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Conserved domains on  [gi|1179834730|gb|ORJ25326|]
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LacI family transcriptional regulator [Rouxiella badensis]

Protein Classification

LacI family DNA-binding transcriptional regulator( domain architecture ID 11446715)

LacI family DNA-binding transcriptional regulator functions as an activator or repressor by binding a specific effector ligand that either decreases (induction) or increases DNA-binding affinity (co-repression)

CATH:  3.40.50.2300
Gene Ontology:  GO:0003677|GO:0003700|GO:0006355
PubMed:  8543068|12598694

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
9-339 1.54e-92

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


:

Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 279.39  E-value: 1.54e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730   9 SGKSTLADVAKMTGVSTMTVSRVLREPEKVSPQVREKIEAAISELGYVPNLAASNLASSTSRLVTMVVPSMSTPGCAEFS 88
Cdd:COG1609     1 RKRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  89 EALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIPVVQVGATLATPIGINIGT 168
Cdd:COG1609    81 RGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRPLPDPGVPSVGV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 169 NYGLAIKQLINALALKGYRNIALLCAAHEHHIVQQILSGWHSSILSLNQSPHRVVSSSLPPTVQTGQRLLPDILLNWPEL 248
Cdd:COG1609   161 DNRAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGPRP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 249 DLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKHILAALQGDDVE-ESVM 327
Cdd:COG1609   241 TAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPpERVL 320

                         330
                  ....*....|..
gi 1179834730 328 LPSTLMLRGSTA 339
Cdd:COG1609   321 LPPELVVRESTA 332
 
Name Accession Description Interval E-value
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
9-339 1.54e-92

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 279.39  E-value: 1.54e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730   9 SGKSTLADVAKMTGVSTMTVSRVLREPEKVSPQVREKIEAAISELGYVPNLAASNLASSTSRLVTMVVPSMSTPGCAEFS 88
Cdd:COG1609     1 RKRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  89 EALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIPVVQVGATLATPIGINIGT 168
Cdd:COG1609    81 RGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRPLPDPGVPSVGV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 169 NYGLAIKQLINALALKGYRNIALLCAAHEHHIVQQILSGWHSSILSLNQSPHRVVSSSLPPTVQTGQRLLPDILLNWPEL 248
Cdd:COG1609   161 DNRAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGPRP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 249 DLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKHILAALQGDDVE-ESVM 327
Cdd:COG1609   241 TAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPpERVL 320

                         330
                  ....*....|..
gi 1179834730 328 LPSTLMLRGSTA 339
Cdd:COG1609   321 LPPELVVRESTA 332
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
 71-337 1.29e-91

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: 274.37  E-value: 1.29e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  71 LVTMVVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIP 150
Cdd:cd01575     1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEHTPATRKLLRAAGIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 151 VVQVGATLATPIGINIGTNYGLAIKQLINALALKGYRNIALLCAAHEHHI-VQQILSGWHSSILSLNQSPHRVVSSSLPP 229
Cdd:cd01575    81 VVETWDLPDDPIDMAVGFSNFAAGRAMARHLIERGYRRIAFVGARLDGDSrARQRLEGFRDALAEAGLPLPLVLLVELPS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 230 TVQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQT 309
Cdd:cd01575   161 SFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVRVPRYEIGRKA 240

                         250       260
                  ....*....|....*....|....*....
gi 1179834730 310 GKHILAALQGDDVEESVM-LPSTLMLRGS 337
Cdd:cd01575   241 AELLLARLEGEEPEPRVVdLGFELVRRES 269
PRK14987 PRK14987
HTH-type transcriptional regulator GntR;
11-327 1.58e-50

HTH-type transcriptional regulator GntR;


Pssm-ID: 184949 [Multi-domain]  Cd Length: 331  Bit Score: 170.98  E-value: 1.58e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  11 KSTLADVAKMTGVSTMTVSRVLREPEKVSPQVREKIEAAISELGYVPNLAASNLASSTSRLVTMVVPSMSTPGCAEFSEA 90
Cdd:PRK14987    5 RPVLQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  91 LYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIPVVQVGATLATPIGINIGTNY 170
Cdd:PRK14987   85 IESVTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIEVAGIPVVELMDSQSPCLDIAVGFDN 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 171 GLAIKQLINALALKGYRNIALLCAA-HEHHIVQQilSGWHSSILSLNQSPHRVVSSSlPPTVQTGQRLLPDILLNWPELD 249
Cdd:PRK14987  165 FEAARQMTTAIIARGHRHIAYLGARlDERTIIKQ--KGYEQAMLDAGLVPYSVMVEQ-SSSYSSGIELIRQARREYPQLD 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1179834730 250 LLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKHILAALQGDDVEESVM 327
Cdd:PRK14987  242 GVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARIRGESVTPKML 319
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
13-80 9.18e-25

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 95.35  E-value: 9.18e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1179834730   13 TLADVAKMTGVSTMTVSRVLREPEKVSPQVREKIEAAISELGYVPNLAASNLASSTSRLVTMVVPSMS 80
Cdd:smart00354   2 TIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDIT 69
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
 181-338 4.87e-23

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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 433159 [Multi-domain]  Cd Length: 160  Bit Score: 93.56  E-value: 4.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 181 LALKGYRNIALLCAAHEHH--IVQQILSGWHSSILSLNQSPHRVVSSSLPPTVQTGQRLLPDILLNWPelDLLICTSDEL 258
Cdd:pfam13377   2 LAELGHRRIALIGPEGDRDdpYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARERLRWLGALP--TAVFVANDEV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 259 ASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKHILAALQGDD-VEESVMLPSTLMLRGS 337
Cdd:pfam13377  80 ALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPaPPERVLLPPELVERES 159


                  .
gi 1179834730 338 T 338
Cdd:pfam13377 160 T 160
 
Name Accession Description Interval E-value
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
9-339 1.54e-92

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 279.39  E-value: 1.54e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730   9 SGKSTLADVAKMTGVSTMTVSRVLREPEKVSPQVREKIEAAISELGYVPNLAASNLASSTSRLVTMVVPSMSTPGCAEFS 88
Cdd:COG1609     1 RKRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  89 EALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIPVVQVGATLATPIGINIGT 168
Cdd:COG1609    81 RGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRPLPDPGVPSVGV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 169 NYGLAIKQLINALALKGYRNIALLCAAHEHHIVQQILSGWHSSILSLNQSPHRVVSSSLPPTVQTGQRLLPDILLNWPEL 248
Cdd:COG1609   161 DNRAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGPRP 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 249 DLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKHILAALQGDDVE-ESVM 327
Cdd:COG1609   241 TAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPpERVL 320

                         330
                  ....*....|..
gi 1179834730 328 LPSTLMLRGSTA 339
Cdd:COG1609   321 LPPELVVRESTA 332
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
 71-337 1.29e-91

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: 274.37  E-value: 1.29e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  71 LVTMVVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIP 150
Cdd:cd01575     1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEHTPATRKLLRAAGIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 151 VVQVGATLATPIGINIGTNYGLAIKQLINALALKGYRNIALLCAAHEHHI-VQQILSGWHSSILSLNQSPHRVVSSSLPP 229
Cdd:cd01575    81 VVETWDLPDDPIDMAVGFSNFAAGRAMARHLIERGYRRIAFVGARLDGDSrARQRLEGFRDALAEAGLPLPLVLLVELPS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 230 TVQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQT 309
Cdd:cd01575   161 SFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVRVPRYEIGRKA 240

                         250       260
                  ....*....|....*....|....*....
gi 1179834730 310 GKHILAALQGDDVEESVM-LPSTLMLRGS 337
Cdd:cd01575   241 AELLLARLEGEEPEPRVVdLGFELVRRES 269
PRK14987 PRK14987
HTH-type transcriptional regulator GntR;
11-327 1.58e-50

HTH-type transcriptional regulator GntR;


Pssm-ID: 184949 [Multi-domain]  Cd Length: 331  Bit Score: 170.98  E-value: 1.58e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  11 KSTLADVAKMTGVSTMTVSRVLREPEKVSPQVREKIEAAISELGYVPNLAASNLASSTSRLVTMVVPSMSTPGCAEFSEA 90
Cdd:PRK14987    5 RPVLQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  91 LYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIPVVQVGATLATPIGINIGTNY 170
Cdd:PRK14987   85 IESVTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIEVAGIPVVELMDSQSPCLDIAVGFDN 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 171 GLAIKQLINALALKGYRNIALLCAA-HEHHIVQQilSGWHSSILSLNQSPHRVVSSSlPPTVQTGQRLLPDILLNWPELD 249
Cdd:PRK14987  165 FEAARQMTTAIIARGHRHIAYLGARlDERTIIKQ--KGYEQAMLDAGLVPYSVMVEQ-SSSYSSGIELIRQARREYPQLD 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1179834730 250 LLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKHILAALQGDDVEESVM 327
Cdd:PRK14987  242 GVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARIRGESVTPKML 319
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
 71-333 4.95e-41

