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Conserved domains on  [gi|2067338314|dbj|GJA59047|]
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LysR family transcriptional regulator [Aeromonas caviae]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK10216 super family cl32479
HTH-type transcriptional regulator YidZ;
6-309 3.76e-55

HTH-type transcriptional regulator YidZ;


The actual alignment was detected with superfamily member PRK10216:

Pssm-ID: 182312 [Multi-domain]  Cd Length: 319  Bit Score: 182.33  E-value: 3.76e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314   6 LARIDLNLLIILQVLLEERNGSRAARRLHLSQSAVSKALGRLRETFDDPLFVRSAYGMDPTPRALDLQQQLQPILLSLDN 85
Cdd:PRK10216    5 LTTLDLNLLLCLQLLMQERSVTKAAKRMNVTPSAVSKSLAKLRAWFDDPLFVNTPLGLSPTPLMVSMEQNLAEWMQMGNQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314  86 LIQPPDFD-PTSTEREFVIASmdsaftlfaPLYLSELKRQAPGIRLRYEE-------WTEHSLTEMSQGQVDIAFTVREN 157
Cdd:PRK10216   85 LLDKPHHQtPRGLKFELAAES---------PLMMIMLNALSKRIYQRYPQatiklrnWDYDSLDAITRGEVDIGFTGRES 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 158 CINSDFRLDTLPNAICQRLLtIDDLTCL-VQRDHPALQEpEWDLARYLAYPHVQTYCEGRDRWMLDHKLAEQDLYRRIEA 236
Cdd:PRK10216  156 HPRSRELLSLLPLAIDFEVL-FSDLPCVwLRKDHPALHE-EWNLDTFLRYPHISICWEQSDTWALDDVLQELGRERTIAL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 237 TVPSFEAALRMGM--HSDMIVTLSRlYARHATQVY--PLVPLPLPIALDSISHL-----LIWHQRHEEDPGHRWLRETLL 307
Cdd:PRK10216  234 SLPEFEQSLFMAAqpDHLLLATAPR-YCQYYNQLHqlPLVALPLPFDESQQKKLevpftLLWHKRNSHNPKIVWLRETIK 312

                  ..
gi 2067338314 308 AL 309
Cdd:PRK10216  313 NL 314
 
Name Accession Description Interval E-value
PRK10216 PRK10216
HTH-type transcriptional regulator YidZ;
6-309 3.76e-55

HTH-type transcriptional regulator YidZ;


Pssm-ID: 182312 [Multi-domain]  Cd Length: 319  Bit Score: 182.33  E-value: 3.76e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314   6 LARIDLNLLIILQVLLEERNGSRAARRLHLSQSAVSKALGRLRETFDDPLFVRSAYGMDPTPRALDLQQQLQPILLSLDN 85
Cdd:PRK10216    5 LTTLDLNLLLCLQLLMQERSVTKAAKRMNVTPSAVSKSLAKLRAWFDDPLFVNTPLGLSPTPLMVSMEQNLAEWMQMGNQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314  86 LIQPPDFD-PTSTEREFVIASmdsaftlfaPLYLSELKRQAPGIRLRYEE-------WTEHSLTEMSQGQVDIAFTVREN 157
Cdd:PRK10216   85 LLDKPHHQtPRGLKFELAAES---------PLMMIMLNALSKRIYQRYPQatiklrnWDYDSLDAITRGEVDIGFTGRES 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 158 CINSDFRLDTLPNAICQRLLtIDDLTCL-VQRDHPALQEpEWDLARYLAYPHVQTYCEGRDRWMLDHKLAEQDLYRRIEA 236
Cdd:PRK10216  156 HPRSRELLSLLPLAIDFEVL-FSDLPCVwLRKDHPALHE-EWNLDTFLRYPHISICWEQSDTWALDDVLQELGRERTIAL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 237 TVPSFEAALRMGM--HSDMIVTLSRlYARHATQVY--PLVPLPLPIALDSISHL-----LIWHQRHEEDPGHRWLRETLL 307
Cdd:PRK10216  234 SLPEFEQSLFMAAqpDHLLLATAPR-YCQYYNQLHqlPLVALPLPFDESQQKKLevpftLLWHKRNSHNPKIVWLRETIK 312

                  ..
gi 2067338314 308 AL 309
Cdd:PRK10216  313 NL 314
PBP2_Nitroaromatics_like cd08417
The C-terminal substrate binding domain of LysR-type transcriptional regulators that involved ...
100-309 4.18e-54

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: 175.48  E-value: 4.18e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 100 EFVIASMDSAFTLFAPLYLSELKRQAPGIRLRYEEWTEHSLTE-MSQGQVDIAFTVrencinsdfrLDTLPNAICQRLLT 178
Cdd:cd08417     1 TFRIAASDYLEALLLPPLLARLRQEAPGVRLRFVPLDRDDLEEaLESGEIDLAIGV----------FPELPPGLRSQPLF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 179 IDDLTCLVQRDHPALQEPeWDLARYLAYPHVQTYCEGRDRWMLDHKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTLS 258
Cdd:cd08417    71 EDRFVCVARKDHPLAGGP-LTLEDYLAAPHVLVSPRGRGHGLVDDALAELGLSRRVALTVPHFLAAPALVAGTDLIATVP 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2067338314 259 RLYARHATQVYPLVPLPLPIALDSISHLLIWHQRHEEDPGHRWLRETLLAL 309
Cdd:cd08417   150 RRLAEALAERLGLRVLPLPFELPPFTVSLYWHPRRDRDPAHRWLRELIAEL 200
LysR COG0583
DNA-binding transcriptional regulator, LysR family [Transcription];
9-310 1.88e-30

