6.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKsnlynPNISYYLSFK 162
Cdd:cd06296    1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSD-----PTSRQLRLLR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYE-QLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDD-LQGKYRMKGYIQALGEAKLNFLPEHV 240
Cdd:cd06296   76 SAGIPFVLIDPVGEpDPDLPSVGATNWAGGRLATEHLLDLGHRRIAVITGPPRsVSGRARLAGYRAALAEAGIAVDPDLV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 241 LFFDTESkqHLGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQKnAHVKLTTLTHP 320
Cdd:cd06296  156 REGDFTY--EAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARW-TSPPLTTVHQP 232
                        250
                 ....*....|
gi 640667755 321 QEQMGRDAAD 330
Cdd:cd06296  233 LREMGAVAVR 242
PBP1_GalR cd01544
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ...
83-353 3.26e-24

ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalR is a dimeric protein like GalS and is exclusively involved in the regulation of galactose permease, the low-affinity galactose transporter. GalS is involved in regulating expression of the high-affinity galactose transporter encoded by the mgl operon. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are structurally homologous to the periplasmic sugar binding of ABC-type transport systems.


Pssm-ID: 380486 [Multi-domain]  Cd Length: 269  Bit Score: 99.90  E-value: 3.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTY-----ISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEkkalemmLSFGVDGLIV--EPTKSNLynpni 155
Cdd:cd01544    1 TIGIIQWYseeeeLEDPYYLSIRLGIEKEAKKLGYEIKTIFRDDEDLES-------LLEKVDGIIAigKFSKEEI----- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 156 syyLSFKEQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQGKY------RMKGYIQALG 229
Cdd:cd01544   69 ---EKLKKLNPNIVFVDSNPDPDGFDSVVPDFEQAVRQALDYLIELGHRRIGFIGGKEYTSDDGeeiedpRLRAFREYMK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 230 EAKLnFLPEHVLF--FDTESkqhlGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQ 307
Cdd:cd01544  146 EKGL-YNEEYIYIgeFSVES----GYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAK 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 640667755 308 kNAHVKLTTLTHPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELV 353
Cdd:cd01544  221 -YVTPPLTTVHIPTEEMGRTAVRLLLERINGGRTIPKKVLLPTKLI 265
PRK14987 PRK14987
HTH-type transcriptional regulator GntR;
78-358 3.73e-23

HTH-type transcriptional regulator GntR;


Pssm-ID: 184949 [Multi-domain]  Cd Length: 331  Bit Score: 98.56  E-value: 3.73e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  78 HAHMKTIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVepTKSNlYNPNISY 157
Cdd:PRK14987  60 NATSRAIGVLLPSLTNQVFAEVLRGIESVTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLIL--TERT-HTPRTLK 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 158 YLSFKeqDVPLI-MINAYYEQLEVPfLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQGKYRMKGYIQALGEAKLnfL 236
Cdd:PRK14987 137 MIEVA--GIPVVeLMDSQSPCLDIA-VGFDNFEAARQMTTAIIARGHRHIAYLGARLDERTIIKQKGYEQAMLDAGL--V 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 237 PEHVLffdTESKQHLGEQISTFLMAHRH--ELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQKnAHVKL 314
Cdd:PRK14987 212 PYSVM---VEQSSSYSSGIELIRQARREypQLDGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQV-MEPRL 287
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 640667755 315 TTLTHPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELVPGETI 358
Cdd:PRK14987 288 ASVLTPRERMGSIGAERLLARIRGESVTPKMLDLGFTLSPGGSI 331
PRK10727 PRK10727
HTH-type transcriptional regulator GalR;
82-353 1.45e-22

HTH-type transcriptional regulator GalR;


Pssm-ID: 182681 [Multi-domain]  Cd Length: 343  Bit Score: 96.75  E-value: 1.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  82 KTIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKsnLYNPNISyylSF 161
Cdd:PRK10727  60 ETVGLVVGDVSDPFFGAMVKAVEQVAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVVHAKM--IPDAELA---SL 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 162 KEQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGL------ISKTDDlqgkyRMKGYIQALGEAKLNF 235
Cdd:PRK10727 135 MKQIPGMVLINRILPGFENRCIALDDRYGAWLATRHLIQQGHTRIGYlcsnhsISDAED-----RLQGYYDALAESGIPA 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 236 LPEHVLFfdTESKQHLGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAqKNAHVKLT 315
Cdd:PRK10727 210 NDRLVTF--GEPDESGGEQAMTELLGRGRNFTAVACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVS-RYVRPRLT 286
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 640667755 316 TLTHPQEQMGRDAADWMIkKVQGKKNLPDQT-FYEPELV 353
Cdd:PRK10727 287 TVRYPIVTMATQAAELAL-ALADNRPLPEITnVFSPTLV 324
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
84-343 1.48e-22

Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems; Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems, all of which contain the type 1 periplasmic binding protein-like fold. Their specific ligands include lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor; in general the sugar binding domain in this family binds a sugar, which in turn changes the DNA binding activity of the repressor domain. The core structure of the periplasmic binding proteins is classified into two types and they differ in number and order of beta strands in each domain: type 1, which has six beta strands, and type 2, which has five beta strands. These two distinct structural arrangements may have originated from a common ancestor.


Pssm-ID: 380479 [Multi-domain]  Cd Length: 265  Bit Score: 95.39  E-value: 1.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  84 IGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVeptksNLYNPNISYYLSFKE 163
Cdd:cd01537    2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAI-----NLVDPAAAGVAEKAR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 164 -QDVPLIMINAYYEQLEVPFLCLDDVK-SSYLATKELITSGHQQIGLIS-KTDDLQGKYRMKGYIQALGEA--KLNFLPE 238
Cdd:cd01537   77 gQNVPVVFFDKEPSRYDKAYYVITDSKeGGIIQGDLLAKHGHIQIVLLKgPLGHPDAEARLAGVIKELNDKgiKTEQLQL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 239 HVLFFDTESKQHLGEQIstflMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQKNAHVkLTTLT 318
Cdd:cd01537  157 DTGDWDTASGKDKMDQW----LSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPL-LTTIL 231
                        250       260
                 ....*....|....*....|....*
gi 640667755 319 HPQEQMGRDAADWMIKKVQGKKNLP 343
Cdd:cd01537  232 QDANNLGKTTFDLLLNLADNWKIDN 256
PBP1_LacI-like cd06279
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ...
83-357 2.42e-22

ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380502 [Multi-domain]  Cd Length: 284  Bit Score: 95.35  E-value: 2.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIF--P---SIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMlsfgVDGLIVeptksNLYNPNISY 157
Cdd:cd06279    1 AIGVLLPDDLSYAFsdPvaaQFLRGVAEVCEEEGLGLLLLPATDEGSAAAAVRNAA----VDGFIV-----YGLSDDDPA 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 158 YLSFKEQDVPLIMInayyEQ---LEVPFLCLDDVKSSYLATKELITSGHQQIGLIS------------KTDDLQGKY--- 219
Cdd:cd06279   72 VAALRRRGLPLVVV----DGpapPGIPSVGIDDRAAARAAARHLLDLGHRRIAILSlrldrgrergpvSAERLAAATnsv 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 220 ---RMKGYIQALGEAKLNFLPEHVlfFD-TESKQHLGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDL 295
Cdd:cd06279  148 areRLAGYRDALEEAGLDLDDVPV--VEaPGNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRVPEDL 225
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 640667755 296 SIIGQDNSYIAQKnAHVKLTTLTHPQEQMGRDAADWMIKKVQGKKnlPDQTFYEPELVPGET 357
Cdd:cd06279  226 SVTGFDDIPEAAA-ADPGLTTVRQPAVEKGRAAARLLLGLLPGAP--PRPVILPTELVVRAS 284
PBP1_CelR cd06295
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ...
91-360 7.54e-21

ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators; This group includes the ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators. The binding of CelR to the celE promoter is inhibited specifically by cellobiose. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380518 [Multi-domain]  Cd Length: 273  Bit Score: 90.77  E-value: 7.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  91 ISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEmmlSFGVDGLIVEPTKSNlynpnISYYLSFKEQDVPLIM 170
Cdd:cd06295   20 ITDPFFLELLGGISEALTDRGYDMLLSTQDEDANQLARLLD---SGRADGLIVLGQGLD-----HDALRELAQQGLPMVV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 171 INAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQGKYRMKGYIQALGEAKLNFLPEHVLFFDTESKQh 250
Cdd:cd06295   92 WGAPEDGQSYCSVGSDNVKGGALATEHLIEIGRRRIAFLGDPPHPEVADRLQGYRDALAEAGLEADPSLLLSCDFTEES- 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 251 lGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQkNAHVKLTTLTHPQEQMGRDAAD 330
Cdd:cd06295  171 -GYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAA-YFRPPLTTVRQDLALAGRLLVE 248
                        250       260       270
                 ....*....|....*....|....*....|
gi 640667755 331 WMIKKVQGKKnlpdqtfYEPELVPGETIKR 360
Cdd:cd06295  249 KLLALIAGEP-------VTSSMLPVELVVR 271
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
83-346 1.03e-20

Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the periplasmic binding proteins, and the LacI family transcriptional regulators. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The LacI family of proteins consist of transcriptional regulators related to the lac repressor. In this case, generally the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain (pfam00356).


Pssm-ID: 395423 [Multi-domain]  Cd Length: 281  Bit Score: 90.65  E-value: 1.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755   83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVepTKSNLYNPNISYYLsfK 162
Cdd:pfam00532   3 KLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIII--TTPAPSGDDITAKA--E 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  163 EQDVPLIMI-NAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQ-IGLISKTDD-LQGKYRMKGYIQALGEAKLNFLPEH 239
Cdd:pfam00532  79 GYGIPVIAAdDAFDNPDGVPCVMPDDTQAGYESTQYLIAEGHKRpIAVMAGPASaLTARERVQGFMAALAAAGREVKIYH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  240 VLFFDTESKQhlGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIG-LSIPDD-----LSIIGQDNSYIAQkNAHVK 313
Cdd:pfam00532 159 VATGDNDIPD--AALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGrVKIPDIvgigiNSVVGFDGLSKAQ-DTGLY 235
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 640667755  314 LTTLTHPQ---EQMGRDAADWMIKKVQGKKNLPDQT 346
Cdd:pfam00532 236 LSPLTVIQlprQLLGIKASDMVYQWIPKFREHPRVL 271
lacI PRK09526
lac repressor; Reviewed
41-360 4.04e-20

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 90.05  E-value: 4.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  41 RHTVRKAILELSsegflrsekgsgtFVTNQYQTKPAGhAHMKTIGVITTYISDYIfPS-IIRGIESRLNEENYSLLLAST 119
Cdd:PRK09526  37 REKVEAAMAELN-------------YVPNRVAQQLAG-KQSLTIGLATTSLALHA-PSqIAAAIKSRADQLGYSVVISMV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 120 N-NDVEQEKKALEMMLSFGVDGLIVeptksnlynpnisyylsfkeqDVPL-----IMINAYYEqlEVPFLCLD-----DV 188
Cdd:PRK09526 102 ErSGVEACQAAVNELLAQRVSGVII---------------------NVPLedadaEKIVADCA--DVPCLFLDvspqsPV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 189 KS--------SYLATKELITSGHQQIGLISKTDD-LQGKYRMKGYIQALGEAKLNflPEHVLFFDTESKQhlGEQISTFL 259
Cdd:PRK09526 159 NSvsfdpedgTRLGVEHLVELGHQRIALLAGPESsVSARLRLAGWLEYLTDYQLQ--PIAVREGDWSAMS--GYQQTLQM 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 260 MAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIG----QDNSYIaqknaHVKLTTLTHPQEQMGRDAADWMIKK 335
Cdd:PRK09526 235 LREGPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGyddtEDSSYF-----IPPLTTIKQDFRLLGKEAVDRLLAL 309
                        330       340
                 ....*....|....*....|....*
gi 640667755 336 VQGKKNLPdqtfyePELVPGETIKR 360
Cdd:PRK09526 310 SQGQAVKG------SQLLPTSLVVR 328
PRK10014 PRK10014
DNA-binding transcriptional repressor MalI; Provisional
84-353 4.49e-20

DNA-binding transcriptional repressor MalI; Provisional


Pssm-ID: 182193 [Multi-domain]  Cd Length: 342  Bit Score: 89.77  E-value: 4.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  84 IGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNlYNPNISyylSFKE 163
Cdd:PRK10014  67 IGLIVRDLSAPFYAELTAGLTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAGS-SDDLRE---MAEE 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 164 QDVPLIMIN-AYYEQlEVPFLCLDDVKSSYLATKELITSGHQQIG-LISKTDDLQGKYRMKGYIQALGEAKLNFLPEHVL 241
Cdd:PRK10014 143 KGIPVVFASrASYLD-DVDTVRPDNMQAAQLLTEHLIRNGHQRIAwLGGQSSSLTRAERVGGYCATLLKFGLPFHSEWVL 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 242 ffDTESKQHLGEQISTFLMAHRHELTALVCYNDEV------GLEVANvcSEIGLSIPDdlSIIGQDNSYIAQKNA----- 310
Cdd:PRK10014 222 --ECTSSQKQAAEAITALLRHNPTISAVVCYNETIamgawfGLLRAG--RQSGESGVD--RYFEQQVALAAFTDVpeael 295
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 640667755 311 -HVKLTTLTHPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELV 353
Cdd:PRK10014 296 dDPPLTWASTPAREIGRTLADRMMQRITHEETHSRNLIIPPRLI 339
PRK10401 PRK10401
HTH-type transcriptional regulator GalS;
83-354 5.57e-19

