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Conserved domains on  [gi|1123192800|gb|OKW40073|]
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XylR family transcriptional regulator [Escherichia coli]

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); ...
7-277 2.96e-102

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: 303.35  E-value: 2.96e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800   7 RITLLFNANKAYDRQVVEGVGEYLQASQSeWDIFIEEDFR-ARIDKIKDWLGDGVIADFDDKQIEQALADVDVPIVGVGG 85
Cdd:cd01543     1 RVALLLETSRGYGRRLLRGIARYAREHGP-WSLYLEPPGYeELLDLLKGWKGDGIIARLDDPELAEALRRLGIPVVNVSG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  86 SYHLAEsyspVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPessGKRWATEREYAFRQLVAEEKYRGVVYQG-LETAP 164
Cdd:cd01543    80 SRPEPG----FPRVTTDNEAIGRMAAEHLLERGFRHFAFCGFR---NAAWSRERGEGFREALREAGYECHVYESpPSGSS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 165 ENWQHAQNRLADWLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSRVALSSVAQGARQMGY 244
Cdd:cd01543   153 RSWEEEREELADWLKSLPKPVGIFACNDDRARQVLEACREAGIRVPEEVAVLGVDNDELICELSSPPLSSIALDAEQIGY 232
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1123192800 245 QAAKLLHRLLDKEEMPLQRILVPPVRVIERRST 277
Cdd:cd01543   233 EAAELLDRLMRGERVPPEPILIPPLGVVTRQST 265
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
301-384 1.13e-27

helix_turn_helix, arabinose operon control protein;


:

Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 104.56  E-value: 1.13e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  301 GIKVDQVLDAVGISRSNLEKRFKEEVGETIHAMIHAEKLEKARSLLISTTLSINEISQMCGYPSLQYFYSVFKKAYDTTP 380
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80

                   ....
gi 1123192800  381 KEYR 384
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); ...
7-277 2.96e-102

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: 303.35  E-value: 2.96e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800   7 RITLLFNANKAYDRQVVEGVGEYLQASQSeWDIFIEEDFR-ARIDKIKDWLGDGVIADFDDKQIEQALADVDVPIVGVGG 85
Cdd:cd01543     1 RVALLLETSRGYGRRLLRGIARYAREHGP-WSLYLEPPGYeELLDLLKGWKGDGIIARLDDPELAEALRRLGIPVVNVSG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  86 SYHLAEsyspVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPessGKRWATEREYAFRQLVAEEKYRGVVYQG-LETAP 164
Cdd:cd01543    80 SRPEPG----FPRVTTDNEAIGRMAAEHLLERGFRHFAFCGFR---NAAWSRERGEGFREALREAGYECHVYESpPSGSS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 165 ENWQHAQNRLADWLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSRVALSSVAQGARQMGY 244
Cdd:cd01543   153 RSWEEEREELADWLKSLPKPVGIFACNDDRARQVLEACREAGIRVPEEVAVLGVDNDELICELSSPPLSSIALDAEQIGY 232
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1123192800 245 QAAKLLHRLLDKEEMPLQRILVPPVRVIERRST 277
Cdd:cd01543   233 EAAELLDRLMRGERVPPEPILIPPLGVVTRQST 265
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
113-277 8.50e-40

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: 139.01  E-value: 8.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 113 HLKEKGVNRFAFYGLPESSGKRWATEREYAFRQLVAEEKYRGVVYQGLETAPENWQHAQNRLaDWLQTLPpqTGIIAVTD 192
Cdd:pfam13377   1 HLAELGHRRIALIGPEGDRDDPYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARERL-RWLGALP--TAVFVAND 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 193 ARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSRvALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQRILVPPvRVI 272
Cdd:pfam13377  78 EVALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSP-PLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPP-ELV 155

                  ....*
gi 1123192800 273 ERRST 277
Cdd:pfam13377 156 EREST 160
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
21-277 1.31e-30

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 119.53  E-value: 1.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  21 QVVEGVGEYLQA-------SQSEWDIFIEEDFrarIDKIKDWLGDGVI---ADFDDKQIEqALADVDVPIVGVGGSYHLA 90
Cdd:COG1609    78 ELLRGIEEAARErgyqlllANSDEDPEREREA---LRLLLSRRVDGLIlagSRLDDARLE-RLAEAGIPVVLIDRPLPDP 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  91 EsyspVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSgkRWATEREYAFRQLVAEekyRGVVYQGLETAPENW--Q 168
Cdd:COG1609   154 G----VPSVGVDNRAGARLATEHLIELGHRRIAFIGGPADS--SSARERLAGYREALAE---AGLPPDPELVVEGDFsaE 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 169 HAQNRLADWLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSrVALSSVAQGARQMGYQAAK 248
Cdd:COG1609   225 SGYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLT-PPLTTVRQPIEEMGRRAAE 303
                         250       260
                  ....*....|....*....|....*....
gi 1123192800 249 LLHRLLDKEEMPLQRILVPPvRVIERRST 277
Cdd:COG1609   304 LLLDRIEGPDAPPERVLLPP-ELVVREST 331
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
301-384 1.13e-27

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 104.56  E-value: 1.13e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  301 GIKVDQVLDAVGISRSNLEKRFKEEVGETIHAMIHAEKLEKARSLLISTTLSINEISQMCGYPSLQYFYSVFKKAYDTTP 380
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80

                   ....
gi 1123192800  381 KEYR 384
Cdd:smart00342  81 SEYR 84
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
262-384 9.24e-22

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: 94.84  E-value: 9.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 262 QRILVPPVR------VIERRstDYRSLTDPAVIQAMHYIRNHACKGIKVDQVLDAVGISRSNLEKRFKEEVGETIHAMIH 335
Cdd:COG4977   183 RRLVVDPRRpggqaqFSPLL--VPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQ 260
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1123192800 336 AEKLEKARSLLISTTLSINEISQMCGYPSLQYFYSVFKKAYDTTPKEYR 384
Cdd:COG4977   261 RLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYR 309
HTH_18 pfam12833
Helix-turn-helix domain;
309-384 6.94e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 80.33  E-value: 6.94e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1123192800 309 DAVGISRSNLEKRFKEEVGETIHAMIHAEKLEKARSLLISTT-LSINEISQMCGYPSLQYFYSVFKKAYDTTPKEYR 384
Cdd:pfam12833   3 AALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDTgLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
246-390 6.55e-15

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 74.62  E-value: 6.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 246 AAKLLHRLLDKEeMPLQRILVPPVRvierrstdyrsltDPAVIQAMHYIRNHACKGIKVDQVLDAVGISRSNLEKRFKEE 325
Cdd:PRK10572  158 AMNLLERLLLRC-MEAIPESLHPPM-------------DPRVREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQ 223
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1123192800 326 VGETIHAMIHAEKLEKARSLLISTTLSINEISQMCGYPSLQYFYSVFKKAYDTTPKEYRDVNSEV 390
Cdd:PRK10572  224 LGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSEFRARCEEK 288
adjacent_YSIRK TIGR04094
YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only ...
228-384 3.42e-14

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: 73.17  E-value: 3.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 228 SRVALSSVAQGARQMGYQAAKLLH---RLLDKEEMPLQRILVPPVR---------VIERRSTDYRSLTDPAVIQamhYIR 295
Cdd:TIGR04094 219 SIIIFEKLSQLAIQMGVDIVDAYRlrdYYIQEIEEQTSLMDVLKLRdsaiiyfteLLHEISINHHSPLIRAVIQ---YIN 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 296 NHACKGIKVDQVLDAVGISRSNLEKRFKEEVGETIHAMIHAEKLEKARSLLISTtLSINEISQMCGYPSLQYFYSVFKKA 375
Cdd:TIGR04094 296 LNLYDPLKVEEIAKQFFMSESKLRKLFKKEMGISIQEYISKRKIEEAKYLLRSQ-IPVSEVSNELGFYDLSHFSRTFKKH 374

                  ....*....
gi 1123192800 376 YDTTPKEYR 384
Cdd:TIGR04094 375 TGVSPKQYQ 383
lacI PRK09526
lac repressor; Reviewed
21-277 4.40e-08

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 54.23  E-value: 4.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  21 QVVEGVGEYlqASQSEWDIFI-------EEDFRARIDKIKDWLGDGVIADF-----DDKQIEQALADV-----DVPivgv 83
Cdd:PRK09526   80 QIAAAIKSR--ADQLGYSVVIsmversgVEACQAAVNELLAQRVSGVIINVpledaDAEKIVADCADVpclflDVS---- 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  84 ggsyhlaeSYSPVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSG------KRWATEREYAFRQLVAeekyrgvVY 157
Cdd:PRK09526  154 --------PQSPVNSVSFDPEDGTRLGVEHLVELGHQRIALLAGPESSVsarlrlAGWLEYLTDYQLQPIA-------VR 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 158 QGLETAPENWQHAQNRLADwlQTLPpqTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSRvALSSVAQ 237
Cdd:PRK09526  219 EGDWSAMSGYQQTLQMLRE--GPVP--SAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIP-PLTTIKQ 293
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1123192800 238 GARQMGYQAAKLLHRLLDKEEMPLQRILvpPVRVIERRST 277
Cdd:PRK09526  294 DFRLLGKEAVDRLLALSQGQAVKGSQLL--PTSLVVRKST 331
 
Name Accession Description Interval E-value
PBP1_XylR cd01543
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ...
7-277 2.96e-102

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: 303.35  E-value: 2.96e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800   7 RITLLFNANKAYDRQVVEGVGEYLQASQSeWDIFIEEDFR-ARIDKIKDWLGDGVIADFDDKQIEQALADVDVPIVGVGG 85
Cdd:cd01543     1 RVALLLETSRGYGRRLLRGIARYAREHGP-WSLYLEPPGYeELLDLLKGWKGDGIIARLDDPELAEALRRLGIPVVNVSG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  86 SYHLAEsyspVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPessGKRWATEREYAFRQLVAEEKYRGVVYQG-LETAP 164
Cdd:cd01543    80 SRPEPG----FPRVTTDNEAIGRMAAEHLLERGFRHFAFCGFR---NAAWSRERGEGFREALREAGYECHVYESpPSGSS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 165 ENWQHAQNRLADWLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSRVALSSVAQGARQMGY 244
Cdd:cd01543   153 RSWEEEREELADWLKSLPKPVGIFACNDDRARQVLEACREAGIRVPEEVAVLGVDNDELICELSSPPLSSIALDAEQIGY 232
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1123192800 245 QAAKLLHRLLDKEEMPLQRILVPPVRVIERRST 277
Cdd:cd01543   233 EAAELLDRLMRGERVPPEPILIPPLGVVTRQST 265
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
113-277 8.50e-40