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: 144.20  E-value: 4.95e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  71 LVTMVVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIP 150
Cdd:cd06267     1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLAAGIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 151 VVQVGATLATPIGINIGTNYGLAIKQLINALALKGYRNIALLCAAHEHHIVQQILSGWHSSI--LSLNQSPHRVVSSslP 228
Cdd:cd06267    81 VVLIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLSTSRERLEGYRDALaeAGLPVDPELVVEG--D 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 229 PTVQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQ 308
Cdd:cd06267   159 FSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEMGRA 238

                         250       260
                  ....*....|....*....|....*.
gi 1179834730 309 TGKHILAALQGDDVE-ESVMLPSTLM 333
Cdd:cd06267   239 AAELLLERIEGEEEPpRRIVLPTELV 264
PBP1_LacI-like cd06273
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 75-337 1.00e-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: 380497 [Multi-domain]  Cd Length: 268  Bit Score: 141.11  E-value: 1.00e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  75 VVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIPVVQV 154
Cdd:cd06273     5 IVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVGSDHDPELFELLEQRQVPYVLT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 155 GATLATPIGINIGTNYGLAIKQLINALALKGYRNIALLCA-AHEHHIVQQILSGWHSSILSLNQS--PHRVVSSslPPTV 231
Cdd:cd06273    85 WSYDEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGpTAGNDRARARLAGIRDALAERGLElpEERVVEA--PYSI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 232 QTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGK 311
Cdd:cd06273   163 EEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPAREIGELAAR 242

                         250       260
                  ....*....|....*....|....*.
gi 1179834730 312 HILAALQGDDVEESVMLPSTLMLRGS 337
Cdd:cd06273   243 YLLALLEGGPPPKSVELETELIVRES 268
lacI PRK09526
lac repressor; Reviewed
 1-341 2.26e-32

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 123.18  E-value: 2.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730   1 MKAKqrrnsgKSTLADVAKMTGVSTMTVSRVLREPEKVSPQVREKIEAAISELGYVPNLAASNLASSTSRLVTMVVPSMS 80
Cdd:PRK09526    1 MKSK------PVTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTSLA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  81 TPGCAEFSEALYQVLKPKGYNVILA-------EDHYTAADESK-------LIEMMLSYNPAAMVMYDFDcseesnnlllk 146
Cdd:PRK09526   75 LHAPSQIAAAIKSRADQLGYSVVISmversgvEACQAAVNELLaqrvsgvIINVPLEDADAEKIVADCA----------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 147 sTIPVVQVGATLATPIGINIGTNY---GLAIKQLinaLALkGYRNIALLcAAHEHHIVQQI-LSGWHSSILSLNQSPHRV 222
Cdd:PRK09526  144 -DVPCLFLDVSPQSPVNSVSFDPEdgtRLGVEHL---VEL-GHQRIALL-AGPESSVSARLrLAGWLEYLTDYQLQPIAV 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 223 VSSSLppTVQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPY 302
Cdd:PRK09526  218 REGDW--SAMSGYQQTLQMLREGPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDF 295

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1179834730 303 RPMGTQTGKHILAALQGDDVEESVMLPSTLMLRGSTAVH 341
Cdd:PRK09526  296 RLLGKEAVDRLLALSQGQAVKGSQLLPTSLVVRKSTAPP 334
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
 75-337 1.84e-28

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: 111.07  E-value: 1.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  75 VVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMydfdCS-EESNNLLLKSTIPVVQ 153
Cdd:cd06291     5 IVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIIL----GShSLDIEEYKKLNIPIVS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 154 VGATLATPIgINIGT-NYG---LAIKQLINalalKGYRNIALLCAAHEHHIVQQILSGWHSSILSLNQSPHRVVSSSLPP 229
Cdd:cd06291    81 IDRYLSEGI-PSVSSdNYQggrLAAEHLIE----KGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIEIDENDF 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 230 TVQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQT 309
Cdd:cd06291   156 SEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIEEMAKEA 235

                         250       260
                  ....*....|....*....|....*....
gi 1179834730 310 GKHILAALQGDDVEES-VMLPSTLMLRGS 337
Cdd:cd06291   236 VELLLKLIEGEEIEESrIVLPVELIERET 264
PBP1_GalS-like cd06270
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ...
 74-335 4.77e-28

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: 109.92  E-value: 4.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  74 MVVPSMSTPgcaEFSEALYQ---VLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIP 150
Cdd:cd06270     4 LVVPDLSGP---FFGSLLKGaerVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEELILIAEKIPP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 151 VVQVGATLATPIGINIGT-NYG---LAIKQLINalalKGYRNIALLCAAHEHHIVQQILSGWHSSI--LSLNQSPHRVVS 224
Cdd:cd06270    81 LVVINRYIPGLADRCVWLdNEQggrLAAEHLLD----LGHRRIACITGPLDIPDARERLAGYRDALaeAGIPLDPSLIIE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 225 SslPPTVQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRP 304
Cdd:cd06270   157 G--DFTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHYPIEE 234

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1179834730 305 MGTQTGKHILAALQGDDVEESVMLPSTLMLR 335
Cdd:cd06270   235 MAQAAAELALNLAYGEPLPISHEFTPTLIER 265
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
 75-333 6.01e-27

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: 106.81  E-value: 6.01e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  75 VVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIPVVQV 154
Cdd:cd01542     5 IVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEITDEHRKALKKLKIPVVVL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 155 GATLAtpiGIN--IGTNYGlAIKQLINALALKGYRNIALLCAAHEHHIV-QQILSGWHSSILSLNQSPHRVVSSSLppTV 231
Cdd:cd01542    85 GQEHE---GFScvYHDDYG-AGKLLGEYLLKKGHKNIAYIGVDEEDIAVgVARKQGYLDALKEHGIDEVEIVETDF--SM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 232 QTGQRLLPDILLNwPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGK 311
Cdd:cd01542   159 ESGYEAAKELLKE-NKPDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEAGEKAAE 237

                         250       260
                  ....*....|....*....|..
gi 1179834730 312 HILAALQGDDVEESVMLPSTLM 333
Cdd:cd01542   238 LLLDMIEGEKVPKKQKLPYELI 259
PRK10401 PRK10401
HTH-type transcriptional regulator GalS;
13-340 2.11e-26

HTH-type transcriptional regulator GalS;


Pssm-ID: 236681 [Multi-domain]  Cd Length: 346  Bit Score: 107.17  E-value: 2.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  13 TLADVAKMTGVSTMTVSRVLREPEKVSPQVREKIEAAISELGYVPNLAASNLASSTSRLVTMVVPSMSTPGCAEFSEALY 92
Cdd:PRK10401    3 TIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAVD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  93 QVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIPVVQVGATLA----TPIGINIGT 168
Cdd:PRK10401   83 LVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDQIPGMVLINRVVPgyahRCVCLDNVS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 169 NYGLAIKQLINalalKGYRNIALLCAAHEHHIVQQILSGWHSSILSLNQSPHRVVSSSLPPTVQTGQRLLPDILLNWPEL 248
Cdd:PRK10401  163 GARMATRMLLN----NGHQRIGYLSSSHGIEDDAMRRAGWMSALKEQGIIPPESWIGTGTPDMQGGEAAMVELLGRNLQL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 249 DLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKHIL--AALQGDDVEESV 326
Cdd:PRK10401  239 TAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALqgAAGNLDPRASHC 318

                         330
                  ....*....|....
gi 1179834730 327 MLPsTLMLRGSTAV 340
Cdd:PRK10401  319 FMP-TLVRRHSVAT 331
PRK10727 PRK10727
HTH-type transcriptional regulator GalR;
12-339 5.37e-26

HTH-type transcriptional regulator GalR;


Pssm-ID: 182681 [Multi-domain]  Cd Length: 343  Bit Score: 105.99  E-value: 5.37e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  12 STLADVAKMTGVSTMTVSRVLREPEKVSPQVREKIEAAISELGYVPNLAASNLASSTSRLVTMVVPSMSTPGCAEFSEAL 91
Cdd:PRK10727    2 ATIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  92 YQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIPVVQVGATLA--TPIGINIGTN 169
Cdd:PRK10727   82 EQVAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVVHAKMIPDAELASLMKQIPGMVLINRILPgfENRCIALDDR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 170 YG--LAIKQLINalalKGYRNIALLCAAHEHHIVQQILSGWHSSI----LSLNQsphRVVSSSLPPTVqTGQRLLPDILL 243
Cdd:PRK10727  162 YGawLATRHLIQ----QGHTRIGYLCSNHSISDAEDRLQGYYDALaesgIPAND---RLVTFGEPDES-GGEQAMTELLG 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 244 NWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKHILAALQGDDVE 323
Cdd:PRK10727  234 RGRNFTAVACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELALALADNRPLP 313

                         330
                  ....*....|....*..
gi 1179834730 324 ESV-MLPSTLMLRGSTA 339
Cdd:PRK10727  314 EITnVFSPTLVRRHSVS 330
PRK11041 PRK11041
DNA-binding transcriptional regulator CytR; Provisional
 35-339 5.89e-26