HTH-type transcriptional regulator GalS;


Pssm-ID: 236681 [Multi-domain]  Cd Length: 346  Bit Score: 86.75  E-value: 5.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEpTKSnLYNPNISyylSFK 162
Cdd:PRK10401  61 TIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVH-SKA-LSDDELA---QFM 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQGKY-RMKGYIQALGEAKLnfLPEHVL 241
Cdd:PRK10401 136 DQIPGMVLINRVVPGYAHRCVCLDNVSGARMATRMLLNNGHQRIGYLSSSHGIEDDAmRRAGWMSALKEQGI--IPPESW 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 242 FFDTESKQHLGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAqKNAHVKLTTLTHPQ 321
Cdd:PRK10401 214 IGTGTPDMQGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIA-RYTDPQLTTVRYPI 292
                        250       260       270
                 ....*....|....*....|....*....|...
gi 640667755 322 EQMGRDAADWMIKKVQGKKNLPDQTFYEPELVP 354
Cdd:PRK10401 293 ASMAKLATELALQGAAGNLDPRASHCFMPTLVR 325
MngR COG2188
DNA-binding transcriptional regulator, GntR family [Transcription];
17-70 2.45e-18

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


Pssm-ID: 441791 [Multi-domain]  Cd Length: 238  Bit Score: 82.99  E-value: 2.45e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 640667755  17 LTGDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFVTNQ 70
Cdd:COG2188   19 ESGELPPGDRLPSERELAEEFGVSRMTVRKALDELVEEGLLERRQGRGTFVAEP 72
WHTH_GntR cd07377
Winged helix-turn-helix (WHTH) DNA-binding domain of the GntR family of transcriptional ...
17-68 1.60e-17

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: 75.95  E-value: 1.60e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 640667755  17 LTGDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFVT 68
Cdd:cd07377   15 LSGELKPGDRLPSERELAEELGVSRTTVREALRELEAEGLVERRPGRGTFVA 66
PBP1_XylR cd01543
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ...
130-351 1.17e-16

ligand-binding domain of DNA transcription repressor specific for xylose (XylR); Ligand-binding domain of DNA transcription repressor specific for xylose (XylR), a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of XylR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380485 [Multi-domain]  Cd Length: 265  Bit Score: 78.78  E-value: 1.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 130 LEMMLSFGVDGLIVeptksNLYNPNIsyYLSFKEQDVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLI 209
Cdd:cd01543   43 LDLLKGWKGDGIIA-----RLDDPEL--AEALRRLGIPVVNVSGSRPEPGFPRVTTDNEAIGRMAAEHLLERGFRHFAFC 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 210 SKTDDLQGKYRMKGYIQALGEAKLnflPEHVLFFDTESKQHLGEQISTFLMAHRHEL---TALVCYNDEVGLEVANVCSE 286
Cdd:cd01543  116 GFRNAAWSRERGEGFREALREAGY---ECHVYESPPSGSSRSWEEEREELADWLKSLpkpVGIFACNDDRARQVLEACRE 192
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 640667755 287 IGLSIPDDLSIIGQDNSYIAQKNAHVKLTTLTHPQEQMGRDAA---DWMIKkvqGKKNLPDQTFYEPE 351
Cdd:cd01543  193 AGIRVPEEVAVLGVDNDELICELSSPPLSSIALDAEQIGYEAAellDRLMR---GERVPPEPILIPPL 257
PBP1_hexuronate_repressor-like cd06272
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ...
83-353 2.03e-16

ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and close homologs, all members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and its close homologs from other bacteria, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380496 [Multi-domain]  Cd Length: 266  Bit Score: 78.18  E-value: 2.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVI--TTYISDYIfPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTksnlyNPNISYYLS 160
Cdd:cd06272    1 TIGLYwpSVGERVAL-TRLLSGINEAISKQGYNINLSICPYKVGHLCTAKGLFSENRFDGVIVFGI-----SDSDIEYLN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 161 FKEQDVPLIMINAYYEQLevPFLCLDDVKSSYLATKELITSGHQQIGLI--SKTDDLQgKYRMKGYIQALGEAKLNFLPE 238
Cdd:cd06272   75 KNKPKIPIVLYNRESPKY--STVNVDNEKAGRLAVLLLIQKGHKSIAYIgnPNSNRNQ-TLRGKGFIETCEKHGIHLSDS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 239 HVlfFDTESKQHLGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNsyIAQKN-AHVKLTTL 317
Cdd:cd06272  152 II--DSRGLSIEGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISIPEDISIVSYDN--IPQEArSDPPLTVV 227
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 640667755 318 THPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELV 353
Cdd:cd06272  228 GVPIEKIAEESLRLILKLIEGRENEIQQLILYPELI 263
PBP1_AglR_RafR-like cd06271
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ...
95-353 3.19e-16

ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380495 [Multi-domain]  Cd Length: 264  Bit Score: 77.47  E-value: 3.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  95 IFPSIIRGIESRLNEENYSLLLASTNNDvEQEKKALEMMLSFGVDGLIVepTKSNLYNPNISYylsFKEQDVPLIMINAY 174
Cdd:cd06271   16 TVSE*VSGITEEAGTTGYHLLVWPFEEA-ES*VPIRDLVETGSADGVIL--SEIEPNDPRVQF---LTKQNFPFVAHGRS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 175 YEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQ-GKYRMKGYIQALGEAKLNFLPehvlfFDTESKQHLGE 253
Cdd:cd06271   90 D*PIGHAWVDIDNEAGAYEAVERLAGLGHRRIAFIVPPARYSpHDRRLQGYVRA*RDAGLTGYP-----LDADTTLEAGR 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 254 QISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNSYIAQKNAHVKLTTLTHPQEQMGRDAADWMI 333
Cdd:cd06271  165 AAAQRLLALSPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSAPFLGAMITPPLTTVHAPIAEAGRELAKALL 244
                        250       260
                 ....*....|....*....|
gi 640667755 334 KKVQGKKNLPDQTFYEPELV 353
Cdd:cd06271  245 ARIDGEDPETLQVLVQPSLS 264
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
83-352 8.98e-16

periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.


