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Conserved domains on  [gi|1370811475|gb|AVR17932|]
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LacI family DNA-binding transcriptional regulator [Burkholderia vietnamiensis]

Protein Classification

LacI family DNA-binding transcriptional regulator( domain architecture ID 11265709)

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)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP1_LacI-like cd06273
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 81-347 7.30e-105

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: 308.67  E-value: 7.30e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPYV 160
Cdd:cd06273     3 GAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVGSDHDPELFELLEQRQVPYV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 161 VTYAYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIMQPSADNDRVQARLRGIHETLAARGLAVRPVHQHEGPATI 240
Cdd:cd06273    83 LTWSYDEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGNDRARARLAGIRDALAERGLELPEERVVEAPYSI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 241 AFGRASLRTIADSGPtRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAA 320
Cdd:cd06273   163 EEGREALRRLLARPP-RPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPAREIGELAA 241

                         250       260
                  ....*....|....*....|....*..
gi 1370811475 321 RALLDALEHGAVGPGCAVLPELRVRES 347
Cdd:cd06273   242 RYLLALLEGGPPPKSVELETELIVRES 268
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
24-89 1.86e-22

helix_turn _helix lactose operon repressor;


:

Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 89.18  E-value: 1.86e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370811475   24 DVAKLAGVSTATVSRVYNDPGKVSADVQQRVRDAARTLNWIPNAAGRALASTRTHITGAIIPTLDD 89
Cdd:smart00354   5 DVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
 
Name Accession Description Interval E-value
PBP1_LacI-like cd06273
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 81-347 7.30e-105

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: 308.67  E-value: 7.30e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPYV 160
Cdd:cd06273     3 GAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVGSDHDPELFELLEQRQVPYV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 161 VTYAYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIMQPSADNDRVQARLRGIHETLAARGLAVRPVHQHEGPATI 240
Cdd:cd06273    83 LTWSYDEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGNDRARARLAGIRDALAERGLELPEERVVEAPYSI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 241 AFGRASLRTIADSGPtRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAA 320
Cdd:cd06273   163 EEGREALRRLLARPP-RPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPAREIGELAA 241

                         250       260
                  ....*....|....*....|....*..
gi 1370811475 321 RALLDALEHGAVGPGCAVLPELRVRES 347
Cdd:cd06273   242 RYLLALLEGGPPPKSVELETELIVRES 268
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
24-351 2.93e-98

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 294.41  E-value: 2.93e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  24 DVAKLAGVSTATVSRVYNDPGKVSADVQQRVRDAARTLNWIPNAAGRALASTRTHITGAIIPTLDDQVFASQVAGMQAVM 103
Cdd:COG1609     8 DVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLRGIEEAA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 104 AEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPYVVTYAYRDDSPHCCIGFDNRAAFA 183
Cdd:COG1609    88 RERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRPLPDPGVPSVGVDNRAGAR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 184 RLTTHLLDLGHRDFAIIMQPsADNDRVQARLRGIHETLAARGLAVRPVHQHEGPATIAFGRASLRTIADSGPtRPTAVIC 263
Cdd:COG1609   168 LATEHLIELGHRRIAFIGGP-ADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGP-RPTAIFC 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 264 GNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALLDALEHGAVGPGCAVLP-EL 342
Cdd:COG1609   246 ANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERVLLPpEL 325


                  ....*....
gi 1370811475 343 RVRESAAPP 351
Cdd:COG1609   326 VVRESTAPA 334
PRK10703 PRK10703
HTH-type transcriptional repressor PurR;
24-349 7.85e-40

HTH-type transcriptional repressor PurR;


Pssm-ID: 236739 [Multi-domain]  Cd Length: 341  Bit Score: 143.71  E-value: 7.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  24 DVAKLAGVSTATVSRVYNDPGKVSADVQQRVRDAARTLNWIPNAAGRALASTRTHITGAIIPTLDDQVFASQVAGMQAVM 103
Cdd:PRK10703    6 DVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEAVEKNC 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 104 AEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHR-VPYVVTYAYRDDSPHCCIGFDNRAAF 182
Cdd:PRK10703   86 YQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLLAMLEEYRhIPMVVMDWGEAKADFTDAIIDNAFEG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 183 ARLTT-HLLDLGHRDFAIIMQPSADNDRVQaRLRGIHETLAARGLAVRPVHQHEGPATIAFGRASLRTIAdSGPTRPTAV 261
Cdd:PRK10703  166 GYLAGrYLIERGHRDIGVIPGPLERNTGAG-RLAGFMKAMEEANIKVPEEWIVQGDFEPESGYEAMQQIL-SQKHRPTAV 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 262 ICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALLDALEHGAVGPGC-AVLP 340
Cdd:PRK10703  244 FCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRIVNKREEPQTiEVHP 323


                  ....*....
gi 1370811475 341 ELRVRESAA 349
Cdd:PRK10703  324 RLVERRSVA 332
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
 188-347 3.23e-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://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433159 [Multi-domain]  Cd Length: 160  Bit Score: 94.33  E-value: 3.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 188 HLLDLGHRDFAIIMQPSADNDRV-QARLRGIHETLAARGLAVRPVhqhEGPATIAFGRASLRTIADSGPTRPTAVICGND 266
Cdd:pfam13377   1 HLAELGHRRIALIGPEGDRDDPYsDLRERGFREAARELGLDVEPT---LYAGDDEAEAAAARERLRWLGALPTAVFVAND 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 267 ALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALLDALEHGAVGPGCAVLP-ELRVR 345
Cdd:pfam13377  78 EVALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPpELVER 157


                  ..
gi 1370811475 346 ES 347
Cdd:pfam13377 158 ES 159
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
24-89 1.86e-22

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 89.18  E-value: 1.86e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370811475   24 DVAKLAGVSTATVSRVYNDPGKVSADVQQRVRDAARTLNWIPNAAGRALASTRTHITGAIIPTLDD 89
Cdd:smart00354   5 DVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
HTH_LacI cd01392
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ...
 24-74 5.18e-17

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: 73.98  E-value: 5.18e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370811475  24 DVAKLAGVSTATVSRVYNDPGKVSADVQQRVRDAARTLNWIPNAAGRALAS 74
Cdd:cd01392     2 DIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
LacI pfam00356
Bacterial regulatory proteins, lacI family;
24-66 1.42e-13

Bacterial regulatory proteins, lacI family;


Pssm-ID: 306791 [Multi-domain]  Cd Length: 46  Bit Score: 64.20  E-value: 1.42e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370811475  24 DVAKLAGVSTATVSRVYNDPGKVSADVQQRVRDAARTLNWIPN 66
Cdd:pfam00356   4 DVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
 
Name Accession Description Interval E-value
PBP1_LacI-like cd06273
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 81-347 7.30e-105

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: 308.67  E-value: 7.30e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPYV 160
Cdd:cd06273     3 GAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVGSDHDPELFELLEQRQVPYV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 161 VTYAYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIMQPSADNDRVQARLRGIHETLAARGLAVRPVHQHEGPATI 240
Cdd:cd06273    83 LTWSYDEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGNDRARARLAGIRDALAERGLELPEERVVEAPYSI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 241 AFGRASLRTIADSGPtRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAA 320
Cdd:cd06273   163 EEGREALRRLLARPP-RPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPAREIGELAA 241

                         250       260
                  ....*....|....*....|....*..
gi 1370811475 321 RALLDALEHGAVGPGCAVLPELRVRES 347
Cdd:cd06273   242 RYLLALLEGGPPPKSVELETELIVRES 268
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
24-351 2.93e-98

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 294.41  E-value: 2.93e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  24 DVAKLAGVSTATVSRVYNDPGKVSADVQQRVRDAARTLNWIPNAAGRALASTRTHITGAIIPTLDDQVFASQVAGMQAVM 103
Cdd:COG1609     8 DVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLRGIEEAA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 104 AEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPYVVTYAYRDDSPHCCIGFDNRAAFA 183
Cdd:COG1609    88 RERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRPLPDPGVPSVGVDNRAGAR 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 184 RLTTHLLDLGHRDFAIIMQPsADNDRVQARLRGIHETLAARGLAVRPVHQHEGPATIAFGRASLRTIADSGPtRPTAVIC 263
Cdd:COG1609   168 LATEHLIELGHRRIAFIGGP-ADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGP-RPTAIFC 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 264 GNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALLDALEHGAVGPGCAVLP-EL 342
Cdd:COG1609   246 ANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERVLLPpEL 325


                  ....*....
gi 1370811475 343 RVRESAAPP 351
Cdd:COG1609   326 VVRESTAPA 334
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
 81-347 9.65e-64

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: 203.88  E-value: 9.65e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPYV 160
Cdd:cd01575     3 AVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEHTPATRKLLRAAGIPVV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 161 VTYAYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIMQPSADNDRVQARLRGIHETLAARGLAVRPVHQHEGPATI 240
Cdd:cd01575    83 ETWDLPDDPIDMAVGFSNFAAGRAMARHLIERGYRRIAFVGARLDGDSRARQRLEGFRDALAEAGLPLPLVLLVELPSSF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 241 AFGRASLRTIADSGPtRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAA 320
Cdd:cd01575   163 ALGREALAELLARHP-DLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVRVPRYEIGRKAA 241

                         250       260
                  ....*....|....*....|....*...
gi 1370811475 321 RALLDALEHGAVGPGCAVLP-ELRVRES 347
Cdd:cd01575   242 ELLLARLEGEEPEPRVVDLGfELVRRES 269
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
 81-340 6.56e-57

