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Conserved domains on  [gi|488138380|ref|WP_002209588|]
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MULTISPECIES: D-xylose utilization transcriptional activator XylR [Yersinia pseudotuberculosis complex]

Protein Classification

XylR family transcriptional regulator( domain architecture ID 11546740)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP1_XylR cd01543
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ...
 7-282 1.07e-93

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: 281.78  E-value: 1.07e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380   7 RITLLFNANKVYDRQVVEGVGEYLQASQcNWDIFIEEDFRC-RIDNIKDWLGDGVIADFDDRQIEQLLANVNVPIVGVGG 85
Cdd:cd01543    1 RVALLLETSRGYGRRLLRGIARYAREHG-PWSLYLEPPGYEeLLDLLKGWKGDGIIARLDDPELAEALRRLGIPVVNVSG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  86 SYHQsedyPSVDYIATDNKALVNAAFMHLKEKGLNRFAFYGLPascGMRWAQEREYAFRQLVSAEQYQGVVYQGMATA-P 164
Cdd:cd01543   80 SRPE----PGFPRVTTDNEAIGRMAAEHLLERGFRHFAFCGFR---NAAWSRERGEGFREALREAGYECHVYESPPSGsS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 165 DNWQYAQNRLADWVQTLPHQTGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLSRVALSSVVQGTRQMGY 244
Cdd:cd01543  153 RSWEEEREELADWLKSLPKPVGIFACNDDRARQVLEACREAGIRVPEEVAVLGVDNDELICELSSPPLSSIALDAEQIGY 232

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 488138380 245 RAAKLLHQRLKlrqkqQTDPPLQRILVPPVKVMARRST 282
Cdd:cd01543  233 EAAELLDRLMR-----GERVPPEPILIPPLGVVTRQST 265
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
306-389 2.01e-26

helix_turn_helix, arabinose operon control protein;


:

Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 101.09  E-value: 2.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380   306 GIKVEQVLDAVGMSRSNLEKRFKDEVGQTIHGVIHEEKLDRARNLLAATSLPINEISQMCGYPSLQYFYSVFKKGYSITP 385
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 488138380   386 KEHR 389
Cdd:smart00342  81 SEYR 84
 
Name Accession Description Interval E-value
PBP1_XylR cd01543
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ...
 7-282 1.07e-93

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: 281.78  E-value: 1.07e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380   7 RITLLFNANKVYDRQVVEGVGEYLQASQcNWDIFIEEDFRC-RIDNIKDWLGDGVIADFDDRQIEQLLANVNVPIVGVGG 85
Cdd:cd01543    1 RVALLLETSRGYGRRLLRGIARYAREHG-PWSLYLEPPGYEeLLDLLKGWKGDGIIARLDDPELAEALRRLGIPVVNVSG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  86 SYHQsedyPSVDYIATDNKALVNAAFMHLKEKGLNRFAFYGLPascGMRWAQEREYAFRQLVSAEQYQGVVYQGMATA-P 164
Cdd:cd01543   80 SRPE----PGFPRVTTDNEAIGRMAAEHLLERGFRHFAFCGFR---NAAWSRERGEGFREALREAGYECHVYESPPSGsS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 165 DNWQYAQNRLADWVQTLPHQTGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLSRVALSSVVQGTRQMGY 244
Cdd:cd01543  153 RSWEEEREELADWLKSLPKPVGIFACNDDRARQVLEACREAGIRVPEEVAVLGVDNDELICELSSPPLSSIALDAEQIGY 232

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 488138380 245 RAAKLLHQRLKlrqkqQTDPPLQRILVPPVKVMARRST 282
Cdd:cd01543  233 EAAELLDRLMR-----GERVPPEPILIPPLGVVTRQST 265
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
 113-282 4.89e-34

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: 123.99  E-value: 4.89e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  113 HLKEKGLNRFAFYGLPASCGMRWAQEREYAFRQLVSAEQYQGVVYQGMATAPDNWQYAQNRLaDWVQTLPhqTGIIAVTD 192
Cdd:pfam13377   1 HLAELGHRRIALIGPEGDRDDPYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARERL-RWLGALP--TAVFVAND 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  193 ARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLSRvALSSVVQGTRQMGYRAAKLLHQRLklrqkQQTDPPLQRILVP 272
Cdd:pfam13377  78 EVALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSP-PLTTVRVDAEELGRAAAELLLDLL-----NGEPAPPERVLLP 151

                         170
                  ....*....|
gi 488138380  273 PvKVMARRST 282
Cdd:pfam13377 152 P-ELVEREST 160
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
306-389 2.01e-26

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 101.09  E-value: 2.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380   306 GIKVEQVLDAVGMSRSNLEKRFKDEVGQTIHGVIHEEKLDRARNLLAATSLPINEISQMCGYPSLQYFYSVFKKGYSITP 385
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 488138380   386 KEHR 389
Cdd:smart00342  81 SEYR 84
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
21-282 6.92e-26

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 106.82  E-value: 6.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  21 QVVEGVGEYLQA-------SQCNWDIFIEEDFrcrIDNIKDWLGDGVI---ADFDDRQIEQLlANVNVPIVGVGgSYHQS 90
Cdd:COG1609   78 ELLRGIEEAARErgyqlllANSDEDPEREREA---LRLLLSRRVDGLIlagSRLDDARLERL-AEAGIPVVLID-RPLPD 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  91 EDYPSVDyiaTDNKAlvnAAFM---HLKEKGLNRFAFYGLPAscGMRWAQEREYAFRQLVSAeqyQGVVYQGMATAPDNW 167
Cdd:COG1609  153 PGVPSVG---VDNRA---GARLateHLIELGHRRIAFIGGPA--DSSSARERLAGYREALAE---AGLPPDPELVVEGDF 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 168 QY--AQNRLADWVQTLPHQTGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLSrVALSSVVQGTRQMGYR 245
Cdd:COG1609  222 SAesGYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLT-PPLTTVRQPIEEMGRR 300

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 488138380 246 AAKLLHQRLklrqkQQTDPPLQRILVPPvKVMARRST 282
Cdd:COG1609  301 AAELLLDRI-----EGPDAPPERVLLPP-ELVVREST 331
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 285-393 1.50e-20

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


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 91.37  E-value: 1.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 285 RSLRDPAVIQAMHYIRHHACKGIKVEQVLDAVGMSRSNLEKRFKDEVGQTIHGVIHEEKLDRARNLLAATSLPINEISQM 364
Cdd:COG4977  205 LGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAA 284

                         90       100
                 ....*....|....*....|....*....
gi 488138380 365 CGYPSLQYFYSVFKKGYSITPKEHRDKYG 393
Cdd:COG4977  285 CGFGSASHFRRAFRRRFGVSPSAYRRRFR 313
HTH_18 pfam12833
Helix-turn-helix domain;
314-391 6.39e-17

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 74.93  E-value: 6.39e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488138380  314 DAVGMSRSNLEKRFKDEVGQTIHGVIHEEKLDRARNLLA-ATSLPINEISQMCGYPSLQYFYSVFKKGYSITPKEHRDK 391
Cdd:pfam12833   3 AALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLeDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRRR 81
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
288-397 3.63e-16

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 78.09  E-value: 3.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 288 RDPAVIQAMHYIRHHACKGIKVEQVLDAVGMSRSNLEKRFKDEVGQTIHGVIHEEKLDRARNLLAATSLPINEISQMCGY 367
Cdd:PRK10572 181 MDPRVREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGY 260

                         90       100       110
                 ....*....|....*....|....*....|
gi 488138380 368 PSLQYFYSVFKKGYSITPKEHRDKYGEVSY 397
Cdd:PRK10572 261 DDQLYFSRVFKKCTGASPSEFRARCEEKNN 290
adjacent_YSIRK TIGR04094
YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only ...
 288-389 7.58e-12

YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only one protein with the YSIRK variant form of signal peptide (TIGR01168) were examined for conserved genes near that one tagged protein. This protein is found adjacent to at various classes of repetitive or low-complexity YSIRK proteins (whether unique in genome or not), in a range of species (Enterococcus faecalis X98, Ruminococcus torques, Coprobacillus sp. D7, Lysinibacillus fusiformis ZC1, Streptococcus equi subsp. equi 4047, etc). The affliated YSIRK proteins include Streptococcal protective antigen (see ) and proteins with the Rib/alpha/Esp surface antigen repeat (see TIGR02331). The last quarter of this protein has an AraC family helix-turn-helix (HTH)transcriptional regulator domain.


Pssm-ID: 274977 [Multi-domain]  Cd Length: 383  Bit Score: 66.24  E-value: 7.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  288 RDPAVIQAMHYIRHHACKGIKVEQVLDAVGMSRSNLEKRFKDEVGQTIHGVIHEEKLDRARNLLAAtSLPINEISQMCGY 367
Cdd:TIGR04094 283 HSPLIRAVIQYINLNLYDPLKVEEIAKQFFMSESKLRKLFKKEMGISIQEYISKRKIEEAKYLLRS-QIPVSEVSNELGF 361

                          90       100
                  ....*....|....*....|..
gi 488138380  368 PSLQYFYSVFKKGYSITPKEHR 389
Cdd:TIGR04094 362 YDLSHFSRTFKKHTGVSPKQYQ 383
lacI PRK09526
lac repressor; Reviewed
 43-282 2.71e-04

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 42.67  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  43 EDFRCRIDNIKDWLGDGVIADF--DDRQIEQLLA-NVNVPIVgvggsYHQSEDYPSVDYIATDNKALVNAAFMHLKEKGL 119
Cdd:PRK09526 107 EACQAAVNELLAQRVSGVIINVplEDADAEKIVAdCADVPCL-----FLDVSPQSPVNSVSFDPEDGTRLGVEHLVELGH 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 120 NRFAFYGLPA---SCGMR---WAQEREYAFRQLVSaeqyqgvVYQGMATAPDNWQYAQNRLADwvqtLPHQTGIIAVTDA 193
Cdd:PRK09526 182 QRIALLAGPEssvSARLRlagWLEYLTDYQLQPIA-------VREGDWSAMSGYQQTLQMLRE----GPVPSAILVANDQ 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 194 RARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLSRvALSSVVQGTRQMGYRAAKLLHQRLklrqkQQTDPPLQRILvpP 273
Cdd:PRK09526 251 MALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIP-PLTTIKQDFRLLGKEAVDRLLALS-----QGQAVKGSQLL--P 322


                 ....*....
gi 488138380 274 VKVMARRST 282
Cdd:PRK09526 323 TSLVVRKST 331
 
Name Accession Description Interval E-value
PBP1_XylR cd01543
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ...
 7-282 1.07e-93