Pssm-ID: 380478 [Multi-domain]  Cd Length: 268  Bit Score: 76.45  E-value: 8.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYNPNIsyyLSFK 162
Cdd:cd01536    1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAV---KKAN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYEQLE--VPFLCLDDVKSSYLATKELIT--SGHQQIGLIS-KTDDLQGKYRMKGYIQALGEAKlnflP 237
Cdd:cd01536   78 AAGIPVVAVDTDIDGGGdvVAFVGTDNYEAGKLAGEYLAEalGGKGKVAILEgPPGSSTAIDRTKGFKEALKKYP----D 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 238 EHVLF-----FDTESKQhlgEQISTFLMAHRhELTALVCYNDEVGLEVANVCSEIGLSipDDLSIIGQDNS---YIAQKN 309
Cdd:cd01536  154 IEIVAeqpanWDRAKAL---TVTENLLQANP-DIDAVFAANDDMALGAAEALKAAGRT--GDIKIVGVDGTpeaLKAIKD 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 640667755 310 AHVKLTTLTHPqEQMGRDAADWMIKKVQGKKnLPDQTFYEPEL 352
Cdd:cd01536  228 GELDATVAQDP-YLQGYLAVEAAVKLLNGEK-VPKEILTPVTL 268
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
82-358 2.17e-15

ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH domain [Carbohydrate transport and metabolism];


Pssm-ID: 441483 [Multi-domain]  Cd Length: 307  Bit Score: 75.73  E-value: 2.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  82 KTIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYNPNISyylSF 161
Cdd:COG1879   34 KTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDALAPALK---KA 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 162 KEQDVPLIMINAYYEQLE-VPFLCLDDVKSSYLATKELI--TSGHQQIGLISKTDDLQG-KYRMKGYIQALGEA-KLNFL 236
Cdd:COG1879  111 KAAGIPVVTVDSDVDGSDrVAYVGSDNYAAGRLAAEYLAkaLGGKGKVAILTGSPGAPAaNERTDGFKEALKEYpGIKVV 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 237 PEHVLFFDTESKQhlgEQISTFLMAHrHELTALVCYNDEVGLEVANVCSEIGLsiPDDLSIIGQDNS-----YIAQKNAH 311
Cdd:COG1879  191 AEQYADWDREKAL---EVMEDLLQAH-PDIDGIFAANDGMALGAAQALKAAGR--KGDVKVVGFDGSpealqAIKDGTID 264
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 640667755 312 VkltTLTHPQEQMGRDAADWMIKKVQGKKnLPDQTFYEPELVPGETI 358
Cdd:COG1879  265 A---TVAQDPYLQGYLAVDAALKLLKGKE-VPKEILTPPVLVTKENV 307
GntR pfam00392
Bacterial regulatory proteins, gntR family; This family of regulatory proteins consists of the ...
17-67 1.48e-14

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: 67.64  E-value: 1.48e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 640667755   17 LTGDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFV 67
Cdd:pfam00392  14 LSGRLRPGDKLPSERELAAEFGVSRTTVREALRRLEAEGLVERRQGRGTFV 64
FadR COG2186
DNA-binding transcriptional regulator, FadR family [Transcription];
17-69 7.38e-14

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


Pssm-ID: 441789 [Multi-domain]  Cd Length: 232  Bit Score: 70.35  E-value: 7.38e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 640667755  17 LTGDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFVTN 69
Cdd:COG2186   21 LSGELKPGDRLPSERELAEQLGVSRTTVREALRALEALGLVEVRQGGGTFVRE 73
HTH_GNTR smart00345
helix_turn_helix gluconate operon transcriptional repressor;
17-67 1.18e-13

helix_turn_helix gluconate operon transcriptional repressor;


Pssm-ID: 197669 [Multi-domain]  Cd Length: 60  Bit Score: 64.90  E-value: 1.18e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 640667755    17 LTGDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFV 67
Cdd:smart00345  10 VSGELRPGDKLPSERELAAQLGVSRTTVREALSRLEAEGLVQRRPGSGTFV 60
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
84-340 2.68e-13

Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins. This domain recognizes fructose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433182 [Multi-domain]  Cd Length: 259  Bit Score: 68.88  E-value: 2.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755   84 IGVITTYISDYIFPSIIRGIESRLNEENYSLLL-ASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYNPNISYYlsfK 162
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVvGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKA---K 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  163 EQDVPLIMINAYYEQ-LEVPFLCLDDVKSSYLATKELITS--GHQQIGLISKT-DDLQGKYRMKGYIQALGE--AKLNFL 236
Cdd:pfam13407  78 DAGIPVVTFDSDAPSsPRLAYVGFDNEAAGEAAGELLAEAlgGKGKVAILSGSpGDPNANERIDGFKKVLKEkyPGIKVV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  237 PEHVLFFDTESKQhlGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSipDDLSIIGQDNS-----YIaqKNAH 311
Cdd:pfam13407 158 AEVEGTNWDPEKA--QQQMEALLTAYPNPLDGIISPNDGMAGGAAQALEAAGLA--GKVVVTGFDATpealeAI--KDGT 231
                         250       260
                  ....*....|....*....|....*....
gi 640667755  312 VKLTTLTHPQEQmGRDAADWMIKKVQGKK 340
Cdd:pfam13407 232 IDATVLQDPYGQ-GYAAVELAAALLKGKK 259
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
83-359 8.48e-13

periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group includes periplasmic D-threitol-binding protein ThpA and xylitol/L-sorbitol-binding protein XypA, which are part of sugar ABC-type transport systems. Both ThpA and XypA share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.


Pssm-ID: 380536 [Multi-domain]  Cd Length: 277  Bit Score: 67.68  E-value: 8.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYNPNISyylSFK 162
Cdd:cd06313    1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVE---KAK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYE-QLEVPFLCLDDVKSSYLATKELItsghQQIGLISKTDDLQGKY-------RMKGYIQALGEA-KL 233
Cdd:cd06313   78 EAGIPLVGVNALIEnEDLTAYVGSDDVVAGELEGQAVA----DRLGGKGNVVILEGPIgqsaqidRGKGIENVLKKYpDI 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 234 NFLPEHVLFFDTESKQHLGEqisTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLsipDDLSIIGQD---NSYIAQKNA 310
Cdd:cd06313  154 KVLAEQTANWSRDEAMSLME---NWLQAYGDEIDGIIAQNDDMALGALQAVKAAGR---DDIPVVGIDgieDALQAVKSG 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 640667755 311 HVKLTTLTHPQEQmGRDAADWMIKKVQGKKnLPDQTFYEPELVPGETIK 359
Cdd:cd06313  228 ELIATVLQDAEAQ-GKGAVEVAVDAVKGEG-VEKKYYIPFVLVTKDNVD 274
C_P_lyase_phnF TIGR02325
phosphonates metabolism transcriptional regulator PhnF; All members of the seed alignment for ...
19-78 3.07e-12

phosphonates metabolism transcriptional regulator PhnF; All members of the seed alignment for this family are predicted helix-turn-helix transcriptional regulatory proteins of the broader gntR and are found associated with genes for the import and degradation of phosphonates and/or related compounds (e.g. phosphonites) with a direct C-P bond. [Transport and binding proteins, Anions, Regulatory functions, DNA interactions]


