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Conserved domains on  [gi|15829896|ref|NP_308669|]
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transcriptional regulator [Escherichia coli O157:H7 str. Sakai]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11482 super family cl32694
DNA-binding transcriptional regulator;
7-300 3.82e-39

DNA-binding transcriptional regulator;


The actual alignment was detected with superfamily member PRK11482:

Pssm-ID: 183159 [Multi-domain]  Cd Length: 317  Bit Score: 139.47  E-value: 3.82e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896    7 LKKFDLNLLVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTGLNLHHHLEKNLRGLEQ 86
Cdd:PRK11482  26 LRNIDLNLLTIFEAVYVHKGIVNAAKILNLTPSAISQSIQKLRVIFPDPLFIRKGQGVTPTAYATHLHEYISQGLESILG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896   87 TINIVNKSELKKNFIIHGPQLISCSNNSMLIRCLRQDSSvEIECHDILMSaeNAEELLVHRKADLVITQMPVISRSVICM 166
Cdd:PRK11482 106 ALDITGSYDKQRTITIATTPSVGALVMPVIYQAIKTHYP-QLLLRNIPIS--DAENQLSQFQTDLIIDTHSCSNRTIQHH 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896  167 PLHTIRNTLICSNRHPRITDNSTYEQIMAEEFTQLISKSAGVDDIQMEIDERFMNRKISFRGSSLLTIINSIAVTDLLGI 246
Cdd:PRK11482 183 VLFTDNVVLVCRQGHPLLSLEDDEETLDNAEHTLLLPEGQNFSGLRQRLQEMFPDRQISFSSYNILTIAALIASSDMLGI 262

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15829896  247 VPYELYNSHRDFLNLKEIKLeHPL--PSIKLYISYNKSSLNNLVFSRFIDRLNECF 300
Cdd:PRK11482 263 MPSRFYNLFSRCWPLEKLPF-PSLneEQIDFSLHYNKLSLRDPVLENVIDVIRNAF 317
 
Name Accession Description Interval E-value
PRK11482 PRK11482
DNA-binding transcriptional regulator;
7-300 3.82e-39

DNA-binding transcriptional regulator;


Pssm-ID: 183159 [Multi-domain]  Cd Length: 317  Bit Score: 139.47  E-value: 3.82e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896    7 LKKFDLNLLVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTGLNLHHHLEKNLRGLEQ 86
Cdd:PRK11482  26 LRNIDLNLLTIFEAVYVHKGIVNAAKILNLTPSAISQSIQKLRVIFPDPLFIRKGQGVTPTAYATHLHEYISQGLESILG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896   87 TINIVNKSELKKNFIIHGPQLISCSNNSMLIRCLRQDSSvEIECHDILMSaeNAEELLVHRKADLVITQMPVISRSVICM 166
Cdd:PRK11482 106 ALDITGSYDKQRTITIATTPSVGALVMPVIYQAIKTHYP-QLLLRNIPIS--DAENQLSQFQTDLIIDTHSCSNRTIQHH 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896  167 PLHTIRNTLICSNRHPRITDNSTYEQIMAEEFTQLISKSAGVDDIQMEIDERFMNRKISFRGSSLLTIINSIAVTDLLGI 246
Cdd:PRK11482 183 VLFTDNVVLVCRQGHPLLSLEDDEETLDNAEHTLLLPEGQNFSGLRQRLQEMFPDRQISFSSYNILTIAALIASSDMLGI 262

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15829896  247 VPYELYNSHRDFLNLKEIKLeHPL--PSIKLYISYNKSSLNNLVFSRFIDRLNECF 300
Cdd:PRK11482 263 MPSRFYNLFSRCWPLEKLPF-PSLneEQIDFSLHYNKLSLRDPVLENVIDVIRNAF 317
LysR COG0583
DNA-binding transcriptional regulator, LysR family [Transcription];
10-300 4.70e-33

DNA-binding transcriptional regulator, LysR family [Transcription];


Pssm-ID: 440348 [Multi-domain]  Cd Length: 256  Bit Score: 121.90  E-value: 4.70e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896  10 FDLNLLVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTGLNLHHHLEKNLRGLEQTIN 89
Cdd:COG0583   1 MDLRQLRAFVAVAEEGSFTAAAERLGVSQPAVSRQIRRLEEELGVPLFERTGRGLRLTEAGERLLERARRILAELEEAEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896  90 IVN--KSELKKNFIIHGPQLIScsnNSMLIRCL----RQDSSVEIECHdiLMSAENAEELLVHRKADLVITQMPVISRSV 163
Cdd:COG0583  81 ELRalRGGPRGTLRIGAPPSLA---RYLLPPLLarfrARHPGVRLELR--EGNSDRLVDALLEGELDLAIRLGPPPDPGL 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896 164 ICMPLHTIRNTLICSNRHPritdnstyeqimaeeftqLISKSAGVDDIQmeiderfmnrkisfrgssllTIINSIAVTDL 243
Cdd:COG0583 156 VARPLGEERLVLVASPDHP------------------LARRAPLVNSLE--------------------ALLAAVAAGLG 197