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: 139.01  E-value: 8.50e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 113 HLKEKGVNRFAFYGLPESSGKRWATEREYAFRQLVAEEKYRGVVYQGLETAPENWQHAQNRLaDWLQTLPpqTGIIAVTD 192
Cdd:pfam13377   1 HLAELGHRRIALIGPEGDRDDPYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARERL-RWLGALP--TAVFVAND 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 193 ARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSRvALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQRILVPPvRVI 272
Cdd:pfam13377  78 EVALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSP-PLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPP-ELV 155

                  ....*
gi 1123192800 273 ERRST 277
Cdd:pfam13377 156 EREST 160
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
21-268 3.77e-31

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: 119.16  E-value: 3.77e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  21 QVVEGVGEYlqASQSEWDIFI------EEDFRARIDKIKDWLGDGVI---ADFDDKQIEQaLADVDVPIVGVGGSYHlae 91
Cdd:cd06267    16 ELLRGIEDA--ARERGYSLLLcntdedPEREREYLRLLLSRRVDGIIlapSSLDDELLEE-LLAAGIPVVLIDRRLD--- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  92 sYSPVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSgkRWATEREYAFRQLVAE---EKYRGVVYQGletaPENWQ 168
Cdd:cd06267    90 -GLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDL--STSRERLEGYRDALAEaglPVDPELVVEG----DFSEE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 169 HAQNRLADWLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSrVALSSVAQGARQMGYQAAK 248
Cdd:cd06267   163 SGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLT-PPLTTVRQPAYEMGRAAAE 241
                         250       260
                  ....*....|....*....|
gi 1123192800 249 LLHRLLDKEEMPLQRILVPP 268
Cdd:cd06267   242 LLLERIEGEEEPPRRIVLPT 261
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
21-277 1.31e-30

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 119.53  E-value: 1.31e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  21 QVVEGVGEYLQA-------SQSEWDIFIEEDFrarIDKIKDWLGDGVI---ADFDDKQIEqALADVDVPIVGVGGSYHLA 90
Cdd:COG1609    78 ELLRGIEEAARErgyqlllANSDEDPEREREA---LRLLLSRRVDGLIlagSRLDDARLE-RLAEAGIPVVLIDRPLPDP 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  91 EsyspVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSgkRWATEREYAFRQLVAEekyRGVVYQGLETAPENW--Q 168
Cdd:COG1609   154 G----VPSVGVDNRAGARLATEHLIELGHRRIAFIGGPADS--SSARERLAGYREALAE---AGLPPDPELVVEGDFsaE 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 169 HAQNRLADWLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSrVALSSVAQGARQMGYQAAK 248
Cdd:COG1609   225 SGYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLT-PPLTTVRQPIEEMGRRAAE 303
                         250       260
                  ....*....|....*....|....*....
gi 1123192800 249 LLHRLLDKEEMPLQRILVPPvRVIERRST 277
Cdd:COG1609   304 LLLDRIEGPDAPPERVLLPP-ELVVREST 331
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
301-384 1.13e-27

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 104.56  E-value: 1.13e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  301 GIKVDQVLDAVGISRSNLEKRFKEEVGETIHAMIHAEKLEKARSLLISTTLSINEISQMCGYPSLQYFYSVFKKAYDTTP 380
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80

                   ....
gi 1123192800  381 KEYR 384
Cdd:smart00342  81 SEYR 84
PBP1_AglR_RafR-like cd06292
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ...
17-277 2.79e-22

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: 95.41  E-value: 2.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  17 AYDRQVVEGVGEylQASQSEWD--IFIEEDFRARIDKIKDWLG----DGVI---ADFDDKQIeQALADVDVPIVGVGGsy 87
Cdd:cd06292    16 PFFDEFLAALGH--AAAARGYDvlLFTASGDEDEIDYYRDLVRsrrvDGFVlasTRHDDPRV-RYLHEAGVPFVAFGR-- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  88 hlAESYSPVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSgkRWATEREYAFRQLVAEEKY---RGVVYQGLETAP 164
Cdd:cd06292    91 --ANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPEGS--VPSDDRLAGYRAALEEAGLpfdPGLVVEGENTEE 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 165 ENWQHAQNRLAdwlQTLPPqTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSrVALSSVAQGARQMGY 244
Cdd:cd06292   167 GGYAAAARLLD---LGPPP-TAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTH-PPLTTVRQPIDEIGR 241
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1123192800 245 QAAKLLHRLLDKEEMPLQRILVPPvRVIERRST 277
Cdd:cd06292   242 AVVDLLLAAIEGNPSEPREILLQP-ELVVRESS 273
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
262-384 9.24e-22

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: 94.84  E-value: 9.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 262 QRILVPPVR------VIERRstDYRSLTDPAVIQAMHYIRNHACKGIKVDQVLDAVGISRSNLEKRFKEEVGETIHAMIH 335
Cdd:COG4977   183 RRLVVDPRRpggqaqFSPLL--VPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQ 260
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1123192800 336 AEKLEKARSLLISTTLSINEISQMCGYPSLQYFYSVFKKAYDTTPKEYR 384
Cdd:COG4977   261 RLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYR 309
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
249-384 1.75e-21

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 92.92  E-value: 1.75e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 249 LLHRLLDKEEMPLQRILVPPVRVIERRSTDYRSLTDPAVIQAMHYIRNHACKGIKVDQVLDAVGISRSNLEKRFKEEVGE 328
Cdd:COG2207   116 LLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGT 195
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1123192800 329 TIHAMIHAEKLEKARSLLISTTLSINEISQMCGYPSLQYFYSVFKKAYDTTPKEYR 384
Cdd:COG2207   196 SPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYR 251
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
58-276 3.25e-21

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: 92.20  E-value: 3.25e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  58 DGVI--ADFDDkqiEQALADVDVPIVGVGgsYHLAESyspVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSGKrw 135
Cdd:cd06291    57 DGIIlgSHSLD---IEEYKKLNIPIVSID--RYLSEG---IPSVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSP-- 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 136 ATEREYAFRQLVAEEKYRGVVYQGLETAPeNWQHAQNRLADWLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKLCV 215
Cdd:cd06291   127 ANERYRGFEDALKEAGIEYEIIEIDENDF-SEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQI 205
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1123192800 216 IGIDNEELTRYlSRVALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQRILVpPVRVIERRS 276
Cdd:cd06291   206 IGFDGIEISEL-LYPELTTIRQPIEEMAKEAVELLLKLIEGEEIEESRIVL-PVELIERET 264
PBP1_MalR-like cd06294
ligand-binding domain of maltose transcription regulator MalR which is a member of the ...
21-267 1.47e-20

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: 90.34  E-value: 1.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  21 QVVEGVGEYLQASQSEWDIFIEEDFRARIDKIKDWLG----DGVI---ADFDDkQIEQALADVDVPIVGVGGSYHLAESY 93
Cdd:cd06294    21 EVLRGISQVANENGYSLLLATGNTEEELLEEVKRMVRgrrvDGFIllySKEDD-PLIEYLKEEGFPFVVIGKPLDDNDVL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  94 spvhYIATDNYALVESAFLHLKEKGVNRFAFYGlpESSGKRWATEREYAFRQLVAEEKYRgVVYQGLETAPENWQHAQNR 173
Cdd:cd06294   100 ----YVDNDNVQAGYEATEYLIDKGHKRIAFIG--GDKNLVVSIDRLQGYKQALKEAGLP-LDDDYILLLDFSEEDGYDA 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 174 LADWLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRyLSRVALSSVAQGARQMGYQAAKLLHRL 253
Cdd:cd06294   173 LQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAE-LASPPLTSVDINPYELGREAAKLLINL 251
                         250
                  ....*....|....
gi 1123192800 254 LDKEEMPLQRILVP 267
Cdd:cd06294   252 LEGPESLPKNVIVP 265
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
7-277 5.45e-20

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


Pssm-ID: 380508 [Multi-domain]  Cd Length: 269  Bit Score: 88.82  E-value: 5.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800   7 RITLLFNAnkaydrQVVEGVGEYlqASQSEWDIFI---EEDFRARIDKIKDWLG---DGVI--ADFDDKQIEQALADVDV 78
Cdd:cd06285     8 DLSNPFYA------ELVEGIEDA--ARERGYTVLLadtGDDPERELAALDSLLSrrvDGLIitPARDDAPDLQELAARGV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  79 PIVGVggSYHLAESysPVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPESsgkrWAT--EREYAFRQLVAEekyRGVV 156
Cdd:cd06285    80 PVVLV--DRRIGDT--ALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPLN----ASTgrDRLRGYRRALAE---AGLP 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 157 YQGLETAPENW-----QHAQNRLadwLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSrVA 231
Cdd:cd06285   149 VPDERIVPGGFtieagREAAYRL---LSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLP-PP 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1123192800 232 LSSVAQGARQMGYQAAKLLHRLLDKEEMPLQRILVPPvRVIERRST 277
Cdd:cd06285   225 LTTVRQPKYEMGRRAAELLLQLIEGGGRPPRSITLPP-ELVVREST 269
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
58-272 4.15e-19

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: 86.08  E-value: 4.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  58 DGVI---ADFDDKQIEQALADVDVPIVGVggSYHLAESysPVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSGKR 134
Cdd:cd06289    57 DGLIlspAAGTTAELLRRLKAWGIPVVLA--LRDVPGS--DLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSSTR 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 135 waTEREYAFRQLVAEEKYRGVVYQGLETAPENWQHAQ--NRLadwLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEK 212
Cdd:cd06289   133 --RERLAGFRAALAEAGLPLDESLIVPGPATREAGAEaaREL---LDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRD 207
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 213 LCVIGIDNEELTRyLSRVALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQRILVPPVRVI 272
Cdd:cd06289   208 IAVVGFDDVPEAA-LWTPPLTTVSVHPREIGRRAARLLLRRIEGPDTPPERIIIEPRLVV 266
HTH_18 pfam12833
Helix-turn-helix domain;
309-384 6.94e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 80.33  E-value: 6.94e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1123192800 309 DAVGISRSNLEKRFKEEVGETIHAMIHAEKLEKARSLLISTT-LSINEISQMCGYPSLQYFYSVFKKAYDTTPKEYR 384
Cdd:pfam12833   3 AALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDTgLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYR 79
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
283-384 8.78e-19

