NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|654546228|ref|WP_028013934|]
View 

MULTISPECIES: transcriptional regulator LrhA [Enterobacter]

Protein Classification

LysR family transcriptional regulator( domain architecture ID 11487634)

LysR family transcriptional regulator LrhA is involved in control of the transcription of flagellar, motility, and chemotaxis genes

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK15092 PRK15092
DNA-binding transcriptional repressor LrhA; Provisional
 1-310 0e+00

DNA-binding transcriptional repressor LrhA; Provisional


:

Pssm-ID: 237907 [Multi-domain]  Cd Length: 310  Bit Score: 655.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228   1 MINANRPIMNLDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARK 80
Cdd:PRK15092   1 MINANRPIINLDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  81 ILRFNDEACMSLMFSNLQGVLTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHRPGQ 160
Cdd:PRK15092  81 ILRFNDEACSSLMYSNLQGVLTIGASDDTADTILPFLLNRVSSVYPKLALDVRVKRNAFMMEMLESQEVDLAVTTHRPSS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 161 FDCLTLRTSPTHWYCAAEYVLQKGEPVPLVLLDDPSPFRDMVLTALNEANIPWRLAYVASTLPAVRAAVKAGLGVTARPV 240
Cdd:PRK15092 161 FPALNLRTSPTLWYCAAEYVLQKGEPIPLVLLDEPSPFRDMALATLNAAGIPWRIAYVASTLSAVRAAVKAGLGVTARPV 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 241 EMMSPDLRVLGKSDGLPALPDTEYLLCHNASSHNELAKVVFEAMENYHNPWQFEHVTSEGGDDSLIVEGD 310
Cdd:PRK15092 241 EMMSPDLRVLGESEGLPPLPDTEYLLCRDPNSNNELAQVIFQAMESYHNPWQYSPLSAEEGDDSLLIERD 310
 
Name Accession Description Interval E-value
PRK15092 PRK15092
DNA-binding transcriptional repressor LrhA; Provisional
 1-310 0e+00

DNA-binding transcriptional repressor LrhA; Provisional


Pssm-ID: 237907 [Multi-domain]  Cd Length: 310  Bit Score: 655.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228   1 MINANRPIMNLDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARK 80
Cdd:PRK15092   1 MINANRPIINLDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  81 ILRFNDEACMSLMFSNLQGVLTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHRPGQ 160
Cdd:PRK15092  81 ILRFNDEACSSLMYSNLQGVLTIGASDDTADTILPFLLNRVSSVYPKLALDVRVKRNAFMMEMLESQEVDLAVTTHRPSS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 161 FDCLTLRTSPTHWYCAAEYVLQKGEPVPLVLLDDPSPFRDMVLTALNEANIPWRLAYVASTLPAVRAAVKAGLGVTARPV 240
Cdd:PRK15092 161 FPALNLRTSPTLWYCAAEYVLQKGEPIPLVLLDEPSPFRDMALATLNAAGIPWRIAYVASTLSAVRAAVKAGLGVTARPV 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 241 EMMSPDLRVLGKSDGLPALPDTEYLLCHNASSHNELAKVVFEAMENYHNPWQFEHVTSEGGDDSLIVEGD 310
Cdd:PRK15092 241 EMMSPDLRVLGESEGLPPLPDTEYLLCRDPNSNNELAQVIFQAMESYHNPWQYSPLSAEEGDDSLLIERD 310
PBP2_LrhA_like cd08439
The C-terminal substrate domain of LysR-like regulator LrhA (LysR homologue A) and that of ...
 100-284 2.69e-98

The C-terminal substrate domain of LysR-like regulator LrhA (LysR homologue A) and that of closely related homologs, contains the type 2 periplasmic binding fold; This CD represents the LrhA subfamily of LysR-like bacterial transcriptional regulators, including LrhA, HexA, PecT, and DgdR. LrhA is involved in control of the transcription of flagellar, motility, and chemotaxis genes by regulating the synthesis and concentration of FlhD(2)C(2), the master regulator for the expression of flagellar and chemotaxis genes. The LrhA protein has strong homology to HexA and PecT from plant pathogenic bacteria, in which HexA and PecT act as repressors of motility and of virulence factors, such as exoenzymes required for lytic reactions. DgdR also shares similar characteristics to those of LrhA, HexA and PecT. 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: 176130  Cd Length: 185  Bit Score: 287.31  E-value: 2.69e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 100 VLTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHRPGQFDCLTLRTSPTHWYCAAEY 179
Cdd:cd08439    1 TLRIGCPDDYADTILPFLLNRFASVYPRLAIEVVCKRTPRLMEMLERGEVDLALITHPPPGASATILRRSPTVWYCAAGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 180 VLQKGEPVPLVLLDDPSPFRDMVLTALNEANIPWRLAYVASTLPAVRAAVKAGLGVTARPVEMMSPDLRVLGKSDGLPAL 259
Cdd:cd08439   81 ILAPGEPLPLALLDEPTLDRRAALAALDAAGIPWRIAYAASSLSGLRAAVRAGLGITARTQEMVPPDLRILGESEGLPPL 160