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15829896 244 LGIVPYELYNSHRDFLNLKEIKLEHPLPSIKLYISYNKSSLNNLVFSRFIDRLNECF 300
Cdd:COG0583 198 IALLPRFLAADELAAGRLVALPLPDPPPPRPLYLVWRRRRHLSPAVRAFLDFLREAL 254
HTH_1 pfam00126
Bacterial regulatory helix-turn-helix protein, lysR family;
12-70 1.89e-20

Bacterial regulatory helix-turn-helix protein, lysR family;


Pssm-ID: 459683 [Multi-domain]  Cd Length: 60  Bit Score: 82.82  E-value: 1.89e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15829896    12 LNLLVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTG 70
Cdd:pfam00126   1 LRQLRLFVAVAETGSFTAAAERLGLSQPAVSRQIKRLEEELGVPLFERTTRGVRLTEAG 59
PBP2_LeuO cd08466
The C-terminal substrate binding domain of LysR-type transcriptional regulator LeuO, an ...
 138-286 7.64e-16

The C-terminal substrate binding domain of LysR-type transcriptional regulator LeuO, an activator of leucine synthesis operon, contains the type 2 periplasmic binding fold; LeuO, a LysR-type transcriptional regulator, was originally identified as an activator of the leucine synthesis operon (leuABCD). Subsequently, LeuO was found to be not a specific regulator of the leu gene but a global regulator of unrelated various genes. LeuO activates bglGFB (utilization of beta-D-glucoside) and represses cadCBA (lysine decarboxylation) and dsrA (encoding a regulatory small RNA for translational control of rpoS and hns). LeuO also regulates the yjjQ-bglJ operon which coding for a LuxR-type transcription factor. In Salmonella enterica serovar Typhi, LeuO is a positive regulator of ompS1 (encoding an outer membrane), ompS2 (encoding a pathogenicity determinant), and assT, while LeuO represses the expression of OmpX and Tpx. Both osmS1 and osmS2 influence virulence in the mouse model of Salmonella. In Vibrio cholerae, LeuO is involved in control of biofilm formation and in the stringent response. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 176155 [Multi-domain]  Cd Length: 200  Bit Score: 74.21  E-value: 7.64e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896 138 ENAEELLVHRKADLVITQMPVISRSVICMPLHTIRNTLICSNRHPRITDNSTYEQIMAEEFTQLISKSAGVDDIQMEIDE 217
Cdd:cd08466  39 EDLFEDLRLQEVDLVIDYVPFRDPSFKSELLFEDELVCVARKDHPRIQGSLSLEQYLAEKHVVLSLRRGNLSALDLLTEE 118

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829896 218 RFMNRKISFRGSSLLTIINSIAVTDLLGIVPYELYNSHRDFLNLKEIKLEHPLPSIKLYISYNKSSLNN 286
Cdd:cd08466 119 VLPQRNIAYEVSSLLSMLAVVSQTDLIAIAPRWLADQYAEQLNLQILPLPFKTKPIPLYMVWHKSRERD 187
argP TIGR03298
transcriptional regulator, ArgP family; ArgP used to be known as IciA. ArgP is a positive ...
 10-86 1.72e-07

transcriptional regulator, ArgP family; ArgP used to be known as IciA. ArgP is a positive regulator of argK. It is a negative autoregulator in presence of arginine. It competes with DnaA for oriC iteron (13-mer) binding. It activates dnaA and nrd transcription. It has been demonstrated to be part of the pho regulon (). ArgP mutants convey canavanine (an L-arginine structural homolog) sensitivity. [Cellular processes, Toxin production and resistance, DNA metabolism, DNA replication, recombination, and repair, Regulatory functions, DNA interactions]


Pssm-ID: 274509 [Multi-domain]  Cd Length: 292  Bit Score: 51.46  E-value: 1.72e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829896    10 FDLNLLVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRsGKGIAPTTTGLNLHHHLEKnLRGLEQ 86
Cdd:TIGR03298   1 LDYRQLAALAAVVEEGSFERAAAALSVTPSAVSQRIKALEERLGQPLLVR-TQPCRATEAGQRLLRHARQ-VRLLEA 75
decaheme_TF NF041036
multiheme cytochrome-associated LysR family transcriptional regulator; Members of this family, ...
 26-71 2.26e-07

multiheme cytochrome-associated LysR family transcriptional regulator; Members of this family, including founding member GSU2202 from Geobacter sulfurreducens PCA, are LysR family transcriptional regulators found regularly in the vicinity of multiheme cytochromes such as GSU2203, a decaheme c-type cytochrome.


