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Conserved domains on  [gi|931497206|gb|KPK76671|]
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hypothetical protein AMJ79_05845 [Phycisphaerae bacterium SM23_30]

Protein Classification

XylR family transcriptional regulator( domain architecture ID 11546740)

XylR family transcriptional regulator similar to xylose operon transcription regulator XylR, a DNA transcription repressor that regulates the xylBAFGHR operon and contains an N-terminal periplasmic-binding protein (PBP) fold ligand binding domain and a C-terminal AraC-like DNA binding domain

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP1_XylR cd01543
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ...
3-267 1.26e-134

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: 385.02  E-value: 1.26e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206   3 RVILMIETSRAFGRGLLYGIARYSRIHGPWVFYREPGGLEKSLPDLKNWGADGIIMRNTPKSDV--LSELNLPTILVIHG 80
Cdd:cd01543    1 RVALLLETSRGYGRRLLRGIARYAREHGPWSLYLEPPGYEELLDLLKGWKGDGIIARLDDPELAeaLRRLGIPVVNVSGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  81 KEKKSYyPRIITDGEQIGRMAARHFLDRGFRHFAYCGFDDTSWSQQRCIYFVKTVIQAGFKPHIYQQPKSRVKQCWKNEQ 160
Cdd:cd01543   81 RPEPGF-PRVTTDNEAIGRMAAEHLLERGFRHFAFCGFRNAAWSRERGEGFREALREAGYECHVYESPPSGSSRSWEEER 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 161 VIMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVAVIGVDNDELVCDLSDPPLTSIALNTEKAGYEAAKLLD 240
Cdd:cd01543  160 EELADWLKSLPKPVGIFACNDDRARQVLEACREAGIRVPEEVAVLGVDNDELICELSSPPLSSIALDAEQIGYEAAELLD 239
                        250       260
                 ....*....|....*....|....*..
gi 931497206 241 RLMTQKKKKTRkDIMVRPINIVTRQST 267
Cdd:cd01543  240 RLMRGERVPPE-PILIPPLGVVTRQST 265
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
292-374 3.15e-19

helix_turn_helix, arabinose operon control protein;


:

Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 81.45  E-value: 3.15e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206   292 IRVNDVADASGLSRRVLEKRFRKILNRSVYEEIRRVRIAQVCQMLVETTISISEIALVLGYPGVEHIARYFRKEKGKSLL 371
Cdd:smart00342   2 LTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPS 81

                   ...
gi 931497206   372 AYR 374
Cdd:smart00342  82 EYR 84
 
Name Accession Description Interval E-value
PBP1_XylR cd01543
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ...
3-267 1.26e-134

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: 385.02  E-value: 1.26e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206   3 RVILMIETSRAFGRGLLYGIARYSRIHGPWVFYREPGGLEKSLPDLKNWGADGIIMRNTPKSDV--LSELNLPTILVIHG 80
Cdd:cd01543    1 RVALLLETSRGYGRRLLRGIARYAREHGPWSLYLEPPGYEELLDLLKGWKGDGIIARLDDPELAeaLRRLGIPVVNVSGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  81 KEKKSYyPRIITDGEQIGRMAARHFLDRGFRHFAYCGFDDTSWSQQRCIYFVKTVIQAGFKPHIYQQPKSRVKQCWKNEQ 160
Cdd:cd01543   81 RPEPGF-PRVTTDNEAIGRMAAEHLLERGFRHFAFCGFRNAAWSRERGEGFREALREAGYECHVYESPPSGSSRSWEEER 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 161 VIMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVAVIGVDNDELVCDLSDPPLTSIALNTEKAGYEAAKLLD 240
Cdd:cd01543  160 EELADWLKSLPKPVGIFACNDDRARQVLEACREAGIRVPEEVAVLGVDNDELICELSSPPLSSIALDAEQIGYEAAELLD 239
                        250       260
                 ....*....|....*....|....*..
gi 931497206 241 RLMTQKKKKTRkDIMVRPINIVTRQST 267
Cdd:cd01543  240 RLMRGERVPPE-PILIPPLGVVTRQST 265
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
104-267 2.05e-35

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: 127.45  E-value: 2.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  104 HFLDRGFRHFAYCGF---DDTSWSQQRCIYFVKTVIQAGFKPHIYQQPKSRVKqcwknEQVIMADWLKSL-PKPVGLMAC 179
Cdd:pfam13377   1 HLAELGHRRIALIGPegdRDDPYSDLRERGFREAARELGLDVEPTLYAGDDEA-----EAAAARERLRWLgALPTAVFVA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  180 NDDRGQHALEACKMAGLQVPEEVAVIGVDNDELvCDLSDPPLTSIALNTEKAGYEAAKLLDRLMTQKKKKTRKDIMvrPI 259
Cdd:pfam13377  76 NDEVALGVLQALREAGLRVPEDLSVIGFDDSPL-AALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLL--PP 152

                  ....*...
gi 931497206  260 NIVTRQST 267
Cdd:pfam13377 153 ELVEREST 160
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
18-267 8.29e-33

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 125.31  E-value: 8.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  18 LLYGIARYSRIHGPWVF----YREPGGLEKSLPDLKNWGADGIIM----RNTPKSDVLSELNLPTILV---IHGKEkksy 86
Cdd:COG1609   79 LLRGIEEAARERGYQLLlansDEDPEREREALRLLLSRRVDGLILagsrLDDARLERLAEAGIPVVLIdrpLPDPG---- 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  87 YPRIITDGEQIGRMAARHFLDRGFRHFAY-CGFDDTSWSQQRCIYFVKTVIQAGFKPHiyqqPKSRVKQCWKNE--QVIM 163
Cdd:COG1609  155 VPSVGVDNRAGARLATEHLIELGHRRIAFiGGPADSSSARERLAGYREALAEAGLPPD----PELVVEGDFSAEsgYEAA 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 164 ADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVAVIGVDNDELvCDLSDPPLTSIALNTEKAGYEAAKLLDRLM 243
Cdd:COG1609  231 RRLLARGPRPTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPL-ARYLTPPLTTVRQPIEEMGRRAAELLLDRI 309
                        250       260
                 ....*....|....*....|....
gi 931497206 244 TQKKKKTRKDIMvrPINIVTRQST 267
Cdd:COG1609  310 EGPDAPPERVLL--PPELVVREST 331
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
292-374 3.15e-19

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 81.45  E-value: 3.15e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206   292 IRVNDVADASGLSRRVLEKRFRKILNRSVYEEIRRVRIAQVCQMLVETTISISEIALVLGYPGVEHIARYFRKEKGKSLL 371
Cdd:smart00342   2 LTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPS 81

                   ...
gi 931497206   372 AYR 374
Cdd:smart00342  82 EYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
292-377 7.38e-19

AraC-type DNA-binding domain and AraC-containing proteins [Transcription];


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 85.22  E-value: 7.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 292 IRVNDVADASGLSRRVLEKRFRKILNRSVYEEIRRVRIAQVCQMLVETTISISEIALVLGYPGVEHIARYFRKEKGKSLL 371
Cdd:COG2207  169 LTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPS 248

                 ....*.
gi 931497206 372 AYRKEY 377
Cdd:COG2207  249 EYRKRL 254
HTH_18 pfam12833
Helix-turn-helix domain;
297-375 6.77e-17

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 74.93  E-value: 6.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  297 VADASGLSRRVLEKRFRKILNRSVYEEIRRVRIAQVCQMLVETT-ISISEIALVLGYPGVEHIARYFRKEKGKSLLAYRK 375
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDTgLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
PRK10703 PRK10703
HTH-type transcriptional repressor PurR;
54-266 2.31e-11

HTH-type transcriptional repressor PurR;


Pssm-ID: 236739 [Multi-domain]  Cd Length: 341  Bit Score: 64.36  E-value: 2.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  54 DGI-IMRNTPKSDVLSEL----NLPTILVIHGKEKKSYYPRIITDGEQIGRMAARHFLDRGFRHFAY-CGFDDTSWSQQR 127
Cdd:PRK10703 117 DGLlVMCSEYPEPLLAMLeeyrHIPMVVMDWGEAKADFTDAIIDNAFEGGYLAGRYLIERGHRDIGViPGPLERNTGAGR 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 128 CIYFVKTVIQAGFKPH---IYQ---QPKSRVKQcwkneqviMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEE 201
Cdd:PRK10703 197 LAGFMKAMEEANIKVPeewIVQgdfEPESGYEA--------MQQILSQKHRPTAVFCGGDIMAMGAICAADEMGLRVPQD 268
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931497206 202 VAVIGVDNDElVCDLSDPPLTSIALNTEKAGYEAAK-LLDRLmtQKKKKTRKDIMVRPiNIVTRQS 266
Cdd:PRK10703 269 ISVIGYDNVR-NARYFTPALTTIHQPKDRLGETAFNmLLDRI--VNKREEPQTIEVHP-RLVERRS 330
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
281-374 4.72e-08

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 50.69  E-value: 4.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 281 VRFIRKNSRKTIRVNDVADASGLSRRVLEKRFRKILNRSVYEEIRRVRIAQVCQMLVETTISISEIALVLGYPGVEHIAR 360
Cdd:PRK10219  11 IAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYVSQQTFSR 90
                         90
                 ....*....|....
gi 931497206 361 YFRKEKGKSLLAYR 374
Cdd:PRK10219  91 VFRRQFDRTPSDYR 104
 
Name Accession Description Interval E-value
PBP1_XylR cd01543
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ...
3-267 1.26e-134