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: 185.80  E-value: 6.56e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPYV 160
Cdd:cd06267     3 GLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLAAGIPVV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 161 VTYAYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIMQPSaDNDRVQARLRGIHETLAARGLAVRPVHQHEGPATI 240
Cdd:cd06267    83 LIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPL-DLSTSRERLEGYRDALAEAGLPVDPELVVEGDFSE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 241 AFGRASLRTIADSGPtRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAA 320
Cdd:cd06267   162 ESGYEAARELLALPP-RPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEMGRAAA 240

                         250       260
                  ....*....|....*....|
gi 1370811475 321 RALLDALEHGAVGPGCAVLP 340
Cdd:cd06267   241 ELLLERIEGEEEPPRRIVLP 260
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
 81-346 1.53e-51

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: 172.36  E-value: 1.53e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVG-EAYPAEVFELLDLHRVPY 159
Cdd:cd06289     3 GLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPaAGTTAELLRRLKAWGIPV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 160 VVTYAYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIMQPSADNDRVQaRLRGIHETLAARGLAVRPVHQHEGPAT 239
Cdd:cd06289    83 VLALRDVPGSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSSTRRE-RLAGFRAALAEAGLPLDESLIVPGPAT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 240 IAFGRASLRTIADSGPtRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKA 319
Cdd:cd06289   162 REAGAEAARELLDAAP-PPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHPREIGRRA 240

                         250       260
                  ....*....|....*....|....*...
gi 1370811475 320 ARALLDALEHGAVGPGCAVL-PELRVRE 346
Cdd:cd06289   241 ARLLLRRIEGPDTPPERIIIePRLVVRE 268
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 81-348 2.08e-51

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: 172.03  E-value: 2.08e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPYV 160
Cdd:cd06285     3 GVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQELAARGVPVV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 161 VTYAYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIMQPSaDNDRVQARLRGIHETLAARGLAVRPVHQHEGPATI 240
Cdd:cd06285    83 LVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPL-NASTGRDRLRGYRRALAEAGLPVPDERIVPGGFTI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 241 AFGRASLRTIADSgPTRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAA 320
Cdd:cd06285   162 EAGREAAYRLLSR-PERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEMGRRAA 240

                         250       260
                  ....*....|....*....|....*....
gi 1370811475 321 RALLDALEHGAVGPGCAVL-PELRVRESA 348
Cdd:cd06285   241 ELLLQLIEGGGRPPRSITLpPELVVREST 269
PBP1_LacI-like cd06282
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 81-348 8.79e-47

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: 159.76  E-value: 8.79e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSL-VGEAYPAEVFELLDLHRVPY 159
Cdd:cd06282     3 GVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILtVGDAQGSEALELLEEEGVPY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 160 VVTYAYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIMQPSADNDRVQARLRGIHETLAARGLAVRPVHQHEGPAT 239
Cdd:cd06282    83 VLLFNQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAGDFSASDRARLRYQGYRDALKEAGLKPIPIVEVDFPTN 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 240 iafGRASLRTIADSGPTRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKA 319
Cdd:cd06282   163 ---GLEEALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQPSRDMGRAA 239

                         250       260
                  ....*....|....*....|....*....
gi 1370811475 320 ARALLDALEHGAVGPGcAVLPeLRVRESA 348
Cdd:cd06282   240 ADLLLAEIEGESPPTS-IRLP-HHLREGG 266
PBP1_sucrose_transcription_regulator cd06288
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ...
 96-347 4.05e-45

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: 155.40  E-value: 4.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  96 VAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVsLVGEAYPAEVFELLDLHRVPYVVTYAYRDDSPHCCIG 175
Cdd:cd06288    19 IRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGI-IYASMHHREVTLPPELTDIPLVLLNCFDDDPSLPSVV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 176 FDNRAAFARLTTHLLDLGHRDFAIIMQPSaDNDRVQARLRGIHETLAARGLAVRPVHQHEGPATIAFGRASLRTIADSGP 255
Cdd:cd06288    98 PDDEQGGYLATRHLIEAGHRRIAFIGGPE-DSLATRLRLAGYRAALAEAGIPYDPSLVVHGDWGRESGYEAAKRLLSAPD 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 256 tRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALLDALEHGAVGPG 335
Cdd:cd06288   177 -RPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVALPYYEMGRRAAELLLDGIEGEPPEPG 255

                         250
                  ....*....|...
gi 1370811475 336 CAVLP-ELRVRES 347
Cdd:cd06288   256 VIRVPcPLIERES 268
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
 82-347 5.83e-42

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: 147.30  E-value: 5.83e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  82 AIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDlHRVPYVV 161
Cdd:cd06284     4 VLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILLSGRLDAELLSELS-KRYPIVQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 162 TYAYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIMQPsADNDRVQARLRGIHETLAARGLAVRPVHQHEGPATIA 241
Cdd:cd06284    83 CCEYIPDSGVPSVSIDNEAAAYDATEYLISLGHRRIAHINGP-LDNVYARERLEGYRRALAEAGLPVDEDLIIEGDFSFE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 242 FGRASLRTIADSGPtRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAAR 321
Cdd:cd06284   162 AGYAAARALLALPE-RPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIGETAAE 240

                         250       260
                  ....*....|....*....|....*..
gi 1370811475 322 ALLDALEHGAVGPGCAVLP-ELRVRES 347
Cdd:cd06284   241 LLLEKIEGEGVPPEHIILPhELIVRES 267
PBP1_GalS-like cd06270
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ...
 81-346 1.38e-41

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: 146.13  E-value: 1.38e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPYV 160
Cdd:cd06270     3 GLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEELILIAEKIPPLV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 161 VTYAYRDDSPHCCIGFDNRAAfARLTT-HLLDLGHRDFAIIMQPsADNDRVQARLRGIHETLAARGLAVRPVHQHEGPAT 239
Cdd:cd06270    83 VINRYIPGLADRCVWLDNEQG-GRLAAeHLLDLGHRRIACITGP-LDIPDARERLAGYRDALAEAGIPLDPSLIIEGDFT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 240 IAFGRASLRTIADSGPTrPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKA 319
Cdd:cd06270   161 IEGGYAAAKQLLARGLP-FTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHYPIEEMAQAA 239

                         250       260
                  ....*....|....*....|....*..
gi 1370811475 320 ARALLDALEHGAVGPGCAVLPELRVRE 346
Cdd:cd06270   240 AELALNLAYGEPLPISHEFTPTLIERD 266
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
 81-347 1.84e-40

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: 143.47  E-value: 1.84e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAvsLVGE----AYPA---EVFELLD 153
Cdd:cd01541     3 GVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDG--LIIEptksALPNpnlDLYEELQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 154 LHRVPYVVTYAY--RDDSPHCCIgfDNRAAFARLTTHLLDLGHRDFAIIMQpsADNDRVQARLRGIHETLAARGLAVRPV 231
Cdd:cd01541    81 KKGIPVVFINSYypELDAPSVSL--DDEKGGYLATKHLIDLGHRRIAGIFK--SDDLQGVERYQGFIKALREAGLPIDDD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 232 HQ---HEGPATIAFGRASLRTIADSgPTRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTM 308
Cdd:cd01541   157 RIlwySTEDLEDRFFAEELREFLRR-LSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEPPLTSV 235

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1370811475 309 WVDTDAIGRKAARALLDALEHGAVGPGCAVLPELRVRES 347
Cdd:cd01541   236 VHPKEELGRKAAELLLRMIEEGRKPESVIFPPELIERES 274
PRK10703 PRK10703
HTH-type transcriptional repressor PurR;
24-349 7.85e-40

HTH-type transcriptional repressor PurR;


Pssm-ID: 236739 [Multi-domain]  Cd Length: 341  Bit Score: 143.71  E-value: 7.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  24 DVAKLAGVSTATVSRVYNDPGKVSADVQQRVRDAARTLNWIPNAAGRALASTRTHITGAIIPTLDDQVFASQVAGMQAVM 103
Cdd:PRK10703    6 DVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEAVEKNC 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 104 AEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHR-VPYVVTYAYRDDSPHCCIGFDNRAAF 182
Cdd:PRK10703   86 YQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLLAMLEEYRhIPMVVMDWGEAKADFTDAIIDNAFEG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 183 ARLTT-HLLDLGHRDFAIIMQPSADNDRVQaRLRGIHETLAARGLAVRPVHQHEGPATIAFGRASLRTIAdSGPTRPTAV 261
Cdd:PRK10703  166 GYLAGrYLIERGHRDIGVIPGPLERNTGAG-RLAGFMKAMEEANIKVPEEWIVQGDFEPESGYEAMQQIL-SQKHRPTAV 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 262 ICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALLDALEHGAVGPGC-AVLP 340
Cdd:PRK10703  244 FCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRIVNKREEPQTiEVHP 323


                  ....*....
gi 1370811475 341 ELRVRESAA 349
Cdd:PRK10703  324 RLVERRSVA 332
PBP1_AglR_RafR-like cd06292
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ...
 89-348 9.84e-36

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: 130.85  E-value: 9.84e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  89 DQVFASQVAGMQAVMAEHGITLFLgCSNYDPAQALAQVRAML-SRGVEAVSLVGEAYPAEVFELLDLHRVPYVVTYAYRD 167
Cdd:cd06292    15 DPFFDEFLAALGHAAAARGYDVLL-FTASGDEDEIDYYRDLVrSRRVDGFVLASTRHDDPRVRYLHEAGVPFVAFGRANP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 168 DSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIMQP--SADNDRvqaRLRGIHETLAARGLAVRPVHQHEGPATIAFGRA 245
Cdd:cd06292    94 DLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPegSVPSDD---RLAGYRAALEEAGLPFDPGLVVEGENTEEGGYA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 246 SLRTIADSGPtRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALLD 325
Cdd:cd06292   171 AAARLLDLGP-PPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTVRQPIDEIGRAVVDLLLA 249