DNA-binding transcriptional regulator CytR; Provisional


Pssm-ID: 182923 [Multi-domain]  Cd Length: 309  Bit Score: 105.08  E-value: 5.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  35 PEKVSPQVREKIEAAISELGYVPNLAASNLASSTSRLVTMVVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADE 114
Cdd:PRK11041    1 PEKVSQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 115 SKLIEMMLSYNPAAMVMYD----FDCS-EESNNLllkstIPVV---QVGATLATPIgINIgTNYGLAIKQlINALALKGY 186
Cdd:PRK11041   81 KTFVNLIITKQIDGMLLLGsrlpFDASkEEQRNL-----PPMVmanEFAPELELPT-VHI-DNLTAAFEA-VNYLHELGH 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 187 RNIALLCAAHEHHIVQQILSGWhssILSLNQS-----PHRVVSSSLppTVQTGQRLLpDILLNWPEL-DLLICTSDELAS 260
Cdd:PRK11041  153 KRIACIAGPEEMPLCHYRLQGY---VQALRRCgitvdPQYIARGDF--TFEAGAKAL-KQLLDLPQPpTAVFCHSDVMAL 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 261 GAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKHILAALQGDDVEE-SVMLPSTLMLRGSTA 339
Cdd:PRK11041  227 GALSQAKRMGLRVPQDLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSSgSRLLDCELIIRGSTA 306
PRK10014 PRK10014
DNA-binding transcriptional repressor MalI; Provisional
 11-336 5.24e-25

DNA-binding transcriptional repressor MalI; Provisional


Pssm-ID: 182193 [Multi-domain]  Cd Length: 342  Bit Score: 103.25  E-value: 5.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  11 KSTLADVAKMTGVSTMTVSRVLREPEKVSPQVREKIEAAISELGYVPNLAASNLASSTSRLVTMVVPSMSTPGCAEFSEA 90
Cdd:PRK10014    6 KITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAELTAG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  91 LYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDF-DCSEESNNLLLKSTIPVVQVG-ATLATPIGInIGT 168
Cdd:PRK10014   86 LTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAaGSSDDLREMAEEKGIPVVFASrASYLDDVDT-VRP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 169 NYGLAIKQLINALALKGYRNIALLCAAHEHHIVQQILSGWHSSILS--LNQSPHRVVSSslpptvQTGQRLLPDI---LL 243
Cdd:PRK10014  165 DNMQAAQLLTEHLIRNGHQRIAWLGGQSSSLTRAERVGGYCATLLKfgLPFHSEWVLEC------TSSQKQAAEAitaLL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 244 NW-PELDLLICTSDELASGAIAACHKKGISVPA---------QLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKHI 313
Cdd:PRK10014  239 RHnPTISAVVCYNETIAMGAWFGLLRAGRQSGEsgvdryfeqQVALAAFTDVPEAELDDPPLTWASTPAREIGRTLADRM 318

                         330       340
                  ....*....|....*....|....
gi 1179834730 314 LAALQGDDVE-ESVMLPSTLMLRG 336
Cdd:PRK10014  319 MQRITHEETHsRNLIIPPRLIARK 342
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
13-80 9.18e-25

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 95.35  E-value: 9.18e-25
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1179834730   13 TLADVAKMTGVSTMTVSRVLREPEKVSPQVREKIEAAISELGYVPNLAASNLASSTSRLVTMVVPSMS 80
Cdd:smart00354   2 TIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDIT 69
PRK10423 PRK10423
transcriptional repressor RbsR; Provisional
 16-337 1.16e-24

transcriptional repressor RbsR; Provisional


Pssm-ID: 182448 [Multi-domain]  Cd Length: 327  Bit Score: 102.08  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  16 DVAKMTGVSTMTVSRVLREPEKVSPQVREKIEAAISELGYVPNLAASNLASSTSRLVTMVVPSMSTPGCAEFSEALYQVL 95
Cdd:PRK10423    3 DVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVERSC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  96 KPKGYNVILAEdhyTAADESKLI--------------------------EMMLSYNPAAMVMYD---FDCSEEsnnlllk 146
Cdd:PRK10423   83 FERGYSLVLCN---TEGDEQRMNrnletlmqkrvdgllllctethqpsrEIMQRYPSVPTVMMDwapFDGDSD------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 147 stipVVQVGATLatpiGINIGTNYglaikqLINalalKGYRNIALLCAAHEHHIVQQILSGWHSSI--LSLNQSPHRVVS 224
Cdd:PRK10423  153 ----LIQDNSLL----GGDLATQY------LID----KGYTRIACITGPLDKTPARLRLEGYRAAMkrAGLNIPDGYEVT 214

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 225 SSLppTVQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRP 304
Cdd:PRK10423  215 GDF--EFNGGFDAMQQLLALPLRPQAVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDE 292

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1179834730 305 MGTQTGKHILAALQGDDVEESVM-LPSTLMLRGS 337
Cdd:PRK10423  293 LGELAIDVLIHRMAQPTLQQQRLqLTPELMERGS 326
PBP1_DegA_Like cd19976
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
 71-337 1.59e-24

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: 100.40  E-value: 1.59e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  71 LVTMVVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEES-NNLLLKSTI 149
Cdd:cd19976     1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNISDEAiIKLLKEEKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 150 PVVQVGATLATPIGINIGTNY--G--LAIKQLINalalKGYRNIALLCAAHEHHIVQQILSGWHSSILS--LNQSPHRVV 223
Cdd:cd19976    81 PVVVLDRYIEDNDSDSVGVDDyrGgyEATKYLIE----LGHTRIGCIVGPPSTYNEHERIEGYKNALQDhnLPIDESWIY 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 224 SSSLppTVQTGQRLLPDiLLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYR 303
Cdd:cd19976   157 SGES--SLEGGYKAAEE-LLKSKNPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQPIF 233

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1179834730 304 PMGTQTGKHILAALQGDDVE-ESVMLPSTLMLRGS 337
Cdd:cd19976   234 EMGQEAAKLLLKIIKNPAKKkEEIVLPPELIKRDS 268
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
 72-337 3.76e-24

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: 99.54  E-value: 3.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  72 VTMVVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKsTIPV 151
Cdd:cd06284     2 ILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILLSGRLDAELLSELSK-RYPI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 152 VQV-----GATLATpIGINigtNY---GLAIKQLINalalKGYRNIALLCAAHEHHIVQQILSGW------HSSILSlnq 217
Cdd:cd06284    81 VQCceyipDSGVPS-VSID---NEaaaYDATEYLIS----LGHRRIAHINGPLDNVYARERLEGYrralaeAGLPVD--- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 218 sPHRVVSSSLppTVQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTT 297
Cdd:cd06284   150 -EDLIIEGDF--SFEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTT 226

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1179834730 298 VAIPYRPMGTQTGKHILAALQGDDVE-ESVMLPSTLMLRGS 337
Cdd:cd06284   227 IRQPRYEIGETAAELLLEKIEGEGVPpEHIILPHELIVRES 267
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
 71-335 1.20e-23

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: 98.02  E-value: 1.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  71 LVTMVVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMydfdC-----SEESNNLLL 145
Cdd:cd06289     1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLIL----SpaagtTAELLRRLK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 146 KSTIPVVQVGATLATPIGINIGTNYGLAIKQLINALALKGYRNIALLCAAHEHHIVQQILSGWHSSILSLNQSPHRVVSS 225
Cdd:cd06289    77 AWGIPVVLALRDVPGSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSSTRRERLAGFRAALAEAGLPLDESLIV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 226 SLPPTVQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPM 305
Cdd:cd06289   157 PGPATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHPREI 236

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1179834730 306 GTQTGKHILAALQGDD-VEESVMLPSTLMLR 335
Cdd:cd06289   237 GRRAARLLLRRIEGPDtPPERIIIEPRLVVR 267
PRK10703 PRK10703
HTH-type transcriptional repressor PurR;
12-339 1.24e-23

HTH-type transcriptional repressor PurR;


Pssm-ID: 236739 [Multi-domain]  Cd Length: 341  Bit Score: 99.41  E-value: 1.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  12 STLADVAKMTGVSTMTVSRVLREPEKVSPQVREKIEAAISELGYVPNLAASNLASSTSRLVTMVVPSMSTPGCAEFSEAL 91
Cdd:PRK10703    2 ATIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEAV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  92 YQVLKPKGYNVILAEDHYTAADESKLIEMMLSYN-PAAMVMydfdCSEESNNLL--LK--STIPVV-----QVGATLATP 161
Cdd:PRK10703   82 EKNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRvDGLLVM----CSEYPEPLLamLEeyRHIPMVvmdwgEAKADFTDA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 162 IGINIGTNYGLAIKQLINalalKGYRNIALLCAAHEHHIVQQILSGW----HSSILSLNqsPHRVVSSSLPPtvQTGQRL 237
Cdd:PRK10703  158 IIDNAFEGGYLAGRYLIE----RGHRDIGVIPGPLERNTGAGRLAGFmkamEEANIKVP--EEWIVQGDFEP--ESGYEA 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 238 LPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKHILAAL 317
Cdd:PRK10703  230 MQQILSQKHRPTAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRI 309

                         330       340
                  ....*....|....*....|...
gi 1179834730 318 QGDDVE-ESVMLPSTLMLRGSTA 339
Cdd:PRK10703  310 VNKREEpQTIEVHPRLVERRSVA 332
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
 181-338 4.87e-23

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://0-doi-org.brum.beds.ac.uk/10.1093/femsre/fuab043).