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: 385.02  E-value: 1.26e-134
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206   3 RVILMIETSRAFGRGLLYGIARYSRIHGPWVFYREPGGLEKSLPDLKNWGADGIIMRNTPKSDV--LSELNLPTILVIHG 80
Cdd:cd01543    1 RVALLLETSRGYGRRLLRGIARYAREHGPWSLYLEPPGYEELLDLLKGWKGDGIIARLDDPELAeaLRRLGIPVVNVSGS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  81 KEKKSYyPRIITDGEQIGRMAARHFLDRGFRHFAYCGFDDTSWSQQRCIYFVKTVIQAGFKPHIYQQPKSRVKQCWKNEQ 160
Cdd:cd01543   81 RPEPGF-PRVTTDNEAIGRMAAEHLLERGFRHFAFCGFRNAAWSRERGEGFREALREAGYECHVYESPPSGSSRSWEEER 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 161 VIMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVAVIGVDNDELVCDLSDPPLTSIALNTEKAGYEAAKLLD 240
Cdd:cd01543  160 EELADWLKSLPKPVGIFACNDDRARQVLEACREAGIRVPEEVAVLGVDNDELICELSSPPLSSIALDAEQIGYEAAELLD 239
                        250       260
                 ....*....|....*....|....*..
gi 931497206 241 RLMTQKKKKTRkDIMVRPINIVTRQST 267
Cdd:cd01543  240 RLMRGERVPPE-PILIPPLGVVTRQST 265
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
104-267 2.05e-35

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: 127.45  E-value: 2.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  104 HFLDRGFRHFAYCGF---DDTSWSQQRCIYFVKTVIQAGFKPHIYQQPKSRVKqcwknEQVIMADWLKSL-PKPVGLMAC 179
Cdd:pfam13377   1 HLAELGHRRIALIGPegdRDDPYSDLRERGFREAARELGLDVEPTLYAGDDEA-----EAAAARERLRWLgALPTAVFVA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  180 NDDRGQHALEACKMAGLQVPEEVAVIGVDNDELvCDLSDPPLTSIALNTEKAGYEAAKLLDRLMTQKKKKTRKDIMvrPI 259
Cdd:pfam13377  76 NDEVALGVLQALREAGLRVPEDLSVIGFDDSPL-AALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLL--PP 152

                  ....*...
gi 931497206  260 NIVTRQST 267
Cdd:pfam13377 153 ELVEREST 160
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
18-267 8.29e-33

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 125.31  E-value: 8.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  18 LLYGIARYSRIHGPWVF----YREPGGLEKSLPDLKNWGADGIIM----RNTPKSDVLSELNLPTILV---IHGKEkksy 86
Cdd:COG1609   79 LLRGIEEAARERGYQLLlansDEDPEREREALRLLLSRRVDGLILagsrLDDARLERLAEAGIPVVLIdrpLPDPG---- 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  87 YPRIITDGEQIGRMAARHFLDRGFRHFAY-CGFDDTSWSQQRCIYFVKTVIQAGFKPHiyqqPKSRVKQCWKNE--QVIM 163
Cdd:COG1609  155 VPSVGVDNRAGARLATEHLIELGHRRIAFiGGPADSSSARERLAGYREALAEAGLPPD----PELVVEGDFSAEsgYEAA 230
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 164 ADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVAVIGVDNDELvCDLSDPPLTSIALNTEKAGYEAAKLLDRLM 243
Cdd:COG1609  231 RRLLARGPRPTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPL-ARYLTPPLTTVRQPIEEMGRRAAELLLDRI 309
                        250       260
                 ....*....|....*....|....
gi 931497206 244 TQKKKKTRKDIMvrPINIVTRQST 267
Cdd:COG1609  310 EGPDAPPERVLL--PPELVVREST 331
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
48-255 1.19e-29

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: 114.92  E-value: 1.19e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  48 LKNWGADGIIM----RNTPKSDVLSELNLPTILvIHGKEKKSYYPRIITDGEQIGRMAARHFLDRGFRHFAY-CGFDDTS 122
Cdd:cd06267   51 LLSRRVDGIILapssLDDELLEELLAAGIPVVL-IDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFiGGPLDLS 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 123 WSQQRCIYFVKTVIQAGFKPhiyqqPKSRVKQCWKNEQ---VIMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVP 199
Cdd:cd06267  130 TSRERLEGYRDALAEAGLPV-----DPELVVEGDFSEEsgyEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVP 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 931497206 200 EEVAVIGVDNDELvCDLSDPPLTSIALNTEKAGYEAAKLLDRLMTQKKKKTRKDIM 255
Cdd:cd06267  205 EDISVVGFDDIPL-AALLTPPLTTVRQPAYEMGRAAAELLLERIEGEEEPPRRIVL 259
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
54-266 5.29e-27

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: 107.99  E-value: 5.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  54 DGIIM-RNTPKSDVLSELNLPTILVihGKEKKSYYPRIITDGEQIGRMAARHFLDRGFRHFAY-CGFDDTSWSQQRCIYF 131
Cdd:cd06291   57 DGIILgSHSLDIEEYKKLNIPIVSI--DRYLSEGIPSVSSDNYQGGRLAAEHLIEKGCKKILHiGGPSNNSPANERYRGF 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 132 VKTVIQAGFKPHIYQQPKSRVKQcwKNEQVIMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVAVIGVDNDE 211
Cdd:cd06291  135 EDALKEAGIEYEIIEIDENDFSE--EDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIE 212
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 931497206 212 LvCDLSDPPLTSIALNTEKAGYEAAKLLDRLMTQKKKKTRKDIMvrPINIVTRQS 266
Cdd:cd06291  213 I-SELLYPELTTIRQPIEEMAKEAVELLLKLIEGEEIEESRIVL--PVELIERET 264
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
42-258 6.65e-23

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: 96.44  E-value: 6.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  42 EKSLPDLKNWGADGIIMRNTPKSD----VLSELNLPTILV---IHGKEkksyYPRIITDGEQIGRMAARHFLDRGFRHFA 114
Cdd:cd19977   45 KKYIEMLRAKQVDGIIIAPTGGNEdlieKLVKSGIPVVFVdryIPGLD----VDTVVVDNFKGAYQATEHLIELGHKRIA 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 115 YCGFD-DTSWSQQRCIYFVKTVIQAGFKphiyqQPKSRVKQCWKNEQVI--MADWLKSLPKPVGLMACNDDRGQHALEAC 191
Cdd:cd19977  121 FITYPlELSTRQERLEGYKAALADHGLP-----VDEELIKHVDRQDDVRkaISELLKLEKPPDAIFAANNLITLEVLKAI 195
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931497206 192 KMAGLQVPEEVAVIGVDnDELVCDLSDPPLTSIALNTEKAGYEAAKLLDRLMTQKKKKTRKDIMVRP 258
Cdd:cd19977  196 KELGLRIPDDIALIGFD-DIPWADLFNPPLTVIAQPTYEIGRKAAELLLDRIENKPKGPPRQIVLPT 261
PBP1_DegA_Like cd19976
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
48-266 1.47e-22

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: 95.78  E-value: 1.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  48 LKNWGADGIIM-----RNTPKSDVLSELNLPTILVIHGKEKKSYYpRIITDGEQIGRMAARHFLDRGFRHFAYCGFDDTS 122
Cdd:cd19976   51 LKERNVDGIIIassniSDEAIIKLLKEEKIPVVVLDRYIEDNDSD-SVGVDDYRGGYEATKYLIELGHTRIGCIVGPPST 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 123 WS-QQRciyfVKTVIQAgFKPHIYQQPKSRVKQCW--KNEQVIMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVP 199
Cdd:cd19976  130 YNeHER----IEGYKNA-LQDHNLPIDESWIYSGEssLEGGYKAAEELLKSKNPTAIFAGNDLIAMGVYRAALELGLKIP 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931497206 200 EEVAVIGVDNDELvCDLSDPPLTSIALNTEKAGYEAAKLLDRLMTQKKKKTRKDIMvrPINIVTRQS 266
Cdd:cd19976  205 EDLSVIGFDNIIL-SEYITPALTTIAQPIFEMGQEAAKLLLKIIKNPAKKKEEIVL--PPELIKRDS 268
PBP1_sucrose_transcription_regulator cd06288
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ...
52-266 2.47e-21

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


Pssm-ID: 380511 [Multi-domain]  Cd Length: 268  Bit Score: 92.23  E-value: 2.47e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  52 GADGII---MRNTPKSDVLSELNLPTILViHGKEKKSYYPRIITDGEQIGRMAARHFLDRGFRHFAYCGFDDTSW-SQQR 127
Cdd:cd06288   56 RVDGIIyasMHHREVTLPPELTDIPLVLL-NCFDDDPSLPSVVPDDEQGGYLATRHLIEAGHRRIAFIGGPEDSLaTRLR 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 128 CIYFVKTVIQAGFKPhiyqqPKSRVKQC-WKNEQ--VIMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVAV 204
Cdd:cd06288  135 LAGYRAALAEAGIPY-----DPSLVVHGdWGRESgyEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSV 209
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931497206 205 IGVDNDELVCDLsDPPLTSIALNTEKAGYEAAKLLDRLMTQKKKKTRKdIMVrPINIVTRQS 266
Cdd:cd06288  210 VGFDNQELAAYL-RPPLTTVALPYYEMGRRAAELLLDGIEGEPPEPGV-IRV-PCPLIERES 268
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
52-267 2.82e-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: 380508 [Multi-domain]  Cd Length: 269  Bit Score: 89.21  E-value: 2.82e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  52 GADGIIMRNTP-KSDVLSEL---NLPTILVIHGKEKKSYyPRIITDGEQIGRMAARHFLDRGFRHFAY-CGFDDTSWSQQ 126
Cdd:cd06285   55 RVDGLIITPARdDAPDLQELaarGVPVVLVDRRIGDTAL-PSVTVDNELGGRLATRHLLELGHRRIAVvAGPLNASTGRD 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 127 RCIYFVKTVIQAG---FKPHIYQQPKSRVKqcwknEQVIMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVA 203
Cdd:cd06285  134 RLRGYRRALAEAGlpvPDERIVPGGFTIEA-----GREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLS 208
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931497206 204 VIGVDNDELVcDLSDPPLTSIALNTEKAGYEAAKLLDRLMTQKKKKTRkdIMVRPINIVTRQST 267
Cdd:cd06285  209 VVGFDDIPLA-AFLPPPLTTVRQPKYEMGRRAAELLLQLIEGGGRPPR--SITLPPELVVREST 269
PBP1_LacI-like cd19974
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
42-266 3.99e-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: 89.15  E-value: 3.99e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  42 EKSLPD-LKNWGADGII-MRNTPKS--DVLSELNLPTILVIHgkekksYYPR-----IITDGEQIGRMAARHFLDRGFRH 112
Cdd:cd19974   47 ELNLPSiISEEKVDGIIiLGEISKEylEKLKELGIPVVLVDH------YDEElnadsVLSDNYYGAYKLTSYLIEKGHKK 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 113 FAYCGFDDTSWS-QQRCIYFVKTVIQAGfkphIYQQPKSrvkqCWKNEQVIMADWLKSLPKPVGLM-----ACNDDRGQH 186
Cdd:cd19974  121 IGFVGDINYTSSfMDRYLGYRKALLEAG----LPPEKEE----WLLEDRDDGYGLTEEIELPLKLMlptafVCANDSIAI 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 187 AL-EACKMAGLQVPEEVAVIGVDNDELvCDLSDPPLTSIALNTEKAGYEAAKLLDRLMTQKKKKTRKdIMVRPiNIVTRQ 265
Cdd:cd19974  193 QLiKALKEKGYRVPEDISVVGFDNIEL-AELSTPPLTTVEVDKEAMGRRAVEQLLWRIENPDRPFEK-ILVSG-KLIERD 269