Pssm-ID: 468965 [Multi-domain]  Cd Length: 301  Bit Score: 51.28  E-value: 2.26e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 15829896   26 SISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTGL 71
Cdd:NF041036  17 SFSKAAEKLHLTQSAVSQRIKFLEECYGYQLFDRSGPSLEPTAAGE 62
 
Name Accession Description Interval E-value
PRK11482 PRK11482
DNA-binding transcriptional regulator;
7-300 3.82e-39

DNA-binding transcriptional regulator;


Pssm-ID: 183159 [Multi-domain]  Cd Length: 317  Bit Score: 139.47  E-value: 3.82e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896    7 LKKFDLNLLVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTGLNLHHHLEKNLRGLEQ 86
Cdd:PRK11482  26 LRNIDLNLLTIFEAVYVHKGIVNAAKILNLTPSAISQSIQKLRVIFPDPLFIRKGQGVTPTAYATHLHEYISQGLESILG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896   87 TINIVNKSELKKNFIIHGPQLISCSNNSMLIRCLRQDSSvEIECHDILMSaeNAEELLVHRKADLVITQMPVISRSVICM 166
Cdd:PRK11482 106 ALDITGSYDKQRTITIATTPSVGALVMPVIYQAIKTHYP-QLLLRNIPIS--DAENQLSQFQTDLIIDTHSCSNRTIQHH 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896  167 PLHTIRNTLICSNRHPRITDNSTYEQIMAEEFTQLISKSAGVDDIQMEIDERFMNRKISFRGSSLLTIINSIAVTDLLGI 246
Cdd:PRK11482 183 VLFTDNVVLVCRQGHPLLSLEDDEETLDNAEHTLLLPEGQNFSGLRQRLQEMFPDRQISFSSYNILTIAALIASSDMLGI 262

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 15829896  247 VPYELYNSHRDFLNLKEIKLeHPL--PSIKLYISYNKSSLNNLVFSRFIDRLNECF 300
Cdd:PRK11482 263 MPSRFYNLFSRCWPLEKLPF-PSLneEQIDFSLHYNKLSLRDPVLENVIDVIRNAF 317
LysR COG0583
DNA-binding transcriptional regulator, LysR family [Transcription];
10-300 4.70e-33

DNA-binding transcriptional regulator, LysR family [Transcription];


Pssm-ID: 440348 [Multi-domain]  Cd Length: 256  Bit Score: 121.90  E-value: 4.70e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896  10 FDLNLLVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTGLNLHHHLEKNLRGLEQTIN 89
Cdd:COG0583   1 MDLRQLRAFVAVAEEGSFTAAAERLGVSQPAVSRQIRRLEEELGVPLFERTGRGLRLTEAGERLLERARRILAELEEAEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896  90 IVN--KSELKKNFIIHGPQLIScsnNSMLIRCL----RQDSSVEIECHdiLMSAENAEELLVHRKADLVITQMPVISRSV 163
Cdd:COG0583  81 ELRalRGGPRGTLRIGAPPSLA---RYLLPPLLarfrARHPGVRLELR--EGNSDRLVDALLEGELDLAIRLGPPPDPGL 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896 164 ICMPLHTIRNTLICSNRHPritdnstyeqimaeeftqLISKSAGVDDIQmeiderfmnrkisfrgssllTIINSIAVTDL 243
Cdd:COG0583 156 VARPLGEERLVLVASPDHP------------------LARRAPLVNSLE--------------------ALLAAVAAGLG 197

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 15829896 244 LGIVPYELYNSHRDFLNLKEIKLEHPLPSIKLYISYNKSSLNNLVFSRFIDRLNECF 300
Cdd:COG0583 198 IALLPRFLAADELAAGRLVALPLPDPPPPRPLYLVWRRRRHLSPAVRAFLDFLREAL 254
HTH_1 pfam00126
Bacterial regulatory helix-turn-helix protein, lysR family;
12-70 1.89e-20

Bacterial regulatory helix-turn-helix protein, lysR family;


Pssm-ID: 459683 [Multi-domain]  Cd Length: 60  Bit Score: 82.82  E-value: 1.89e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 15829896    12 LNLLVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTG 70
Cdd:pfam00126   1 LRQLRLFVAVAETGSFTAAAERLGLSQPAVSRQIKRLEEELGVPLFERTTRGVRLTEAG 59
leuO PRK09508
leucine transcriptional activator; Reviewed
 7-283 1.96e-18

