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Conserved domains on  [gi|446381959|ref|WP_000459814|]
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MULTISPECIES: D-xylose utilization transcriptional activator XylR [Salmonella]

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 4.96e-97

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: 290.26  E-value: 4.96e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959   7 RITLLFNANKAYDRQVVEGGGEYLQASQSeWDIFIEEDFR-ARIDNIKEWLGDGVIADYDDDDIAQLLADVDVPIVGVGG 85
Cdd:cd01543    1 RVALLLETSRGYGRRLLRGIARYAREHGP-WSLYLEPPGYeELLDLLKGWKGDGIIARLDDPELAEALRRLGIPVVNVSG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  86 SYHLaenyPAVHYIATDNHALVESAFLHLKEKGVNRFAFYGLPDSsrkHWAAEREYAFRQLVAEEKYRGVVYQG-LETAP 164
Cdd:cd01543   80 SRPE----PGFPRVTTDNEAIGRMAAEHLLERGFRHFAFCGFRNA---AWSRERGEGFREALREAGYECHVYESpPSGSS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 165 ENWQHAQNRLADWLQTLPPQTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLSRVALSSVAQGARQMGY 244
Cdd:cd01543  153 RSWEEEREELADWLKSLPKPVGIFACNDDRARQVLEACREAGIRVPEEVAVLGVDNDELICELSSPPLSSIALDAEQIGY 232
                        250       260       270
                 ....*....|....*....|....*....|...
gi 446381959 245 QAAKLLHRLLAREEMPLQRILVPPVRVIARRST 277
Cdd:cd01543  233 EAAELLDRLMRGERVPPEPILIPPLGVVTRQST 265
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
301-384 3.40e-26

helix_turn_helix, arabinose operon control protein;


:

Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 100.32  E-value: 3.40e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959   301 GIKVEQVLDAVGISRSNLEKRFKEEVGETIHALIHAEKLEKARSLLISTTLAINEISQMCGYPSLQYFYSVFKKEYVTTP 380
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80

                   ....
gi 446381959   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 4.96e-97

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: 290.26  E-value: 4.96e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959   7 RITLLFNANKAYDRQVVEGGGEYLQASQSeWDIFIEEDFR-ARIDNIKEWLGDGVIADYDDDDIAQLLADVDVPIVGVGG 85
Cdd:cd01543    1 RVALLLETSRGYGRRLLRGIARYAREHGP-WSLYLEPPGYeELLDLLKGWKGDGIIARLDDPELAEALRRLGIPVVNVSG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  86 SYHLaenyPAVHYIATDNHALVESAFLHLKEKGVNRFAFYGLPDSsrkHWAAEREYAFRQLVAEEKYRGVVYQG-LETAP 164
Cdd:cd01543   80 SRPE----PGFPRVTTDNEAIGRMAAEHLLERGFRHFAFCGFRNA---AWSRERGEGFREALREAGYECHVYESpPSGSS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 165 ENWQHAQNRLADWLQTLPPQTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLSRVALSSVAQGARQMGY 244
Cdd:cd01543  153 RSWEEEREELADWLKSLPKPVGIFACNDDRARQVLEACREAGIRVPEEVAVLGVDNDELICELSSPPLSSIALDAEQIGY 232
                        250       260       270
                 ....*....|....*....|....*....|...
gi 446381959 245 QAAKLLHRLLAREEMPLQRILVPPVRVIARRST 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 8.23e-39

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: 136.31  E-value: 8.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  113 HLKEKGVNRFAFYGLPDSSRKHWAAEREYAFRQLVAEEKYRGVVYQGLETAPENWQHAQNRLaDWLQTLPpqTGIIAVTD 192
Cdd:pfam13377   1 HLAELGHRRIALIGPEGDRDDPYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARERL-RWLGALP--TAVFVAND 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  193 ARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLSRvALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVPPvRVI 272
Cdd:pfam13377  78 EVALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSP-PLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPP-ELV 155

                  ....*
gi 446381959  273 ARRST 277
Cdd:pfam13377 156 EREST 160
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
46-277 1.06e-28

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 114.53  E-value: 1.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  46 RARIDNIKEWLGDGVI--ADYDDDDIAQLLADVDVPIVGVGGSYHLaenyPAVHYIATDNHALVESAFLHLKEKGVNRFA 123
Cdd:COG1609  107 REALRLLLSRRVDGLIlaGSRLDDARLERLAEAGIPVVLIDRPLPD----PGVPSVGVDNRAGARLATEHLIELGHRRIA 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 124 FYGLPDSSrkHWAAEREYAFRQLVAEekyRGVVYQGLETAPENW--QHAQNRLADWLQTLPPQTGIIAVTDARARHVLQA 201
Cdd:COG1609  183 FIGGPADS--SSARERLAGYREALAE---AGLPPDPELVVEGDFsaESGYEAARRLLARGPRPTAIFCANDLMALGALRA 257
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446381959 202 CEHLHIPVPEKLCVIGIDNEELTRYLSrVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVPPvRVIARRST 277
Cdd:COG1609  258 LREAGLRVPEDVSVVGFDDIPLARYLT-PPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERVLLPP-ELVVREST 331
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
301-384 3.40e-26

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 100.32  E-value: 3.40e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959   301 GIKVEQVLDAVGISRSNLEKRFKEEVGETIHALIHAEKLEKARSLLISTTLAINEISQMCGYPSLQYFYSVFKKEYVTTP 380
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80

                   ....
gi 446381959   381 KEYR 384
Cdd:smart00342  81 SEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
249-390 3.64e-20

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 89.07  E-value: 3.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 249 LLHRLLAREEMPLQRILVPPVRVIARRSTDYRSLTDPAVIQAMHFIRNHACKGIKVEQVLDAVGISRSNLEKRFKEEVGE 328
Cdd:COG2207  116 LLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGT 195
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446381959 329 TIHALIHAEKLEKARSLLISTTLAINEISQMCGYPSLQYFYSVFKKEYVTTPKEYRDQHSEA 390
Cdd:COG2207  196 SPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRAR 257
HTH_18 pfam12833
Helix-turn-helix domain;
309-386 3.67e-17

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 75.70  E-value: 3.67e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446381959  309 DAVGISRSNLEKRFKEEVGETIHALIHAEKLEKARSLLISTT-LAINEISQMCGYPSLQYFYSVFKKEYVTTPKEYRDQ 386
Cdd:pfam12833   3 AALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDTgLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRRR 81
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
246-390 1.83e-15

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 76.17  E-value: 1.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 246 AAKLLHRLLAREeMPLQRILVPPVRviarrstdyrsltDPAVIQAMHFIRNHACKGIKVEQVLDAVGISRSNLEKRFKEE 325
Cdd:PRK10572 158 AMNLLERLLLRC-MEAIPESLHPPM-------------DPRVREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQ 223
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446381959 326 VGETIHALIHAEKLEKARSLLISTTLAINEISQMCGYPSLQYFYSVFKKEYVTTPKEYRDQHSEA 390
Cdd:PRK10572 224 LGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSEFRARCEEK 288
adjacent_YSIRK TIGR04094
YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only ...
228-384 9.45e-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: 72.02  E-value: 9.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  228 SRVALSSVAQGARQMGYQAAKLLH---RLLAREEMPLQRILVPPVR---------VIARRSTDYRSLTDPAVIQamhFIR 295
Cdd:TIGR04094 219 SIIIFEKLSQLAIQMGVDIVDAYRlrdYYIQEIEEQTSLMDVLKLRdsaiiyfteLLHEISINHHSPLIRAVIQ---YIN 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  296 NHACKGIKVEQVLDAVGISRSNLEKRFKEEVGETIHALIHAEKLEKARSLLISTtLAINEISQMCGYPSLQYFYSVFKKE 375
Cdd:TIGR04094 296 LNLYDPLKVEEIAKQFFMSESKLRKLFKKEMGISIQEYISKRKIEEAKYLLRSQ-IPVSEVSNELGFYDLSHFSRTFKKH 374

                  ....*....
gi 446381959  376 YVTTPKEYR 384
Cdd:TIGR04094 375 TGVSPKQYQ 383
lacI PRK09526
lac repressor; Reviewed
43-277 3.49e-07

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 51.53  E-value: 3.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  43 EDFRARIDNIKEWLGDGVI-----ADYDDDDIAQLLADV-----DVPivgvggsyhlaeNYPAVHYIATDNHALVESAFL 112
Cdd:PRK09526 107 EACQAAVNELLAQRVSGVIinvplEDADAEKIVADCADVpclflDVS------------PQSPVNSVSFDPEDGTRLGVE 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 113 HLKEKGVNRFAFYGLPDSS-----R-KHWAAEREYAFRQLVAeekyrgvVYQGLETAPENWQHAQNRLADwlQTLPpqTG 186
Cdd:PRK09526 175 HLVELGHQRIALLAGPESSvsarlRlAGWLEYLTDYQLQPIA-------VREGDWSAMSGYQQTLQMLRE--GPVP--SA 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 187 IIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLSRvALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILv 266
Cdd:PRK09526 244 ILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIP-PLTTIKQDFRLLGKEAVDRLLALSQGQAVKGSQLL- 321
                        250
                 ....*....|.
gi 446381959 267 pPVRVIARRST 277
Cdd:PRK09526 322 -PTSLVVRKST 331
 
Name Accession Description Interval E-value
PBP1_XylR cd01543
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ...
7-277 4.96e-97