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


Pssm-ID: 440348 [Multi-domain]  Cd Length: 256  Bit Score: 115.73  E-value: 1.88e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314   9 IDLNLLIILQVLLEERNGSRAARRLHLSQSAVSKALGRLRETFDDPLFVRSAYGMDPTPRALDLQQQLQPILLSLDNLIQ 88
Cdd:COG0583     1 MDLRQLRAFVAVAEEGSFTAAAERLGVSQPAVSRQIRRLEEELGVPLFERTGRGLRLTEAGERLLERARRILAELEEAEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314  89 PPDFDPTSTEREFVIASMDSAFTLFAPLYLSELKRQAPGIRLRYEEWTEHSLTEM-SQGQVDIAFTVREncinsdfrlDT 167
Cdd:COG0583    81 ELRALRGGPRGTLRIGAPPSLARYLLPPLLARFRARHPGVRLELREGNSDRLVDAlLEGELDLAIRLGP---------PP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 168 LPNAICQRLLTiDDLTCLVQRDHPalqepewdLARYlayphvqtycegrdrwmldhklaeqdlyrriEATVPSFEAALRM 247
Cdd:COG0583   152 DPGLVARPLGE-ERLVLVASPDHP--------LARR-------------------------------APLVNSLEALLAA 191
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2067338314 248 GMHSDMIVTLSRLYARHATQVYPLVPLPLPIALDSISHLLIWHQRHEEDPGHRWLRETLLALI 310
Cdd:COG0583   192 VAAGLGIALLPRFLAADELAAGRLVALPLPDPPPPRPLYLVWRRRRHLSPAVRAFLDFLREAL 254
LysR_substrate pfam03466
LysR substrate binding domain; The structure of this domain is known and is similar to the ...
98-308 1.67e-18

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: 82.34  E-value: 1.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314  98 EREFVIASMDSAFTLFAPLYLSELKRQAPGIRLR-YEEWTEHSLTEMSQGQVDIAFTvrencinsdfRLDTLPNAICQRL 176
Cdd:pfam03466   1 SGRLRIGAPPTLASYLLPPLLARFRERYPDVELElTEGNSEELLDLLLEGELDLAIR----------RGPPDDPGLEARP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 177 LTIDDLTCLVQRDHPALQEPEWDLARYLAYPHVQTYCEGRDRWMLDHKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVT 256
Cdd:pfam03466  71 LGEEPLVLVAPPDHPLARGEPVSLEDLADEPLILLPPGSGLRDLLDRALRAAGLRPRVVLEVNSLEALLQLVAAGLGIAL 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2067338314 257 LSRLYARHATQVYPLVPLPLPIALDSISHLLIWHQRHEEDPGHRWLRETLLA 308
Cdd:pfam03466 151 LPRSAVARELADGRLVALPLPEPPLPRELYLVWRKGRPLSPAVRAFIEFLRE 202
LysR_Sec_metab NF040786
selenium metabolism-associated LysR family transcriptional regulator; LysR family ...
9-153 1.78e-06

selenium metabolism-associated LysR family transcriptional regulator; LysR family transcriptional regulators regularly appear encoded adjacent to selenecysteine incorporation proteins such as SelB. This model represents one especially well-conserved subgroup of such transcription factors from species such as Merdimonas faecis, Sellimonas intestinalis, Syntrophotalea acetylenica, and Hydrogenivirga caldilitoris. Seed alignment members were selected by proximity to selB, but not all family members are expected to have similar genomic locations.


Pssm-ID: 468737 [Multi-domain]  Cd Length: 298  Bit Score: 48.77  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314   9 IDLNLLIILQVLLEERNGSRAARRLHLSQSAVSKALGRLRETFDDPLFVRSAYGMDPTPRALDLQQQLQPILLSLDNLIQ 88
Cdd:NF040786    1 MNLKQLEAFVNVAEYKSFSKAAKKLFLTQPTISAHISSLEKELGVRLFVRNTKEVSLTEDGKLLYEYAKEMLDLWEKLEE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2067338314  89 ppDFDPTSTEREFVI---ASMDSAfTLFAPLYLSELKRQAPGIRLR-YEEWTEHSLTEMSQGQVDIAFT 153
Cdd:NF040786   81 --EFDRYGKESKGVLrigASTIPG-QYLLPELLKKFKEKYPNVRFKlMISDSIKVIELLLEGEVDIGFT 146
decaheme_TF NF041036
multiheme cytochrome-associated LysR family transcriptional regulator; Members of this family, ...
17-66 8.72e-05

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: 43.57  E-value: 8.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2067338314  17 LQVLLEERNGSRAARRLHLSQSAVSKALGRLRETFDDPLFVRSAYGMDPT 66
Cdd:NF041036    9 LVIVAEEGSFSKAAEKLHLTQSAVSQRIKFLEECYGYQLFDRSGPSLEPT 58
 
Name Accession Description Interval E-value
PRK10216 PRK10216
HTH-type transcriptional regulator YidZ;
6-309 3.76e-55

HTH-type transcriptional regulator YidZ;