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: 86.65  E-value: 8.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 283 TDPAVIQAMHYIRNHACKGIKVDQVLDAVGISRSNLEKRFKEEVGETIHAMIHAEKLEKARSLLiSTTLSINEISQMCGY 362
Cdd:COG2169    82 RADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL-QTGLSVTDAAYAAGF 160
                          90       100
                  ....*....|....*....|..
gi 1123192800 363 PSLQYFYSVFKKAYDTTPKEYR 384
Cdd:COG2169   161 GSLSRFYEAFKKLLGMTPSAYR 182
PBP1_GalR cd01544
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ...
58-276 1.43e-18

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: 84.50  E-value: 1.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  58 DGVIA--DFDDKQIEQaLADVDVPIVGVGgSYHLAESYSpvhYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSGKRW 135
Cdd:cd01544    55 DGIIAigKFSKEEIEK-LKKLNPNIVFVD-SNPDPDGFD---SVVPDFEQAVRQALDYLIELGHRRIGFIGGKEYTSDDG 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 136 ATE---REYAFRQLVAE--EKYRGVVYQGLETAPENWQHAQNrladWLQTLPPQTGIIAVTDARARHILQVCEHLHIPVP 210
Cdd:cd01544   130 EEIedpRLRAFREYMKEkgLYNEEYIYIGEFSVESGYEAMKE----LLKEGDLPTAFFVASDPMAIGALRALQEAGIKVP 205
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1123192800 211 EKLCVIGIDNEELTRYLSRvALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQRILVPPvRVIERRS 276
Cdd:cd01544   206 EDISIISFNDIEVAKYVTP-PLTTVHIPTEEMGRTAVRLLLERINGGRTIPKKVLLPT-KLIERES 269
PBP1_RegR_EndR_KdgR-like cd06283
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ...
58-274 1.47e-18

ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR; Ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR, all of which are members of the LacI-GalR family of bacterial transcription regulators. RegR regulates bacterial competence and the expression of virulence factors, including hyaluronidase. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380506 [Multi-domain]  Cd Length: 266  Bit Score: 84.52  E-value: 1.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  58 DGVI----ADFDDKQIEqaLADVDVPIVgvggsyhLAESYSP---VHYIATDNYALVESAFLHLKEKGVNRFAFYGLP-E 129
Cdd:cd06283    57 DGLIlqptGNNNDAYLE--LAQKGLPVV-------LVDRQIEplnWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPiK 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 130 SSGKRwaTEREYAFRQLVAEekyRGVVYQGLETAPENWQHAQNRLADWLQTLPPQ-TGIIAVTDARARHILQVCEHLHIP 208
Cdd:cd06283   128 GISTR--RERLQGFLDALAR---YNIEGDVYVIEIEDTEDLQQALAAFLSQHDGGkTAIFAANGVVLLRVLRALKALGIR 202
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1123192800 209 VPEKLCVIGIDNEELTRyLSRVALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQRILVpPVRVIER 274
Cdd:cd06283   203 IPDDVGLCGFDDWDWAD-LIGPGITTIRQPTYEIGKAAAEILLERIEGDSGEPKEIEL-PSELIIR 266
PBP1_sucrose_transcription_regulator cd06288
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ...
22-276 3.93e-17

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: 80.67  E-value: 3.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  22 VVEGVGEYlqASQSEWDIFIEE--DFRARIDK-IKDWLG---DGVI-ADFDDKQIEQALADVDVPIVgvggsyhLAESYS 94
Cdd:cd06288    18 IIRGAQDA--AEEHGYLLLLANtgGDPELEAEaIRELLSrrvDGIIyASMHHREVTLPPELTDIPLV-------LLNCFD 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  95 P---VHYIATDN----YALVEsaflHLKEKGVNRFAFYGLPESSgkRWATEREYAFRQLVAEekyRGVVYQGLETAPENW 167
Cdd:cd06288    89 DdpsLPSVVPDDeqggYLATR----HLIEAGHRRIAFIGGPEDS--LATRLRLAGYRAALAE---AGIPYDPSLVVHGDW 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 168 QHAQNRLA--DWLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLsRVALSSVAQGARQMGYQ 245
Cdd:cd06288   160 GRESGYEAakRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYL-RPPLTTVALPYYEMGRR 238
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1123192800 246 AAKLLHRLLDKEEMPLQRILVpPVRVIERRS 276
Cdd:cd06288   239 AAELLLDGIEGEPPEPGVIRV-PCPLIERES 268
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
21-276 5.11e-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: 80.28  E-value: 5.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  21 QVVEGVGEYlqASQSEWDIFI------EEDFRARIDKIKDWLGDGVI---ADFDDKQIEQAlaDVDVPIVgvggsyhLAE 91
Cdd:cd06284    16 EILRGIEDA--AAEAGYDVLLgdtdsdPEREDDLLDMLRSRRVDGVIllsGRLDAELLSEL--SKRYPIV-------QCC 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  92 SYSP---VHYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSgkRWATEREYAFRQlvAEEKYrgvvyqGLEtAPENWQ 168
Cdd:cd06284    85 EYIPdsgVPSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDN--VYARERLEGYRR--ALAEA------GLP-VDEDLI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 169 H--------AQNRLADWLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSrVALSSVAQGAR 240
Cdd:cd06284   154 IegdfsfeaGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFS-PSLTTIRQPRY 232
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1123192800 241 QMGYQAAKLLHRLLDKEEMPLQRILVpPVRVIERRS 276
Cdd:cd06284   233 EIGETAAELLLEKIEGEGVPPEHIIL-PHELIVRES 267
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
71-276 7.65e-16

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: 76.93  E-value: 7.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  71 QALADVDVPIVGVGGSYHLAESYSpvhyIATDNyalVESAFL---HLKEKGVNRFAFYGLPESSgkRWATEREYAFRQLV 147
Cdd:cd06293    72 ARLRARGTAVVLLDRPAPGPAGCS----VSVDD---VQGGALavdHLLELGHRRIAFVSGPLRT--RQVAERLAGARAAV 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 148 AEekyRGVVYQGL---ETAPENWQHAQNRLADWLQTLPPQ-TGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEEL 223
Cdd:cd06293   143 AE---AGLDPDEVvreLSAPDANAELGRAAAAQLLAMPPRpTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPF 219
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1123192800 224 TRYLSrVALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQRILVPPvRVIERRS 276
Cdd:cd06293   220 AAAAN-PPLTTVRQPSYELGRAAADLLLDEIEGPGHPHEHVVFQP-ELVVRSS 270
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
58-276 6.37e-15

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


Pssm-ID: 380501 [Multi-domain]  Cd Length: 266  Bit Score: 74.11  E-value: 6.37e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  58 DGVI--ADFDDKQIEQALADVDVPIVGVGGSYHLAesysPVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSgkrW 135
Cdd:cd06278    56 DGVIvtSATLSSELAEECARRGIPVVLFNRVVEDP----GVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPEGT---S 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 136 AT-EREYAFRQLVAEekyRGVVYQGLETAPENWQHAQNRLADWLQTLPPQTGIIAVTDARARHILQVC-EHLHIPVPEKL 213
Cdd:cd06278   129 TSrERERGFRAALAE---LGLPPPAVEAGDYSYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAArQEGGLVVPEDI 205
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1123192800 214 CVIGIDNEELTRYLSrVALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQRILVpPVRVIERRS 276
Cdd:cd06278   206 SVVGFDDIPMAAWPS-YDLTTVRQPIEEMAEAAVDLLLERIENPETPPERRVL-PGELVERGS 266
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
246-390 6.55e-15

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 74.62  E-value: 6.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 246 AAKLLHRLLDKEeMPLQRILVPPVRvierrstdyrsltDPAVIQAMHYIRNHACKGIKVDQVLDAVGISRSNLEKRFKEE 325
Cdd:PRK10572  158 AMNLLERLLLRC-MEAIPESLHPPM-------------DPRVREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQ 223
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1123192800 326 VGETIHAMIHAEKLEKARSLLISTTLSINEISQMCGYPSLQYFYSVFKKAYDTTPKEYRDVNSEV 390
Cdd:PRK10572  224 LGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSEFRARCEEK 288
PBP1_LacI-like cd06273
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
58-276 9.11e-15

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


Pssm-ID: 380497 [Multi-domain]  Cd Length: 268  Bit Score: 73.70  E-value: 9.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  58 DGVI---ADFDDKqIEQALADVDVPIVgVGGSYhlaESYSPVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSGKR 134
Cdd:cd06273    57 DGLIlvgSDHDPE-LFELLEQRQVPYV-LTWSY---DEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGNDR 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 135 wATEREYAFRQLVAEekyrgvvyQGLETAPE-------NWQHAQNRLADWLQTLPPQTGIIAVTDARARHILQVCEHLHI 207
Cdd:cd06273   132 -ARARLAGIRDALAE--------RGLELPEErvveapySIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGI 202
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1123192800 208 PVPEKLCVIGIDNEELTRYLSrVALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQRILvpPVRVIERRS 276
Cdd:cd06273   203 SVPEDLSITGFDDLELAAHLS-PPLTTVRVPAREIGELAARYLLALLEGGPPPKSVEL--ETELIVRES 268
PBP1_DegA_Like cd19976
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
21-276 9.82e-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: 73.44  E-value: 9.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  21 QVVEGVGEYLQasQSEWDIFI---EEDFRAR---IDKIKDWLGDGVI---ADFDDKQIEQALADVDVPIVgvggsyhLAE 91
Cdd:cd19976    16 ELVRGIEDTLN--ELGYNIILcntYNDFEREkkyIQELKERNVDGIIiasSNISDEAIIKLLKEEKIPVV-------VLD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  92 SYSPVH---YIATDNYalvESAFL---HLKEKGVNRFAFYGLPESSGKrwATEREYAFRQLVAEEK---YRGVVYQGLET 162
Cdd:cd19976    87 RYIEDNdsdSVGVDDY---RGGYEatkYLIELGHTRIGCIVGPPSTYN--EHERIEGYKNALQDHNlpiDESWIYSGESS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 163 APENWQHAQnrlaDWLQTLPPqTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSRvALSSVAQGARQM 242
Cdd:cd19976   162 LEGGYKAAE----ELLKSKNP-TAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITP-ALTTIAQPIFEM 235
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1123192800 243 GYQAAKLLHRLLDKEEMPLQRILVPPvRVIERRS 276
Cdd:cd19976   236 GQEAAKLLLKIIKNPAKKKEEIVLPP-ELIKRDS 268
PBP1_CatR-like cd06296
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ...
7-277 1.15e-14