leucine transcriptional activator; Reviewed


Pssm-ID: 181918 [Multi-domain]  Cd Length: 314  Bit Score: 83.53  E-value: 1.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896    7 LKKFDLNLLVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTGlnlhhhleKNLRG-LE 85
Cdd:PRK09508  19 LRMVDLNLLTVFDAVMQEQNITRAAHNLGMSQPAVSNAVARLKVMFNDELFVRYGRGIQPTARA--------RQLFGpVR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896   86 QTINIVnKSEL----------KKNF---------IIHGPQLISCSNNSMLIRCLRQDSSVEiechdilmsaENAEELLVH 146
Cdd:PRK09508  91 QALQLV-QNELpgsgfepessERVFnlcicspldIRLTSQIYNRIEQIAPNIHVVFKSSLN----------QNIEHQLRY 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896  147 RKADLVITQMPVISRSVICMPLHTIRNTLICSNRHPRITDNSTYEQIMAEEFTQL-ISKSAGVDDIQMEIDErfMNRKIS 225
Cdd:PRK09508 160 QETEFVISYEEFDRPEFTSVPLFKDELVLVASKNHPRIKGPITEEQLYNEQHAVVsLDRFASFSQPWYDTVD--KQASIA 237

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15829896  226 FRGSSLLTIINSIAVTDLLGIVPYELYNSHRDFLNLKEIKLEHPLPSIKLYISYNKSS 283
Cdd:PRK09508 238 YQGTALSSVLNVVSQTHLVAIAPRWLAEEFAESLELQILPLPLKNNSRTCYLSWHESA 295
PBP2_LeuO cd08466
The C-terminal substrate binding domain of LysR-type transcriptional regulator LeuO, an ...
 138-286 7.64e-16

The C-terminal substrate binding domain of LysR-type transcriptional regulator LeuO, an activator of leucine synthesis operon, contains the type 2 periplasmic binding fold; LeuO, a LysR-type transcriptional regulator, was originally identified as an activator of the leucine synthesis operon (leuABCD). Subsequently, LeuO was found to be not a specific regulator of the leu gene but a global regulator of unrelated various genes. LeuO activates bglGFB (utilization of beta-D-glucoside) and represses cadCBA (lysine decarboxylation) and dsrA (encoding a regulatory small RNA for translational control of rpoS and hns). LeuO also regulates the yjjQ-bglJ operon which coding for a LuxR-type transcription factor. In Salmonella enterica serovar Typhi, LeuO is a positive regulator of ompS1 (encoding an outer membrane), ompS2 (encoding a pathogenicity determinant), and assT, while LeuO represses the expression of OmpX and Tpx. Both osmS1 and osmS2 influence virulence in the mouse model of Salmonella. In Vibrio cholerae, LeuO is involved in control of biofilm formation and in the stringent response. The topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 176155 [Multi-domain]  Cd Length: 200  Bit Score: 74.21  E-value: 7.64e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896 138 ENAEELLVHRKADLVITQMPVISRSVICMPLHTIRNTLICSNRHPRITDNSTYEQIMAEEFTQLISKSAGVDDIQMEIDE 217
Cdd:cd08466  39 EDLFEDLRLQEVDLVIDYVPFRDPSFKSELLFEDELVCVARKDHPRIQGSLSLEQYLAEKHVVLSLRRGNLSALDLLTEE 118

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829896 218 RFMNRKISFRGSSLLTIINSIAVTDLLGIVPYELYNSHRDFLNLKEIKLEHPLPSIKLYISYNKSSLNN 286
Cdd:cd08466 119 VLPQRNIAYEVSSLLSMLAVVSQTDLIAIAPRWLADQYAEQLNLQILPLPFKTKPIPLYMVWHKSRERD 187
PRK10216 PRK10216
HTH-type transcriptional regulator YidZ;
7-77 7.65e-16

HTH-type transcriptional regulator YidZ;


Pssm-ID: 182312 [Multi-domain]  Cd Length: 319  Bit Score: 76.40  E-value: 7.65e-16
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829896    7 LKKFDLNLLVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTGLNLHHHL 77
Cdd:PRK10216   5 LTTLDLNLLLCLQLLMQERSVTKAAKRMNVTPSAVSKSLAKLRAWFDDPLFVNTPLGLSPTPLMVSMEQNL 75
PBP2_Nitroaromatics_like cd08417
The C-terminal substrate binding domain of LysR-type transcriptional regulators that involved ...
 116-286 2.13e-11

The C-terminal substrate binding domain of LysR-type transcriptional regulators that involved in the catabolism of nitroaromatic/naphthalene compounds and that of related regulators; contains the type 2 periplasmic binding fold; This CD includes the C-terminal substrate binding domain of LysR-type transcriptional regulators involved in the catabolism of dinitrotoluene and similar compounds, such as DntR, NahR, and LinR. The transcription of the genes encoding enzymes involved in such degradation is regulated and expression of these enzymes is enhanced by inducers, which are either an intermediate in the metabolic pathway or compounds to be degraded. Also included are related LysR-type regulators clustered together in phylogenetic trees, including NodD, ToxR, LeuO, SyrM, TdcA, and PnbR. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 176109 [Multi-domain]  Cd Length: 200  Bit Score: 61.85  E-value: 2.13e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896 116 LIRCLRQDS-SVEIECHDIlmSAENAEELLVHRKADLVITQMPVISRSVICMPLHTIRNTLICSNRHPRITDNSTYEQIM 194
Cdd:cd08417  18 LLARLRQEApGVRLRFVPL--DRDDLEEALESGEIDLAIGVFPELPPGLRSQPLFEDRFVCVARKDHPLAGGPLTLEDYL 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896 195 AEE---FTQLISKSAGVDDIqmeIDERFMNRKISFRGSSLLTIINSIAVTDLLGIVPYELYNSHRDFLNLKEIKLEHPLP 271
Cdd:cd08417  96 AAPhvlVSPRGRGHGLVDDA---LAELGLSRRVALTVPHFLAAPALVAGTDLIATVPRRLAEALAERLGLRVLPLPFELP 172