                        170       180
                 ....*....|....*....|....*
gi 654546228 260 PDTEYLLCHNASSHNELAKVVFEAM 284
Cdd:cd08439  161 PDTGYTLCLDPNRPSELAQAFFEAL 185
LysR COG0583
DNA-binding transcriptional regulator, LysR family [Transcription];
11-284 1.38e-35

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


Pssm-ID: 440348 [Multi-domain]  Cd Length: 256  Bit Score: 128.83  E-value: 1.38e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  11 LDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILRFNDEAC- 89
Cdd:COG0583    1 MDLRQLRAFVAVAEEGSFTAAAERLGVSQPAVSRQIRRLEEELGVPLFERTGRGLRLTEAGERLLERARRILAELEEAEa 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  90 -MSLMFSNLQGVLTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHRPGQ--FDCLTL 166
Cdd:COG0583   81 eLRALRGGPRGTLRIGAPPSLARYLLPPLLARFRARHPGVRLELREGNSDRLVDALLEGELDLAIRLGPPPDpgLVARPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 167 RTSPTHWYCAAEYVLQKGEPvplvllddpspfrdmvltalneanipwrlayVASTLPAVRAAVKAGLGVTARPVEMMSPD 246
Cdd:COG0583  161 GEERLVLVASPDHPLARRAP-------------------------------LVNSLEALLAAVAAGLGIALLPRFLAADE 209

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 654546228 247 LRvlgkSDGL-------PALPDTEYLLCHNASSHNELAKVVFEAM 284
Cdd:COG0583  210 LA----AGRLvalplpdPPPPRPLYLVWRRRRHLSPAVRAFLDFL 250
LysR_substrate pfam03466
LysR substrate binding domain; The structure of this domain is known and is similar to the ...
 98-284 8.08e-25

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: 98.90  E-value: 8.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228   98 QGVLTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHRP--GQFDCLTLRTSPTHWYC 175
Cdd:pfam03466   1 SGRLRIGAPPTLASYLLPPLLARFRERYPDVELELTEGNSEELLDLLLEGELDLAIRRGPPddPGLEARPLGEEPLVLVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  176 AAEYVLQKGEPV--------PLVLLDDPSPFRDMVLTALNEANIPWRLAYVASTLPAVRAAVKAGLGVTARPVEMMSPDL 247
Cdd:pfam03466  81 PPDHPLARGEPVsledladePLILLPPGSGLRDLLDRALRAAGLRPRVVLEVNSLEALLQLVAAGLGIALLPRSAVAREL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 654546228  248 ---RVLGKSDGLPALPDTEYLLCHNASSHNELAKVVFEAM 284
Cdd:pfam03466 161 adgRLVALPLPEPPLPRELYLVWRKGRPLSPAVRAFIEFL 200
LysR_Sec_metab NF040786
selenium metabolism-associated LysR family transcriptional regulator; LysR family ...
 9-154 6.45e-17

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: 79.20  E-value: 6.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228   9 MNLDLdlLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILRFNDEA 88
Cdd:NF040786   1 MNLKQ--LEAFVNVAEYKSFSKAAKKLFLTQPTISAHISSLEKELGVRLFVRNTKEVSLTEDGKLLYEYAKEMLDLWEKL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  89 CMSlmFSNLQ----GVLTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVT 154
Cdd:NF040786  79 EEE--FDRYGkeskGVLRIGASTIPGQYLLPELLKKFKEKYPNVRFKLMISDSIKVIELLLEGEVDIGFT 146
argP TIGR03298
transcriptional regulator, ArgP family; ArgP used to be known as IciA. ArgP is a positive ...
 11-119 1.64e-08