Pssm-ID: 182312 [Multi-domain]  Cd Length: 319  Bit Score: 182.33  E-value: 3.76e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314   6 LARIDLNLLIILQVLLEERNGSRAARRLHLSQSAVSKALGRLRETFDDPLFVRSAYGMDPTPRALDLQQQLQPILLSLDN 85
Cdd:PRK10216    5 LTTLDLNLLLCLQLLMQERSVTKAAKRMNVTPSAVSKSLAKLRAWFDDPLFVNTPLGLSPTPLMVSMEQNLAEWMQMGNQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314  86 LIQPPDFD-PTSTEREFVIASmdsaftlfaPLYLSELKRQAPGIRLRYEE-------WTEHSLTEMSQGQVDIAFTVREN 157
Cdd:PRK10216   85 LLDKPHHQtPRGLKFELAAES---------PLMMIMLNALSKRIYQRYPQatiklrnWDYDSLDAITRGEVDIGFTGRES 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 158 CINSDFRLDTLPNAICQRLLtIDDLTCL-VQRDHPALQEpEWDLARYLAYPHVQTYCEGRDRWMLDHKLAEQDLYRRIEA 236
Cdd:PRK10216  156 HPRSRELLSLLPLAIDFEVL-FSDLPCVwLRKDHPALHE-EWNLDTFLRYPHISICWEQSDTWALDDVLQELGRERTIAL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 237 TVPSFEAALRMGM--HSDMIVTLSRlYARHATQVY--PLVPLPLPIALDSISHL-----LIWHQRHEEDPGHRWLRETLL 307
Cdd:PRK10216  234 SLPEFEQSLFMAAqpDHLLLATAPR-YCQYYNQLHqlPLVALPLPFDESQQKKLevpftLLWHKRNSHNPKIVWLRETIK 312

                  ..
gi 2067338314 308 AL 309
Cdd:PRK10216  313 NL 314
PBP2_Nitroaromatics_like cd08417
The C-terminal substrate binding domain of LysR-type transcriptional regulators that involved ...
100-309 4.18e-54

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: 175.48  E-value: 4.18e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 100 EFVIASMDSAFTLFAPLYLSELKRQAPGIRLRYEEWTEHSLTE-MSQGQVDIAFTVrencinsdfrLDTLPNAICQRLLT 178
Cdd:cd08417     1 TFRIAASDYLEALLLPPLLARLRQEAPGVRLRFVPLDRDDLEEaLESGEIDLAIGV----------FPELPPGLRSQPLF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 179 IDDLTCLVQRDHPALQEPeWDLARYLAYPHVQTYCEGRDRWMLDHKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTLS 258
Cdd:cd08417    71 EDRFVCVARKDHPLAGGP-LTLEDYLAAPHVLVSPRGRGHGLVDDALAELGLSRRVALTVPHFLAAPALVAGTDLIATVP 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2067338314 259 RLYARHATQVYPLVPLPLPIALDSISHLLIWHQRHEEDPGHRWLRETLLAL 309
Cdd:cd08417   150 RRLAEALAERLGLRVLPLPFELPPFTVSLYWHPRRDRDPAHRWLRELIAEL 200
PBP2_DntR_like_1 cd08460
The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional ...
101-310 7.25e-34

The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator similar to DntR, which is involved in the catabolism of dinitrotoluene; contains the type 2 periplasmic binding fold; This CD includes an uncharacterized LysR-type transcriptional regulator similar to 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. 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: 176149 [Multi-domain]  Cd Length: 200  Bit Score: 123.08  E-value: 7.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 101 FVIASMDSAFTLFAPLYLSELKRQAPGIRLRYEEWTEHSLTEMSQGQVDIAFTVrencinsdfrLDTLPNAICQRLLTID 180
Cdd:cd08460     2 FTIRANDGFVAAFGPALLAAVAAEAPGVRLRFVPESDKDVDALREGRIDLEIGV----------LGPTGPEIRVQTLFRD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 181 DLTCLVQRDHPALQEPEwDLARYLAYPHVQTYCEGRDRWMLDHKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTLSRL 260
Cdd:cd08460    72 RFVGVVRAGHPLARGPI-TPERYAAAPHVSVSRRGRLHGPIDDALAALGLTRRVVAVVPTFAAALFLARGSDLIALVPER 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2067338314 261 YARHATQVYPLVPLPLPIALDSISHLLIWHQRHEEDPGHRWLRETLLALI 310
Cdd:cd08460   151 VTAAARAGLGLRTFPLPLELPAVTVSQAWHPRFDADPAHRWLRECVREVC 200
LysR COG0583
DNA-binding transcriptional regulator, LysR family [Transcription];
9-310 1.88e-30

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


Pssm-ID: 440348 [Multi-domain]  Cd Length: 256  Bit Score: 115.73  E-value: 1.88e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314   9 IDLNLLIILQVLLEERNGSRAARRLHLSQSAVSKALGRLRETFDDPLFVRSAYGMDPTPRALDLQQQLQPILLSLDNLIQ 88
Cdd:COG0583     1 MDLRQLRAFVAVAEEGSFTAAAERLGVSQPAVSRQIRRLEEELGVPLFERTGRGLRLTEAGERLLERARRILAELEEAEA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314  89 PPDFDPTSTEREFVIASMDSAFTLFAPLYLSELKRQAPGIRLRYEEWTEHSLTEM-SQGQVDIAFTVREncinsdfrlDT 167
Cdd:COG0583    81 ELRALRGGPRGTLRIGAPPSLARYLLPPLLARFRARHPGVRLELREGNSDRLVDAlLEGELDLAIRLGP---------PP 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 168 LPNAICQRLLTiDDLTCLVQRDHPalqepewdLARYlayphvqtycegrdrwmldhklaeqdlyrriEATVPSFEAALRM 247
Cdd:COG0583   152 DPGLVARPLGE-ERLVLVASPDHP--------LARR-------------------------------APLVNSLEALLAA 191
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2067338314 248 GMHSDMIVTLSRLYARHATQVYPLVPLPLPIALDSISHLLIWHQRHEEDPGHRWLRETLLALI 310
Cdd:COG0583   192 VAAGLGIALLPRFLAADELAAGRLVALPLPDPPPPRPLYLVWRRRRHLSPAVRAFLDFLREAL 254
PBP2_SyrM cd08467
The C-terminal substrate binding of LysR-type symbiotic regulator SyrM, which activates ...
100-309 2.09e-29