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: 290.26  E-value: 4.96e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959   7 RITLLFNANKAYDRQVVEGGGEYLQASQSeWDIFIEEDFR-ARIDNIKEWLGDGVIADYDDDDIAQLLADVDVPIVGVGG 85
Cdd:cd01543    1 RVALLLETSRGYGRRLLRGIARYAREHGP-WSLYLEPPGYeELLDLLKGWKGDGIIARLDDPELAEALRRLGIPVVNVSG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  86 SYHLaenyPAVHYIATDNHALVESAFLHLKEKGVNRFAFYGLPDSsrkHWAAEREYAFRQLVAEEKYRGVVYQG-LETAP 164
Cdd:cd01543   80 SRPE----PGFPRVTTDNEAIGRMAAEHLLERGFRHFAFCGFRNA---AWSRERGEGFREALREAGYECHVYESpPSGSS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 165 ENWQHAQNRLADWLQTLPPQTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLSRVALSSVAQGARQMGY 244
Cdd:cd01543  153 RSWEEEREELADWLKSLPKPVGIFACNDDRARQVLEACREAGIRVPEEVAVLGVDNDELICELSSPPLSSIALDAEQIGY 232
                        250       260       270
                 ....*....|....*....|....*....|...
gi 446381959 245 QAAKLLHRLLAREEMPLQRILVPPVRVIARRST 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 8.23e-39

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: 136.31  E-value: 8.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  113 HLKEKGVNRFAFYGLPDSSRKHWAAEREYAFRQLVAEEKYRGVVYQGLETAPENWQHAQNRLaDWLQTLPpqTGIIAVTD 192
Cdd:pfam13377   1 HLAELGHRRIALIGPEGDRDDPYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARERL-RWLGALP--TAVFVAND 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  193 ARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLSRvALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVPPvRVI 272
Cdd:pfam13377  78 EVALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSP-PLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPP-ELV 155

                  ....*
gi 446381959  273 ARRST 277
Cdd:pfam13377 156 EREST 160
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
46-277 1.06e-28

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 114.53  E-value: 1.06e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  46 RARIDNIKEWLGDGVI--ADYDDDDIAQLLADVDVPIVGVGGSYHLaenyPAVHYIATDNHALVESAFLHLKEKGVNRFA 123
Cdd:COG1609  107 REALRLLLSRRVDGLIlaGSRLDDARLERLAEAGIPVVLIDRPLPD----PGVPSVGVDNRAGARLATEHLIELGHRRIA 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 124 FYGLPDSSrkHWAAEREYAFRQLVAEekyRGVVYQGLETAPENW--QHAQNRLADWLQTLPPQTGIIAVTDARARHVLQA 201
Cdd:COG1609  183 FIGGPADS--SSARERLAGYREALAE---AGLPPDPELVVEGDFsaESGYEAARRLLARGPRPTAIFCANDLMALGALRA 257
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446381959 202 CEHLHIPVPEKLCVIGIDNEELTRYLSrVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVPPvRVIARRST 277
Cdd:COG1609  258 LREAGLRVPEDVSVVGFDDIPLARYLT-PPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERVLLPP-ELVVREST 331
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
32-268 1.91e-28

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: 111.84  E-value: 1.91e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  32 ASQSEWDIFI------EEDFRARIDNIKEWLGDGVI--ADYDDDDIAQLLADVDVPIVGVGGSYHlaenYPAVHYIATDN 103
Cdd:cd06267   25 ARERGYSLLLcntdedPEREREYLRLLLSRRVDGIIlaPSSLDDELLEELLAAGIPVVLIDRRLD----GLGVDSVVVDN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 104 HALVESAFLHLKEKGVNRFAFYGLPDSSRkhWAAEREYAFRQLVAE---EKYRGVVYQGletaPENWQHAQNRLADWLQT 180
Cdd:cd06267  101 YAGAYLATEHLIELGHRRIAFIGGPLDLS--TSRERLEGYRDALAEaglPVDPELVVEG----DFSEESGYEAARELLAL 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 181 LPPQTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLSrVALSSVAQGARQMGYQAAKLLHRLLAREEMP 260
Cdd:cd06267  175 PPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLT-PPLTTVRQPAYEMGRAAAELLLERIEGEEEP 253

                 ....*...
gi 446381959 261 LQRILVPP 268
Cdd:cd06267  254 PRRIVLPT 261
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
301-384 3.40e-26

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 100.32  E-value: 3.40e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959   301 GIKVEQVLDAVGISRSNLEKRFKEEVGETIHALIHAEKLEKARSLLISTTLAINEISQMCGYPSLQYFYSVFKKEYVTTP 380
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80

                   ....
gi 446381959   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 ...
70-277 3.40e-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: 95.03  E-value: 3.40e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  70 AQLLADVDVPIVGVGGsyhlAENYPAVHYIATDNHALVESAFLHLKEKGVNRFAFYGLPDSSRkhWAAEREYAFRQLVAE 149
Cdd:cd06292   75 VRYLHEAGVPFVAFGR----ANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPEGSV--PSDDRLAGYRAALEE 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 150 EKY---RGVVYQGLETAPENWQHAQNRLAdwlQTLPPqTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRY 226
Cdd:cd06292  149 AGLpfdPGLVVEGENTEEGGYAAAARLLD---LGPPP-TAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAF 224
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 446381959 227 LSrVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVPPvRVIARRST 277
Cdd:cd06292  225 TH-PPLTTVRQPIDEIGRAVVDLLLAAIEGNPSEPREILLQP-ELVVRESS 273
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
58-276 4.41e-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: 91.81  E-value: 4.41e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  58 DGVIADYDDDDIAQLLaDVDVPIVGVGgsYHLAENYPAVH-------YIATDnhalvesaflHLKEKGVNRFAFYGlpDS 130
Cdd:cd06291   57 DGIILGSHSLDIEEYK-KLNIPIVSID--RYLSEGIPSVSsdnyqggRLAAE----------HLIEKGCKKILHIG--GP 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 131 SRKHWAAEREYAFRQLVAEEKYRGVVYQGLETAPeNWQHAQNRLADWLQTLPPQTGIIAVTDARARHVLQACEHLHIPVP 210
Cdd:cd06291  122 SNNSPANERYRGFEDALKEAGIEYEIIEIDENDF-SEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVP 200
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446381959 211 EKLCVIGIDNEELTRYlSRVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVpPVRVIARRS 276
Cdd:cd06291  201 EDVQIIGFDGIEISEL-LYPELTTIRQPIEEMAKEAVELLLKLIEGEEIEESRIVL-PVELIERET 264
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
249-390 3.64e-20

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 89.07  E-value: 3.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 249 LLHRLLAREEMPLQRILVPPVRVIARRSTDYRSLTDPAVIQAMHFIRNHACKGIKVEQVLDAVGISRSNLEKRFKEEVGE 328
Cdd:COG2207  116 LLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGT 195
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446381959 329 TIHALIHAEKLEKARSLLISTTLAINEISQMCGYPSLQYFYSVFKKEYVTTPKEYRDQHSEA 390
Cdd:COG2207  196 SPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRAR 257
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
262-390 2.56e-19

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: 87.52  E-value: 2.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 262 QRILVPPVR------VIARRstDYRSLTDPAVIQAMHFIRNHACKGIKVEQVLDAVGISRSNLEKRFKEEVGETIHALIH 335
Cdd:COG4977  183 RRLVVDPRRpggqaqFSPLL--VPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQ 260
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446381959 336 AEKLEKARSLLISTTLAINEISQMCGYPSLQYFYSVFKKEYVTTPKEYRDQHSEA 390
Cdd:COG4977  261 RLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRAR 315
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
43-277 4.64e-19

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: 86.13  E-value: 4.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  43 EDFRARIDNikeWLG---DGVI--ADYDDDDIAQLLADVDVPIVGVggSYHLAEnyPAVHYIATDNHALVESAFLHLKEK 117
Cdd:cd06285   42 ERELAALDS---LLSrrvDGLIitPARDDAPDLQELAARGVPVVLV--DRRIGD--TALPSVTVDNELGGRLATRHLLEL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 118 GVNRFAFYGLPDSSRKHwaAEREYAFRQLVAEekyRGVVYQGLETAPENW-----QHAQNRLadwLQTLPPQTGIIAVTD 192
Cdd:cd06285  115 GHRRIAVVAGPLNASTG--RDRLRGYRRALAE---AGLPVPDERIVPGGFtieagREAAYRL---LSRPERPTAVFAAND 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 193 ARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLSrVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVPPvRVI 272
Cdd:cd06285  187 LMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLP-PPLTTVRQPKYEMGRRAAELLLQLIEGGGRPPRSITLPP-ELV 264

                 ....*
gi 446381959 273 ARRST 277
Cdd:cd06285  265 VREST 269
PBP1_MalR-like cd06294
ligand-binding domain of maltose transcription regulator MalR which is a member of the ...
46-267 5.69e-19

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


Pssm-ID: 380517 [Multi-domain]  Cd Length: 269  Bit Score: 85.71  E-value: 5.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  46 RARIDNIKEWLG----DGVI--ADYDDDDIAQLLADVDVPIVGVGGSyhlaENYPAVHYIATDNHALVESAFLHLKEKGV 119
Cdd:cd06294   46 EELLEEVKRMVRgrrvDGFIllYSKEDDPLIEYLKEEGFPFVVIGKP----LDDNDVLYVDNDNVQAGYEATEYLIDKGH 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 120 NRFAFYGlpDSSRKHWAAEREYAFRQLVAEEKYRgVVYQGLETAPENWQHAQNRLADWLQTLPPQTGIIAVTDARARHVL 199
Cdd:cd06294  122 KRIAFIG--GDKNLVVSIDRLQGYKQALKEAGLP-LDDDYILLLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVL 198
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446381959 200 QACEHLHIPVPEKLCVIGIDNEELTRyLSRVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVP 267
Cdd:cd06294  199 RYLQELGLRVPEDVSIISFNNSPLAE-LASPPLTSVDINPYELGREAAKLLINLLEGPESLPKNVIVP 265
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
58-272 1.93e-18