                         250       260
                  ....*....|....*....|....
gi 1370811475 326 ALEHGAVGPGCAVL-PELRVRESA 348
Cdd:cd06292   250 AIEGNPSEPREILLqPELVVRESS 273
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
 92-345 5.55e-35

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


Pssm-ID: 380503 [Multi-domain]  Cd Length: 266  Bit Score: 128.92  E-value: 5.55e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  92 FASQVA-GMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPYVVTYAYRDDSP 170
Cdd:cd06280    13 FFTTIArGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGPSRELKRLLKHGIPIVLIDREVEGLE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 171 HCCIGFDNRAAFARLTTHLLDLGHRDFAIIMQPSaDNDRVQARLRGIHETLAARGLAVRPVHQHEGPATIAFGRASLRTI 250
Cdd:cd06280    93 LDLVAGDNREGAYKAVKHLIELGHRRIGLITGPL-EISTTRERLAGYREALAEAGIPVDESLIFEGDSTIEGGYEAVKAL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 251 ADSGPtRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALLDALEHG 330
Cdd:cd06280   172 LDLPP-RPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQPAYEIGRIAAQLLLERIEGQ 250

                         250
                  ....*....|....*.
gi 1370811475 331 AVGPGCAVLP-ELRVR 345
Cdd:cd06280   251 GEEPRRIVLPtELIIR 266
PBP1_SalR cd01545
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ...
 97-347 7.52e-35

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: 128.44  E-value: 7.52e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  97 AGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSR-GVEAVSLVgeayP-----AEVFELLDLHRVPYVVTYAYRDDSP 170
Cdd:cd01545    19 VGALRACREAGYHLVVEPCDSDDEDLADRLRRFLSRsRPDGVILT----PplsddPALLDALDELGIPYVRIAPGTDDDR 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 171 HCCIGFDNRAAFARLTTHLLDLGHRDFAIIMQPSADNDrVQARLRGIHETLAARGLAVRPVHQHEGPATIAFGRASLRTI 250
Cdd:cd01545    95 SPSVRIDDRAAAREMTRHLIALGHRRIGFIAGPPDHGA-SAERLEGFRDALAEAGLPLDPDLVVQGDFTFESGLEAAEAL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 251 ADsGPTRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALLDALEHG 330
Cdd:cd01545   174 LD-LPDRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTTVRQPIAEMARRAVELLIAAIRGA 252

                         250
                  ....*....|....*...
gi 1370811475 331 AVGPGCAVLP-ELRVRES 347
Cdd:cd01545   253 PAGPERETLPhELVIRES 270
PBP1_LacI-like cd06279
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ...
 87-347 9.66e-35

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: 128.48  E-value: 9.66e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  87 LDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMlsrgVEAVSLVGEAYPAEVFELLDLHRVPYVVTYAyR 166
Cdd:cd06279    14 FSDPVAAQFLRGVAEVCEEEGLGLLLLPATDEGSAAAAVRNAA----VDGFIVYGLSDDDPAVAALRRRGLPLVVVDG-P 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 167 DDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIM----------------QPSADNDRVQARLRGIHETLAARGLAVRP 230
Cdd:cd06279    89 APPGIPSVGIDDRAAARAAARHLLDLGHRRIAILSlrldrgrergpvsaerLAAATNSVARERLAGYRDALEEAGLDLDD 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 231 VHQ-HEGPATIAFGRASLRTIADSGPtRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMW 309
Cdd:cd06279   169 VPVvEAPGNTEEAGRAAARALLALDP-RPTAILCMSDVLALGALRAARERGLRVPEDLSVTGFDDIPEAAAADPGLTTVR 247

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1370811475 310 VDTDAIGRKAARALLDALeHGAVGPGCAVLPELRVRES 347
Cdd:cd06279   248 QPAVEKGRAAARLLLGLL-PGAPPRPVILPTELVVRAS 284
PBP1_PurR cd06275
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ...
 81-347 3.11e-34

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: 126.99  E-value: 3.11e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLD-LHRVPY 159
Cdd:cd06275     3 GLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAELLAaLRSIPV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 160 VVTyayrdDSPHCCIGFD----NRAAFARLTT-HLLDLGHRDFAIIMQPsADNDRVQARLRGIHETLAARGLAVRPVHQH 234
Cdd:cd06275    83 VVL-----DREIAGDNADavldDSFQGGYLATrHLIELGHRRIGCITGP-LEHSVSRERLAGFRRALAEAGIEVPPSWIV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 235 EGPATIAFGRASLRTIAdSGPTRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDA 314
Cdd:cd06275   157 EGDFEPEGGYEAMQRLL-SQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQPKDE 235

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1370811475 315 IGRKAARALLDALEH-GAVGPGCAVLPELRVRES 347
Cdd:cd06275   236 LGELAVELLLDRIENkREEPQSIVLEPELIERES 269
PBP1_CcpA-like cd19975
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
 81-347 3.70e-34

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: 126.52  E-value: 3.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPYV 160
Cdd:cd19975     3 GVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFASGTLTEENKQLLKNMNIPVV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 161 VTYAYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIMQPSADNDRVQARLRGIHETLAARGLavrPVHQH---EGP 237
Cdd:cd19975    83 LVSTESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISGPLDDPNAGYPRYEGYKKALKDAGL---PIKENlivEGD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 238 ATIAFGRASLRTIADSGPtRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGR 317
Cdd:cd19975   160 FSFKSGYQAMKRLLKNKK-LPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQPFYEMGK 238

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1370811475 318 KAARALLDALEHGAVGPGCAVLP-ELRVRES 347
Cdd:cd19975   239 KAVELLLDLIKNEKKEEKSIVLPhQIIERES 269
PRK11041 PRK11041
DNA-binding transcriptional regulator CytR; Provisional
 43-351 8.84e-34

DNA-binding transcriptional regulator CytR; Provisional


Pssm-ID: 182923 [Multi-domain]  Cd Length: 309  Bit Score: 126.65  E-value: 8.84e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  43 PGKVSADVQQRVRDAARTLNWIPNAAGRALASTRTHITGAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQA 122
Cdd:PRK11041    1 PEKVSQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 123 LAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPYVVTYAYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIMQ 202
Cdd:PRK11041   81 KTFVNLIITKQIDGMLLLGSRLPFDASKEEQRNLPPMVMANEFAPELELPTVHIDNLTAAFEAVNYLHELGHKRIACIAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 203 PSaDNDRVQARLRGIHETLAARGLAVRPVHQHEGPATIAFGRASLRTIADSgPTRPTAVICGNDALALGALLEAQAMGIA 282
Cdd:PRK11041  161 PE-EMPLCHYRLQGYVQALRRCGITVDPQYIARGDFTFEAGAKALKQLLDL-PQPPTAVFCHSDVMALGALSQAKRMGLR 238

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 283 VPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALLDALEHGAVGPGCAVLP-ELRVRESAAPP 351
Cdd:PRK11041  239 VPQDLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSSGSRLLDcELIIRGSTAAP 308
PRK10423 PRK10423
transcriptional repressor RbsR; Provisional
 24-348 9.94e-34

transcriptional repressor RbsR; Provisional


Pssm-ID: 182448 [Multi-domain]  Cd Length: 327  Bit Score: 127.12  E-value: 9.94e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  24 DVAKLAGVSTATVSRVYNDPGKVSADVQQRVRDAARTLNWIPNAAGRALASTRTHITGAIIPTLDDQVFASQVAGMQAVM 103
Cdd:PRK10423    3 DVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVERSC 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 104 AEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLV-GEAY--PAEVfelldLHRVPYVVTyAYRDDSP---HCCIGFD 177
Cdd:PRK10423   83 FERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLcTETHqpSREI-----MQRYPSVPT-VMMDWAPfdgDSDLIQD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 178 NRAAFARLTT-HLLDLGHRDFAIIMQPSadnDRVQARLR--GIHETLAARGLAVRPVHQHEGPATIAFGRASLRTIAdSG 254
Cdd:PRK10423  157 NSLLGGDLATqYLIDKGYTRIACITGPL---DKTPARLRleGYRAAMKRAGLNIPDGYEVTGDFEFNGGFDAMQQLL-AL 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 255 PTRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALLDALEHGAVGP 334
Cdd:PRK10423  233 PLRPQAVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQ 312

                         330
                  ....*....|....*
gi 1370811475 335 GCAVL-PELRVRESA 348
Cdd:PRK10423  313 QRLQLtPELMERGSV 327
PBP1_LacI-like cd06290
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 81-347 1.17e-33

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: 125.42  E-value: 1.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLhRVPyV 160
Cdd:cd06290     3 GVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEELLKLLAE-GIP-V 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 161 VTYAYRDDSPHC-CIGFDNRAAFARLTTHLLDLGHRDFAIIMQPsADNDRVQARLRGIHETLAARGLAVRPVHQHEGPAT 239
Cdd:cd06290    81 VLVDRELEGLNLpVVNVDNEQGGYNATNHLIDLGHRRIVHISGP-EDHPDAQERYAGYRRALEDAGLEVDPRLIVEGDFT 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 240 IAFGRASLRTIADSGptRP-TAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRK 318
Cdd:cd06290   160 EESGYEAMKKLLKRG--GPfTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYEMGKT 237