Pssm-ID: 433159 [Multi-domain]  Cd Length: 160  Bit Score: 93.56  E-value: 4.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 181 LALKGYRNIALLCAAHEHH--IVQQILSGWHSSILSLNQSPHRVVSSSLPPTVQTGQRLLPDILLNWPelDLLICTSDEL 258
Cdd:pfam13377   2 LAELGHRRIALIGPEGDRDdpYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARERLRWLGALP--TAVFVANDEV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 259 ASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKHILAALQGDD-VEESVMLPSTLMLRGS 337
Cdd:pfam13377  80 ALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPaPPERVLLPPELVERES 159


                  .
gi 1179834730 338 T 338
Cdd:pfam13377 160 T 160
PBP1_CcpA-like cd19975
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
 75-337 2.39e-21

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: 91.85  E-value: 2.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  75 VVPSMSTPGCAEFSEALYQVLKPKGYNVILaedHYTAADESKLIE---MMLSYNPAAMVMydfdCS---EESNNLLLKST 148
Cdd:cd19975     5 IIPDISNSFFAEILKGIEDEARENGYSVIL---CNTGSDEEREKKylqLLKEKRVDGIIF----ASgtlTEENKQLLKNM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 149 -IPVVQVGATLATP----IGINigtNYGLA---IKQLINalalKGYRNIALLCA-AHEHHIVQQILSGWHSSIL--SLNQ 217
Cdd:cd19975    78 nIPVVLVSTESEDPdipsVKID---DYQAAydaTNYLIK----KGHRKIAMISGpLDDPNAGYPRYEGYKKALKdaGLPI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 218 SPHRVVSSSLppTVQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTT 297
Cdd:cd19975   151 KENLIVEGDF--SFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTT 228

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1179834730 298 VAIPYRPMGTQTGKHILAALQGDDVEE-SVMLPSTLMLRGS 337
Cdd:cd19975   229 VSQPFYEMGKKAVELLLDLIKNEKKEEkSIVLPHQIIERES 269
PBP1_sucrose_transcription_regulator cd06288
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ...
 98-337 2.48e-21

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: 91.84  E-value: 2.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  98 KGYNVILAEDHYTAADESKLIEMMLSYNPAAMV---MYdfdcSEESNNLLLKSTIPVVQVGATLATPIGINIGTN----- 169
Cdd:cd06288    29 HGYLLLLANTGGDPELEAEAIRELLSRRVDGIIyasMH----HREVTLPPELTDIPLVLLNCFDDDPSLPSVVPDdeqgg 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 170 YgLAIKQLINAlalkGYRNIALLC-----------------AAHEHHIVQ----QILSGWHSSilSLNQSPHRVVSSSLP 228
Cdd:cd06288   105 Y-LATRHLIEA----GHRRIAFIGgpedslatrlrlagyraALAEAGIPYdpslVVHGDWGRE--SGYEAAKRLLSAPDR 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 229 PTVqtgqrllpdillnwpeldlLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQ 308
Cdd:cd06288   178 PTA-------------------IFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVALPYYEMGRR 238

                         250       260       270
                  ....*....|....*....|....*....|
gi 1179834730 309 TGKHILAALQGDDVEES-VMLPSTLMLRGS 337
Cdd:cd06288   239 AAELLLDGIEGEPPEPGvIRVPCPLIERES 268
PBP1_CcpB-like cd06286
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ...
 75-335 3.24e-21

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: 91.07  E-value: 3.24e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  75 VVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMlsynpaAMVMYD--FDCSEEsNNLllkSTI--- 149
Cdd:cd06286     5 VVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELL------KTKQIDglIITSRE-NDW---EVIepy 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 150 ----PVVQVGATLATPIGInIGTNYGLAIKQLINALALKGYRNIALLCA--AHEHHIVQQILSGWHSSI--LSLNQSPHR 221
Cdd:cd06286    75 akygPIVLCEETDSPDIPS-VYIDRYEAYLEALEYLKEKGHRKIGYCLGrpESSSASTQARLKAYQDVLgeHGLSLREEW 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 222 VVSSSLppTVQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQIcsPSLTTVAIP 301
Cdd:cd06286   154 IFTNCH--TIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISEL--LNLTTIDQP 229

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1179834730 302 YRPMGTQTGKHILAALQGDDVeESVMLPSTLMLR 335
Cdd:cd06286   230 LEEMGKEAFELLLSQLESKEP-TKKELPSKLIER 262
PBP1_LacI cd01574
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ...
 99-337 2.21e-20

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: 89.18  E-value: 2.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  99 GYNVILAE-DHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIPVVQVGATLATPIGInIGTNYGLAIKQL 177
Cdd:cd01574    29 GYSVSIATvDEDDPASVREALDRLLSQRVDGIIVIAPDEAVLEALRRLPPGLPVVIVGSGPSPGVPT-VSIDQEEGARLA 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 178 INALALKGYRNIALLCAAHEHHIVQQILSGWHSSILSLNQSPHRVVSSSLPPT--VQTGQRLLPDillnwPELDLLICTS 255
Cdd:cd01574   108 TRHLLELGHRRIAHIAGPLDWVDARARLRGWREALEEAGLPPPPVVEGDWSAAsgYRAGRRLLDD-----GPVTAVFAAN 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 256 DELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKHILAALQGDD-VEESVMLPSTLML 334
Cdd:cd01574   183 DQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDFAELGRRAVELLLALIEGPApPPESVLLPPELVV 262


                  ...
gi 1179834730 335 RGS 337
Cdd:cd01574   263 RES 265
HTH_LacI cd01392
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ...
 15-66 2.37e-20

Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; HTH-DNA binding domain of the LacI (lactose operon repressor) family of bacterial transcriptional regulators and their putative homologs found in plants. The LacI family has more than 500 members distributed among almost all bacterial species. The monomeric proteins of the LacI family contain common structural features that include a small DNA-binding domain with a helix-turn-helix motif in the N-terminus, a regulatory ligand-binding domain which exhibits the type I periplasmic binding protein fold in the C-terminus for oligomerization and for effector binding, and an approximately 18-amino acid linker connecting these two functional domains. In LacI-like transcriptional regulators, the ligands are monosaccharides including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars, with a few exceptions. When the C-terminal domain of the LacI family repressor binds its ligand, it undergoes a conformational change which affects the DNA-binding affinity of the repressor. In Escherichia coli, LacI represses transcription by binding with high affinity to the lac operon at a specific operator DNA sequence until it interacts with the physiological inducer allolactose or a non-degradable analog IPTG (isopropyl-beta-D-thiogalactopyranoside). Induction of the repressor lowers its affinity for the operator sequence, thereby allowing transcription of the lac operon structural genes (lacZ, lacY, and LacA). The lac repressor occurs as a tetramer made up of two functional dimers. Thus, two DNA binding domains of a dimer are required to bind the inverted repeat sequences of the operator DNA binding sites.


Pssm-ID: 143331 [Multi-domain]  Cd Length: 52  Bit Score: 82.84  E-value: 2.37e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1179834730  15 ADVAKMTGVSTMTVSRVLREPEKVSPQVREKIEAAISELGYVPNLAASNLAS 66
Cdd:cd01392     1 KDIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
PBP1_AglR_RafR-like cd06292
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ...
 85-338 6.25e-20

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: 88.09  E-value: 6.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  85 AEFSEALYQVLKPKGYNVILAEdHYTAADESKLIEMML-SYNPAAMVMYDFDCSEESNNLLLKSTIPVVQVGATLATPIG 163
Cdd:cd06292    19 DEFLAALGHAAAARGYDVLLFT-ASGDEDEIDYYRDLVrSRRVDGFVLASTRHDDPRVRYLHEAGVPFVAFGRANPDLDF 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 164 INIGTNYGLAIKQLINALALKGYRNIALLCAAHEHHIVQQILSGWHSSILSLNQSPHR--VVSSSLppTVQTGQRLLPDi 241
Cdd:cd06292    98 PWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPEGSVPSDDRLAGYRAALEEAGLPFDPglVVEGEN--TEEGGYAAAAR- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 242 LLNWPE-LDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKHILAALQGD 320
Cdd:cd06292   175 LLDLGPpPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTVRQPIDEIGRAVVDLLLAAIEGN 254

                         250
                  ....*....|....*....
gi 1179834730 321 DVE-ESVMLPSTLMLRGST 338
Cdd:cd06292   255 PSEpREILLQPELVVRESS 273
PBP1_LacI-like cd06279
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ...
 78-337 2.32e-19