                       170
                ....*....|....*
gi 15829896 272 SIKLYISYNKSSLNN 286
Cdd:cd08417 173 PFTVSLYWHPRRDRD 187
PBP2_DntR_NahR_LinR_like cd08459
The C-terminal substrate binding domain of LysR-type transcriptional regulators that are ...
 116-276 9.31e-10

The C-terminal substrate binding domain of LysR-type transcriptional regulators that are involved in the catabolism of dinitrotoluene, naphthalene and gamma-hexachlorohexane; contains the type 2 periplasmic binding fold; This CD includes LysR-like bacterial transcriptional regulators, DntR, NahR, and LinR, which are involved in the degradation of aromatic compounds. The transcription of the genes encoding enzymes involved in such degradation is regulated and expression of these enzymes is enhanced by inducers, which are either an intermediate in the metabolic pathway or compounds to be degraded. DntR from Burkholderia species controls genes encoding enzymes for oxidative degradation of the nitro-aromatic compound 2,4-dinitrotoluene. The active form of DntR is homotetrameric, consisting of a dimer of dimers. NahR is a salicylate-dependent transcription activator of the nah and sal operons for naphthalene degradation. Salicylic acid is an intermediate of the oxidative degradation of the aromatic ring in soil bacteria. LinR positively regulates expression of the genes (linD and linE) encoding enzymes for gamma-hexachlorocyclohexane (a haloorganic insecticide) degradation. Expression of linD and linE are induced by their substrates, 2,5-dichlorohydroquinone (2,5-DCHQ) and chlorohydroquinone (CHQ). The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 176148 [Multi-domain]  Cd Length: 201  Bit Score: 57.20  E-value: 9.31e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896 116 LIRCLRQDS-SVEIECHDIlmSAENAEELLVHRKADLVITQMPVISRSVICMPLHTIRNTLICSNRHPRITDNSTYEQIM 194
Cdd:cd08459  18 LLAALREVApGVRIETVRL--PVDELEEALESGEIDLAIGYLPDLGAGFFQQRLFRERYVCLVRKDHPRIGSTLTLEQFL 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896 195 AEEFTQLISKSAGVDDIQMEIDERFMNRKISFRGSSLLTIINSIAVTDLLGIVPYELYNSHRDFLNLKEIKLEHPLPS-- 272
Cdd:cd08459  96 AARHVVVSASGTGHGLVEQALREAGIRRRIALRVPHFLALPLIVAQTDLVATVPERLARLFARAGGLRIVPLPFPLPPfe 175


                ....
gi 15829896 273 IKLY 276
Cdd:cd08459 176 VKLY 179
PRK10086 PRK10086
DNA-binding transcriptional regulator DsdC;
7-88 2.67e-09

DNA-binding transcriptional regulator DsdC;


Pssm-ID: 182231 [Multi-domain]  Cd Length: 311  Bit Score: 56.93  E-value: 2.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896    7 LKKFDLNLLVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTGLNLHHHLEKNLRGLEQ 86
Cdd:PRK10086  11 LNGWQLSKLHTFEVAARHQSFALAADELSLTPSAVSHRINQLEEELGIKLFVRSHRKVELTEEGKRVFWALKSSLDTLNQ 90


                 ..
gi 15829896   87 TI 88
Cdd:PRK10086  91 EI 92
PRK11139 PRK11139
DNA-binding transcriptional activator GcvA; Provisional
 12-70 9.76e-08

DNA-binding transcriptional activator GcvA; Provisional


Pssm-ID: 182990 [Multi-domain]  Cd Length: 297  Bit Score: 52.15  E-value: 9.76e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 15829896   12 LNLLVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTG 70
Cdd:PRK11139   8 LNALRAFEAAARHLSFTRAAEELFVTQAAVSHQIKALEDFLGLKLFRRRNRSLLLTEEG 66
argP TIGR03298
transcriptional regulator, ArgP family; ArgP used to be known as IciA. ArgP is a positive ...
 10-86 1.72e-07

transcriptional regulator, ArgP family; ArgP used to be known as IciA. ArgP is a positive regulator of argK. It is a negative autoregulator in presence of arginine. It competes with DnaA for oriC iteron (13-mer) binding. It activates dnaA and nrd transcription. It has been demonstrated to be part of the pho regulon (). ArgP mutants convey canavanine (an L-arginine structural homolog) sensitivity. [Cellular processes, Toxin production and resistance, DNA metabolism, DNA replication, recombination, and repair, Regulatory functions, DNA interactions]