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: 73.46  E-value: 1.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800   7 RITLLFNA-NKAYDRQVVEGVGEYLQASqsEWDIFIEEDfRARIDKIKDWLG-------DGVIA---DFDDKQIEqALAD 75
Cdd:cd06296     1 LIDLVLPQlDSPYALEVLRGVERAAAAA--GLDLVVTAT-RAGRAPVDDWVRravargsAGVVLvtsDPTSRQLR-LLRS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  76 VDVPIVGVGGsyhLAESYSPVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSgkRWATEREYAFRQLVAEekyrgv 155
Cdd:cd06296    77 AGIPFVLIDP---VGEPDPDLPSVGATNWAGGRLATEHLLDLGHRRIAVITGPPRS--VSGRARLAGYRAALAE------ 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 156 vyQGLETAPE-----NWQHAQN-RLADWLQTLP-PQTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLS 228
Cdd:cd06296   146 --AGIAVDPDlvregDFTYEAGyRAARELLELPdPPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTS 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1123192800 229 rVALSSVAQGARQMGYQAAKLLHRLLDKeEMPLQRILVPPVRVIERRST 277
Cdd:cd06296   224 -PPLTTVHQPLREMGAVAVRLLLRLLEG-GPPDARRIELATELVVRGST 270
PBP1_CcpA-like cd19975
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
21-276 1.46e-14

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: 72.97  E-value: 1.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  21 QVVEGVGEylQASQSEWDIFI---EEDFrariDKIKDWLG-------DGVI--ADFDDKQIEQALADVDVPIVGVggSYH 88
Cdd:cd19975    16 EILKGIED--EARENGYSVILcntGSDE----EREKKYLQllkekrvDGIIfaSGTLTEENKQLLKNMNIPVVLV--STE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  89 LAESYSPvhYIATDNYALVESAFLHLKEKGVNRFAFYGLP---ESSGkrwaTEREYAFRQLVAEekyrgvvyQGLeTAPE 165
Cdd:cd19975    88 SEDPDIP--SVKIDDYQAAYDATNYLIKKGHRKIAMISGPlddPNAG----YPRYEGYKKALKD--------AGL-PIKE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 166 NW-----------QHAQNRLadwLQTLPPQTGIIAVTDARARHILQvCEHLH-IPVPEKLCVIGIDNEELTRYlSRVALS 233
Cdd:cd19975   153 NLivegdfsfksgYQAMKRL---LKNKKLPTAVFAASDEMALGVIS-AAYDHgIRVPEDISVIGFDNTEIAEM-SIPPLT 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1123192800 234 SVAQGARQMGYQAAKLLHRLLDKEEMPLQRILVpPVRVIERRS 276
Cdd:cd19975   228 TVSQPFYEMGKKAVELLLDLIKNEKKEEKSIVL-PHQIIERES 269
PBP1_LacI-like cd06279
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ...
58-276 1.61e-14

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: 73.40  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  58 DGVIA--DFDDKQIEQALADVDVPIVGVGGsyhlaESYSPVHYIATDNYALVESAFLHLKEKGVNRFAFYGLP---ESSG 132
Cdd:cd06279    58 DGFIVygLSDDDPAVAALRRRGLPLVVVDG-----PAPPGIPSVGIDDRAAARAAARHLLDLGHRRIAILSLRldrGRER 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 133 KRWATEREYAFRQLVAEEKYRGVVyQGLETA------------PENWQHAQNRLADWLQTLPPQ-TGIIAVTDARARHIL 199
Cdd:cd06279   133 GPVSAERLAAATNSVARERLAGYR-DALEEAgldlddvpvveaPGNTEEAGRAAARALLALDPRpTAILCMSDVLALGAL 211
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1123192800 200 QVCEHLHIPVPEKLCVIGIDNEELTRyLSRVALSSVAQGARQMGYQAAKLLHRLLDKEEmPLQRILvpPVRVIERRS 276
Cdd:cd06279   212 RAARERGLRVPEDLSVTGFDDIPEAA-AADPGLTTVRQPAVEKGRAAARLLLGLLPGAP-PRPVIL--PTELVVRAS 284
PBP1_LacI cd01574
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ...
42-276 3.09e-14

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: 72.23  E-value: 3.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  42 EEDFRARIDKIKDWLGDGVIADFDDKQIEQALADV--DVPIVGVGGSYHlaesySPVHYIATDNYALVESAFLHLKEKGV 119
Cdd:cd01574    42 PASVREALDRLLSQRVDGIIVIAPDEAVLEALRRLppGLPVVIVGSGPS-----PGVPTVSIDQEEGARLATRHLLELGH 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 120 NRFAFYGLPESSGKrwATEREYAFRQLVAEekyRGVVYQglETAPENWQ-----HAQNRLADwlqtLPPQTGIIAVTDAR 194
Cdd:cd01574   117 RRIAHIAGPLDWVD--ARARLRGWREALEE---AGLPPP--PVVEGDWSaasgyRAGRRLLD----DGPVTAVFAANDQM 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 195 ARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSrVALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQRILVPPvRVIER 274
Cdd:cd01574   186 ALGALRALHERGLRVPEDVSVVGFDDIPEAAYFV-PPLTTVRQDFAELGRRAVELLLALIEGPAPPPESVLLPP-ELVVR 263

                  ..
gi 1123192800 275 RS 276
Cdd:cd01574   264 ES 265
adjacent_YSIRK TIGR04094
YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only ...
228-384 3.42e-14

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: 73.17  E-value: 3.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 228 SRVALSSVAQGARQMGYQAAKLLH---RLLDKEEMPLQRILVPPVR---------VIERRSTDYRSLTDPAVIQamhYIR 295
Cdd:TIGR04094 219 SIIIFEKLSQLAIQMGVDIVDAYRlrdYYIQEIEEQTSLMDVLKLRdsaiiyfteLLHEISINHHSPLIRAVIQ---YIN 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 296 NHACKGIKVDQVLDAVGISRSNLEKRFKEEVGETIHAMIHAEKLEKARSLLISTtLSINEISQMCGYPSLQYFYSVFKKA 375
Cdd:TIGR04094 296 LNLYDPLKVEEIAKQFFMSESKLRKLFKKEMGISIQEYISKRKIEEAKYLLRSQ-IPVSEVSNELGFYDLSHFSRTFKKH 374

                  ....*....
gi 1123192800 376 YDTTPKEYR 384
Cdd:TIGR04094 375 TGVSPKQYQ 383
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
95-269 4.28e-14

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: 71.79  E-value: 4.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  95 PVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPE--SSGKrwatEREYAFRQLVAEekyrgvvyQGLEtAPENWQHAQN 172
Cdd:cd19977    92 DVDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLelSTRQ----ERLEGYKAALAD--------HGLP-VDEELIKHVD 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 173 RLAD-------WLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLsRVALSSVAQGARQMGYQ 245
Cdd:cd19977   159 RQDDvrkaiseLLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLF-NPPLTVIAQPTYEIGRK 237
                         170       180
                  ....*....|....*....|....*
gi 1123192800 246 AAKLL-HRLLDKEEMPLQRILVPPV 269
Cdd:cd19977   238 AAELLlDRIENKPKGPPRQIVLPTE 262
PBP1_LacI-like cd06290
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
22-276 8.33e-13

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


Pssm-ID: 380513 [Multi-domain]  Cd Length: 267  Bit Score: 68.03  E-value: 8.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  22 VVEGVGEYLQASQ-------SEWDIFIEEDfraRIDKIKDWLGDGVI---ADFDDKQIEqaLADVDVPIVGVGGSYHLAE 91
Cdd:cd06290    17 ILNGIEEVLAESGytlivstSHWNADRELE---ILRLLLARKVDGIIvvgGFGDEELLK--LLAEGIPVVLVDRELEGLN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  92 syspVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSgkRWATEREYAFRQlVAEEKyrgvvyqGLETAPE------ 165
Cdd:cd06290    92 ----LPVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDH--PDAQERYAGYRR-ALEDA-------GLEVDPRlivegd 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 166 -NWQHAQNRLADWLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLsRVALSSVAQGARQMGY 244
Cdd:cd06290   158 fTEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYT-TPPLTTVRQPLYEMGK 236
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1123192800 245 QAAKLLHRLLDKEEMPlQRILVPPVRVIERRS 276
Cdd:cd06290   237 TAAEILLELIEGKGRP-PRRIILPTELVIRES 267
PBP1_PurR cd06275
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ...
113-276 1.41e-12

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: 67.28  E-value: 1.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 113 HLKEKGVNRFAFYGLPEssGKRWATEREYAFRQLVAEEKYRG----VVYQGLEtaPENWQHAQNRLadwLQTLPPQTGII 188
Cdd:cd06275   111 HLIELGHRRIGCITGPL--EHSVSRERLAGFRRALAEAGIEVppswIVEGDFE--PEGGYEAMQRL---LSQPPRPTAVF 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 189 AVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSRvALSSVAQGARQMGYQAA-KLLHRLLDKEEmPLQRILVP 267
Cdd:cd06275   184 ACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSP-ALTTIHQPKDELGELAVeLLLDRIENKRE-EPQSIVLE 261

                  ....*....
gi 1123192800 268 PvRVIERRS 276
Cdd:cd06275   262 P-ELIERES 269
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
104-276 2.99e-12

