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Conserved domains on  [gi|2769562395|ref|WP_366484845|]
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substrate-binding domain-containing protein [uncultured Arthrobacter sp.]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
2-315 2.94e-88

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


:

Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 267.45  E-value: 2.94e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395   2 SRALRAqaDPALSDApsasiTR-HIIEVADRLGYRPDPYAASLRTRRSMSIGVLVPRLSDVVLATIYEGIEQSAALSGYQ 80
Cdd:COG1609    21 SRVLNG--PPRVSEE-----TReRVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLRGIEEAARERGYQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  81 VAVANTYDDPERHRKYLGLMSSRRVDGLILADAHLG---VAQSHPTDVPTVLVNRRCPG--FLSVSGADIVGGGLVASHF 155
Cdd:COG1609    94 LLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDdarLERLAEAGIPVVLIDRPLPDpgVPSVGVDNRAGARLATEHL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 156 ADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIG 235
Cdd:COG1609   174 IELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGPRPTAIFCANDLMALG 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 236 AMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAGQTLIDVLAGKPAAP--TLITPSLKARQSSGP 313
Cdd:COG1609   254 ALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPerVLLPPELVVRESTAP 333


                  ..
gi 2769562395 314 AR 315
Cdd:COG1609   334 AP 335
 
Name Accession Description Interval E-value
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
2-315 2.94e-88

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 267.45  E-value: 2.94e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395   2 SRALRAqaDPALSDApsasiTR-HIIEVADRLGYRPDPYAASLRTRRSMSIGVLVPRLSDVVLATIYEGIEQSAALSGYQ 80
Cdd:COG1609    21 SRVLNG--PPRVSEE-----TReRVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLRGIEEAARERGYQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  81 VAVANTYDDPERHRKYLGLMSSRRVDGLILADAHLG---VAQSHPTDVPTVLVNRRCPG--FLSVSGADIVGGGLVASHF 155
Cdd:COG1609    94 LLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDdarLERLAEAGIPVVLIDRPLPDpgVPSVGVDNRAGARLATEHL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 156 ADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIG 235
Cdd:COG1609   174 IELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGPRPTAIFCANDLMALG 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 236 AMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAGQTLIDVLAGKPAAP--TLITPSLKARQSSGP 313
Cdd:COG1609   254 ALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPerVLLPPELVVRESTAP 333


                  ..
gi 2769562395 314 AR 315
Cdd:COG1609   334 AP 335
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 50-311 3.39e-78

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: 239.44  E-value: 3.39e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILADAHLGVAQSH---PTDVP 126
Cdd:cd06285     1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQelaARGVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 127 TVLVNRRCPG--FLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSFD 204
Cdd:cd06285    81 VVLVDRRIGDtaLPSVTVDNELGGRLATRHLLELGHRRIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDERIVPGGFT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 205 VEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAG 284
Cdd:cd06285   161 IEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEMGRRAA 240

                         250       260
                  ....*....|....*....|....*....
gi 2769562395 285 QTLIDVLAGKPAAPTLIT--PSLKARQSS 311
Cdd:cd06285   241 ELLLQLIEGGGRPPRSITlpPELVVREST 269
PRK10423 PRK10423
transcriptional repressor RbsR; Provisional
 18-310 1.72e-43

transcriptional repressor RbsR; Provisional


Pssm-ID: 182448 [Multi-domain]  Cd Length: 327  Bit Score: 151.78  E-value: 1.72e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  18 SASITRHIIEVADRLGYRPDPYAASLRTRRSMSIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYL 97
Cdd:PRK10423   26 SEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  98 GLMSSRRVDGLIL--ADAHL---GVAQSHPTdVPTVLVNRrCPgFLSVSgaDIV------GGGLVASHFADLGHDHLGVI 166
Cdd:PRK10423  106 ETLMQKRVDGLLLlcTETHQpsrEIMQRYPS-VPTVMMDW-AP-FDGDS--DLIqdnsllGGDLATQYLIDKGYTRIACI 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 167 AGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLM 246
Cdd:PRK10423  181 TGPLDKTPARLRLEGYRAAMKRAGLNIPDGYEVTGDFEFNGGFDAMQQLLALPLRPQAVFTGNDAMAVGVYQALYQAGLS 260

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2769562395 247 PGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAGQTLIDVLAGKPAAPTLI--TPSLKARQS 310
Cdd:PRK10423  261 VPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQRLqlTPELMERGS 326
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
 154-311 1.12e-26

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: 102.80  E-value: 1.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 154 HFADLGHDHLGVIA--GPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSFDVEGGREaaRRLLALEPRPTAIFAVNDY 231
Cdd:pfam13377   1 HLAELGHRRIALIGpeGDRDDPYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAAR--ERLRWLGALPTAVFVANDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 232 AAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAGQTLIDVLAGKPAAP--TLITPSLKARQ 309
Cdd:pfam13377  79 VALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPerVLLPPELVERE 158


                  ..
gi 2769562395 310 SS 311
Cdd:pfam13377 159 ST 160
fruct_sucro_rep TIGR02417
D-fructose-responsive transcription factor; Members of this family belong the lacI ...
 18-309 6.05e-23

D-fructose-responsive transcription factor; Members of this family belong the lacI helix-turn-helix family (pfam00356) of DNA-binding transcriptional regulators. All members are from the proteobacteria. Characterized members act as positive and negative transcriptional regulators of fructose and sucrose transport and metabolism. Sucrose is a disaccharide composed of fructose and glucose; D-fructose-1-phosphate rather than an intact sucrose moiety has been shown to act as the inducer. [Regulatory functions, DNA interactions]


Pssm-ID: 131470 [Multi-domain]  Cd Length: 327  Bit Score: 96.74  E-value: 6.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  18 SASITRHIIEVADRLGYRPDPYAASLRTRRSMSIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYL 97
Cdd:TIGR02417  30 SQETVERVMAVVREQGYQPNIHAASLRAGRSRTIGLVIPDLENYSYARIAKELEQQCREAGYQLLIACSDDNPDQEKVVI 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  98 GLMSSRRVDGLIladahlgVAQSHPTD-----------VPTVLVNRRCP--GFLSVSGADIVGGGLVASHFADLGHDHLG 164
Cdd:TIGR02417 110 ENLLARQVDALI-------VASCMPPEdayyqklqnegLPVVALDRSLDdeHFCSVISDDVDAAAELIERLLSQHADEFW 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 165 VIAGPTWASTSIDRVTGFRETsrARGLDLPDSAVVASSFDVEGGREAARRLLALEPR-PTAIFAVNDYAAIGAMGEMRDQ 243
Cdd:TIGR02417 183 YLGAQPELSVSRDRLAGFRQA--LKQATLEVEWVYGGNYSRESGYQMFAKLCARLGRlPQALFTTSYTLLEGVLDYMLER 260

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2769562395 244 GLMPgADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAGQTLIDVLAGKPAAP--TLITPSLKARQ 309
Cdd:TIGR02417 261 PLLD-SQLHLATFGDNYLLDFLPLPINSVAQQHRQLAWHALELALAAIDGKKPEPgqRYIPRTLQIRH 327
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
22-60 4.83e-06

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 43.73  E-value: 4.83e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2769562395   22 TRH-IIEVADRLGYRPDPYAASLRTRRSMSIGVLVPRLSD 60
Cdd:smart00354  31 TREkVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
 
Name Accession Description Interval E-value
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
2-315 2.94e-88

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 267.45  E-value: 2.94e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395   2 SRALRAqaDPALSDApsasiTR-HIIEVADRLGYRPDPYAASLRTRRSMSIGVLVPRLSDVVLATIYEGIEQSAALSGYQ 80
Cdd:COG1609    21 SRVLNG--PPRVSEE-----TReRVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLRGIEEAARERGYQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  81 VAVANTYDDPERHRKYLGLMSSRRVDGLILADAHLG---VAQSHPTDVPTVLVNRRCPG--FLSVSGADIVGGGLVASHF 155
Cdd:COG1609    94 LLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDdarLERLAEAGIPVVLIDRPLPDpgVPSVGVDNRAGARLATEHL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 156 ADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIG 235
Cdd:COG1609   174 IELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGPRPTAIFCANDLMALG 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 236 AMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAGQTLIDVLAGKPAAP--TLITPSLKARQSSGP 313
Cdd:COG1609   254 ALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPerVLLPPELVVRESTAP 333


                  ..
gi 2769562395 314 AR 315
Cdd:COG1609   334 AP 335
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 50-311 3.39e-78

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: 239.44  E-value: 3.39e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILADAHLGVAQSH---PTDVP 126
Cdd:cd06285     1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQelaARGVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 127 TVLVNRRCPG--FLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSFD 204
Cdd:cd06285    81 VVLVDRRIGDtaLPSVTVDNELGGRLATRHLLELGHRRIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDERIVPGGFT 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 205 VEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAG 284
Cdd:cd06285   161 IEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEMGRRAA 240

                         250       260
                  ....*....|....*....|....*....
gi 2769562395 285 QTLIDVLAGKPAAPTLIT--PSLKARQSS 311
Cdd:cd06285   241 ELLLQLIEGGGRPPRSITlpPELVVREST 269
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
 51-302 1.00e-70

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: 220.08  E-value: 1.00e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILADAHLG---VAQSHPTDVPT 127
Cdd:cd06267     2 IGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDdelLEELLAAGIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 128 VLVNRRCPG--FLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSFDV 205
Cdd:cd06267    82 VLIDRRLDGlgVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLSTSRERLEGYRDALAEAGLPVDPELVVEGDFSE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 206 EGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAGQ 285
Cdd:cd06267   162 ESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEMGRAAAE 241

                         250
                  ....*....|....*..
gi 2769562395 286 TLIDVLAGKPAAPTLIT 302
Cdd:cd06267   242 LLLERIEGEEEPPRRIV 258
PBP1_PurR cd06275
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ...
 50-310 4.53e-64

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: 203.26  E-value: 4.53e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILA-----DAHLGVAQSHPtD 124
Cdd:cd06275     1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMcsemtDDDAELLAALR-S 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 125 VPTVLVNRRCPG--FLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASS 202
Cdd:cd06275    80 IPVVVLDREIAGdnADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSVSRERLAGFRRALAEAGIEVPPSWIVEGD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 203 FDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRI 282
Cdd:cd06275   160 FEPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQPKDELGEL 239

                         250       260       270
                  ....*....|....*....|....*....|
gi 2769562395 283 AGQTLIDVLAGKPAAPT--LITPSLKARQS 310
Cdd:cd06275   240 AVELLLDRIENKREEPQsiVLEPELIERES 269
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 50-310 4.06e-55

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: 180.16  E-value: 4.06e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILA-----DAHLgvAQSHPTD 124
Cdd:cd06293     1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTpsdddLSHL--ARLRARG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 125 VPTVLVNRRCPGF--LSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASS 202
Cdd:cd06293    79 TAVVLLDRPAPGPagCSVSVDDVQGGALAVDHLLELGHRRIAFVSGPLRTRQVAERLAGARAAVAEAGLDPDEVVRELSA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 203 FD--VEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMG 280
Cdd:cd06293   159 PDanAELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQPSYELG 238

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2769562395 281 RIAGQTLIDVLAGKPAAPTLIT--PSLKARQS 310
Cdd:cd06293   239 RAAADLLLDEIEGPGHPHEHVVfqPELVVRSS 270
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
 51-310 6.92e-55

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: 179.66  E-value: 6.92e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILADAHLGVAQSHPTD--VPTV 128
Cdd:cd06284     2 ILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILLSGRLDAELLSELSkrYPIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 129 LVNRRCP--GFLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSFDVE 206
Cdd:cd06284    82 QCCEYIPdsGVPSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDNVYARERLEGYRRALAEAGLPVDEDLIIEGDFSFE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 207 GGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAGQT 286
Cdd:cd06284   162 AGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIGETAAEL 241

                         250       260
                  ....*....|....*....|....*.
gi 2769562395 287 LIDVLAGKPAAPT--LITPSLKARQS 310
Cdd:cd06284   242 LLEKIEGEGVPPEhiILPHELIVRES 267
PBP1_GalS-like cd06270
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ...
 50-309 1.40e-54

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: 178.87  E-value: 1.40e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLIL-----ADAHLGVAQSHPTd 124
Cdd:cd06270     1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILhsralSDEELILIAEKIP- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 125 vPTVLVNRRCPGFL--SVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASS 202
Cdd:cd06270    80 -PLVVINRYIPGLAdrCVWLDNEQGGRLAAEHLLDLGHRRIACITGPLDIPDARERLAGYRDALAEAGIPLDPSLIIEGD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 203 FDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRI 282
Cdd:cd06270   159 FTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHYPIEEMAQA 238

                         250       260
                  ....*....|....*....|....*...
gi 2769562395 283 AGQTLIDVLAGKPAAPTLI-TPSLKARQ 309
Cdd:cd06270   239 AAELALNLAYGEPLPISHEfTPTLIERD 266
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
 51-309 2.36e-54