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: 86.49  E-value: 2.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  78 SMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEmmlsynpaAMVmyD----FDCSEESNNL--LLKSTIPV 151
Cdd:cd06279    13 AFSDPVAAQFLRGVAEVCEEEGLGLLLLPATDEGSAAAAVRN--------AAV--DgfivYGLSDDDPAVaaLRRRGLPL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 152 VQVGATLATPIG-INIgTNYGlAIKQLINALALKGYRNIALLC-----------------AAHEHHIVQQILSGWHSSI- 212
Cdd:cd06279    83 VVVDGPAPPGIPsVGI-DDRA-AARAAARHLLDLGHRRIAILSlrldrgrergpvsaerlAAATNSVARERLAGYRDALe 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 213 ---LSLNQSPhrVVSSSlPPTVQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQ 289
Cdd:cd06279   161 eagLDLDDVP--VVEAP-GNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRVPEDLSVTGFDDIPEAA 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1179834730 290 ICSPSLTTVAIPYRPMGTQTGkHILAALQGDDVEESVMLPSTLMLRGS 337
Cdd:cd06279   238 AADPGLTTVRQPAVEKGRAAA-RLLLGLLPGAPPRPVILPTELVVRAS 284
PBP1_GalR cd01544
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ...
 89-337 2.40e-19

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: 86.04  E-value: 2.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  89 EALYQVLKPKGYNVILaedHYTAADESKLIEMMLSynpAAMVMYDFdcSEESNNLLLKSTIPVVQVGATLAtPIGIN-IG 167
Cdd:cd01544    24 LGIEKEAKKLGYEIKT---IFRDDEDLESLLEKVD---GIIAIGKF--SKEEIEKLKKLNPNIVFVDSNPD-PDGFDsVV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 168 TNYGLAIKQLINALALKGYRNIALLCAAHEHHIVQQI-----LSGWHSSILSLN-QSPHRVVSSSLppTVQTGQRLLPDI 241
Cdd:cd01544    95 PDFEQAVRQALDYLIELGHRRIGFIGGKEYTSDDGEEiedprLRAFREYMKEKGlYNEEYIYIGEF--SVESGYEAMKEL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 242 LLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKHILAALQGD- 320
Cdd:cd01544   173 LKEGDLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTPPLTTVHIPTEEMGRTAVRLLLERINGGr 252

                         250
                  ....*....|....*..
gi 1179834730 321 DVEESVMLPSTLMLRGS 337
Cdd:cd01544   253 TIPKKVLLPTKLIERES 269
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
 74-333 2.46e-19

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: 86.04  E-value: 2.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  74 MVVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIPVVQ 153
Cdd:cd19977     4 LIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNEDLIEKLVKSGIPVVF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 154 VGATLAtpiGINIGT----NYGlAIKQLINALALKGYRNIALLCAAHEHHIVQQILSGWHSSILSLN--QSPHRVVSSSL 227
Cdd:cd19977    84 VDRYIP---GLDVDTvvvdNFK-GAYQATEHLIELGHKRIAFITYPLELSTRQERLEGYKAALADHGlpVDEELIKHVDR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 228 PPTVQtgqRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGT 307
Cdd:cd19977   160 QDDVR---KAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQPTYEIGR 236

                         250       260
                  ....*....|....*....|....*...
gi 1179834730 308 QTGKHILAALQGDDVEES--VMLPSTLM 333
Cdd:cd19977   237 KAAELLLDRIENKPKGPPrqIVLPTELI 264
PBP1_RegR_EndR_KdgR-like cd06283
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ...
 71-335 1.25e-18

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: 84.14  E-value: 1.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  71 LVTMVVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIP 150
Cdd:cd06283     1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPTGNNNDAYLELAQKGLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 151 VVQVGATLATPIGINIGTNYGLAIKQLINALALKGYRNIALLCAAHEHHIVQQI-LSGWHsSILSLNQSPHRVVssslpp 229
Cdd:cd06283    81 VVLVDRQIEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPIKGISTRRErLQGFL-DALARYNIEGDVY------ 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 230 TV-QTGQRLLPDILLNW-----PELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYR 303
Cdd:cd06283   154 VIeIEDTEDLQQALAAFlsqhdGGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQPTY 233

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1179834730 304 PMGTQTGKHILAALQGDDVEESVM-LPSTLMLR 335
Cdd:cd06283   234 EIGKAAAEILLERIEGDSGEPKEIeLPSELIIR 266
PBP1_LacI-like cd06290
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 75-337 8.20e-18

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: 81.89  E-value: 8.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  75 VVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNnLLLKSTIPVVQV 154
Cdd:cd06290     5 LVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEELL-KLLAEGIPVVLV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 155 GATLATPIGINIGT-NYG---LAIKQLINalalKGYRNIALLCAAHEHHIVQQILSGWHSSILS--LNQSPHRVVSSSLp 228
Cdd:cd06290    84 DRELEGLNLPVVNVdNEQggyNATNHLID----LGHRRIVHISGPEDHPDAQERYAGYRRALEDagLEVDPRLIVEGDF- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 229 pTVQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQ 308
Cdd:cd06290   159 -TEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYEMGKT 237

                         250       260       270
                  ....*....|....*....|....*....|
gi 1179834730 309 TGKHILAALQGD-DVEESVMLPSTLMLRGS 337
Cdd:cd06290   238 AAEILLELIEGKgRPPRRIILPTELVIRES 267
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 71-337 9.84e-18

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: 81.55  E-value: 9.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  71 LVTMVVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIP 150
Cdd:cd06293     1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSHLARLRARGTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 151 VVQVGATLATPIGINIGTNYGLAIKQLINALALKGYRNIALLcaAHEHHIVQ--QILSGWHSSI--LSLNQSPHRVVSSS 226
Cdd:cd06293    81 VVLLDRPAPGPAGCSVSVDDVQGGALAVDHLLELGHRRIAFV--SGPLRTRQvaERLAGARAAVaeAGLDPDEVVRELSA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 227 LPPTVQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMG 306
Cdd:cd06293   159 PDANAELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQPSYELG 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1179834730 307 TQTGKHILAAL-QGDDVEESVMLPSTLMLRGS 337
Cdd:cd06293   239 RAAADLLLDEIeGPGHPHEHVVFQPELVVRSS 270
PBP1_CatR-like cd06296
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ...
 71-338 1.41e-17

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: 81.17  E-value: 1.41e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  71 LVTMVVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIP 150
Cdd:cd06296     1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQLRLLRSAGIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 151 VVQVGATLATPIGI-NIG-TNYG---LAIKQLinaLALkGYRNIALLCAAHEHHIVQQILSGWHSSI--LSLNQSPHRVV 223
Cdd:cd06296    81 FVLIDPVGEPDPDLpSVGaTNWAggrLATEHL---LDL-GHRRIAVITGPPRSVSGRARLAGYRAALaeAGIAVDPDLVR 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 224 SSSLPPtvQTGQRLLPDiLLNWPELDLLI-CTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPY 302
Cdd:cd06296   157 EGDFTY--EAGYRAARE-LLELPDPPTAVfAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVHQPL 233

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1179834730 303 RPMGTQTGKHILAALQGDDVEES-VMLPSTLMLRGST 338
Cdd:cd06296   234 REMGAVAVRLLLRLLEGGPPDARrIELATELVVRGST 270
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 72-338 1.54e-17

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: 81.12  E-value: 1.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  72 VTMVVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIPV 151
Cdd:cd06285     2 IGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQELAARGVPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 152 VQVGATLATPIGINIGT-NYG---LAIKQLinaLALkGYRNIALLCAAHEHHIVQQILSGWHSSILSLNQSPHRVVSSSL 227
Cdd:cd06285    82 VLVDRRIGDTALPSVTVdNELggrLATRHL---LEL-GHRRIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDERIVPG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 228 PPTVQTGQRLLPDiLLNWPELDLLI-CTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMG 306
Cdd:cd06285   158 GFTIEAGREAAYR-LLSRPERPTAVfAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEMG 236

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1179834730 307 TQTGKHILAALQGDDVE-ESVMLPSTLMLRGST 338
Cdd:cd06285   237 RRAAELLLQLIEGGGRPpRSITLPPELVVREST 269
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
 93-337 1.69e-17

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: 81.06  E-value: 1.69e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  93 QVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNL-----LLKSTIPVVQVGA---TLATP-IG 163
Cdd:cd01541    23 SVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEPTKSALPNPNLdlyeeLQKKGIPVVFINSyypELDAPsVS 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 164 INigtNYG---LAIKQLINalalKGYRNIALLC----------------AAHEHHI-VQQILSGWHSSIlSLNQSPHRvv 223
Cdd:cd01541   103 LD---DEKggyLATKHLID----LGHRRIAGIFksddlqgveryqgfikALREAGLpIDDDRILWYSTE-DLEDRFFA-- 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 224 ssslpptvqtgqRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYR 303
Cdd:cd01541   173 ------------EELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEPPLTSVVHPKE 240