The C-terminal substrate binding of LysR-type symbiotic regulator SyrM, which activates expression of nodulation gene NodD3, contains the type 2 periplasmic binding fold; Rhizobium is a nitrogen fixing bacteria present in the roots of leguminous plants, which fixes atmospheric nitrogen to the soil. Most Rhizobium species possess multiple nodulation (nod) genes for the development of nodules. For example, Rhizobium meliloti possesses three copies of nodD genes. NodD1 and NodD2 activate nod operons when Rhizobium is exposed to inducers synthesized by the host plant, while NodD3 acts independent of plant inducers and requires the symbiotic regulator SyrM for nod gene expression. SyrM activates the expression of the regulatory nodulation gene nodD3. In turn, NodD3 activates expression of syrM. In addition, SyrM is involved in exopolysaccharide synthesis. 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: 176156 [Multi-domain]  Cd Length: 200  Bit Score: 111.38  E-value: 2.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 100 EFVIASMDSAFTLFAPLYLSELKRQAPGIRLRYEEW-TEHSLTEMSQGQVDIAFTvrencinsdfRLDTLPNAICQRLLT 178
Cdd:cd08467     1 GFTLAMPDYAEVALLPRLAPRLRERAPGLDLRLCPIgDDLAERGLEQGTIDLAVG----------RFAVPPDGLVVRRLY 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 179 IDDLTCLVQRDHPALqEPEWDLARYLAYPHVQTYCEGRDRWMLDHKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTLS 258
Cdd:cd08467    71 DDGFACLVRHGHPAL-AQEWTLDDFATLRHVAIAPPGRLFGGIYKRLENLGLKRNVAIAVSSFLTAAATVAATDLIATVP 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2067338314 259 RLYARHATQVYPLVPLPLPIALDSISHLLIWHQRHEEDPGHRWLRETLLAL 309
Cdd:cd08467   150 RRVATQVAAMLPLRVVPPPVDLGTFPVMLIWHERYQHDPAHRWLRKLIAAA 200
PBP2_DntR_NahR_LinR_like cd08459
The C-terminal substrate binding domain of LysR-type transcriptional regulators that are ...
100-309 1.37e-28

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: 109.20  E-value: 1.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 100 EFVIASMDSAFTLFAPLYLSELKRQAPGIRLRYEEWTEHSL-TEMSQGQVDIAFtvrencinsdFRLDTLPNAICQRLLT 178
Cdd:cd08459     1 TFRIAMSDIGEMYFLPRLLAALREVAPGVRIETVRLPVDELeEALESGEIDLAI----------GYLPDLGAGFFQQRLF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 179 IDDLTCLVQRDHPALQEPeWDLARYLAYPHVQTYCEGRDRWMLDHKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTLS 258
Cdd:cd08459    71 RERYVCLVRKDHPRIGST-LTLEQFLAARHVVVSASGTGHGLVEQALREAGIRRRIALRVPHFLALPLIVAQTDLVATVP 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2067338314 259 RLYARHATQVYPLVPLPLPIALDSISHLLIWHQRHEEDPGHRWLRETLLAL 309
Cdd:cd08459   150 ERLARLFARAGGLRIVPLPFPLPPFEVKLYWHRRFHRDPGNRWLRQLVAEL 200
PBP2_DntR_like_4 cd08463
The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional ...
100-306 3.25e-28

The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator similar to DntR, which is involved in the catabolism of dinitrotoluene; contains the type 2 periplasmic binding fold; This CD includes an uncharacterized LysR-type transcriptional regulator similar to 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. 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: 176152 [Multi-domain]  Cd Length: 203  Bit Score: 108.17  E-value: 3.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 100 EFVIASMDSAFTLFAPLYLSELKRQAPGIRLryeewTEHSLTE-------MSQGQVDIaftVRENCINSDFRLDTLPnai 172
Cdd:cd08463     1 TFRIAAPDYLNALFLPELVARFRREAPGARL-----EIHPLGPdfdyeraLASGELDL---VIGNWPEPPEHLHLSP--- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 173 cqrlLTIDDLTCLVQRDHPALQEPEWDLARYLAYPHV--QTYCEGRdRWMLDHKLAEQDLYRRIEATVPSFEAALRMGMH 250
Cdd:cd08463    70 ----LFSDEIVCLMRADHPLARRGLMTLDDYLEAPHLapTPYSVGQ-RGVIDSHLARLGLKRNIVVTVPYFGLAPYMLAQ 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2067338314 251 SDMIVTLSRLYARHATQVYPLVPLPLPIALDSISHLLIWHQRHEEDPGHRWLRETL 306
Cdd:cd08463   145 SDLVFTTGRHFAEHYAKLLPLAVVDAPIEFPRMRYYQLWHERSHRSPEHRWLRRLV 200
PBP2_DntR_like_2 cd08464
The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional ...
101-309 1.34e-24