                         250       260       270
                  ....*....|....*....|....*....|
gi 1370811475 319 AARALLDALEHGAVGPGCAVLP-ELRVRES 347
Cdd:cd06290   238 AAEILLELIEGKGRPPRRIILPtELVIRES 267
lacI PRK09526
lac repressor; Reviewed
 22-356 6.67e-33

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 125.11  E-value: 6.67e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  22 LGDVAKLAGVSTATVSRVYNDPGKVSADVQQRVRDAARTLNWIPNAAGRALASTRTHITGAIipTLDDQVFA-SQV-AGM 99
Cdd:PRK09526    8 LYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLA--TTSLALHApSQIaAAI 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 100 QAVMAEHGITLFLGCSNYDPAQAL-AQVRAMLSRGVEAVsLVGeaYPAEVFELLDLHRVPYVVTYAYRDDSPH---CCIG 175
Cdd:PRK09526   86 KSRADQLGYSVVISMVERSGVEACqAAVNELLAQRVSGV-IIN--VPLEDADAEKIVADCADVPCLFLDVSPQspvNSVS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 176 FDNRAAfARLTT-HLLDLGHRDFAIIMQPSadnDRVQARLR--GIHETLAARGLAvrPVHQHEGPATIAFGRASLRTIAD 252
Cdd:PRK09526  163 FDPEDG-TRLGVeHLVELGHQRIALLAGPE---SSVSARLRlaGWLEYLTDYQLQ--PIAVREGDWSAMSGYQQTLQMLR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 253 SGPtRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALLDALEHGAV 332
Cdd:PRK09526  237 EGP-VPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLLALSQGQAV 315

                         330       340
                  ....*....|....*....|....*
gi 1370811475 333 gPGCAVLP-ELRVRESAAPPHSEAP 356
Cdd:PRK09526  316 -KGSQLLPtSLVVRKSTAPPNTQTA 339
PBP1_AglR-like cd20010
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ...
 81-334 4.64e-32

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: 121.12  E-value: 4.64e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPT----LDDQVFASQVAGMQAVMAEHGITLFLGcSNYDPAQALAQVRAMLSRG-VEAVSLvgeAYPAEVFE----L 151
Cdd:cd20010     3 GLVLPLdpgdLGDPFFLEFLAGLSEALAERGLDLLLA-PAPSGEDELATYRRLVERGrVDGFIL---ARTRVNDPriayL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 152 LDLhRVPYVVTYAYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIMQPSADNdRVQARLRGIHETLAARGLAVRPV 231
Cdd:cd20010    79 LER-GIPFVVHGRSESGAPYAWVDIDNEGAFRRATRRLLALGHRRIALLNGPEELN-FAHQRRDGYRAALAEAGLPVDPA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 232 HQHEGPATIAFGRASLRTIADSGPtRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREI-RPALTTMWV 310
Cdd:cd20010   157 LVREGPLTEEGGYQAARRLLALPP-PPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLLPALEYfSPPLTTTRS 235

                         250       260
                  ....*....|....*....|....
gi 1370811475 311 DTDAIGRKAARALLDALEHGAVGP 334
Cdd:cd20010   236 SLRDAGRRLAEMLLALIDGEPAAE 259
PBP1_LacI cd01574
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ...
 81-347 2.86e-31

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: 118.84  E-value: 2.86e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLG-CSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPY 159
Cdd:cd01574     3 GVIATGLSLYGPASTLAGIERAARERGYSVSIAtVDEDDPASVREALDRLLSQRVDGIIVIAPDEAVLEALRRLPPGLPV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 160 VVTYAyRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIMQPSaDNDRVQARLRGIHETLAARGLAVRPVHqhEGPAT 239
Cdd:cd01574    83 VIVGS-GPSPGVPTVSIDQEEGARLATRHLLELGHRRIAHIAGPL-DWVDARARLRGWREALEEAGLPPPPVV--EGDWS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 240 IAFGRASLRTIADSGPtrPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKA 319
Cdd:cd01574   159 AASGYRAGRRLLDDGP--VTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDFAELGRRA 236

                         250       260       270
                  ....*....|....*....|....*....|
gi 1370811475 320 ARALLDALEhGAVGPGCAVL--PELRVRES 347
Cdd:cd01574   237 VELLLALIE-GPAPPPESVLlpPELVVRES 265
PBP1_CatR-like cd06296
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ...
 85-347 4.53e-31

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: 118.53  E-value: 4.53e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  85 PTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPYVVTYA 164
Cdd:cd06296     7 PQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQLRLLRSAGIPFVLIDP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 165 YRDDSPHC-CIGFDNRAAFARLTTHLLDLGHRDFAIIMQPsADNDRVQARLRGIHETLAARGLAVRPVHQHEGPATIAFG 243
Cdd:cd06296    87 VGEPDPDLpSVGATNWAGGRLATEHLLDLGHRRIAVITGP-PRSVSGRARLAGYRAALAEAGIAVDPDLVREGDFTYEAG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 244 RASLRTIADSgPTRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARAL 323
Cdd:cd06296   166 YRAARELLEL-PDPPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVHQPLREMGAVAVRLL 244

                         250       260
                  ....*....|....*....|....*
gi 1370811475 324 LDALEHGAVGPGCAVLP-ELRVRES 347
Cdd:cd06296   245 LRLLEGGPPDARRIELAtELVVRGS 269
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 92-347 1.49e-30

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: 116.99  E-value: 1.49e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  92 FASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPyVVTYAYRDDSPH 171
Cdd:cd06293    14 FAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSHLARLRARGTA-VVLLDRPAPGPA 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 172 -CCIGFDNRAAFARLTTHLLDLGHRDFAIImQPSADNDRVQARLRGIHETLAARGLAVRP-VHQHE-GPATIAFGRASLR 248
Cdd:cd06293    93 gCSVSVDDVQGGALAVDHLLELGHRRIAFV-SGPLRTRQVAERLAGARAAVAEAGLDPDEvVRELSaPDANAELGRAAAA 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 249 TIAdSGPTRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALLDALE 328
Cdd:cd06293   172 QLL-AMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQPSYELGRAAADLLLDEIE 250

                         250       260
                  ....*....|....*....|
gi 1370811475 329 HGAVGPGCAVL-PELRVRES 347
Cdd:cd06293   251 GPGHPHEHVVFqPELVVRSS 270
PRK10727 PRK10727
HTH-type transcriptional regulator GalR;
24-355 2.60e-30

HTH-type transcriptional regulator GalR;


Pssm-ID: 182681 [Multi-domain]  Cd Length: 343  Bit Score: 118.32  E-value: 2.60e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  24 DVAKLAGVSTATVSRVYNDPGKVSADVQQRVRDAARTLNWIPNAAGRALASTRTHITGAIIPTLDDQVFASQVAGMQAVM 103
Cdd:PRK10727    6 DVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKAVEQVA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 104 AEHGITLFLGcSNYDPAQALAQVRAMLSRGVEAvSLVGEAYPAEVFELLDLHR-VPYVVT-------YAYRddsphcCIG 175
Cdd:PRK10727   86 YHTGNFLLIG-NGYHNEQKERQAIEQLIRHRCA-ALVVHAKMIPDAELASLMKqIPGMVLinrilpgFENR------CIA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 176 FDNRAAFARLTTHLLDLGHRDFAIIMQPSADNDrVQARLRGIHETLAARGLAVRPVHQHEGPATIAFGRASLRTIADSGP 255
Cdd:PRK10727  158 LDDRYGAWLATRHLIQQGHTRIGYLCSNHSISD-AEDRLQGYYDALAESGIPANDRLVTFGEPDESGGEQAMTELLGRGR 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 256 TRpTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALLdALEHGAVGPG 335
Cdd:PRK10727  237 NF-TAVACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELAL-ALADNRPLPE 314

                         330       340
                  ....*....|....*....|..
gi 1370811475 336 CAVL--PELRVRESAAPPHSEA 355
Cdd:PRK10727  315 ITNVfsPTLVRRHSVSTPSLEA 336
PBP1_DegA_Like cd19976
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
 81-347 5.92e-30

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: 115.42  E-value: 5.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLV-GEAYPAEVFELLDLHRVPY 159
Cdd:cd19976     3 GLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIAsSNISDEAIIKLLKEEKIPV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 160 VVTYAYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIMQPSAdNDRVQARLRGIHETLAARGLAVRPVHQHEGPAT 239
Cdd:cd19976    83 VVLDRYIEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPS-TYNEHERIEGYKNALQDHNLPIDESWIYSGESS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 240 IAFGRASLRTIADSGPtrPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKA 319
Cdd:cd19976   162 LEGGYKAAEELLKSKN--PTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQPIFEMGQEA 239

                         250       260
                  ....*....|....*....|....*....
gi 1370811475 320 ARALLDALEHGAVGPGCAVL-PELRVRES 347
Cdd:cd19976   240 AKLLLKIIKNPAKKKEEIVLpPELIKRDS 268
PBP1_LacI-like cd06281
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 81-347 1.96e-28

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: 111.56  E-value: 1.96e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSL-VGEAYPAEVFELLDLHRVPY 159
Cdd:cd06281     3 GCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILtPGDEDDPELAAALARLDIPV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 160 VVTYayRD-DSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIMqPSADNDRVQARLRGIHETLAARGLAVRPVHQHEGPA 238
Cdd:cd06281    83 VLID--RDlPGDIDSVLVDHRSGVRQATEYLLSLGHRRIALLT-GGPDIRPGRERIAGFKAAFAAAGLPPDPDLVRLGSF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 239 TIAFGRASLRTIAdSGPTRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRK 318
Cdd:cd06281   160 SADSGFREAMALL-RQPRPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDLDAVGRA 238