                 .
gi 931497206 266 S 266
Cdd:cd19974  270 S 270
PBP1_MalR-like cd06294
ligand-binding domain of maltose transcription regulator MalR which is a member of the ...
54-256 1.92e-19

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: 86.87  E-value: 1.92e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  54 DGIIMRNTPKSDV----LSELNLPTILVihGK-EKKSYYPRIITDGEQIGRMAARHFLDRGFRHFAYCGFD-DTSWSQQR 127
Cdd:cd06294   62 DGFILLYSKEDDPlieyLKEEGFPFVVI--GKpLDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDkNLVVSIDR 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 128 CIYFVKTVIQAGFKPH---IYQQPKSRvkqcwKNEQVIMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVAV 204
Cdd:cd06294  140 LQGYKQALKEAGLPLDddyILLLDFSE-----EDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSI 214
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 931497206 205 IGVDNDELvCDLSDPPLTSIALNTEKAGYEAAKLLDRLMtQKKKKTRKDIMV 256
Cdd:cd06294  215 ISFNNSPL-AELASPPLTSVDINPYELGREAAKLLINLL-EGPESLPKNVIV 264
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
48-255 2.42e-19

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: 86.82  E-value: 2.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  48 LKNWGADGIIMRNT-PKSDVLSELN--LPTILVIHGKEKKSYyPRIITDGEQIGRMAARHFLDRGFRHFAYCGFDDTS-W 123
Cdd:cd06284   51 LRSRRVDGVILLSGrLDAELLSELSkrYPIVQCCEYIPDSGV-PSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDNvY 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 124 SQQRCIYFVKTVIQAG-FKPHIYQQP-----KSRVKqcwkneqvIMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQ 197
Cdd:cd06284  130 ARERLEGYRRALAEAGlPVDEDLIIEgdfsfEAGYA--------AARALLALPERPTAIFCASDELAIGAIKALRRAGLR 201
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 931497206 198 VPEEVAVIGVDNDELvCDLSDPPLTSIALNTEKAGYEAAKLLDRLMTQKKKKTRKDIM 255
Cdd:cd06284  202 VPEDVSVIGFDDIEF-AEMFSPSLTTIRQPRYEIGETAAELLLEKIEGEGVPPEHIIL 258
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
93-266 2.79e-19

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: 86.39  E-value: 2.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  93 DGEQIGRMAARHFLDRGFRHFAYCGFDDTSWS--QQRCIYFVKTVIQAGFKPH---IYQQPKS----RvkqcwkneqVIM 163
Cdd:cd01575   99 SNFAAGRAMARHLIERGYRRIAFVGARLDGDSraRQRLEGFRDALAEAGLPLPlvlLVELPSSfalgR---------EAL 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 164 ADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVAVIGVDNDELVCDLSdPPLTSIALNTEKAGYEAAK-LLDRL 242
Cdd:cd01575  170 AELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALP-PALTTVRVPRYEIGRKAAElLLARL 248
                        170       180
                 ....*....|....*....|....
gi 931497206 243 mtQKKKKTRKDIMVrPINIVTRQS 266
Cdd:cd01575  249 --EGEEPEPRVVDL-GFELVRRES 269
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
292-374 3.15e-19

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 81.45  E-value: 3.15e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206   292 IRVNDVADASGLSRRVLEKRFRKILNRSVYEEIRRVRIAQVCQMLVETTISISEIALVLGYPGVEHIARYFRKEKGKSLL 371
Cdd:smart00342   2 LTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPS 81

                   ...
gi 931497206   372 AYR 374
Cdd:smart00342  82 EYR 84
PBP1_CcpA-like cd19975
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
4-266 4.63e-19

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: 86.07  E-value: 4.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206   4 VILMIETSRAFGRgLLYGIARYSRIHGPWVF----YREPGGLEKSLPDLKNWGADGII-MRNTPKSD---VLSELNLPTI 75
Cdd:cd19975    4 VIIPDISNSFFAE-ILKGIEDEARENGYSVIlcntGSDEEREKKYLQLLKEKRVDGIIfASGTLTEEnkqLLKNMNIPVV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  76 LVIHgKEKKSYYPRIITDGEQIGRMAARHFLDRGFRHFAYCG--FDDTSWSQQRCIYFVKTVIQAG--FKPHIYQQPKSR 151
Cdd:cd19975   83 LVST-ESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISgpLDDPNAGYPRYEGYKKALKDAGlpIKENLIVEGDFS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 152 VKQCWKNeqviMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVAVIGVDNDELvCDLSDPPLTSIALNTEKA 231
Cdd:cd19975  162 FKSGYQA----MKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEI-AEMSIPPLTTVSQPFYEM 236
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 931497206 232 GYEAAKLLDRLMTQKKKKTRKDIMvrPINIVTRQS 266
Cdd:cd19975  237 GKKAVELLLDLIKNEKKEEKSIVL--PHQIIERES 269
PBP1_LacI cd01574
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ...
5-266 4.89e-19

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: 85.71  E-value: 4.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206   5 ILMIETSRaFG-RGLLYGIARYSRIHGpwvfY---------REPGGLEKSLPDLKNWGADGIIMrNTPKSDVLSEL---- 70
Cdd:cd01574    4 VIATGLSL-YGpASTLAGIERAARERG----YsvsiatvdeDDPASVREALDRLLSQRVDGIIV-IAPDEAVLEALrrlp 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  71 -NLPTILVIHGKEKKsyYPRIITDGEQIGRMAARHFLDRGFRHFAY-CGfdDTSW--SQQRCIYFVKTVIQAGFKPHIyq 146
Cdd:cd01574   78 pGLPVVIVGSGPSPG--VPTVSIDQEEGARLATRHLLELGHRRIAHiAG--PLDWvdARARLRGWREALEEAGLPPPP-- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 147 qpksrvkqcwkneqVIMADW-----------LKSLPKPVGLMACNDD--RGqhALEACKMAGLQVPEEVAVIGVDnDELV 213
Cdd:cd01574  152 --------------VVEGDWsaasgyragrrLLDDGPVTAVFAANDQmaLG--ALRALHERGLRVPEDVSVVGFD-DIPE 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 931497206 214 CDLSDPPLTSIALNTEKAGYEAAKLLDRLMtQKKKKTRKDIMVRPiNIVTRQS 266
Cdd:cd01574  215 AAYFVPPLTTVRQDFAELGRRAVELLLALI-EGPAPPPESVLLPP-ELVVRES 265
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
292-377 7.38e-19

AraC-type DNA-binding domain and AraC-containing proteins [Transcription];


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 85.22  E-value: 7.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 292 IRVNDVADASGLSRRVLEKRFRKILNRSVYEEIRRVRIAQVCQMLVETTISISEIALVLGYPGVEHIARYFRKEKGKSLL 371
Cdd:COG2207  169 LTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPS 248

                 ....*.
gi 931497206 372 AYRKEY 377
Cdd:COG2207  249 EYRKRL 254
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
52-257 5.35e-18

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: 82.99  E-value: 5.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  52 GADGIIM------RNTPKSDV---LSELNLPTILvIHgkekkSYY-----PRIITDGEQIGRMAARHFLDRGFRHFA-YC 116
Cdd:cd01541   55 NVDGLIIeptksaLPNPNLDLyeeLQKKGIPVVF-IN-----SYYpeldaPSVSLDDEKGGYLATKHLIDLGHRRIAgIF 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 117 GFDDTSwSQQRCIYFVKTVIQAGfkphiYQQPKSRVkqCW-KNEQVIMAD-------WLKSLPKPVGLMACNDDRGQHAL 188
Cdd:cd01541  129 KSDDLQ-GVERYQGFIKALREAG-----LPIDDDRI--LWySTEDLEDRFfaeelreFLRRLSRCTAIVCYNDEIALRLI 200
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931497206 189 EACKMAGLQVPEEVAVIGVDNDELvCDLSDPPLTSIALNTEKAGYEAAKLLDRLMTQKKKKTRK----DIMVR 257
Cdd:cd01541  201 QALREAGLRVPEDLSVVGFDDSYL-ASLSEPPLTSVVHPKEELGRKAAELLLRMIEEGRKPESVifppELIER 272
PBP1_AglR-like cd20010
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ...
53-243 9.83e-18

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: 82.21  E-value: 9.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  53 ADGII----MRNTPKSDVLSELNLPtiLVIHGK-EKKSYYPRIITDGEQIGRMAARHFLDRGFRHFAYC-GFDDTSWSQQ 126
Cdd:cd20010   60 VDGFIlartRVNDPRIAYLLERGIP--FVVHGRsESGAPYAWVDIDNEGAFRRATRRLLALGHRRIALLnGPEELNFAHQ 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 127 RCIYFVKTVIQAGFKP---HIYQQPKSRVkqcwkNEQVIMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVA 203
Cdd:cd20010  138 RRDGYRAALAEAGLPVdpaLVREGPLTEE-----GGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVS 212
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 931497206 204 VIGVDNDELVCDLSDPPLTSIALNTEKAGYEAAKLLDRLM 243
Cdd:cd20010  213 VIGHDDLLPALEYFSPPLTTTRSSLRDAGRRLAEMLLALI 252
PBP1_GalR cd01544
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ...
34-266 4.33e-17