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: 84.15  E-value: 1.93e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  58 DGVI---ADYDDDDIAQLLADVDVPIV----GVGGSyhlaenypAVHYIATDNHALVESAFLHLKEKGVNRFAFYG-LPD 129
Cdd:cd06289   57 DGLIlspAAGTTAELLRRLKAWGIPVVlalrDVPGS--------DLDYVGIDNRLGAQLATEHLIALGHRRIAFLGgLSD 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 130 SSRkhwAAEREYAFRQLVAEEKYRGVVYQGLETAPENWQHAQ--NRLadwLQTLPPQTGIIAVTDARARHVLQACEHLHI 207
Cdd:cd06289  129 SST---RRERLAGFRAALAEAGLPLDESLIVPGPATREAGAEaaREL---LDAAPPPTAVVCFNDLVALGAMLALRRRGL 202
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446381959 208 PVPEKLCVIGIDNEELTRyLSRVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVPPVRVI 272
Cdd:cd06289  203 EPGRDIAVVGFDDVPEAA-LWTPPLTTVSVHPREIGRRAARLLLRRIEGPDTPPERIIIEPRLVV 266
PBP1_RegR_EndR_KdgR-like cd06283
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ...
71-267 4.53e-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: 83.37  E-value: 4.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  71 QLLADVDVPIVgvggsyhLAENY---PAVHYIATDNHALVESAFLHLKEKGVNRFAFYGLPD---SSRkhwaAEREYAFR 144
Cdd:cd06283   72 LELAQKGLPVV-------LVDRQiepLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPIkgiSTR----RERLQGFL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 145 QLVAEekyRGVVYQGLETAPENWQHAQNRLADWLQTLPPQ-TGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEEL 223
Cdd:cd06283  141 DALAR---YNIEGDVYVIEIEDTEDLQQALAAFLSQHDGGkTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDW 217
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 446381959 224 TRyLSRVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVP 267
Cdd:cd06283  218 AD-LIGPGITTIRQPTYEIGKAAAEILLERIEGDSGEPKEIELP 260
HTH_18 pfam12833
Helix-turn-helix domain;
309-386 3.67e-17

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 75.70  E-value: 3.67e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446381959  309 DAVGISRSNLEKRFKEEVGETIHALIHAEKLEKARSLLISTT-LAINEISQMCGYPSLQYFYSVFKKEYVTTPKEYRDQ 386
Cdd:pfam12833   3 AALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDTgLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRRR 81
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
58-276 1.40e-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: 78.85  E-value: 1.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  58 DGVIADYDDDDIAQL--LADVDVPIVGVGgsyHLAENyPAVHYIATDNhalVESAFL---HLKEKGVNRFAFYGLPDSSR 132
Cdd:cd06293   57 RGLIVTPSDDDLSHLarLRARGTAVVLLD---RPAPG-PAGCSVSVDD---VQGGALavdHLLELGHRRIAFVSGPLRTR 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 133 khWAAEREYAFRQLVAEekyRGVVYQGL---ETAPENWQHAQNRLADWLQTLPPQ-TGIIAVTDARARHVLQACEHLHIP 208
Cdd:cd06293  130 --QVAERLAGARAAVAE---AGLDPDEVvreLSAPDANAELGRAAAAQLLAMPPRpTAVFAANDLLALGLLAGLRRAGLR 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446381959 209 VPEKLCVIGIDNEELTRYLSrVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVPPvRVIARRS 276
Cdd:cd06293  205 VPDDVSVVGYDDLPFAAAAN-PPLTTVRQPSYELGRAAADLLLDEIEGPGHPHEHVVFQP-ELVVRSS 270
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
283-390 6.29e-16

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: 78.17  E-value: 6.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 283 TDPAVIQAMHFIRNHACKGIKVEQVLDAVGISRSNLEKRFKEEVGETIHALIHAEKLEKARSLLiSTTLAINEISQMCGY 362
Cdd:COG2169   82 RADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL-QTGLSVTDAAYAAGF 160
                         90       100
                 ....*....|....*....|....*...
gi 446381959 363 PSLQYFYSVFKKEYVTTPKEYRDQHSEA 390
Cdd:COG2169  161 GSLSRFYEAFKKLLGMTPSAYRRGGAGA 188
PBP1_sucrose_transcription_regulator cd06288
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ...
58-276 1.07e-15

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: 76.43  E-value: 1.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  58 DGVI-ADYDDDDIAQLLADVDVPIVGVggsYHLAENyPAVHYIATDNHAlveSAFL---HLKEKGVNRFAFYGLPDSSRK 133
Cdd:cd06288   58 DGIIyASMHHREVTLPPELTDIPLVLL---NCFDDD-PSLPSVVPDDEQ---GGYLatrHLIEAGHRRIAFIGGPEDSLA 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 134 hwAAEREYAFRQLVAEekyRGVVYQGLETAPENWQHAQNRLA--DWLQTLPPQTGIIAVTDARARHVLQACEHLHIPVPE 211
Cdd:cd06288  131 --TRLRLAGYRAALAE---AGIPYDPSLVVHGDWGRESGYEAakRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPE 205
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446381959 212 KLCVIGIDNEELTRYLsRVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVpPVRVIARRS 276
Cdd:cd06288  206 DLSVVGFDNQELAAYL-RPPLTTVALPYYEMGRRAAELLLDGIEGEPPEPGVIRV-PCPLIERES 268
PBP1_LacI cd01574
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ...
42-276 1.14e-15

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: 76.08  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  42 EEDFRARIDNIKEWLGDGVI--ADYDDDDIAQLLADVDVPIVGVGGSYHlaenyPAVHYIATDNHALVESAFLHLKEKGV 119
Cdd:cd01574   42 PASVREALDRLLSQRVDGIIviAPDEAVLEALRRLPPGLPVVIVGSGPS-----PGVPTVSIDQEEGARLATRHLLELGH 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 120 NRFAFYGLPDSSRKhwAAEREYAFRQLVAEekyRGVVYQglETAPENWQ-----HAQNRLADwlqtLPPQTGIIAVTDAR 194
Cdd:cd01574  117 RRIAHIAGPLDWVD--ARARLRGWREALEE---AGLPPP--PVVEGDWSaasgyRAGRRLLD----DGPVTAVFAANDQM 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 195 ARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLSrVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVPPvRVIAR 274
Cdd:cd01574  186 ALGALRALHERGLRVPEDVSVVGFDDIPEAAYFV-PPLTTVRQDFAELGRRAVELLLALIEGPAPPPESVLLPP-ELVVR 263

                 ..
gi 446381959 275 RS 276
Cdd:cd01574  264 ES 265
PBP1_LacI-like cd06273
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
71-276 1.70e-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: 75.62  E-value: 1.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  71 QLLADVDVPIVgVGGSYHLAENYPAvhyIATDNHALVESAFLHLKEKGVNRFAFYG--LPDSSRkhwAAEREYAFRQLVA 148
Cdd:cd06273   72 ELLEQRQVPYV-LTWSYDEDSPHPS---IGFDNRAAAARAAQHLLDLGHRRIAVISgpTAGNDR---ARARLAGIRDALA 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 149 EekyrgvvyQGLETAPE-------NWQHAQNRLADWLQTLPPQTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNE 221
Cdd:cd06273  145 E--------RGLELPEErvveapySIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDL 216
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446381959 222 ELTRYLSrVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILvpPVRVIARRS 276
Cdd:cd06273  217 ELAAHLS-PPLTTVRVPAREIGELAARYLLALLEGGPPPKSVEL--ETELIVRES 268
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
246-390 1.83e-15

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 76.17  E-value: 1.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 246 AAKLLHRLLAREeMPLQRILVPPVRviarrstdyrsltDPAVIQAMHFIRNHACKGIKVEQVLDAVGISRSNLEKRFKEE 325
Cdd:PRK10572 158 AMNLLERLLLRC-MEAIPESLHPPM-------------DPRVREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQ 223
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446381959 326 VGETIHALIHAEKLEKARSLLISTTLAINEISQMCGYPSLQYFYSVFKKEYVTTPKEYRDQHSEA 390
Cdd:PRK10572 224 LGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSEFRARCEEK 288
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
58-276 6.62e-15

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: 74.11  E-value: 6.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  58 DGVIADYDDDDIAQLLADVD-VPIVGVGgSYHLAENYPAVHyiaTDNHALVESAFLHLKEKGVNRFAFYGLPDSSrkHWA 136
Cdd:cd06284   57 DGVILLSGRLDAELLSELSKrYPIVQCC-EYIPDSGVPSVS---IDNEAAAYDATEYLISLGHRRIAHINGPLDN--VYA 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 137 AEREYAFRQlvAEEKYrgvvyqGLEtAPENWQH--------AQNRLADWLQTLPPQTGIIAVTDARARHVLQACEHLHIP 208
Cdd:cd06284  131 RERLEGYRR--ALAEA------GLP-VDEDLIIegdfsfeaGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLR 201
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446381959 209 VPEKLCVIGIDNEELTRYLSrVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVpPVRVIARRS 276
Cdd:cd06284  202 VPEDVSVIGFDDIEFAEMFS-PSLTTIRQPRYEIGETAAELLLEKIEGEGVPPEHIIL-PHELIVRES 267
PBP1_LacI-like cd06279
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ...
58-276 1.07e-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: 73.78  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  58 DGVIA--DYDDDDIAQLLADVDVPIVGVGGSYHlaenyPAVHYIATDNHALVESAFLHLKEKGVNRFAFYGLP---DSSR 132
Cdd:cd06279   58 DGFIVygLSDDDPAVAALRRRGLPLVVVDGPAP-----PGIPSVGIDDRAAARAAARHLLDLGHRRIAILSLRldrGRER 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 133 KHWAAEREYAFRQLVAEEKYRGVVyQGLETA------------PENWQHAQNRLADWLQTLPPQ-TGIIAVTDARARHVL 199
Cdd:cd06279  133 GPVSAERLAAATNSVARERLAGYR-DALEEAgldlddvpvveaPGNTEEAGRAAARALLALDPRpTAILCMSDVLALGAL 211
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446381959 200 QACEHLHIPVPEKLCVIGIDNEELTRyLSRVALSSVAQGARQMGYQAAKLLHRLLAREEmPLQRILvpPVRVIARRS 276
Cdd:cd06279  212 RAARERGLRVPEDLSVTGFDDIPEAA-AADPGLTTVRQPAVEKGRAAARLLLGLLPGAP-PRPVIL--PTELVVRAS 284
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
98-269 1.34e-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: 72.95  E-value: 1.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  98 YIATDNHALVESAFLHLKEKGVNRFAFYGLP--DSSRKhwaaEREYAFRQLVAEekyrgvvyQGLEtAPENWQHAQNRLA 175
Cdd:cd19977   95 TVVVDNFKGAYQATEHLIELGHKRIAFITYPleLSTRQ----ERLEGYKAALAD--------HGLP-VDEELIKHVDRQD 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 176 D-------WLQTLPPQTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLsRVALSSVAQGARQMGYQAAK 248
Cdd:cd19977  162 DvrkaiseLLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLF-NPPLTVIAQPTYEIGRKAAE 240
                        170       180
                 ....*....|....*....|..
gi 446381959 249 LL-HRLLAREEMPLQRILVPPV 269
Cdd:cd19977  241 LLlDRIENKPKGPPRQIVLPTE 262
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
58-276 1.88e-14