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1370811475 319 AARALLDALEHGAVGPGCAVL--PELRVRES 347
Cdd:cd06281   239 AAELLLDRIEGPPAGPPRRIVvpTELILRDS 269
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
 81-347 9.77e-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: 109.53  E-value: 9.77e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVgeAYPAEVFELLDLHRvPYV 160
Cdd:cd06291     3 GLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILG--SHSLDIEEYKKLNI-PIV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 161 -VTyayRDDSPH-CCIGFDNRAAfARLTT-HLLDLGHRDFAIIMQPSADNDRVQaRLRGIHETLAARGLAVRPVHQHEGP 237
Cdd:cd06291    80 sID---RYLSEGiPSVSSDNYQG-GRLAAeHLIEKGCKKILHIGGPSNNSPANE-RYRGFEDALKEAGIEYEIIEIDEND 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 238 ATIAFGRASLRTIADSGPtRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGR 317
Cdd:cd06291   155 FSEEDAYELAKELLEKYP-DIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIEEMAK 233

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1370811475 318 KAARALLDALEHGAVGPGCAVLP-ELRVRES 347
Cdd:cd06291   234 EAVELLLKLIEGEEIEESRIVLPvELIERET 264
PRK10014 PRK10014
DNA-binding transcriptional repressor MalI; Provisional
 24-340 2.38e-27

DNA-binding transcriptional repressor MalI; Provisional


Pssm-ID: 182193 [Multi-domain]  Cd Length: 342  Bit Score: 110.18  E-value: 2.38e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  24 DVAKLAGVSTATVSRVYNDPGKVSADVQQRVRDAARTLNWIPNAAGRALASTRTHITGAIIPTLDDQVFASQVAGMQAVM 103
Cdd:PRK10014   11 DVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAELTAGLTEAL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 104 AEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVF-ELLDLHRVPYVVT--YAYRDDSPhcCIGFDNRA 180
Cdd:PRK10014   91 EAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAGSSDDLrEMAEEKGIPVVFAsrASYLDDVD--TVRPDNMQ 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 181 AFARLTTHLLDLGHRDFAIIMQPSADNDRVQaRLRGIHETLAARGLAVRPVHQHEGPATiafGRASLRTIAD---SGPTr 257
Cdd:PRK10014  169 AAQLLTEHLIRNGHQRIAWLGGQSSSLTRAE-RVGGYCATLLKFGLPFHSEWVLECTSS---QKQAAEAITAllrHNPT- 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 258 PTAVICGNDALALGALLEAQAMGIAVPA---------ELSITGFDDVALAREIRPALTtmWVDTDA--IGRKAARALLDA 326
Cdd:PRK10014  244 ISAVVCYNETIAMGAWFGLLRAGRQSGEsgvdryfeqQVALAAFTDVPEAELDDPPLT--WASTPAreIGRTLADRMMQR 321

                         330
                  ....*....|....
gi 1370811475 327 LEHGAVGPGCAVLP 340
Cdd:PRK10014  322 ITHEETHSRNLIIP 335
PBP1_LacI-like cd06299
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ...
 81-347 4.66e-27

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: 107.75  E-value: 4.66e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPYV 160
Cdd:cd06299     3 GLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGENSEGLQALIAQGLPVV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 161 VTYAYRDDSPHC-CIGFDNRAAFARLTTHLLDLGHRDFAIIMQPsADNDRVQARLRGIHETLAARGLAVRPVHQHEGPAT 239
Cdd:cd06299    83 FVDREVEGLGGVpVVTSDNRPGAREAVEYLVSLGHRRIGYISGP-LSTSTGRERLAAFRAALTAAGIPIDEELVAFGDFR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 240 IAFGRASLRTIADsGPTRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKA 319
Cdd:cd06299   162 QDSGAAAAHRLLS-RGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVERIGRRA 240

                         250       260
                  ....*....|....*....|....*...
gi 1370811475 320 ARALLDALEHGAVGPGCAVLPELRVRES 347
Cdd:cd06299   241 VELLLALIENGGRATSIRVPTELIPRES 268
PRK14987 PRK14987
HTH-type transcriptional regulator GntR;
21-334 2.72e-26

HTH-type transcriptional regulator GntR;


Pssm-ID: 184949 [Multi-domain]  Cd Length: 331  Bit Score: 107.03  E-value: 2.72e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  21 VLGDVAKLAGVSTATVSRVYNDPGKVSADVQQRVRDAARTLNWIPNAAGRALASTRTHITGAIIPTLDDQVFASQVAGMQ 100
Cdd:PRK14987    7 VLQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGIE 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 101 AVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPYVVTYAYRDDSPHCCIGFDNRA 180
Cdd:PRK14987   87 SVTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIEVAGIPVVELMDSQSPCLDIAVGFDNFE 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 181 AFARLTTHLLDLGHRDFAIImqPSADNDRVQARLRGIHETLAARGLAVRPVhQHEGPATIAFGRASLRTIADSGPtRPTA 260
Cdd:PRK14987  167 AARQMTTAIIARGHRHIAYL--GARLDERTIIKQKGYEQAMLDAGLVPYSV-MVEQSSSYSSGIELIRQARREYP-QLDG 242

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370811475 261 VICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALLDALEHGAVGP 334
Cdd:PRK14987  243 VFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARIRGESVTP 316
PBP1_GalR cd01544
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ...
 130-347 1.90e-25

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: 103.37  E-value: 1.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 130 LSRGVEAVSLVGEAYPAEVFELLDLHRvPYVVTYAYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAII-------MQ 202
Cdd:cd01544    50 LLEKVDGIIAIGKFSKEEIEKLKKLNP-NIVFVDSNPDPDGFDSVVPDFEQAVRQALDYLIELGHRRIGFIggkeytsDD 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 203 PSADNDRvqaRLRGIHETLAARGLaVRPVHQHEGPATIAFGRASLRTIADSGPtRPTAVICGNDalalgalleaqAM--- 279
Cdd:cd01544   129 GEEIEDP---RLRAFREYMKEKGL-YNEEYIYIGEFSVESGYEAMKELLKEGD-LPTAFFVASD-----------PMaig 192

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370811475 280 --------GIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALLDALEHGAVGPGCAVLP-ELRVRES 347
Cdd:cd01544   193 alralqeaGIKVPEDISIISFNDIEVAKYVTPPLTTVHIPTEEMGRTAVRLLLERINGGRTIPKKVLLPtKLIERES 269
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
 79-332 5.71e-24

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: 99.11  E-value: 5.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  79 ITGAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVP 158
Cdd:cd01542     1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEITDEHRKALKKLKIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 159 yVVTYAyRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIMQPSADNDRVQARLRGIHETLAARGLAvrPVHQHEGPA 238
Cdd:cd01542    81 -VVVLG-QEHEGFSCVYHDDYGAGKLLGEYLLKKGHKNIAYIGVDEEDIAVGVARKQGYLDALKEHGID--EVEIVETDF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 239 TIAFGRASLRTIADSGPtrPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRK 318
Cdd:cd01542   157 SMESGYEAAKELLKENK--PDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEAGEK 234

                         250
                  ....*....|....
gi 1370811475 319 AARALLDALEHGAV 332
Cdd:cd01542   235 AAELLLDMIEGEKV 248
PBP1_CelR cd06295
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ...
 76-347 7.43e-24

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: 98.86  E-value: 7.43e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  76 RTHITGAIIPTLD-------DQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQAlaqVRAMLSRGVEAVSLVGEAYPAEV 148
Cdd:cd06295     2 RSRTIAVVVPMDPhgdqsitDPFFLELLGGISEALTDRGYDMLLSTQDEDANQL---ARLLDSGRADGLIVLGQGLDHDA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 149 FELLDLHRVPYVVTYAYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIImqpSADNDR-VQARLRGIHETLAARGLA 227
Cdd:cd06295    79 LRELAQQGLPMVVWGAPEDGQSYCSVGSDNVKGGALATEHLIEIGRRRIAFL---GDPPHPeVADRLQGYRDALAEAGLE 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 228 VRPVHQHEGPATIAFGRASLRTIADSGpTRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTT 307
Cdd:cd06295   156 ADPSLLLSCDFTEESGYAAMRALLDSG-TAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFRPPLTT 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1370811475 308 MWVDTDAIGRKAARALLDALEHGAVGPgcAVLP-ELRVRES 347
Cdd:cd06295   235 VRQDLALAGRLLVEKLLALIAGEPVTS--SMLPvELVVRES 273
PBP1_RegR_EndR_KdgR-like cd06283
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ...
 92-345 7.63e-24

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: 98.78  E-value: 7.63e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  92 FASQV-AGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSL--VGEAYPAEVFELLDlhRVPYVvtYAYRDD 168
Cdd:cd06283    13 FSSLLlKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILqpTGNNNDAYLELAQK--GLPVV--LVDRQI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 169 SPHCC--IGFDNRAAFARLTTHLLDLGHRDFAIIMQPSADNDRVQARLRGIHETLAARGLAVR--PVHQHEGPATiafgR 244
Cdd:cd06283    89 EPLNWdtVVTDNYDATYEATEHLKEQGYERIVFVTEPIKGISTRRERLQGFLDALARYNIEGDvyVIEIEDTEDL----Q 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 245 ASLRTIADSGPTRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALL 324
Cdd:cd06283   165 QALAAFLSQHDGGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQPTYEIGKAAAEILL 244