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: 80.26  E-value: 4.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  34 FYREPGGLEKSLPDLknwgaDGIIM--RNTPKS-DVLSELNlPTILVIHGKEKKSYYPRIITDGEQIGRMAARHFLDRGF 110
Cdd:cd01544   40 IFRDDEDLESLLEKV-----DGIIAigKFSKEEiEKLKKLN-PNIVFVDSNPDPDGFDSVVPDFEQAVRQALDYLIELGH 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 111 RHFAYCGFDDTSWSQQ------RCIYFVKTVIQAGFkphiyqQPKSRVKQCWKNEQV---IMADWLKSLPKPVGLMACND 181
Cdd:cd01544  114 RRIGFIGGKEYTSDDGeeiedpRLRAFREYMKEKGL------YNEEYIYIGEFSVESgyeAMKELLKEGDLPTAFFVASD 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 182 --DRGqhALEACKMAGLQVPEEVAVIGVDNDELVCDLSdPPLTSIALNTEKAGYEAAKLLDRLMTQKKKKTRKdIMVrPI 259
Cdd:cd01544  188 pmAIG--ALRALQEAGIKVPEDISIISFNDIEVAKYVT-PPLTTVHIPTEEMGRTAVRLLLERINGGRTIPKK-VLL-PT 262

                 ....*..
gi 931497206 260 NIVTRQS 266
Cdd:cd01544  263 KLIERES 269
HTH_18 pfam12833
Helix-turn-helix domain;
297-375 6.77e-17

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 74.93  E-value: 6.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  297 VADASGLSRRVLEKRFRKILNRSVYEEIRRVRIAQVCQMLVETT-ISISEIALVLGYPGVEHIARYFRKEKGKSLLAYRK 375
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDTgLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
PBP1_GalS-like cd06270
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ...
14-255 9.44e-17

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: 79.10  E-value: 9.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  14 FGRgLLYGIARYSRIHGPWVF----YREPGGLEKSLPDLKNWGADGIIM--RNTPKSDV--LSELNLPTILV---IHGKE 82
Cdd:cd06270   14 FGS-LLKGAERVARAHGKQLLitsgHHDAEEEREAIEFLLDRRCDAIILhsRALSDEELilIAEKIPPLVVInryIPGLA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  83 KKSYYPriitDGEQIGRMAARHFLDRGFRHFAY-CGFDDTSWSQQRCIYFVKTVIQAGFKPhiyqqpksrvkqcwKNEQV 161
Cdd:cd06270   93 DRCVWL----DNEQGGRLAAEHLLDLGHRRIACiTGPLDIPDARERLAGYRDALAEAGIPL--------------DPSLI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 162 IMADW------------LKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVAVIGVDNDELvCDLSDPPLTSIALNTE 229
Cdd:cd06270  155 IEGDFtieggyaaakqlLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPL-ARYLSPKLTTVHYPIE 233
                        250       260
                 ....*....|....*....|....*.
gi 931497206 230 KAGYEAAKLLDRLMTQKKKKTRKDIM 255
Cdd:cd06270  234 EMAQAAAELALNLAYGEPLPISHEFT 259
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
52-255 1.07e-16

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: 79.15  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  52 GADGIIM---RNTPKSDV--LSELNLPTILV---IHGKEkksyYPRIITDGEQIGRMAARHFLDRGFRHFAYCG-FDDTS 122
Cdd:cd06289   55 GVDGLILspaAGTTAELLrrLKAWGIPVVLAlrdVPGSD----LDYVGIDNRLGAQLATEHLIALGHRRIAFLGgLSDSS 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 123 WSQQRCIYFVKTVIQAGFKP---HIYQQPKSRvkqcwKNEQVIMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVP 199
Cdd:cd06289  131 TRRERLAGFRAALAEAGLPLdesLIVPGPATR-----EAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPG 205
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 931497206 200 EEVAVIGVDNDELvCDLSDPPLTSIALNTEKAGYEAAKLLDRLMTQKKKKTRKDIM 255
Cdd:cd06289  206 RDIAVVGFDDVPE-AALWTPPLTTVSVHPREIGRRAARLLLRRIEGPDTPPERIII 260
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
270-377 1.13e-16

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 79.82  E-value: 1.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 270 LSIEDKEVAEAVRFIRKNSRKTIRVNDVADASGLSRRVLEKRFRKILNRSVYEEIRRVRIAQVCQMLVETTISISEIALV 349
Cdd:COG4977  205 LGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAA 284
                         90       100
                 ....*....|....*....|....*...
gi 931497206 350 LGYPGVEHIARYFRKEKGKSLLAYRKEY 377
Cdd:COG4977  285 CGFGSASHFRRAFRRRFGVSPSAYRRRF 312
PBP1_CelR cd06295
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ...
52-266 1.08e-15

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: 76.52  E-value: 1.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  52 GADGIIM----RNTPKSDVLSELNLPTIlVIHGKEKKSYYPRIITDGEQIGRMAARHFLDRGFRHFAYCGFDDTSWSQQR 127
Cdd:cd06295   63 RADGLIVlgqgLDHDALRELAQQGLPMV-VWGAPEDGQSYCSVGSDNVKGGALATEHLIEIGRRRIAFLGDPPHPEVADR 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 128 CIYFVKTVIQAGFK--PHIYQQPKSRVKQCWKneqvIMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVAVI 205
Cdd:cd06295  142 LQGYRDALAEAGLEadPSLLLSCDFTEESGYA----AMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVV 217
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931497206 206 GVDNDELvCDLSDPPLTSIALNTEKAGyeaAKLLDRLMTQKKKKTRKDIMVrPINIVTRQS 266
Cdd:cd06295  218 GYDDIPL-AAYFRPPLTTVRQDLALAG---RLLVEKLLALIAGEPVTSSML-PVELVVRES 273
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
45-239 3.88e-15

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: 74.62  E-value: 3.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  45 LPDLKNWGADGIIMrnTPKSDVLSEL------NLPTILVIHGKEKKSYyPRIITDGEQIGRMAARHFLDRGFRHFAYC-G 117
Cdd:cd06293   48 LEMLESQRVRGLIV--TPSDDDLSHLarlrarGTAVVLLDRPAPGPAG-CSVSVDDVQGGALAVDHLLELGHRRIAFVsG 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 118 FDDTSWSQQRCIYFVKTVIQAGFKPHIYQQPKSRVKQCWKNEQVIMADWLKSLPKPVGLMACNDdrgQHALEACK---MA 194
Cdd:cd06293  125 PLRTRQVAERLAGARAAVAEAGLDPDEVVRELSAPDANAELGRAAAAQLLAMPPRPTAVFAAND---LLALGLLAglrRA 201
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 931497206 195 GLQVPEEVAVIGVDNDELVcDLSDPPLTSIALNTEKAGYEAAKLL 239
Cdd:cd06293  202 GLRVPDDVSVVGYDDLPFA-AAANPPLTTVRQPSYELGRAAADLL 245
PBP1_LacI-like cd06273
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
52-242 4.69e-15

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: 74.47  E-value: 4.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  52 GADGIIMRNTPKSDVLSEL----NLPTILvIHGKEKKSYYPRIITDGEQIGRMAARHFLDRGFRHFAYCG--FDDTSWSQ 125
Cdd:cd06273   55 GVDGLILVGSDHDPELFELleqrQVPYVL-TWSYDEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISgpTAGNDRAR 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 126 QRCIYFVKTVIQAGFKP---HIYQQPKSrvkqcWKNEQVIMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEV 202
Cdd:cd06273  134 ARLAGIRDALAERGLELpeeRVVEAPYS-----IEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISVPEDL 208
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 931497206 203 AVIGVDNDELvCDLSDPPLTSIALNTEKAGYEAAK-LLDRL 242
Cdd:cd06273  209 SITGFDDLEL-AAHLSPPLTTVRVPAREIGELAARyLLALL 248
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
48-254 1.03e-14

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: 73.30  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  48 LKNWGADGIIM---RNTPK-SDVLSELNLPTILVihGKEKKsYYPRIITDGEQIGRMAARHFLDRGFRHFAYCGFDDTSW 123
Cdd:cd01542   51 LARQKVDGIILfatEITDEhRKALKKLKIPVVVL--GQEHE-GFSCVYHDDYGAGKLLGEYLLKKGHKNIAYIGVDEEDI 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 124 S--QQRciyfvKTVIQAGFKphIYQQPKSRVKQC---WKNEQVIMADWLKSlPKPVGLMACNDDRGQHALEACKMAGLQV 198
Cdd:cd01542  128 AvgVAR-----KQGYLDALK--EHGIDEVEIVETdfsMESGYEAAKELLKE-NKPDAIICATDNIALGAIKALRELGIKI 199
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 931497206 199 PEEVAVIGVDNDELvCDLSDPPLTSIALNTEKAGYEAAKLLDRLMTQKKKKTRKDI 254
Cdd:cd01542  200 PEDISVAGFGGYDL-SEFVSPSLTTVKFDYEEAGEKAAELLLDMIEGEKVPKKQKL 254
PBP1_PurR cd06275
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ...
89-266 3.73e-14

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: 71.90  E-value: 3.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  89 RIITDGEQIGRMAARHFLDRGFRHFAY-CGFDDTSWSQQRCIYFVKTVIQAGFKPhiyqqpksrvkqcwKNEQVIMADW- 166
Cdd:cd06275   96 AVLDDSFQGGYLATRHLIELGHRRIGCiTGPLEHSVSRERLAGFRRALAEAGIEV--------------PPSWIVEGDFe 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 167 ----------LKSLP-KPVGLMACNDDRGQHALEACKMAGLQVPEEVAVIGVDNDELVCDLSdPPLTSIALNTEKAGYEA 235
Cdd:cd06275  162 peggyeamqrLLSQPpRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFS-PALTTIHQPKDELGELA 240
                        170       180       190
                 ....*....|....*....|....*....|..
gi 931497206 236 A-KLLDRLmtQKKKKTRKDIMVRPINIVtRQS 266
Cdd:cd06275  241 VeLLLDRI--ENKREEPQSIVLEPELIE-RES 269
PBP1_CcpA_TTHA0807 cd06297
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ...
53-266 4.31e-14