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


Pssm-ID: 380501 [Multi-domain]  Cd Length: 266  Bit Score: 72.57  E-value: 1.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  58 DGVI--ADYDDDDIAQLLADVDVPIVGVGGSYHLaenyPAVHYIATDNHALVESAFLHLKEKGVNRFAFYGLPDSSRKHw 135
Cdd:cd06278   56 DGVIvtSATLSSELAEECARRGIPVVLFNRVVED----PGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPEGTSTS- 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 136 aAEREYAFRQLVAEekyRGVVYQGLETAPENWQHAQNRLADWLQTLPPQTGIIAVTDARARHVLQAC-EHLHIPVPEKLC 214
Cdd:cd06278  131 -RERERGFRAALAE---LGLPPPAVEAGDYSYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAArQEGGLVVPEDIS 206
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446381959 215 VIGIDNEELTRYLSrVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVpPVRVIARRS 276
Cdd:cd06278  207 VVGFDDIPMAAWPS-YDLTTVRQPIEEMAEAAVDLLLERIENPETPPERRVL-PGELVERGS 266
PBP1_GalR cd01544
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ...
58-276 2.15e-14

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: 72.56  E-value: 2.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  58 DGVIA--DYDDDDIAQLLADVDvPIVGVGGSYhlaeNYPAVHYIATDNHALVESAFLHLKEKGVNRFAFYGLPDSSRKHW 135
Cdd:cd01544   55 DGIIAigKFSKEEIEKLKKLNP-NIVFVDSNP----DPDGFDSVVPDFEQAVRQALDYLIELGHRRIGFIGGKEYTSDDG 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 136 AAE---REYAFRQLVAE--EKYRGVVYQGLETAPENWQHAQNrladWLQTLPPQTGIIAVTDARARHVLQACEHLHIPVP 210
Cdd:cd01544  130 EEIedpRLRAFREYMKEkgLYNEEYIYIGEFSVESGYEAMKE----LLKEGDLPTAFFVASDPMAIGALRALQEAGIKVP 205
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446381959 211 EKLCVIGIDNEELTRYLSRvALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVPPvRVIARRS 276
Cdd:cd01544  206 EDISIISFNDIEVAKYVTP-PLTTVHIPTEEMGRTAVRLLLERINGGRTIPKKVLLPT-KLIERES 269
PBP1_PurR cd06275
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ...
113-276 3.15e-14

ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli; Ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli. This dimeric PurR belongs to the LacI-GalR family of transcription regulators and is activated to bind to DNA operator sites by initially binding either of high affinity corepressors, hypoxanthine or guanine. PurR is composed of two functional domains: aan N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the purine transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380499 [Multi-domain]  Cd Length: 269  Bit Score: 72.29  E-value: 3.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 113 HLKEKGVNRFAFygLPDSSRKHWAAEREYAFRQLVAEEKYRG----VVYQGLEtaPENWQHAQNRLadwLQTLPPQTGII 188
Cdd:cd06275  111 HLIELGHRRIGC--ITGPLEHSVSRERLAGFRRALAEAGIEVppswIVEGDFE--PEGGYEAMQRL---LSQPPRPTAVF 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 189 AVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLSRvALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVPP 268
Cdd:cd06275  184 ACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSP-ALTTIHQPKDELGELAVELLLDRIENKREEPQSIVLEP 262

                 ....*...
gi 446381959 269 vRVIARRS 276
Cdd:cd06275  263 -ELIERES 269
PBP1_DegA_Like cd19976
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
185-276 5.11e-14

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: 71.51  E-value: 5.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 185 TGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLSRvALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRI 264
Cdd:cd19976  179 TAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITP-ALTTIAQPIFEMGQEAAKLLLKIIKNPAKKKEEI 257
                         90
                 ....*....|..
gi 446381959 265 LVPPvRVIARRS 276
Cdd:cd19976  258 VLPP-ELIKRDS 268
adjacent_YSIRK TIGR04094
YSIRK-targeted surface antigen transcriptional regulator; Bacteria whose genomes encode only ...
228-384 9.45e-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: 72.02  E-value: 9.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  228 SRVALSSVAQGARQMGYQAAKLLH---RLLAREEMPLQRILVPPVR---------VIARRSTDYRSLTDPAVIQamhFIR 295
Cdd:TIGR04094 219 SIIIFEKLSQLAIQMGVDIVDAYRlrdYYIQEIEEQTSLMDVLKLRdsaiiyfteLLHEISINHHSPLIRAVIQ---YIN 295
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  296 NHACKGIKVEQVLDAVGISRSNLEKRFKEEVGETIHALIHAEKLEKARSLLISTtLAINEISQMCGYPSLQYFYSVFKKE 375
Cdd:TIGR04094 296 LNLYDPLKVEEIAKQFFMSESKLRKLFKKEMGISIQEYISKRKIEEAKYLLRSQ-IPVSEVSNELGFYDLSHFSRTFKKH 374

                  ....*....
gi 446381959  376 YVTTPKEYR 384
Cdd:TIGR04094 375 TGVSPKQYQ 383
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
71-276 2.18e-13

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: 69.83  E-value: 2.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  71 QLLADVDVPIVGVGGsyhLAENyPAVHYIATDNHALVESAFLHLKEKGVNRFAFYG--LPDSSRkhwAAEREYAFRQlVA 148
Cdd:cd01575   72 KLLRAAGIPVVETWD---LPDD-PIDMAVGFSNFAAGRAMARHLIERGYRRIAFVGarLDGDSR---ARQRLEGFRD-AL 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 149 EEKYRGVVYQGLETAPENWQHAQNRLADWLQTLPPQTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLS 228
Cdd:cd01575  144 AEAGLPLPLVLLVELPSSFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALP 223
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446381959 229 rVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVPPvRVIARRS 276
Cdd:cd01575  224 -PALTTVRVPRYEIGRKAAELLLARLEGEEPEPRVVDLGF-ELVRRES 269
PBP1_CcpA-like cd19975
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
31-276 2.87e-13

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: 69.51  E-value: 2.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  31 QASQSEWDIFI---EEDFRARIDNI---KEWLGDGVI--ADYDDDDIAQLLADVDVPIVGVGgSYHLAENYPavhYIATD 102
Cdd:cd19975   24 EARENGYSVILcntGSDEEREKKYLqllKEKRVDGIIfaSGTLTEENKQLLKNMNIPVVLVS-TESEDPDIP---SVKID 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 103 NHALVESAFLHLKEKGVNRFAFYGLPDSSRKHwAAEREYAFRQLVAEekyrgvvyQGLeTAPENW-----------QHAQ 171
Cdd:cd19975  100 DYQAAYDATNYLIKKGHRKIAMISGPLDDPNA-GYPRYEGYKKALKD--------AGL-PIKENLivegdfsfksgYQAM 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 172 NRLadwLQTLPPQTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYlSRVALSSVAQGARQMGYQAAKLLH 251
Cdd:cd19975  170 KRL---LKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEM-SIPPLTTVSQPFYEMGKKAVELLL 245
                        250       260
                 ....*....|....*....|....*
gi 446381959 252 RLLAREEMPLQRILVpPVRVIARRS 276
Cdd:cd19975  246 DLIKNEKKEEKSIVL-PHQIIERES 269
PBP1_CatR-like cd06296
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ...
58-277 7.89e-13

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: 68.07  E-value: 7.89e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  58 DGVIADYDDDDIAQL--LADVDVPIVGVGGsyhLAENYPAVHYIATDNHALVESAFLHLKEKGVNRFAFYGLPDSSRkhW 135
Cdd:cd06296   57 AGVVLVTSDPTSRQLrlLRSAGIPFVLIDP---VGEPDPDLPSVGATNWAGGRLATEHLLDLGHRRIAVITGPPRSV--S 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 136 AAEREYAFRQLVAEekyrgvvyQGLETAPE-----NWQHAQ--NRLADWLQTLPPQTGIIAVTDARARHVLQACEHLHIP 208
Cdd:cd06296  132 GRARLAGYRAALAE--------AGIAVDPDlvregDFTYEAgyRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLR 203
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446381959 209 VPEKLCVIGIDNEELTRYLSrVALSSVAQGARQMGYQAAKLLHRLLaREEMPLQRILVPPVRVIARRST 277
Cdd:cd06296  204 VPDDLSVIGFDDTPPARWTS-PPLTTVHQPLREMGAVAVRLLLRLL-EGGPPDARRIELATELVVRGST 270
PBP1_AglR-like cd20010
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ...
71-271 5.64e-12