                         250       260
                  ....*....|....*....|..
gi 1370811475 325 DALEHGAVGPGCAVLP-ELRVR 345
Cdd:cd06283   245 ERIEGDSGEPKEIELPsELIIR 266
PBP1_MalR-like cd06294
ligand-binding domain of maltose transcription regulator MalR which is a member of the ...
 81-343 8.39e-24

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: 98.81  E-value: 8.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFA----SQV-AGMQAVMAEHGITLFLGCSNyDPAQALAQVRAMLSRG-VEAVSLVgeaYPAE---VFEL 151
Cdd:cd06294     3 GLVLPSSAEELFQnpffSEVlRGISQVANENGYSLLLATGN-TEEELLEEVKRMVRGRrVDGFILL---YSKEddpLIEY 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 152 LDLHRVPYVVTYAYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIImQPSADNDRVQARLRGIHETLAARGLAVRPV 231
Cdd:cd06294    79 LKEEGFPFVVIGKPLDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFI-GGDKNLVVSIDRLQGYKQALKEAGLPLDDD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 232 HQHEGPATIAFGRASLRTIADSGPtRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVD 311
Cdd:cd06294   158 YILLLDFSEEDGYDALQELLSKPP-PPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSVDIN 236

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1370811475 312 TDAIGRKAARALLDALEHGAVGPGCAVLP-ELR 343
Cdd:cd06294   237 PYELGREAAKLLINLLEGPESLPKNVIVPhELI 269
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
 188-347 3.23e-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://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433159 [Multi-domain]  Cd Length: 160  Bit Score: 94.33  E-value: 3.23e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 188 HLLDLGHRDFAIIMQPSADNDRV-QARLRGIHETLAARGLAVRPVhqhEGPATIAFGRASLRTIADSGPTRPTAVICGND 266
Cdd:pfam13377   1 HLAELGHRRIALIGPEGDRDDPYsDLRERGFREAARELGLDVEPT---LYAGDDEAEAAAARERLRWLGALPTAVFVAND 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 267 ALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALLDALEHGAVGPGCAVLP-ELRVR 345
Cdd:pfam13377  78 EVALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPpELVER 157


                  ..
gi 1370811475 346 ES 347
Cdd:pfam13377 158 ES 159
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
24-89 1.86e-22

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 89.18  E-value: 1.86e-22
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370811475   24 DVAKLAGVSTATVSRVYNDPGKVSADVQQRVRDAARTLNWIPNAAGRALASTRTHITGAIIPTLDD 89
Cdd:smart00354   5 DVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
 81-334 2.80e-22

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: 94.52  E-value: 2.80e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAV-------------SLVGEAYPAe 147
Cdd:cd19977     3 GLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIiiaptggnedlieKLVKSGIPV- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 148 VF--ELLDLHRVPYVVTyayrddsphccigfDNRAAFARLTTHLLDLGHRDFAIIMQPSADNDRVQaRLRGIHETLAARG 225
Cdd:cd19977    82 VFvdRYIPGLDVDTVVV--------------DNFKGAYQATEHLIELGHKRIAFITYPLELSTRQE-RLEGYKAALADHG 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 226 LAVRPVHQHEGPATIAfGRASLRTIADSGPtRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPAL 305
Cdd:cd19977   147 LPVDEELIKHVDRQDD-VRKAISELLKLEK-PPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPL 224

                         250       260
                  ....*....|....*....|....*....
gi 1370811475 306 TTMWVDTDAIGRKAARALLDALEHGAVGP 334
Cdd:cd19977   225 TVIAQPTYEIGRKAAELLLDRIENKPKGP 253
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 118-347 2.87e-22

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: 94.52  E-value: 2.87e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 118 DPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPyVVTYAYRDDSPHC-CIGFDNRAAFARLTTHLLDLGHRD 196
Cdd:cd06278    39 DEDDVDDALRQLLQYRVDGVIVTSATLSSELAEECARRGIP-VVLFNRVVEDPGVdSVSCDNRAGGRLAADLLLAAGHRR 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 197 FAIIMQPsADNDRVQARLRGIHETLAARGLavRPVHQHEGPATIAFGRASLRTIADSgPTRPTAVICGNDALAL-GALLE 275
Cdd:cd06278   118 IAFLGGP-EGTSTSRERERGFRAALAELGL--PPPAVEAGDYSYEGGYEAARRLLAA-PDRPDAIFCANDLMALgALDAA 193

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370811475 276 AQAMGIAVPAELSITGFDDVALAReiRPA--LTTMWVDTDAIGRKAARALLDALEHGAVGPGCAVLP-ELRVRES 347
Cdd:cd06278   194 RQEGGLVVPEDISVVGFDDIPMAA--WPSydLTTVRQPIEEMAEAAVDLLLERIENPETPPERRVLPgELVERGS 266
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
 81-340 1.34e-21

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: 92.69  E-value: 1.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAE-VFELLDLHRVPY 159
Cdd:cd01537     3 GVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAgVAEKARGQNVPV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 160 VV-TYAYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIMQPSADNDrVQARLRGIHETLAARGLAVRPVHQHEGPA 238
Cdd:cd01537    83 VFfDKEPSRYDKAYYVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHPD-AEARLAGVIKELNDKGIKTEQLQLDTGDW 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 239 TIAFGRASLRTIAdSGPTRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRK 318
Cdd:cd01537   162 DTASGKDKMDQWL-SGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDANNLGKT 240

                         250       260
                  ....*....|....*....|..
gi 1370811475 319 AARALLDALEHGAVGPGCAVLP 340
Cdd:cd01537   241 TFDLLLNLADNWKIDNKVVRVP 262
PRK10401 PRK10401
HTH-type transcriptional regulator GalS;
24-308 1.57e-20

HTH-type transcriptional regulator GalS;


Pssm-ID: 236681 [Multi-domain]  Cd Length: 346  Bit Score: 90.99  E-value: 1.57e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  24 DVAKLAGVSTATVSRVYNDPGKVSADVQQRVRDAARTLNWIPNAAGRALASTRTHITGAIIPTLDDQVFASQVAGMQAVM 103
Cdd:PRK10401    6 DVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAVDLVA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 104 AEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEvfELLD-LHRVPYVVT-------YAYRddsphcCIG 175
Cdd:PRK10401   86 QQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDD--ELAQfMDQIPGMVLinrvvpgYAHR------CVC 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 176 FDNRAAFARLTTHLLDLGHRDFAIIMQPSADNDRVQaRLRGIHETLAARGLAVRPVHQHEGPATIAFGRASLRTIADSGp 255
Cdd:PRK10401  158 LDNVSGARMATRMLLNNGHQRIGYLSSSHGIEDDAM-RRAGWMSALKEQGIIPPESWIGTGTPDMQGGEAAMVELLGRN- 235

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370811475 256 TRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTM 308
Cdd:PRK10401  236 LQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTV 288
PBP1_LacI-like cd19974
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 103-347 4.74e-20

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: 88.38  E-value: 4.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 103 MAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEaYPAEVFELLDLHRVPYVVTYAYRDDSPHCCIGFDNRAAF 182
Cdd:cd19974    28 LSELGYNLVLEIISDEDEEELNLPSIISEEKVDGIIILGE-ISKEYLEKLKELGIPVVLVDHYDEELNADSVLSDNYYGA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 183 ARLTTHLLDLGHRDFAIIMQPSADNDrVQARLRGIHETLAARGLAVRPVHQH-EGPATIAFGRASLRTIADSgpTRPTAV 261
Cdd:cd19974   107 YKLTSYLIEKGHKKIGFVGDINYTSS-FMDRYLGYRKALLEAGLPPEKEEWLlEDRDDGYGLTEEIELPLKL--MLPTAF 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 262 ICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALLDALEHGAVGPG-CAVLP 340
Cdd:cd19974   184 VCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLTTVEVDKEAMGRRAVEQLLWRIENPDRPFEkILVSG 263


                  ....*..
gi 1370811475 341 ELRVRES 347
Cdd:cd19974   264 KLIERDS 270
PBP1_LacI-like cd06277
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 121-347 8.49e-20

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: 87.68  E-value: 8.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 121 QALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPYVVTYAYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAII 200
Cdd:cd06277    49 DFDEILKELTDDQSSGIILLGTELEEKQIKLFQDVSIPVVVVDNYFEDLNFDCVVIDNEDGAYEAVKYLVELGHTRIGYL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 201 mQPSADNDRVQARLRGIHETLAARGLAVRPvhqhegPATIAFG------RASLRTIADSGPTRPTAVICGNDALALGALL 274
Cdd:cd06277   129 -ASSYRIKNFEERRRGFRKAMRELGLSEDP------EPEFVVSvgpegaYKDMKALLDTGPKLPTAFFAENDIIALGCIK 201

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370811475 275 EAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALLDALEHGAVGPGCAVLP-ELRVRES 347
Cdd:cd06277   202 ALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRRLIEKIKDPDGGTLKILVStKLVERGS 275
PBP1_RafR-like cd20009
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ...
 169-328 1.10e-17

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: 81.82  E-value: 1.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 169 SPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIMqPSADNDRVQARLRGIHETLAARGLAVRPVHQHEGPATIAFGRASLR 248
Cdd:cd20009    93 TPHAYFDFDNEAFAYEAVRRLAARGRRRIALVA-PPRELTYAQHRLRGFRRALAEAGLEVEPLLIVTLDSSAEAIRAAAR 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 249 TIADSGPtRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAARALLDALE 328
Cdd:cd20009   172 RLLRQPP-RPDGIICASEIAALGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPIDTLYEDIEEAGRFLAEALLRRIE 250
PBP1_CcpA cd06298
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ...
 81-323 1.17e-17