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: 281.78  E-value: 1.07e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380   7 RITLLFNANKVYDRQVVEGVGEYLQASQcNWDIFIEEDFRC-RIDNIKDWLGDGVIADFDDRQIEQLLANVNVPIVGVGG 85
Cdd:cd01543    1 RVALLLETSRGYGRRLLRGIARYAREHG-PWSLYLEPPGYEeLLDLLKGWKGDGIIARLDDPELAEALRRLGIPVVNVSG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  86 SYHQsedyPSVDYIATDNKALVNAAFMHLKEKGLNRFAFYGLPascGMRWAQEREYAFRQLVSAEQYQGVVYQGMATA-P 164
Cdd:cd01543   80 SRPE----PGFPRVTTDNEAIGRMAAEHLLERGFRHFAFCGFR---NAAWSRERGEGFREALREAGYECHVYESPPSGsS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 165 DNWQYAQNRLADWVQTLPHQTGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLSRVALSSVVQGTRQMGY 244
Cdd:cd01543  153 RSWEEEREELADWLKSLPKPVGIFACNDDRARQVLEACREAGIRVPEEVAVLGVDNDELICELSSPPLSSIALDAEQIGY 232

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 488138380 245 RAAKLLHQRLKlrqkqQTDPPLQRILVPPVKVMARRST 282
Cdd:cd01543  233 EAAELLDRLMR-----GERVPPEPILIPPLGVVTRQST 265
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
 113-282 4.89e-34

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: 123.99  E-value: 4.89e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  113 HLKEKGLNRFAFYGLPASCGMRWAQEREYAFRQLVSAEQYQGVVYQGMATAPDNWQYAQNRLaDWVQTLPhqTGIIAVTD 192
Cdd:pfam13377   1 HLAELGHRRIALIGPEGDRDDPYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARERL-RWLGALP--TAVFVAND 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  193 ARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLSRvALSSVVQGTRQMGYRAAKLLHQRLklrqkQQTDPPLQRILVP 272
Cdd:pfam13377  78 EVALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSP-PLTTVRVDAEELGRAAAELLLDLL-----NGEPAPPERVLLP 151

                         170
                  ....*....|
gi 488138380  273 PvKVMARRST 282
Cdd:pfam13377 152 P-ELVEREST 160
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
 21-273 1.06e-26

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: 107.22  E-value: 1.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  21 QVVEGVGEYLQA-------SQCNWDIFIEEDFrcrIDNIKDWLGDGVI---ADFDDRQIEQLLANvNVPIVGVGGSYhqs 90
Cdd:cd06267   16 ELLRGIEDAARErgyslllCNTDEDPEREREY---LRLLLSRRVDGIIlapSSLDDELLEELLAA-GIPVVLIDRRL--- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  91 eDYPSVDYIATDNKALVNAAFMHLKEKGLNRFAFYGLPAScgMRWAQEREYAFRQLVSA---EQYQGVVYQGmataPDNW 167
Cdd:cd06267   89 -DGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLD--LSTSRERLEGYRDALAEaglPVDPELVVEG----DFSE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 168 QYAQNRLADWVQTLPHQTGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLSrVALSSVVQGTRQMGYRAA 247
Cdd:cd06267  162 ESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLT-PPLTTVRQPAYEMGRAAA 240

                        250       260
                 ....*....|....*....|....*.
gi 488138380 248 KLLHQRLKlrqkqQTDPPLQRILVPP 273
Cdd:cd06267  241 ELLLERIE-----GEEEPPRRIVLPT 261
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
306-389 2.01e-26

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 101.09  E-value: 2.01e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380   306 GIKVEQVLDAVGMSRSNLEKRFKDEVGQTIHGVIHEEKLDRARNLLAATSLPINEISQMCGYPSLQYFYSVFKKGYSITP 385
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 488138380   386 KEHR 389
Cdd:smart00342  81 SEYR 84
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
21-282 6.92e-26

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 106.82  E-value: 6.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  21 QVVEGVGEYLQA-------SQCNWDIFIEEDFrcrIDNIKDWLGDGVI---ADFDDRQIEQLlANVNVPIVGVGgSYHQS 90
Cdd:COG1609   78 ELLRGIEEAARErgyqlllANSDEDPEREREA---LRLLLSRRVDGLIlagSRLDDARLERL-AEAGIPVVLID-RPLPD 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  91 EDYPSVDyiaTDNKAlvnAAFM---HLKEKGLNRFAFYGLPAscGMRWAQEREYAFRQLVSAeqyQGVVYQGMATAPDNW 167
Cdd:COG1609  153 PGVPSVG---VDNRA---GARLateHLIELGHRRIAFIGGPA--DSSSARERLAGYREALAE---AGLPPDPELVVEGDF 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 168 QY--AQNRLADWVQTLPHQTGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLSrVALSSVVQGTRQMGYR 245
Cdd:COG1609  222 SAesGYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLT-PPLTTVRQPIEEMGRR 300

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 488138380 246 AAKLLHQRLklrqkQQTDPPLQRILVPPvKVMARRST 282
Cdd:COG1609  301 AAELLLDRI-----EGPDAPPERVLLPP-ELVVREST 331
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
173-392 3.14e-21

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 92.15  E-value: 3.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 173 RLADWVQTLPHQTGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLSRVALSSVVQGTRQMGYRAAKLLHQ 252
Cdd:COG2207   35 VLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLLLVGLLLLLLLLLLLLLLLLLLLLL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 253 RLKLRQKQQTDPPLQRILVPPVKVMARRSTDFRSLRDPAVIQAMHYIRHHACKGIKVEQVLDAVGMSRSNLEKRFKDEVG 332
Cdd:COG2207  115 LLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETG 194

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 333 QTIHGVIHEEKLDRARNLLAATSLPINEISQMCGYPSLQYFYSVFKKGYSITPKEHRDKY 392
Cdd:COG2207  195 TSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRL 254
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 285-393 1.50e-20

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


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 91.37  E-value: 1.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 285 RSLRDPAVIQAMHYIRHHACKGIKVEQVLDAVGMSRSNLEKRFKDEVGQTIHGVIHEEKLDRARNLLAATSLPINEISQM 364
Cdd:COG4977  205 LGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAA 284

                         90       100
                 ....*....|....*....|....*....
gi 488138380 365 CGYPSLQYFYSVFKKGYSITPKEHRDKYG 393
Cdd:COG4977  285 CGFGSASHFRRAFRRRFGVSPSAYRRRFR 313
PBP1_AglR_RafR-like cd06292
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ...
 18-282 2.13e-20

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


Pssm-ID: 380515 [Multi-domain]  Cd Length: 273  Bit Score: 90.02  E-value: 2.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  18 YDRQVVEGVGEYLQASQCNWDIFIEEDFRCRIDNIKDWLG----DGVI---ADFDDRQIeQLLANVNVPIVGVGGSYHQS 90
Cdd:cd06292   17 FFDEFLAALGHAAAARGYDVLLFTASGDEDEIDYYRDLVRsrrvDGFVlasTRHDDPRV-RYLHEAGVPFVAFGRANPDL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  91 eDYPSVDyiaTDNKALVNAAFMHLKEKGLNRFAFYGLPAscGMRWAQEREYAFRQLVSAEQY---QGVVYQGMATAPDNW 167
Cdd:cd06292   96 -DFPWVD---VDGAAGMRQAVRHLIALGHRRIGLIGGPE--GSVPSDDRLAGYRAALEEAGLpfdPGLVVEGENTEEGGY 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 168 QYAQNRLAdwvqtLPHQ-TGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLSrVALSSVVQGTRQMGYRA 246
Cdd:cd06292  170 AAAARLLD-----LGPPpTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTH-PPLTTVRQPIDEIGRAV 243

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 488138380 247 AKLLHQRLklrqkQQTDPPLQRILVPPvKVMARRST 282
Cdd:cd06292  244 VDLLLAAI-----EGNPSEPREILLQP-ELVVRESS 273
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 7-282 7.00e-18

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


Pssm-ID: 380508 [Multi-domain]  Cd Length: 269  Bit Score: 82.66  E-value: 7.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380   7 RITLLFNAnkvydrQVVEGVGEYLQASQCNwdIFI---EEDFRCRIDNIKDWLG---DGVI---ADFDDRQIeQLLANVN 77
Cdd:cd06285    8 DLSNPFYA------ELVEGIEDAARERGYT--VLLadtGDDPERELAALDSLLSrrvDGLIitpARDDAPDL-QELAARG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  78 VPIVGVGgsyHQSEDyPSVDYIATDNKAlvnAAFM---HLKEKGLNRFAFYGLPAScgmrW--AQEREYAFRQlVSAEQY 152
Cdd:cd06285   79 VPVVLVD---RRIGD-TALPSVTVDNEL---GGRLatrHLLELGHRRIAVVAGPLN----AstGRDRLRGYRR-ALAEAG 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 153 QGVVYQGMATAPDNWQYAQNRLADWVQTLPHQTGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLSrVAL 232
Cdd:cd06285  147 LPVPDERIVPGGFTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLP-PPL 225

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 488138380 233 SSVVQGTRQMGYRAAKLLHQRLKLRQKqqtdPPLQRILVPPVKVmaRRST 282
Cdd:cd06285  226 TTVRQPKYEMGRRAAELLLQLIEGGGR----PPRSITLPPELVV--REST 269
PBP1_MalR-like cd06294
ligand-binding domain of maltose transcription regulator MalR which is a member of the ...
 21-272 1.43e-17

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


Pssm-ID: 380517 [Multi-domain]  Cd Length: 269  Bit Score: 81.86  E-value: 1.43e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  21 QVVEGVGEylQASQCNWDIFI-----EEDfrcRIDNIKDWLG----DGVI---ADFDDrQIEQLLANVNVPIVGVGgsyh 88
Cdd:cd06294   21 EVLRGISQ--VANENGYSLLLatgntEEE---LLEEVKRMVRgrrvDGFIllySKEDD-PLIEYLKEEGFPFVVIG---- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  89 QSEDYPSVDYIATDNkalVNAAFM---HLKEKGLNRFAFYGLPAscGMRWAQEREYAFRQLVSaEQYQGVVYQGMATAPD 165
Cdd:cd06294   91 KPLDDNDVLYVDNDN---VQAGYEateYLIDKGHKRIAFIGGDK--NLVVSIDRLQGYKQALK-EAGLPLDDDYILLLDF 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 166 NWQYAQNRLADWVQTLPHQTGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRyLSRVALSSVVQGTRQMGYR 245
Cdd:cd06294  165 SEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAE-LASPPLTSVDINPYELGRE 243

                        250       260
                 ....*....|....*....|....*..
gi 488138380 246 AAKLLHQRLKLRQKQQTdpplqRILVP 272
Cdd:cd06294  244 AAKLLINLLEGPESLPK-----NVIVP 265
PBP1_GalR cd01544
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ...
 58-281 2.71e-17