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: 54.92  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228   11 LDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARhGRNKLLTEHGIQLLGYARKilrfndeacM 90
Cdd:TIGR03298   1 LDYRQLAALAAVVEEGSFERAAAALSVTPSAVSQRIKALEERLGQPLLVR-TQPCRATEAGQRLLRHARQ---------V 70

                          90       100
                  ....*....|....*....|....*....
gi 654546228   91 SLMFSNLQGvlTLGASDESADTILPFLLN 119
Cdd:TIGR03298  71 RLLEAELLA--ELPGLAPGAPTRLTIAVN 97
decaheme_TF NF041036
multiheme cytochrome-associated LysR family transcriptional regulator; Members of this family, ...
 16-87 4.04e-08

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: 53.59  E-value: 4.04e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654546228  16 LRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILRFNDE 87
Cdd:NF041036   6 LKTLVIVAEEGSFSKAAEKLHLTQSAVSQRIKFLEECYGYQLFDRSGPSLEPTAAGEMVLEKARRILDIEDS 77
 
Name Accession Description Interval E-value
PRK15092 PRK15092
DNA-binding transcriptional repressor LrhA; Provisional
 1-310 0e+00

DNA-binding transcriptional repressor LrhA; Provisional


Pssm-ID: 237907 [Multi-domain]  Cd Length: 310  Bit Score: 655.56  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228   1 MINANRPIMNLDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARK 80
Cdd:PRK15092   1 MINANRPIINLDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  81 ILRFNDEACMSLMFSNLQGVLTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHRPGQ 160
Cdd:PRK15092  81 ILRFNDEACSSLMYSNLQGVLTIGASDDTADTILPFLLNRVSSVYPKLALDVRVKRNAFMMEMLESQEVDLAVTTHRPSS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 161 FDCLTLRTSPTHWYCAAEYVLQKGEPVPLVLLDDPSPFRDMVLTALNEANIPWRLAYVASTLPAVRAAVKAGLGVTARPV 240
Cdd:PRK15092 161 FPALNLRTSPTLWYCAAEYVLQKGEPIPLVLLDEPSPFRDMALATLNAAGIPWRIAYVASTLSAVRAAVKAGLGVTARPV 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 241 EMMSPDLRVLGKSDGLPALPDTEYLLCHNASSHNELAKVVFEAMENYHNPWQFEHVTSEGGDDSLIVEGD 310
Cdd:PRK15092 241 EMMSPDLRVLGESEGLPPLPDTEYLLCRDPNSNNELAQVIFQAMESYHNPWQYSPLSAEEGDDSLLIERD 310
PBP2_LrhA_like cd08439
The C-terminal substrate domain of LysR-like regulator LrhA (LysR homologue A) and that of ...
 100-284 2.69e-98

The C-terminal substrate domain of LysR-like regulator LrhA (LysR homologue A) and that of closely related homologs, contains the type 2 periplasmic binding fold; This CD represents the LrhA subfamily of LysR-like bacterial transcriptional regulators, including LrhA, HexA, PecT, and DgdR. LrhA is involved in control of the transcription of flagellar, motility, and chemotaxis genes by regulating the synthesis and concentration of FlhD(2)C(2), the master regulator for the expression of flagellar and chemotaxis genes. The LrhA protein has strong homology to HexA and PecT from plant pathogenic bacteria, in which HexA and PecT act as repressors of motility and of virulence factors, such as exoenzymes required for lytic reactions. DgdR also shares similar characteristics to those of LrhA, HexA and PecT. 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: 176130  Cd Length: 185  Bit Score: 287.31  E-value: 2.69e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 100 VLTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHRPGQFDCLTLRTSPTHWYCAAEY 179
Cdd:cd08439    1 TLRIGCPDDYADTILPFLLNRFASVYPRLAIEVVCKRTPRLMEMLERGEVDLALITHPPPGASATILRRSPTVWYCAAGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 180 VLQKGEPVPLVLLDDPSPFRDMVLTALNEANIPWRLAYVASTLPAVRAAVKAGLGVTARPVEMMSPDLRVLGKSDGLPAL 259
Cdd:cd08439   81 ILAPGEPLPLALLDEPTLDRRAALAALDAAGIPWRIAYAASSLSGLRAAVRAGLGITARTQEMVPPDLRILGESEGLPPL 160