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: 81.57  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPYV 160
Cdd:cd06298     3 GVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMGDELTEEIREEFKRSPVPVV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 161 VTYAYRDDS--PHCCIgfDNRAAFARLTTHLLDLGHRDFAIIMQPSADNDRVQARLRGIHETLAARGLAVRPVHQHEGPA 238
Cdd:cd06298    83 LAGTVDSDHeiPSVNI--DYEQAAYDATKSLIDKGHKKIAFVSGPLKEYINNDKKLQGYKRALEEAGLEFNEPLIFEGDY 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 239 TIAFGRASLRTIADSGptRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRK 318
Cdd:cd06298   161 DYDSGYELYEELLESG--EPDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPLYDIGAV 238


                  ....*
gi 1370811475 319 AARAL 323
Cdd:cd06298   239 AMRLL 243
HTH_LacI cd01392
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ...
 24-74 5.18e-17

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: 73.98  E-value: 5.18e-17
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370811475  24 DVAKLAGVSTATVSRVYNDPGKVSADVQQRVRDAARTLNWIPNAAGRALAS 74
Cdd:cd01392     2 DIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
PBP1_AglR_RafR-like cd06271
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ...
 85-328 3.01e-16

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


Pssm-ID: 380495 [Multi-domain]  Cd Length: 264  Bit Score: 77.47  E-value: 3.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  85 PTLDDQVFASQVAGMQAVMAEHGitLFLGCSNYDPAQALAQVRAMLSRG-VEAVSLVGEAYPAEVFELLDLHRVPYVVTY 163
Cdd:cd06271    10 ETELNGTVSE*VSGITEEAGTTG--YHLLVWPFEEAES*VPIRDLVETGsADGVILSEIEPNDPRVQFLTKQNFPFVAHG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 164 AYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIImQPSADNDRVQARLRGIHETLAARGLAVRPVHqheGPATIAFG 243
Cdd:cd06271    88 RSD*PIGHAWVDIDNEAGAYEAVERLAGLGHRRIAFI-VPPARYSPHDRRLQGYVRA*RDAGLTGYPLD---ADTTLEAG 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 244 RASLRTIADSGPtRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVA-LAREIRPALTTMWVDTDAIGRKAARA 322
Cdd:cd06271   164 RAAAQRLLALSP-RPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSAPfLGAMITPPLTTVHAPIAEAGRELAKA 242


                  ....*.
gi 1370811475 323 LLDALE 328
Cdd:cd06271   243 LLARID 248
PBP1_FruR cd06274
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ...
 81-340 4.12e-15

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: 74.17  E-value: 4.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFELLDLHRVPYV 160
Cdd:cd06274     3 GLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAPSTPPDDIYYLCQAAGLPVV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 161 VTYAYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFA-IIMQPSADNdrVQARLRGIHETLAARGLAVRPVHQHEGPAT 239
Cdd:cd06274    83 FLDRPFSGSDAPSVVSDNRAGARALTEKLLAAGPGEIYfLGGRPELPS--TAERIRGFRAALAEAGITEGDDWILAEGYD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 240 IAFGRASLRTIADSGPTRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGrKA 319
Cdd:cd06274   161 RESGYQLMAELLARLGGLPQALFTSSLTLLEGVLRFLRERLGAIPSDLVLGTFDDHPLLDFLPNPVDSVRQDHDEIA-EH 239

                         250       260
                  ....*....|....*....|.
gi 1370811475 320 ARALLDALEHGAVGPGCAVLP 340
Cdd:cd06274   240 AFELLDALIEGQPEPGVIIIP 260
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
 77-334 4.55e-15

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: 74.47  E-value: 4.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  77 THITGAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVG------------EAY 144
Cdd:pfam00532   1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTpapsgdditakaEGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 145 PAEVFELLDLHRVPYVVTyayrddsphcCIGFDNRAAFARLTTHLLDLGHRDFAIIMQPSADNDRVQARLRGIHETLAAR 224
Cdd:pfam00532  81 GIPVIAADDAFDNPDGVP----------CVMPDDTQAGYESTQYLIAEGHKRPIAVMAGPASALTARERVQGFMAALAAA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 225 GLAVRPVHQHEGPATIAFGRASLRTIADSGPTrPTAVICGNDALALGALLEAQAMG---------IAVPAELSITGFDDV 295
Cdd:pfam00532 151 GREVKIYHVATGDNDIPDAALAANAMLVSHPT-IDAIVAMNDEAAMGAVRALLKQGrvkipdivgIGINSVVGFDGLSKA 229

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1370811475 296 ALAREIRPALTTMWVDTDAIGRKAARALLDALEHGAVGP 334
Cdd:pfam00532 230 QDTGLYLSPLTVIQLPRQLLGIKASDMVYQWIPKFREHP 268
PBP1_CcpB-like cd06286
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ...
 81-332 1.36e-14

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: 72.58  E-value: 1.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHG--ITLFLgcSNYDPA---QALAQVRAmlsRGVEAVSLVGEAYPAEVFElldlh 155
Cdd:cd06286     3 GVVVPYIDHPYFSQLINGIAEAAFKKGyqVLLLQ--TNYDKEkelRALELLKT---KQIDGLIITSRENDWEVIE----- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 156 rvPY-----VVTYAYRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIM-QPSADNDRVQARLRGIHETLAARGLAVR 229
Cdd:cd06286    73 --PYakygpIVLCEETDSPDIPSVYIDRYEAYLEALEYLKEKGHRKIGYCLgRPESSSASTQARLKAYQDVLGEHGLSLR 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 230 PVHQHEGPATIAFGRASLRTIADSGPtRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREirPALTTMW 309
Cdd:cd06286   151 EEWIFTNCHTIEDGYKLAKKLLALKE-RPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISEL--LNLTTID 227

                         250       260
                  ....*....|....*....|...
gi 1370811475 310 VDTDAIGRKAARALLDALEHGAV 332
Cdd:cd06286   228 QPLEEMGKEAFELLLSQLESKEP 250
LacI pfam00356
Bacterial regulatory proteins, lacI family;
24-66 1.42e-13

Bacterial regulatory proteins, lacI family;


Pssm-ID: 306791 [Multi-domain]  Cd Length: 46  Bit Score: 64.20  E-value: 1.42e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1370811475  24 DVAKLAGVSTATVSRVYNDPGKVSADVQQRVRDAARTLNWIPN 66
Cdd:pfam00356   4 DVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
PRK11303 PRK11303
catabolite repressor/activator;
22-191 5.59e-11

catabolite repressor/activator;


Pssm-ID: 236897 [Multi-domain]  Cd Length: 328  Bit Score: 62.97  E-value: 5.59e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  22 LGDVAKLAGVSTATVSRVYNdpGK-----VSADVQQRVRDAARTLNWIPNAAGRALASTRTHITGAIIPTLDDQVFASQV 96
Cdd:PRK11303    3 LDEIARLAGVSRTTASYVIN--GKakqyrVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSYARIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  97 AGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVsLVGEAYPAE--VFELLDLHRVPyVVTYAYRDDSPH-CC 173
Cdd:PRK11303   81 KYLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDAL-IVSTSLPPEhpFYQRLQNDGLP-IIALDRALDREHfTS 158

                         170
                  ....*....|....*...
gi 1370811475 174 IGFDNRAAFARLTTHLLD 191
Cdd:PRK11303  159 VVSDDQDDAEMLAESLLK 176
PBP1_CcpA_TTHA0807 cd06297
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ...
 173-347 1.24e-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: 61.33  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 173 CIGFDNRAAFARLTTHLLDLGHRD---FAIIMQPSADNDRVQARLRGIHETLAARGLAVRP---VHQHEGPAtiaFGRAS 246
Cdd:cd06297    93 CVYVDNVKGGFMATEYLAGLGEREyvfFGIEEDTVFTETVFREREQGFLEALNKAGRPISSsrmFRIDNSSK---KAECL 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 247 LRTIADSGPTrPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREirPALTTMWVDTDAIGRKAARALLDA 326
Cdd:cd06297   170 ARELLKKADN-PAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAAS--PGLTTVRQPVEEMGEAAAKLLLKR 246

                         170       180
                  ....*....|....*....|..
gi 1370811475 327 L-EHGAVGPGCAVLPELRVRES 347
Cdd:cd06297   247 LnEYGGPPRSLKFEPELIVRES 268
PBP1_hexuronate_repressor-like cd06272
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ...
 160-346 5.85e-10

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: 59.31  E-value: 5.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 160 VVTYAyRDDSPHCCIGFDNRAAFARLTTHLLDLGHRDFAIIMQPSAdNDRVQARLRGIHETLAARGLAVRPVHQHEGPAT 239
Cdd:cd06272    82 IVLYN-RESPKYSTVNVDNEKAGRLAVLLLIQKGHKSIAYIGNPNS-NRNQTLRGKGFIETCEKHGIHLSDSIIDSRGLS 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 240 IAFGRASLRTIADSgPTRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKA 319
Cdd:cd06272   160 IEGGDNAAKKLLKK-KTLPKAIFCNSDDIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLTVVGVPIEKIAEES 238

                         170       180
                  ....*....|....*....|....*...
gi 1370811475 320 ARALLDALEHGAVGPGCAVL-PELRVRE 346
Cdd:cd06272   239 LRLILKLIEGRENEIQQLILyPELIFRE 266
PBP1_XylR cd01543
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ...
 139-347 5.90e-08