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1179834730 304 PMGTQTGKHILAALQGDDVEESVMLPSTLMLRGS 337
Cdd:cd01541   241 ELGRKAAELLLRMIEEGRKPESVIFPPELIERES 274
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 71-337 2.57e-17

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: 80.27  E-value: 2.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  71 LVTMVVPSMSTPGCAEFSEALYQVLKPKGYNVIL--AEDHYTAADeskLIEMMLSYNPAAMVMYDFDCSEESNNLLLKST 148
Cdd:cd06278     1 LVGVVVGDLSNPFYAELLEELSRALQARGLRPLLfnVDDEDDVDD---ALRQLLQYRVDGVIVTSATLSSELAEECARRG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 149 IPVVQVGATLATPIGINIGTNYGLAIKQLINALALKGYRNIALLCAAHEHHIVQQILSGWHSSILSLNQSPHRVVSSSLp 228
Cdd:cd06278    78 IPVVLFNRVVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPEGTSTSRERERGFRAALAELGLPPPAVEAGDY- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 229 pTVQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGI-SVPAQLAIAGLgDgDIAQICSPS--LTTVAIPYRPM 305
Cdd:cd06278   157 -SYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAARQEGGlVVPEDISVVGF-D-DIPMAAWPSydLTTVRQPIEEM 233

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1179834730 306 GTQTGKHILAALQGDDVE-ESVMLPSTLMLRGS 337
Cdd:cd06278   234 AEAAVDLLLERIENPETPpERRVLPGELVERGS 266
PBP1_MalR-like cd06294
ligand-binding domain of maltose transcription regulator MalR which is a member of the ...
 87-333 5.56e-17

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: 79.55  E-value: 5.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  87 FSEALY---QVLKPKGYNVILAedhyTAADESKLIEMMLSYNPAAMV-----MYdfdcSEESN---NLLLKSTIPVVQVG 155
Cdd:cd06294    19 FSEVLRgisQVANENGYSLLLA----TGNTEEELLEEVKRMVRGRRVdgfilLY----SKEDDpliEYLKEEGFPFVVIG 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 156 ATLATPIGINIGTNYGLAIKQLINALALKGYRNIALLCAAHEHHIVQQILSGWHSSILSLN-QSPHRVV---SSSLPPtv 231
Cdd:cd06294    91 KPLDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVSIDRLQGYKQALKEAGlPLDDDYIlllDFSEED-- 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 232 qtGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAI-PYRpMGTQTG 310
Cdd:cd06294   169 --GYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSVDInPYE-LGREAA 245

                         250       260
                  ....*....|....*....|....
gi 1179834730 311 KHILAALQGDDVE-ESVMLPSTLM 333
Cdd:cd06294   246 KLLINLLEGPESLpKNVIVPHELI 269
PBP1_SalR cd01545
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ...
 149-337 7.27e-17

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: 79.14  E-value: 7.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 149 IPVVQVGATLATPIGINIGTNYGLAIKQLINALALKGYRNIALLCAAHEHHIVQQILSGWHSSI--LSLNQSPHRVVSS- 225
Cdd:cd01545    81 IPYVRIAPGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGPPDHGASAERLEGFRDALaeAGLPLDPDLVVQGd 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 226 -SLPPTVQTGQRLLpdillnwpelDL------LICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTV 298
Cdd:cd01545   161 fTFESGLEAAEALL----------DLpdrptaIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTTV 230

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1179834730 299 AIPYRPMGTQTGKHILAALQG-DDVEESVMLPSTLMLRGS 337
Cdd:cd01545   231 RQPIAEMARRAVELLIAAIRGaPAGPERETLPHELVIRES 270
PBP1_LacI-like cd06282
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 75-337 8.55e-17

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: 78.86  E-value: 8.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  75 VVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDfdCSEESN---NLLLKSTIPV 151
Cdd:cd06282     5 LIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTV--GDAQGSealELLEEEGVPY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 152 VQVGATLATPIGINIGTNYGLAIKQLINALALKGYRNIALL-----------------CAAHEHHIVQqilsgwHSSI-- 212
Cdd:cd06282    83 VLLFNQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVagdfsasdrarlryqgyRDALKEAGLK------PIPIve 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 213 --LSLNQSP---HRVVSSSLPPTVqtgqrllpdillnwpeldlLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDI 287
Cdd:cd06282   157 vdFPTNGLEealTSLLSGPNPPTA-------------------LFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAI 217

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1179834730 288 AQICSPSLTTVAIPYRPMGTQTGKHILAALQGDDVEESVMLPSTLMLRGS 337
Cdd:cd06282   218 GELLTPTLATVVQPSRDMGRAAADLLLAEIEGESPPTSIRLPHHLREGGS 267
PBP1_CcpA cd06298
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ...
 72-337 1.49e-16

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: 78.49  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  72 VTMVVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIPV 151
Cdd:cd06298     2 VGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMGDELTEEIREEFKRSPVPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 152 VQVGATLATP-IG-INIgtNYGLAIKQLINALALKGYRNIALLCAAHEHHIVQQI-LSGWHSSILS--LNQSPHRVVSSS 226
Cdd:cd06298    82 VLAGTVDSDHeIPsVNI--DYEQAAYDATKSLIDKGHKKIAFVSGPLKEYINNDKkLQGYKRALEEagLEFNEPLIFEGD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 227 lpPTVQTGQRLLPdILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMG 306
Cdd:cd06298   160 --YDYDSGYELYE-ELLESGEPDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPLYDIG 236

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1179834730 307 TQTGKHILAALQGDDVEES-VMLPSTLMLRGS 337
Cdd:cd06298   237 AVAMRLLTKLMNKEEVEETiVKLPHSIIWRQS 268
LacI pfam00356
Bacterial regulatory proteins, lacI family;
13-58 1.77e-16

Bacterial regulatory proteins, lacI family;


Pssm-ID: 306791 [Multi-domain]  Cd Length: 46  Bit Score: 72.28  E-value: 1.77e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1179834730  13 TLADVAKMTGVSTMTVSRVLREPEKVSPQVREKIEAAISELGYVPN 58
Cdd:pfam00356   1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
PBP1_PurR cd06275
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ...
 74-337 3.37e-16

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: 77.30  E-value: 3.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  74 MVVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYN-------PAAMVMYDFDCSEESNNlllk 146
Cdd:cd06275     4 LLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRvdglllmCSEMTDDDAELLAALRS---- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 147 stIPVVQVGATLATPIGINIGTN-----YgLAIKQLINalalKGYRNIALLCAAHEHHIVQQILSGWHSSI--LSLNQSP 219
Cdd:cd06275    80 --IPVVVLDREIAGDNADAVLDDsfqggY-LATRHLIE----LGHRRIGCITGPLEHSVSRERLAGFRRALaeAGIEVPP 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 220 HRVVSSSLppTVQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVA 299
Cdd:cd06275   153 SWIVEGDF--EPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIH 230

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1179834730 300 IPYRPMGTQTGKHILAALQG-DDVEESVMLPSTLMLRGS 337
Cdd:cd06275   231 QPKDELGELAVELLLDRIENkREEPQSIVLEPELIERES 269
PBP1_CelR cd06295
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ...
 185-337 4.27e-14

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: 71.51  E-value: 4.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 185 GYRNIALLCAAhEHHIVQQILSGWhssILSLNQSPHRVVSSSLPP---TVQTGQRLLPDILLNWPELDLLICTSDELASG 261
Cdd:cd06295   123 GRRRIAFLGDP-PHPEVADRLQGY---RDALAEAGLEADPSLLLScdfTEESGYAAMRALLDSGTAFDAIFAASDLIAMG 198

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1179834730 262 AIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKHILAALQGDDVeESVMLPSTLMLRGS 337
Cdd:cd06295   199 AIRALRERGISVPGDVAVVGYDDIPLAAYFRPPLTTVRQDLALAGRLLVEKLLALIAGEPV-TSSMLPVELVVRES 273
PBP1_LacI-like cd06281
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 72-337 2.51e-13

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: 69.19  E-value: 2.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  72 VTMVVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMY-DFDCSEESNNLLLKSTIP 150
Cdd:cd06281     2 VGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILTpGDEDDPELAAALARLDIP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 151 VVQVGATLATPIGInIGTNYGLAIKQLINALALKGYRNIALLCAAHEHHIVQQILSGWHSSILSLNQSPHRVVSSSLPPT 230
Cdd:cd06281    82 VVLIDRDLPGDIDS-VLVDHRSGVRQATEYLLSLGHRRIALLTGGPDIRPGRERIAGFKAAFAAAGLPPDPDLVRLGSFS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 231 VQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTG 310
Cdd:cd06281   161 ADSGFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDLDAVGRAAA 240

                         250       260
                  ....*....|....*....|....*....
gi 1179834730 311 KHILAALQGDDVE--ESVMLPSTLMLRGS 337
Cdd:cd06281   241 ELLLDRIEGPPAGppRRIVVPTELILRDS 269
PBP1_LacI-like cd19974
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 89-337 4.72e-11