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: 66.36  E-value: 2.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 104 YALVEsaflHLKEKGVNRFAFYGLPESSGKRwATEREYAFRQlVAEEKYRGVVYQGLETAPENWQHAQNRLADWLQTLPP 183
Cdd:cd01575   105 RAMAR----HLIERGYRRIAFVGARLDGDSR-ARQRLEGFRD-ALAEAGLPLPLVLLVELPSSFALGREALAELLARHPD 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 184 QTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSrVALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQR 263
Cdd:cd01575   179 LDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALP-PALTTVRVPRYEIGRKAAELLLARLEGEEPEPRV 257
                         170
                  ....*....|...
gi 1123192800 264 ILVPPvRVIERRS 276
Cdd:cd01575   258 VDLGF-ELVRRES 269
PBP1_SalR cd01545
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ...
65-276 5.37e-12

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: 65.65  E-value: 5.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  65 DDKQIEQALADVDVPIVGVGGsyhlAESYSPVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSGKrwATEREYAFR 144
Cdd:cd01545    68 DDPALLDALDELGIPYVRIAP----GTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGPPDHGA--SAERLEGFR 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 145 QLVAE---EKYRGVVYQGLETapenWQHAQNRLADWLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNE 221
Cdd:cd01545   142 DALAEaglPLDPDLVVQGDFT----FESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDS 217
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1123192800 222 ELTRYLSRvALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQRILVPPvRVIERRS 276
Cdd:cd01545   218 PIARLVWP-PLTTVRQPIAEMARRAVELLIAAIRGAPAGPERETLPH-ELVIRES 270
PBP1_GalS-like cd06270
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ...
58-274 1.10e-11

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: 64.46  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  58 DGVI--ADFDDKQIEQALADVDVPIVGVGgsYHLAESysPVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPESsgKRW 135
Cdd:cd06270    57 DAIIlhSRALSDEELILIAEKIPPLVVIN--RYIPGL--ADRCVWLDNEQGGRLAAEHLLDLGHRRIACITGPLD--IPD 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 136 ATEREYAFRQLVAEekyrgvvyQGLETAPE-----NWQHAQNRLAdwLQTL----PPQTGIIAVTDARARHILQVCEHLH 206
Cdd:cd06270   131 ARERLAGYRDALAE--------AGIPLDPSliiegDFTIEGGYAA--AKQLlargLPFTALFAYNDDMAIGALAALHEAG 200
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1123192800 207 IPVPEKLCVIGIDNEELTRYLSrVALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQRILVPpvRVIER 274
Cdd:cd06270   201 IKVPEDVSVIGFDDVPLARYLS-PKLTTVHYPIEEMAQAAAELALNLAYGEPLPISHEFTP--TLIER 265
PBP1_CcpB-like cd06286
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ...
95-274 1.17e-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: 64.49  E-value: 1.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  95 PVHYIATDNYALVESAFLHLKEKGVNRFAF-YGLPESSGkRWATEREYAFRQLVAEEKyrgvvyqglETAPENWQ--HAQ 171
Cdd:cd06286    90 DIPSVYIDRYEAYLEALEYLKEKGHRKIGYcLGRPESSS-ASTQARLKAYQDVLGEHG---------LSLREEWIftNCH 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 172 N-----RLADWLQTLPPQ-TGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLsrvALSSVAQGARQMGYQ 245
Cdd:cd06286   160 TiedgyKLAKKLLALKERpDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISELL---NLTTIDQPLEEMGKE 236
                         170       180
                  ....*....|....*....|....*....
gi 1123192800 246 AAKLLHRLLDKEEmplQRILVPPVRVIER 274
Cdd:cd06286   237 AFELLLSQLESKE---PTKKELPSKLIER 262
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
69-258 1.47e-11

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: 64.25  E-value: 1.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  69 IEQALADvDVPIVGVGgsyHLAESYSPVHYIATDNYA----LVESAFLHLKEKGvNRFAFYGLPESSGkrwATEREYAFR 144
Cdd:pfam13407  73 LKKAKDA-GIPVVTFD---SDAPSSPRLAYVGFDNEAageaAGELLAEALGGKG-KVAILSGSPGDPN---ANERIDGFK 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 145 QlVAEEKYRGVVYQGlETAPENW--QHAQNRLADWLQTLPPQT-GIIAVTDARARHILQVCEHLHIPvpEKLCVIGIDNE 221
Cdd:pfam13407 145 K-VLKEKYPGIKVVA-EVEGTNWdpEKAQQQMEALLTAYPNPLdGIISPNDGMAGGAAQALEAAGLA--GKVVVTGFDAT 220
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1123192800 222 ELTRYL--SRVALSSVAQGARQMGYQAAKLLHRLLDKEE 258
Cdd:pfam13407 221 PEALEAikDGTIDATVLQDPYGQGYAAVELAAALLKGKK 259
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
58-265 4.26e-11

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: 62.90  E-value: 4.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  58 DGVI--ADFDDKQIEQALADVDVPIVGVGgsyhlaESYSPVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPEssgKRW 135
Cdd:cd01542    57 DGIIlfATEITDEHRKALKKLKIPVVVLG------QEHEGFSCVYHDDYGAGKLLGEYLLKKGHKNIAYIGVDE---EDI 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 136 AT--EREYAFRQLVAEEKYRGVVYQgleTAPENWQHAQNRLADWLQTLPPqTGIIAVTDARARHILQVCEHLHIPVPEKL 213
Cdd:cd01542   128 AVgvARKQGYLDALKEHGIDEVEIV---ETDFSMESGYEAAKELLKENKP-DAIICATDNIALGAIKALRELGIKIPEDI 203
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1123192800 214 CVIGIDNEELTRYLSRvALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQRIL 265
Cdd:cd01542   204 SVAGFGGYDLSEFVSP-SLTTVKFDYEEAGEKAAELLLDMIEGEKVPKKQKL 254
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
60-271 8.55e-11

ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH domain [Carbohydrate transport and metabolism];


Pssm-ID: 441483 [Multi-domain]  Cd Length: 307  Bit Score: 62.25  E-value: 8.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  60 VIADFDDKQIEQAL---ADVDVPIVGVGGSyhlAESYSPVHYIATDNYA----LVESAFLHLKEKGvNRFAFYGLPESSg 132
Cdd:COG1879    94 IVSPVDPDALAPALkkaKAAGIPVVTVDSD---VDGSDRVAYVGSDNYAagrlAAEYLAKALGGKG-KVAILTGSPGAP- 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 133 krWATEREYAFRQLVAEekYRGVVYQGLETAPENWQHAQNRLADWLQTLPPQTGIIAVTDARARHILQVCEHLHIPvpEK 212
Cdd:COG1879   169 --AANERTDGFKEALKE--YPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRK--GD 242
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1123192800 213 LCVIGID-NEELTRYL-SRVALSSVAQGARQMGYQAAKLLHRLLDKEEMPlQRILVPPVRV 271
Cdd:COG1879   243 VKVVGFDgSPEALQAIkDGTIDATVAQDPYLQGYLAVDAALKLLKGKEVP-KEILTPPVLV 302
ftrA PRK09393
transcriptional activator FtrA; Provisional
262-384 1.31e-10

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 61.90  E-value: 1.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 262 QRILVPPVR-----------VIERRSTDYRSLtdpaviqaMHYIRNHACKGIKVDQVLDAVGISRSNLEKRFKEEVGETI 330
Cdd:PRK09393  192 RRLVVPPHRdggqaqfvprpVASRESDRLGPL--------IDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTP 263
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1123192800 331 HAMIHAEKLEKARSLLISTTLSINEISQMCGYPSLQYFYSVFKKAYDTTPKEYR 384
Cdd:PRK09393  264 AEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYR 317
PBP1_CcpA_TTHA0807 cd06297
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ...
8-276 1.38e-10

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


Pssm-ID: 380520 [Multi-domain]  Cd Length: 268  Bit Score: 61.33  E-value: 1.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800   8 ITLLFNANKAYDRqVVEGVGEYLQASQSEWDIFIEEDfRARIDKIKD-----WLGDGVI-ADFD-DKQIEQALADVDVPI 80
Cdd:cd06297     4 LLVPEVMTPFYMR-LLTGVERALDENRYDLAIFPLLS-EYRLEKYLRnstlaYQCDGLVmASLDlTELFEEVIVPTEKPV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  81 VgvggsyhLAESYSP-VHYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSGKRWATEREYAFRQLVAEEKY-RGVVYQ 158
Cdd:cd06297    82 V-------LIDANSMgYDCVYVDNVKGGFMATEYLAGLGEREYVFFGIEEDTVFTETVFREREQGFLEALNKAgRPISSS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 159 GLETAPENWQHAQNRLADWLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTrylSRVALSSVAQG 238
Cdd:cd06297   155 RMFRIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWA---ASPGLTTVRQP 231
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1123192800 239 ARQMGYQAAKLLHRLLDKEEMPLQRILVPPvRVIERRS 276
Cdd:cd06297   232 VEEMGEAAAKLLLKRLNEYGGPPRSLKFEP-ELIVRES 268
PBP1_AglR-like cd20010
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ...
21-271 2.10e-10

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


Pssm-ID: 380665 [Multi-domain]  Cd Length: 269  Bit Score: 60.64  E-value: 2.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  21 QVVEGVGEYLqaSQSEWDIFI-----EEDFRARIDK-IKDWLGDGVIAD---FDDKQIEQaLADVDVPIVgVGGSYHLAE 91
Cdd:cd20010    20 EFLAGLSEAL--AERGLDLLLapapsGEDELATYRRlVERGRVDGFILArtrVNDPRIAY-LLERGIPFV-VHGRSESGA 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  92 SYSpvhYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSGkrWATEREYAFRQLVAEE--KYRGVVYQGLETAPENWQH 169
Cdd:cd20010    96 PYA---WVDIDNEGAFRRATRRLLALGHRRIALLNGPEELN--FAHQRRDGYRAALAEAglPVDPALVREGPLTEEGGYQ 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 170 AQNRLadwLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSRVALSSVAQGARQMGYQAAKL 249
Cdd:cd20010   171 AARRL---LALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLLPALEYFSPPLTTTRSSLRDAGRRLAEM 247
                         250       260
                  ....*....|....*....|..
gi 1123192800 250 LHRLLDKEEMPLQRILVPPVRV 271
Cdd:cd20010   248 LLALIDGEPAAELQELWPPELI 269
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
166-276 5.53e-10

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: 59.49  E-value: 5.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 166 NWQHAQNRLADWLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYlSRVALSSVAQGARQMGYQ 245
Cdd:cd01541   167 EDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASL-SEPPLTSVVHPKEELGRK 245
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1123192800 246 AAKLLHRLLDkEEMPLQRILVPPvRVIERRS 276
Cdd:cd01541   246 AAELLLRMIE-EGRKPESVIFPP-ELIERES 274
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
49-269 1.90e-09

periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.