The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator similar to DntR, which is involved in the catabolism of dinitrotoluene; contains the type 2 periplasmic binding fold; This CD includes an uncharacterized LysR-type transcriptional regulator similar to 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. 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: 176153 [Multi-domain]  Cd Length: 200  Bit Score: 98.46  E-value: 1.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 101 FVIASMDSAFTLFAPLYLSELKRQAPGIRLRYEewTEHSLT--EM-SQGQVDIAFTVrencinsdfrLDTLPNAICQRLL 177
Cdd:cd08464     2 FRIGLSDDVESWLAPPLLAALRAEAPGVRLVFR--QVDPFNvgDMlDRGEIDLAIGV----------FGELPAWLKREVL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 178 TIDDLTCLVQRDHPALQEPeWDLARYLAYPHVQTYCEGRDRWMLDHKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTL 257
Cdd:cd08464    70 YTEGYACLFDPQQLSLSAP-LTLEDYVARPHVLVSYRGGLRGFVDDALAELGRSRRVVASTPHFAALPALLRGTPLIATV 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2067338314 258 SRLYARHATQVYPLVPLPLPIALDSISHLLIWHQRHEEDPGHRWLRETLLAL 309
Cdd:cd08464   149 PARLARAWAAALGLRASPPPLDLPEFPISLLWHARTDNDPALVWLREQIVQA 200
PBP2_NodD cd08462
The C-terminal substsrate binding domain of NodD family of LysR-type transcriptional ...
100-308 2.58e-24

The C-terminal substsrate binding domain of NodD family of LysR-type transcriptional regulators that regulates the expression of nodulation (nod) genes; contains the type 2 periplasmic binding fold; The nodulation (nod) genes in soil bacteria play important roles in the development of nodules. nod genes are involved in synthesis of Nod factors that are required for bacterial entry into root hairs. Thirteen nod genes have been identified and are classified into five transcription units: nodD, nodABCIJ, nodFEL, nodMNT, and nodO. NodD is negatively auto-regulates its own expression of nodD gene, while other nod genes are inducible and positively regulated by NodD in the presence of flavonoids released by plant roots. This substrate-binding domain has 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: 176151 [Multi-domain]  Cd Length: 200  Bit Score: 97.70  E-value: 2.58e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 100 EFVIASMDSAFTLFAPLYLSELKRQAPGIRLRYEEWTEHSLTEMSQGQVDIAFTVrencinSDFRLDTLPnaiCQRLLTi 179
Cdd:cd08462     1 HFRIIASDYVITVLLPPVIERVAREAPGVRFELLPPDDQPHELLERGEVDLLIAP------ERFMSDGHP---SEPLFE- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 180 DDLTCLVQRDHPALQEpEWDLARYLAYPHVQT-YCEGRDRWMLDHKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTLS 258
Cdd:cd08462    71 EEFVCVVWADNPLVGG-ELTAEQYFSAGHVVVrFGRNRRPSFEDWFLNEYGLKRRVEVVTPSFSSIPPLLVGTNRIATLH 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2067338314 259 RLYARHATQVYPLVPLPLPIALDSISHLLIWHQRHEEDPGHRWLRETLLA 308
Cdd:cd08462   150 RRLAEQFARRLPLRILPLPFPLPPMREALQWHRYRNNDPGLIWLRELIIE 199
PBP2_LeuO cd08466
The C-terminal substrate binding domain of LysR-type transcriptional regulator LeuO, an ...
100-309 2.74e-24

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: 97.71  E-value: 2.74e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 100 EFVIASMDSAFTLFAPLYLSELKRQAPGIRLRYEEWTEHSLTE-MSQGQVDIAFTVrencinsdfrLDTLPNAICQRLLT 178
Cdd:cd08466     1 TFNIAANETLDLLLLPRLLARLKQLAPNISLRESPSSEEDLFEdLRLQEVDLVIDY----------VPFRDPSFKSELLF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 179 IDDLTCLVQRDHPALQEPeWDLARYLAYPHVqTYCEGRDRWMLDHKLAEQDLY-RRIEATVPSFEAALRMGMHSDMIVTL 257
Cdd:cd08466    71 EDELVCVARKDHPRIQGS-LSLEQYLAEKHV-VLSLRRGNLSALDLLTEEVLPqRNIAYEVSSLLSMLAVVSQTDLIAIA 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2067338314 258 SRLYARHATQVYPLVPLPLPIALDSISHLLIWHQRHEEDPGHRWLRETLLAL 309
Cdd:cd08466   149 PRWLADQYAEQLNLQILPLPFKTKPIPLYMVWHKSRERDPAHQWLREQIKQL 200
leuO PRK09508
leucine transcriptional activator; Reviewed
5-306 3.95e-24

leucine transcriptional activator; Reviewed


Pssm-ID: 181918 [Multi-domain]  Cd Length: 314  Bit Score: 100.10  E-value: 3.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314   5 QLARIDLNLLIILQVLLEERNGSRAARRLHLSQSAVSKALGRLRETFDDPLFVRSAYGMDPTPRALDLQQQLQPILLSLD 84
Cdd:PRK09508   18 QLRMVDLNLLTVFDAVMQEQNITRAAHNLGMSQPAVSNAVARLKVMFNDELFVRYGRGIQPTARARQLFGPVRQALQLVQ 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314  85 NLIQPPDFDPTSTEREFVIASMDSAFTLFAPLYLSELKRQAPGIRLRYEEWTEHSLTEMSQGQvDIAFTVrencinSDFR 164
Cdd:PRK09508   98 NELPGSGFEPESSERVFNLCICSPLDIRLTSQIYNRIEQIAPNIHVVFKSSLNQNIEHQLRYQ-ETEFVI------SYEE 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 165 LDTlPNAICQRLLTiDDLTCLVQRDHPALQEP--EWDLAR-YLAYPHVQTYCEGRDRWMLDHKLAEQDLYrriEATvpSF 241
Cdd:PRK09508  171 FDR-PEFTSVPLFK-DELVLVASKNHPRIKGPitEEQLYNeQHAVVSLDRFASFSQPWYDTVDKQASIAY---QGT--AL 243
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2067338314 242 EAALRMGMHSDMIVTLSRLYARHATQVYPLVPLPLPIALDSISHLLIWHQRHEEDPGHRWLRETL 306
Cdd:PRK09508  244 SSVLNVVSQTHLVAIAPRWLAEEFAESLELQILPLPLKNNSRTCYLSWHESAGRDKGHQWMEELL 308
PBP2_PnbR cd08469
The C-terminal substrate binding domain of LysR-type transcriptional regulator PnbR, which is ...
101-306 1.44e-23