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: 65.65  E-value: 5.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  71 QLLADVDVPIVgVGGSYHLAENYPavhYIATDNHALVESAFLHLKEKGVNRFAFYGLPDSSrkHWAAEREYAFRQLVAEE 150
Cdd:cd20010   76 AYLLERGIPFV-VHGRSESGAPYA---WVDIDNEGAFRRATRRLLALGHRRIALLNGPEEL--NFAHQRRDGYRAALAEA 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 151 --KYRGVVYQGLETAPENWQHAQNRLadwLQTLPPQTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLS 228
Cdd:cd20010  150 glPVDPALVREGPLTEEGGYQAARRL---LALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLLPALEYF 226
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446381959 229 RVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVPPVRV 271
Cdd:cd20010  227 SPPLTTTRSSLRDAGRRLAEMLLALIDGEPAAELQELWPPELI 269
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
89-255 9.92e-12

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: 64.64  E-value: 9.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959   89 LAENYPAVHYIATDNHA----LVESAFLHLKEKGvNRFAFYGLPDSSRkhwAAEREYAFRQlVAEEKYRGVVYQGlETAP 164
Cdd:pfam13407  89 DAPSSPRLAYVGFDNEAageaAGELLAEALGGKG-KVAILSGSPGDPN---ANERIDGFKK-VLKEKYPGIKVVA-EVEG 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  165 ENW--QHAQNRLADWLQTLPPQT-GIIAVTDARARHVLQACEHLHIPvpEKLCVIGIDNEELTRYL--SRVALSSVAQGA 239
Cdd:pfam13407 163 TNWdpEKAQQQMEALLTAYPNPLdGIISPNDGMAGGAAQALEAAGLA--GKVVVTGFDATPEALEAikDGTIDATVLQDP 240
                         170
                  ....*....|....*.
gi 446381959  240 RQMGYQAAKLLHRLLA 255
Cdd:pfam13407 241 YGQGYAAVELAAALLK 256
PBP1_SalR cd01545
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ...
69-276 4.13e-11

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: 62.96  E-value: 4.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  69 IAQLLADVDVPIVGVGGsyhlAENYPAVHYIATDNHALVESAFLHLKEKGVNRFAFY-GLPDSSRkhwAAEREYAFRQLV 147
Cdd:cd01545   72 LLDALDELGIPYVRIAP----GTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIaGPPDHGA---SAERLEGFRDAL 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 148 AE---EKYRGVVYQGLETapenWQHAQNRLADWLQTLPPQTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELT 224
Cdd:cd01545  145 AEaglPLDPDLVVQGDFT----FESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIA 220
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446381959 225 RYLSRvALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVPPvRVIARRS 276
Cdd:cd01545  221 RLVWP-PLTTVRQPIAEMARRAVELLIAAIRGAPAGPERETLPH-ELVIRES 270
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
99-274 5.03e-11

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: 62.66  E-value: 5.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  99 IATDNHALVESAFLHLKEKGVNRFAF-YGLPDSSRkhwAAEREYAFRQLVAEekyrgvvyQGLETaPENWQH-------- 169
Cdd:cd06280   96 VAGDNREGAYKAVKHLIELGHRRIGLiTGPLEIST---TRERLAGYREALAE--------AGIPV-DESLIFegdstieg 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 170 AQNRLADWLQTLPPQTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRyLSRVALSSVAQGARQMGYQAAKL 249
Cdd:cd06280  164 GYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFE-IVDPPLTVVAQPAYEIGRIAAQL 242
                        170       180
                 ....*....|....*....|....*
gi 446381959 250 LHRLLAREEMPLQRILVPPvRVIAR 274
Cdd:cd06280  243 LLERIEGQGEEPRRIVLPT-ELIIR 266
PBP1_GalS-like cd06270
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ...
72-274 1.78e-10

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


Pssm-ID: 380494 [Multi-domain]  Cd Length: 266  Bit Score: 61.00  E-value: 1.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  72 LLADVDVPIVGVGgsYHLAEnyPAVHYIATDNHALVESAFLHLKEKGVNRFAFYGLPDSsrKHWAAEREYAFRQLVAEek 151
Cdd:cd06270   73 LIAEKIPPLVVIN--RYIPG--LADRCVWLDNEQGGRLAAEHLLDLGHRRIACITGPLD--IPDARERLAGYRDALAE-- 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 152 yrgvvyQGLETAPE-----NWQHAQNRLAdwLQTL----PPQTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEE 222
Cdd:cd06270  145 ------AGIPLDPSliiegDFTIEGGYAA--AKQLlargLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVP 216
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446381959 223 LTRYLSrVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVPpvRVIAR 274
Cdd:cd06270  217 LARYLS-PKLTTVHYPIEEMAQAAAELALNLAYGEPLPISHEFTP--TLIER 265
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
78-276 2.90e-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: 60.65  E-value: 2.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  78 VPIVGVGGSYhlaENyPAVHYIATDNhalVESAFL---HLKEKGVNRFAFYGLPDSSRKHwaaEREYAFRQLVAEekyRG 154
Cdd:cd01541   84 IPVVFINSYY---PE-LDAPSVSLDD---EKGGYLatkHLIDLGHRRIAGIFKSDDLQGV---ERYQGFIKALRE---AG 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 155 VVYQ-----GLETAPENWQHAQNRLADWLQTLPPQTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYlSR 229
Cdd:cd01541  151 LPIDddrilWYSTEDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASL-SE 229
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 446381959 230 VALSSVAQGARQMGYQAAKLLHRLLaREEMPLQRILVPPvRVIARRS 276
Cdd:cd01541  230 PPLTSVVHPKEELGRKAAELLLRMI-EEGRKPESVIFPP-ELIERES 274
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
69-271 3.34e-10

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: 60.71  E-value: 3.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  69 IAQLLADVDVPIVGVGGSyhlAENYPAVHYIATDN--------HALVEsaflHLKEKGvNRFAFYGLPDSSrkhWAAERE 140
Cdd:COG1879  106 ALKKAKAAGIPVVTVDSD---VDGSDRVAYVGSDNyaagrlaaEYLAK----ALGGKG-KVAILTGSPGAP---AANERT 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 141 YAFRQLVAEekYRGVVYQGLETAPENWQHAQNRLADWLQTLPPQTGIIAVTDARARHVLQACEHLHIPvpEKLCVIGID- 219
Cdd:COG1879  175 DGFKEALKE--YPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRK--GDVKVVGFDg 250
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446381959 220 NEELTRYL-SRVALSSVAQGARQMGYQAAKLLHRLLAREEMPlQRILVPPVRV 271
Cdd:COG1879  251 SPEALQAIkDGTIDATVAQDPYLQGYLAVDAALKLLKGKEVP-KEILTPPVLV 302
PBP1_CcpB-like cd06286
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ...
92-260 9.03e-10

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: 58.71  E-value: 9.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  92 NYPAVHYIATDNHALVESAFLHLKEKGVNRFAF-YGLPDSSRKHwAAEREYAFRQLVAEEKyrgvvyqglETAPENWQ-- 168
Cdd:cd06286   87 DSPDIPSVYIDRYEAYLEALEYLKEKGHRKIGYcLGRPESSSAS-TQARLKAYQDVLGEHG---------LSLREEWIft 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 169 HAQN-----RLADWLQTLPPQ-TGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLsrvALSSVAQGARQM 242
Cdd:cd06286  157 NCHTiedgyKLAKKLLALKERpDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISELL---NLTTIDQPLEEM 233
                        170
                 ....*....|....*...
gi 446381959 243 GYQAAKLLHRLLAREEMP 260
Cdd:cd06286  234 GKEAFELLLSQLESKEPT 251
PBP1_LacI-like cd06299
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ...
46-276 3.74e-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: 3.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  46 RARIDNIKEWLGDGVIADYDDDDIAQLLADVD--VPIVGVGgsyHLAENYPAVHYIATDNHALVESAFLHLKEKGVNRFA 123
Cdd:cd06299   45 DESLEMLLSQRVDGIIAVPTGENSEGLQALIAqgLPVVFVD---REVEGLGGVPVVTSDNRPGAREAVEYLVSLGHRRIG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 124 FYGLPDSSRKhwAAEREYAFR------------QLVAEEKYRGVVyqGLEtapenwqhAQNRLadwLQTLPPQTGIIAVT 191
Cdd:cd06299  122 YISGPLSTST--GRERLAAFRaaltaagipideELVAFGDFRQDS--GAA--------AAHRL---LSRGDPPTALIAGD 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 192 DARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLSRvALSSVAQGARQMGYQAAKLLHRLLAREEMPlqRILVPPVRV 271
Cdd:cd06299  187 SLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSP-PLTVIAQPVERIGRRAVELLLALIENGGRA--TSIRVPTEL 263

                 ....*
gi 446381959 272 IARRS 276
Cdd:cd06299  264 IPRES 268
PBP1_CcpA_TTHA0807 cd06297
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ...
8-276 4.30e-09

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: 57.09  E-value: 4.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959   8 ITLLFNANKAYDRqVVEGGGEYLQASQSEWDIFIEEDfRARIDNIKE-----WLGDGVIADYDDddIAQLLADVDV---- 78
Cdd:cd06297    4 LLVPEVMTPFYMR-LLTGVERALDENRYDLAIFPLLS-EYRLEKYLRnstlaYQCDGLVMASLD--LTELFEEVIVptek 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  79 PIVGVGgsyhlaENYPAVHYIATDNHALVESAFLHLKEKGVNRFAFyglpdssrkhWAAEREYAFRQLVAEEKYRG---- 154
Cdd:cd06297   80 PVVLID------ANSMGYDCVYVDNVKGGFMATEYLAGLGEREYVF----------FGIEEDTVFTETVFREREQGflea 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 155 -------VVYQGLETAPENWQHAQNRLADWLQTLPPQTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTryl 227
Cdd:cd06297  144 lnkagrpISSSRMFRIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWA--- 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 446381959 228 SRVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVPPvRVIARRS 276
Cdd:cd06297  221 ASPGLTTVRQPVEEMGEAAAKLLLKRLNEYGGPPRSLKFEP-ELIVRES 268
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
58-265 6.77e-09