Pssm-ID: 380478 [Multi-domain]  Cd Length: 268  Bit Score: 57.96  E-value: 1.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  49 IDKIKDWLGDGV----IADFDDKQIEQAL---ADVDVPIVGVGGSyhlAESYSPVH-YIATDNYA--------LVEsafl 112
Cdd:cd01536    45 ISQIEDLIAQGVdaiiIAPVDSEALVPAVkkaNAAGIPVVAVDTD---IDGGGDVVaFVGTDNYEagklageyLAE---- 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 113 HLKEKGvNRFAFYGLPESSgkrWATEREYAFRQlvAEEKYRGVVYqgLETAPENWQ--HAQNRLADWLQTLPPQTGIIAV 190
Cdd:cd01536   118 ALGGKG-KVAILEGPPGSS---TAIDRTKGFKE--ALKKYPDIEI--VAEQPANWDraKALTVTENLLQANPDIDAVFAA 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 191 TDARARHILQVCEHLHIPvpEKLCVIGIDN--EELTRYLSRVALSSVAQGARQMGYQAAKLLHRLLDKEEMPlQRILVPP 268
Cdd:cd01536   190 NDDMALGAAEALKAAGRT--GDIKIVGVDGtpEALKAIKDGELDATVAQDPYLQGYLAVEAAVKLLNGEKVP-KEILTPV 266

                  .
gi 1123192800 269 V 269
Cdd:cd01536   267 T 267
PBP1_LacI-like cd06277
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
39-276 3.39e-09

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


Pssm-ID: 380500 [Multi-domain]  Cd Length: 275  Bit Score: 57.25  E-value: 3.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  39 IFIEEDFRARIDKIKDWLGDGVI---ADFDDKQIEQaLADVDVPIVGVGGSYHlaesYSPVHYIATDNYALVESAFLHLK 115
Cdd:cd06277    44 VDIGDDFDEILKELTDDQSSGIIllgTELEEKQIKL-FQDVSIPVVVVDNYFE----DLNFDCVVIDNEDGAYEAVKYLV 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 116 EKGVNRFafyGLPESSGK-RWATEREYAFRQLVAEekyRGVVYQG-----LETAPENwqhAQNRLADWLQTLPPQ-TGII 188
Cdd:cd06277   119 ELGHTRI---GYLASSYRiKNFEERRRGFRKAMRE---LGLSEDPepefvVSVGPEG---AYKDMKALLDTGPKLpTAFF 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 189 AVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRyLSRVALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQRILVpP 268
Cdd:cd06277   190 AENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSA-MVDPPLTTIHVPKEQMGKLAVRRLIEKIKDPDGGTLKILV-S 267

                  ....*...
gi 1123192800 269 VRVIERRS 276
Cdd:cd06277   268 TKLVERGS 275
PBP1_LacI-like cd06299
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ...
58-276 4.67e-09

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: 56.90  E-value: 4.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  58 DGVIA--DFDDKQIEQALADVDVPIVGVGgsyHLAESYSPVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSGKrw 135
Cdd:cd06299    57 DGIIAvpTGENSEGLQALIAQGLPVVFVD---REVEGLGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYISGPLSTST-- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 136 ATEREYAFR------------QLVAEEKYRGVVyqGLEtapenwqhAQNRLadwLQTLPPQTGIIAVTDARARHILQVCE 203
Cdd:cd06299   132 GRERLAAFRaaltaagipideELVAFGDFRQDS--GAA--------AAHRL---LSRGDPPTALIAGDSLMALGAIQALR 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1123192800 204 HLHIPVPEKLCVIGIDNEELTRYLSRvALSSVAQGARQMGYQAAKLLHRLLDKEEMPlqRILVPPVRVIERRS 276
Cdd:cd06299   199 ELGLRIGDDVSLISFDDVPWFELLSP-PLTVIAQPVERIGRRAVELLLALIENGGRA--TSIRVPTELIPRES 268
PBP1_LacI-like cd19974
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
58-276 5.05e-09

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


Pssm-ID: 380629 [Multi-domain]  Cd Length: 270  Bit Score: 56.79  E-value: 5.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  58 DGVI--ADFDDKQIEQaLADVDVPIVgvggsyhLAESYSPVH---YIATDNYALVESAFLHLKEKGVNRFAFYGLPESSg 132
Cdd:cd19974    60 DGIIilGEISKEYLEK-LKELGIPVV-------LVDHYDEELnadSVLSDNYYGAYKLTSYLIEKGHKKIGFVGDINYT- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 133 kRWATEREYAFRQLVAEekyrgvvyQGLETAPENW----QHAQNRLADWLQtLPPQ----TGIIAVTDARArhiLQVCEH 204
Cdd:cd19974   131 -SSFMDRYLGYRKALLE--------AGLPPEKEEWlledRDDGYGLTEEIE-LPLKlmlpTAFVCANDSIA---IQLIKA 197
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1123192800 205 LH---IPVPEKLCVIGIDNEELTRYLSrVALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQRILVpPVRVIERRS 276
Cdd:cd19974   198 LKekgYRVPEDISVVGFDNIELAELST-PPLTTVEVDKEAMGRRAVEQLLWRIENPDRPFEKILV-SGKLIERDS 270
PBP1_CcpA cd06298
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ...
185-276 9.41e-09

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: 55.76  E-value: 9.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 185 TGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNeelTRY--LSRVALSSVAQGARQMGYQAAKLLHRLLDKEEMpLQ 262
Cdd:cd06298   179 DAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDN---TRYatMSRPQLTSINQPLYDIGAVAMRLLTKLMNKEEV-EE 254
                          90
                  ....*....|....
gi 1123192800 263 RILVPPVRVIERRS 276
Cdd:cd06298   255 TIVKLPHSIIWRQS 268
PBP1_LacI-like cd06287
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
58-276 1.00e-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: 380510 [Multi-domain]  Cd Length: 268  Bit Score: 55.89  E-value: 1.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  58 DGVIA---DFDDKQIEQaLADVDVPIVGVGGSyhlAESYSPVHYIATDNYALVESAFLHLKEKGVNRFAfygLPESSGKR 134
Cdd:cd06287    58 DGAIVvepTVEDPILAR-LRQRGVPVVSIGRA---PGTDEPVPYVDLQSAATARLLLEHLHGAGARQVA---LLTGSSRR 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 135 WA-TEREYAFRQLVAEEKYRGVVYQGLETAPENwqHAQNRLADWLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKL 213
Cdd:cd06287   131 NSsLESEAAYLRFAQEYGTTPVVYKVPESEGER--AGYEAAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPEDL 208
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1123192800 214 CVIgidneelTRY------LSRVALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQRIlvPPVRVIERRS 276
Cdd:cd06287   209 MVV-------TRYdgirarTADPPLTAVDLHLDRVARTAIDLLFASLSGEERSVEVG--PAPELVVRAS 268
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
287-384 1.57e-08

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 52.23  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 287 VIQAM-HYIRNHACKGIKVDQVLDAVGISRSNLEKRFKEEVGETIHAMIHAEKLEKARSLLISTTLSINEISQMCGYPSL 365
Cdd:PRK10219    6 IIQTLiAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYVSQ 85
                          90
                  ....*....|....*....
gi 1123192800 366 QYFYSVFKKAYDTTPKEYR 384
Cdd:PRK10219   86 QTFSRVFRRQFDRTPSDYR 104
PBP1_AglR_RafR-like cd06271
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ...
58-269 1.80e-08

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: 55.12  E-value: 1.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  58 DGVI---ADFDDKQIeQALADVDVPIVGVGGSyHLAESYSpvhYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSGkr 134
Cdd:cd06271    59 DGVIlseIEPNDPRV-QFLTKQNFPFVAHGRS-D*PIGHA---WVDIDNEAGAYEAVERLAGLGHRRIAFIVPPARYS-- 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 135 WATEREYAFRQLVAEEKYRGVVYQGlETAPENWQHAQNRLadwLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKLC 214
Cdd:cd06271   132 PHDRRLQGYVRA*RDAGLTGYPLDA-DTTLEAGRAAAQRL---LALSPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVS 207
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1123192800 215 VIGIDNEELTRYLSRVALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQRILVPPV 269
Cdd:cd06271   208 IIGKDSAPFLGAMITPPLTTVHAPIAEAGRELAKALLARIDGEDPETLQVLVQPS 262
PRK10371 PRK10371
transcriptional regulator MelR;
287-384 3.82e-08

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 54.44  E-value: 3.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 287 VIQAMHYIRNHACKGIKVDQVLDAVGISRSNLEKRFKEEVGETIHAMIHAEKLEKARSLLISTTLSINEISQMCGYPSLQ 366
Cdd:PRK10371  193 VSQMLGFIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSS 272
                          90
                  ....*....|....*...
gi 1123192800 367 YFYSVFKKAYDTTPKEYR 384
Cdd:PRK10371  273 RFYSTFGKYVGMSPQQYR 290
lacI PRK09526
lac repressor; Reviewed
21-277 4.40e-08

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 54.23  E-value: 4.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  21 QVVEGVGEYlqASQSEWDIFI-------EEDFRARIDKIKDWLGDGVIADF-----DDKQIEQALADV-----DVPivgv 83
Cdd:PRK09526   80 QIAAAIKSR--ADQLGYSVVIsmversgVEACQAAVNELLAQRVSGVIINVpledaDAEKIVADCADVpclflDVS---- 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  84 ggsyhlaeSYSPVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSG------KRWATEREYAFRQLVAeekyrgvVY 157
Cdd:PRK09526  154 --------PQSPVNSVSFDPEDGTRLGVEHLVELGHQRIALLAGPESSVsarlrlAGWLEYLTDYQLQPIA-------VR 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 158 QGLETAPENWQHAQNRLADwlQTLPpqTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSRvALSSVAQ 237
Cdd:PRK09526  219 EGDWSAMSGYQQTLQMLRE--GPVP--SAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIP-PLTTIKQ 293
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1123192800 238 GARQMGYQAAKLLHRLLDKEEMPLQRILvpPVRVIERRST 277
Cdd:PRK09526  294 DFRLLGKEAVDRLLALSQGQAVKGSQLL--PTSLVVRKST 331
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
309-383 4.80e-08