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: 71.73  E-value: 4.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  53 ADGIIMRNTPKSDVLSELNLPT---ILVIHGKEKKsyYPRIITDGEQIGRMAARHFLDRGFRHFAYCGFDDTSwsqqrci 129
Cdd:cd06297   56 CDGLVMASLDLTELFEEVIVPTekpVVLIDANSMG--YDCVYVDNVKGGFMATEYLAGLGEREYVFFGIEEDT------- 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 130 YFVKTVIQAGFKPHIYQQPKSRVKQCWKNEQVI----------MADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVP 199
Cdd:cd06297  127 VFTETVFREREQGFLEALNKAGRPISSSRMFRIdnsskkaeclARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVG 206
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 931497206 200 EEVAVIGVDNDELVcdlSDPPLTSIALNTEKAGYEAAKLLDRLMtQKKKKTRKDIMVRPINIVtRQS 266
Cdd:cd06297  207 EDVAVIGFDGQPWA---ASPGLTTVRQPVEEMGEAAAKLLLKRL-NEYGGPPRSLKFEPELIV-RES 268
PBP1_LacI-like cd06290
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
42-266 8.21e-14

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: 70.72  E-value: 8.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  42 EKSLPDLKNWGADGIIMRNTPKSDVLSELNLPTI-LVIHGKEKKSY-YPRIITDGEQIGRMAARHFLDRGFRHFAYC-GF 118
Cdd:cd06290   45 LEILRLLLARKVDGIIVVGGFGDEELLKLLAEGIpVVLVDRELEGLnLPVVNVDNEQGGYNATNHLIDLGHRRIVHIsGP 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 119 DDTSWSQQRciyfvktviQAGFKpHIYQQPKSRVKQcwknEQVIMADWL---------KSLPKPV---GLMACNDDRGQH 186
Cdd:cd06290  125 EDHPDAQER---------YAGYR-RALEDAGLEVDP----RLIVEGDFTeesgyeamkKLLKRGGpftAIFAANDLMALG 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 187 ALEACKMAGLQVPEEVAVIGVDnDELVCDLSDPPLTSIALNTEKAGYEAAKLLDRLMTQKKKKTRKDIMvrPINIVTRQS 266
Cdd:cd06290  191 AMKALREAGIRVPDDVSVIGFD-DLPFSKYTTPPLTTVRQPLYEMGKTAAEILLELIEGKGRPPRRIIL--PTELVIRES 267
PBP1_hexuronate_repressor-like cd06272
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ...
54-244 2.78e-13

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: 69.32  E-value: 2.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  54 DGIIMRNTPKSDVLS-ELNLPTI-LVIHGKEKKSYyPRIITDGEQIGRMAARHFLDRGFRHFAYCGFDDTSWSQQ-RCIY 130
Cdd:cd06272   58 DGVIVFGISDSDIEYlNKNKPKIpIVLYNRESPKY-STVNVDNEKAGRLAVLLLIQKGHKSIAYIGNPNSNRNQTlRGKG 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 131 FVKTVIQAGFK---PHIYQQPKSrvKQCWKNEQVIMADwLKSLPKpvGLMACNDDRGQHALEACKMAGLQVPEEVAVIGV 207
Cdd:cd06272  137 FIETCEKHGIHlsdSIIDSRGLS--IEGGDNAAKKLLK-KKTLPK--AIFCNSDDIALGVLRVLKENGISIPEDISIVSY 211
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 931497206 208 DNDeLVCDLSDPPLTSIALNTEKAGYEAAKLLDRLMT 244
Cdd:cd06272  212 DNI-PQEARSDPPLTVVGVPIEKIAEESLRLILKLIE 247
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
36-266 1.39e-12

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: 67.17  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  36 REPGGLEKSLPDLKNWGADGIIMRN-TPKSDV---LSELNLPTILvIHGKEKKSYYPRIITDGEQIGRMAARHFLDRGFR 111
Cdd:cd06278   38 DDEDDVDDALRQLLQYRVDGVIVTSaTLSSELaeeCARRGIPVVL-FNRVVEDPGVDSVSCDNRAGGRLAADLLLAAGHR 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 112 HFAYC-GFDDTSWSQQRCIYFVKTVIQAGFKPHIYQQPKSRVKQCWKneqvIMADWLKSLPKPVGLMACNDDRGQHALEA 190
Cdd:cd06278  117 RIAFLgGPEGTSTSRERERGFRAALAELGLPPPAVEAGDYSYEGGYE----AARRLLAAPDRPDAIFCANDLMALGALDA 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 191 CKMA-GLQVPEEVAVIGVDNDEL----VCDLS--DPPLTSIALntekagyEAAKLLDRLMTQKKKKTRKDIMvrPINIVT 263
Cdd:cd06278  193 ARQEgGLVVPEDISVVGFDDIPMaawpSYDLTtvRQPIEEMAE-------AAVDLLLERIENPETPPERRVL--PGELVE 263

                 ...
gi 931497206 264 RQS 266
Cdd:cd06278  264 RGS 266
PBP1_AglR_RafR-like cd06292
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ...
13-267 1.41e-12

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: 67.29  E-value: 1.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  13 AFGRGLLYGIARYSRIHG--PWVFYREPGGLEKSLPD--LKNWGADGIIM----RNTPKSDVLSELNLPTIlVIHGKEKK 84
Cdd:cd06292   16 PFFDEFLAALGHAAAARGydVLLFTASGDEDEIDYYRdlVRSRRVDGFVLastrHDDPRVRYLHEAGVPFV-AFGRANPD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  85 SYYPRIITDGEQIGRMAARHFLDRGFRHFAY-CGFDDTSWSQQRCIYFVKTVIQAGFKPHIYQQPKSRVKQcwKNEQVIM 163
Cdd:cd06292   95 LDFPWVDVDGAAGMRQAVRHLIALGHRRIGLiGGPEGSVPSDDRLAGYRAALEEAGLPFDPGLVVEGENTE--EGGYAAA 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 164 ADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVAVIGVDNDELVcDLSDPPLTSIALNTEKAGYEAAKLLDRLM 243
Cdd:cd06292  173 ARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLA-AFTHPPLTTVRQPIDEIGRAVVDLLLAAI 251
                        250       260
                 ....*....|....*....|....
gi 931497206 244 tQKKKKTRKDIMVRPiNIVTRQST 267
Cdd:cd06292  252 -EGNPSEPREILLQP-ELVVRESS 273
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
52-251 3.79e-12

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: 65.74  E-value: 3.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  52 GADGIIMrnTPKSDVLSEL------NLPTILV---IHGKEKksyyPRIITDGEQIGRMAARHFLDRGFRHFAYC-GFDDT 121
Cdd:cd06280   55 QVDGIIL--APSAGPSRELkrllkhGIPIVLIdreVEGLEL----DLVAGDNREGAYKAVKHLIELGHRRIGLItGPLEI 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 122 SWSQQRCIYFVKTVIQAGFKphiyqqpksrVKQCW--KNEQVIMADW------LKSLPKPVGLMACNDDRGQHALEACKM 193
Cdd:cd06280  129 STTRERLAGYREALAEAGIP----------VDESLifEGDSTIEGGYeavkalLDLPPRPTAIFATNNLMAVGALRALRE 198
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 931497206 194 AGLQVPEEVAVIGVDNDELVcDLSDPPLTSIALNTEKAGYEAAK-LLDRLMTQKKKKTR 251
Cdd:cd06280  199 RGLEIPQDISVVGFDDSDWF-EIVDPPLTVVAQPAYEIGRIAAQlLLERIEGQGEEPRR 256
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
52-258 4.17e-12

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: 65.73  E-value: 4.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  52 GADG-IIMRNTPKSDVLSEL----NLPTILVIHGKEKKSYYPRIITDGEQIGRMAARHFLDRGFRHFAYC-GFDDTSWSQ 125
Cdd:cd01537   55 RVKGlAINLVDPAAAGVAEKargqNVPVVFFDKEPSRYDKAYYVITDSKEGGIIQGDLLAKHGHIQIVLLkGPLGHPDAE 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 126 QRCIYFVKTVIQAGFKphiyQQPKSRVKQCWKNEQVI--MADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVA 203
Cdd:cd01537  135 ARLAGVIKELNDKGIK----TEQLQLDTGDWDTASGKdkMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDIS 210
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 931497206 204 VIGVDN-DELVCdlSDPPLTSIALNTEKAGYEAAKLLDRLmTQKKKKTRKDIMVRP 258
Cdd:cd01537  211 VFGYDAlPEALK--SGPLLTTILQDANNLGKTTFDLLLNL-ADNWKIDNKVVRVPY 263
PBP1_RegR_EndR_KdgR-like cd06283
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ...
52-254 9.94e-12

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: 64.49  E-value: 9.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  52 GADGIIMRNT-PKSDVLSEL---NLPTILV---IHGKEkksyYPRIITDGEQIGRMAARHFLDRGFRHFAYCG--FDDTS 122
Cdd:cd06283   55 RVDGLILQPTgNNNDAYLELaqkGLPVVLVdrqIEPLN----WDTVVTDNYDATYEATEHLKEQGYERIVFVTepIKGIS 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 123 WSQQRciyfvktviQAGFKpHIYQQPKSRVKQCW----KNEQVIM--ADWLK-SLPKPVGLMACNDDRGQHALEACKMAG 195
Cdd:cd06283  131 TRRER---------LQGFL-DALARYNIEGDVYVieieDTEDLQQalAAFLSqHDGGKTAIFAANGVVLLRVLRALKALG 200
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 196 LQVPEEVAVIGVDNDELvCDLSDPPLTSIALNTEKAGYEAAK-LLDRLMTQKKKKTRKDI 254
Cdd:cd06283  201 IRIPDDVGLCGFDDWDW-ADLIGPGITTIRQPTYEIGKAAAEiLLERIEGDSGEPKEIEL 259
PBP1_LacI-like cd06281
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
43-266 1.97e-11