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: 56.35  E-value: 6.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  58 DGVI--ADYDDDDIAQLLADVDVPIVGVGGSYhlaENYPAVHYiatDNHALVESAFLHLKEKGVNRFAFYGLPdssrkhw 135
Cdd:cd01542   57 DGIIlfATEITDEHRKALKKLKIPVVVLGQEH---EGFSCVYH---DDYGAGKLLGEYLLKKGHKNIAYIGVD------- 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 136 aaEREYAfrqlVAEEKYRGVvYQGLETAPE----------NWQHAQNRLADWLQTLPPqTGIIAVTDARARHVLQACEHL 205
Cdd:cd01542  124 --EEDIA----VGVARKQGY-LDALKEHGIdeveivetdfSMESGYEAAKELLKENKP-DAIICATDNIALGAIKALREL 195
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 206 HIPVPEKLCVIGIDNEELTRYLSRvALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRIL 265
Cdd:cd01542  196 GIKIPEDISVAGFGGYDLSEFVSP-SLTTVKFDYEEAGEKAAELLLDMIEGEKVPKKQKL 254
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
98-269 1.19e-08

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: 55.65  E-value: 1.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  98 YIATDNHA--------LVEsaflHLKEKGvNRFAFYGLPDSSrkhWAAEREYAFRQlvAEEKYRGVVYqgLETAPENWQ- 168
Cdd:cd01536   99 FVGTDNYEagklageyLAE----ALGGKG-KVAILEGPPGSS---TAIDRTKGFKE--ALKKYPDIEI--VAEQPANWDr 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 169 -HAQNRLADWLQTLPPQTGIIAVTDARARHVLQACEHLHIPvpEKLCVIGIDN--EELTRYLSRVALSSVAQGARQMGYQ 245
Cdd:cd01536  167 aKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRT--GDIKIVGVDGtpEALKAIKDGELDATVAQDPYLQGYL 244
                        170       180
                 ....*....|....*....|....
gi 446381959 246 AAKLLHRLLAREEMPlQRILVPPV 269
Cdd:cd01536  245 AVEAAVKLLNGEKVP-KEILTPVT 267
ftrA PRK09393
transcriptional activator FtrA; Provisional
262-386 1.24e-08

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 56.13  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 262 QRILVPPVR-----------VIARRSTDYRSLtdpaviqaMHFIRNHACKGIKVEQVLDAVGISRSNLEKRFKEEVGETI 330
Cdd:PRK09393 192 RRLVVPPHRdggqaqfvprpVASRESDRLGPL--------IDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTP 263
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446381959 331 HALIHAEKLEKARSLLISTTLAINEISQMCGYPSLQYFYSVFKKEYVTTPKEYRDQ 386
Cdd:PRK09393 264 AEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRKR 319
PBP1_LacI-like cd06290
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
33-276 1.31e-08

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


Pssm-ID: 380513 [Multi-domain]  Cd Length: 267  Bit Score: 55.31  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  33 SQSEWDIFIEED-----FRARIDNIkewlgdgVIADYDDDDIAQLLADVDVPIVGVGGSyhlaENYPAVHYIATDNHALV 107
Cdd:cd06290   35 STSHWNADRELEilrllLARKVDGI-------IVVGGFGDEELLKLLAEGIPVVLVDRE----LEGLNLPVVNVDNEQGG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 108 ESAFLHLKEKGVNRFAFYGLPDSSRKhwAAEREYAFRQlVAEEKyrgvvyqGLETAPE-------NWQHAQNRLADWLQT 180
Cdd:cd06290  104 YNATNHLIDLGHRRIVHISGPEDHPD--AQERYAGYRR-ALEDA-------GLEVDPRlivegdfTEESGYEAMKKLLKR 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 181 LPPQTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLsRVALSSVAQGARQMGYQAAKLLHRLLAREEMP 260
Cdd:cd06290  174 GGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYT-TPPLTTVRQPLYEMGKTAAEILLELIEGKGRP 252
                        250
                 ....*....|....*.
gi 446381959 261 lQRILVPPVRVIARRS 276
Cdd:cd06290  253 -PRRIILPTELVIRES 267
PBP1_AglR_RafR-like cd06271
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ...
71-269 1.70e-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: 1.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  71 QLLADVDVPIVGVGGSyHLAENYPavhYIATDNHALVESAFLHLKEKGVNRFAFYGLPDSSRKHWAAEREYafrqlVAEE 150
Cdd:cd06271   74 QFLTKQNFPFVAHGRS-D*PIGHA---WVDIDNEAGAYEAVERLAGLGHRRIAFIVPPARYSPHDRRLQGY-----VRA* 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 151 KYRGVVYQGL--ETAPENWQHAQNRLadwLQTLPPQTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLS 228
Cdd:cd06271  145 RDAGLTGYPLdaDTTLEAGRAAAQRL---LALSPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSAPFLGAMI 221
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446381959 229 RVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVPPV 269
Cdd:cd06271  222 TPPLTTVHAPIAEAGRELAKALLARIDGEDPETLQVLVQPS 262
PBP1_LacI-like cd06287
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
69-276 2.34e-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: 54.73  E-value: 2.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  69 IAQLLADVDVPIVGVGGSYHLAENYPAVHYIATDNHALVesaFLHLKEKGVNRFAFygLPDSSRKHWAAEREYAFRQLVA 148
Cdd:cd06287   71 ILARLRQRGVPVVSIGRAPGTDEPVPYVDLQSAATARLL---LEHLHGAGARQVAL--LTGSSRRNSSLESEAAYLRFAQ 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 149 EEKYRGVVYQGLETAPENWQHAQNRLAdwLQTLPPQTGIIAVTDARARHVLQACEHLHIPVPEKLCVIgidneelTRY-- 226
Cdd:cd06287  146 EYGTTPVVYKVPESEGERAGYEAAAAL--LAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPEDLMVV-------TRYdg 216
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446381959 227 ----LSRVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRIlvPPVRVIARRS 276
Cdd:cd06287  217 irarTADPPLTAVDLHLDRVARTAIDLLFASLSGEERSVEVG--PAPELVVRAS 268
PBP1_LacI-like cd06282
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
58-265 3.52e-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: 380505 [Multi-domain]  Cd Length: 267  Bit Score: 54.21  E-value: 3.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  58 DGVI---ADYDDDDIAQLLADVDVPIVGVggsYHLAEN--YPAVhyiATDNHALVESAFLHLKEKGVNRFAFYGLP--DS 130
Cdd:cd06282   57 DGLIltvGDAQGSEALELLEEEGVPYVLL---FNQTENssHPFV---SVDNRLASYDVAEYLIALGHRRIAMVAGDfsAS 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 131 SRkhwAAEREYAFRQLVAEEKY--RGVVYQGLETApenwQHAQNRLADWLQTLPPqTGIIAVTDARARHVLQACEHLHIP 208
Cdd:cd06282  131 DR---ARLRYQGYRDALKEAGLkpIPIVEVDFPTN----GLEEALTSLLSGPNPP-TALFCSNDLLALSVISALRRLGIR 202
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446381959 209 VPEKLCVIGIDNEELTRYLSRvALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRIL 265
Cdd:cd06282  203 VPDDVSVIGFDGIAIGELLTP-TLATVVQPSRDMGRAAADLLLAEIEGESPPTSIRL 258
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
294-335 4.92e-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: 48.69  E-value: 4.92e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 446381959  294 IRNHACKGIKVEQVLDAVGISRSNLEKRFKEEVGETIHALIH 335
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
PBP1_LacI-like cd06277
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
70-266 4.98e-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: 380500 [Multi-domain]  Cd Length: 275  Bit Score: 53.78  E-value: 4.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  70 AQLLADVDVPIVGVGGSYHlaenYPAVHYIATDNHALVESAFLHLKEKGVNRFAFygLPDSSRKHWAAEREYAFRQLVAE 149
Cdd:cd06277   77 IKLFQDVSIPVVVVDNYFE----DLNFDCVVIDNEDGAYEAVKYLVELGHTRIGY--LASSYRIKNFEERRRGFRKAMRE 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 150 ekyRGVVYQG-----LETAPENwqhAQNRLADWLQTLPPQ-TGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEEL 223
Cdd:cd06277  151 ---LGLSEDPepefvVSVGPEG---AYKDMKALLDTGPKLpTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPV 224
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 446381959 224 TRyLSRVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILV 266
Cdd:cd06277  225 SA-MVDPPLTTIHVPKEQMGKLAVRRLIEKIKDPDGGTLKILV 266
PBP1_CcpA cd06298
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ...
58-276 6.52e-08

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: 53.45  E-value: 6.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  58 DGVI--ADYDDDDIAQLLADVDVPIVGVGGSYHLAEnYPAVhyiATDNHALVESAFLHLKEKGVNRFAFYGLP---DSSR 132
Cdd:cd06298   57 DGIIfmGDELTEEIREEFKRSPVPVVLAGTVDSDHE-IPSV---NIDYEQAAYDATKSLIDKGHKKIAFVSGPlkeYINN 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 133 KHWAAEREYAFRQ--LVAEEKY----RGVVYQGLETAPEnwqhaqnrladwLQTLPPQTGIIAVTDARARHVLQACEHLH 206
Cdd:cd06298  133 DKKLQGYKRALEEagLEFNEPLifegDYDYDSGYELYEE------------LLESGEPDAAIVVRDEIAVGLLNAAQDRG 200
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446381959 207 IPVPEKLCVIGIDNeelTRY--LSRVALSSVAQGARQMGYQAAKLLHRLLAREEMpLQRILVPPVRVIARRS 276
Cdd:cd06298  201 LKVPEDLEIIGFDN---TRYatMSRPQLTSINQPLYDIGAVAMRLLTKLMNKEEV-EETIVKLPHSIIWRQS 268
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
304-383 6.59e-08