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 53.92  E-value: 4.80e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1123192800 309 DAVGISRSNLEKRFKEEVGETIHAMIHAeKLEKARSLLISTTLSINEISQMCGYPSLQYFYSVFKKAYDTTPKEY 383
Cdd:PRK15186  205 DSLYMSCSTLKRKLKQENTSFSEVYLNA-RMNKATKLLRNSEYNITRVAYMCGYDSASYFTCVFKKHFKTTPSEF 278
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
303-383 6.04e-08

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 53.85  E-value: 6.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 303 KVDQVLDAVGISRSNLEKRFKEEvGETIHAMIHAEKLEKARSLLISTTLSINEISQMCGYPSLQYFYSVFKKAYDTTPKE 382
Cdd:PRK15185  224 KLTDVADHIFMSTSTLKRKLAEE-GTSFSDIYLSARMNQAAKLLRIGNHNVNAVALKCGYDSTSYFIQCFKKYFKTTPST 302

                  .
gi 1123192800 383 Y 383
Cdd:PRK15185  303 F 303
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
99-274 7.96e-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: 7.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  99 IATDN----YALVEsaflHLKEKGVNRFAF-YGLPESSGKRwatEREYAFRQLVAEekyrgvvyQGLETaPENWQH---- 169
Cdd:cd06280    96 VAGDNregaYKAVK----HLIELGHRRIGLiTGPLEISTTR---ERLAGYREALAE--------AGIPV-DESLIFegds 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 170 ----AQNRLADWLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRyLSRVALSSVAQGARQMGYQ 245
Cdd:cd06280   160 tiegGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFE-IVDPPLTVVAQPAYEIGRI 238
                         170       180
                  ....*....|....*....|....*....
gi 1123192800 246 AAKLLHRLLDKEEMPLQRILVPPvRVIER 274
Cdd:cd06280   239 AAQLLLERIEGQGEEPRRIVLPT-ELIIR 266
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
347-384 8.77e-08

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: 47.92  E-value: 8.77e-08
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1123192800 347 ISTTLSINEISQMCGYpSLQYFYSVFKKAYDTTPKEYR 384
Cdd:pfam00165   5 LSTNLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYR 41
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
294-335 9.21e-08

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: 47.92  E-value: 9.21e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1123192800 294 IRNHACKGIKVDQVLDAVGISRSNLEKRFKEEVGETIHAMIH 335
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
PBP1_LacI-like cd06281
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
58-276 1.07e-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: 380504 [Multi-domain]  Cd Length: 270  Bit Score: 52.63  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  58 DGVIA---DFDDKQIEQALADVDVPIVgvggsyhLAESYSPVHY--IATDNYALVESAFLHLKEKGVNRFAFygLPESSG 132
Cdd:cd06281    57 DGLILtpgDEDDPELAAALARLDIPVV-------LIDRDLPGDIdsVLVDHRSGVRQATEYLLSLGHRRIAL--LTGGPD 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 133 KRWATEREYAFRQLVAEekyrgvvyQGLETAPE-------NWQHAQNRLADWLQTLPPQTGIIAVTDARARHILQVCEHL 205
Cdd:cd06281   128 IRPGRERIAGFKAAFAA--------AGLPPDPDlvrlgsfSADSGFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAA 199
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1123192800 206 HIPVPEKLCVIGIDNEELTRYLSRvALSSVAQGARQMGYQAAK-LLHRLLDKEEMPLQRILVPPvRVIERRS 276
Cdd:cd06281   200 GLRIPGDLSVVSIGDSDLAELHDP-PITAIRWDLDAVGRAAAElLLDRIEGPPAGPPRRIVVPT-ELILRDS 269
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
313-385 1.72e-07

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 52.24  E-value: 1.72e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1123192800 313 ISRSNLEKRFKEEvgETIHAMIHAE-KLEKARSLLISTTLSINEISQMCGYPSLQYFYSVFKKAYDTTPKEYRD 385
Cdd:PRK09978  170 MSPSLLKKKLREE--ETSYSQLLTEcRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFRNYYGMTPTEYQE 241
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
304-389 2.45e-07

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 52.03  E-value: 2.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 304 VDQVLDAVGISRSNLEKRFKEEVGETIHAMIHAEKLEKARSLLISTTLSINEISQMCGYPSLQYFYSVFKKAYDTTPKEY 383
Cdd:PRK13500  225 LDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDSNYFSVVFTRETGMTPSQW 304

                  ....*.
gi 1123192800 384 RDVNSE 389
Cdd:PRK13500  305 RHLNSQ 310
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
234-384 4.03e-07

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 50.83  E-value: 4.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 234 SVAQGARQMGYQAAKLLHRLlDKEEMPLQRILVPPVRVIERRSTDYRSLTDPA--VIQAMHYIRNHACKGIKVDQVLDAV 311
Cdd:PRK13503  119 SVLQQVRQLVAQMEQQEESN-DLEAIASREILFMQLLVLLRKSSLQENGENSDarLNQLLAWLEDHFAEEVNWEALADQF 197
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1123192800 312 GISRSNLEKRFKEEVGETIHAMIHAEKLEKARSLLISTTLSINEISQMCGYPSLQYFYSVFKKAYDTTPKEYR 384
Cdd:PRK13503  198 SLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGDSNHFSTLFRREFSWSPRDIR 270
PRK09940 PRK09940
transcriptional regulator YdeO; Provisional
303-384 9.38e-07

transcriptional regulator YdeO; Provisional


Pssm-ID: 182157 [Multi-domain]  Cd Length: 253  Bit Score: 49.70  E-value: 9.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 303 KVDQVLDAVGISRSNLEKRFKEEvGETIHAMIHAEKLEKARSLlISTTLSINEISQMCGYPSLQYFYSVFKKAYDTTP-- 380
Cdd:PRK09940  152 KLKDICDCLYISESLLKKKLKQE-QTTFSQILLDARMQHAKNL-IRVEGSVNKIAEQCGYASTSYFIYAFRKHFGNSPkr 229

                  ....*.
gi 1123192800 381 --KEYR 384
Cdd:PRK09940  230 vsKEYR 235
PBP1_LacI-like cd06282
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
58-265 2.15e-06

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


Pssm-ID: 380505 [Multi-domain]  Cd Length: 267  Bit Score: 48.82  E-value: 2.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  58 DGVIADFDDKQIEQALADVD---VPIVGVggsYHLAESYSpVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSGKR 134
Cdd:cd06282    57 DGLILTVGDAQGSEALELLEeegVPYVLL---FNQTENSS-HPFVSVDNRLASYDVAEYLIALGHRRIAMVAGDFSASDR 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 135 wATEREYAFRQLVAEekyrgvvyQGLETAP-------ENwQHAQNRLADWLQTLPPqTGIIAVTDARARHILQVCEHLHI 207
Cdd:cd06282   133 -ARLRYQGYRDALKE--------AGLKPIPivevdfpTN-GLEEALTSLLSGPNPP-TALFCSNDLLALSVISALRRLGI 201
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1123192800 208 PVPEKLCVIGIDNEELTRYLSRvALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQRIL 265
Cdd:cd06282   202 RVPDDVSVIGFDGIAIGELLTP-TLATVVQPSRDMGRAAADLLLAEIEGESPPTSIRL 258
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
15-260 5.37e-06

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


Pssm-ID: 380533 [Multi-domain]  Cd Length: 272  Bit Score: 47.72  E-value: 5.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  15 NKAYDRQVVEGV---GEYLQASQSEWDIFIEEDFRARIDKIKDWLGDG----VIADFDDKQIEQALADV---DVPIV--- 81
Cdd:cd06310    10 TSAFWRTVREGAeaaAKDLGVKIIFVGPESEEDVAGQNSLLEELINKKpdaiVVAPLDSEDLVDPLKDAkdkGIPVIvid 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  82 -GVGGSYHLAesyspvhYIATDNYALVESAFLHLKEKGVNRFAFYGLPESSGKRWATEREYAFRQLVAEEkYRGVVYQGL 160
Cdd:cd06310    90 sGIKGDAYLS-------YIATDNYAAGRLAAQKLAEALGGKGKVAVLSLTAGNSTTDQREEGFKEYLKKH-PGGIKVLAS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 161 ETAPENWQHAQNRLADWLQTLPPQTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSRVALSSVAQGAR 240
Cdd:cd06310   162 QYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGQIKIVGFDSQEELLDALKNGKIDALVVQNPY 241
                         250       260
                  ....*....|....*....|
gi 1123192800 241 QMGYQAAKLLHRLLDKEEMP 260
Cdd:cd06310   242 EIGYEGIKLALKLLKGEEVP 261
PRK10703 PRK10703
HTH-type transcriptional repressor PurR;
164-280 1.12e-05

HTH-type transcriptional repressor PurR;


Pssm-ID: 236739 [Multi-domain]  Cd Length: 341  Bit Score: 47.03  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 164 PENWQHAQNRLADwLQTLPpqTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSRvALSSVAQGARQMG 243
Cdd:PRK10703  223 PESGYEAMQQILS-QKHRP--TAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTP-ALTTIHQPKDRLG 298
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1123192800 244 YQAAK-LLHRLLDKEEMPlQRILVPPvRVIERRST------DYR 280
Cdd:PRK10703  299 ETAFNmLLDRIVNKREEP-QTIEVHP-RLVERRSVadgpfrDYR 340
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
314-389 1.14e-05

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 46.59  E-value: 1.14e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1123192800 314 SRSNLEKRFKEEVGETIHAMIHAEKLEKARSLLISTTLSINEISQMCGYPSLQYFYSVFKKAYDTTPKEYRDVNSE 389
Cdd:PRK13502  205 SERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWRHLSNQ 280
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
77-275 5.78e-05