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


Pssm-ID: 380486 [Multi-domain]  Cd Length: 269  Bit Score: 81.03  E-value: 2.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVIA--DFDDRQIEQLLAnVNVPIVGVGgsyhQSEDYPSVDYIATDNKALVNAAFMHLKEKGLNRFAF---YGLPASCG 132
Cdd:cd01544   55 DGIIAigKFSKEEIEKLKK-LNPNIVFVD----SNPDPDGFDSVVPDFEQAVRQALDYLIELGHRRIGFiggKEYTSDDG 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 133 MRWAQEREYAFRQLVSA--EQYQGVVYQGMATAPDNWQYAQNRLADWvqTLPhqTGIIAVTDARARHLLQVCEHLDIAVP 210
Cdd:cd01544  130 EEIEDPRLRAFREYMKEkgLYNEEYIYIGEFSVESGYEAMKELLKEG--DLP--TAFFVASDPMAIGALRALQEAGIKVP 205

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488138380 211 EKLSVIGIDNEELTRYLSRvALSSV-VQgTRQMGYRAAKLLHQRLklrqKQQTDPPLQRILvpPVKVMARRS 281
Cdd:cd01544  206 EDISIISFNDIEVAKYVTP-PLTTVhIP-TEEMGRTAVRLLLERI----NGGRTIPKKVLL--PTKLIERES 269
HTH_18 pfam12833
Helix-turn-helix domain;
314-391 6.39e-17

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 74.93  E-value: 6.39e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488138380  314 DAVGMSRSNLEKRFKDEVGQTIHGVIHEEKLDRARNLLA-ATSLPINEISQMCGYPSLQYFYSVFKKGYSITPKEHRDK 391
Cdd:pfam12833   3 AALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLeDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRRR 81
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
 14-281 8.51e-17

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: 79.51  E-value: 8.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  14 ANKVYDrQVVEGVGEYLQASqcNWDIFI------EEDFRCRIDNIKDWLGDGVI---ADFDDRQIEQLlaNVNVPIVGVg 84
Cdd:cd06284   10 SNPFYS-EILRGIEDAAAEA--GYDVLLgdtdsdPEREDDLLDMLRSRRVDGVIllsGRLDAELLSEL--SKRYPIVQC- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  85 gsyhqSE--DYPSVDYIATDNKAlvnAAFM---HLKEKGLNRFAFYGLPAscGMRWAQEREYAFRQlvsAEQYQGVVYQG 159
Cdd:cd06284   84 -----CEyiPDSGVPSVSIDNEA---AAYDateYLISLGHRRIAHINGPL--DNVYARERLEGYRR---ALAEAGLPVDE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 160 MATAPDNWQYAQNRLAdwVQTL----PHQTGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLSrVALSSV 235
Cdd:cd06284  151 DLIIEGDFSFEAGYAA--ARALlalpERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFS-PSLTTI 227

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 488138380 236 VQGTRQMGYRAAKLLHQRLklrqkQQTDPPLQRILVpPVKVMARRS 281
Cdd:cd06284  228 RQPRYEIGETAAELLLEKI-----EGEGVPPEHIIL-PHELIVRES 267
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
 58-273 1.66e-16

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


Pssm-ID: 380512 [Multi-domain]  Cd Length: 268  Bit Score: 78.76  E-value: 1.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVI----ADFDDRQIEQLLANvNVPIV----GVGGSyhqsedypSVDYIATDNKALVNAAFMHLKEKGLNRFAFYGLPA 129
Cdd:cd06289   57 DGLIlspaAGTTAELLRRLKAW-GIPVVlalrDVPGS--------DLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLS 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 130 SCGMRwaQEREYAFRQLVSAEQYQGVVYQGMATAPDNWQYAQ--NRLADwVQTLPhqTGIIAVTDARARHLLQVCEHLDI 207
Cdd:cd06289  128 DSSTR--RERLAGFRAALAEAGLPLDESLIVPGPATREAGAEaaRELLD-AAPPP--TAVVCFNDLVALGAMLALRRRGL 202

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488138380 208 AVPEKLSVIGIDNEELTRyLSRVALSSVVQGTRQMGYRAAKLLHQRLklrqkQQTDPPLQRILVPP 273
Cdd:cd06289  203 EPGRDIAVVGFDDVPEAA-LWTPPLTTVSVHPREIGRRAARLLLRRI-----EGPDTPPERIIIEP 262
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
288-397 3.63e-16

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 78.09  E-value: 3.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 288 RDPAVIQAMHYIRHHACKGIKVEQVLDAVGMSRSNLEKRFKDEVGQTIHGVIHEEKLDRARNLLAATSLPINEISQMCGY 367
Cdd:PRK10572 181 MDPRVREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGY 260

                         90       100       110
                 ....*....|....*....|....*....|
gi 488138380 368 PSLQYFYSVFKKGYSITPKEHRDKYGEVSY 397
Cdd:PRK10572 261 DDQLYFSRVFKKCTGASPSEFRARCEEKNN 290
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
 58-281 6.01e-16

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: 77.18  E-value: 6.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVIAdFDDRQIEQLLANVNVPIVGVGGSYhqSEDYPSVdyiATDNKALVNAAFMHLKEKGLNRFAFYG--LPASCgmrw 135
Cdd:cd06291   57 DGIIL-GSHSLDIEEYKKLNIPIVSIDRYL--SEGIPSV---SSDNYQGGRLAAEHLIEKGCKKILHIGgpSNNSP---- 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 136 AQEREYAFRQLVSAEQYQGVVYQgMATAPDNWQYAQNRLADWVQTLPHQTGIIAVTDARARHLLQVCEHLDIAVPEKLSV 215
Cdd:cd06291  127 ANERYRGFEDALKEAGIEYEIIE-IDENDFSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQI 205

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488138380 216 IGIDNEELTRYlSRVALSSVVQGTRQMGYRAAKLLHQRLKLRQKQQTdpplqRILVpPVKVMARRS 281
Cdd:cd06291  206 IGFDGIEISEL-LYPELTTIRQPIEEMAKEAVELLLKLIEGEEIEES-----RIVL-PVELIERET 264
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 288-389 2.97e-15

Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), contains Zn-binding and two AraC-type DNA-binding domains [Replication, recombination and repair];


Pssm-ID: 441772 [Multi-domain]  Cd Length: 358  Bit Score: 76.25  E-value: 2.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 288 RDPAVIQAMHYIRHHACKGIKVEQVLDAVGMSRSNLEKRFKDEVGQTIHGVIHEEKLDRARNLLaATSLPINEISQMCGY 367
Cdd:COG2169   82 RADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL-QTGLSVTDAAYAAGF 160

                         90       100
                 ....*....|....*....|..
gi 488138380 368 PSLQYFYSVFKKGYSITPKEHR 389
Cdd:COG2169  161 GSLSRFYEAFKKLLGMTPSAYR 182
PBP1_DegA_Like cd19976
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
 21-273 4.65e-15

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: 74.59  E-value: 4.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  21 QVVEGVGEYLQasQCNWDIFI---EEDFRCRIDNIKDWLG---DGVI---ADFDDRQIEQLLANVNVPIVGVGgSYHQSE 91
Cdd:cd19976   16 ELVRGIEDTLN--ELGYNIILcntYNDFEREKKYIQELKErnvDGIIiasSNISDEAIIKLLKEEKIPVVVLD-RYIEDN 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  92 DYPSV--D-----YIATDnkalvnaafmHLKEKGLNRFAF-YGLPASCGMrwaQEREYAFRQLVSAEQ---YQGVVYQGM 160
Cdd:cd19976   93 DSDSVgvDdyrggYEATK----------YLIELGHTRIGCiVGPPSTYNE---HERIEGYKNALQDHNlpiDESWIYSGE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 161 ATAPDNWQYAQNRLADwvqtlPHQTGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLSRvALSSVVQGTR 240
Cdd:cd19976  160 SSLEGGYKAAEELLKS-----KNPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITP-ALTTIAQPIF 233

                        250       260       270
                 ....*....|....*....|....*....|...
gi 488138380 241 QMGYRAAKLLHQRLKlrqkqQTDPPLQRILVPP 273
Cdd:cd19976  234 EMGQEAAKLLLKIIK-----NPAKKKEEIVLPP 261
PBP1_RegR_EndR_KdgR-like cd06283
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ...
 65-272 6.03e-15

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: 74.12  E-value: 6.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  65 DDRQIEQLLANVNVPIVGVGGSYHQSEdypsVDYIATDNKALVNAAFMHLKEKGLNRFAFYGLPAScGMRWAQEREYAFR 144
Cdd:cd06283   66 NNNDAYLELAQKGLPVVLVDRQIEPLN----WDTVVTDNYDATYEATEHLKEQGYERIVFVTEPIK-GISTRRERLQGFL 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 145 QLVSAEQYQGVVYQgmaTAPDNWQYAQNRLADWVQTLPHQ-TGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEEL 223
Cdd:cd06283  141 DALARYNIEGDVYV---IEIEDTEDLQQALAAFLSQHDGGkTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDW 217

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 488138380 224 TRyLSRVALSSVVQGTRQMGYRAAKLLHQRLKlrqkqQTDPPLQRILVP 272
Cdd:cd06283  218 AD-LIGPGITTIRQPTYEIGKAAAEILLERIE-----GDSGEPKEIELP 260
PBP1_sucrose_transcription_regulator cd06288
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ...
 58-272 2.80e-14

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: 72.20  E-value: 2.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVI-ADFDDRQIEQLLANVNVPIVGVGGsYHQSEDYPSVDYiatDNkalVNAAFM---HLKEKGLNRFAFYGLPAScgM 133
Cdd:cd06288   58 DGIIyASMHHREVTLPPELTDIPLVLLNC-FDDDPSLPSVVP---DD---EQGGYLatrHLIEAGHRRIAFIGGPED--S 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 134 RWAQEREYAFRQLVSAEqyqGVVYQGMATAPDNWQYAQNRLA--DWVQTLPHQTGIIAVTDARARHLLQVCEHLDIAVPE 211
Cdd:cd06288  129 LATRLRLAGYRAALAEA---GIPYDPSLVVHGDWGRESGYEAakRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPE 205

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488138380 212 KLSVIGIDNEELTRYLsRVALSSVVQGTRQMGYRAAKLLhqrlkLRQKQQTDPPLQRILVP 272
Cdd:cd06288  206 DLSVVGFDNQELAAYL-RPPLTTVALPYYEMGRRAAELL-----LDGIEGEPPEPGVIRVP 260
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 58-273 7.68e-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: 380516 [Multi-domain]  Cd Length: 270  Bit Score: 71.15  E-value: 7.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVI---ADFDDRQIEQLLAnVNVPIVgvggSYHQSEDYPSVDYIATDNKALVNAAFMHLKEKGLNRFAFYGLPAScgMR 134
Cdd:cd06293   57 RGLIvtpSDDDLSHLARLRA-RGTAVV----LLDRPAPGPAGCSVSVDDVQGGALAVDHLLELGHRRIAFVSGPLR--TR 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 135 WAQEREYAFRQLV--SAEQYQGVVYQGmaTAPDNWQYAQNRLADWVQTLPHQ-TGIIAVTDARARHLLQVCEHLDIAVPE 211
Cdd:cd06293  130 QVAERLAGARAAVaeAGLDPDEVVREL--SAPDANAELGRAAAAQLLAMPPRpTAVFAANDLLALGLLAGLRRAGLRVPD 207