                        170       180
                 ....*....|....*....|....*
gi 654546228 260 PDTEYLLCHNASSHNELAKVVFEAM 284
Cdd:cd08439  161 PDTGYTLCLDPNRPSELAQAFFEAL 185
LysR COG0583
DNA-binding transcriptional regulator, LysR family [Transcription];
11-284 1.38e-35

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


Pssm-ID: 440348 [Multi-domain]  Cd Length: 256  Bit Score: 128.83  E-value: 1.38e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  11 LDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILRFNDEAC- 89
Cdd:COG0583    1 MDLRQLRAFVAVAEEGSFTAAAERLGVSQPAVSRQIRRLEEELGVPLFERTGRGLRLTEAGERLLERARRILAELEEAEa 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  90 -MSLMFSNLQGVLTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHRPGQ--FDCLTL 166
Cdd:COG0583   81 eLRALRGGPRGTLRIGAPPSLARYLLPPLLARFRARHPGVRLELREGNSDRLVDALLEGELDLAIRLGPPPDpgLVARPL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 167 RTSPTHWYCAAEYVLQKGEPvplvllddpspfrdmvltalneanipwrlayVASTLPAVRAAVKAGLGVTARPVEMMSPD 246
Cdd:COG0583  161 GEERLVLVASPDHPLARRAP-------------------------------LVNSLEALLAAVAAGLGIALLPRFLAADE 209

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 654546228 247 LRvlgkSDGL-------PALPDTEYLLCHNASSHNELAKVVFEAM 284
Cdd:COG0583  210 LA----AGRLvalplpdPPPPRPLYLVWRRRRHLSPAVRAFLDFL 250
LysR_substrate pfam03466
LysR substrate binding domain; The structure of this domain is known and is similar to the ...
 98-284 8.08e-25

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: 98.90  E-value: 8.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228   98 QGVLTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHRP--GQFDCLTLRTSPTHWYC 175
Cdd:pfam03466   1 SGRLRIGAPPTLASYLLPPLLARFRERYPDVELELTEGNSEELLDLLLEGELDLAIRRGPPddPGLEARPLGEEPLVLVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  176 AAEYVLQKGEPV--------PLVLLDDPSPFRDMVLTALNEANIPWRLAYVASTLPAVRAAVKAGLGVTARPVEMMSPDL 247
Cdd:pfam03466  81 PPDHPLARGEPVsledladePLILLPPGSGLRDLLDRALRAAGLRPRVVLEVNSLEALLQLVAAGLGIALLPRSAVAREL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 654546228  248 ---RVLGKSDGLPALPDTEYLLCHNASSHNELAKVVFEAM 284
Cdd:pfam03466 161 adgRLVALPLPEPPLPRELYLVWRKGRPLSPAVRAFIEFL 200
PBP2_LTTR_substrate cd05466
The substrate binding domain of LysR-type transcriptional regulators (LTTRs), a member of the ...
 101-284 2.37e-19

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: 84.19  E-value: 2.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 101 LTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHRPGQ--FDCLTLRTSPTHWYCAAE 178
Cdd:cd05466    2 LRIGASPSIAAYLLPPLLAAFRQRYPGVELSLVEGGSSELLEALLEGELDLAIVALPVDDpgLESEPLFEEPLVLVVPPD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 179 YVLQKGEPV--------PLVLLDDPSPFRDMVLTALNEANIPWRLAYVASTLPAVRAAVKAGLGVTARP----VEMMSPD 246
Cdd:cd05466   82 HPLAKRKSVtladladePLILFERGSGLRRLLDRAFAEAGFTPNIALEVDSLEAIKALVAAGLGIALLPesavEELADGG 161

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 654546228 247 LRVLGKSDglPALPDTEYLLCHNASSHNELAKVVFEAM 284
Cdd:cd05466  162 LVVLPLED--PPLSRTIGLVWRKGRYLSPAARAFLELL 197
LysR_Sec_metab NF040786
selenium metabolism-associated LysR family transcriptional regulator; LysR family ...
 9-154 6.45e-17

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: 79.20  E-value: 6.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228   9 MNLDLdlLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILRFNDEA 88
Cdd:NF040786   1 MNLKQ--LEAFVNVAEYKSFSKAAKKLFLTQPTISAHISSLEKELGVRLFVRNTKEVSLTEDGKLLYEYAKEMLDLWEKL 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  89 CMSlmFSNLQ----GVLTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVT 154
Cdd:NF040786  79 EEE--FDRYGkeskGVLRIGASTIPGQYLLPELLKKFKEKYPNVRFKLMISDSIKVIELLLEGEVDIGFT 146
HTH_1 pfam00126
Bacterial regulatory helix-turn-helix protein, lysR family;
13-71 9.42e-14