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: 53.36  E-value: 5.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 139 LVGEAYPAEVFELLDLhRVPYVVTYAYRDDSPHCCIGFDNRAAfARL-TTHLLDLGHRDFAIImqpSADNDR-VQARLRG 216
Cdd:cd01543    55 IARLDDPELAEALRRL-GIPVVNVSGSRPEPGFPRVTTDNEAI-GRMaAEHLLERGFRHFAFC---GFRNAAwSRERGEG 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 217 IHETLAARGLAVR--PVHQHEGPATIAFGRASLRTIADSGPtRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDD 294
Cdd:cd01543   130 FREALREAGYECHvyESPPSGSSRSWEEEREELADWLKSLP-KPVGIFACNDDRARQVLEACREAGIRVPEEVAVLGVDN 208

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370811475 295 VALAREI-RPALTTMWVDTDAIGRKAARaLLDAL-EHGAVGPGCAVLPELRV--RES 347
Cdd:cd01543   209 DELICELsSPPLSSIALDAEQIGYEAAE-LLDRLmRGERVPPEPILIPPLGVvtRQS 264
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 81-332 6.93e-06

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: 47.23  E-value: 6.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEA--VSLVGEAYPAEVFELLDLHRVP 158
Cdd:COG1879    37 GFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAiiVSPVDPDALAPALKKAKAAGIP 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 159 yVVTY--AYRDDSPHCCIGFDNRAAfARLTTHLL--DLGHRDFAIIMQPSADNDRVQARLRGIHETLAARGlAVRPVHQH 234
Cdd:COG1879   117 -VVTVdsDVDGSDRVAYVGSDNYAA-GRLAAEYLakALGGKGKVAILTGSPGAPAANERTDGFKEALKEYP-GIKVVAEQ 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 235 EGPATIAFGRASLRTIADSGPtRPTAVICGNDALALGALLEAQAMGIAvpAELSITGFDDVALARE-IR--PALTTMWVD 311
Cdd:COG1879   194 YADWDREKALEVMEDLLQAHP-DIDGIFAANDGMALGAAQALKAAGRK--GDVKVVGFDGSPEALQaIKdgTIDATVAQD 270

                         250       260
                  ....*....|....*....|.
gi 1370811475 312 TDAIGRKAARALLDALEHGAV 332
Cdd:COG1879   271 PYLQGYLAVDAALKLLKGKEV 291
Periplasmic_Binding_Protein_type1 cd01391
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
 79-338 1.37e-05

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


Pssm-ID: 380477 [Multi-domain]  Cd Length: 280  Bit Score: 46.11  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  79 ITGAIIPTLD--DQVFASQ-VAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLVGEAYPAEVFE-LLDL 154
Cdd:cd01391     1 IIGVVTSSLHqiREQFGIQrVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGPGSSSVAIVIQnLAQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 155 HRVPYVVTYAYRDDSPHCCIG-------FDNRAAFARLTTHLLDLGHRDFAIIMQPSADNDRvqARLRGIHETLAARGLa 227
Cdd:cd01391    81 FDIPQLALDATSQDLSDKTLYkyflsvvFSDTLGARLGLDIVKRKNWTYVAAIHGEGLNSGE--LRMAGFKELAKQEGI- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 228 vRPVHQHEGPA-TIAFGRASLRTIADSGPtRPTAVICGNDALALGALLEAQAMGiaVPAELSITGFDDVALAREIR---- 302
Cdd:cd01391   158 -CIVASDKADWnAGEKGFDRALRKLREGL-KARVIVCANDMTARGVLSAMRRLG--LVGDVSVIGSDGWADRDEVGyeve 233

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1370811475 303 -PALTTMWVDTDAIGRKAARALLDALEHGAVGPGCAV 338
Cdd:cd01391   234 aNGLTTIKQQKMGFGITAIKAMADGSQNMHEEVWFDE 270
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
 81-223 1.37e-04

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: 42.94  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLV---GEAYPAEVFELLDLHrV 157
Cdd:cd01536     3 GVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIApvdSEALVPAVKKANAAG-I 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370811475 158 PYVV--TYAYRDDSPHCCIGFDNRAAFARLTTHLLD-LGHRDFAIIMQPSADNDRVQARLRGIHETLAA 223
Cdd:cd01536    82 PVVAvdTDIDGGGDVVAFVGTDNYEAGKLAGEYLAEaLGGKGKVAILEGPPGSSTAIDRTKGFKEALKK 150
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 83-328 7.09e-04

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


Pssm-ID: 433182 [Multi-domain]  Cd Length: 259  Bit Score: 40.76  E-value: 7.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  83 IIPTLDDQVFASQVAGMQAVMAEHGIT-LFLGCSNYDPAQALAQVRAMLSRGVEA--VSLVGEAYPAEVFELLDLHRVPy 159
Cdd:pfam13407   4 VPKSTGNPFFQAAEEGAEEAAKELGGEvIVVGPAEADAAEQVAQIEDAIAQGVDAiiVAPVDPTALAPVLKKAKDAGIP- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 160 VVTY-----AYRDDsphCCIGFDNRAAFARLTTHLLD-LGHRDFAIIMQPSADNDRVQARLRGIHETLAARGLAVRPVHQ 233
Cdd:pfam13407  83 VVTFdsdapSSPRL---AYVGFDNEAAGEAAGELLAEaLGGKGKVAILSGSPGDPNANERIDGFKKVLKEKYPGIKVVAE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 234 HEGPA-TIAFGRASLRTIADSGPTRPTAVICGNDALALGALLEAQAMGIAvpAELSITGFDDVALARE-IRPALTTMWVD 311
Cdd:pfam13407 160 VEGTNwDPEKAQQQMEALLTAYPNPLDGIISPNDGMAGGAAQALEAAGLA--GKVVVTGFDATPEALEaIKDGTIDATVL 237

                         250
                  ....*....|....*....
gi 1370811475 312 TDA--IGRKAARALLDALE 328
Cdd:pfam13407 238 QDPygQGYAAVELAAALLK 256
PBP1_ABC_ligand_binding-like cd06326
periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to ...
 117-255 7.42e-04

periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This group includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type transport systems that are predicted to be involved in the uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); its ligand specificity has not been determined experimentally, however.


Pssm-ID: 380549 [Multi-domain]  Cd Length: 339  Bit Score: 40.99  E-value: 7.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 117 YDPAQALAQVRAMLSR-GVEA-VSLVGEAYPAEVFELLDLHRVPYVVTYA-----YRDDSPHcciGFDNRAAFA----RL 185
Cdd:cd06326    51 YDPARTVENTRQLIEQdKVVAlFGYVGTANVEAVLPLLEEAGVPLVGPLTgadslREPGNPY---VFHVRASYAdeveKI 127

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370811475 186 TTHLLDLGHRDFAIIMQpsaDNDRVQARLRGIHETLAARGLAVrpvhqhegPATIAFGRAS------LRTIADSGP 255
Cdd:cd06326   128 VRHLATLGLKRIAVVYQ---DDPFGKEGLAAAEAALAARGLEP--------VATAAVARNAadvaaaAAALAAAKP 192
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
 81-222 9.29e-04

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


Pssm-ID: 380536 [Multi-domain]  Cd Length: 277  Bit Score: 40.33  E-value: 9.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  81 GAIIPTLDDQVFASQVAGMQAVMAEHGITLFLGCSNYDPAQALAQVRAMLSRGVEAVSLV---GEAYPAEVFELLDlHRV 157
Cdd:cd06313     3 GFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVpvdADALAPAVEKAKE-AGI 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370811475 158 PYVVTYAYRDDSPHCC-IGFDNRAAFARLTTHLLDL--GHRDFAIIMQPSADNDRVQaRLRGIHETLA 222
Cdd:cd06313    82 PLVGVNALIENEDLTAyVGSDDVVAGELEGQAVADRlgGKGNVVILEGPIGQSAQID-RGKGIENVLK 148
PRK10339 PRK10339
DNA-binding transcriptional repressor EbgR; Provisional
 22-345 1.51e-03

DNA-binding transcriptional repressor EbgR; Provisional


Pssm-ID: 182389 [Multi-domain]  Cd Length: 327  Bit Score: 40.13  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  22 LGDVAKLAGVSTATVSRVYN-DPG-KVSADVQQRVRDAARTLNWIPNAAGRALASTRTHITGAIIPT------LDDQVFA 93
Cdd:PRK10339    4 LKDIAIEAGVSLATVSRVLNdDPTlNVKEETKHRILEIAEKLEYKTSSARKLQTGAVNQHHILAIYSyqqeleINDPYYL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475  94 SQVAGMQAVMAEHGITLfLGCSNYDPAQALAQVRAMLsrgveavsLVGEAyPAEVFELLDLHRVPYVVTYAYRDDSPHCC 173
Cdd:PRK10339   84 AIRHGIETQCEKLGIEL-TNCYEHSGLPDIKNVTGIL--------IVGKP-TPALRAAASALTDNICFIDFHEPGSGYDA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 174 IGFDnraaFARLTTHLLDL----GHRDFAIIM---QPSADNDRVQA-----RLRGIhetlaarglaVRPVHQHEGPATIA 241
Cdd:PRK10339  154 VDID----LARISKEIIDFyinqGVNRIGFIGgedEPGKADIREVAfaeygRLKQV----------VREEDIWRGGFSSS 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370811475 242 FG-RASLRTIADSgpTRPTAVICGNDALALGALLEAQAMGIAVPAELSITGFDDVALAREIRPALTTMWVDTDAIGRKAA 320
Cdd:PRK10339  220 SGyELAKQMLARE--DYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGV 297

                         330       340
                  ....*....|....*....|....*.
gi 1370811475 321 RALLDALEHGAVGPGCAVLP-ELRVR 345
Cdd:PRK10339  298 NLLYEKARDGRALPLLVFVPsKLKLR 323
 
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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