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 53.53  E-value: 6.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 304 VEQVLDAVGISRSNLEKRFKEEVGETIHALIHAeKLEKARSLLISTTLAINEISQMCGYPSLQYFYSVFKKEYVTTPKEY 383
Cdd:PRK15186 200 LKDISDSLYMSCSTLKRKLKQENTSFSEVYLNA-RMNKATKLLRNSEYNITRVAYMCGYDSASYFTCVFKKHFKTTPSEF 278
PBP1_LacI-like cd19974
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
72-276 7.99e-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: 380629 [Multi-domain]  Cd Length: 270  Bit Score: 52.94  E-value: 7.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  72 LLADVDVPIVGVGgsyHLAENYPAvHYIATDNhalVESAFL---HLKEKGVNRFAFYGLPDSSRKHWaaEREYAFRQLVA 148
Cdd:cd19974   75 KLKELGIPVVLVD---HYDEELNA-DSVLSDN---YYGAYKltsYLIEKGHKKIGFVGDINYTSSFM--DRYLGYRKALL 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 149 EekyrgvvyQGLETAPENW----QHAQNRLADWLQtLPPQ----TGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDN 220
Cdd:cd19974  146 E--------AGLPPEKEEWlledRDDGYGLTEEIE-LPLKlmlpTAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDN 216
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446381959 221 EELTRYLSrVALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILVpPVRVIARRS 276
Cdd:cd19974  217 IELAELST-PPLTTVEVDKEAMGRRAVEQLLWRIENPDRPFEKILV-SGKLIERDS 270
PRK10371 PRK10371
transcriptional regulator MelR;
252-384 9.02e-08

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 53.28  E-value: 9.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 252 RLLAREEMPL----------QRILVPPVRVIARRSTDYRSLTdpAVIQAMHFIRNHACKGIKVEQVLDAVGISRSNLEKR 321
Cdd:PRK10371 150 RQLAIDEIGLmlkrfslsgwEPILVNKTSRTHKNSVSRHAQF--YVSQMLGFIAENYDQALTINDVAEHVKLNANYAMGI 227
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446381959 322 FKEEVGETIHALIHAEKLEKARSLLISTTLAINEISQMCGYPSLQYFYSVFKKEYVTTPKEYR 384
Cdd:PRK10371 228 FQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSSRFYSTFGKYVGMSPQQYR 290
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
287-386 9.22e-08

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 49.92  E-value: 9.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 287 VIQAM-HFIRNHACKGIKVEQVLDAVGISRSNLEKRFKEEVGETIHALIHAEKLEKARSLLISTTLAINEISQMCGYPSL 365
Cdd:PRK10219   6 IIQTLiAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYVSQ 85
                         90       100
                 ....*....|....*....|.
gi 446381959 366 QYFYSVFKKEYVTTPKEYRDQ 386
Cdd:PRK10219  86 QTFSRVFRRQFDRTPSDYRHR 106
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
313-391 1.19e-07

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 52.62  E-value: 1.19e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446381959 313 ISRSNLEKRFKEEvGETIHALIHAEKLEKARSLLISTTLAINEISQMCGYPSLQYFYSVFKKEYVTTPKEYRDQHSEAL 391
Cdd:PRK09978 170 MSPSLLKKKLREE-ETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFRNYYGMTPTEYQERSAQGL 247
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
234-391 1.76e-07

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 51.99  E-value: 1.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 234 SVAQGARQMGYQAAKL-----LHRLLAREEMPLQrilvppVRVIARRSTDYRSLTDPA--VIQAMHFIRNHACKGIKVEQ 306
Cdd:PRK13503 119 SVLQQVRQLVAQMEQQeesndLEAIASREILFMQ------LLVLLRKSSLQENGENSDarLNQLLAWLEDHFAEEVNWEA 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 307 VLDAVGISRSNLEKRFKEEVGETIHALIHAEKLEKARSLLISTTLAINEISQMCGYPSLQYFYSVFKKEYVTTPKEYRDQ 386
Cdd:PRK13503 193 LADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGDSNHFSTLFRREFSWSPRDIRQG 272

                 ....*
gi 446381959 387 HSEAL 391
Cdd:PRK13503 273 RDGFL 277
PBP1_CelR cd06295
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ...
58-276 2.16e-07

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: 51.87  E-value: 2.16e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  58 DGVIADYDDDDIAQL--LADVDVPIVGVGGSyhlaENYPAVHYIATDNHALVESAFLHLKEKGVNRFAFYGLPDSsrkhw 135
Cdd:cd06295   65 DGLIVLGQGLDHDALreLAQQGLPMVVWGAP----EDGQSYCSVGSDNVKGGALATEHLIEIGRRRIAFLGDPPH----- 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 136 aaeREYAFRqlvaeekYRGVVyQGLETAPENWQHAQNRLADW------------LQTLPPQTGIIAVTDARARHVLQACE 203
Cdd:cd06295  136 ---PEVADR-------LQGYR-DALAEAGLEADPSLLLSCDFteesgyaamralLDSGTAFDAIFAASDLIAMGAIRALR 204
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446381959 204 HLHIPVPEKLCVIGIDNEELTRYlSRVALSSVAQGARQMGYQAAKLLHRLLAREemPLQRILVpPVRVIARRS 276
Cdd:cd06295  205 ERGISVPGDVAVVGYDDIPLAAY-FRPPLTTVRQDLALAGRLLVEKLLALIAGE--PVTSSML-PVELVVRES 273
lacI PRK09526
lac repressor; Reviewed
43-277 3.49e-07

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 51.53  E-value: 3.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  43 EDFRARIDNIKEWLGDGVI-----ADYDDDDIAQLLADV-----DVPivgvggsyhlaeNYPAVHYIATDNHALVESAFL 112
Cdd:PRK09526 107 EACQAAVNELLAQRVSGVIinvplEDADAEKIVADCADVpclflDVS------------PQSPVNSVSFDPEDGTRLGVE 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 113 HLKEKGVNRFAFYGLPDSS-----R-KHWAAEREYAFRQLVAeekyrgvVYQGLETAPENWQHAQNRLADwlQTLPpqTG 186
Cdd:PRK09526 175 HLVELGHQRIALLAGPESSvsarlRlAGWLEYLTDYQLQPIA-------VREGDWSAMSGYQQTLQMLRE--GPVP--SA 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 187 IIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLSRvALSSVAQGARQMGYQAAKLLHRLLAREEMPLQRILv 266
Cdd:PRK09526 244 ILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIP-PLTTIKQDFRLLGKEAVDRLLALSQGQAVKGSQLL- 321
                        250
                 ....*....|.
gi 446381959 267 pPVRVIARRST 277
Cdd:PRK09526 322 -PTSLVVRKST 331
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
303-383 5.08e-07

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 50.76  E-value: 5.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 303 KVEQVLDAVGISRSNLEKRFKEEvGETIHALIHAEKLEKARSLLISTTLAINEISQMCGYPSLQYFYSVFKKEYVTTPKE 382
Cdd:PRK15185 224 KLTDVADHIFMSTSTLKRKLAEE-GTSFSDIYLSARMNQAAKLLRIGNHNVNAVALKCGYDSTSYFIQCFKKYFKTTPST 302

                 .
gi 446381959 383 Y 383
Cdd:PRK15185 303 F 303
PRK09940 PRK09940
transcriptional regulator YdeO; Provisional
303-386 8.40e-07

transcriptional regulator YdeO; Provisional


Pssm-ID: 182157 [Multi-domain]  Cd Length: 253  Bit Score: 49.70  E-value: 8.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 303 KVEQVLDAVGISRSNLEKRFKEEVGETIHALIHAeKLEKARSLlISTTLAINEISQMCGYPSLQYFYSVFKKEYVTTP-- 380
Cdd:PRK09940 152 KLKDICDCLYISESLLKKKLKQEQTTFSQILLDA-RMQHAKNL-IRVEGSVNKIAEQCGYASTSYFIYAFRKHFGNSPkr 229

                 ....*...
gi 446381959 381 --KEYRDQ 386
Cdd:PRK09940 230 vsKEYRCQ 237
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
347-384 1.96e-06

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


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 44.07  E-value: 1.96e-06
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 446381959  347 ISTTLAINEISQMCGYpSLQYFYSVFKKEYVTTPKEYR 384
Cdd:pfam00165   5 LSTNLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYR 41
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
304-389 3.01e-06

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 48.56  E-value: 3.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 304 VEQVLDAVGISRSNLEKRFKEEVGETIHALIHAEKLEKARSLLISTTLAINEISQMCGYPSLQYFYSVFKKEYVTTPKEY 383
Cdd:PRK13500 225 LDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDSNYFSVVFTRETGMTPSQW 304

                 ....*.
gi 446381959 384 RDQHSE 389
Cdd:PRK13500 305 RHLNSQ 310
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
314-384 6.72e-06

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 47.36  E-value: 6.72e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446381959 314 SRSNLEKRFKEEVGETIHALIHAEKLEKARSLLISTTLAINEISQMCGYPSLQYFYSVFKKEYVTTPKEYR 384
Cdd:PRK13502 205 SERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWR 275
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
313-386 8.02e-06