Pssm-ID: 131378 [Multi-domain]  Cd Length: 238  Bit Score: 65.58  E-value: 3.07e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755   19 GDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFVTNQYQTKPAGH 78
Cdd:TIGR02325  24 GHLRAGDYLPAEMQLAERFGVNRHTVRRAIAALVERGLLRAEQGRGTFVAARRIDYPLSA 83
PBP1_FruR cd06274
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ...
83-297 3.97e-12

ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs; Ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to members of the type 1 periplasmic binding protein superfamily. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor


Pssm-ID: 380498 [Multi-domain]  Cd Length: 264  Bit Score: 65.69  E-value: 3.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTksnlYNPNISYYLSFK 162
Cdd:cd06274    1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAPS----TPPDDIYYLCQA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQdVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLI------SKTDDlqgkyRMKGYIQALGEAKLNFL 236
Cdd:cd06274   77 AG-LPVVFLDRPFSGSDAPSVVSDNRAGARALTEKLLAAGPGEIYFLggrpelPSTAE-----RIRGFRAALAEAGITEG 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 640667755 237 PEHVLFFDTESKQhlGEQ-ISTFLMAHRHELTALVCyNDEVGLE-VANVCSEIGLSIPDDLSI 297
Cdd:cd06274  151 DDWILAEGYDRES--GYQlMAELLARLGGLPQALFT-SSLTLLEgVLRFLRERLGAIPSDLVL 210
his_ut_repres TIGR02018
histidine utilization repressor, proteobacterial; This model represents a proteobacterial ...
18-133 1.03e-11

histidine utilization repressor, proteobacterial; This model represents a proteobacterial histidine utilization repressor. It is usually found clustered with the enzymes HutUHIG so that it can regulate its own expression as well. A number of species have several paralogs and may fine-tune the regulation according to levels of degradation intermediates such as urocanate. This family belongs to the larger GntR family of transcriptional regulators. [Energy metabolism, Amino acids and amines, Regulatory functions, DNA interactions]


Pssm-ID: 188194 [Multi-domain]  Cd Length: 230  Bit Score: 63.88  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755   18 TGDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFVtnqyqTKPAGHAHMKTIgvittyisdyifP 97
Cdd:TIGR02018  16 SGEWPPGHRIPSEHELVAQYGCSRMTVNRALRELTDAGLLERRQGVGTFV-----AEPKAQSALLEI------------R 78
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 640667755   98 SIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMM 133
Cdd:TIGR02018  79 NIADEIVARGHRYRYELLELETRRATAEDAAALALP 114
PRK11402 PRK11402
transcriptional regulator PhoB;
19-70 1.36e-11

transcriptional regulator PhoB;


Pssm-ID: 183118 [Multi-domain]  Cd Length: 241  Bit Score: 63.70  E-value: 1.36e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 640667755  19 GDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFVTNQ 70
Cdd:PRK11402  25 GVYQAGQQIPTENELCTQYNVSRITIRKAISDLVADGVLIRWQGKGTFVQSQ 76
YhcF COG1725
DNA-binding transcriptional regulator YhcF, GntR family [Transcription];
17-70 1.71e-10

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


Pssm-ID: 441331 [Multi-domain]  Cd Length: 114  Bit Score: 57.88  E-value: 1.71e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 640667755  17 LTGDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFVTNQ 70
Cdd:COG1725   24 ASGELKPGDRLPSVRELAAELGVNPNTVAKAYRELEDEGLIETRRGKGTFVAED 77
PBP1_RafR-like cd20009
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ...
98-353 2.47e-10

Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar proteins; Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380664 [Multi-domain]  Cd Length: 266  Bit Score: 60.24  E-value: 2.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  98 SIIRGIESRLNEENYSLLLASTNNDvEQEKKALEMMLSFG-VDGLIVEPTKSNlyNPNISYYLsfkEQDVPLI------- 169
Cdd:cd20009   18 QLISGISEALRGTPYHLVVTPEFPG-DDPLEPVRYIVENRlADGIIISHTEPQ--DPRVRYLL---ERGFPFVthgrtel 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 170 MI-NAYYEqlevpflcLDDVKSSYLATKELITSGHQQIGLISKTDDLQ-GKYRMKGYIQALGEAKLNFLPEHVLffDTES 247
Cdd:cd20009   92 STpHAYFD--------FDNEAFAYEAVRRLAARGRRRIALVAPPRELTyAQHRLRGFRRALAEAGLEVEPLLIV--TLDS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 248 KQHLGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQDNS----YIAqknahVKLTTLTHPQEQ 323
Cdd:cd20009  162 SAEAIRAAARRLLRQPPRPDGIICASEIAALGALAGLEDAGLVVGRDVDVVAKETSpildYFR-----PPIDTLYEDIEE 236
                        250       260       270
                 ....*....|....*....|....*....|
gi 640667755 324 MGRDAADWMIKKVQGKKNLPDQTFYEPELV 353
Cdd:cd20009  237 AGRFLAEALLRRIEGEPAEPLQTLERPELI 266
GntR COG1802
DNA-binding transcriptional regulator, GntR family [Transcription];
17-68 2.46e-09

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


Pssm-ID: 441407 [Multi-domain]  Cd Length: 222  Bit Score: 56.85  E-value: 2.46e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 640667755  17 LTGDYRIGERIpTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFVT 68
Cdd:COG1802   25 LSGELPPGERL-SEAELAERLGVSRTPVREALRRLEAEGLVEIRPNRGARVA 75
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
17-70 8.18e-09

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: 56.76  E-value: 8.18e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 640667755  17 LTGDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFVTNQ 70
Cdd:COG1167   26 LSGRLPPGDRLPSSRELAAQLGVSRSTVVRAYEELEAEGLIESRPGSGTFVAAR 79
PRK09764 PRK09764
GntR family transcriptional regulator;
19-67 1.30e-08

GntR family transcriptional regulator;


Pssm-ID: 182065 [Multi-domain]  Cd Length: 240  Bit Score: 54.83  E-value: 1.30e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 640667755  19 GDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFV 67
Cdd:PRK09764  21 GELKPGDALPTESALQTEFGVSRVTVRQALRQLVEQQILESIQGSGTYV 69
PRK10079 PRK10079
phosphonate metabolism transcriptional regulator PhnF; Provisional
17-67 1.76e-07

phosphonate metabolism transcriptional regulator PhnF; Provisional


Pssm-ID: 182227 [Multi-domain]  Cd Length: 241  Bit Score: 51.70  E-value: 1.76e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 640667755  17 LTGDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFV 67
Cdd:PRK10079  25 LRQHYRCGDYLPAEQQLAARYEVNRHTLRRAIDQLVEKGWVQRRQGVGVLV 75
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
96-353 3.73e-07