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


Pssm-ID: 380504 [Multi-domain]  Cd Length: 270  Bit Score: 63.80  E-value: 1.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  43 KSLPDLKNWGADGIIM-----RNTPKSDVLSELNLPTILVihGKEKKSYYPRIITDGEQIGRMAARHFLDRGFRHFAYCG 117
Cdd:cd06281   46 ELLSLFQRRRVDGLILtpgdeDDPELAAALARLDIPVVLI--DRDLPGDIDSVLVDHRSGVRQATEYLLSLGHRRIALLT 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 118 FDDTSW-SQQRCIYFVKTVIQAG--FKPHIYQQPKSRVKQCWKneqvIMADWLKSLPKPVGLMACNDDRGQHALEACKMA 194
Cdd:cd06281  124 GGPDIRpGRERIAGFKAAFAAAGlpPDPDLVRLGSFSADSGFR----EAMALLRQPRPPTAIIALGTQLLAGVLRAVRAA 199
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 931497206 195 GLQVPEEVAVIGVDNDELVcDLSDPPLTSIALNTEKAGYEAAK-LLDRLMTQKKKKTRKdIMVrPINIVTRQS 266
Cdd:cd06281  200 GLRIPGDLSVVSIGDSDLA-ELHDPPITAIRWDLDAVGRAAAElLLDRIEGPPAGPPRR-IVV-PTELILRDS 269
PRK10703 PRK10703
HTH-type transcriptional repressor PurR;
54-266 2.31e-11

HTH-type transcriptional repressor PurR;


Pssm-ID: 236739 [Multi-domain]  Cd Length: 341  Bit Score: 64.36  E-value: 2.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  54 DGI-IMRNTPKSDVLSEL----NLPTILVIHGKEKKSYYPRIITDGEQIGRMAARHFLDRGFRHFAY-CGFDDTSWSQQR 127
Cdd:PRK10703 117 DGLlVMCSEYPEPLLAMLeeyrHIPMVVMDWGEAKADFTDAIIDNAFEGGYLAGRYLIERGHRDIGViPGPLERNTGAGR 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 128 CIYFVKTVIQAGFKPH---IYQ---QPKSRVKQcwkneqviMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEE 201
Cdd:PRK10703 197 LAGFMKAMEEANIKVPeewIVQgdfEPESGYEA--------MQQILSQKHRPTAVFCGGDIMAMGAICAADEMGLRVPQD 268
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931497206 202 VAVIGVDNDElVCDLSDPPLTSIALNTEKAGYEAAK-LLDRLmtQKKKKTRKDIMVRPiNIVTRQS 266
Cdd:PRK10703 269 ISVIGYDNVR-NARYFTPALTTIHQPKDRLGETAFNmLLDRI--VNKREEPQTIEVHP-RLVERRS 330
PBP1_LacI-like cd06282
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
67-239 2.69e-11

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


Pssm-ID: 380505 [Multi-domain]  Cd Length: 267  Bit Score: 63.46  E-value: 2.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  67 LSELNLPTILViHGKEKKSYYPRIITDGEQIGRMAARHFLDRGFRHFAYCG--FDDTSWSQQRCIYFVKTVIQAGFKP-H 143
Cdd:cd06282   75 LEEEGVPYVLL-FNQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAgdFSASDRARLRYQGYRDALKEAGLKPiP 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 144 IYQQPKSRVKQcwknEQVIMADWLKSLPkPVGLMACNDDRGQHALEACKMAGLQVPEEVAVIGVDNDELvCDLSDPPLTS 223
Cdd:cd06282  154 IVEVDFPTNGL----EEALTSLLSGPNP-PTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAI-GELLTPTLAT 227
                        170
                 ....*....|....*.
gi 931497206 224 IALNTEKAGYEAAKLL 239
Cdd:cd06282  228 VVQPSRDMGRAAADLL 243
PBP1_CatR-like cd06296
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ...
52-267 4.47e-11

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: 62.68  E-value: 4.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  52 GADGIIMRNTPKS----DVLSELNLPTILVIHGKEKKSYYPRIITDGEQIGRMAARHFLDRGFRHFAY-CGFDDTSWSQQ 126
Cdd:cd06296   55 GSAGVVLVTSDPTsrqlRLLRSAGIPFVLIDPVGEPDPDLPSVGATNWAGGRLATEHLLDLGHRRIAViTGPPRSVSGRA 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 127 RCIYFVKTVIQAGFKPHiyqqpKSRVKQC-WKNEQVI-MADWLKSLPK-PVGLMACNDDRGQHALEACKMAGLQVPEEVA 203
Cdd:cd06296  135 RLAGYRAALAEAGIAVD-----PDLVREGdFTYEAGYrAARELLELPDpPTAVFAGNDEQALGVYRAARALGLRVPDDLS 209
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 204 VIGVDnDELVCDLSDPPLTSIALNTEKAGYEAAKLLDRLmtqkkkktRKDIMV--RPI----NIVTRQST 267
Cdd:cd06296  210 VIGFD-DTPPARWTSPPLTTVHQPLREMGAVAVRLLLRL--------LEGGPPdaRRIelatELVVRGST 270
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
47-264 9.71e-11

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: 62.25  E-value: 9.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  47 DLKNWGADGIIMrNTPKSDVLSEL-------NLPTILVIHGKEKKSYYPRIITDGEQIGRMAARHFLDRGFRHFAYC--- 116
Cdd:COG1879   84 DLIAQGVDAIIV-SPVDPDALAPAlkkakaaGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGGKGKVAilt 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 117 GFDDTSWSQQRCIYFvKTVIQAGFKPHIYQQPKSRvkqcWKNEQV--IMADWLKSLPKPVGLMACNDDRGQHALEACKMA 194
Cdd:COG1879  163 GSPGAPAANERTDGF-KEALKEYPGIKVVAEQYAD----WDREKAleVMEDLLQAHPDIDGIFAANDGMALGAAQALKAA 237
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931497206 195 GLQvpEEVAVIGVD-NDELVCDLSDPPLT-SIALNTEKAGYEAAKLLDRLMtqKKKKTRKDIMVrPINIVTR 264
Cdd:COG1879  238 GRK--GDVKVVGFDgSPEALQAIKDGTIDaTVAQDPYLQGYLAVDAALKLL--KGKEVPKEILT-PPVLVTK 304
PBP1_SalR cd01545
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ...
7-266 1.05e-10

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: 61.80  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206   7 MIETSRAFGRGLLygiarysrIHGpwVFYREPGGLEKSLPDLKNWGADGIIM-----RNTPKSDVLSELNLPTILvIHGK 81
Cdd:cd01545   21 ALRACREAGYHLV--------VEP--CDSDDEDLADRLRRFLSRSRPDGVILtpplsDDPALLDALDELGIPYVR-IAPG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  82 EKKSYYPRIITDGEQIGRMAARHFLDRGFRHFAY-CGFDDTSWSQQRCIYFVKTVIQAGFKPhiyqqPKSRVKQCW---K 157
Cdd:cd01545   90 TDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFiAGPPDHGASAERLEGFRDALAEAGLPL-----DPDLVVQGDftfE 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 158 NEQVIMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVAVIGVDNDELVCDLSdPPLTSIALNTEKAGYEAAK 237
Cdd:cd01545  165 SGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVW-PPLTTVRQPIAEMARRAVE 243
                        250       260
                 ....*....|....*....|....*....
gi 931497206 238 LLDRLMtQKKKKTRKDIMVRPiNIVTRQS 266
Cdd:cd01545  244 LLIAAI-RGAPAGPERETLPH-ELVIRES 270
PBP1_AglR_RafR-like cd06271
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ...
19-242 2.17e-10

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: 60.52  E-value: 2.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  19 LYGIARYSRIHG----PWVFyrEPGGLEKSLPDLKNWG-ADGIIMR----NTPKSDVLSELNLPtiLVIHGKEKKSY-YP 88
Cdd:cd06271   21 VSGITEEAGTTGyhllVWPF--EEAES*VPIRDLVETGsADGVILSeiepNDPRVQFLTKQNFP--FVAHGRSD*PIgHA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  89 RIITDGEQIGRMAARHFLDRGFRHFAYCGFD-DTSWSQQRCIYFVKTVIQAGFKPHIYQQPKSRVKQcwkneQVIMADWL 167
Cdd:cd06271   97 WVDIDNEAGAYEAVERLAGLGHRRIAFIVPPaRYSPHDRRLQGYVRA*RDAGLTGYPLDADTTLEAG-----RAAAQRLL 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 931497206 168 KSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVAVIGVDNDELVCDLSDPPLTSIALNTEKAGYEAAK-LLDRL 242
Cdd:cd06271  172 ALSPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSAPFLGAMITPPLTTVHAPIAEAGRELAKaLLARI 247
PBP1_LacI-like cd06299
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ...
14-243 4.81e-10

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: 59.60  E-value: 4.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  14 FGRgLLYGIARYSRIHGPWVFY----REPGGLEKSLPDLKNWGADGIIM----RNTPKSDVLSELNLPTILVIHGKEKKS 85
Cdd:cd06299   14 FAE-LASGIEDEARAHGYSVILgnsdEDPEREDESLEMLLSQRVDGIIAvptgENSEGLQALIAQGLPVVFVDREVEGLG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  86 YYPRIITDGEQIGRMAARHFLDRGFRHFAYC-GFDDTSWSQQRCIYFVKTVIQAGFKPhiyqqpksrvkqcwkNEQVIM- 163
Cdd:cd06299   93 GVPVVTSDNRPGAREAVEYLVSLGHRRIGYIsGPLSTSTGRERLAAFRAALTAAGIPI---------------DEELVAf 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 164 -----------ADWLKSLPKPV-GLMACNDDRGQHALEACKMAGLQVPEEVAVIGVDNDELVcDLSDPPLTSIALNTEKA 231
Cdd:cd06299  158 gdfrqdsgaaaAHRLLSRGDPPtALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWF-ELLSPPLTVIAQPVERI 236
                        250
                 ....*....|..
gi 931497206 232 GYEAAKLLDRLM 243
Cdd:cd06299  237 GRRAVELLLALI 248
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
47-256 3.27e-09