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: 62.57  E-value: 4.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  89 EALYQVLKPKGYNVILAEDhyTAADESKLIemmlsyNPAAMVMYDFD-------CSEESNNLLLKSTIPVVQVGA-TLAT 160
Cdd:cd19974    22 QGIEKELSELGYNLVLEII--SDEDEEELN------LPSIISEEKVDgiiilgeISKEYLEKLKELGIPVVLVDHyDEEL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 161 PIGINIGTNYgLAIKQLINALALKGYRNIALLCAAHEHHIVQQILSGWHSSI----LSLNQSPHRVvssslpPTVQTGQR 236
Cdd:cd19974    94 NADSVLSDNY-YGAYKLTSYLIEKGHKKIGFVGDINYTSSFMDRYLGYRKALleagLPPEKEEWLL------EDRDDGYG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 237 LLPDILL----NWPelDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKH 312
Cdd:cd19974   167 LTEEIELplklMLP--TAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLTTVEVDKEAMGRRAVEQ 244

                         250       260
                  ....*....|....*....|....*.
gi 1179834730 313 ILAALQG-DDVEESVMLPSTLMLRGS 337
Cdd:cd19974   245 LLWRIENpDRPFEKILVSGKLIERDS 270
PBP1_LacI-like cd06299
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ...
 75-337 8.98e-11

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: 61.53  E-value: 8.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  75 VVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIPVVQV 154
Cdd:cd06299     5 LVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGENSEGLQALIAQGLPVVFV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 155 GATLATPIGINIGT--NYGlAIKQLINALALKGYRNIALLCAAHEHHIVQQILSGWHSSILSLNQSPHRVVSSSLPPTVQ 232
Cdd:cd06299    85 DREVEGLGGVPVVTsdNRP-GAREAVEYLVSLGHRRIGYISGPLSTSTGRERLAAFRAALTAAGIPIDEELVAFGDFRQD 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 233 TGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKH 312
Cdd:cd06299   164 SGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVERIGRRAVEL 243

                         250       260
                  ....*....|....*....|....*
gi 1179834730 313 ILAALQGDDVEESVMLPSTLMLRGS 337
Cdd:cd06299   244 LLALIENGGRATSIRVPTELIPRES 268
PBP1_LacI-like cd06277
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 98-337 1.30e-10

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: 61.10  E-value: 1.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  98 KGYNVILAEDHYTAaDESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIPVVQVGA----TLATPIGINigtNYG-- 171
Cdd:cd06277    35 YGYNLLISSVDIGD-DFDEILKELTDDQSSGIILLGTELEEKQIKLFQDVSIPVVVVDNyfedLNFDCVVID---NEDga 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 172 -LAIKQLINalalKGYRNIALLCAAHEHHIVQQILSGWHSSI----LSLNQSPHRVVSSSlPPTVQTGQRLLPDILLNWP 246
Cdd:cd06277   111 yEAVKYLVE----LGHTRIGYLASSYRIKNFEERRRGFRKAMrelgLSEDPEPEFVVSVG-PEGAYKDMKALLDTGPKLP 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 247 ELdlLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKHILAALQGDDVEESV 326
Cdd:cd06277   186 TA--FFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRRLIEKIKDPDGGTLK 263

                         250
                  ....*....|..
gi 1179834730 327 MLPST-LMLRGS 337
Cdd:cd06277   264 ILVSTkLVERGS 275
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 48-332 2.68e-10

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: 60.32  E-value: 2.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  48 AAISELGYVPNLAASNLASSTSRLVTMVVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPA 127
Cdd:COG1879    12 LALALAACGSAAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVD 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 128 AMVMYDFDcSEESNNLLLKST---IPVVQVGATLATPIGI-NIGT-NYG---LAIKQLINALALKGyrNIALLCAAHEHH 199
Cdd:COG1879    92 AIIVSPVD-PDALAPALKKAKaagIPVVTVDSDVDGSDRVaYVGSdNYAagrLAAEYLAKALGGKG--KVAILTGSPGAP 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 200 IVQQILSGWHSSIlslNQSPHRVVSSSLPP--TVQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQL 277
Cdd:COG1879   169 AANERTDGFKEAL---KEYPGIKVVAEQYAdwDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRKGDVKV 245

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1179834730 278 --------AIAGLGDGDIAqicspslTTVAIPYRPMGTQTGKHILAALQGDDVEESVMLPSTL 332
Cdd:COG1879   246 vgfdgspeALQAIKDGTID-------ATVAQDPYLQGYLAVDAALKLLKGKEVPKEILTPPVL 301
PBP1_CcpA_TTHA0807 cd06297
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ...
 71-320 6.26e-10

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: 59.02  E-value: 6.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  71 LVTMVVPSMSTPGCAEFSEALYQVLKPKGYNVILaedhYTAADESKLIEMM----LSYNPAAMVMYDFDCSEESNNLLLK 146
Cdd:cd06297     1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAI----FPLLSEYRLEKYLrnstLAYQCDGLVMASLDLTELFEEVIVP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 147 STIPVVQVGATLATPIGINIGTNYGLAIKQliNALALKGYRNIALLCAAHEHHIVQQILSGWHSSIL-SLNQ-----SPH 220
Cdd:cd06297    77 TEKPVVLIDANSMGYDCVYVDNVKGGFMAT--EYLAGLGEREYVFFGIEEDTVFTETVFREREQGFLeALNKagrpiSSS 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 221 RVVSSSLppTVQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQicSPSLTTVAI 300
Cdd:cd06297   155 RMFRIDN--SSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAA--SPGLTTVRQ 230

                         250       260
                  ....*....|....*....|
gi 1179834730 301 PYRPMGTQTGKHILAALQGD 320
Cdd:cd06297   231 PVEEMGEAAAKLLLKRLNEY 250
PBP1_AglR-like cd20010
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ...
 142-332 6.76e-10

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: 59.10  E-value: 6.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 142 NLLLKSTIPVVQVGATLATP----IGINigtNYGlAIKQLINALALKGYRNIALLCAAHEHHIVQQILSGWHSSI--LSL 215
Cdd:cd20010    76 AYLLERGIPFVVHGRSESGApyawVDID---NEG-AFRRATRRLLALGHRRIALLNGPEELNFAHQRRDGYRAALaeAGL 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 216 NQSPHRVVSSslPPTVQTGQRLLpDILLNWPEL-DLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDG-DIAQICSP 293
Cdd:cd20010   152 PVDPALVREG--PLTEEGGYQAA-RRLLALPPPpTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLlPALEYFSP 228

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1179834730 294 SLTTVAIPYRPMGTQTGKHILAALQGDDVEE-SVMLPSTL 332
Cdd:cd20010   229 PLTTTRSSLRDAGRRLAEMLLALIDGEPAAElQELWPPEL 268
PRK11303 PRK11303
catabolite repressor/activator;
13-284 1.23e-09

catabolite repressor/activator;


Pssm-ID: 236897 [Multi-domain]  Cd Length: 328  Bit Score: 58.74  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  13 TLADVAKMTGVSTMTVSRVLR---EPEKVSPQVREKIEAAISELGYVPNLAASNLASSTSRLVTMVVPSMSTPGCAEFSE 89
Cdd:PRK11303    2 KLDEIARLAGVSRTTASYVINgkaKQYRVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSYARIAK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  90 ALYQVLKPKGYNVILA--EDHytAADESKLIEMMLSYNPAAMVMYdfDCSEESNNLLLK---STIPVVQVGATLATPIGI 164
Cdd:PRK11303   82 YLERQARQRGYQLLIAcsDDQ--PDNEMRCAEHLLQRQVDALIVS--TSLPPEHPFYQRlqnDGLPIIALDRALDREHFT 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 165 NIGTNYGLAIKQLINALALKGYRNIALLCAAHEHHIVQQILSGWHSSILSLNQSPHRVVSSSLppTVQTGQRLLPDILLN 244
Cdd:PRK11303  158 SVVSDDQDDAEMLAESLLKFPAESILLLGALPELSVSFEREQGFRQALKDDPREVHYLYANSF--EREAGAQLFEKWLET 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1179834730 245 WPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGD 284
Cdd:PRK11303  236 HPMPDALFTTSYTLLQGVLDVLLERPGELPSDLAIATFGD 275
PRK10339 PRK10339
DNA-binding transcriptional repressor EbgR; Provisional
 244-338 3.92e-09

DNA-binding transcriptional repressor EbgR; Provisional


Pssm-ID: 182389 [Multi-domain]  Cd Length: 327  Bit Score: 57.08  E-value: 3.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 244 NWPELdlLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQtGKHILA--ALQGDD 321
Cdd:PRK10339  233 DYPKA--LFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQ-GVNLLYekARDGRA 309

                          90
                  ....*....|....*..
gi 1179834730 322 VEESVMLPSTLMLRGST 338
Cdd:PRK10339  310 LPLLVFVPSKLKLRGTT 326
PBP1_XylR cd01543
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ...
 115-338 5.93e-09