Pssm-ID: 274509 [Multi-domain]  Cd Length: 292  Bit Score: 51.46  E-value: 1.72e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829896    10 FDLNLLVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRsGKGIAPTTTGLNLHHHLEKnLRGLEQ 86
Cdd:TIGR03298   1 LDYRQLAALAAVVEEGSFERAAAALSVTPSAVSQRIKALEERLGQPLLVR-TQPCRATEAGQRLLRHARQ-VRLLEA 75
decaheme_TF NF041036
multiheme cytochrome-associated LysR family transcriptional regulator; Members of this family, ...
 26-71 2.26e-07

multiheme cytochrome-associated LysR family transcriptional regulator; Members of this family, including founding member GSU2202 from Geobacter sulfurreducens PCA, are LysR family transcriptional regulators found regularly in the vicinity of multiheme cytochromes such as GSU2203, a decaheme c-type cytochrome.


Pssm-ID: 468965 [Multi-domain]  Cd Length: 301  Bit Score: 51.28  E-value: 2.26e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 15829896   26 SISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTGL 71
Cdd:NF041036  17 SFSKAAEKLHLTQSAVSQRIKFLEECYGYQLFDRSGPSLEPTAAGE 62
rbcR CHL00180
LysR transcriptional regulator; Provisional
 10-87 6.21e-07

LysR transcriptional regulator; Provisional


Pssm-ID: 177082 [Multi-domain]  Cd Length: 305  Bit Score: 50.02  E-value: 6.21e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829896   10 FDLNLLVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTGLNLHHHLEKNLRGLEQT 87
Cdd:CHL00180   5 FTLDQLRILKAIATEGSFKKAAESLYISQPAVSLQIKNLEKQLNIPLFDRSKNKASLTEAGELLLRYGNRILALCEET 82
PBP2_LTTR_substrate cd05466
The substrate binding domain of LysR-type transcriptional regulators (LTTRs), a member of the ...
 126-296 9.58e-07

The substrate binding domain of LysR-type transcriptional regulators (LTTRs), a member of the type 2 periplasmic binding fold protein superfamily; This model and hierarchy represent the the substrate-binding domain of the LysR-type transcriptional regulators that form the largest family of prokaryotic transcription factor. Homologs of some of LTTRs with similar domain organizations are also found in the archaea and eukaryotic organisms. The LTTRs are composed of two functional domains joined by a linker helix involved in oligomerization: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal substrate-binding domain, which is structurally homologous to the type 2 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcriptional repressor undergoes a conformational change upon substrate binding which in turn changes the DNA binding affinity of the repressor. The genes controlled by the LTTRs have diverse functional roles including amino acid biosynthesis, CO2 fixation, antibiotic resistance, degradation of aromatic compounds, oxidative stress responses, nodule formation of nitrogen-fixing bacteria, synthesis of virulence factors, toxin production, attachment and secretion, to name a few. The structural topology of this substrate-binding domain is most similar to that of the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the PBP2 superfamily includes the substrate-binding domains from ionotropic glutamate receptors, LysR-like transcriptional regulators, and unorthodox sensor proteins involved in signal transduction.


Pssm-ID: 176102 [Multi-domain]  Cd Length: 197  Bit Score: 48.37  E-value: 9.58e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896 126 VEIECHDilMSAENAEELLVHRKADLVITQMPVISRSVICMPLHTIRNTLICSNRHPRITDNS-TYEQIMAEEFTQLISK 204
Cdd:cd05466  29 VELSLVE--GGSSELLEALLEGELDLAIVALPVDDPGLESEPLFEEPLVLVVPPDHPLAKRKSvTLADLADEPLILFERG 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896 205 SAGVDDIQMEIDERFMNRKISFRGSSLLTIINSIAVTDLLGIVPYELYNSHRDFlNLKEIKLEHPLPSIKLYISYNKSSL 284
Cdd:cd05466 107 SGLRRLLDRAFAEAGFTPNIALEVDSLEAIKALVAAGLGIALLPESAVEELADG-GLVVLPLEDPPLSRTIGLVWRKGRY 185

                       170
                ....*....|..
gi 15829896 285 NNLVFSRFIDRL 296
Cdd:cd05466 186 LSPAARAFLELL 197
LysR_substrate pfam03466
LysR substrate binding domain; The structure of this domain is known and is similar to the ...
 126-298 2.09e-06