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: 178.14  E-value: 2.36e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILA------DAHLGVAQSHptD 124
Cdd:cd06289     2 VGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSpaagttAELLRRLKAW--G 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 125 VPTVLVNRRCPG--FLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASS 202
Cdd:cd06289    80 IPVVLALRDVPGsdLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSSTRRERLAGFRAALAEAGLPLDESLIVPGP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 203 FDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRI 282
Cdd:cd06289   160 ATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHPREIGRR 239

                         250       260
                  ....*....|....*....|....*....
gi 2769562395 283 AGQTLIDVLAGKPAAPT--LITPSLKARQ 309
Cdd:cd06289   240 AARLLLRRIEGPDTPPEriIIEPRLVVRE 268
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
 50-308 1.37e-53

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: 176.30  E-value: 1.37e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILADA-----HLGVAQSHptD 124
Cdd:cd06280     1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSagpsrELKRLLKH--G 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 125 VPTVLVNRRCPGF-LSVSGADIVGGGLVAS-HFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASS 202
Cdd:cd06280    79 IPIVLIDREVEGLeLDLVAGDNREGAYKAVkHLIELGHRRIGLITGPLEISTTRERLAGYREALAEAGIPVDESLIFEGD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 203 FDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRI 282
Cdd:cd06280   159 STIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQPAYEIGRI 238

                         250       260
                  ....*....|....*....|....*...
gi 2769562395 283 AGQTLIDVLAGKPAAPTLI--TPSLKAR 308
Cdd:cd06280   239 AAQLLLERIEGQGEEPRRIvlPTELIIR 266
PBP1_DegA_Like cd19976
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
 50-310 1.98e-52

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: 173.20  E-value: 1.98e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILA------DAHLGVAQSHPT 123
Cdd:cd19976     1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIAssnisdEAIIKLLKEEKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 124 dvPTVLVNRRCP--GFLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVAS 201
Cdd:cd19976    81 --PVVVLDRYIEdnDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPSTYNEHERIEGYKNALQDHNLPIDESWIYSG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 202 SFDVEGGREAARRLLALEPrPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIArELLCP-LSSVDNSVISMG 280
Cdd:cd19976   159 ESSLEGGYKAAEELLKSKN-PTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILS-EYITPaLTTIAQPIFEMG 236

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2769562395 281 RIAGQTLIDVLAGKPAAPT--LITPSLKARQS 310
Cdd:cd19976   237 QEAAKLLLKIIKNPAKKKEeiVLPPELIKRDS 268
PBP1_LacI-like cd06273
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 50-310 2.77e-52

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: 172.69  E-value: 2.77e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILadahlgVAQSHPTDVPTVL 129
Cdd:cd06273     1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLIL------VGSDHDPELFELL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 130 VNRRCP-----------GFLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWAS-TSIDRVTGFRETSRARGLDLPDSA 197
Cdd:cd06273    75 EQRQVPyvltwsydedsPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGNdRARARLAGIRDALAERGLELPEER 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 198 VVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGL-MPGaDIAVVGYNDINIARELLCPLSSVDNSV 276
Cdd:cd06273   155 VVEAPYSIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGIsVPE-DLSITGFDDLELAAHLSPPLTTVRVPA 233

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2769562395 277 ISMGRIAGQTLIDVLAGK-PAAPTLITPSLKARQS 310
Cdd:cd06273   234 REIGELAARYLLALLEGGpPPKSVELETELIVRES 268
PBP1_sucrose_transcription_regulator cd06288
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ...
 50-310 4.51e-52

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: 172.35  E-value: 4.51e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLAT-IYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILADAHLGVAQ--SHPTDVP 126
Cdd:cd06288     1 TIGLITDDIATTPFAGdIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYASMHHREVTlpPELTDIP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 127 TVLVNRR--CPGFLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSFD 204
Cdd:cd06288    81 LVLLNCFddDPSLPSVVPDDEQGGYLATRHLIEAGHRRIAFIGGPEDSLATRLRLAGYRAALAEAGIPYDPSLVVHGDWG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 205 VEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAG 284
Cdd:cd06288   161 RESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVALPYYEMGRRAA 240

                         250       260
                  ....*....|....*....|....*...
gi 2769562395 285 QTLIDVLAGK--PAAPTLITPSLKARQS 310
Cdd:cd06288   241 ELLLDGIEGEppEPGVIRVPCPLIERES 268
PBP1_AglR_RafR-like cd06292
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ...
 51-311 6.68e-51

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: 169.37  E-value: 6.68e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVP----RLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILADAHLG---VAQSHPT 123
Cdd:cd06292     2 IGYVVPelpgGFSDPFFDEFLAALGHAAAARGYDVLLFTASGDEDEIDYYRDLVRSRRVDGFVLASTRHDdprVRYLHEA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 124 DVPTVLVNRRCPG--FLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVAS 201
Cdd:cd06292    82 GVPFVAFGRANPDldFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPEGSVPSDDRLAGYRAALEEAGLPFDPGLVVEG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 202 SFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGR 281
Cdd:cd06292   162 ENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTVRQPIDEIGR 241

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2769562395 282 IAGQTLIDVLAGKPAAPT--LITPSLKARQSS 311
Cdd:cd06292   242 AVVDLLLAAIEGNPSEPReiLLQPELVVRESS 273
PBP1_CcpA-like cd19975
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
 51-295 1.62e-50

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: 168.50  E-value: 1.62e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILADAHLGVAQS---HPTDVPT 127
Cdd:cd19975     2 IGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFASGTLTEENKqllKNMNIPV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 128 VLVNRRC--PGFLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTW-ASTSIDRVTGFRETSRARGLDLPDSAVVASSFD 204
Cdd:cd19975    82 VLVSTESedPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISGPLDdPNAGYPRYEGYKKALKDAGLPIKENLIVEGDFS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 205 VEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGL-MPGaDIAVVGYNDINIARELLCPLSSVDNSVISMGRIA 283
Cdd:cd19975   162 FKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIrVPE-DISVIGFDNTEIAEMSIPPLTTVSQPFYEMGKKA 240

                         250
                  ....*....|..
gi 2769562395 284 GQTLIDVLAGKP 295
Cdd:cd19975   241 VELLLDLIKNEK 252
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
 51-299 1.16e-49

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: 165.78  E-value: 1.16e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILA------DAHLGVAQSHptd 124
Cdd:cd19977     2 IGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAptggneDLIEKLVKSG--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 125 VPTVLVNRRCPGFlsvsGADIV------GGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSaV 198
Cdd:cd19977    79 IPVVFVDRYIPGL----DVDTVvvdnfkGAYQATEHLIELGHKRIAFITYPLELSTRQERLEGYKAALADHGLPVDEE-L 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 199 VASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGL-MPGaDIAVVGYNDINIARELLCPLSSVDNSVI 277
Cdd:cd19977   154 IKHVDRQDDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLrIPD-DIALIGFDDIPWADLFNPPLTVIAQPTY 232

                         250       260
                  ....*....|....*....|..
gi 2769562395 278 SMGRIAGQTLIDVLAGKPAAPT 299
Cdd:cd19977   233 EIGRKAAELLLDRIENKPKGPP 254
PBP1_LacI-like cd06299
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ...
 50-310 5.85e-49

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: 164.37  E-value: 5.85e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILA---DAHLGVAQSHPTDVP 126
Cdd:cd06299     1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVptgENSEGLQALIAQGLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 127 TVLVNRRCPGFLSVS--GADIVGG-GLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSF 203
Cdd:cd06299    81 VVFVDREVEGLGGVPvvTSDNRPGaREAVEYLVSLGHRRIGYISGPLSTSTGRERLAAFRAALTAAGIPIDEELVAFGDF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 204 DVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIA 283
Cdd:cd06299   161 RQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVERIGRRA 240

                         250       260
                  ....*....|....*....|....*...
gi 2769562395 284 GQTLIDVLA-GKPAAPTLITPSLKARQS 310
Cdd:cd06299   241 VELLLALIEnGGRATSIRVPTELIPRES 268
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
 51-310 7.01e-49

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


Pssm-ID: 380514 [Multi-domain]  Cd Length: 264  Bit Score: 163.85  E-value: 7.01e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILADAHLGVAQSHPTDVPTVLV 130
Cdd:cd06291     2 IGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILGSHSLDIEEYKKLNIPIVSI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 131 NRRC-PGFLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSFDVEGGR 209
Cdd:cd06291    82 DRYLsEGIPSVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIEIDENDFSEEDAY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 210 EAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAGQTLID 289
Cdd:cd06291   162 ELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIEEMAKEAVELLLK 241

                         250       260
                  ....*....|....*....|...
gi 2769562395 290 VLAGKPAAPTLIT--PSLKARQS 310
Cdd:cd06291   242 LIEGEEIEESRIVlpVELIERET 264
PBP1_LacI-like cd06290
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 50-310 4.78e-47

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


Pssm-ID: 380513 [Multi-domain]  Cd Length: 267  Bit Score: 159.32  E-value: 4.78e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILADAHLGVAQS--HPTDVPT 127
Cdd:cd06290     1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEELLklLAEGIPV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 128 VLVNRRCPG--FLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSFDV 205
Cdd:cd06290    81 VLVDRELEGlnLPVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDHPDAQERYAGYRRALEDAGLEVDPRLIVEGDFTE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 206 EGGREAARRLLAlEPRP-TAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAG 284
Cdd:cd06290   161 ESGYEAMKKLLK-RGGPfTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYEMGKTAA 239

                         250       260
                  ....*....|....*....|....*...
gi 2769562395 285 QTLIDVLAGKPAAPTLITPSLK--ARQS 310
Cdd:cd06290   240 EILLELIEGKGRPPRRIILPTElvIRES 267
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 51-310 1.24e-44

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: 153.07  E-value: 1.24e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTyDDPERHRKYLGLMSSRRVDGLILADAHLG---VAQSHPTDVPT 127
Cdd:cd06278     2 VGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNV-DDEDDVDDALRQLLQYRVDGVIVTSATLSselAEECARRGIPV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 128 VLVNRR--CPGFLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPdsAVVASSFDV 205
Cdd:cd06278    81 VLFNRVveDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPEGTSTSRERERGFRAALAELGLPPP--AVEAGDYSY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 206 EGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLM-PGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAG 284
Cdd:cd06278   159 EGGYEAARRLLAAPDRPDAIFCANDLMALGALDAARQEGGLvVPEDISVVGFDDIPMAAWPSYDLTTVRQPIEEMAEAAV 238

                         250       260
                  ....*....|....*....|....*...
gi 2769562395 285 QTLIDVLAGKPAAP--TLITPSLKARQS 310
Cdd:cd06278   239 DLLLERIENPETPPerRVLPGELVERGS 266
PRK10423 PRK10423
transcriptional repressor RbsR; Provisional
 18-310 1.72e-43

transcriptional repressor RbsR; Provisional


Pssm-ID: 182448 [Multi-domain]  Cd Length: 327  Bit Score: 151.78  E-value: 1.72e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  18 SASITRHIIEVADRLGYRPDPYAASLRTRRSMSIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYL 97
Cdd:PRK10423   26 SEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVERSCFERGYSLVLCNTEGDEQRMNRNL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  98 GLMSSRRVDGLIL--ADAHL---GVAQSHPTdVPTVLVNRrCPgFLSVSgaDIV------GGGLVASHFADLGHDHLGVI 166
Cdd:PRK10423  106 ETLMQKRVDGLLLlcTETHQpsrEIMQRYPS-VPTVMMDW-AP-FDGDS--DLIqdnsllGGDLATQYLIDKGYTRIACI 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 167 AGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLM 246
Cdd:PRK10423  181 TGPLDKTPARLRLEGYRAAMKRAGLNIPDGYEVTGDFEFNGGFDAMQQLLALPLRPQAVFTGNDAMAVGVYQALYQAGLS 260

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2769562395 247 PGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAGQTLIDVLAGKPAAPTLI--TPSLKARQS 310
Cdd:PRK10423  261 VPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQRLqlTPELMERGS 326
PBP1_LacI cd01574
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ...
 50-310 2.69e-43

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: 149.65  E-value: 2.69e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANT-YDDPERHRKYLGLMSSRRVDGLILADAH---LGVAQSHPTDV 125
Cdd:cd01574     1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATVdEDDPASVREALDRLLSQRVDGIIVIAPDeavLEALRRLPPGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 126 PTVLVNRRC-PGFLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDsaVVASSFD 204
Cdd:cd01574    81 PVVIVGSGPsPGVPTVSIDQEEGARLATRHLLELGHRRIAHIAGPLDWVDARARLRGWREALEEAGLPPPP--VVEGDWS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 205 VEGGREAARRLLAlEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAG 284
Cdd:cd01574   159 AASGYRAGRRLLD-DGPVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDFAELGRRAV 237

                         250       260
                  ....*....|....*....|....*...
gi 2769562395 285 QTLIDVLAGKPAAP--TLITPSLKARQS 310
Cdd:cd01574   238 ELLLALIEGPAPPPesVLLPPELVVRES 265
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
 51-310 4.34e-42