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488138380 212 KLSVIGIDNEELTRYLSrVALSSVVQGTRQMGYRAAKLLhqrlkLRQKQQTDPPLQRILVPP 273
Cdd:cd06293  208 DVSVVGYDDLPFAAAAN-PPLTTVRQPSYELGRAAADLL-----LDEIEGPGHPHEHVVFQP 263
PBP1_AglR-like cd20010
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ...
 21-273 2.34e-13

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: 69.50  E-value: 2.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  21 QVVEGVGEYLqaSQCNWDIFI--------EEDFRCRIdnIKDWLGDGVI----ADFDDRqIEQLLANvNVPIVgVGGSYH 88
Cdd:cd20010   20 EFLAGLSEAL--AERGLDLLLapapsgedELATYRRL--VERGRVDGFIlartRVNDPR-IAYLLER-GIPFV-VHGRSE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  89 QSEDYPSVDyiaTDNKALVNAAFMHLKEKGLNRFAFYGLPAScgMRWAQEREYAFRQLVSA---EQYQGVVYQGMATAPD 165
Cdd:cd20010   93 SGAPYAWVD---IDNEGAFRRATRRLLALGHRRIALLNGPEE--LNFAHQRRDGYRAALAEaglPVDPALVREGPLTEEG 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 166 NWQYAQNRLAdwvqtLPHQ-TGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLSRVALSSVVQGTRQMGY 244
Cdd:cd20010  168 GYQAARRLLA-----LPPPpTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLLPALEYFSPPLTTTRSSLRDAGR 242

                        250       260
                 ....*....|....*....|....*....
gi 488138380 245 RAAKLLHQRLKlrqkqQTDPPLQRILVPP 273
Cdd:cd20010  243 RLAEMLLALID-----GEPAAELQELWPP 266
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
 58-274 6.36e-13

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: 68.33  E-value: 6.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVI---ADFDDRQIEQLLANvNVPIVGVGGSYHQSEdypsVDYIATDNKALVNAAFMHLKEKGLNRFAFYGLPASCGMR 134
Cdd:cd19977   57 DGIIiapTGGNEDLIEKLVKS-GIPVVFVDRYIPGLD----VDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLELSTR 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 135 waQEREYAFRQ-------LVSAEQYQGV-VYQGMATAPDNWQYAQNRLadwvqtlphqTGIIAVTDARARHLLQVCEHLD 206
Cdd:cd19977  132 --QERLEGYKAaladhglPVDEELIKHVdRQDDVRKAISELLKLEKPP----------DAIFAANNLITLEVLKAIKELG 199

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488138380 207 IAVPEKLSVIGIDNEELTRYLsRVALSSVVQGTRQMGYRAAKLLHQRLKLRQKQQTdpplQRILVPPV 274
Cdd:cd19977  200 LRIPDDIALIGFDDIPWADLF-NPPLTVIAQPTYEIGRKAAELLLDRIENKPKGPP----RQIVLPTE 262
PBP1_LacI-like cd06279
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ...
 18-250 6.94e-13

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: 68.39  E-value: 6.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  18 YDRQVVEGVGEYLQASQCNWDIFIEEDFRCRIDNIKDWLGDGVIA--DFDDRQIEQLLANVNVPIVGVGGSYHqsEDYPS 95
Cdd:cd06279   18 VAAQFLRGVAEVCEEEGLGLLLLPATDEGSAAAAVRNAAVDGFIVygLSDDDPAVAALRRRGLPLVVVDGPAP--PGIPS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  96 VdyiATDNKALVNAAFMHLKEKGLNRFAFYGLPASCGMR---WAQEREYAFRQLVSAEQYQGVVyQGMATA--------- 163
Cdd:cd06279   96 V---GIDDRAAARAAARHLLDLGHRRIAILSLRLDRGRErgpVSAERLAAATNSVARERLAGYR-DALEEAgldlddvpv 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 164 ---PDNWQYAQNRLADWV-QTLPHQTGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRyLSRVALSSVVQGT 239
Cdd:cd06279  172 veaPGNTEEAGRAAARALlALDPRPTAILCMSDVLALGALRAARERGLRVPEDLSVTGFDDIPEAA-AADPGLTTVRQPA 250

                        250
                 ....*....|.
gi 488138380 240 RQMGYRAAKLL 250
Cdd:cd06279  251 VEKGRAAARLL 261
adjacent_YSIRK TIGR04094
YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only ...
 288-389 7.58e-12

YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only one protein with the YSIRK variant form of signal peptide (TIGR01168) were examined for conserved genes near that one tagged protein. This protein is found adjacent to at various classes of repetitive or low-complexity YSIRK proteins (whether unique in genome or not), in a range of species (Enterococcus faecalis X98, Ruminococcus torques, Coprobacillus sp. D7, Lysinibacillus fusiformis ZC1, Streptococcus equi subsp. equi 4047, etc). The affliated YSIRK proteins include Streptococcal protective antigen (see ) and proteins with the Rib/alpha/Esp surface antigen repeat (see TIGR02331). The last quarter of this protein has an AraC family helix-turn-helix (HTH)transcriptional regulator domain.


Pssm-ID: 274977 [Multi-domain]  Cd Length: 383  Bit Score: 66.24  E-value: 7.58e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  288 RDPAVIQAMHYIRHHACKGIKVEQVLDAVGMSRSNLEKRFKDEVGQTIHGVIHEEKLDRARNLLAAtSLPINEISQMCGY 367
Cdd:TIGR04094 283 HSPLIRAVIQYINLNLYDPLKVEEIAKQFFMSESKLRKLFKKEMGISIQEYISKRKIEEAKYLLRS-QIPVSEVSNELGF 361

                          90       100
                  ....*....|....*....|..
gi 488138380  368 PSLQYFYSVFKKGYSITPKEHR 389
Cdd:TIGR04094 362 YDLSHFSRTFKKHTGVSPKQYQ 383
PBP1_CcpA-like cd19975
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
 58-255 1.17e-11

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: 64.50  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVI--ADFDDRQIEQLLANVNVPIVGVGGSYHQSeDYPSVDyiaTDNKALVNAAFMHLKEKGLNRFAFYGLPA---SCG 132
Cdd:cd19975   57 DGIIfaSGTLTEENKQLLKNMNIPVVLVSTESEDP-DIPSVK---IDDYQAAYDATNYLIKKGHRKIAMISGPLddpNAG 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 133 mrwaQEREYAFRQlvsAEQYQGVVYqgmataPDNW-QYAQNRLADWVQTL-------PHQTGIIAVTDARARHLLQVCEH 204
Cdd:cd19975  133 ----YPRYEGYKK---ALKDAGLPI------KENLiVEGDFSFKSGYQAMkrllknkKLPTAVFAASDEMALGVISAAYD 199

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488138380 205 LDIAVPEKLSVIGIDNEELTRYlSRVALSSVVQGTRQMGYRAAKLLHQRLK 255
Cdd:cd19975  200 HGIRVPEDISVIGFDNTEIAEM-SIPPLTTVSQPFYEMGKKAVELLLDLIK 249
PBP1_PurR cd06275
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ...
 113-281 3.37e-11

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: 63.04  E-value: 3.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 113 HLKEKGLNRFAFYGLPAscGMRWAQEREYAFRQlvsAEQYQGV------VYQGMATAPDNWQyAQNRLAdwvqTLPHQ-T 185
Cdd:cd06275  111 HLIELGHRRIGCITGPL--EHSVSRERLAGFRR---ALAEAGIevppswIVEGDFEPEGGYE-AMQRLL----SQPPRpT 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 186 GIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLSRvALSSVVQGTRQMGYRAAKLLHQRLklrqkQQTDPP 265
Cdd:cd06275  181 AVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSP-ALTTIHQPKDELGELAVELLLDRI-----ENKREE 254

                        170
                 ....*....|....*.
gi 488138380 266 LQRILVPPVKVMaRRS 281
Cdd:cd06275  255 PQSIVLEPELIE-RES 269
PBP1_CcpB-like cd06286
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ...
 87-255 5.49e-11

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: 62.56  E-value: 5.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  87 YHQSEDYPSVdYIatDNKALVNAAFMHLKEKGLNRFAF-YGLPASCGMRwAQEREYAFR------QLVSAEQYqgvVYQG 159
Cdd:cd06286   85 ETDSPDIPSV-YI--DRYEAYLEALEYLKEKGHRKIGYcLGRPESSSAS-TQARLKAYQdvlgehGLSLREEW---IFTN 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 160 MATAPDNWQYAQNrladWVQTLPHQTGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLsrvALSSVVQGT 239
Cdd:cd06286  158 CHTIEDGYKLAKK----LLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISELL---NLTTIDQPL 230

                        170
                 ....*....|....*.
gi 488138380 240 RQMGYRAAKLLHQRLK 255
Cdd:cd06286  231 EEMGKEAFELLLSQLE 246
PBP1_LacI-like cd06273
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 58-281 5.99e-11

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


Pssm-ID: 380497 [Multi-domain]  Cd Length: 268  Bit Score: 62.53  E-value: 5.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVI---ADFDDRqIEQLLANVNVPIVgVGGSYHQSEDYPSVDYiatDNKALVNAAFMHLKEKGLNRFAFYGLPASCGMR 134
Cdd:cd06273   57 DGLIlvgSDHDPE-LFELLEQRQVPYV-LTWSYDEDSPHPSIGF---DNRAAAARAAQHLLDLGHRRIAVISGPTAGNDR 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 135 wAQEREYAFRQLVSAeqyqgvvyQGMATAPD-----NWQYAQNRLAdwVQTL----PHQTGIIAVTDARARHLLQVCEHL 205
Cdd:cd06273  132 -ARARLAGIRDALAE--------RGLELPEErvveaPYSIEEGREA--LRRLlarpPRPTAIICGNDVLALGALAECRRL 200

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488138380 206 DIAVPEKLSVIGIDNEELTRYLSrVALSSVVQGTRQMGYRAAKLLHQRLklrqkQQTDPPLQRILvpPVKVMARRS 281
Cdd:cd06273  201 GISVPEDLSITGFDDLELAAHLS-PPLTTVRVPAREIGELAARYLLALL-----EGGPPPKSVEL--ETELIVRES 268
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
 21-281 8.19e-11