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: 44.27  E-value: 5.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  77 DVPIV----GVGGSYHLAesyspvhYIATDNYalvESAFL-------HLKEKGV--NRFAFYGLPESSgkRWATEREYAF 143
Cdd:cd06319    80 KIPVViadiGTGGGDYVS-------YIISDNY---DGGYQageylaeALKENGWggGSVGIIAIPQSR--VNGQARTAGF 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 144 RQLVAEEKYRGVVYQ--GLETAPENWQHAQnrlaDWLQTLPPQTGIIAVTDARARHILQVCEHLHipVPEKLCVIGID-N 220
Cdd:cd06319   148 EDALEEAGVEEVALRqtPNSTVEETYSAAQ----DLLAANPDIKGIFAQNDQMAQGALQAIEEAG--RTGDILVVGFDgD 221
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1123192800 221 EELTRYLSRVALS-SVAQGARQMGYQAAKLLHRLLDKEEMPLQRILVpPVRVIERR 275
Cdd:cd06319   222 PEALDLIKDGKLDgTVAQQPFGMGARAVELAIQALNGDNTVEKEIYL-PVLLVTSE 276
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
313-384 7.73e-05

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 44.12  E-value: 7.73e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1123192800 313 ISRSNLEKRFKEEVGETIHAMIHAEKLEKARSLLISTTLSINEISQMCGYPSLQYFYSVFKKAYDTTPKEYR 384
Cdd:PRK13501  204 LVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFSAVFTREAGMTPRDYR 275
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
68-258 8.44e-05

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


Pssm-ID: 380660 [Multi-domain]  Cd Length: 274  Bit Score: 43.77  E-value: 8.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  68 QIEQAlADVDVPIVGV--GgsyhlAESYSPVHYIATDNYALVESAFLHLKE--KGVNRFAFYGLPESSGKrwATEREYAF 143
Cdd:cd20005    74 QLEKA-KEKGIPVVTFdsG-----VPSDLPLATVATDNYAAGALAADHLAEliGGKGKVAIVAHDATSET--GIDRRDGF 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 144 RQLVaEEKYRG-----VVYQGLETapenwQHAQNRLADWLQTLPPQTGIIAVTDARARHILQVCEHLHipVPEKLCVIGI 218
Cdd:cd20005   146 KDEI-KEKYPDikvvnVQYGVGDH-----AKAADIAKAILQANPDLKGIYATNEGAAIGVANALKEMG--KLGKIKVVGF 217
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1123192800 219 DNEELT-RYL-SRVALSSVAQGARQMGYQAAKLLHRLLDKEE 258
Cdd:cd20005   218 DSGEAQiDAIkNGVIAGSVTQNPYGMGYKTVKAAVKALKGEE 259
PRK11041 PRK11041
DNA-binding transcriptional regulator CytR; Provisional
178-257 8.62e-05

DNA-binding transcriptional regulator CytR; Provisional


Pssm-ID: 182923 [Multi-domain]  Cd Length: 309  Bit Score: 44.22  E-value: 8.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 178 LQTLP-PQTGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYlSRVALSSVAQGARQMGYQAAKLL------ 250
Cdd:PRK11041  207 LLDLPqPPTAVFCHSDVMALGALSQAKRMGLRVPQDLSIIGFDDIDLAQY-CDPPLTTVAQPRYEIGREAMLLLleqlqg 285
                          90
                  ....*....|...
gi 1123192800 251 ------HRLLDKE 257
Cdd:PRK11041  286 hhvssgSRLLDCE 298
PBP1_CelR cd06295
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ...
65-276 2.40e-04

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: 42.62  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  65 DDKQIEQALADvDVPIVGVGGSyhlaESYSPVHYIATDNYALVESAFLHLKEKGVNRFAFYGLPESsgkrwateREYAFR 144
Cdd:cd06295    75 DHDALRELAQQ-GLPMVVWGAP----EDGQSYCSVGSDNVKGGALATEHLIEIGRRRIAFLGDPPH--------PEVADR 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 145 qlvaeekYRGVVyQGLETAPENWQHAQNRLADW------------LQTLPPQTGIIAVTDARArhiLQVCEHLH---IPV 209
Cdd:cd06295   142 -------LQGYR-DALAEAGLEADPSLLLSCDFteesgyaamralLDSGTAFDAIFAASDLIA---MGAIRALRergISV 210
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1123192800 210 PEKLCVIGIDNEELTRYlSRVALSSVAQGARQMGYQAAKLLHRLLDKEemPLQRILVpPVRVIERRS 276
Cdd:cd06295   211 PGDVAVVGYDDIPLAAY-FRPPLTTVRQDLALAGRLLVEKLLALIAGE--PVTSSML-PVELVVRES 273
PRK10423 PRK10423
transcriptional repressor RbsR; Provisional
182-276 2.49e-04

transcriptional repressor RbsR; Provisional


Pssm-ID: 182448 [Multi-domain]  Cd Length: 327  Bit Score: 42.76  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 182 PPQtGIIAVTDARARHILQVCEHLHIPVPEKLCVIGIDNEELTRYLSRvALSSVAQGARQMGYQAAK-LLHRLLDKEEMP 260
Cdd:PRK10423  235 RPQ-AVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTP-PLTTIHQPKDELGELAIDvLIHRMAQPTLQQ 312
                          90
                  ....*....|....*.
gi 1123192800 261 LQRILVPpvRVIERRS 276
Cdd:PRK10423  313 QRLQLTP--ELMERGS 326
PBP1_hexuronate_repressor-like cd06272
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ...
58-267 4.88e-04

ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and close homologs, all members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and its close homologs from other bacteria, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380496 [Multi-domain]  Cd Length: 266  Bit Score: 41.59  E-value: 4.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  58 DGVI-ADFDDKQIEQA-LADVDVPIVGVGgsyHLAESYSPVHyiaTDNYALVESAFLHLKEKGVNRFAFYGLPESSgkRW 135
Cdd:cd06272    58 DGVIvFGISDSDIEYLnKNKPKIPIVLYN---RESPKYSTVN---VDNEKAGRLAVLLLIQKGHKSIAYIGNPNSN--RN 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 136 ATEREYAFRQLVAEEK----YRGVVYQGLETapENWQHAQNRLADwLQTLPpqTGIIAVTDARARHILQVCEHLHIPVPE 211
Cdd:cd06272   130 QTLRGKGFIETCEKHGihlsDSIIDSRGLSI--EGGDNAAKKLLK-KKTLP--KAIFCNSDDIALGVLRVLKENGISIPE 204
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1123192800 212 KLCVIGIDNeELTRYLSRVALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQ-RILVP 267
Cdd:cd06272   205 DISIVSYDN-IPQEARSDPPLTVVGVPIEKIAEESLRLILKLIEGRENEIQqLILYP 260
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
42-274 9.17e-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: 40.68  E-value: 9.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  42 EEDFRARIDKIKDWLGDG----VIADFDDKQIEQ---ALADVDVPIVGV----GGsyhlaesYSPVHYIATDNYALVESA 110
Cdd:cd20004    40 EDDVEAQIQIIEYFIDQGvdgiVLAPLDRKALVApveRARAQGIPVVIIdsdlGG-------DAVISFVATDNYAAGRLA 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 111 FLHLKE--KGVNRFAFYGLPESSGKrwATEREYAFRQ---------LVAEEKYRGVvyqgleTAPEnwqhAQNRLADWLQ 179
Cdd:cd20004   113 AKRMAKllNGKGKVALLRLAKGSAS--TTDRERGFLEalkklapglKVVDDQYAGG------TVGE----ARSSAENLLN 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 180 TLPPQTGIIAVTDARARHILQVCEHlhIPVPEKLCVIGID-NEELTRYLSRVALSS-VAQGARQMGYQAAKLLHRLLdKE 257
Cdd:cd20004   181 QYPDVDGIFTPNESTTIGALRALRR--LGLAGKVKFIGFDaSDLLLDALRAGEISAlVVQDPYRMGYLGVKTAVAAL-RG 257
                         250
                  ....*....|....*..
gi 1123192800 258 EMPLQRIlVPPVRVIER 274
Cdd:cd20004   258 KPVPKRI-DTGVVLVTK 273
COG2984 COG2984
ABC-type uncharacterized transport system, periplasmic component [General function prediction ...
172-263 8.60e-03

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


Pssm-ID: 442223  Cd Length: 284  Bit Score: 37.58  E-value: 8.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 172 NRLADWLQTLPPQT-GIIAVTD----ARARHILQVCEHLHIPVpeklcvIGIDNEELTRYlsrvALSSVAQGARQMGYQA 246
Cdd:COG2984   173 NEIQQALQSLAGKVdAIYVPTDntvvSALEAIAKVAARAKIPV------FGGDDSSVKAG----ALAGYGIDYYELGRQA 242
                          90       100
                  ....*....|....*....|
gi 1123192800 247 AKLLHRLLDKE---EMPLQR 263
Cdd:COG2984   243 AEMALRILKGEkpaDIPVET 262
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
76-268 9.03e-03

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


Pssm-ID: 380545 [Multi-domain]  Cd Length: 270  Bit Score: 37.64  E-value: 9.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800  76 VDVPIVGVggsyhlaesySPVHYIATDNYA---LVESAFLHLKEKGVNRFAFYGLPESSGKRwatEREYAFR-------- 144
Cdd:cd06322    86 VDVKADGA----------KVVTHVGTDNYAggkLAGEYALKALLGGGGKIAIIDYPEVESVV---LRVNGFKeaikkypn 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1123192800 145 -QLVAEEKYRGVVYQGLETApenwqhaqnrlADWLQTLPPQTGIIAVTDARARHILQVCEHLHipVPEKLCVIGID-NEE 222
Cdd:cd06322   153 iEIVAEQPGDGRREEALAAT-----------EDMLQANPDLDGIFAIGDPAALGALTAIESAG--KEDKIKVIGFDgNPE 219
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1123192800 223 LTRYLSR--VALSSVAQGARQMGYQAAKLLHRLLDKEEMPLQrILVPP 268
Cdd:cd06322   220 AIKAIAKggKIKADIAQQPDKIGQETVEAIVKYLAGETVEKE-ILIPP 266
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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