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: 146.49  E-value: 4.34e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILADAHlgvaqsHPTDVPTVLV 130
Cdd:cd01575     2 VAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTE------HTPATRKLLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 131 NRRCP----GFLSVSGADI-VG------GGLVASHFADLGHDHLGVIAGPTWAST-SIDRVTGFRETSRARGLDLPDSAV 198
Cdd:cd01575    76 AAGIPvvetWDLPDDPIDMaVGfsnfaaGRAMARHLIERGYRRIAFVGARLDGDSrARQRLEGFRDALAEAGLPLPLVLL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 199 VASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGL-MPGaDIAVVGYNDINIARELLCPLSSVDNSVI 277
Cdd:cd01575   156 VELPSSFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIrVPG-DIAIAGFGDLDIAAALPPALTTVRVPRY 234

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2769562395 278 SMGRIAGQTLIDVLAGKPAAPTLIT--PSLKARQS 310
Cdd:cd01575   235 EIGRKAAELLLARLEGEEPEPRVVDlgFELVRRES 269
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
 51-303 2.52e-41

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: 144.17  E-value: 2.52e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLIL-----ADAHLGVAQShpTDV 125
Cdd:cd01542     2 IGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILfateiTDEHRKALKK--LKI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 126 PTVLVNRRCPGFLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTW-ASTSIDRVTGFRETSRARGLDLPDsaVVASSFD 204
Cdd:cd01542    80 PVVVLGQEHEGFSCVYHDDYGAGKLLGEYLLKKGHKNIAYIGVDEEdIAVGVARKQGYLDALKEHGIDEVE--IVETDFS 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 205 VEGGREAARRLLALEPrPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAG 284
Cdd:cd01542   158 MESGYEAAKELLKENK-PDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEAGEKAA 236

                         250
                  ....*....|....*....
gi 2769562395 285 QTLIDVLAGKPAAPTLITP 303
Cdd:cd01542   237 ELLLDMIEGEKVPKKQKLP 255
PBP1_SalR cd01545
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ...
 51-310 3.62e-41

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: 144.24  E-value: 3.62e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVAN-TYDDPERHRKYLGLMSSRRVDGLILA----DAHLGVAQSHPTDV 125
Cdd:cd01545     2 IGLLYDNPSASYVSALQVGALRACREAGYHLVVEPcDSDDEDLADRLRRFLSRSRPDGVILTpplsDDPALLDALDELGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 126 PTVLVNRRC--PGFLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSF 203
Cdd:cd01545    82 PYVRIAPGTddDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGPPDHGASAERLEGFRDALAEAGLPLDPDLVVQGDF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 204 DVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIA 283
Cdd:cd01545   162 TFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTTVRQPIAEMARRA 241

                         250       260
                  ....*....|....*....|....*....
gi 2769562395 284 GQTLIDVLAGKPAAPTLIT--PSLKARQS 310
Cdd:cd01545   242 VELLIAAIRGAPAGPERETlpHELVIRES 270
PRK10703 PRK10703
HTH-type transcriptional repressor PurR;
32-315 1.07e-39

HTH-type transcriptional repressor PurR;


Pssm-ID: 236739 [Multi-domain]  Cd Length: 341  Bit Score: 142.17  E-value: 1.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  32 LGYRPDPYAASLRTRRSMSIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLIL- 110
Cdd:PRK10703   43 LHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEAVEKNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVm 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 111 ----ADAHLGVAQSHpTDVPTVLVNRrcpGFLSVSGADIV------GGGLVASHFADLGHDHLGVIAGPTWASTSIDRVT 180
Cdd:PRK10703  123 cseyPEPLLAMLEEY-RHIPMVVMDW---GEAKADFTDAIidnafeGGYLAGRYLIERGHRDIGVIPGPLERNTGAGRLA 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 181 GFRETSRARGLDLPDSAVVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDIN 260
Cdd:PRK10703  199 GFMKAMEEANIKVPEEWIVQGDFEPESGYEAMQQILSQKHRPTAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVR 278

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2769562395 261 IARELLCPLSSVDNSVISMGRIAGQTLIDVLAGKPAAPTLI--TPSLKARQS--SGPAR 315
Cdd:PRK10703  279 NARYFTPALTTIHQPKDRLGETAFNMLLDRIVNKREEPQTIevHPRLVERRSvaDGPFR 337
PBP1_LacI-like cd06281
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 50-310 1.57e-36

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: 131.98  E-value: 1.57e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILA---DAHLGVAQSHP-TDV 125
Cdd:cd06281     1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILTpgdEDDPELAAALArLDI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 126 PTVLVNRRCPGFLSVSGADIVGGGLVA-SHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSFD 204
Cdd:cd06281    81 PVVLIDRDLPGDIDSVLVDHRSGVRQAtEYLLSLGHRRIALLTGGPDIRPGRERIAGFKAAFAAAGLPPDPDLVRLGSFS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 205 VEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAG 284
Cdd:cd06281   161 ADSGFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDLDAVGRAAA 240

                         250       260
                  ....*....|....*....|....*....
gi 2769562395 285 QTLIDVLAGKPAAPT---LITPSLKARQS 310
Cdd:cd06281   241 ELLLDRIEGPPAGPPrriVVPTELILRDS 269
PBP1_CcpB-like cd06286
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ...
 51-308 2.81e-36

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: 131.13  E-value: 2.81e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILAD-----------AHLG--- 116
Cdd:cd06286     2 IGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLIITSrendweviepyAKYGpiv 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 117 -VAQSHPTDVPTVLVNRRcPGFLsvsgadivgggLVASHFADLGHDHLGVIAG--PTWASTSIDRVTGFRETSRARGLDL 193
Cdd:cd06286    82 lCEETDSPDIPSVYIDRY-EAYL-----------EALEYLKEKGHRKIGYCLGrpESSSASTQARLKAYQDVLGEHGLSL 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 194 PDSAVVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELlcPLSSVD 273
Cdd:cd06286   150 REEWIFTNCHTIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISELL--NLTTID 227

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2769562395 274 NSVISMGRIAGQTLIDVLAGKPAAPTLITPSLKAR 308
Cdd:cd06286   228 QPLEEMGKEAFELLLSQLESKEPTKKELPSKLIER 262
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
 51-310 5.63e-36

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: 130.76  E-value: 5.63e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILAdahlGVAQSHPTD------ 124
Cdd:cd01541     2 IGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIE----PTKSALPNPnldlye 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 125 ------VPTVLVNRRCPGF--LSVSGADIVGGGLVASHFADLGHDHLGVIAgPTWASTSIDRVTGFRETSRARGLDLPDS 196
Cdd:cd01541    78 elqkkgIPVVFINSYYPELdaPSVSLDDEKGGYLATKHLIDLGHRRIAGIF-KSDDLQGVERYQGFIKALREAGLPIDDD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 197 AVV---ASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGL-MPGaDIAVVGYNDINIARELLCPLSSV 272
Cdd:cd01541   157 RILwysTEDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLrVPE-DLSVVGFDDSYLASLSEPPLTSV 235

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2769562395 273 DNSVISMGRIAGQTLIDVL-AGKPAAPTLITPSLKARQS 310
Cdd:cd01541   236 VHPKEELGRKAAELLLRMIeEGRKPESVIFPPELIERES 274
PBP1_CatR-like cd06296
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ...
 51-295 6.19e-36

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: 130.47  E-value: 6.19e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILA-----DAHLGVAQShpTDV 125
Cdd:cd06296     2 IDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVtsdptSRQLRLLRS--AGI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 126 PTVLVNRRC---PGFLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASS 202
Cdd:cd06296    80 PFVLIDPVGepdPDLPSVGATNWAGGRLATEHLLDLGHRRIAVITGPPRSVSGRARLAGYRAALAEAGIAVDPDLVREGD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 203 FDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRI 282
Cdd:cd06296   160 FTYEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVHQPLREMGAV 239

                         250
                  ....*....|...
gi 2769562395 283 AGQTLIDVLAGKP 295
Cdd:cd06296   240 AVRLLLRLLEGGP 252
PBP1_LacI-like cd06282
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 51-303 2.59e-35

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: 128.55  E-value: 2.59e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLIL----ADAHLGVAQSHPTDVP 126
Cdd:cd06282     2 IGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILtvgdAQGSEALELLEEEGVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 127 TVLV----NRRCPGFLSVSgaDIVGGGLVASHFADLGHDHLGVIAGPTWAST-SIDRVTGFRETSRARGLDLPDsaVVAS 201
Cdd:cd06282    82 YVLLfnqtENSSHPFVSVD--NRLASYDVAEYLIALGHRRIAMVAGDFSASDrARLRYQGYRDALKEAGLKPIP--IVEV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 202 SFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGR 281
Cdd:cd06282   158 DFPTNGLEEALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQPSRDMGR 237

                         250       260
                  ....*....|....*....|..
gi 2769562395 282 IAGQTLIDVLAGKPAAPTLITP 303
Cdd:cd06282   238 AAADLLLAEIEGESPPTSIRLP 259
PRK11041 PRK11041
DNA-binding transcriptional regulator CytR; Provisional
 18-315 8.41e-34

DNA-binding transcriptional regulator CytR; Provisional


Pssm-ID: 182923 [Multi-domain]  Cd Length: 309  Bit Score: 125.88  E-value: 8.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  18 SASiTRHIIEVADR-LGYRPDPYAASLRTRRSMSIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKY 96
Cdd:PRK11041    5 SQA-TRQRVEQAVLeVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTF 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  97 LGLMSSRRVDGLILADAHLgvaqshPTDV---------PTVLVNRRCPGF-LSVSGADIVGGGLVA-SHFADLGHDHLGV 165
Cdd:PRK11041   84 VNLIITKQIDGMLLLGSRL------PFDAskeeqrnlpPMVMANEFAPELeLPTVHIDNLTAAFEAvNYLHELGHKRIAC 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 166 IAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGL 245
Cdd:PRK11041  158 IAGPEEMPLCHYRLQGYVQALRRCGITVDPQYIARGDFTFEAGAKALKQLLDLPQPPTAVFCHSDVMALGALSQAKRMGL 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2769562395 246 MPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAGQTLIDVLAGKPAAP--TLITPSLKARQSSGPAR 315
Cdd:PRK11041  238 RVPQDLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSSgsRLLDCELIIRGSTAAPP 309
PBP1_MalR-like cd06294
ligand-binding domain of maltose transcription regulator MalR which is a member of the ...
 51-302 2.01e-33

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: 123.85  E-value: 2.01e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVV-----LATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILADAHLG---VAQSHP 122
Cdd:cd06294     2 IGLVLPSSAEELfqnpfFSEVLRGISQVANENGYSLLLATGNTEEELLEEVKRMVRGRRVDGFILLYSKEDdplIEYLKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 123 TDVPTVLVNR--RCPGFLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVA 200
Cdd:cd06294    82 EGFPFVVIGKplDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVSIDRLQGYKQALKEAGLPLDDDYILL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 201 SSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMG 280
Cdd:cd06294   162 LDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSVDINPYELG 241

                         250       260
                  ....*....|....*....|..
gi 2769562395 281 RIAGQTLIDVLAGKPAAPTLIT 302
Cdd:cd06294   242 REAAKLLINLLEGPESLPKNVI 263
PBP1_AglR-like cd20010
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ...
 50-305 3.06e-32

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


Pssm-ID: 380665 [Multi-domain]  Cd Length: 269  Bit Score: 120.73  E-value: 3.06e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVP----RLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILADAHLG---VAQSHP 122
Cdd:cd20010     1 AIGLVLPldpgDLGDPFFLEFLAGLSEALAERGLDLLLAPAPSGEDELATYRRLVERGRVDGFILARTRVNdprIAYLLE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 123 TDVPTVlVNRRCPGFLSVSGADI--VGGGLVA-SHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVV 199
Cdd:cd20010    81 RGIPFV-VHGRSESGAPYAWVDIdnEGAFRRAtRRLLALGHRRIALLNGPEELNFAHQRRDGYRAALAEAGLPVDPALVR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 200 ASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCP-LSSVDNSVIS 278
Cdd:cd20010   160 EGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLLPALEYFSPpLTTTRSSLRD 239

                         250       260
                  ....*....|....*....|....*....
gi 2769562395 279 MGRIAGQTLIDVLAGKPAAP--TLITPSL 305
Cdd:cd20010   240 AGRRLAEMLLALIDGEPAAElqELWPPEL 268
PBP1_GalR cd01544
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ...
 65-310 9.71e-31

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: 116.47  E-value: 9.71e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  65 TIYEGIEQSAALSGYQVAVANTYDDPERHRkylglmsSRRVDGLILadahLG------VAQSHPTDVPTVLVNRRC--PG 136
Cdd:cd01544    21 SIRLGIEKEAKKLGYEIKTIFRDDEDLESL-------LEKVDGIIA----IGkfskeeIEKLKKLNPNIVFVDSNPdpDG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 137 FLSVSgADIVGGGLVA-SHFADLGHDHLGVIAGPTWASTSID-----RVTGFRETSRARGLDLPDsAVVASSFDVEGGRE 210
Cdd:cd01544    90 FDSVV-PDFEQAVRQAlDYLIELGHRRIGFIGGKEYTSDDGEeiedpRLRAFREYMKEKGLYNEE-YIYIGEFSVESGYE 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 211 AARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAGQTLIDV 290
Cdd:cd01544   168 AMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTPPLTTVHIPTEEMGRTAVRLLLER 247