LysR substrate binding domain; The structure of this domain is known and is similar to the periplasmic binding proteins. This domain binds a variety of ligands that caries in size and structure, such as amino acids, sugar phosphates, organic acids, metal cations, flavonoids, C6-ring carboxylic acids, H2O2, HOCl, homocysteine, NADPH, ATP, sulphate, muropeptides, acetate, salicylate, citrate, phenol- and quinolone derivatives, acetylserines, fatty acid CoA, shikimate, chorismate, homocysteine, indole-3-acetic acid, Na(I), c-di-GMP, ppGpp and hydrogen peroxide (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 460931 [Multi-domain]  Cd Length: 205  Bit Score: 47.67  E-value: 2.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896   126 VEIECHdiLMSAENAEELLVHRKADLVITQMPVISRSVICMPLHTIRNTLICSNRHPRITDNS-TYEQIMAEEFTQLISK 204
Cdd:pfam03466  31 VELELT--EGNSEELLDLLLEGELDLAIRRGPPDDPGLEARPLGEEPLVLVAPPDHPLARGEPvSLEDLADEPLILLPPG 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896   205 SAGVDDIQMEIDERFMNRKISFRGSSLLTIINSIAVTDLLGIVPYELYNSHRDFLNLKEIKLEHPLPSIKLYISYNKSSL 284
Cdd:pfam03466 109 SGLRDLLDRALRAAGLRPRVVLEVNSLEALLQLVAAGLGIALLPRSAVARELADGRLVALPLPEPPLPRELYLVWRKGRP 188

                         170
                  ....*....|....
gi 15829896   285 NNLVFSRFIDRLNE 298
Cdd:pfam03466 189 LSPAVRAFIEFLRE 202
PRK11233 PRK11233
nitrogen assimilation transcriptional regulator; Provisional
 26-86 2.09e-06

nitrogen assimilation transcriptional regulator; Provisional


Pssm-ID: 183045 [Multi-domain]  Cd Length: 305  Bit Score: 48.53  E-value: 2.09e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829896   26 SISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTGLNLHHHLEKNLRGLEQ 86
Cdd:PRK11233  17 SLTQAAEVLHIAQPALSQQVATLEGELNQQLLIRTKRGVTPTEAGKILYTHARAILRQCEQ 77
PRK03635 PRK03635
ArgP/LysG family DNA-binding transcriptional regulator;
29-83 6.64e-06

ArgP/LysG family DNA-binding transcriptional regulator;


Pssm-ID: 235144 [Multi-domain]  Cd Length: 294  Bit Score: 46.69  E-value: 6.64e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15829896   29 KAAESLYITPSAVSQSLQRLRAQFNDPLFIRsGKGIAPTTTG---LNLHHH---LEKNLRG 83
Cdd:PRK03635  21 RAAQKLHITQSAVSQRIKALEERVGQVLLVR-TQPCRPTEAGqrlLRHARQvrlLEAELLG 80
PRK13348 PRK13348
HTH-type transcriptional regulator ArgP;
10-85 7.13e-06

HTH-type transcriptional regulator ArgP;


Pssm-ID: 237357 [Multi-domain]  Cd Length: 294  Bit Score: 46.50  E-value: 7.13e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829896   10 FDLNLLVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRsGKGIAPTTTGLNLHHHLEKnLRGLE 85
Cdd:PRK13348   2 LDYKQLEALAAVVETGSFERAARRLHVTPSAVSQRIKALEESLGQPLLVR-GRPCRPTPAGQRLLRHLRQ-VALLE 75
PRK10341 PRK10341
transcriptional regulator TdcA;
15-93 1.30e-05

transcriptional regulator TdcA;


Pssm-ID: 182391 [Multi-domain]  Cd Length: 312  Bit Score: 46.01  E-value: 1.30e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829896   15 LVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTGLNLHHHLEKNLRGLEQTINIVNK 93
Cdd:PRK10341  12 LVVFQEVIRSGSIGSAAKELGLTQPAVSKIINDIEDYFGVELIVRKNTGVTLTPAGQVLLSRSESITREMKNMVNEING 90
nhaR PRK11062
transcriptional activator NhaR; Provisional
 13-70 1.14e-04

transcriptional activator NhaR; Provisional


Pssm-ID: 182938 [Multi-domain]  Cd Length: 296  Bit Score: 43.07  E-value: 1.14e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15829896   13 NLLVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTG 70
Cdd:PRK11062   7 NHLYYFWMVCKEGSVVGAAEALFLTPQTITGQIKALEERLQGKLFKRKGRGLEPTELG 64
PRK15092 PRK15092
DNA-binding transcriptional repressor LrhA; Provisional
 11-82 1.29e-04

DNA-binding transcriptional repressor LrhA; Provisional


Pssm-ID: 237907 [Multi-domain]  Cd Length: 310  Bit Score: 42.71  E-value: 1.29e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829896   11 DLNLLVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTGLNLHHHLEKNLR 82
Cdd:PRK15092  12 DLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILR 83
PBP2_TdcA cd08418
The C-terminal substrate binding domain of LysR-type transcriptional regulator TdcA, which is ...
 221-299 1.84e-04