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: 62.19  E-value: 8.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  21 QVVEGVGEYLQASQCNWDIFI-EEDFRCRIDNIKDWLG---DGVIAD-------FDDRQIEQLLANVNVPIVGVGGSYHQ 89
Cdd:cd01541   16 SIIQGIESVLSENGYSLLLALtNNDVEKEREILESLLDqnvDGLIIEptksalpNPNLDLYEELQKKGIPVVFINSYYPE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  90 sedyPSVDYIATDNkalVNAAFM---HLKEKGLNRFAFYglpascgmrwaqereyaFRqlvsAEQYQGVV-YQGMATA-- 163
Cdd:cd01541   96 ----LDAPSVSLDD---EKGGYLatkHLIDLGHRRIAGI-----------------FK----SDDLQGVErYQGFIKAlr 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 164 ------PDNW-----------QYAQNRLADWVQTLPHQTGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRY 226
Cdd:cd01541  148 eaglpiDDDRilwystedledRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASL 227

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488138380 227 lSRVALSSVVQGTRQMGYRAAKLLHQRLKLRQKQqtdpplQRILVPPvKVMARRS 281
Cdd:cd01541  228 -SEPPLTSVVHPKEELGRKAAELLLRMIEEGRKP------ESVIFPP-ELIERES 274
PBP1_CatR-like cd06296
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ...
 58-282 2.13e-10

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: 60.75  E-value: 2.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVIA---DFDDRQIEqLLANVNVPIVGVGGSYHQSEDYPSVdyiATDNKALVNAAFMHLKEKGLNRFAFYGLPAscGMR 134
Cdd:cd06296   57 AGVVLvtsDPTSRQLR-LLRSAGIPFVLIDPVGEPDPDLPSV---GATNWAGGRLATEHLLDLGHRRIAVITGPP--RSV 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 135 WAQEREYAFRQLVSAeqyqgvvyQGMATAPD-----NWQYAQN--------RLADwvqtLPhqTGIIAVTDARARHLLQV 201
Cdd:cd06296  131 SGRARLAGYRAALAE--------AGIAVDPDlvregDFTYEAGyraarellELPD----PP--TAVFAGNDEQALGVYRA 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 202 CEHLDIAVPEKLSVIGIDNEELTRYLSrVALSSVVQGTRQMGYRAAKLLHQRLKLRqkqqtDPPLQRILVPPVKVmARRS 281
Cdd:cd06296  197 ARALGLRVPDDLSVIGFDDTPPARWTS-PPLTTVHQPLREMGAVAVRLLLRLLEGG-----PPDARRIELATELV-VRGS 269


                 .
gi 488138380 282 T 282
Cdd:cd06296  270 T 270
PBP1_LacI-like cd19974
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 58-281 2.87e-10

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


Pssm-ID: 380629 [Multi-domain]  Cd Length: 270  Bit Score: 60.64  E-value: 2.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVI--ADFDDRQIEQLlANVNVPIVGVGgsyHQSEDYPSvDYIATDNkalVNAAFM---HLKEKGLNRFAFYGLPASCg 132
Cdd:cd19974   60 DGIIilGEISKEYLEKL-KELGIPVVLVD---HYDEELNA-DSVLSDN---YYGAYKltsYLIEKGHKKIGFVGDINYT- 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 133 mRWAQEREYAFRQlvsAEQYQGVVYQgmataPDNW----QYAQNRLADWVQT-----LPhqTGIIAVTDARARHLLQVCE 203
Cdd:cd19974  131 -SSFMDRYLGYRK---ALLEAGLPPE-----KEEWlledRDDGYGLTEEIELplklmLP--TAFVCANDSIAIQLIKALK 199

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488138380 204 HLDIAVPEKLSVIGIDNEELTRYLSrVALSSVVQGTRQMGYRAAKLLHQRLklrqkQQTDPPLQRILVpPVKVMARRS 281
Cdd:cd19974  200 EKGYRVPEDISVVGFDNIELAELST-PPLTTVEVDKEAMGRRAVEQLLWRI-----ENPDRPFEKILV-SGKLIERDS 270
PBP1_SalR cd01545
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ...
 65-267 4.94e-10

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


Pssm-ID: 380487 [Multi-domain]  Cd Length: 270  Bit Score: 59.88  E-value: 4.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  65 DDRQIEQLLANVNVPIVGVGgSYHQSEDYPSVdyiATDNKALVNAAFMHLKEKGLNRFAFYGLPASCGMrwAQEREYAFR 144
Cdd:cd01545   68 DDPALLDALDELGIPYVRIA-PGTDDDRSPSV---RIDDRAAAREMTRHLIALGHRRIGFIAGPPDHGA--SAERLEGFR 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 145 QLVSA---EQYQGVVYQGMATAPDNWQYAQNRLadwvqTLPHQ-TGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDN 220
Cdd:cd01545  142 DALAEaglPLDPDLVVQGDFTFESGLEAAEALL-----DLPDRpTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDD 216

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 488138380 221 EELTRYLSRvALSSVVQGTRQMGYRAAKLLHQRLKLRQKQQTDPPLQ 267
Cdd:cd01545  217 SPIARLVWP-PLTTVRQPIAEMARRAVELLIAAIRGAPAGPERETLP 262
PBP1_CcpA_TTHA0807 cd06297
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ...
 8-254 5.51e-10

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


Pssm-ID: 380520 [Multi-domain]  Cd Length: 268  Bit Score: 59.79  E-value: 5.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380   8 ITLLFNANKVYDRqVVEGVGEYLQASQCNWDIFI------EEDFRCRIDNIKdwLGDGVIA---DFDDRqIEQLLANVNV 78
Cdd:cd06297    4 LLVPEVMTPFYMR-LLTGVERALDENRYDLAIFPllseyrLEKYLRNSTLAY--QCDGLVMaslDLTEL-FEEVIVPTEK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  79 PIVGVGgsyhqsEDYPSVDYIATDNKALVNAAFMHLKEKGLNRFAFyglpascgmrWAQEREYAFRQLVSAEQYQG---- 154
Cdd:cd06297   80 PVVLID------ANSMGYDCVYVDNVKGGFMATEYLAGLGEREYVF----------FGIEEDTVFTETVFREREQGflea 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 155 -------VVYQGMATAPDNWQYAQNRLADWVQTLPHQTGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTryl 227
Cdd:cd06297  144 lnkagrpISSSRMFRIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWA--- 220

                        250       260
                 ....*....|....*....|....*..
gi 488138380 228 SRVALSSVVQGTRQMGYRAAKLLHQRL 254
Cdd:cd06297  221 ASPGLTTVRQPVEEMGEAAAKLLLKRL 247
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 58-281 6.03e-10

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


Pssm-ID: 380501 [Multi-domain]  Cd Length: 266  Bit Score: 59.47  E-value: 6.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVI---ADFDDRQIEQLLANvNVPIVGVGGsyhQSEDyPSVDYIATDNKALVNAAFMHLKEKGLNRFAFYGLPAScgmR 134
Cdd:cd06278   56 DGVIvtsATLSSELAEECARR-GIPVVLFNR---VVED-PGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPEG---T 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 135 WA-QEREYAFRQLVSAeqyQG----VVYQGMATAPDNWQYAQNRLADwvQTLPhqTGIIAVTD---------ARARHLLq 200
Cdd:cd06278  128 STsRERERGFRAALAE---LGlpppAVEAGDYSYEGGYEAARRLLAA--PDRP--DAIFCANDlmalgaldaARQEGGL- 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 201 vcehldiAVPEKLSVIGIDNEELTRYLSrVALSSVVQGTRQMGYRAAKLLHQRLklrqKQQTDPPLQRILvpPVKVMARR 280
Cdd:cd06278  200 -------VVPEDISVVGFDDIPMAAWPS-YDLTTVRQPIEEMAEAAVDLLLERI----ENPETPPERRVL--PGELVERG 265


                 .
gi 488138380 281 S 281
Cdd:cd06278  266 S 266
PBP1_GalS-like cd06270
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ...
 58-267 6.26e-10

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: 59.46  E-value: 6.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVI--ADFDDRQIEQLLANVNVPIVGVGGSYHQSEDYpsvdYIATDNKAlvnAAFM---HLKEKGLNRFAFYGLPASCg 132
Cdd:cd06270   57 DAIIlhSRALSDEELILIAEKIPPLVVINRYIPGLADR----CVWLDNEQ---GGRLaaeHLLDLGHRRIACITGPLDI- 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 133 mRWAQEREYAFRQlvsAEQYQGVVYQGMATAPDNWQYAQNRLAdwVQTLPHQ----TGIIAVTDARARHLLQVCEHLDIA 208
Cdd:cd06270  129 -PDARERLAGYRD---ALAEAGIPLDPSLIIEGDFTIEGGYAA--AKQLLARglpfTALFAYNDDMAIGALAALHEAGIK 202

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488138380 209 VPEKLSVIGIDNEELTRYLSrVALSSVVQGTRQMGYRAAKLLhqrLKLRQKQQTDPPLQ 267
Cdd:cd06270  203 VPEDVSVIGFDDVPLARYLS-PKLTTVHYPIEEMAQAAAELA---LNLAYGEPLPISHE 257
PBP1_AglR_RafR-like cd06271
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ...
 58-274 6.51e-10

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


Pssm-ID: 380495 [Multi-domain]  Cd Length: 264  Bit Score: 59.36  E-value: 6.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVI---ADFDDRQIeQLLANVNVPIVGVGGSyHQSEDYPSVDYiatDNKALVNAAFMHLKEKGLNRFAFYGLPAScgMR 134
Cdd:cd06271   59 DGVIlseIEPNDPRV-QFLTKQNFPFVAHGRS-D*PIGHAWVDI---DNEAGAYEAVERLAGLGHRRIAFIVPPAR--YS 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 135 WAQEREYAFRQLVSAEQYQGVVYQGMATAPDNWQYAQnRLAdwvQTLPHQTGIIAVTDARARHLLQVCEHLDIAVPEKLS 214
Cdd:cd06271  132 PHDRRLQGYVRA*RDAGLTGYPLDADTTLEAGRAAAQ-RLL---ALSPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVS 207

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 215 VIGIDNEELTRYLSRVALSSVVQGTRQMGYRAAKLLHQRLKLRqkqqtDPPLQRILVPPV 274
Cdd:cd06271  208 IIGKDSAPFLGAMITPPLTTVHAPIAEAGRELAKALLARIDGE-----DPETLQVLVQPS 262
PBP1_LacI-like cd06277
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 39-271 9.65e-10