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: 57.19  E-value: 3.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  47 DLKNWGADGIIMrNTPKSDVLSEL-------NLPTILV---IHGKEKKSYYprIITDGEQIGRMAARHFLDR--GFRHFA 114
Cdd:cd01536   50 DLIAQGVDAIII-APVDSEALVPAvkkanaaGIPVVAVdtdIDGGGDVVAF--VGTDNYEAGKLAGEYLAEAlgGKGKVA 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 115 YCGFD-DTSWSQQRCIYFVKtVIQAGFKPHI-YQQPKSrvkqcWKNEQV--IMADWLKSLPKPVGLMACNDDRGQHALEA 190
Cdd:cd01536  127 ILEGPpGSSTAIDRTKGFKE-ALKKYPDIEIvAEQPAN-----WDRAKAltVTENLLQANPDIDAVFAANDDMALGAAEA 200
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 931497206 191 CKMAGLQvpEEVAVIGVDNDELVCDL-SDPPLT-SIALNTEKAGYEAAKLLDRLMtqKKKKTRKDIMV 256
Cdd:cd01536  201 LKAAGRT--GDIKIVGVDGTPEALKAiKDGELDaTVAQDPYLQGYLAVEAAVKLL--NGEKVPKEILT 264
PRK10423 PRK10423
transcriptional repressor RbsR; Provisional
98-224 1.13e-08

transcriptional repressor RbsR; Provisional


Pssm-ID: 182448 [Multi-domain]  Cd Length: 327  Bit Score: 55.86  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  98 GRMAARHFLDRGFRHFAyC--GFDDTSWSQQRCIYFVKTVIQAGFK-PHIYqqpksrvkqcwkneqVIMADW-------- 166
Cdd:PRK10423 162 GDLATQYLIDKGYTRIA-CitGPLDKTPARLRLEGYRAAMKRAGLNiPDGY---------------EVTGDFefnggfda 225
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931497206 167 ---LKSLPK-PVGLMACNDDRGQHALEACKMAGLQVPEEVAVIGVDNDELVCDLSdPPLTSI 224
Cdd:PRK10423 226 mqqLLALPLrPQAVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMT-PPLTTI 286
PBP1_LacI-like cd06279
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ...
54-239 1.32e-08

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: 55.68  E-value: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  54 DGIIMRNTPKSDVLSEL----NLPtiLVIHGKEKKSYYPRIITDGEQIGRMAARHFLDRGFRHFAYCGFDDTSWSQQRCI 129
Cdd:cd06279   58 DGFIVYGLSDDDPAVAAlrrrGLP--LVVVDGPAPPGIPSVGIDDRAAARAAARHLLDLGHRRIAILSLRLDRGRERGPV 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 130 YFVK------TVI-------QAGFKPHIYQQPKSRVKQCWKNEQ---VIMADWLKSL-PKPVGLMACNDDRGQHALEACK 192
Cdd:cd06279  136 SAERlaaatnSVArerlagyRDALEEAGLDLDDVPVVEAPGNTEeagRAAARALLALdPRPTAILCMSDVLALGALRAAR 215
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 931497206 193 MAGLQVPEEVAVIGVDNDELvCDLSDPPLTSIALNTEKAGYEAAKLL 239
Cdd:cd06279  216 ERGLRVPEDLSVTGFDDIPE-AAAADPGLTTVRQPAVEKGRAAARLL 261
PBP1_CcpB-like cd06286
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ...
88-247 1.99e-08

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: 54.86  E-value: 1.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  88 PRIITDGEQIGRMAARHFLDRGFRHFAYCGFDDTSWS---QQRciyfvktviQAGFKpHIYQQPKSRVKQCWKNEQVI-M 163
Cdd:cd06286   92 PSVYIDRYEAYLEALEYLKEKGHRKIGYCLGRPESSSastQAR---------LKAYQ-DVLGEHGLSLREEWIFTNCHtI 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 164 AD-------WLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVAVIGVDNDELvCDLsdPPLTSIALNTEKAGYEAA 236
Cdd:cd06286  162 EDgyklakkLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPI-SEL--LNLTTIDQPLEEMGKEAF 238
                        170
                 ....*....|.
gi 931497206 237 KLLDRLMTQKK 247
Cdd:cd06286  239 ELLLSQLESKE 249
lacI PRK09526
lac repressor; Reviewed
21-267 2.89e-08

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 55.00  E-value: 2.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  21 GIARYSRIHGPWV---FYREPGG--LEKSLPDLKNWGADGIIMrNTPKSD----VLSELNLPTILVIHGKEKKSYYPRII 91
Cdd:PRK09526  84 AIKSRADQLGYSVvisMVERSGVeaCQAAVNELLAQRVSGVII-NVPLEDadaeKIVADCADVPCLFLDVSPQSPVNSVS 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  92 TDGEQIGRMAARHFLDRGFRHFAYCGFDDTSWSQQ-RCIYFVKTVIQAGFKPhiyqqpksrvkqcwknEQVIMADW---- 166
Cdd:PRK09526 163 FDPEDGTRLGVEHLVELGHQRIALLAGPESSVSARlRLAGWLEYLTDYQLQP----------------IAVREGDWsams 226
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 167 --------LKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVAVIGVDndelvcDLSD-----PPLTSIALNTEKAGY 233
Cdd:PRK09526 227 gyqqtlqmLREGPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYD------DTEDssyfiPPLTTIKQDFRLLGK 300
                        250       260       270
                 ....*....|....*....|....*....|....
gi 931497206 234 EAAKLLDRLMTQKKKKTRKDImvrPINIVTRQST 267
Cdd:PRK09526 301 EAVDRLLALSQGQAVKGSQLL---PTSLVVRKST 331
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
281-374 4.72e-08

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 50.69  E-value: 4.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 281 VRFIRKNSRKTIRVNDVADASGLSRRVLEKRFRKILNRSVYEEIRRVRIAQVCQMLVETTISISEIALVLGYPGVEHIAR 360
Cdd:PRK10219  11 IAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYVSQQTFSR 90
                         90
                 ....*....|....
gi 931497206 361 YFRKEKGKSLLAYR 374
Cdd:PRK10219  91 VFRRQFDRTPSDYR 104
ftrA PRK09393
transcriptional activator FtrA; Provisional
283-377 2.01e-07

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 52.27  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 283 FIRKNSRKTIRVNDVADASGLSRRVLEKRFRKILNRSVYEEIRRVRIAQVCQMLVETTISISEIALVLGYPGVEHIARYF 362
Cdd:PRK09393 226 WMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHF 305
                         90
                 ....*....|....*
gi 931497206 363 RKEKGKSLLAYRKEY 377
Cdd:PRK09393 306 RRRAATSPAAYRKRF 320
PBP1_RafR-like cd20009
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ...
53-242 4.46e-07

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: 50.61  E-value: 4.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  53 ADGIIMRNT----PKSDVLSELNLPtiLVIHGK-EKKSYYPRIITDGEQIGRMAARHFLDRGFRHFA-YCGFDDTSWSQQ 126
Cdd:cd20009   58 ADGIIISHTepqdPRVRYLLERGFP--FVTHGRtELSTPHAYFDFDNEAFAYEAVRRLAARGRRRIAlVAPPRELTYAQH 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 127 RCIYFVKTVIQAGFKPHIYQQ-----PKSRVKQcwkneqvIMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEE 201
Cdd:cd20009  136 RLRGFRRALAEAGLEVEPLLIvtldsSAEAIRA-------AARRLLRQPPRPDGIICASEIAALGALAGLEDAGLVVGRD 208
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 931497206 202 VAVIGVDNDELVcDLSDPPLTSIALNTEKAGYEAAK-LLDRL 242
Cdd:cd20009  209 VDVVAKETSPIL-DYFRPPIDTLYEDIEEAGRFLAEaLLRRI 249
PBP1_LacI-like cd06277
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
90-266 1.15e-06

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: 49.55  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  90 IITDGEQIGRMAARHFLDRGFRHFAY-CGFDDTSWSQQRCIYFVKTVIQAGFKPhiYQQPKSRVKQCWKNEQVIMADWLK 168
Cdd:cd06277  102 VVIDNEDGAYEAVKYLVELGHTRIGYlASSYRIKNFEERRRGFRKAMRELGLSE--DPEPEFVVSVGPEGAYKDMKALLD 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 169 SLPK-PVGLMACNDDRGQHALEACKMAGLQVPEEVAVIGVDnDELVCDLSDPPLTSIALNTEKAGYEAAKLLDRLMTQKK 247
Cdd:cd06277  180 TGPKlPTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFD-DIPVSAMVDPPLTTIHVPKEQMGKLAVRRLIEKIKDPD 258
                        170
                 ....*....|....*....
gi 931497206 248 KKTRKDIMvrPINIVTRQS 266
Cdd:cd06277  259 GGTLKILV--STKLVERGS 275
PRK11041 PRK11041
DNA-binding transcriptional regulator CytR; Provisional
167-239 2.31e-06

DNA-binding transcriptional regulator CytR; Provisional


Pssm-ID: 182923 [Multi-domain]  Cd Length: 309  Bit Score: 48.84  E-value: 2.31e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 931497206 167 LKSLPKPVGLMAC-NDDRGQHALEACKMAGLQVPEEVAVIGVDNDELvCDLSDPPLTSIALNTEKAGYEAAKLL 239
Cdd:PRK11041 207 LLDLPQPPTAVFChSDVMALGALSQAKRMGLRVPQDLSIIGFDDIDL-AQYCDPPLTTVAQPRYEIGREAMLLL 279
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
47-210 2.37e-06