The C-terminal substrate binding domain of LysR-type transcriptional regulator PnbR, which is involved in regulating the pnb genes encoding enzymes for 4-nitrobenzoate catabolism, contains the type 2 periplasmic binding fold; PnbR is the regulator of one or both of the two pnb genes that encoding enzymes for 4-nitrobenzoate catabolism. In Pseudomonas putida strain, pnbA encodes a 4-nitrobenzoate reductase, which is responsible for catalyzing the direct reduction of 4-nitrobenzoate to 4-hydroxylaminobenzoate, and pnbB encodes a 4-hydroxylaminobenzoate lyase, which catalyzes the conversion of 4-hydroxylaminobenzoate to 3, 4-dihydroxybenzoic acid and ammonium. 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: 176158  Cd Length: 221  Bit Score: 96.32  E-value: 1.44e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 101 FVIASMDSAFTLFAPLYLSELKRQAPGIRLRYEEWTEHSLTE-MSQGQVDIAFTVRENcinsdfrldtLPNAICQRLLTI 179
Cdd:cd08469     2 FVIAANDYVTAVLLPALVRRLETEAPGIDLRIRPVTRLDLAEqLDLGRIDLVIGIFEQ----------IPPRFRRRTLFD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 180 DDLTCLVQRDHPALQEPeWDLARYLAYPHVQTYCEGR---------------------DRWMLDHKLAEQDLYRRIEATV 238
Cdd:cd08469    72 EDEVWVMRKDHPAARGA-LTIETLARYPHIVVSLGGEeegavsgfiserglarqtemfDRRALEEAFRESGLVPRVAVTV 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2067338314 239 PSFEAALRMGMHSDMIVTLSRLYARHATQVYPLVPLPLPIALDSISHLLIWHQRHEEDPGHRWLRETL 306
Cdd:cd08469   151 PHALAVPPLLADSDMLALLPRSLARAFAERGGLVMKEPPYPPPPVQIRAVWHERHDNDPAVAWLREMI 218
PBP2_DntR_like_3 cd08461
The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional ...
101-308 4.18e-23

The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator similar to DntR, which is involved in the catabolism of dinitrotoluene; contains the type 2 periplasmic binding fold; This CD includes an uncharacterized LysR-type transcriptional regulator similar to 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. 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: 176150 [Multi-domain]  Cd Length: 198  Bit Score: 94.66  E-value: 4.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 101 FVIASMDSAFTLFAPLYLSELKRQAPGIRLRYEEWTEHSLT-EMSQGQVDIAFTVRENcinsdfrldTLPNAICQRLLTi 179
Cdd:cd08461     2 LVIAATDYAQKAILPPLLAALRQEAPGVRVAIRDLESDNLEaQLERGEVDLALTTPEY---------APDGLRSRPLFE- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 180 DDLTCLVQRDHPALQEPeWDLARYLAYPH-VQTYCEGRDRWMLDHKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTLS 258
Cdd:cd08461    72 ERYVCVTRRGHPLLQGP-LSLDQFCALDHiVVSPSGGGFAGSTDEALAALGLTRNVVLSVPSFLVVPEILAATDMVAFVP 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2067338314 259 RLYARHATQvypLVPLPLPIALDSISHLLIWHQRHEEDPGHRWLRETLLA 308
Cdd:cd08461   151 SRLVPNLEG---LQEVELPLEPPGFDVVMAWHERTHRDPAHRWLRELLAA 197
PBP2_ToxR cd08465
The C-terminal substrate binding domain of LysR-type transcriptional regulator ToxR regulates ...
101-306 5.70e-21

The C-terminal substrate binding domain of LysR-type transcriptional regulator ToxR regulates the expression of the toxoflavin biosynthesis genes; contains the type 2 periplasmic bindinig fold; In soil bacterium Burkholderia glumae, ToxR regulates the toxABCDE and toxFGHI operons in the presence of toxoflavin as a coinducer. Additionally, the expression of both operons requires a transcriptional activator, ToxJ, whose expression is regulated by the TofI or TofR quorum-sensing system. The biosynthesis of toxoflavin is suggested to be synthesized in a pathway common to the synthesis of riboflavin. 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: 176154  Cd Length: 200  Bit Score: 88.91  E-value: 5.70e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 101 FVIASMDSAFTLFAPLYLSELKRQAPGIRLRYEEWTEHSLTE-MSQGQVDIAFTVrencinsdfrLDTLPNAICQRLLTI 179
Cdd:cd08465     2 FRLAMSDYGARLVLPALMRQLRAEAPGIDLAVSQASREAMLAqVADGEIDLALGV----------FPELPEELHAETLFE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 180 DDLTCLVQRDH-PAlqEPEWDLARYLAYPHVQTYCEGRDRWMLDHKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTLS 258
Cdd:cd08465    72 ERFVCLADRATlPA--SGGLSLDAWLARPHVLVAMRGDAANEIDRALAARGLRRRVALTLPHWGVAPELIAGTDLILTVA 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2067338314 259 RLYARHATQVYPLVPLPLPIALDSISHLLIWHQRHEEDPGHRWLRETL 306
Cdd:cd08465   150 RRALDALRLDERLAVFAPPFPIPPFAFQQIWHQRREGDPAHRWLRERI 197
PBP2_Pa0477 cd08468
The C-terminal substrate biniding domain of an uncharacterized LysR-like transcriptional ...
100-309 2.56e-20