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


Pssm-ID: 459683 [Multi-domain]  Cd Length: 60  Bit Score: 64.71  E-value: 9.42e-14
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 654546228   13 LDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHG 71
Cdd:pfam00126   1 LRQLRLFVAVAETGSFTAAAERLGLSQPAVSRQIKRLEEELGVPLFERTTRGVRLTEAG 59
rbcR CHL00180
LysR transcriptional regulator; Provisional
 13-134 1.81e-13

LysR transcriptional regulator; Provisional


Pssm-ID: 177082 [Multi-domain]  Cd Length: 305  Bit Score: 69.66  E-value: 1.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  13 LDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILRFNDEACMSL 92
Cdd:CHL00180   7 LDQLRILKAIATEGSFKKAAESLYISQPAVSLQIKNLEKQLNIPLFDRSKNKASLTEAGELLLRYGNRILALCEETCRAL 86

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 654546228  93 M-FSNLQ-GVLTLGASDESADTILPFLLNRISSVYPKLALDVSV 134
Cdd:CHL00180  87 EdLKNLQrGTLIIGASQTTGTYLMPRLIGLFRQRYPQINVQLQV 130
PRK10837 PRK10837
putative DNA-binding transcriptional regulator; Provisional
 9-268 4.12e-11

putative DNA-binding transcriptional regulator; Provisional


Pssm-ID: 182768 [Multi-domain]  Cd Length: 290  Bit Score: 62.40  E-value: 4.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228   9 MNLDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILRFNDEa 88
Cdd:PRK10837   1 MHITLRQLEVFAEVLKSGSTTQASVMLALSQSAVSAALTDLEGQLGVQLFDRVGKRLVVNEHGRLLYPRALALLEQAVE- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  89 cMSLMFSNLQGVLTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDL-----------VVTthR 157
Cdd:PRK10837  80 -IEQLFREDNGALRIYASSTIGNYILPAMIARYRRDYPQLPLELSVGNSQDVINAVLDFRVDIgliegpchspeLIS--E 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 158 PGQFDCLTLRTSPTHWYCAAEYVLQKGEPVPLVLLDDPSPFRDmVLTALNEANIP-WRLAYVASTLPAVRAAVKAGLGVT 236
Cdd:PRK10837 157 PWLEDELVVFAAPDSPLARGPVTLEQLAAAPWILRERGSGTRE-IVDYLLLSHLPrFELAMELGNSEAIKHAVRHGLGIS 235

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 654546228 237 --ARPVEMMSPDLRVLGKSD-GLPALPDTEYLLCH 268
Cdd:PRK10837 236 clSRRVIADQLQAGTLVEVAvPLPRLMRTLYRIHH 270
PRK03601 PRK03601
HTH-type transcriptional regulator HdfR;
11-158 3.79e-10

HTH-type transcriptional regulator HdfR;


Pssm-ID: 235137 [Multi-domain]  Cd Length: 275  Bit Score: 59.65  E-value: 3.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  11 LDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILRFNDEACM 90
Cdd:PRK03601   1 MDTELLKTFLEVSRTRHFGRAAESLYLTQSAVSFRIRQLENQLGVNLFTRHRNNIRLTAAGERLLPYAETLMNTWQAAKK 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654546228  91 SLMFSNLQGVLTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHRP 158
Cdd:PRK03601  81 EVAHTSQHNELSIGASASLWECMLTPWLGRLYQNQEALQFEARIAQRQSLVKQLHERQLDLLITTEAP 148
PRK11139 PRK11139
DNA-binding transcriptional activator GcvA; Provisional
 16-280 6.13e-09