                         250       260
                  ....*....|....*....|..
gi 2769562395 291 LAGKPAAP--TLITPSLKARQS 310
Cdd:cd01544   248 INGGRTIPkkVLLPTKLIERES 269
PBP1_CelR cd06295
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ...
 46-310 1.00e-30

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: 116.58  E-value: 1.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  46 RRSMSIGVLVP-------RLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGlmsSRRVDGLIL---ADAHL 115
Cdd:cd06295     1 QRSRTIAVVVPmdphgdqSITDPFFLELLGGISEALTDRGYDMLLSTQDEDANQLARLLD---SGRADGLIVlgqGLDHD 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 116 GVAQSHPTDVPTVLVNRRCPG--FLSVSGADIVGGGLVASHFADLGHDHLGVIaGPTWASTSIDRVTGFRETSRARGLDL 193
Cdd:cd06295    78 ALRELAQQGLPMVVWGAPEDGqsYCSVGSDNVKGGALATEHLIEIGRRRIAFL-GDPPHPEVADRLQGYRDALAEAGLEA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 194 PDSAVVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVD 273
Cdd:cd06295   157 DPSLLLSCDFTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFRPPLTTVR 236

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2769562395 274 NSVISMGRIAGQTLIDVLAGKPAAPTLITPSLKARQS 310
Cdd:cd06295   237 QDLALAGRLLVEKLLALIAGEPVTSSMLPVELVVRES 273
PBP1_LacI-like cd06279
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ...
 50-310 5.59e-30

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: 115.00  E-value: 5.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPR-----LSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMssrrVDGLILadahLGVAQSHPT- 123
Cdd:cd06279     1 AIGVLLPDdlsyaFSDPVAAQFLRGVAEVCEEEGLGLLLLPATDEGSAAAAVRNAA----VDGFIV----YGLSDDDPAv 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 124 ------DVPTVLV-NRRCPGFLSVSGADIVGGGLVASHFADLGHDHLGVIAGP-----------------TWASTSIDRV 179
Cdd:cd06279    73 aalrrrGLPLVVVdGPAPPGIPSVGIDDRAAARAAARHLLDLGHRRIAILSLRldrgrergpvsaerlaaATNSVARERL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 180 TGFRETSRARGLDLPDSAVV-ASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYND 258
Cdd:cd06279   153 AGYRDALEEAGLDLDDVPVVeAPGNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRVPEDLSVTGFDD 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2769562395 259 INIARELLCPLSSVDNSVISMGRIAGQTLIDVLAGKPAAPTLITPSLKARQS 310
Cdd:cd06279   233 IPEAAAADPGLTTVRQPAVEKGRAAARLLLGLLPGAPPRPVILPTELVVRAS 284
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
 50-301 5.74e-30

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: 114.65  E-value: 5.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLI----LADAHLGVAQSHPTDV 125
Cdd:cd01537     1 RIGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAinlvDPAAAGVAEKARGQNV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 126 PTVLVNR---RCPGFLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASS 202
Cdd:cd01537    81 PVVFFDKepsRYDKAYYVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKTEQLQLDTGD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 203 FDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRI 282
Cdd:cd01537   161 WDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDANNLGKT 240

                         250
                  ....*....|....*....
gi 2769562395 283 AGQTLIDVLAGKPAAPTLI 301
Cdd:cd01537   241 TFDLLLNLADNWKIDNKVV 259
PBP1_hexuronate_repressor-like cd06272
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ...
 51-309 1.08e-29

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: 113.62  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVV-LATIYEGIEQSAALSGYQ-VAVANTYDDPERHRKyLGLMSSRRVDGLILA---DAHLGVAQSHPTDV 125
Cdd:cd06272     2 IGLYWPSVGERVaLTRLLSGINEAISKQGYNiNLSICPYKVGHLCTA-KGLFSENRFDGVIVFgisDSDIEYLNKNKPKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 126 PTVLVNRRCPGFLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSFDV 205
Cdd:cd06272    81 PIVLYNRESPKYSTVNVDNEKAGRLAVLLLIQKGHKSIAYIGNPNSNRNQTLRGKGFIETCEKHGIHLSDSIIDSRGLSI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 206 EGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDnsvISMGRIAG- 284
Cdd:cd06272   161 EGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLTVVG---VPIEKIAEe 237

                         250       260
                  ....*....|....*....|....*....
gi 2769562395 285 --QTLIDVLAGKPAAPT--LITPSLKARQ 309
Cdd:cd06272   238 slRLILKLIEGRENEIQqlILYPELIFRE 266
PRK10401 PRK10401
HTH-type transcriptional regulator GalS;
25-310 5.82e-27

HTH-type transcriptional regulator GalS;


Pssm-ID: 236681 [Multi-domain]  Cd Length: 346  Bit Score: 108.33  E-value: 5.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  25 IIEVADRLGYRPDPYAASLRTRRSMSIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRR 104
Cdd:PRK10401   36 VMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAVDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQR 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 105 VDGLI-----LADAHLGVAQSHptdVP-TVLVNRRCPGFL-SVSGADIVGGGLVASH-FADLGHDHLGVIAGPTWASTSI 176
Cdd:PRK10401  116 CNALIvhskaLSDDELAQFMDQ---IPgMVLINRVVPGYAhRCVCLDNVSGARMATRmLLNNGHQRIGYLSSSHGIEDDA 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 177 DRVTGFRETSRARGLDLPDSAVVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGY 256
Cdd:PRK10401  193 MRRAGWMSALKEQGIIPPESWIGTGTPDMQGGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGF 272

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2769562395 257 NDINIARELLCPLSSVDNSVISMGRIAGQTLIDVLAGK--PAAPTLITPSLKARQS 310
Cdd:PRK10401  273 DDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNldPRASHCFMPTLVRRHS 328
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
 154-311 1.12e-26

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: 102.80  E-value: 1.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 154 HFADLGHDHLGVIA--GPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSFDVEGGREaaRRLLALEPRPTAIFAVNDY 231
Cdd:pfam13377   1 HLAELGHRRIALIGpeGDRDDPYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAAR--ERLRWLGALPTAVFVANDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 232 AAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAGQTLIDVLAGKPAAP--TLITPSLKARQ 309
Cdd:pfam13377  79 VALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPerVLLPPELVERE 158


                  ..
gi 2769562395 310 SS 311
Cdd:pfam13377 159 ST 160
PBP1_RegR_EndR_KdgR-like cd06283
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ...
 51-304 1.74e-25

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: 102.63  E-value: 1.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLIL------ADAHLGVAQSHptd 124
Cdd:cd06283     2 IGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILqptgnnNDAYLELAQKG--- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 125 VPTVLVNRRCPGFlsvsGADIVGGGL------VASHFADLGHDHLGVIAGP-TWASTSIDRVTGFRETSRARGLDLPDSA 197
Cdd:cd06283    79 LPVVLVDRQIEPL----NWDTVVTDNydatyeATEHLKEQGYERIVFVTEPiKGISTRRERLQGFLDALARYNIEGDVYV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 198 VvassfDVEGGREAARRLLAL----EPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVD 273
Cdd:cd06283   155 I-----EIEDTEDLQQALAAFlsqhDGGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIR 229

                         250       260       270
                  ....*....|....*....|....*....|..
gi 2769562395 274 NSVISMGRIAGQTLIDVLAGK-PAAPTLITPS 304
Cdd:cd06283   230 QPTYEIGKAAAEILLERIEGDsGEPKEIELPS 261
PBP1_AglR_RafR-like cd06271
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ...
 69-305 2.98e-23

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: 96.34  E-value: 2.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  69 GIEQSAALSGYQVAVAnTYDDPERHRKYLGLMSSRRVDGLILADAHLG---VAQSHPTDVPTVLVNR-RCP-GFLSVSGA 143
Cdd:cd06271    23 GITEEAGTTGYHLLVW-PFEEAES*VPIRDLVETGSADGVILSEIEPNdprVQFLTKQNFPFVAHGRsD*PiGHAWVDID 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 144 DIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASsfdVEGGREAARRLLALEPRPT 223
Cdd:cd06271   102 NEAGAYEAVERLAGLGHRRIAFIVPPARYSPHDRRLQGYVRA*RDAGLTGYPLDADTT---LEAGRAAAQRLLALSPRPT 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 224 AIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCP-LSSVDNSVISMGRIAGQTLIDVLAGKPAA--PTL 300
Cdd:cd06271   179 AIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSAPFLGAMITPpLTTVHAPIAEAGRELAKALLARIDGEDPEtlQVL 258


                  ....*
gi 2769562395 301 ITPSL 305
Cdd:cd06271   259 VQPSL 263
fruct_sucro_rep TIGR02417
D-fructose-responsive transcription factor; Members of this family belong the lacI ...
 18-309 6.05e-23

D-fructose-responsive transcription factor; Members of this family belong the lacI helix-turn-helix family (pfam00356) of DNA-binding transcriptional regulators. All members are from the proteobacteria. Characterized members act as positive and negative transcriptional regulators of fructose and sucrose transport and metabolism. Sucrose is a disaccharide composed of fructose and glucose; D-fructose-1-phosphate rather than an intact sucrose moiety has been shown to act as the inducer. [Regulatory functions, DNA interactions]


Pssm-ID: 131470 [Multi-domain]  Cd Length: 327  Bit Score: 96.74  E-value: 6.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  18 SASITRHIIEVADRLGYRPDPYAASLRTRRSMSIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYL 97
Cdd:TIGR02417  30 SQETVERVMAVVREQGYQPNIHAASLRAGRSRTIGLVIPDLENYSYARIAKELEQQCREAGYQLLIACSDDNPDQEKVVI 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  98 GLMSSRRVDGLIladahlgVAQSHPTD-----------VPTVLVNRRCP--GFLSVSGADIVGGGLVASHFADLGHDHLG 164
Cdd:TIGR02417 110 ENLLARQVDALI-------VASCMPPEdayyqklqnegLPVVALDRSLDdeHFCSVISDDVDAAAELIERLLSQHADEFW 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 165 VIAGPTWASTSIDRVTGFRETsrARGLDLPDSAVVASSFDVEGGREAARRLLALEPR-PTAIFAVNDYAAIGAMGEMRDQ 243
Cdd:TIGR02417 183 YLGAQPELSVSRDRLAGFRQA--LKQATLEVEWVYGGNYSRESGYQMFAKLCARLGRlPQALFTTSYTLLEGVLDYMLER 260

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2769562395 244 GLMPgADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAGQTLIDVLAGKPAAP--TLITPSLKARQ 309
Cdd:TIGR02417 261 PLLD-SQLHLATFGDNYLLDFLPLPINSVAQQHRQLAWHALELALAAIDGKKPEPgqRYIPRTLQIRH 327
PBP1_CcpA cd06298
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ...
 50-283 8.98e-23

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: 95.05  E-value: 8.98e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILADAHLG---VAQSHPTDVP 126
Cdd:cd06298     1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMGDELTeeiREEFKRSPVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 127 TVLVNRRCPG--FLSV------SGADIVggglvaSHFADLGHDHLGVIAGPTWASTSID-RVTGFRETSRARGLDLPDSA 197
Cdd:cd06298    81 VVLAGTVDSDheIPSVnidyeqAAYDAT------KSLIDKGHKKIAFVSGPLKEYINNDkKLQGYKRALEEAGLEFNEPL 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 198 VVASSFDVEGGREAARRLLALEpRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIArELLCP-LSSVDNSV 276
Cdd:cd06298   155 IFEGDYDYDSGYELYEELLESG-EPDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYA-TMSRPqLTSINQPL 232


                  ....*..
gi 2769562395 277 ISMGRIA 283
Cdd:cd06298   233 YDIGAVA 239
lacI PRK09526
lac repressor; Reviewed
 13-315 2.24e-22

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 95.45  E-value: 2.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  13 LSDAPSASI-TRHIIEVA-DRLGYRPDPYAASLRTRRSMSIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVAnTYDDP 90
Cdd:PRK09526   26 LNQASHVSAkTREKVEAAmAELNYVPNRVAQQLAGKQSLTIGLATTSLALHAPSQIAAAIKSRADQLGYSVVIS-MVERS 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  91 ERH--RKYLGLMSSRRVDGLIL-----ADAHLGVAQSHPtDVPTVL--VNRRCPGFlSVSGADIVGGGLVASHFADLGHD 161
Cdd:PRK09526  105 GVEacQAAVNELLAQRVSGVIInvpleDADAEKIVADCA-DVPCLFldVSPQSPVN-SVSFDPEDGTRLGVEHLVELGHQ 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 162 HLGVIAGPTWASTSIDRVTGFRETSRARGLDlpDSAVVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMR 241
Cdd:PRK09526  183 RIALLAGPESSVSARLRLAGWLEYLTDYQLQ--PIAVREGDWSAMSGYQQTLQMLREGPVPSAILVANDQMALGVLRALH 260