The C-terminal substrate biniding domain of an uncharacterized LysR-like transcriptional regulator Pa0477 related to DntR, contains the type 2 periplasmic binding fold; LysR-type transcriptional regulator Pa0477 is related to DntR, which controls genes encoding enzymes for oxidative degradation of the nitro-aromatic compound 2,4-dinitrotoluene. 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. 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: 176157 [Multi-domain]  Cd Length: 202  Bit Score: 87.11  E-value: 2.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 100 EFVIASMD-SAFTLFAPLyLSELKRQAPGIRLRYEEWTEH-SLTEMSQGQVDIAFtvrencinsDFRLDT--LPNAICQR 175
Cdd:cd08468     1 RFRFAVTDyTALAVMPRL-MARLEELAPSVRLNLVHAEQKlPLDALLAGEIDFAL---------GYSHDDgaEPRLIEER 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 176 LLTIDDLTCLVQRDHPALQEPewDLARYLAYPHVQTYCEGRDRWMLDHKLAEQDLYRRIEATVPSFEAALRMGMHSDMIV 255
Cdd:cd08468    71 DWWEDTYVVIASRDHPRLSRL--TLDAFLAERHLVVTPWNEDRGVVDQVLEKQGLEREIALQLPNVLNAPFIVASSDLLM 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2067338314 256 TLSRLYARHATQVYPLVPLPLPIALDSISHLLIWHQRHEEDPGHRWLRETLLAL 309
Cdd:cd08468   149 TLPRQAARALAEALPLELFDLPFDMPPYRLKLYSHRQHENSAANQWLIEQLDGL 202
LysR_substrate pfam03466
LysR substrate binding domain; The structure of this domain is known and is similar to the ...
98-308 1.67e-18

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: 82.34  E-value: 1.67e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314  98 EREFVIASMDSAFTLFAPLYLSELKRQAPGIRLR-YEEWTEHSLTEMSQGQVDIAFTvrencinsdfRLDTLPNAICQRL 176
Cdd:pfam03466   1 SGRLRIGAPPTLASYLLPPLLARFRERYPDVELElTEGNSEELLDLLLEGELDLAIR----------RGPPDDPGLEARP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 177 LTIDDLTCLVQRDHPALQEPEWDLARYLAYPHVQTYCEGRDRWMLDHKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVT 256
Cdd:pfam03466  71 LGEEPLVLVAPPDHPLARGEPVSLEDLADEPLILLPPGSGLRDLLDRALRAAGLRPRVVLEVNSLEALLQLVAAGLGIAL 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2067338314 257 LSRLYARHATQVYPLVPLPLPIALDSISHLLIWHQRHEEDPGHRWLRETLLA 308
Cdd:pfam03466 151 LPRSAVARELADGRLVALPLPEPPLPRELYLVWRKGRPLSPAVRAFIEFLRE 202
HTH_1 pfam00126
Bacterial regulatory helix-turn-helix protein, lysR family;
11-69 3.29e-15

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


Pssm-ID: 459683 [Multi-domain]  Cd Length: 60  Bit Score: 68.95  E-value: 3.29e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2067338314  11 LNLLIILQVLLEERNGSRAARRLHLSQSAVSKALGRLRETFDDPLFVRSAYGMDPTPRA 69
Cdd:pfam00126   1 LRQLRLFVAVAETGSFTAAAERLGLSQPAVSRQIKRLEEELGVPLFERTTRGVRLTEAG 59
PRK11482 PRK11482
DNA-binding transcriptional regulator;
6-277 1.94e-12

DNA-binding transcriptional regulator;


Pssm-ID: 183159 [Multi-domain]  Cd Length: 317  Bit Score: 66.67  E-value: 1.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314   6 LARIDLNLLIILQVLLEERNGSRAARRLHLSQSAVSKALGRLRETFDDPLFVRSAYGMDPTPRALDLQQQLQP---ILLS 82
Cdd:PRK11482   26 LRNIDLNLLTIFEAVYVHKGIVNAAKILNLTPSAISQSIQKLRVIFPDPLFIRKGQGVTPTAYATHLHEYISQgleSILG 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314  83 LDNLIQPPDfdptsTEREFVIASMDSAFTLFAPLYLSELKRQAPGIRLRYEEWTEhSLTEMSQGQVDIAftvrencINSD 162
Cdd:PRK11482  106 ALDITGSYD-----KQRTITIATTPSVGALVMPVIYQAIKTHYPQLLLRNIPISD-AENQLSQFQTDLI-------IDTH 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 163 FRLDtlpNAICQRLLTIDDLTCLVQRDHPALQEPEwDLARYLAYPHVQTYCEGRDRWMLDHKLAEQDLYRRIEATVPSFE 242
Cdd:PRK11482  173 SCSN---RTIQHHVLFTDNVVLVCRQGHPLLSLED-DEETLDNAEHTLLLPEGQNFSGLRQRLQEMFPDRQISFSSYNIL 248
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 2067338314 243 AALRMGMHSDMI-VTLSRLYARhATQVYPLVPLPLP 277
Cdd:PRK11482  249 TIAALIASSDMLgIMPSRFYNL-FSRCWPLEKLPFP 283
PBP2_LTTR_substrate cd05466
The substrate binding domain of LysR-type transcriptional regulators (LTTRs), a member of the ...
100-306 6.61e-09