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


Pssm-ID: 380500 [Multi-domain]  Cd Length: 275  Bit Score: 58.79  E-value: 9.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  39 IFIEEDFRCRIDNIKDWLGDGVI---ADFDDRQIeQLLANVNVPIVGVGGSYHqsedYPSVDYIATDNKALVNAAFMHLK 115
Cdd:cd06277   44 VDIGDDFDEILKELTDDQSSGIIllgTELEEKQI-KLFQDVSIPVVVVDNYFE----DLNFDCVVIDNEDGAYEAVKYLV 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 116 EKGLNRFafyGLPASCG-MRWAQEREYAFRQlvsAEQYQGVVYQG-----MATAPDNWQYAQNRLADWVQTLPhqTGIIA 189
Cdd:cd06277  119 ELGHTRI---GYLASSYrIKNFEERRRGFRK---AMRELGLSEDPepefvVSVGPEGAYKDMKALLDTGPKLP--TAFFA 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 190 VTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRyLSRVALSSVVQGTRQMGYRAAKLLHQRLKlrqkqQTDPPLQRI 269
Cdd:cd06277  191 ENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSA-MVDPPLTTIHVPKEQMGKLAVRRLIEKIK-----DPDGGTLKI 264


                 ..
gi 488138380 270 LV 271
Cdd:cd06277  265 LV 266
PBP1_LacI cd01574
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ...
 58-273 1.11e-09

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: 58.75  E-value: 1.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVIA-DFDDRQIEQL-LANVNVPIVGVGGSyhqseDYPSVDYIATDNKALVNAAFMHLKEKGLNRFAFYGLPascgMRW 135
Cdd:cd01574   58 DGIIViAPDEAVLEALrRLPPGLPVVIVGSG-----PSPGVPTVSIDQEEGARLATRHLLELGHRRIAHIAGP----LDW 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 136 --AQEREYAFRQ-LVSAEQYQGVVYQGmatapdNWQ----YAQ-NRLADwvqtLPHQTGIIAVTDARARHLLQVCEHLDI 207
Cdd:cd01574  129 vdARARLRGWREaLEEAGLPPPPVVEG------DWSaasgYRAgRRLLD----DGPVTAVFAANDQMALGALRALHERGL 198

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488138380 208 AVPEKLSVIGIDNEELTRYLSrVALSSVVQGTRQMGYRAAKLLhqrlkLRQKQQTDPPLQRILVPP 273
Cdd:cd01574  199 RVPEDVSVVGFDDIPEAAYFV-PPLTTVRQDFAELGRRAVELL-----LALIEGPAPPPESVLLPP 258
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
 71-281 1.44e-09

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: 58.28  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  71 QLLANVNVPIVGVGgsyhqseDYPS--VDY-IATDNKALVNAAFMHLKEKGLNRFAFYGLPASCGMRwAQEREYAFRQLV 147
Cdd:cd01575   72 KLLRAAGIPVVETW-------DLPDdpIDMaVGFSNFAAGRAMARHLIERGYRRIAFVGARLDGDSR-ARQRLEGFRDAL 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 148 SAEQYQGVVYQGMATAPdnwQYAQNR--LADWVQTLPHQTGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTR 225
Cdd:cd01575  144 AEAGLPLPLVLLVELPS---SFALGReaLAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAA 220

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488138380 226 YLSrVALSSVVQGTRQMGYRAAKLLHQRLklrqkQQTDPPLQRILVPPvKVMARRS 281
Cdd:cd01575  221 ALP-PALTTVRVPRYEIGRKAAELLLARL-----EGEEPEPRVVDLGF-ELVRRES 269
ftrA PRK09393
transcriptional activator FtrA; Provisional
 240-393 1.56e-09

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 58.82  E-value: 1.56e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 240 RQMGYRAAKLLHQRLKL---RQKQQTdpplQRILVPpvkVMARRSTDFRSLrdpaviqaMHYIRHHACKGIKVEQVLDAV 316
Cdd:PRK09393 180 RDFGSEAANRVARRLVVpphRDGGQA----QFVPRP---VASRESDRLGPL--------IDWMRAHLAEPHTVASLAARA 244

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488138380 317 GMSRSNLEKRFKDEVGQTIHGVIHEEKLDRARNLLAATSLPINEISQMCGYPSLQYFYSVFKKGYSITPKEHRDKYG 393
Cdd:PRK09393 245 AMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRKRFG 321
PBP1_LacI-like cd06290
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 22-281 1.26e-08

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: 55.31  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  22 VVEGVGEYLQASQ-------CNWDIFIEED-----FRCRIDNIKdwlgdgVIADFDDRQIEQLLANvNVPIVGVGGSyhq 89
Cdd:cd06290   17 ILNGIEEVLAESGytlivstSHWNADRELEilrllLARKVDGII------VVGGFGDEELLKLLAE-GIPVVLVDRE--- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  90 sEDYPSVDYIATDNkalVNAAFM---HLKEKGLNRFAFYGLPAScgMRWAQEREYAFRQ-LVSA--EQYQGVVYQGMATA 163
Cdd:cd06290   87 -LEGLNLPVVNVDN---EQGGYNatnHLIDLGHRRIVHISGPED--HPDAQERYAGYRRaLEDAglEVDPRLIVEGDFTE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 164 PDNWQYAQNRLADWVqtlpHQTGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLsRVALSSVVQGTRQMG 243
Cdd:cd06290  161 ESGYEAMKKLLKRGG----PFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYT-TPPLTTVRQPLYEMG 235

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 488138380 244 YRAAKLLHQRLklrqkqQTDPPLQRILVPPVKVMARRS 281
Cdd:cd06290  236 KTAAEILLELI------EGKGRPPRRIILPTELVIRES 267
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
 58-270 1.34e-08

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: 55.19  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVI--ADFDDRQIEQLLANVNVPIVGVGgsyHQSEDYPSV---DYIATdnKALVNaafmHLKEKGLNRFAFYGLPascg 132
Cdd:cd01542   57 DGIIlfATEITDEHRKALKKLKIPVVVLG---QEHEGFSCVyhdDYGAG--KLLGE----YLLKKGHKNIAYIGVD---- 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 133 mrwaqEREYAfrqlVSAEQYQGVvYQGMATAPD----------NWQYAQNRLADWVQTLPHqTGIIAVTDARARHLLQVC 202
Cdd:cd01542  124 -----EEDIA----VGVARKQGY-LDALKEHGIdeveivetdfSMESGYEAAKELLKENKP-DAIICATDNIALGAIKAL 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488138380 203 EHLDIAVPEKLSVIGIDNEELTRYLSRvALSSVVQGTRQMGYRAAKLLhqrlkLRQKQQTDPPLQRIL 270
Cdd:cd01542  193 RELGIKIPEDISVAGFGGYDLSEFVSP-SLTTVKFDYEEAGEKAAELL-----LDMIEGEKVPKKQKL 254
PBP1_LacI-like cd06299
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ...
 58-250 3.84e-08

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: 54.21  E-value: 3.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVIADFDDRQIEQLLANVN--VPIVGVGgsyHQSEDYPSVDYIATDNKALVNAAFMHLKEKGLNRFAFYGLPASCGMrw 135
Cdd:cd06299   57 DGIIAVPTGENSEGLQALIAqgLPVVFVD---REVEGLGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYISGPLSTST-- 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 136 AQEREYAFRQLVSA---EQYQGVVYQGMATAPDNWQyAQNRLADWVQTLphqTGIIAVTDARARHLLQVCEHLDIAVPEK 212
Cdd:cd06299  132 GRERLAAFRAALTAagiPIDEELVAFGDFRQDSGAA-AAHRLLSRGDPP---TALIAGDSLMALGAIQALRELGLRIGDD 207

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 488138380 213 LSVIGIDNEELTRYLSRvALSSVVQGTRQMGYRAAKLL 250
Cdd:cd06299  208 VSLISFDDVPWFELLSP-PLTVIAQPVERIGRRAVELL 244
PBP1_LacI-like cd06281
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 40-272 5.79e-08

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: 53.40  E-value: 5.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  40 FIEEDFRCRIDnikdwlgdGVIA---DFDDRQIEQLLANVNVPIVGVGGsyhqseDYPS-VDYIATDNKALVNAAFMHLK 115
Cdd:cd06281   47 LLSLFQRRRVD--------GLILtpgDEDDPELAAALARLDIPVVLIDR------DLPGdIDSVLVDHRSGVRQATEYLL 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 116 EKGLNRFAFygLPASCGMRWAQEREYAFRQLVSAeqyqgvvyQGMATAPD----NWQYAQNRLADWVQTLPHQ---TGII 188
Cdd:cd06281  113 SLGHRRIAL--LTGGPDIRPGRERIAGFKAAFAA--------AGLPPDPDlvrlGSFSADSGFREAMALLRQPrppTAII 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 189 A--------VTDA-RARHLlqvcehldiAVPEKLSVIGIDNEELTRYLSRvALSSVVQGTRQMGYRAAKLLHQRLklrqK 259
Cdd:cd06281  183 AlgtqllagVLRAvRAAGL---------RIPGDLSVVSIGDSDLAELHDP-PITAIRWDLDAVGRAAAELLLDRI----E 248

                        250
                 ....*....|...
gi 488138380 260 QQTDPPLQRILVP 272
Cdd:cd06281  249 GPPAGPPRRIVVP 261
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
 318-391 5.86e-08

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 53.39  E-value: 5.86e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488138380 318 MSRSNLEKRFKDEvGQTIHGVIHEEKLDRARNLLAATSLPINEISQMCGYPSLQYFYSVFKKGYSITPKEHRDK 391
Cdd:PRK09978 170 MSPSLLKKKLREE-ETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFRNYYGMTPTEYQER 242
PBP1_CelR cd06295
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ...
 58-281 8.77e-08

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: 53.02  E-value: 8.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVI----ADFDDRQIEqlLANVNVPIVgVGGSYHQSEDYPSVDyiaTDNKALVNAAFMHLKEKGLNRFAFYGLPascgm 133
Cdd:cd06295   65 DGLIvlgqGLDHDALRE--LAQQGLPMV-VWGAPEDGQSYCSVG---SDNVKGGALATEHLIEIGRRRIAFLGDP----- 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 134 rwaQEREYAFRqlvsaeqYQGVVyQGMATAPDNWQYAQNRLADW--------VQTLPHQT----GIIAVTDARArhlLQV 201
Cdd:cd06295  134 ---PHPEVADR-------LQGYR-DALAEAGLEADPSLLLSCDFteesgyaaMRALLDSGtafdAIFAASDLIA---MGA 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 202 CEHLD---IAVPEKLSVIGIDNEELTRYlSRVALSSVVQGTRQmgyrAAKLLHQRLkLRqkQQTDPPLQRILVpPVKVMA 278
Cdd:cd06295  200 IRALRergISVPGDVAVVGYDDIPLAAY-FRPPLTTVRQDLAL----AGRLLVEKL-LA--LIAGEPVTSSML-PVELVV 270


                 ...
gi 488138380 279 RRS 281
Cdd:cd06295  271 RES 273
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
 58-279 9.00e-08