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2769562395 242 DQGLMPGADIAVVGYNDiniARELLC---PLSSVDNSVISMGRIAGQTLIDVLAGKPAAPTLITP-SLKARQSSGPAR 315
Cdd:PRK09526  261 ESGLRVPGQISVIGYDD---TEDSSYfipPLTTIKQDFRLLGKEAVDRLLALSQGQAVKGSQLLPtSLVVRKSTAPPN 335
PBP1_FruR cd06274
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ...
 50-253 4.36e-22

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


Pssm-ID: 380498 [Multi-domain]  Cd Length: 264  Bit Score: 93.04  E-value: 4.36e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILA-----DAHLGVAQSHptD 124
Cdd:cd06274     1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVApstppDDIYYLCQAA--G 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 125 VPTVLVNRRCPG--FLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASS 202
Cdd:cd06274    79 LPVVFLDRPFSGsdAPSVVSDNRAGARALTEKLLAAGPGEIYFLGGRPELPSTAERIRGFRAALAEAGITEGDDWILAEG 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2769562395 203 FDVEGGREAARRLLA-LEPRPTAIFaVNDYAAI-GAMGEMRDQGLMPGADIAV 253
Cdd:cd06274   159 YDRESGYQLMAELLArLGGLPQALF-TSSLTLLeGVLRFLRERLGAIPSDLVL 210
PRK10727 PRK10727
HTH-type transcriptional regulator GalR;
13-313 4.96e-22

HTH-type transcriptional regulator GalR;


Pssm-ID: 182681 [Multi-domain]  Cd Length: 343  Bit Score: 94.44  E-value: 4.96e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  13 LSDAPSAS-ITRHIIEVA-DRLGYRPDPYAASLRTRRSMSIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDP 90
Cdd:PRK10727   22 INNSPKASeASRLAVHSAmESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKAVEQVAYHTGNFLLIGNGYHNE 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  91 ERHRKYLGLMSSRRVDGLI-----LADAHLGVAQSHptdVP-TVLVNRRCPGFLS--VSGADIVGGGLVASHFADLGHDH 162
Cdd:PRK10727  102 QKERQAIEQLIRHRCAALVvhakmIPDAELASLMKQ---IPgMVLINRILPGFENrcIALDDRYGAWLATRHLIQQGHTR 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 163 LGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRD 242
Cdd:PRK10727  179 IGYLCSNHSISDAEDRLQGYYDALAESGIPANDRLVTFGEPDESGGEQAMTELLGRGRNFTAVACYNDSMAAGAMGVLND 258

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2769562395 243 QGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAGQTLIDVLAGKPAAPT--LITPSLKARQSSGP 313
Cdd:PRK10727  259 NGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELALALADNRPLPEItnVFSPTLVRRHSVST 331
PBP1_LacI-like cd06277
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 64-306 1.01e-21

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: 92.30  E-value: 1.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  64 ATIYEGIEQSAALSGYQVAVANTYDDPERHrKYLGLMSSRRVDGLILadahLG-------VAQSHPTDVPTVLVNRRCP- 135
Cdd:cd06277    22 SELIDGIEREARKYGYNLLISSVDIGDDFD-EILKELTDDQSSGIIL----LGteleekqIKLFQDVSIPVVVVDNYFEd 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 136 -GFLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGL-DLPDSAVVASSfDVEGGREAAR 213
Cdd:cd06277    97 lNFDCVVIDNEDGAYEAVKYLVELGHTRIGYLASSYRIKNFEERRRGFRKAMRELGLsEDPEPEFVVSV-GPEGAYKDMK 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 214 RLLA-LEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAGQTLIDVLA 292
Cdd:cd06277   176 ALLDtGPKLPTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRRLIEKIK 255

                         250
                  ....*....|....
gi 2769562395 293 GKPAAPTLITPSLK 306
Cdd:cd06277   256 DPDGGTLKILVSTK 269
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 51-303 7.90e-21

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: 90.75  E-value: 7.90e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILA--DAHLG---VAQSHPTDV 125
Cdd:COG1879    36 IGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVSpvDPDALapaLKKAKAAGI 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 126 PTVLVNRRCPGFLSVS--GADIVGGG-LVASHFADL--GHDHLGVIAGPTWASTSIDRVTGFRETSRARgldlPDSAVVA 200
Cdd:COG1879   116 PVVTVDSDVDGSDRVAyvGSDNYAAGrLAAEYLAKAlgGKGKVAILTGSPGAPAANERTDGFKEALKEY----PGIKVVA 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 201 SS---FDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPgaDIAVVGYNDINIARELLCP---LSSVDN 274
Cdd:COG1879   192 EQyadWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRKG--DVKVVGFDGSPEALQAIKDgtiDATVAQ 269

                         250       260
                  ....*....|....*....|....*....
gi 2769562395 275 SVISMGRIAGQTLIDVLAGKPAAPTLITP 303
Cdd:COG1879   270 DPYLQGYLAVDAALKLLKGKEVPKEILTP 298
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
 51-303 2.70e-20

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: 88.39  E-value: 2.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILA--DAHL---GVAQSHPTDV 125
Cdd:cd01536     2 IGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIApvDSEAlvpAVKKANAAGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 126 PTVLVNRRCPGF---LSVSGAD-IVGGGLVASHFADL--GHDHLGVIAGPTWASTSIDRVTGFREtsrarGL-DLPDSAV 198
Cdd:cd01536    82 PVVAVDTDIDGGgdvVAFVGTDnYEAGKLAGEYLAEAlgGKGKVAILEGPPGSSTAIDRTKGFKE-----ALkKYPDIEI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 199 VAS---SFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLmpGADIAVVGYNDINIAREL-----LcpLS 270
Cdd:cd01536   157 VAEqpaNWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGR--TGDIKIVGVDGTPEALKAikdgeL--DA 232

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2769562395 271 SVDNSVISMGRIAGQTLIDVLAGKPAAPTLITP 303
Cdd:cd01536   233 TVAQDPYLQGYLAVEAAVKLLNGEKVPKEILTP 265
PBP1_CcpA_TTHA0807 cd06297
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ...
 50-310 3.34e-20

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: 88.29  E-value: 3.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILADAHLGVAQSH---PTDVP 126
Cdd:cd06297     1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLLSEYRLEKYLRNSTLAYQCDGLVMASLDLTELFEEvivPTEKP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 127 TVLVNRRCPGFLSVSGADIVGGGLVASHFADLGHDHL---GVIAGPTWASTSI-DRVTGFRETSRARGLDLPDSAVVASS 202
Cdd:cd06297    81 VVLIDANSMGYDCVYVDNVKGGFMATEYLAGLGEREYvffGIEEDTVFTETVFrEREQGFLEALNKAGRPISSSRMFRID 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 203 FDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIARELlcPLSSVDNSVISMGRI 282
Cdd:cd06297   161 NSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAASP--GLTTVRQPVEEMGEA 238

                         250       260       270
                  ....*....|....*....|....*....|
gi 2769562395 283 AGQTLIDVLAGKPAAPTLI--TPSLKARQS 310
Cdd:cd06297   239 AAKLLLKRLNEYGGPPRSLkfEPELIVRES 268
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
 50-265 8.70e-20

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


Pssm-ID: 395423 [Multi-domain]  Cd Length: 281  Bit Score: 87.18  E-value: 8.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILADAHLG----VAQSHPTDV 125
Cdd:pfam00532   3 KLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPAPSgddiTAKAEGYGI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 126 PTVLVNRRC---PGFLSVSGADIVGGGLVASHFADLGHDH-LGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVAS 201
Cdd:pfam00532  83 PVIAADDAFdnpDGVPCVMPDDTQAGYESTQYLIAEGHKRpIAVMAGPASALTARERVQGFMAALAAAGREVKIYHVATG 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2769562395 202 SFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDINIAREL 265
Cdd:pfam00532 163 DNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGRVKIPDIVGIGINSVVGFDGL 226
PRK11303 PRK11303
catabolite repressor/activator;
28-227 1.29e-19

catabolite repressor/activator;


Pssm-ID: 236897 [Multi-domain]  Cd Length: 328  Bit Score: 87.63  E-value: 1.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  28 VADRLGYRPDPYAASLRTRRSMSIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDG 107
Cdd:PRK11303   41 VVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSYARIAKYLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDA 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 108 LIladahlgVAQSHPTD-----------VPTVLVNRRC--PGFLSVSGADIVGGGLVASHFADLGHDHLGVI-AGPTwAS 173
Cdd:PRK11303  121 LI-------VSTSLPPEhpfyqrlqndgLPIIALDRALdrEHFTSVVSDDQDDAEMLAESLLKFPAESILLLgALPE-LS 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2769562395 174 TSIDRVTGFRETsrARGLDLPDSAVVASSFDVEGGREAARRLLALEPRPTAIFA 227
Cdd:PRK11303  193 VSFEREQGFRQA--LKDDPREVHYLYANSFEREAGAQLFEKWLETHPMPDALFT 244
PBP1_RafR-like cd20009
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ...
 152-305 3.26e-19

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: 85.28  E-value: 3.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 152 ASHFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSFDVEGGREAARRLLALEPRPTAIFAVNDY 231
Cdd:cd20009   110 VRRLAARGRRRIALVAPPRELTYAQHRLRGFRRALAEAGLEVEPLLIVTLDSSAEAIRAAARRLLRQPPRPDGIICASEI 189

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2769562395 232 AAIGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAGQTLIDVLAGKPAAP--TLITPSL 305
Cdd:cd20009   190 AALGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPIDTLYEDIEEAGRFLAEALLRRIEGEPAEPlqTLERPEL 265
PRK14987 PRK14987
HTH-type transcriptional regulator GntR;
18-301 4.56e-19

HTH-type transcriptional regulator GntR;


Pssm-ID: 184949 [Multi-domain]  Cd Length: 331  Bit Score: 86.23  E-value: 4.56e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  18 SASITRHIIEVADRLGYRPDPYAASLRTRRSMSIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYL 97
Cdd:PRK14987   33 SVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGIESVTDAHGYQTMLAHYGYKPEMEQERL 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  98 GLMSSRRVDGLILAD---AHLGVAQSHPTDVPTV-LVNRRCP------GFLSVSGADIVGGGLVAShfadlGHDHLGVIa 167
Cdd:PRK14987  113 ESMLSWNIDGLILTErthTPRTLKMIEVAGIPVVeLMDSQSPcldiavGFDNFEAARQMTTAIIAR-----GHRHIAYL- 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 168 GPTWASTSIDRVTGFRETSRARGLdLPDSAVVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMP 247
Cdd:PRK14987  187 GARLDERTIIKQKGYEQAMLDAGL-VPYSVMVEQSSSYSSGIELIRQARREYPQLDGVFCTNDDLAVGAAFECQRLGLKV 265

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2769562395 248 GADIAVVGYNDINIARELLCPLSSVDNSVISMGRIAGQTLIDVLAGKPAAPTLI 301
Cdd:PRK14987  266 PDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARIRGESVTPKML 319
PBP1_XylR cd01543
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ...
 87-311 6.23e-18

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: 81.86  E-value: 6.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  87 YDDPERHRKYLGLMSSRRVDGLI--LADAHLGVAQSHpTDVPTVLV--NRRCPGFLSVSGADIVGGGLVASHFADLGHDH 162
Cdd:cd01543    33 YLEPPGYEELLDLLKGWKGDGIIarLDDPELAEALRR-LGIPVVNVsgSRPEPGFPRVTTDNEAIGRMAAEHLLERGFRH 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 163 LGVIAGPTWAStSIDRVTGFRETSRARGLDLP--DSAVVASSFDVEGGREA-ARRLLALePRPTAIFAVNDYAAIGAMGE 239
Cdd:cd01543   112 FAFCGFRNAAW-SRERGEGFREALREAGYECHvyESPPSGSSRSWEEEREElADWLKSL-PKPVGIFACNDDRARQVLEA 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 240 MRDQGL-MPgADIAVVGY-NDiniarELLC-----PLSSVDNSVISMGRIAGQTLIDVLAGKPAAPTLIT---PSLKARQ 309
Cdd:cd01543   190 CREAGIrVP-EEVAVLGVdND-----ELICelsspPLSSIALDAEQIGYEAAELLDRLMRGERVPPEPILippLGVVTRQ 263


                  ..
gi 2769562395 310 SS 311
Cdd:cd01543   264 ST 265
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
 68-303 6.27e-17

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: 79.19  E-value: 6.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  68 EGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILA-------DAHLGVAQShpTDVPTVLVNRrcpGFLSV 140
Cdd:cd06309    19 KSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISpidatgwDPVLKEAKD--AGIPVILVDR---TIDGE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 141 SGADIVGggLVASHFADLGHD--------------HLGVIAGPTWASTSIDRVTGFRETSRARgldlPDSAVVAS---SF 203
Cdd:cd06309    94 DGSLYVT--FIGSDFVEEGRRaaewlvknykggkgNVVELQGTAGSSVAIDRSKGFREVIKKH----PNIKIVASqsgNF 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 204 DVEGGREAARRLLALEPRP-TAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDIN------IARELLCplssvdnSV 276
Cdd:cd06309   168 TREKGQKVMENLLQAGPGDiDVIYAHNDDMALGAIQALKEAGLKPGKDVLVVGIDGQKdaleaiKAGELNA-------TV 240