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: 54.91  E-value: 6.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 100 EFVIASMDSAFTLFAPLYLSELKRQAPGIRLRYEEWTEHSLTEM-SQGQVDIAFTvrencinsdfRLDTLPNAICQRLLT 178
Cdd:cd05466     1 TLRIGASPSIAAYLLPPLLAAFRQRYPGVELSLVEGGSSELLEAlLEGELDLAIV----------ALPVDDPGLESEPLF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 179 IDDLTCLVQRDHPALQEPEWDLARYLAYPHVQTYCEGRDRWMLDHKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTLS 258
Cdd:cd05466    71 EEPLVLVVPPDHPLAKRKSVTLADLADEPLILFERGSGLRRLLDRAFAEAGFTPNIALEVDSLEAIKALVAAGLGIALLP 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2067338314 259 RLYARHATQvYPLVPLPLPIALDSISHLLIWHQRHEEDPGHRWLRETL 306
Cdd:cd05466   151 ESAVEELAD-GGLVVLPLEDPPLSRTIGLVWRKGRYLSPAARAFLELL 197
LysR_Sec_metab NF040786
selenium metabolism-associated LysR family transcriptional regulator; LysR family ...
9-153 1.78e-06

selenium metabolism-associated LysR family transcriptional regulator; LysR family transcriptional regulators regularly appear encoded adjacent to selenecysteine incorporation proteins such as SelB. This model represents one especially well-conserved subgroup of such transcription factors from species such as Merdimonas faecis, Sellimonas intestinalis, Syntrophotalea acetylenica, and Hydrogenivirga caldilitoris. Seed alignment members were selected by proximity to selB, but not all family members are expected to have similar genomic locations.


Pssm-ID: 468737 [Multi-domain]  Cd Length: 298  Bit Score: 48.77  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314   9 IDLNLLIILQVLLEERNGSRAARRLHLSQSAVSKALGRLRETFDDPLFVRSAYGMDPTPRALDLQQQLQPILLSLDNLIQ 88
Cdd:NF040786    1 MNLKQLEAFVNVAEYKSFSKAAKKLFLTQPTISAHISSLEKELGVRLFVRNTKEVSLTEDGKLLYEYAKEMLDLWEKLEE 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2067338314  89 ppDFDPTSTEREFVI---ASMDSAfTLFAPLYLSELKRQAPGIRLR-YEEWTEHSLTEMSQGQVDIAFT 153
Cdd:NF040786   81 --EFDRYGKESKGVLrigASTIPG-QYLLPELLKKFKEKYPNVRFKlMISDSIKVIELLLEGEVDIGFT 146
PBP2_TdcA cd08418
The C-terminal substrate binding domain of LysR-type transcriptional regulator TdcA, which is ...
109-304 2.87e-06

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: 47.35  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 109 AFTLFAPLyLSELKRQAPGIRLRYEEWTEHS-LTEMSQGQVDIAftvrencINSdFRLDTLPNAICQRLLTIDDLTCLVQ 187
Cdd:cd08418    11 AHTLMPAV-INRFKEQFPDVQISIYEGQLSSlLPELRDGRLDFA-------IGT-LPDEMYLKELISEPLFESDFVVVAR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2067338314 188 RDHPALQEPewDLARYLAYPHVQTYCEGRDRWMLDHKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTLSRLYARHATQ 267
Cdd:cd08418    82 KDHPLQGAR--SLEELLDASWVLPGTRMGYYNNLLEALRRLGYNPRVAVRTDSIVSIINLVEKADFLTILSRDMGRGPLD 159
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2067338314 268 VYPLVPLPLPIALDSISHLLIWHQRHEEDPGHRWLRE 304
Cdd:cd08418   160 SFRLITIPVEEPLPSADYYLIYRKKSRLTPLAEQLVE 196
PRK09986 PRK09986
LysR family transcriptional regulator;
3-60 6.16e-06

LysR family transcriptional regulator;


Pssm-ID: 182183 [Multi-domain]  Cd Length: 294  Bit Score: 47.02  E-value: 6.16e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2067338314   3 LEQLARIDLNLLIILQVLLEERNGSRAARRLHLSQSAVSKALGRLRETFDDPLFVRSA 60
Cdd:PRK09986    1 MERLYRIDLKLLRYFLAVAEELHFGRAAARLNISQPPLSIHIKELEDQLGTPLFIRHS 58
decaheme_TF NF041036
multiheme cytochrome-associated LysR family transcriptional regulator; Members of this family, ...
17-66 8.72e-05

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: 43.57  E-value: 8.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2067338314  17 LQVLLEERNGSRAARRLHLSQSAVSKALGRLRETFDDPLFVRSAYGMDPT 66
Cdd:NF041036    9 LVIVAEEGSFSKAAEKLHLTQSAVSQRIKFLEECYGYQLFDRSGPSLEPT 58
PRK13348 PRK13348
HTH-type transcriptional regulator ArgP;
9-59 7.36e-04

HTH-type transcriptional regulator ArgP;


Pssm-ID: 237357 [Multi-domain]  Cd Length: 294  Bit Score: 40.72  E-value: 7.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2067338314   9 IDLNLLIILQVLLEERNGSRAARRLHLSQSAVSKALGRLRETFDDPLFVRS 59
Cdd:PRK13348    2 LDYKQLEALAAVVETGSFERAARRLHVTPSAVSQRIKALEESLGQPLLVRG 52
rbcR CHL00180
LysR transcriptional regulator; Provisional
11-59 3.01e-03

LysR transcriptional regulator; Provisional


Pssm-ID: 177082 [Multi-domain]  Cd Length: 305  Bit Score: 38.85  E-value: 3.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2067338314  11 LNLLIILQVLLEERNGSRAARRLHLSQSAVSKALGRLRETFDDPLFVRS 59
Cdd:CHL00180    7 LDQLRILKAIATEGSFKKAAESLYISQPAVSLQIKNLEKQLNIPLFDRS 55
 
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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