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380542 [Multi-domain]  Cd Length: 278  Bit Score: 50.82  E-value: 3.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  96 FPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKS----NLYNPnisyylsFKEQDVPLIM- 170
Cdd:cd06319   14 WQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSsaapTVLDL-------ANEAKIPVVIa 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 171 -INA---YYeqleVPFLCLDDVKSSYLATKELI------TSGHQQIGLIS-KTDDLQGKYRMKGYIQALGEAKLNflpEH 239
Cdd:cd06319   87 dIGTgggDY----VSYIISDNYDGGYQAGEYLAealkenGWGGGSVGIIAiPQSRVNGQARTAGFEDALEEAGVE---EV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 240 VLFFDTESKQHLGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSipDDLSIIGQDNSYIAQKnaHVKLTTL-- 317
Cdd:cd06319  160 ALRQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRT--GDILVVGFDGDPEALD--LIKDGKLdg 235
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 640667755 318 THPQE--QMGRDAADWMIKKVQGkKNLPDQTFYEPELV 353
Cdd:cd06319  236 TVAQQpfGMGARAVELAIQALNG-DNTVEKEIYLPVLL 272
Periplasmic_Binding_Protein_type1 cd01391
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
84-355 5.13e-07

Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.


Pssm-ID: 380477 [Multi-domain]  Cd Length: 280  Bit Score: 50.73  E-value: 5.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  84 IGVITT--YISDYIFPS-IIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPtkSNLYNPNISYYLS 160
Cdd:cd01391    2 IGVVTSslHQIREQFGIqRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGPG--SSSVAIVIQNLAQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 161 FKEQ-----DVPLIMINAYYEQLEVPFLCLDDVKSSYLATKELITSGHQQIGLISKTDDLQGKYRMKGYIQALGEAKLNF 235
Cdd:cd01391   80 LFDIpqlalDATSQDLSDKTLYKYFLSVVFSDTLGARLGLDIVKRKNWTYVAAIHGEGLNSGELRMAGFKELAKQEGICI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 236 LPEHVLFFDTESKqhlGEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSipDDLSIIG----QDNSYIAQKNAH 311
Cdd:cd01391  160 VASDKADWNAGEK---GFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLV--GDVSVIGsdgwADRDEVGYEVEA 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 640667755 312 VKLTTLTHPQEQMGRDAADWMIKKVQGKKNLPDQTFYEPELVPG 355
Cdd:cd01391  235 NGLTTIKQQKMGFGITAIKAMADGSQNMHEEVWFDEKGDALGRY 278
PRK10421 PRK10421
DNA-binding transcriptional repressor LldR; Provisional
24-75 8.63e-07

DNA-binding transcriptional repressor LldR; Provisional


Pssm-ID: 236690 [Multi-domain]  Cd Length: 253  Bit Score: 49.77  E-value: 8.63e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 640667755  24 GERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFVtnQYQTKP 75
Cdd:PRK10421  23 GMKLPAERQLAMQLGVSRNSLREALAKLVSEGVLLSRRGGGTFI--RWRHET 72
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
108-352 1.80e-06

monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380625 [Multi-domain]  Cd Length: 275  Bit Score: 48.79  E-value: 1.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 108 NEENYSLLLASTNN--DVEQEKKALEMMLSFGVDGLIVEPTKSNLYNPNISyylsfKEQDVPLIMIN---------AYYE 176
Cdd:cd19970   27 EANGYELLVKGIKQetDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLK-----KAVDAGIAVINidnrldadaLKEG 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 177 QLEVPFLCLDDVKSSYLATKEL---ITSGHQQIGL--ISKTDDLQGkyRMKGYIQALGEAKLNFLPEHVLFFDTESKQhl 251
Cdd:cd19970  102 GINVPFVGPDNRQGAYLAGDYLakkLGKGGKVAIIegIPGADNAQQ--RKAGFLKAFEEAGMKIVASQSANWEIDEAN-- 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 252 gEQISTFLMAHRhELTALVCYNDEVGLEVANVCSEIGLSipDDLSIIGQDNsyIAQKNAHVK----LTTLTHPQEQMGRD 327
Cdd:cd19970  178 -TVAANLLTAHP-DIRGILCANDNMALGAIKAVDAAGKA--GKVLVVGFDN--IPAVRPLLKdgkmLATIDQHPAKQAVY 251
                        250       260
                 ....*....|....*....|....*
gi 640667755 328 AADWMIKKVQGKKnLPDQTFYEPEL 352
Cdd:cd19970  252 GIEYALKMLNGEE-VPGWVKTPVEL 275
PRK11523 PRK11523
transcriptional regulator ExuR;
19-85 1.80e-06

transcriptional regulator ExuR;


Pssm-ID: 183176 [Multi-domain]  Cd Length: 253  Bit Score: 48.69  E-value: 1.80e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  19 GDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFVTN---QYQTKPAGHAHMKTIG 85
Cdd:PRK11523  24 GVYLVGDKLPAERFIADEKNVSRTVVREAIIMLEVEGYVEVRKGSGIHVVSnqpRHQQAADNNMEFANYG 93
pdhR PRK09464
pyruvate dehydrogenase complex transcriptional repressor PdhR;
17-70 3.46e-06

pyruvate dehydrogenase complex transcriptional repressor PdhR;


Pssm-ID: 181879 [Multi-domain]  Cd Length: 254  Bit Score: 47.71  E-value: 3.46e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 640667755  17 LTGDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFVTNQ 70
Cdd:PRK09464  24 LEGTLRPGEKLPPERELAKQFDVSRPSLREAIQRLEAKGLLLRRQGGGTFVQSS 77
PRK10225 PRK10225
Uxu operon transcriptional regulator;
2-67 4.12e-06

Uxu operon transcriptional regulator;


Pssm-ID: 182318 [Multi-domain]  Cd Length: 257  Bit Score: 47.71  E-value: 4.12e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 640667755   2 KKKYQIIIDDIKSKILTGDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFV 67
Cdd:PRK10225   8 QRPYQEVGAMIRDLIIKTPYNPGERLPPEREIAEMLDVTRTVVREALIMLEIKGLVEVRRGAGIYV 73
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
100-359 5.73e-06

periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; Periplasmic binding domain of ABC-type YtfQ-like transport systems. The YtfQ protein from Escherichia coli is up-regulated under glucose-limited conditions and shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their ligand specificity is not determined experimentally.