The C-terminal substrate binding domain of LysR-type transcriptional regulator TdcA, which is involved in the degradation of L-serine and L-threonine, contains the type 2 periplasmic binding fold; TdcA, a member of the LysR family, activates the expression of the anaerobically-regulated tdcABCDEFG operon which is involved in the degradation of L-serine and L-threonine to acetate and propionate, respectively. The tdc operon is comprised of one regulatory gene tdcA and six structural genes, tdcB to tdcG. The expression of the tdc operon is affected by several transcription factors including the cAMP receptor protein (CRP), integration host factor (IHF), histone-like protein (HU), and the operon specific regulators TdcA and TcdR. TcdR is divergently transcribed from the operon and encodes a small protein that is required for efficient expression of the Escherichia coli tdc operon. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 176110 [Multi-domain]  Cd Length: 201  Bit Score: 41.57  E-value: 1.84e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15829896 221 NRKISFRGSSLLTIINSIAVTDLLGIVPYELYNSHRDFLNLKEIKLEHPLPSIKLYISYNKSSLNNLVFSRFIDRLNEC 299
Cdd:cd08418 123 NPRVAVRTDSIVSIINLVEKADFLTILSRDMGRGPLDSFRLITIPVEEPLPSADYYLIYRKKSRLTPLAEQLVELFRRY 201
PRK09801 PRK09801
LysR family transcriptional regulator;
1-111 5.49e-04

LysR family transcriptional regulator;


Pssm-ID: 182085 [Multi-domain]  Cd Length: 310  Bit Score: 40.79  E-value: 5.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896    1 MTNLYDLKKfDLNLLVifECIYQHlSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTGLNLHHHLEKN 80
Cdd:PRK09801   1 MLNSWPLAK-DLQVLV--EIVHSG-SFSAAAATLGQTPAFVTKRIQILENTLATTLLNRSARGVALTESGQRCYEHALEI 76

                         90       100       110
                 ....*....|....*....|....*....|.
gi 15829896   81 LRGLEQTINIVNKSELKKNFIIHgpqlISCS 111
Cdd:PRK09801  77 LTQYQRLVDDVTQIKTRPEGMIR----IGCS 103
PRK11242 PRK11242
DNA-binding transcriptional regulator CynR; Provisional
 23-85 6.56e-04

DNA-binding transcriptional regulator CynR; Provisional


Pssm-ID: 183051 [Multi-domain]  Cd Length: 296  Bit Score: 40.71  E-value: 6.56e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829896   23 QHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTGLNLHHHLEKNLRGLE 85
Cdd:PRK11242  14 EHGNFTRAAEALHVSQPTLSQQIRQLEESLGVQLFDRSGRTVRLTDAGEVYLRYARRALQDLE 76
PRK10094 PRK10094
HTH-type transcriptional activator AllS;
10-91 1.06e-03

HTH-type transcriptional activator AllS;


Pssm-ID: 182237 [Multi-domain]  Cd Length: 308  Bit Score: 40.17  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896   10 FDLNLLVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTG----------LNLHHHLEK 79
Cdd:PRK10094   2 FDPETLRTFIAVAETGSFSKAAERLCKTTATISYRIKLLEENTGVALFFRTTRSVTLTAAGehllsqardwLSWLESMPS 81

                         90
                 ....*....|....*.
gi 15829896   80 NLR----GLEQTINIV 91
Cdd:PRK10094  82 ELQqvndGVERQVNIV 97
PRK09986 PRK09986
LysR family transcriptional regulator;
7-91 1.79e-03

LysR family transcriptional regulator;


Pssm-ID: 182183 [Multi-domain]  Cd Length: 294  Bit Score: 39.32  E-value: 1.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829896    7 LKKFDLNLLVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTGLNLHHHLEKNLRGLEQ 86
Cdd:PRK09986   4 LYRIDLKLLRYFLAVAEELHFGRAAARLNISQPPLSIHIKELEDQLGTPLFIRHSRSVVLTHAGKILMEESRRLLDNAEQ 83


                 ....*
gi 15829896   87 TINIV 91
Cdd:PRK09986  84 SLARV 88
PRK09791 PRK09791
LysR family transcriptional regulator;
12-76 4.03e-03

LysR family transcriptional regulator;


Pssm-ID: 182077 [Multi-domain]  Cd Length: 302  Bit Score: 38.20  E-value: 4.03e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15829896   12 LNLLVIFECIYQHLSISKAAESLYITPSAVSQSLQRLRAQFNDPLFIRSGKGIAPTTTGLNLHHH 76
Cdd:PRK09791   7 IHQIRAFVEVARQGSIRGASRMLNMSQPALTKSIQELEEGLAAQLFFRRSKGVTLTDAGESFYQH 71
 
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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