DNA-binding transcriptional activator GcvA; Provisional


Pssm-ID: 182990 [Multi-domain]  Cd Length: 297  Bit Score: 56.00  E-value: 6.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  16 LRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILRFNDEACMSLMFS 95
Cdd:PRK11139  11 LRAFEAAARHLSFTRAAEELFVTQAAVSHQIKALEDFLGLKLFRRRNRSLLLTEEGQRYFLDIREIFDQLAEATRKLRAR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  96 NLQGVLTLgasdesadTILP-----FLLNRISSV---YPklALDVSVKRNAFMVEMLNENkVDLVV---TTHRPGqfdcl 164
Cdd:PRK11139  91 SAKGALTV--------SLLPsfaiqWLVPRLSSFneaHP--DIDVRLKAVDRLEDFLRDD-VDVAIrygRGNWPG----- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 165 tLRTSPTHwycaAEYV--------LQKGEPVP-------LVLL--DDPSPFRDMVLTA-LNEANIPWRLAYVASTLpAVR 226
Cdd:PRK11139 155 -LRVEKLL----DEYLlpvcspalLNGGKPLKtpedlarHTLLhdDSREDWRAWFRAAgLDDLNVQQGPIFSHSSM-ALQ 228

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 654546228 227 AAVkAGLGVT-ARPVeMMSPDLR----VLGKSDGLPAlPDTEYLLCHnaSSHNELAKVV 280
Cdd:PRK11139 229 AAI-HGQGVAlGNRV-LAQPEIEagrlVCPFDTVLPS-PNAFYLVCP--DSQAELPKVA 282
PRK10094 PRK10094
HTH-type transcriptional activator AllS;
11-82 6.18e-09

HTH-type transcriptional activator AllS;


Pssm-ID: 182237 [Multi-domain]  Cd Length: 308  Bit Score: 55.97  E-value: 6.18e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654546228  11 LDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKIL 82
Cdd:PRK10094   2 FDPETLRTFIAVAETGSFSKAAERLCKTTATISYRIKLLEENTGVALFFRTTRSVTLTAAGEHLLSQARDWL 73
PBP2_PAO1_like cd08412
The C-terminal substrate-binding domain of putative LysR-type transcriptional regulator ...
 101-260 6.26e-09

The C-terminal substrate-binding domain of putative LysR-type transcriptional regulator PAO1-like, a member of the type 2 periplasmic binding fold protein superfamily; This family includes the C-terminal substrate domain of a putative LysR-type transcriptional regulator from the plant pathogen Pseudomonas aeruginosa PAO1and its closely related homologs. The LysR-type transcriptional regulators (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, nodule formation of N2 fixing bacteria, and synthesis of virulence factors, to a 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: 176104 [Multi-domain]  Cd Length: 198  Bit Score: 54.86  E-value: 6.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 101 LTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVT--THRPGQFDCLTLRTSPTHWYCAAE 178
Cdd:cd08412    2 LRIGCFSTLAPYYLPGLLRRFREAYPGVEVRVVEGNQEELEEGLRSGELDLALTydLDLPEDIAFEPLARLPPYVWLPAD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 179 YVLQKGEPV--------PLVLLDDPsPFRDMVLTALNEANIPWRLAYVASTLPAVRAAVKAGLGVT---ARPVEMMSPD- 246
Cdd:cd08412   82 HPLAGKDEVsladlaaePLILLDLP-HSREYFLSLFAAAGLTPRIAYRTSSFEAVRSLVANGLGYSllnDRPYRPWSYDg 160

                        170
                 ....*....|....*.
gi 654546228 247 --LRVLGKSDGLPALP 260
Cdd:cd08412  161 krLVRRPLADPVPPLR 176
PRK09906 PRK09906
DNA-binding transcriptional regulator HcaR; Provisional
 11-244 1.28e-08

DNA-binding transcriptional regulator HcaR; Provisional


Pssm-ID: 182137 [Multi-domain]  Cd Length: 296  Bit Score: 55.16  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  11 LDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILRFNDEA-C 89
Cdd:PRK09906   1 MELRHLRYFVAVAEELNFTKAAEKLHTAQPSLSQQIKDLENCVGVPLLVRDKRKVALTAAGEVFLQDARAILEQAEKAkL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  90 MSLMFSNLQGVLTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVT---THRPGqFDCLTL 166
Cdd:PRK09906  81 RARKIVQEDRQLTIGFVPSAEVNLLPKVLPMFRLRHPDTLIELVSLITTQQEEKLRRGELDVGFMrhpVYSDE-IDYLEL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 167 RTSPTHWYCAAEYVLQKGEPVPLVLLDD-----PSP-----FRDMVLTALNEANIPWRLAYVASTLPAVRAAVKAGLGVT 236
Cdd:PRK09906 160 LDEPLVVVLPVDHPLAHEKEITAAQLDGvnfisTDPaysgsLAPIIKAWFAQHNSQPNIVQVATNILVTMNLVGMGLGCT 239