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: 53.03  E-value: 9.00e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVI---ADFDDRQIEQLLANvNVPIV----GVGGsyhqsedyPSVDYIATDNKALVNAAFMHLKEKGLNRFAF-YGLPA 129
Cdd:cd06280   57 DGIIlapSAGPSRELKRLLKH-GIPIVlidrEVEG--------LELDLVAGDNREGAYKAVKHLIELGHRRIGLiTGPLE 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 130 SCGMRwaqEREYAFRQlvsAEQYQGVVYqgmataPDNW-QYAQNRLA-------DWVQTLPHQTGIIAVTDARARHLLQV 201
Cdd:cd06280  128 ISTTR---ERLAGYRE---ALAEAGIPV------DESLiFEGDSTIEggyeavkALLDLPPRPTAIFATNNLMAVGALRA 195

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488138380 202 CEHLDIAVPEKLSVIGIDNEELTRyLSRVALSSVVQGTRQMGYRAAKLLHQRLKlrqKQQTDPPlqRILVPPvKVMAR 279
Cdd:cd06280  196 LRERGLEIPQDISVVGFDDSDWFE-IVDPPLTVVAQPAYEIGRIAAQLLLERIE---GQGEEPR--RIVLPT-ELIIR 266
PBP1_LacI-like cd06282
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 58-272 2.90e-07

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


Pssm-ID: 380505 [Multi-domain]  Cd Length: 267  Bit Score: 51.51  E-value: 2.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVI---ADFDDRQIEQLLANVNVPIVGVggsYHQSEDyPSVDYIATDN-KALVNAAFmHLKEKGLNRFAFYGLPASCGM 133
Cdd:cd06282   57 DGLIltvGDAQGSEALELLEEEGVPYVLL---FNQTEN-SSHPFVSVDNrLASYDVAE-YLIALGHRRIAMVAGDFSASD 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 134 RwAQEREYAFRQlvsAEQYQGVVYQGMATAPDNwqyaQNRLADWVQTL----PHQTGIIAVTDARARHLLQVCEHLDIAV 209
Cdd:cd06282  132 R-ARLRYQGYRD---ALKEAGLKPIPIVEVDFP----TNGLEEALTSLlsgpNPPTALFCSNDLLALSVISALRRLGIRV 203

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488138380 210 PEKLSVIGIDNEELTRYLSRvALSSVVQGTRQMGYRAAKLLHQRLKLRQkqqtdpPLQRILVP 272
Cdd:cd06282  204 PDDVSVIGFDGIAIGELLTP-TLATVVQPSRDMGRAAADLLLAEIEGES------PPTSIRLP 259
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 69-255 3.29e-07

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: 51.16  E-value: 3.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380   69 IEQLLANvNVPIVGVGgsyHQSEDYPSVDYIATDN----KALVNAAFMHLKEKGlNRFAFYGLPascGMRWAQEREYAFR 144
Cdd:pfam13407  73 LKKAKDA-GIPVVTFD---SDAPSSPRLAYVGFDNeaagEAAGELLAEALGGKG-KVAILSGSP---GDPNANERIDGFK 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  145 QlVSAEQYQGVVYQGmATAPDNWQY--AQNRLADWVQTLPHQT-GIIAVTDARARHLLQVCEHLDIAvpEKLSVIGIDNE 221
Cdd:pfam13407 145 K-VLKEKYPGIKVVA-EVEGTNWDPekAQQQMEALLTAYPNPLdGIISPNDGMAGGAAQALEAAGLA--GKVVVTGFDAT 220

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 488138380  222 ELTRYL--SRVALSSVVQGTRQMGYRAAKLLHQRLK 255
Cdd:pfam13407 221 PEALEAikDGTIDATVLQDPYGQGYAAVELAAALLK 256
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
 309-387 5.13e-07

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 50.83  E-value: 5.13e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488138380 309 VEQVLDAVGMSRSNLEKRFKDEvGQTIHGVIHEEKLDRARNLLAATSLPINEISQMCGYPSLQYFYSVFKKGYSITPKE 387
Cdd:PRK15186 200 LKDISDSLYMSCSTLKRKLKQE-NTSFSEVYLNARMNKATKLLRNSEYNITRVAYMCGYDSASYFTCVFKKHFKTTPSE 277
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
 308-385 5.94e-07

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 50.76  E-value: 5.94e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488138380 308 KVEQVLDAVGMSRSNLEKRFKDEvGQTIHGVIHEEKLDRARNLLAATSLPINEISQMCGYPSLQYFYSVFKKGYSITP 385
Cdd:PRK15185 224 KLTDVADHIFMSTSTLKRKLAEE-GTSFSDIYLSARMNQAAKLLRIGNHNVNAVALKCGYDSTSYFIQCFKKYFKTTP 300
PBP1_LacI-like cd06287
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 58-271 8.85e-07

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


Pssm-ID: 380510 [Multi-domain]  Cd Length: 268  Bit Score: 50.11  E-value: 8.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVIA---DFDDRQIEQLLANvNVPIVGVGGSYHQSEDYPSVDYIATDNKALVNAafmHLKEKGLNRFAfygLPASCGMR 134
Cdd:cd06287   58 DGAIVvepTVEDPILARLRQR-GVPVVSIGRAPGTDEPVPYVDLQSAATARLLLE---HLHGAGARQVA---LLTGSSRR 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 135 WAQ-EREYAFRQLVSAEQYQGVVYQGMATAPDNWQYAQNRLAdwVQTLPHQTGIIAVTDARARHLLQVCEHLDIAVPEKL 213
Cdd:cd06287  131 NSSlESEAAYLRFAQEYGTTPVVYKVPESEGERAGYEAAAAL--LAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPEDL 208

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488138380 214 SVIgidneelTRYLSRVALSSVVQGT------RQMGYRAAKLLHQRLKLRQKQQTDPPLQRILV 271
Cdd:cd06287  209 MVV-------TRYDGIRARTADPPLTavdlhlDRVARTAIDLLFASLSGEERSVEVGPAPELVV 265
PRK10371 PRK10371
transcriptional regulator MelR;
232-389 1.07e-06

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 49.82  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 232 LSSVVQGTRQMGYRAAKLLHQRLKLRQkqqtdppLQRILVPPVKVMARRSTDFRSLRdpAVIQAMHYIRHHACKGIKVEQ 311
Cdd:PRK10371 142 LNSPNEQIRQLAIDEIGLMLKRFSLSG-------WEPILVNKTSRTHKNSVSRHAQF--YVSQMLGFIAENYDQALTIND 212

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488138380 312 VLDAVGMSRSNLEKRFKDEVGQTIHGVIHEEKLDRARNLLAATSLPINEISQMCGYPSLQYFYSVFKKGYSITPKEHR 389
Cdd:PRK10371 213 VAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSSRFYSTFGKYVGMSPQQYR 290
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 299-340 1.91e-06

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


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 44.07  E-value: 1.91e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 488138380  299 IRHHACKGIKVEQVLDAVGMSRSNLEKRFKDEVGQTIHGVIH 340
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
PRK09940 PRK09940
transcriptional regulator YdeO; Provisional
 308-392 3.35e-06

transcriptional regulator YdeO; Provisional


Pssm-ID: 182157 [Multi-domain]  Cd Length: 253  Bit Score: 48.16  E-value: 3.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 308 KVEQVLDAVGMSRSNLEKRFKDEvGQTIHGVIHEEKLDRARNLLAATSlPINEISQMCGYPSLQYFYSVFKKGYSITPKE 387
Cdd:PRK09940 152 KLKDICDCLYISESLLKKKLKQE-QTTFSQILLDARMQHAKNLIRVEG-SVNKIAEQCGYASTSYFIYAFRKHFGNSPKR 229


                 ....*
gi 488138380 388 HRDKY 392
Cdd:PRK09940 230 VSKEY 234
PBP1_CcpA cd06298
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ...
 58-250 6.02e-06

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: 47.29  E-value: 6.02e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  58 DGVI--ADFDDRQIEQLLANVNVPIVGVGGSYHQSEdYPSVdyiATDNKALVNAAFMHLKEKGLNRFAFYGLPascgMRW 135
Cdd:cd06298   57 DGIIfmGDELTEEIREEFKRSPVPVVLAGTVDSDHE-IPSV---NIDYEQAAYDATKSLIDKGHKKIAFVSGP----LKE 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 136 AQEREYAFRQLVSAEQYQGVVYQGMATAPDNWQYAQN-RLADWVQTLPHQTGIIAVTDARARHLLQVCEHLDIAVPEKLS 214
Cdd:cd06298  129 YINNDKKLQGYKRALEEAGLEFNEPLIFEGDYDYDSGyELYEELLESGEPDAAIVVRDEIAVGLLNAAQDRGLKVPEDLE 208

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 488138380 215 VIGIDNeelTRY--LSRVALSSVVQGTRQMGYRAAKLL 250
Cdd:cd06298  209 IIGFDN---TRYatMSRPQLTSINQPLYDIGAVAMRLL 243
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 352-389 1.66e-05

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


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 41.76  E-value: 1.66e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 488138380  352 AATSLPINEISQMCGYpSLQYFYSVFKKGYSITPKEHR 389
Cdd:pfam00165   5 LSTNLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYR 41
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
294-389 3.83e-05

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 45.05  E-value: 3.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 294 QAMHYIRHHACKGIKVEQVLDAVGMSRSNLEKRFKDEVGQTIHGVIHEEKLDRARNLLAATSLPINEISQMCGYPSLQYF 373
Cdd:PRK13503 175 QLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGDSNHF 254

                         90
                 ....*....|....*.
gi 488138380 374 YSVFKKGYSITPKEHR 389
Cdd:PRK13503 255 STLFRREFSWSPRDIR 270
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
319-389 3.90e-05

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 45.05  E-value: 3.90e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488138380 319 SRSNLEKRFKDEVGQTIHGVIHEEKLDRARNLLAATSLPINEISQMCGYPSLQYFYSVFKKGYSITPKEHR 389
Cdd:PRK13502 205 SERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWR 275
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
309-389 4.50e-05

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 45.09  E-value: 4.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 309 VEQVLDAVGMSRSNLEKRFKDEVGQTIHGVIHEEKLDRARNLLAATSLPINEISQMCGYPSLQYFYSVFKKGYSITPKEH 388
Cdd:PRK13500 225 LDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDSNYFSVVFTRETGMTPSQW 304


                 .
gi 488138380 389 R 389
Cdd:PRK13500 305 R 305
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
318-392 4.52e-05