                         250       260       270
                  ....*....|....*....|....*....|
gi 2769562395 277 IS---MGRIAGQTLIDVLAGKPAAPTLITP 303
Cdd:cd06309   241 ECnplFGPTAFDTIAKLLAGEKVPKLIIVE 270
PBP1_LacI-like cd19974
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 50-288 4.64e-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: 380629 [Multi-domain]  Cd Length: 270  Bit Score: 71.04  E-value: 4.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVL---ATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILA-----DAHLGVAQsh 121
Cdd:cd19974     1 NIAVLIPERFFGDNsfyGKIYQGIEKELSELGYNLVLEIISDEDEEELNLPSIISEEKVDGIIILgeiskEYLEKLKE-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 122 pTDVPTVLVNrrcpgFLSVSG-ADIV------GGGLVASHFADLGHDHLGVIaGPTWASTSI-DRVTGFRETSRARGLDL 193
Cdd:cd19974    79 -LGIPVVLVD-----HYDEELnADSVlsdnyyGAYKLTSYLIEKGHKKIGFV-GDINYTSSFmDRYLGYRKALLEAGLPP 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 194 -PDSAVVASSFDVEGGREAARRLLALEpRPTAIFAVNDYAAIGAMGEMRDQGL-MPGaDIAVVGYNDINIARELLCPLSS 271
Cdd:cd19974   152 eKEEWLLEDRDDGYGLTEEIELPLKLM-LPTAFVCANDSIAIQLIKALKEKGYrVPE-DISVVGFDNIELAELSTPPLTT 229

                         250
                  ....*....|....*..
gi 2769562395 272 VDNSVISMGRIAGQTLI 288
Cdd:cd19974   230 VEVDKEAMGRRAVEQLL 246
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
 50-303 3.58e-13

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


Pssm-ID: 380546 [Multi-domain]  Cd Length: 268  Bit Score: 68.48  E-value: 3.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLIL----ADA-HLGVAQSHPTD 124
Cdd:cd06323     1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLInptdSDAvSPAVEEANEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 125 VPTVLVNRRCPGFLSVS--GADIVGGGLVASHF-ADLGHDHLGV-----IAGptwASTSIDRVTGFRETSRARgldlPDS 196
Cdd:cd06323    81 IPVITVDRSVTGGKVVShiASDNVAGGEMAAEYiAKKLGGKGKVvelqgIPG---TSAARERGKGFHNAIAKY----PKI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 197 AVVAS---SFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGlmpGADIAVVGYNDINIA------RELlc 267
Cdd:cd06323   154 NVVASqtaDFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAG---RKDVIVVGFDGTPDAvkavkdGKL-- 228

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2769562395 268 pLSSVDNSVISMGRIAGQTLIDVLAGKPAAPTLITP 303
Cdd:cd06323   229 -AATVAQQPEEMGAKAVETADKYLKGEKVPKKIPVP 263
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 51-295 1.86e-12

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


Pssm-ID: 380627 [Multi-domain]  Cd Length: 269  Bit Score: 66.31  E-value: 1.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLIL-----ADAHLGVAQSHPTDV 125
Cdd:cd19972     2 IGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYipagaTAAAVPVKAARAAGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 126 PTVLVNRRCPGF---LSVSGADIVGGGLVASHFADL--GHDHLGVIAGPTWASTSIDRVTGFREtsrarGLD-LPDSAVV 199
Cdd:cd19972    82 PVIAVDRNPEDApgdTFIATDSVAAAKELGEWVIKQtgGKGEIAILHGQLGTTPEVDRTKGFQE-----ALAeAPGIKVV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 200 A---SSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLmpGADIAVVGYNDINIArellcpLSSVDNSV 276
Cdd:cd19972   157 AeqtADWDQDEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGL--DHKIWVVGFDGDVAG------LKAVKDGV 228

                         250       260
                  ....*....|....*....|....*...
gi 2769562395 277 IS---------MGRIAGQTLIDVLAGKP 295
Cdd:cd19972   229 LDatmtqqtqkMGRLAVDSAIDLLNGKA 256
Periplasmic_Binding_Protein_type1 cd01391
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
 137-292 5.23e-12

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


Pssm-ID: 380477 [Multi-domain]  Cd Length: 280  Bit Score: 64.98  E-value: 5.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 137 FLSVSGADIVGGGLVASHFADLGHDHLGVIAGPTWASTSIdRVTGFRETSRARGLDLPDSAVvASSFDVEGGREAARRLL 216
Cdd:cd01391   104 FLSVVFSDTLGARLGLDIVKRKNWTYVAAIHGEGLNSGEL-RMAGFKELAKQEGICIVASDK-ADWNAGEKGFDRALRKL 181

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2769562395 217 ALEPRPTAIFAVNDYAAIGAMGEMRDQGLMpgADIAVVGYNDINIARELlcPLSSVDNSVISMG---RIAGQTLIDVLA 292
Cdd:cd01391   182 REGLKARVIVCANDMTARGVLSAMRRLGLV--GDVSVIGSDGWADRDEV--GYEVEANGLTTIKqqkMGFGITAIKAMA 256
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 51-305 1.87e-11

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: 63.45  E-value: 1.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILA--DAhLGVAQS----HPTD 124
Cdd:cd06322     2 IGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILApvDS-GGIVPAieaaNEAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 125 VPTVLVNRRCPGFLSVS--GADIVGGG-LVASHFADLGHDHLGVIAGPTW--ASTSIDRVTGFRETSRARgldlPDSAVV 199
Cdd:cd06322    81 IPVFTVDVKADGAKVVThvGTDNYAGGkLAGEYALKALLGGGGKIAIIDYpeVESVVLRVNGFKEAIKKY----PNIEIV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 200 AS---SFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLmpGADIAVVGYNDINIARELLCPLSSVDNSV 276
Cdd:cd06322   157 AEqpgDGRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGK--EDKIKVIGFDGNPEAIKAIAKGGKIKADI 234

                         250       260       270
                  ....*....|....*....|....*....|....
gi 2769562395 277 IS----MGRIAGQTLIDVLAGKPAAP-TLITPSL 305
Cdd:cd06322   235 AQqpdkIGQETVEAIVKYLAGETVEKeILIPPKL 268
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
 51-302 2.56e-11

periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The periplasmic binding protein (PBP) IbpA mediates the uptake of myo-inositol by an ABC transporter that consists of the PBP IbpA, the transmembrane permease IatP, and the ABC IatA. IbpA shares 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: 380623 [Multi-domain]  Cd Length: 271  Bit Score: 62.79  E-value: 2.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILA----DAHLGVAQSH-PTDV 125
Cdd:cd19968     2 IGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSpidvKALVPAIEAAiKAGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 126 PTVLVNRRCPG--FLSVSGADIVGGG-LVASHFADL--GHDHLGVIAGPTWASTSIDRVTGFRETSRARgldlPDSAVVA 200
Cdd:cd19968    82 PVVTVDRRAEGaaPVPHVGADNVAGGrEVAKFVVDKlpNGAKVIELTGTPGSSPAIDRTKGFHEELAAG----PKIKVVF 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 201 S---SFDVEGGREAARRLL-ALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGaDIAVVGYNDINIAR------ELLCpls 270
Cdd:cd19968   158 EqtgNFERDEGLTVMENILtSLPGPPDAIICANDDMALGAIEAMRAAGLDLK-KVKVIGFDAVPDALqaikdgELYA--- 233

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2769562395 271 SVDNSVISMGRIAGQTLIDVLAGKPA------APTLIT 302
Cdd:cd19968   234 TVEQPPGGQARTALRILVDYLKDKKApkkvnlKPKLIT 271
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
 51-303 4.63e-11

periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis; Periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis. The members of this group are belonging to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Like other periplasmic receptors of the ABC-type transport systems, the allose-binding protein consists of two alpha/beta domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding.


Pssm-ID: 380543 [Multi-domain]  Cd Length: 283  Bit Score: 62.28  E-value: 4.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSG--YQVAVANTYDDPERHRKYLGLMSSRRVDGLILA---DAHL--GVAQSHPT 123
Cdd:cd06320     2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGvkVDVQAAPSETDTQGQLNLLETMLNKGYDAILVSpisDTNLipPIEKANKK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 124 DVPTVLVNR-RCPGFLSVSGADIVG---------GGLVASHFADLGHD--HLGVIAGPTWASTSIDRVTGFRET-SRARG 190
Cdd:cd06320    82 GIPVINLDDaVDADALKKAGGKVTSfigtdnvaaGALAAEYIAEKLPGggKVAIIEGLPGNAAAEARTKGFKETfKKAPG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 191 LDLpdSAVVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLmpGADIAVVGYNDINIARELLCP-- 268
Cdd:cd06320   162 LKL--VASQPADWDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAGK--TGKVLVVGTDGIPEAKKSIKAge 237

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2769562395 269 LS-SVDNSVISMGRIAGQTLIDVLAGKPAAPTLITP 303
Cdd:cd06320   238 LTaTVAQYPYLEGAMAVEAALRLLQGQKVPAVVATP 273
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 50-301 5.83e-11

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: 380544 [Multi-domain]  Cd Length: 270  Bit Score: 61.92  E-value: 5.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQV---AVANTYDdPERHRKYLGLMSSRRVDGLIL-----ADAHLGVAQSH 121
Cdd:cd06321     1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINPGAkvtVVDARYD-LAKQFSQIDDFIAQGVDLILLnaadsAGIEPAIKRAK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 122 PTDVPTVLVNRRCPGFLSVSGADIVGGG-LVASHFADL--GHDHLGVIAGPTwASTSIDRVTGFRET-SRARGLDLPDSA 197
Cdd:cd06321    80 DAGIIVVAVDVAAEGADATVTTDNVQAGyLACEYLVEQlgGKGKVAIIDGPP-VSAVIDRVNGCKEAlAEYPGIKLVDDQ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 198 vvASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYNDinIARELLCPLSSVDNSVI 277
Cdd:cd06321   159 --NGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRDDIVITSVDGSPE--AVAALKREGSPFIATAA 234

                         250       260
                  ....*....|....*....|....*...
gi 2769562395 278 ----SMGRIAGQTLIDVLAGKPAAPTLI 301
Cdd:cd06321   235 qdpyDMARKAVELALKILNGQEPAPELV 262
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 51-293 9.32e-11

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: 61.22  E-value: 9.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLIL-------ADAHLGVAQShpT 123
Cdd:cd06319     2 IGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIIsptnssaAPTVLDLANE--A 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 124 DVPTVLVNRRCPG--FLSVSGADIVGGG-LVASHFADL------GHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLP 194
Cdd:cd06319    80 KIPVVIADIGTGGgdYVSYIISDNYDGGyQAGEYLAEAlkengwGGGSVGIIAIPQSRVNGQARTAGFEDALEEAGVEEV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 195 DSAVVASsFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLmpGADIAVVGYNDINIARELLCP---LSS 271
Cdd:cd06319   160 ALRQTPN-STVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGR--TGDILVVGFDGDPEALDLIKDgklDGT 236

                         250       260
                  ....*....|....*....|..
gi 2769562395 272 VDNSVISMGRIAGQTLIDVLAG 293
Cdd:cd06319   237 VAQQPFGMGARAVELAIQALNG 258
PRK10014 PRK10014
DNA-binding transcriptional repressor MalI; Provisional
 31-308 1.15e-10

DNA-binding transcriptional repressor MalI; Provisional


Pssm-ID: 182193 [Multi-domain]  Cd Length: 342  Bit Score: 61.65  E-value: 1.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  31 RLGYRPDPYAASLRTRRSMSIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLIL 110
Cdd:PRK10014   47 ELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAELTAGLTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVI 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 111 ADA-----HLgVAQSHPTDVPTVLVNRRCpgflSVSGADIVG------GGLVASHFADLGHDHLGVIAGPTWASTSIDRV 179
Cdd:PRK10014  127 AGAagssdDL-REMAEEKGIPVVFASRAS----YLDDVDTVRpdnmqaAQLLTEHLIRNGHQRIAWLGGQSSSLTRAERV 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 180 TGFRETSRARGLDLPDSAVVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGA-MGEMRD--QGLMPGAD------ 250
Cdd:PRK10014  202 GGYCATLLKFGLPFHSEWVLECTSSQKQAAEAITALLRHNPTISAVVCYNETIAMGAwFGLLRAgrQSGESGVDryfeqq 281

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 251 IAVVGYNDINIARELLCPLSSVDNSVISMGRIAGQTLIDVLAGKPAAP--TLITPSLKAR 308
Cdd:PRK10014  282 VALAAFTDVPEAELDDPPLTWASTPAREIGRTLADRMMQRITHEETHSrnLIIPPRLIAR 341
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 137-303 1.00e-09