Pssm-ID: 380532 [Multi-domain]  Cd Length: 285  Bit Score: 47.21  E-value: 5.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 100 IRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYNPnisYYLSFKEQDVPLIM----INAYY 175
Cdd:cd06309   18 TKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDP---VLKEAKDAGIPVILvdrtIDGED 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 176 EQLEVPFLCLDDVKSSYLATKelITSGHQQIGLIsKTDDLQGKY-------RMKGYIQALGEA-KLNFLPEHVLFFDTES 247
Cdd:cd06309   95 GSLYVTFIGSDFVEEGRRAAE--WLVKNYKGGKG-NVVELQGTAgssvaidRSKGFREVIKKHpNIKIVASQSGNFTREK 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 248 KQhlgEQISTFLMAHRHELTALVCYNDEVGLEVANVCSEIGLSIPDDLSIIGQD---NSYIAQKNAHVKLTTLTHPqeQM 324
Cdd:cd06309  172 GQ---KVMENLLQAGPGDIDVIYAHNDDMALGAIQALKEAGLKPGKDVLVVGIDgqkDALEAIKAGELNATVECNP--LF 246
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 640667755 325 GRDAADwMIKKVQGKKNLPDQTFYEPELVPGETIK 359
Cdd:cd06309  247 GPTAFD-TIAKLLAGEKVPKLIIVEERLFDKDNAA 280
PRK14999 PRK14999
histidine utilization repressor; Provisional
18-67 6.21e-06

histidine utilization repressor; Provisional


Pssm-ID: 184961 [Multi-domain]  Cd Length: 241  Bit Score: 46.85  E-value: 6.21e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 640667755  18 TGDYRIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSEKGSGTFV 67
Cdd:PRK14999  27 GGVWQPHDRIPSEAELVAQYGFSRMTINRALRELTDEGWLVRLQGVGTFV 76
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
83-353 8.04e-06

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380545 [Multi-domain]  Cd Length: 270  Bit Score: 46.89  E-value: 8.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYNPNIsyyLSFK 162
Cdd:cd06322    1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAI---EAAN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAyyeqlevpfLCLDDVKSSYLAT-------------KELITSGHQQIGLISKTDDLQGKYRMKGYIQALG 229
Cdd:cd06322   78 EAGIPVFTVDV---------KADGAKVVTHVGTdnyaggklageyaLKALLGGGGKIAIIDYPEVESVVLRVNGFKEAIK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 230 EAK----LNFLPEHVlffDTESKQHLGEQIstfLMAHRhELTALVCYNDEVGLEVANVCSEIGLSipDDLSIIGQDNSYI 305
Cdd:cd06322  149 KYPnieiVAEQPGDG---RREEALAATEDM---LQANP-DLDGIFAIGDPAALGALTAIESAGKE--DKIKVIGFDGNPE 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 640667755 306 A----QKNAHVKLTTLTHPqEQMGRDAADWMIKKVQGKKnLPDQTFYEPELV 353
Cdd:cd06322  220 AikaiAKGGKIKADIAQQP-DKIGQETVEAIVKYLAGET-VEKEILIPPKLY 269
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
83-362 2.20e-05

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380540 [Multi-domain]  Cd Length: 281  Bit Score: 45.44  E-value: 2.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYNPNISyylSFK 162
Cdd:cd06317    1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIK---RAS 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAyyeQLEVPFLCLDDVKSSYLATKEL-------ITS---GHQQIGLISKTDDLQGKYRMKGYIQALGEAk 232
Cdd:cd06317   78 EAGIPVIAYDA---VIPSDFQAAQVGVDNLEGGKEIgkyaadyIKAelgGQAKIGVVGALSSLIQNQRQKGFEEALKAN- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 233 lnflPEhVLFFDTESKQHLGEQ---ISTFLMAHRHELTALVCYNDE--VGLeVANVCSEiglSIPDDLSIIGQDNS--YI 305
Cdd:cd06317  154 ----PG-VEIVATVDGQNVQEKalsAAENLLTANPDLDAIYATGEPalLGA-VAAVRSQ---GRQGKIKVFGWDLTkqAI 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 640667755 306 AQK--NAHVKLTTLTHPqEQMGRDAADWMIKKVQGKKnLPDQTFYEPELVPGETIKRIK 362
Cdd:cd06317  225 FLGidEGVLQAVVQQDP-EKMGYEAVKAAVKAIKGED-VEKTIDVPPTIVTKENVDQFR 281
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
118-232 4.32e-05

monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380620 [Multi-domain]  Cd Length: 272  Bit Score: 44.57  E-value: 4.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 118 STNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYNPNISYYLsfkEQDVPLIMINA---YYEQLEVPFLCLDDVKSSY-- 192
Cdd:cd19965   37 PQTFDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRAL---DAGIPVVAFNVdapGGENARLAFVGQDLYPAGYvl 113
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 640667755 193 ---LATKELITSGHQQIGlISKTDDLQGKYRMKGYIQALGEAK 232
Cdd:cd19965  114 gkrIAEKFKPGGGHVLLG-ISTPGQSALEQRLDGIKQALKEYG 155
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
83-353 1.43e-04

periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380541 [Multi-domain]  Cd Length: 282  Bit Score: 43.17  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYNPNISyylSFK 162
Cdd:cd06318    1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVK---AAK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINAYYEQLE--VPFLCLDDVKSSYLATKELI-TSGHQQIGLISKTDDLQGKY---RMKGYIQALGEAKL--- 233
Cdd:cd06318   78 AAGIPVITVDSALDPSAnvATQVGRDNKQNGVLVGKEAAkALGGDPGKIIELSGDKGNEVsrdRRDGFLAGVNEYQLrky 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 234 -------------NFLPEHVLffdtESKQHLgeqistfLMAHRhELTALVCYNDEVGLEVANVCSEIGLSipDDL---SI 297
Cdd:cd06318  158 gksnikvvaqpygNWIRSGAV----AAMEDL-------LQAHP-DINVVYAENDDMALGAMKALKAAGML--DKVkvaGA 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 640667755 298 IGQDNSYIAQKNAHVKLTTLTHPqEQMGRDAADWMIKKVQGKKNLPDQTFYEPELV 353
Cdd:cd06318  224 DGQKEALKLIKDGKYVATGLNDP-DLLGKTAVDTAAKVVKGEESFPEFTYTPTALI 278
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
96-353 2.08e-04

periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs; Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis D-ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group belong to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.