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 44.90  E-value: 4.52e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488138380 318 MSRSNLEKRFKDEVGQTIHGVIHEEKLDRARNLLAATSLPINEISQMCGYPSLQYFYSVFKKGYSITPKEHRDKY 392
Cdd:PRK13501 204 LVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFSAVFTREAGMTPRDYRQRF 278
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 60-255 1.02e-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: 380659 [Multi-domain]  Cd Length: 273  Bit Score: 43.76  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  60 VIADFDD----RQIEQLLANvNVPIVGV----GGSYHQSedypsvdYIATDNKA--LVNAAFM--HLKEKG---LNRFAf 124
Cdd:cd20004   62 VLAPLDRkalvAPVERARAQ-GIPVVIIdsdlGGDAVIS-------FVATDNYAagRLAAKRMakLLNGKGkvaLLRLA- 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 125 yGLPASCGMR---WAQE-REYAFRQLVSAEQYQGVvyqgmaTAPDnwqyAQNRLADWVQTLPHQTGIIAVTDARARHLLQ 200
Cdd:cd20004  133 -KGSASTTDRergFLEAlKKLAPGLKVVDDQYAGG------TVGE----ARSSAENLLNQYPDVDGIFTPNESTTIGALR 201

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488138380 201 VCEhlDIAVPEKLSVIGID-NEELTRYLSRVALSS-VVQGTRQMGYRAAKLLHQRLK 255
Cdd:cd20004  202 ALR--RLGLAGKVKFIGFDaSDLLLDALRAGEISAlVVQDPYRMGYLGVKTAVAALR 256
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 98-276 2.66e-04

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: 42.60  E-value: 2.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  98 YIATDNKA----LVNAAFMHLKEKGlNRFAFYGLPascGMRWAQEREYAFRQLVSAeqyqgvvYQGM---ATAPDNWQY- 169
Cdd:COG1879  132 YVGSDNYAagrlAAEYLAKALGGKG-KVAILTGSP---GAPAANERTDGFKEALKE-------YPGIkvvAEQYADWDRe 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 170 -AQNRLADWVQTLPHQTGIIAVTDARARHLLQVCEHLDIAvpEKLSVIGID-NEELTRYL-SRVALSSVVQGTRQMGYRA 246
Cdd:COG1879  201 kALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRK--GDVKVVGFDgSPEALQAIkDGTIDATVAQDPYLQGYLA 278

                        170       180       190
                 ....*....|....*....|....*....|
gi 488138380 247 AKLLHQRLKlrqkqQTDPPlQRILVPPVKV 276
Cdd:COG1879  279 VDAALKLLK-----GKEVP-KEILTPPVLV 302
lacI PRK09526
lac repressor; Reviewed
 43-282 2.71e-04

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 42.67  E-value: 2.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  43 EDFRCRIDNIKDWLGDGVIADF--DDRQIEQLLA-NVNVPIVgvggsYHQSEDYPSVDYIATDNKALVNAAFMHLKEKGL 119
Cdd:PRK09526 107 EACQAAVNELLAQRVSGVIINVplEDADAEKIVAdCADVPCL-----FLDVSPQSPVNSVSFDPEDGTRLGVEHLVELGH 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 120 NRFAFYGLPA---SCGMR---WAQEREYAFRQLVSaeqyqgvVYQGMATAPDNWQYAQNRLADwvqtLPHQTGIIAVTDA 193
Cdd:PRK09526 182 QRIALLAGPEssvSARLRlagWLEYLTDYQLQPIA-------VREGDWSAMSGYQQTLQMLRE----GPVPSAILVANDQ 250

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 194 RARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLSRvALSSVVQGTRQMGYRAAKLLHQRLklrqkQQTDPPLQRILvpP 273
Cdd:PRK09526 251 MALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIP-PLTTIKQDFRLLGKEAVDRLLALS-----QGQAVKGSQLL--P 322


                 ....*....
gi 488138380 274 VKVMARRST 282
Cdd:PRK09526 323 TSLVVRKST 331
PRK10703 PRK10703
HTH-type transcriptional repressor PurR;
156-289 2.82e-04

HTH-type transcriptional repressor PurR;


Pssm-ID: 236739 [Multi-domain]  Cd Length: 341  Bit Score: 42.40  E-value: 2.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 156 VYQGMATAPDNWQYAQNRLADwvQTLPhqTGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLSRvALSSV 235
Cdd:PRK10703 216 IVQGDFEPESGYEAMQQILSQ--KHRP--TAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTP-ALTTI 290

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488138380 236 VQGTRQMGYRAAKLLHQRLKLRQKQQtdpplQRILVPPVKVMaRRSTDFRSLRD 289
Cdd:PRK10703 291 HQPKDRLGETAFNMLLDRIVNKREEP-----QTIEVHPRLVE-RRSVADGPFRD 338
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 77-255 3.05e-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: 380542 [Multi-domain]  Cd Length: 278  Bit Score: 42.35  E-value: 3.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  77 NVPIV----GVGGSYHQSedypsvdYIATDNK--ALVNAAFM--HLKEKGL--NRFAFYGLPAScgMRWAQEREYAFRQL 146
Cdd:cd06319   80 KIPVViadiGTGGGDYVS-------YIISDNYdgGYQAGEYLaeALKENGWggGSVGIIAIPQS--RVNGQARTAGFEDA 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 147 VSAEQYQGVVYQGMA--TAPDNWQYAQNRLAdwvqTLPHQTGIIAVTDARARHLLQVCEhlDIAVPEKLSVIGID-NEEL 223
Cdd:cd06319  151 LEEAGVEEVALRQTPnsTVEETYSAAQDLLA----ANPDIKGIFAQNDQMAQGALQAIE--EAGRTGDILVVGFDgDPEA 224

                        170       180       190
                 ....*....|....*....|....*....|...
gi 488138380 224 TRYLSRVALS-SVVQGTRQMGYRAAKLLHQRLK 255
Cdd:cd06319  225 LDLIKDGKLDgTVAQQPFGMGARAVELAIQALN 257
PRK11041 PRK11041
DNA-binding transcriptional regulator CytR; Provisional
 180-255 1.34e-03

DNA-binding transcriptional regulator CytR; Provisional


Pssm-ID: 182923 [Multi-domain]  Cd Length: 309  Bit Score: 40.37  E-value: 1.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488138380 180 TLPHQ-TGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYlSRVALSSVVQGTRQMGYRAAKLLHQRLK 255
Cdd:PRK11041 209 DLPQPpTAVFCHSDVMALGALSQAKRMGLRVPQDLSIIGFDDIDLAQY-CDPPLTTVAQPRYEIGREAMLLLLEQLQ 284
PRK15044 PRK15044
transcriptional regulator SirC; Provisional
 318-385 1.35e-03

transcriptional regulator SirC; Provisional


Pssm-ID: 185004 [Multi-domain]  Cd Length: 295  Bit Score: 40.40  E-value: 1.35e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488138380 318 MSRSNLEKRFKDEvGQTIHGVIHEEKLDRARNLLAATSLPINEISQMCGYPSLQYFYSVFKKGYSITP 385
Cdd:PRK15044 220 MSVSSLKRKLAAE-EVSFSKIYLDARMNQAIKLLRMGAGNISQVATMCGYDTPSYFIAIFKRHFKITP 286
PBP1_RafR-like cd20009
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ...
 8-273 1.35e-03

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: 40.21  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380   8 ITLLFNANKVYD---RQVVEGVGEYLQASQCNWDIFIEEDFRCRIDNIKDW----LGDGVIAD----FDDRQieQLLANV 76
Cdd:cd20009    2 IALVLPTEDEIDgftSQLISGISEALRGTPYHLVVTPEFPGDDPLEPVRYIvenrLADGIIIShtepQDPRV--RYLLER 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  77 NVPIVGVGGSyHQSEDYPSVDYiatDNKALVNAAFMHLKEKGLNRFAFYGLPAscGMRWAQEREYAFRQlvsAEQYQGVv 156
Cdd:cd20009   80 GFPFVTHGRT-ELSTPHAYFDF---DNEAFAYEAVRRLAARGRRRIALVAPPR--ELTYAQHRLRGFRR---ALAEAGL- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 157 yQGMATAPDNWQYAQNRLADWVQTL----PHQTGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGIDNEELTRYLsRVAL 232
Cdd:cd20009  150 -EVEPLLIVTLDSSAEAIRAAARRLlrqpPRPDGIICASEIAALGALAGLEDAGLVVGRDVDVVAKETSPILDYF-RPPI 227

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 488138380 233 SSVVQGTRQMGYRAAKLLHQRLKlrqkQQTDPPLQRILVPP 273
Cdd:cd20009  228 DTLYEDIEEAGRFLAEALLRRIE----GEPAEPLQTLERPE 264
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
 63-274 2.48e-03

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: 39.54  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  63 DFDDRQIEQLLANVNVPIVGVGGSyhqSEDYPSVDYIATDNKALVNAAFMHLKEKGLNRFAFYGLP---ASCGMRWAQER 139
Cdd:cd01537   65 DPAAAGVAEKARGQNVPVVFFDKE---PSRYDKAYYVITDSKEGGIIQGDLLAKHGHIQIVLLKGPlghPDAEARLAGVI 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 140 EYAFRQLVSAEQYQGVvyQGMATAPDNWQYAQNRLADwvqtlPHQ-TGIIAVTDARARHLLQVCEHLDIAVPEKLSVIGI 218
Cdd:cd01537  142 KELNDKGIKTEQLQLD--TGDWDTASGKDKMDQWLSG-----PNKpTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGY 214

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 488138380 219 DNEELTRYlSRVALSSVVQGTRQMGYRAAKLLhqrLKLRQKQQTDPplQRILVPPV 274
Cdd:cd01537  215 DALPEALK-SGPLLTTILQDANNLGKTTFDLL---LNLADNWKIDN--KVVRVPYV 264
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
 49-255 9.94e-03

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: 37.55  E-value: 9.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380  49 IDNIKDWLGDGV----IADFDDRQIEQLLANVN---VPIVGVGGSYHQSEDYPSvdYIATDN----KALVNAAFMHLKEK 117
Cdd:cd01536   45 ISQIEDLIAQGVdaiiIAPVDSEALVPAVKKANaagIPVVAVDTDIDGGGDVVA--FVGTDNyeagKLAGEYLAEALGGK 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488138380 118 GlNRFAFYGLPascGMRWAQEREYAFRQlvSAEQYQG--VVyqgmATAPDNWQY--AQNRLADWVQTLPHQTGIIAVTDA 193
Cdd:cd01536  123 G-KVAILEGPP---GSSTAIDRTKGFKE--ALKKYPDieIV----AEQPANWDRakALTVTENLLQANPDIDAVFAANDD 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488138380 194 RARHLLQVCEHLDIAvpEKLSVIGIDN--EELTRYLSRVALSSVVQGTRQMGYRAAKLLHQRLK 255
Cdd:cd01536  193 MALGAAEALKAAGRT--GDIKIVGVDGtpEALKAIKDGELDATVAQDPYLQGYLAVEAAVKLLN 254
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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