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 47.21  E-value: 8.02e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446381959 313 ISRSNLEKRFKEEVGETIHALIHAEKLEKARSLLISTTLAINEISQMCGYPSLQYFYSVFKKEYVTTPKEYRDQ 386
Cdd:PRK13501 204 LVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFSAVFTREAGMTPRDYRQR 277
PBP1_LacI-like cd06281
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
58-276 1.13e-05

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: 46.46  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  58 DGVIADY---DDDDIAQLLADVDVPIVGVGGSyhLAENYPAVhyiATDnHAL-VESAFLHLKEKGVNRFAfygLPDSSRK 133
Cdd:cd06281   57 DGLILTPgdeDDPELAAALARLDIPVVLIDRD--LPGDIDSV---LVD-HRSgVRQATEYLLSLGHRRIA---LLTGGPD 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 134 HWAA-EREYAFRQLVAEekyrgvvyQGLETAPE-------NWQHAQNRLADWLQTLPPQTGIIAVTDARARHVLQACEHL 205
Cdd:cd06281  128 IRPGrERIAGFKAAFAA--------AGLPPDPDlvrlgsfSADSGFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAA 199
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446381959 206 HIPVPEKLCVIGIDNEELTRYLSRvALSSVAQGARQMGYQAAK-LLHRLLAREEMPLQRILVPPvRVIARRS 276
Cdd:cd06281  200 GLRIPGDLSVVSIGDSDLAELHDP-PITAIRWDLDAVGRAAAElLLDRIEGPPAGPPRRIVVPT-ELILRDS 269
PRK10703 PRK10703
HTH-type transcriptional repressor PurR;
164-280 3.96e-05

HTH-type transcriptional repressor PurR;


Pssm-ID: 236739 [Multi-domain]  Cd Length: 341  Bit Score: 45.10  E-value: 3.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 164 PENWQHAQNRLADwLQTLPpqTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLSRvALSSVAQGARQMG 243
Cdd:PRK10703 223 PESGYEAMQQILS-QKHRP--TAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTP-ALTTIHQPKDRLG 298
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 446381959 244 YQAAK-LLHRLLAREEMPlQRILVPPvRVIARRST------DYR 280
Cdd:PRK10703 299 ETAFNmLLDRIVNKREEP-QTIEVHP-RLVERRSVadgpfrDYR 340
PRK11041 PRK11041
DNA-binding transcriptional regulator CytR; Provisional
178-250 4.65e-05

DNA-binding transcriptional regulator CytR; Provisional


Pssm-ID: 182923 [Multi-domain]  Cd Length: 309  Bit Score: 44.99  E-value: 4.65e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446381959 178 LQTLP-PQTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYlSRVALSSVAQGARQMGYQAAKLL 250
Cdd:PRK11041 207 LLDLPqPPTAVFCHSDVMALGALSQAKRMGLRVPQDLSIIGFDDIDLAQY-CDPPLTTVAQPRYEIGREAMLLL 279
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
69-275 1.31e-04

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


Pssm-ID: 380542 [Multi-domain]  Cd Length: 278  Bit Score: 43.50  E-value: 1.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  69 IAQLLADVDVPIV----GVGGSYHLAenypavhYIATDNHalvESAFL-------HLKEKGV--NRFAFYGLPDSSRkhW 135
Cdd:cd06319   72 VLDLANEAKIPVViadiGTGGGDYVS-------YIISDNY---DGGYQageylaeALKENGWggGSVGIIAIPQSRV--N 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 136 AAEREYAFRQLVAEEKYRGVVYQ--GLETAPENWQHAQnrlaDWLQTLPPQTGIIAVTDARARHVLQACEHLHipVPEKL 213
Cdd:cd06319  140 GQARTAGFEDALEEAGVEEVALRqtPNSTVEETYSAAQ----DLLAANPDIKGIFAQNDQMAQGALQAIEEAG--RTGDI 213
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446381959 214 CVIGID-NEELTRYLSRVALS-SVAQGARQMGYQAAKLLHRLLAREEMPLQRILVpPVRVIARR 275
Cdd:cd06319  214 LVVGFDgDPEALDLIKDGKLDgTVAQQPFGMGARAVELAIQALNGDNTVEKEIYL-PVLLVTSE 276
PRK10423 PRK10423
transcriptional repressor RbsR; Provisional
182-276 2.38e-04

transcriptional repressor RbsR; Provisional


Pssm-ID: 182448 [Multi-domain]  Cd Length: 327  Bit Score: 42.76  E-value: 2.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 182 PPQtGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEELTRYLSRvALSSVAQGARQMGYQAAK-LLHRlLAREEMP 260
Cdd:PRK10423 235 RPQ-AVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTP-PLTTIHQPKDELGELAIDvLIHR-MAQPTLQ 311
                         90
                 ....*....|....*.
gi 446381959 261 LQRILVPPVrVIARRS 276
Cdd:PRK10423 312 QQRLQLTPE-LMERGS 326
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
71-258 1.42e-03

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: 39.92  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  71 QLLADVDVPIV----GVGGSYHLAenypavhYIATDNHALVESAFLHLKE--KGVNRFAFYGLPDSSRKhwAAEREYAFR 144
Cdd:cd20005   76 EKAKEKGIPVVtfdsGVPSDLPLA-------TVATDNYAAGALAADHLAEliGGKGKVAIVAHDATSET--GIDRRDGFK 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 145 QLVaEEKYRG-----VVYQGLETapenwQHAQNRLADWLQTLPPQTGIIAVTDARARHVLQACEHLHipVPEKLCVIGID 219
Cdd:cd20005  147 DEI-KEKYPDikvvnVQYGVGDH-----AKAADIAKAILQANPDLKGIYATNEGAAIGVANALKEMG--KLGKIKVVGFD 218
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 446381959 220 NEELT-RYL-SRVALSSVAQGARQMGYQAAKLLHRLLAREE 258
Cdd:cd20005  219 SGEAQiDAIkNGVIAGSVTQNPYGMGYKTVKAAVKALKGEE 259
PBP1_hexuronate_repressor-like cd06272
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ...
78-267 1.70e-03

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: 39.66  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  78 VPIVGVGgsyHLAENYPAVHyiaTDNHALVESAFLHLKEKGVNRFAFYGLPDSSRKHwaAEREYAFRQLVAEEK----YR 153
Cdd:cd06272   80 IPIVLYN---RESPKYSTVN---VDNEKAGRLAVLLLIQKGHKSIAYIGNPNSNRNQ--TLRGKGFIETCEKHGihlsDS 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 154 GVVYQGLETapENWQHAQNRLADwLQTLPpqTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNeELTRYLSRVALS 233
Cdd:cd06272  152 IIDSRGLSI--EGGDNAAKKLLK-KKTLP--KAIFCNSDDIALGVLRVLKENGISIPEDISIVSYDN-IPQEARSDPPLT 225
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446381959 234 SVAQGARQMGYQAAKLLHRLL-AREEMPLQRILVP 267
Cdd:cd06272  226 VVGVPIEKIAEESLRLILKLIeGRENEIQQLILYP 260
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
98-274 2.19e-03

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: 39.52  E-value: 2.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  98 YIATDNHALVESAFLH----LKEKG---VNRFAfyglPDSSRkhwAAEREYAFRQ---------LVAEEKYRGVvyqgle 161
Cdd:cd20004  100 FVATDNYAAGRLAAKRmaklLNGKGkvaLLRLA----KGSAS---TTDRERGFLEalkklapglKVVDDQYAGG------ 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 162 TAPEnwqhAQNRLADWLQTLPPQTGIIAVTDARARHVLQACEHlhIPVPEKLCVIGID-NEELTRYLSRVALSS-VAQGA 239
Cdd:cd20004  167 TVGE----ARSSAENLLNQYPDVDGIFTPNESTTIGALRALRR--LGLAGKVKFIGFDaSDLLLDALRAGEISAlVVQDP 240
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 446381959 240 RQMGYQAAKLLHRLLaREEMPLQRIlVPPVRVIAR 274
Cdd:cd20004  241 YRMGYLGVKTAVAAL-RGKPVPKRI-DTGVVLVTK 273
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
176-268 5.14e-03

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


Pssm-ID: 380545 [Multi-domain]  Cd Length: 270  Bit Score: 38.41  E-value: 5.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 176 DWLQTLPPQTGIIAVTDARARHVLQACEHLHipVPEKLCVIGID-NEELTRYLSR--VALSSVAQGARQMGYQAAKLLHR 252
Cdd:cd06322  174 DMLQANPDLDGIFAIGDPAALGALTAIESAG--KEDKIKVIGFDgNPEAIKAIAKggKIKADIAQQPDKIGQETVEAIVK 251
                         90
                 ....*....|....*.
gi 446381959 253 LLAREEMPLQrILVPP 268
Cdd:cd06322  252 YLAGETVEKE-ILIPP 266
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
74-260 5.76e-03

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: 38.09  E-value: 5.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959  74 ADVDVPIV----GVGGSYHLAenypavhYIATDNHALVESA----FLHLKEKG---VNRFAfyglPDSSRkhwAAEREYA 142
Cdd:cd06310   79 KDKGIPVIvidsGIKGDAYLS-------YIATDNYAAGRLAaqklAEALGGKGkvaVLSLT----AGNST---TDQREEG 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446381959 143 FRQLVAEEkYRGVVYQGLETAPENWQHAQNRLADWLQTLPPQTGIIAVTDARARHVLQACEHLHIPVPEKLCVIGIDNEE 222
Cdd:cd06310  145 FKEYLKKH-PGGIKVLASQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGQIKIVGFDSQEEL 223
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 446381959 223 LTRYLSRVALSSVAQGARQMGYQAAKLLHRLLAREEMP 260
Cdd:cd06310  224 LDALKNGKIDALVVQNPYEIGYEGIKLALKLLKGEEVP 261
 
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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