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


Pssm-ID: 380625 [Multi-domain]  Cd Length: 275  Bit Score: 58.42  E-value: 1.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 137 FLSVSGADivGGGLVASHFADL--GHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLpdSAVVASSFDVEGGREAARR 214
Cdd:cd19970   107 FVGPDNRQ--GAYLAGDYLAKKlgKGGKVAIIEGIPGADNAQQRKAGFLKAFEEAGMKI--VASQSANWEIDEANTVAAN 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 215 LLALEPRPTAIFAVNDYAAIGAMGEMRDQGLmpGADIAVVGYNDINIARELLCP---LSSVDNSVISMGRIAGQTLIDVL 291
Cdd:cd19970   183 LLTAHPDIRGILCANDNMALGAIKAVDAAGK--AGKVLVVGFDNIPAVRPLLKDgkmLATIDQHPAKQAVYGIEYALKML 260

                         170
                  ....*....|..
gi 2769562395 292 AGKPAAPTLITP 303
Cdd:cd19970   261 NGEEVPGWVKTP 272
PRK10339 PRK10339
DNA-binding transcriptional repressor EbgR; Provisional
 13-272 4.14e-09

DNA-binding transcriptional repressor EbgR; Provisional


Pssm-ID: 182389 [Multi-domain]  Cd Length: 327  Bit Score: 56.69  E-value: 4.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  13 LSDAPSASI---TRH-IIEVADRLGYRPDPyAASLRTRRSMSIGVLV-------PRLSDVVLATIYEGIEQSAALSGyqV 81
Cdd:PRK10339   22 LNDDPTLNVkeeTKHrILEIAEKLEYKTSS-ARKLQTGAVNQHHILAiysyqqeLEINDPYYLAIRHGIETQCEKLG--I 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  82 AVANTYDdperhrkYLGLMSSRRVDGLILA--DAHLGVAQSHPTDVPTVLVNRRCPGflsvSGADIVGGGL------VAS 153
Cdd:PRK10339   99 ELTNCYE-------HSGLPDIKNVTGILIVgkPTPALRAAASALTDNICFIDFHEPG----SGYDAVDIDLariskeIID 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 154 HFADLGHDHLGVIAGPTWASTSIDRVTGFRETSRARGLdLPDSAVVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAA 233
Cdd:PRK10339  168 FYINQGVNRIGFIGGEDEPGKADIREVAFAEYGRLKQV-VREEDIWRGGFSSSSGYELAKQMLAREDYPKALFVASDSIA 246

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2769562395 234 IGAMGEMRDQGLMPGADIAVVGYNDINIARELLCPLSSV 272
Cdd:PRK10339  247 IGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTV 285
PBP1_LacI-like cd06287
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 105-310 5.58e-09

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: 55.89  E-value: 5.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 105 VDGLILADAHLG---VAQSHPTDVPTVLVNRRCPGFLSVSGADIVGGG---LVASHFADLGHDHLGVIAGPTWASTSIDR 178
Cdd:cd06287    57 VDGAIVVEPTVEdpiLARLRQRGVPVVSIGRAPGTDEPVPYVDLQSAAtarLLLEHLHGAGARQVALLTGSSRRNSSLES 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 179 VTGFRETSRARGLDlPDSAVVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPGADIAVVGYND 258
Cdd:cd06287   137 EAAYLRFAQEYGTT-PVVYKVPESEGERAGYEAAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPEDLMVVTRYD 215

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2769562395 259 INIARELLCPLSSVDNSVISMGRIAGQTLIDVLAGK-PAAPTLITPSLKARQS 310
Cdd:cd06287   216 GIRARTADPPLTAVDLHLDRVARTAIDLLFASLSGEeRSVEVGPAPELVVRAS 268
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 51-295 5.68e-09

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


Pssm-ID: 433182 [Multi-domain]  Cd Length: 259  Bit Score: 55.78  E-value: 5.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQV-AVANTYDDPERHRKYLGLMSSRRVDGLILADAHLGVAQS-----HPTD 124
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEViVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPvlkkaKDAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 125 VPTVLVNRRCPGF--LSVSGAD-IVGGGLVASHFADL--GHDHLGVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVV 199
Cdd:pfam13407  81 IPVVTFDSDAPSSprLAYVGFDnEAAGEAAGELLAEAlgGKGKVAILSGSPGDPNANERIDGFKKVLKEKYPGIKVVAEV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 200 ASSF-DVEGGREAARRLLALEPRPT-AIFAVNDYAAIGAMGEMRDQGLmpGADIAVVGYNDINIARELL-----CplSSV 272
Cdd:pfam13407 161 EGTNwDPEKAQQQMEALLTAYPNPLdGIISPNDGMAGGAAQALEAAGL--AGKVVVTGFDATPEALEAIkdgtiD--ATV 236

                         250       260
                  ....*....|....*....|...
gi 2769562395 273 DNSVISMGRIAGQTLIDVLAGKP 295
Cdd:pfam13407 237 LQDPYGQGYAAVELAAALLKGKK 259
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
 50-303 1.53e-08

TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria; TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria. The Tor respiratory system is consists of three proteins (TorC, TorA, and TorD) and is induced in the presence of TMAO. The TMAO control is tightly regulated by three proteins: TorS, TorT, and TorR. Thus, the disruption of any of these proteins can abolish the Tor respiratory induction. TorT shares homology with the sugar-binding domain of the type 1 periplasmic binding proteins. The members of TorT-like family bind TMAO or related compounds and are predicted to be involved in signal transduction and/or substrate transport.


Pssm-ID: 380529 [Multi-domain]  Cd Length: 269  Bit Score: 54.51  E-value: 1.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVV-LATIYeGIEQSAALSG--YQVAVANTYDDPERHRKYLGLMSSRRVDGLILA----DAHLG-VAQSH 121
Cdd:cd06306     1 KICVLFPHLKDSYwVGVNY-GIVDEAKRLGvkLTVYEAGGYTNLSKQISQLEDCVASGADAILLGaisfDGLDPkVAEAA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 122 PTDVPTV-LVNR-RCPGFLSVSGADIVG-GGLVASHFADLGHD---HLGVIAGPTWASTSIDRVTGFRETsrargLDLPD 195
Cdd:cd06306    80 AAGIPVIdLVNGiDSPKVAARVLVDFYDmGYLAGEYLVEHHPGkpvKVAWFPGPAGAGWAEDREKGFKEA-----LAGSN 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 196 SAVVASSF---DVEGGREAARRLLALEPRPTAIFAvNDYAAIGAMGEMRDQGLMPgaDIAVVGYNDIN-----IARELLc 267
Cdd:cd06306   155 VEIVATKYgdtGKAVQLNLVEDALQAHPDIDYIVG-NAVAAEAAVGALREAGLTG--KVKVVSTYLTPgvyrgIKRGKI- 230

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2769562395 268 pLSSVDNSVISMGRIAGQTLIDVLAGKPAAPTLITP 303
Cdd:cd06306   231 -LAAPSDQPVLQGRIAVDQAVRALEGKPVPKHVGPP 265
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 148-304 2.20e-08

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


Pssm-ID: 380661 [Multi-domain]  Cd Length: 274  Bit Score: 54.14  E-value: 2.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 148 GGLVASHFADLGHdhLGVIAGPTWASTSIDRVTGFRETsrarGLDLPDSAVVASSF---DVEGGREAARRLLALEPRPTA 224
Cdd:cd20006   115 GEKLASLLGEKGK--VAIVSFVKGSSTAIEREEGFKQA----LAEYPNIKIVETEYcdsDEEKAYEITKELLSKYPDING 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 225 IFAVNDYAAIGAMGEMRDQGLmpGADIAVVGYNDINIARELLcplssvDNSVI---------SMGRIAGQTLIDVLAGKP 295
Cdd:cd20006   189 IVALNEQSTLGAARALKELGL--GGKVKVVGFDSSVEEIQLL------EEGIIdalvvqnpfNMGYLSVQAAVDLLNGKK 260


                  ....*....
gi 2769562395 296 AAPTLITPS 304
Cdd:cd20006   261 IPKRIDTGS 269
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 50-295 2.32e-08

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


Pssm-ID: 380659 [Multi-domain]  Cd Length: 273  Bit Score: 54.16  E-value: 2.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAV--ANTYDDPERHRKYLGLMSSRRVDGLILADAHLG-----VAQSHP 122
Cdd:cd20004     1 CIAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWrgPSREDDVEAQIQIIEYFIDQGVDGIVLAPLDRKalvapVERARA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 123 TDVPTVLVNRRCPG--FLSVSGADIVGGG-LVASHFADLGHDH-----LGVIAGPtwASTSiDRVTGFRETSRARGLDLp 194
Cdd:cd20004    81 QGIPVVIIDSDLGGdaVISFVATDNYAAGrLAAKRMAKLLNGKgkvalLRLAKGS--ASTT-DRERGFLEALKKLAPGL- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 195 dsAVVASSF---DVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLmpGADIAVVGYNdiniARELLcpLSS 271
Cdd:cd20004   157 --KVVDDQYaggTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGL--AGKVKFIGFD----ASDLL--LDA 226

                         250       260       270
                  ....*....|....*....|....*....|...
gi 2769562395 272 VDNSVIS---------MGRIAGQTLIDVLAGKP 295
Cdd:cd20004   227 LRAGEISalvvqdpyrMGYLGVKTAVAALRGKP 259
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
 64-304 4.81e-08

periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic binding domain of two-component sensor kinase signaling systems, some of which are fused with a C-terminal histidine kinase A domain (HisK) and/or a signal receiver domain (REC). Members of this group share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily and are predicted to be involved in sensing of environmental stimuli; their substrate specificities, however, are not known in detail.


Pssm-ID: 380531 [Multi-domain]  Cd Length: 268  Bit Score: 53.32  E-value: 4.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  64 ATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLIL----ADAHLGVAQS-HPTDVPTVLVNRRCPG-- 136
Cdd:cd06308    16 AMNEEIKAEAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVspneADALTPVVKKaYDAGIPVIVLDRKVSGdd 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 137 FLSVSGADIVGGGLVASHF-ADLGHDHLGV--IAGPTWASTSIDRVTGFRETSRarglDLPDSAVVAS---SFDVEGGRE 210
Cdd:cd06308    96 YTAFIGADNVEIGRQAGEYiAELLNGKGNVveIQGLPGSSPAIDRHKGFLEAIA----KYPGIKIVASqdgDWLRDKAIK 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 211 AARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMPgaDIAVVGYNDINIARELLCPLSSVDNSVI--SMGRIAGQTLI 288
Cdd:cd06308   172 VMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGREK--EIKIIGVDGLPEAGEKAVKDGILAATFLypTGGKEAIEAAL 249

                         250
                  ....*....|....*.
gi 2769562395 289 DVLAGKPAAPTLITPS 304
Cdd:cd06308   250 KILNGEKVPKEIVLPT 265
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
 51-264 2.68e-07

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


Pssm-ID: 380622 [Multi-domain]  Cd Length: 272  Bit Score: 51.17  E-value: 2.68e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILADAHL-----GVAQSHPTDV 125
Cdd:cd19967     2 VAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADAdasiaAVKKAKDAGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 126 PTVLVNRRCPGfLSVSGADIV-----GGGLVASHFADL-GHDHLGV-IAGPTWASTSIDRVTGFRETsrargLD-LPDSA 197
Cdd:cd19967    82 PVFLIDREINA-EGVAVAQIVsdnyqGAVLLAQYFVKLmGEKGLYVeLLGKESDTNAQLRSQGFHSV-----IDqYPELK 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 198 VVAS---SFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLmpGADIAVVGYNDINIARE 264
Cdd:cd19967   156 MVAQqsaDWDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGR--AGDVIIVGFDGSNDVRD 223
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 65-303 3.40e-07

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


Pssm-ID: 380662 [Multi-domain]  Cd Length: 271  Bit Score: 50.70  E-value: 3.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  65 TIYEGIEQSAALSGYQ--VAVANTYDdPERHRKYLGLMSSRRVDGLILA----DAHLG-VAQSHPTDVPTVLVNRRC--P 135
Cdd:cd20007    16 TMQCGAEAAAKELGVEldVQGPPTFD-PTLQTPIVNAVIAKKPDALLIAptdpQALIApLKRAADAGIKVVTVDTTLgdP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 136 GFL--SVSGADIVGGGLVASHFADL--GHDHLGVIAGPTWASTSIDRVTGFRETSRARGlDLPDSAVVASSFDVEGGREA 211
Cdd:cd20007    95 SFVlsQIASDNVAGGALAAEALAELigGKGKVLVINSTPGVSTTDARVKGFAEEMKKYP-GIKVLGVQYSENDPAKAASI 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 212 ARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMpgADIAVVGYNdiniarellCPLSSV----DNSV--------ISM 279
Cdd:cd20007   174 VAAALQANPDLAGIFGTNTFSAEGAAAALRNAGKT--GKVKVVGFD---------ASPAQVeqlkAGTIdaliaqkpAEI 242