Pssm-ID: 380546 [Multi-domain]  Cd Length: 268  Bit Score: 42.28  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  96 FPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYNPNISyylSFKEQDVPLIMINAYY 175
Cdd:cd06323   14 FVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVE---EANEAGIPVITVDRSV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 176 EQLEV-PFLCLDDVKSSYLATKELItsghQQIGLISKTDDLQG-------KYRMKGYIQALGEA-KLNFLPEHVLFFDTE 246
Cdd:cd06323   91 TGGKVvSHIASDNVAGGEMAAEYIA----KKLGGKGKVVELQGipgtsaaRERGKGFHNAIAKYpKINVVASQTADFDRT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 247 SKQHLGEQIstfLMAHRhELTALVCYNDEVGLevaNVCSEIGLSIPDDLSIIGQDNSYIAQ---KNAHVKLTTLTHPqEQ 323
Cdd:cd06323  167 KGLNVMENL---LQAHP-DIDAVFAHNDEMAL---GAIQALKAAGRKDVIVVGFDGTPDAVkavKDGKLAATVAQQP-EE 238
                        250       260       270
                 ....*....|....*....|....*....|
gi 640667755 324 MGRDAADWMIKKVQGKKnLPDQTFYEPELV 353
Cdd:cd06323  239 MGAKAVETADKYLKGEK-VPKKIPVPLKLV 267
PBP1_ABC_xylose_binding-like cd19993
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
103-342 5.36e-04

periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380648 [Multi-domain]  Cd Length: 287  Bit Score: 41.31  E-value: 5.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 103 IESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYNPNISyylSFKEQDVPLIMINAYYEQLEVPF 182
Cdd:cd19993   21 MKKALEKAGAKYISADAQSSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVE---KAAAEGIPVIAYDRLIENPIAFY 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 183 LCLDDVKSSYLATKELIT---SGHQQIGLISKTDDLQGKYRmKGYIQALGEA----KLNFLPE-HVLFFDTESKQHLGEQ 254
Cdd:cd19993   98 ISFDNVEVGRMQARGVLKakpEGNYVFIKGSPTDPNADFLR-AGQMEVLQPAidsgKIKIVGEqYTDGWKPANAQKNMEQ 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 255 IstfLMAHRHELTALVCYNDEVGLEVANVCSEIGL--SIPddlsIIGQDnsyiAQKNA--HVKLTTLT----HPQEQMGR 326
Cdd:cd19993  177 I---LTANNNKVDAVVASNDGTAGGAVAALAAQGLagKVP----VSGQD----ADKAAlnRIALGTQTvtvwKDARELGK 245
                        250
                 ....*....|....*.
gi 640667755 327 DAADWMIKKVQGKKNL 342
Cdd:cd19993  246 EAAEIAVELAKGTKIE 261
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
83-340 9.90e-04

monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380626 [Multi-domain]  Cd Length: 267  Bit Score: 40.26  E-value: 9.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVITTYISDYIFPSIIRGIESRLNEENYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYNPNIsyyLSFK 162
Cdd:cd19971    1 KFGFSYMTMNNPFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPAL---EAAK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 163 EQDVPLIMINA--YYEQLEVPFLCLDDVKSSYLATKELI--TSGHQQIGLISKTDDLQGKYRMKGYIQALGEAKlNFlpE 238
Cdd:cd19971   78 EAGIPVINVDTpvKDTDLVDSTIASDNYNAGKLCGEDMVkkLPEGAKIAVLDHPTAESCVDRIDGFLDAIKKNP-KF--E 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 239 HVLFFDTESKQHLG-EQISTFLMAHrHELTALVCYNDEVGLEVANVCSEIGLsiPDDLSIIGQDNSYIAQK---NAHVKL 314
Cdd:cd19971  155 VVAQQDGKGQLEVAmPIMEDILQAH-PDLDAVFALNDPSALGALAALKAAGK--LGDILVYGVDGSPDAKAaikDGKMTA 231
                        250       260
                 ....*....|....*....|....*.
gi 640667755 315 TTLTHPQEqMGRDAADWMIKKVQGKK 340
Cdd:cd19971  232 TAAQSPIE-IGKKAVETAYKILNGEK 256
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
83-350 1.25e-03

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380663 [Multi-domain]  Cd Length: 277  Bit Score: 40.29  E-value: 1.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVIT-TYISDYiFPSIIRGIESRLNEE--NYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVEPTKSNLYNPNISYYl 159
Cdd:cd20008    1 KIAVIVkDTDSEY-WQTVLKGAEKAAKELgvEVTFLGPATEADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAA- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 160 sfkEQDVPLIMINA-----YYeqleVPFLCLDDVKSSYLATKELitsghqqIGLISKTDDLQGKY--------------R 220
Cdd:cd20008   79 ---DAGIPVVLVDSgantdDY----DAFLATDNVAAGALAADEL-------AELLKASGGGKGKVaiisfqagsqtlvdR 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755 221 MKGYIQALGEAKLNFLPEHVLFFDTESKQHLGeQISTFLMAHRhELTALVCYNDEVGLEVANVCSEIGLSipDDLSIIGQ 300
Cdd:cd20008  145 EEGFRDYIKEKYPDIEIVDVQYSDGDIAKALN-QTTDLLTANP-DLVGIFGANNPSAVGVAQALAEAGKA--GKIVLVGF 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 640667755 301 DNSYI---AQKNAHVKLTTLTHPqEQMGRDAADWMIKKVQGKKnlPDQTFYEP 350
Cdd:cd20008  221 DSSPDevaLLKSGVIKALVVQDP-YQMGYEGVKTAVKALKGEE--IVEKNVDT 270
PBP1_GGBP cd01539
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ...
83-172 4.32e-03

periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species; Periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species. GGBP is a member of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic GGBP is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380481 [Multi-domain]  Cd Length: 302  Bit Score: 38.72  E-value: 4.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 640667755  83 TIGVIT-----TYISdyifpSIIRGIESRLNEE-NYSLLLASTNNDVEQEKKALEMMLSFGVDGLIVeptksNLYNPNIS 156
Cdd:cd01539    2 KIGVFIynyddTFIS-----SVRKALEKAAKAGgKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVV-----NLVDRTAA 71
                         90
                 ....*....|....*...
gi 640667755 157 YYL--SFKEQDVPLIMIN 172
Cdd:cd01539   72 QTIidKAKAANIPVIFFN 89
HTH_41 pfam14502
Helix-turn-helix domain;
22-67 8.97e-03

Helix-turn-helix domain;


Pssm-ID: 433997 [Multi-domain]  Cd Length: 48  Bit Score: 34.00  E-value: 8.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 640667755   22 RIGERIPTESSLQDMYQVSRHTVRKAILELSSEGFLRSE-KG-SGTFV 67
Cdd:pfam14502   1 KAGERLPTISEYSHKFELSVGTVQKALKKLEDMKAIQLErRGhNGTYL 48
 
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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