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: 56.06  E-value: 5.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 115 SKLIEMMLSYNPAAMVMYDFDCSEESnnLLLKSTIPVVQVGATLATPIGINIGTNY----GLAIKQLINalalKGYRNIA 190
Cdd:cd01543    40 EELLDLLKGWKGDGIIARLDDPELAE--ALRRLGIPVVNVSGSRPEPGFPRVTTDNeaigRMAAEHLLE----RGFRHFA 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 191 LlCAAHEHHIVQQILSGWHSSILSLNQSPH--RVVSSSLPPTVQTGQRLLPDILLNWPeldL---LICTSDELASGAIAA 265
Cdd:cd01543   114 F-CGFRNAAWSRERGEGFREALREAGYECHvyESPPSGSSRSWEEEREELADWLKSLP---KpvgIFACNDDRARQVLEA 189

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1179834730 266 CHKKGISVPAQLAIAGLGDGD-IAQICSPSLTTVAIPYRPMGTQTGKHILAALQGDDVEESVML--PSTLMLRGST 338
Cdd:cd01543   190 CREAGIRVPEEVAVLGVDNDElICELSSPPLSSIALDAEQIGYEAAELLDRLMRGERVPPEPILipPLGVVTRQST 265
PBP1_hexuronate_repressor-like cd06272
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ...
 87-327 6.53e-08

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: 53.15  E-value: 6.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  87 FSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKSTIPVVQVGATLATPIGINI 166
Cdd:cd06272    18 LLSGINEAISKQGYNINLSICPYKVGHLCTAKGLFSENRFDGVIVFGISDSDIEYLNKNKPKIPIVLYNRESPKYSTVNV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 167 gtNYGLAIKQLINALALKGYRNIALL-------------------CAAHEHHIVQQILSGWHSSILSLNQSPHRVVSSSL 227
Cdd:cd06272    98 --DNEKAGRLAVLLLIQKGHKSIAYIgnpnsnrnqtlrgkgfietCEKHGIHLSDSIIDSRGLSIEGGDNAAKKLLKKKT 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 228 PPTVqtgqrllpdillnwpeldlLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGT 307
Cdd:cd06272   176 LPKA-------------------IFCNSDDIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLTVVGVPIEKIAE 236

                         250       260
                  ....*....|....*....|
gi 1179834730 308 QTGKHILAALQGDDVEESVM 327
Cdd:cd06272   237 ESLRLILKLIEGRENEIQQL 256
PBP1_RafR-like cd20009
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ...
 179-324 9.49e-08

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: 52.54  E-value: 9.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 179 NALALKGYRNIALLCAAHEHHIVQQILSGWHSSI--LSLNQSPHRVVSSSLPPtvQTGQRLLPDILLNWPELDLLICTSD 256
Cdd:cd20009   111 RRLAARGRRRIALVAPPRELTYAQHRLRGFRRALaeAGLEVEPLLIVTLDSSA--EAIRAAARRLLRQPPRPDGIICASE 188

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1179834730 257 ELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKHILAALQGDDVEE 324
Cdd:cd20009   189 IAALGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPIDTLYEDIEEAGRFLAEALLRRIEGEPAEP 256
PBP1_LacI-like cd06287
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 241-337 6.95e-07

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: 380510 [Multi-domain]  Cd Length: 268  Bit Score: 49.73  E-value: 6.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 241 ILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKHILAALQGD 320
Cdd:cd06287   172 LLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPEDLMVVTRYDGIRARTADPPLTAVDLHLDRVARTAIDLLFASLSGE 251

                          90
                  ....*....|....*..
gi 1179834730 321 DVEESVMLPSTLMLRGS 337
Cdd:cd06287   252 ERSVEVGPAPELVVRAS 268
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
 75-314 4.53e-06

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: 47.51  E-value: 4.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  75 VVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDCSEESNNLLLKST-IPVVQ 153
Cdd:pfam00532   7 LVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPAPSGDDITAKAEGYgIPVIA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 154 VGATLATPIGINIGTN-----YGLAIKQLINAlalkGYRNIALLCAAHEHHI-----VQQILSGWHSSILSLNQSPHRVV 223
Cdd:pfam00532  87 ADDAFDNPDGVPCVMPddtqaGYESTQYLIAE----GHKRPIAVMAGPASALtarerVQGFMAALAAAGREVKIYHVATG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 224 SSSLPptvqTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKG---------ISVPAQLAIAGLGDGDIAQICSPS 294
Cdd:pfam00532 163 DNDIP----DAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGrvkipdivgIGINSVVGFDGLSKAQDTGLYLSP 238

                         250       260
                  ....*....|....*....|
gi 1179834730 295 LTTVAIPYRPMGTQTGKHIL 314
Cdd:pfam00532 239 LTVIQLPRQLLGIKASDMVY 258
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
 72-332 1.35e-05

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: 46.02  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  72 VTMVVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYDFDcSEESNNLLLKST--- 148
Cdd:cd01536     2 IGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVD-SEALVPAVKKANaag 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 149 IPVVQVGATLATPIGI--NIGT-NYGLAIKQ---LINALALKGyrNIALLCAAHEHHIVQQILSGWHSSilsLNQSPHRV 222
Cdd:cd01536    81 IPVVAVDTDIDGGGDVvaFVGTdNYEAGKLAgeyLAEALGGKG--KVAILEGPPGSSTAIDRTKGFKEA---LKKYPDIE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 223 VSSSLPP--TVQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISvpAQLAIAGLgDGD---IAQICSPSLT- 296
Cdd:cd01536   156 IVAEQPAnwDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRT--GDIKIVGV-DGTpeaLKAIKDGELDa 232

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1179834730 297 TVAIPYRPMGTQTGKHILAALQGDDVEESVMLPSTL 332
Cdd:cd01536   233 TVAQDPYLQGYLAVEAAVKLLNGEKVPKEILTPVTL 268
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
 85-332 2.01e-05

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: 45.31  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  85 AEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMydfDCSEESNNLLLK----STIPVV--QVGATL 158
Cdd:cd01537    15 SVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAI---NLVDPAAAGVAEkargQNVPVVffDKEPSR 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 159 ATPIGiNIGTNYGLAIKQLINALALKGYRNIALLCAAHEHHIVQQILSGWHSSilsLNQSPHRVVSSSLPP---TVQTGQ 235
Cdd:cd01537    92 YDKAY-YVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHPDAEARLAGVIKE---LNDKGIKTEQLQLDTgdwDTASGK 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 236 RLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDGDIAQICSPSLTTVAIPYRPMGTQTGKHILA 315
Cdd:cd01537   168 DKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDANNLGKTTFDLLLN 247

                         250
                  ....*....|....*...
gi 1179834730 316 ALQ-GDDVEESVMLPSTL 332
Cdd:cd01537   248 LADnWKIDNKVVRVPYVL 265
PBP1_FruR cd06274
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ...
 71-284 2.48e-04

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: 42.19  E-value: 2.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730  71 LVTMVVPSMSTPGCAEFSEALYQVLKPKGYNVILAEDHYTAADESKLIEMMLSYNPAAMVMYdfDCSEESNN--LLLKST 148
Cdd:cd06274     1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVA--PSTPPDDIyyLCQAAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 149 IPVVQV----GATLATPIginIGTNYGLAiKQLINALALKGYRNIALLCAAHEHHIVQQILSGWHSSILSLNQSPHRVVS 224
Cdd:cd06274    79 LPVVFLdrpfSGSDAPSV---VSDNRAGA-RALTEKLLAAGPGEIYFLGGRPELPSTAERIRGFRAALAEAGITEGDDWI 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1179834730 225 SSLPPTVQTGQRLLPDILLNWPEL-DLLICTSDELASGAIAACHKKGISVPAQLAIAGLGD 284
Cdd:cd06274   155 LAEGYDRESGYQLMAELLARLGGLpQALFTSSLTLLEGVLRFLRERLGAIPSDLVLGTFDD 215
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 240-333 2.46e-03

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: 39.18  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 240 DILLNWPELDLLICTSDELASGAIAACHKKG----ISV-------PAQLAIAGLGD--GDIAQicspslttvaIPYRpMG 306
Cdd:cd06322   174 DMLQANPDLDGIFAIGDPAALGALTAIESAGkedkIKVigfdgnpEAIKAIAKGGKikADIAQ----------QPDK-IG 242

                          90       100
                  ....*....|....*....|....*..
gi 1179834730 307 TQTGKHILAALQGDDVEESVMLPSTLM 333
Cdd:cd06322   243 QETVEAIVKYLAGETVEKEILIPPKLY 269
PBP1_AglR_RafR-like cd06271
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ...
 229-324 3.62e-03

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: 38.56  E-value: 3.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1179834730 229 PTVQTGQRLLPDILLNWPELDLLICTSDELASGAIAACHKKGISVPAQLAIAGLGDG-DIAQICSPSLTTVAIPYRPMGT 307
Cdd:cd06271   158 TTLEAGRAAAQRLLALSPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSApFLGAMITPPLTTVHAPIAEAGR 237

                          90
                  ....*....|....*..
gi 1179834730 308 QTGKHILAALQGDDVEE 324
Cdd:cd06271   238 ELAKALLARIDGEDPET 254
 
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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