                         250       260
                  ....*....|....*....|....
gi 2769562395 280 GRIAGQTLIDVLAGKPAAPTLITP 303
Cdd:cd20007   243 GYLAVEQAVAALTGKPVPKDILTP 266
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 101-257 7.75e-07

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 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: 380547 [Multi-domain]  Cd Length: 317  Bit Score: 49.91  E-value: 7.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 101 SSRRVDGLILADAHLGVAQ----SHPTDVPTVLVNR---------------RCPGFL-SVSGADIVGGGLVASHFADLGH 160
Cdd:cd06324    55 RPPKPDYLILVNEKGVAPEllelAEQAKIPVFLINNdltdeerallgkpreKFKYWLgSIVPDNEQAGYLLAKALIKAAR 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 161 D-------HLGVIAGPTWASTSIDRVTG----FRETSRARGLDlpdsaVVASSFDVEGGREAARRLLALEPRPTAIFAVN 229
Cdd:cd06324   135 KksddgkiRVLAISGDKSTPASILREQGlrdaLAEHPDVTLLQ-----IVYANWSEDEAYQKTEKLLQRYPDIDIVWAAN 209

                         170       180
                  ....*....|....*....|....*...
gi 2769562395 230 DYAAIGAMGEMRDQGLMPGADIAVVGYN 257
Cdd:cd06324   210 DAMALGAIDALEEAGLKPGKDVLVGGID 237
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 50-303 8.30e-07

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


Pssm-ID: 380540 [Multi-domain]  Cd Length: 281  Bit Score: 49.68  E-value: 8.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILADahLGVAQSHPT------ 123
Cdd:cd06317     1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDA--IDVNGSIPAikrase 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 124 -DVPTVLVNRRCP-GFLS--VSGADIVGGGLVASHFAD------LGHDHLGVIaGPTWASTSIDRVTGFRETSRAR-GLD 192
Cdd:cd06317    79 aGIPVIAYDAVIPsDFQAaqVGVDNLEGGKEIGKYAADyikaelGGQAKIGVV-GALSSLIQNQRQKGFEEALKANpGVE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 193 LpdSAVVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLmpGADIAVVGYNDINIARELLCP---- 268
Cdd:cd06317   158 I--VATVDGQNVQEKALSAAENLLTANPDLDAIYATGEPALLGAVAAVRSQGR--QGKIKVFGWDLTKQAIFLGIDegvl 233

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2769562395 269 LSSVDNSVISMGRIAGQTLIDVLAGKPAAPTLITP 303
Cdd:cd06317   234 QAVVQQDPEKMGYEAVKAAVKAIKGEDVEKTIDVP 268
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 172-304 1.93e-06

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


Pssm-ID: 380626 [Multi-domain]  Cd Length: 267  Bit Score: 48.35  E-value: 1.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 172 ASTSIDRVTGFRETSRarglDLPDSAVVASsFDVEGGREAA----RRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMp 247
Cdd:cd19971   133 AESCVDRIDGFLDAIK----KNPKFEVVAQ-QDGKGQLEVAmpimEDILQAHPDLDAVFALNDPSALGALAALKAAGKL- 206

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 248 gADIAVVGYNDINIARELLCP---LSSVDNSVISMGRIAGQTLIDVLAGKPAAPTLITPS 304
Cdd:cd19971   207 -GDILVYGVDGSPDAKAAIKDgkmTATAAQSPIEIGKKAVETAYKILNGEKVEKEIVVPT 265
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 50-295 2.79e-06

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


Pssm-ID: 380533 [Multi-domain]  Cd Length: 272  Bit Score: 47.72  E-value: 2.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAV--ANTYDDPERHRKYLGLMSSRRVDGLILA---DAHL--GVAQSHP 122
Cdd:cd06310     1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFvgPESEEDVAGQNSLLEELINKKPDAIVVApldSEDLvdPLKDAKD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 123 TDVPTVLVNRRCPG--FLSVSGADIVGGGLVASH--FADLGHD-HLGVIAGPTWASTSIDRVTGFRE--TSRARGLDLPD 195
Cdd:cd06310    81 KGIPVIVIDSGIKGdaYLSYIATDNYAAGRLAAQklAEALGGKgKVAVLSLTAGNSTTDQREEGFKEylKKHPGGIKVLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 196 SAVvaSSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLmpGADIAVVGYnDINiaRELLCPLSS--VD 273
Cdd:cd06310   161 SQY--AGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKL--SGQIKIVGF-DSQ--EELLDALKNgkID 233

                         250       260
                  ....*....|....*....|....*.
gi 2769562395 274 NSVIS----MGRIAGQTLIDVLAGKP 295
Cdd:cd06310   234 ALVVQnpyeIGYEGIKLALKLLKGEE 259
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
 51-305 4.28e-06

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


Pssm-ID: 380541 [Multi-domain]  Cd Length: 282  Bit Score: 47.41  E-value: 4.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLIL--ADAHlGVAQS----HPTD 124
Cdd:cd06318     2 IGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILnpVDPE-GLTPAvkaaKAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 125 VPTVLVNR---RCPGFLSVSGADIVGGGLVASHFA--DLGHD--HLGVIAGPTWASTSIDRVTGFRE---TSRARGLDLP 194
Cdd:cd06318    81 IPVITVDSaldPSANVATQVGRDNKQNGVLVGKEAakALGGDpgKIIELSGDKGNEVSRDRRDGFLAgvnEYQLRKYGKS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 195 DSAVVASSF---DVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLMpgADIAVVGYNDINIARELLCP--- 268
Cdd:cd06318   161 NIKVVAQPYgnwIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGML--DKVKVAGADGQKEALKLIKDgky 238

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 2769562395 269 LSSVDNSVISMGRIAGQTLIDVLAGKPAAP--TLITPSL 305
Cdd:cd06318   239 VATGLNDPDLLGKTAVDTAAKVVKGEESFPefTYTPTAL 277
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
22-60 4.83e-06

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 43.73  E-value: 4.83e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2769562395   22 TRH-IIEVADRLGYRPDPYAASLRTRRSMSIGVLVPRLSD 60
Cdd:smart00354  31 TREkVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
 51-255 2.82e-05

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: 44.95  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  51 IGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLILA--DAHLG---VAQSHPTDV 125
Cdd:cd06313     2 IGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVpvDADALapaVEKAKEAGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 126 PTVLVNRRCPGFLS---VSGADIVGGGLVASHFADL--GHDHLGVIAGPTWASTSIDRVTGFRETsrarGLDLPDSAVVA 200
Cdd:cd06313    82 PLVGVNALIENEDLtayVGSDDVVAGELEGQAVADRlgGKGNVVILEGPIGQSAQIDRGKGIENV----LKKYPDIKVLA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 201 SSfDVEGGREAARRLLA--LEPRPT---AIFAVNDYAAIGAMGEMRDQGLmpgADIAVVG 255
Cdd:cd06313   158 EQ-TANWSRDEAMSLMEnwLQAYGDeidGIIAQNDDMALGALQAVKAAGR---DDIPVVG 213
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 148-256 4.75e-05

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


Pssm-ID: 380660 [Multi-domain]  Cd Length: 274  Bit Score: 44.16  E-value: 4.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 148 GGLVASHFADLGHD--HLGVIAGPTWASTSIDRVTGFRETSRArglDLPDSAVVASSFDVEGGREA---ARRLLALEPRP 222
Cdd:cd20005   109 GALAADHLAELIGGkgKVAIVAHDATSETGIDRRDGFKDEIKE---KYPDIKVVNVQYGVGDHAKAadiAKAILQANPDL 185

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2769562395 223 TAIFAVNDYAAIGAMGEMRDQGLmpGADIAVVGY 256
Cdd:cd20005   186 KGIYATNEGAAIGVANALKEMGK--LGKIKVVGF 217
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
50-257 1.08e-04

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 43.15  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  50 SIGVLVPRLSDVVLATIYEGIEQSAALSGYQVAVANTYDDPERHRKYLGLMSSRRVDGLIL----ADAhLG--VAQSHPT 123
Cdd:PRK10653   28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLInptdSDA-VGnaVKMANQA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 124 DVPTVLVNRRCPGFLSVS--GADIVGGGLVASHF--ADLGHD----HLGVIAGptwASTSIDRVTGFRETSRARGLDLPD 195
Cdd:PRK10653  107 NIPVITLDRGATKGEVVShiASDNVAGGKMAGDFiaKKLGEGakviQLEGIAG---TSAARERGEGFKQAVAAHKFNVLA 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2769562395 196 SAvvASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGlmpGADIAVVGYN 257
Cdd:PRK10653  184 SQ--PADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KSDVMVVGFD 240
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 125-254 3.42e-04

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: 380534 [Multi-domain]  Cd Length: 270  Bit Score: 41.58  E-value: 3.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 125 VPTVLVNRRCPGFLSVS--GADIVGGGLVASHFadLGhDHLG------VIAGPTWASTSIDRVTGFRETSRARgldlPDS 196
Cdd:cd06311    81 IPVVNFDRGLNVLIYDLyvAGDNPGMGVVSAEY--IG-KKLGgkgnvvVLEVPSSGSVNEERVAGFKEVIKGN----PGI 153

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2769562395 197 AVV---ASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQGLmpgADIAVV 254
Cdd:cd06311   154 KILamqAGDWTREDGLKVAQDILTKNKKIDAVWAADDDMAIGVLQAIKEAGR---TDIKVM 211
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 164-301 3.89e-04

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


Pssm-ID: 380663 [Multi-domain]  Cd Length: 277  Bit Score: 41.45  E-value: 3.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 164 GVIAGPTWASTSIDRVTGFRETSRARGLDLPDSAVVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMRDQ 243
Cdd:cd20008   130 AIISFQAGSQTLVDREEGFRDYIKEKYPDIEIVDVQYSDGDIAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEA 209

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2769562395 244 GLmpGADIAVVGY--NDINIArellcplsSVDNSVIS---------MGRIAGQTLIDVLAGKPAAPTLI 301
Cdd:cd20008   210 GK--AGKIVLVGFdsSPDEVA--------LLKSGVIKalvvqdpyqMGYEGVKTAVKALKGEEIVEKNV 268
COG2984 COG2984
ABC-type uncharacterized transport system, periplasmic component [General function prediction ...
 63-297 7.56e-04

ABC-type uncharacterized transport system, periplasmic component [General function prediction only];


Pssm-ID: 442223  Cd Length: 284  Bit Score: 40.66  E-value: 7.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395  63 LATIYEGIEQSAALSGY----QVAVANTYDDPERHRKYLGLMSSRRVDgLILA---DAHLGVAQSHPtDVPTVlvnrrcp 135
Cdd:COG2984    16 LDAAREGFKDGLAEAGYgknlKLDYQNAQGDQATAAQIAAKLVADKPD-LIVAigtPAAQAAANATK-DIPVV------- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 136 gFLSVSgaDIVGGGLVASHFADLGH------------------------DHLGVIAGPTwASTSIDRVTGFRETSRARGL 191
Cdd:COG2984    87 -FTAVT--DPVGAGLVKSLEKPGGNvtgvsdllpiekqlelikkllpdaKRIGVLYNPS-EANSVAQVEELKKAAKKLGL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 192 DLpDSAVVASSFDVEggreaaRRLLALEPRPTAIFAVND---YAAIGAMGEMRDQglmpgADIAVVGYNDINIARELLCp 268
Cdd:COG2984   163 EL-VEATVTSSNEIQ------QALQSLAGKVDAIYVPTDntvVSALEAIAKVAAR-----AKIPVFGGDDSSVKAGALA- 229

                         250       260
                  ....*....|....*....|....*....
gi 2769562395 269 lsSVDNSVISMGRIAGQTLIDVLAGKPAA 297
Cdd:COG2984   230 --GYGIDYYELGRQAAEMALRILKGEKPA 256
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
 163-303 8.95e-04

periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs; Periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs from other bacteria. They are members of the type 1 periplasmic binding protein superfamily which consists of two domains connected by a three-stranded hinge. TmGBP is specific for glucose and its binding pocket is buried at the interface of the two domains. TmGBP also exhibits high thermostability and the highest structural similarity to E. coli glucose binding protein (ecGBP).


Pssm-ID: 380537 [Multi-domain]  Cd Length: 271  Bit Score: 40.26  E-value: 8.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2769562395 163 LGVIAGPTWASTSIDRVTGFRET-SRARGLDLPDsaVVASSFDVEGGREAARRLLALEPRPTAIFAVNDYAAIGAMGEMR 241
Cdd:cd06314   125 VAIITGGLGADNLNERIQGFKDAlKGSPGIEIVD--PLSDNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALK 202

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2769562395 242 DQGlmPGADIAVVGYNDINIARELLcplssvDNSVIS---------MGRIAGQTLIDVL-AGKPAAPTLITP 303
Cdd:cd06314   203 DAG--KVGKVKIVGFDTLPETLQGI------KDGVIAatvgqrpyeMGYLSVKLLYKLLkGGKPVPDVIDTG 266
 
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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