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


Pssm-ID: 380542 [Multi-domain]  Cd Length: 278  Bit Score: 48.51  E-value: 2.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  47 DLKNWGADGIIMRNT-PKS-----DVLSELNLPTILVIHGKEKKSYYPRIITDGEQIGRMAARHFLDR------GFRHFA 114
Cdd:cd06319   50 DLIAQGVDGIIISPTnSSAaptvlDLANEAKIPVVIADIGTGGGDYVSYIISDNYDGGYQAGEYLAEAlkengwGGGSVG 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 115 YCGFDDTS-WSQQRCIYFVKTVIQAGFKP-HIYQQPKSRVKQCWKneqvIMADWLKSLPKPVGLMACNDDRGQHALEACK 192
Cdd:cd06319  130 IIAIPQSRvNGQARTAGFEDALEEAGVEEvALRQTPNSTVEETYS----AAQDLLAANPDIKGIFAQNDQMAQGALQAIE 205
                        170
                 ....*....|....*...
gi 931497206 193 MAGLQvpEEVAVIGVDND 210
Cdd:cd06319  206 EAGRT--GDILVVGFDGD 221
PRK14987 PRK14987
HTH-type transcriptional regulator GntR;
5-242 2.44e-06

HTH-type transcriptional regulator GntR;


Pssm-ID: 184949 [Multi-domain]  Cd Length: 331  Bit Score: 48.87  E-value: 2.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206   5 ILMIETSRAFGRGL-----------LYGIARYSRIHGPWV----FYREPGGLEKSLPDLKNWGADGIIM---RNTPKSdv 66
Cdd:PRK14987  57 ILSNATSRAIGVLLpsltnqvfaevLRGIESVTDAHGYQTmlahYGYKPEMEQERLESMLSWNIDGLILterTHTPRT-- 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  67 LSELNLPTILVIHGKEKKSYYPRIIT--DGEQIGRMAARHFLDRGFRHFAYCG--FDDTSWSQQRCiyFVKTVIQAGFKP 142
Cdd:PRK14987 135 LKMIEVAGIPVVELMDSQSPCLDIAVgfDNFEAARQMTTAIIARGHRHIAYLGarLDERTIIKQKG--YEQAMLDAGLVP 212
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 143 HIYQQPKSrvkQCWKNEQVIMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVAVIGVDNDElVCDLSDPPLT 222
Cdd:PRK14987 213 YSVMVEQS---SSYSSGIELIRQARREYPQLDGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHD-IGQVMEPRLA 288
                        250       260
                 ....*....|....*....|.
gi 931497206 223 SIALNTEKAG-YEAAKLLDRL 242
Cdd:PRK14987 289 SVLTPRERMGsIGAERLLARI 309
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
18-239 2.51e-06

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


Pssm-ID: 395423 [Multi-domain]  Cd Length: 281  Bit Score: 48.66  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206   18 LLYGIARYSRIHGPWVFYREPGGLEKSLPD----LKNWGADGIIMRN-TPKSDVL----SELNLPTILVIHGKEKKSYYP 88
Cdd:pfam00532  19 LVKGITKAAKDHGFDVFLLAVGDGEDTLTNaidlLLASGADGIIITTpAPSGDDItakaEGYGIPVIAADDAFDNPDGVP 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206   89 RIITDGEQIGRMAARHFLDRGFRHFAYC--GFDDTSWSQQRCIYFVKTVIQAGFKPHIYQQPKSrvkqcwKNEQVIMADW 166
Cdd:pfam00532  99 CVMPDDTQAGYESTQYLIAEGHKRPIAVmaGPASALTARERVQGFMAALAAAGREVKIYHVATG------DNDIPDAALA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  167 LKSL----PKPVGLMACNDDRGQHALEACKMAG-LQVPEEV-----AVIGVDNDELVCD--LSDPPLTSIALNTEKAGYE 234
Cdd:pfam00532 173 ANAMlvshPTIDAIVAMNDEAAMGAVRALLKQGrVKIPDIVgiginSVVGFDGLSKAQDtgLYLSPLTVIQLPRQLLGIK 252

                  ....*
gi 931497206  235 AAKLL 239
Cdd:pfam00532 253 ASDMV 257
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
274-377 2.53e-05

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 45.35  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 274 DKEVAEAVRFIRKNSRKTIRVNDVADASGLSRRVLEKRFRKILNRSVYEEIRRVRIAQVCQMLVETTISISEIALVLGYP 353
Cdd:PRK10572 182 DPRVREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYD 261
                         90       100
                 ....*....|....*....|....
gi 931497206 354 GVEHIARYFRKEKGKSLLAYRKEY 377
Cdd:PRK10572 262 DQLYFSRVFKKCTGASPSEFRARC 285
PRK10371 PRK10371
transcriptional regulator MelR;
277-375 6.57e-05

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 44.43  E-value: 6.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 277 VAEAVRFIRKNSRKTIRVNDVADASGLSRRVLEKRFRKILNRSVYEEIRRVRIAQVCQMLVETTISISEIALVLGYPGVE 356
Cdd:PRK10371 193 VSQMLGFIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSS 272
                         90
                 ....*....|....*....
gi 931497206 357 HIARYFRKEKGKSLLAYRK 375
Cdd:PRK10371 273 RFYSTFGKYVGMSPQQYRK 291
PBP1_CcpA cd06298
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ...
195-266 1.50e-04

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: 43.05  E-value: 1.50e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 931497206 195 GLQVPEEVAVIGVDNDELVcDLSDPPLTSIALNTEKAGYEAAKLLDRLMTqKKKKTRKDIMVrPINIVTRQS 266
Cdd:cd06298  200 GLKVPEDLEIIGFDNTRYA-TMSRPQLTSINQPLYDIGAVAMRLLTKLMN-KEEVEETIVKL-PHSIIWRQS 268
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
71-256 1.89e-04

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


Pssm-ID: 380532 [Multi-domain]  Cd Length: 285  Bit Score: 42.98  E-value: 1.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  71 NLPTILV---IHGKEKKSYYPRIITDGEQIGRMAAR----HFLDRGFRHFAYCGFDDTSWSQQRciyfvktviQAGFKPH 143
Cdd:cd06309   80 GIPVILVdrtIDGEDGSLYVTFIGSDFVEEGRRAAEwlvkNYKGGKGNVVELQGTAGSSVAIDR---------SKGFREV 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 144 IYQQPKSRV--KQC--WKNE--QVIMADWLKSLPKPV-GLMACNDDRGQHALEACKMAGLQVPEEVAVIGVD-------- 208
Cdd:cd06309  151 IKKHPNIKIvaSQSgnFTREkgQKVMENLLQAGPGDIdVIYAHNDDMALGAIQALKEAGLKPGKDVLVVGIDgqkdalea 230
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 931497206 209 --NDELVCDLSDPPLtsialntekAGYEAAKLLDRLMtqKKKKTRKDIMV 256
Cdd:cd06309  231 ikAGELNATVECNPL---------FGPTAFDTIAKLL--AGEKVPKLIIV 269
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
156-248 2.08e-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: 42.64  E-value: 2.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 156 WKNEQV--IMADWLKSLPKPV-GLMACNDDRGQHALEACKMAGLqvpEEVAVIGVDNDElvcDlsdppltsiALNTEKAG 232
Cdd:cd06313  163 WSRDEAmsLMENWLQAYGDEIdGIIAQNDDMALGALQAVKAAGR---DDIPVVGIDGIE---D---------ALQAVKSG 227
                         90
                 ....*....|....*.
gi 931497206 233 YEAAKLLDRLMTQKKK 248
Cdd:cd06313  228 ELIATVLQDAEAQGKG 243
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
284-325 7.41e-04

Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the N-terminal arm of AraC binds to the DNA binding domain (pfam00165) and helps to hold the two DNA binding domains in a relative orientation that favours DNA looping. In the presence of arabinose, the arms bind over the arabinose on the dimerization domain, thus freeing the DNA-binding domains. The freed DNA-binding domains are then able to assume a conformation suitable for binding to the adjacent DNA sites that are utilized when AraC activates transcription, and hence AraC ceases looping the DNA when arabinose is added.


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 36.75  E-value: 7.41e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 931497206  284 IRKNSRKTIRVNDVADASGLSRRVLEKRFRKILNRSVYEEIR 325
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
PBP1_LacI-like cd06287
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
167-266 9.95e-04

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


Pssm-ID: 380510 [Multi-domain]  Cd Length: 268  Bit Score: 40.48  E-value: 9.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 167 LKSLPKPVGLMACNDDRGQHALEACKMAGLQVPEEVAVIgVDNDELVCDLSDPPLTSIALNTEKAGYEAAKLLDRLMTQK 246
Cdd:cd06287  173 LAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPEDLMVV-TRYDGIRARTADPPLTAVDLHLDRVARTAIDLLFASLSGE 251
                         90       100
                 ....*....|....*....|
gi 931497206 247 KKKTRKDIMVRpinIVTRQS 266
Cdd:cd06287  252 ERSVEVGPAPE---LVVRAS 268
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
304-374 1.67e-03

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 40.04  E-value: 1.67e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 931497206 304 SRRVLEKRFRKILNRSVYEEIRRVRIAQVCQMLVETTISISEIALVLGYPGVEHIARYFRKEKGKSLLAYR 374
Cdd:PRK13502 205 SERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWR 275
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
294-374 5.09e-03

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 38.54  E-value: 5.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206 294 VNDVADASGLSRRVLEKRFRKILNRSVYEEIRRVRIAQVCQMLVETTISISEIALVLGYPGVEHIARYFRKEKGKSLLAY 373
Cdd:PRK13500 225 LDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDSNYFSVVFTRETGMTPSQW 304

                 .
gi 931497206 374 R 374
Cdd:PRK13500 305 R 305
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
90-211 6.60e-03

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


Pssm-ID: 380545 [Multi-domain]  Cd Length: 270  Bit Score: 38.03  E-value: 6.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 931497206  90 IITDGEQIGRMAARHFLDRGFRHFAYCG---FDDTSWSQQRciyfvktviQAGFKPHIYQQPKSRVKQcwknEQ------ 160
Cdd:cd06322   99 VGTDNYAGGKLAGEYALKALLGGGGKIAiidYPEVESVVLR---------VNGFKEAIKKYPNIEIVA----EQpgdgrr 165
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 931497206 161 ----VIMADWLKSLPKPVGLMACNDDRGQHALEACKMAGLQvpEEVAVIGVD-NDE 211
Cdd:cd06322  166 eealAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGKE--DKIKVIGFDgNPE 219
 
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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