                 ....*...
gi 654546228 237 ARPVEMMS 244
Cdd:PRK09906 240 IIPGYMNN 247
argP TIGR03298
transcriptional regulator, ArgP family; ArgP used to be known as IciA. ArgP is a positive ...
 11-119 1.64e-08

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: 54.92  E-value: 1.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228   11 LDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARhGRNKLLTEHGIQLLGYARKilrfndeacM 90
Cdd:TIGR03298   1 LDYRQLAALAAVVEEGSFERAAAALSVTPSAVSQRIKALEERLGQPLLVR-TQPCRATEAGQRLLRHARQ---------V 70

                          90       100
                  ....*....|....*....|....*....
gi 654546228   91 SLMFSNLQGvlTLGASDESADTILPFLLN 119
Cdd:TIGR03298  71 RLLEAELLA--ELPGLAPGAPTRLTIAVN 97
PRK09791 PRK09791
LysR family transcriptional regulator;
10-162 2.41e-08

LysR family transcriptional regulator;


Pssm-ID: 182077 [Multi-domain]  Cd Length: 302  Bit Score: 54.38  E-value: 2.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  10 NLDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKI---LRFND 86
Cdd:PRK09791   4 QVKIHQIRAFVEVARQGSIRGASRMLNMSQPALTKSIQELEEGLAAQLFFRRSKGVTLTDAGESFYQHASLIleeLRAAQ 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654546228  87 EACMSLMfSNLQGVLTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHRPGQFD 162
Cdd:PRK09791  84 EDIRQRQ-GQLAGQINIGMGASIARSLMPAVISRFHQQHPQVKVRIMEGQLVSMINELRQGELDFTINTYYQGPYD 158
PRK11716 PRK11716
HTH-type transcriptional activator IlvY;
40-154 4.01e-08

HTH-type transcriptional activator IlvY;


Pssm-ID: 236961 [Multi-domain]  Cd Length: 269  Bit Score: 53.28  E-value: 4.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  40 SAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILRFNDEACMSLMFSN--LQGVLTLGASDESADTILPFL 117
Cdd:PRK11716   6 STLSRQIQRLEEELGQPLFVRDNRSVTLTEAGEELRPFAQQTLLQWQQLRHTLDQQGpsLSGELSLFCSVTAAYSHLPPI 85

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 654546228 118 LNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVT 154
Cdd:PRK11716  86 LDRFRAEHPLVEIKLTTGDAADAVEKVQSGEADLAIA 122
decaheme_TF NF041036
multiheme cytochrome-associated LysR family transcriptional regulator; Members of this family, ...
 16-87 4.04e-08

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: 53.59  E-value: 4.04e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654546228  16 LRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILRFNDE 87
Cdd:NF041036   6 LKTLVIVAEEGSFSKAAEKLHLTQSAVSQRIKFLEECYGYQLFDRSGPSLEPTAAGEMVLEKARRILDIEDS 77
PRK12680 PRK12680
LysR family transcriptional regulator;
11-155 6.74e-08

LysR family transcriptional regulator;


Pssm-ID: 183677 [Multi-domain]  Cd Length: 327  Bit Score: 53.09  E-value: 6.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  11 LDLDLLRTFVAVAD--LNtFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRN-KLLTEHGIQLLGYARKILR--FN 85
Cdd:PRK12680   1 MTLTQLRYLVAIADaeLN-ITLAAARVHATQPGLSKQLKQLEDELGFLLFVRKGRSlESVTPAGVEVIERARAVLSeaNN 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  86 DEACMSLMFSNLQGVLTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTT 155
Cdd:PRK12680  80 IRTYAANQRRESQGQLTLTTTHTQARFVLPPAVAQIKQAYPQVSVHLQQAAESAALDLLGQGDADIAIVS 149
PRK12682 PRK12682
transcriptional regulator CysB-like protein; Reviewed
 38-157 1.57e-07

transcriptional regulator CysB-like protein; Reviewed


Pssm-ID: 183679 [Multi-domain]  Cd Length: 309  Bit Score: 51.92  E-value: 1.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  38 TQSAVSQQMQRLEQLVGKELFARHGRN-KLLTEHGIQLLGYARKILR-FNDEACMSLMFSNLQ-GVLTLGASDESADTIL 114
Cdd:PRK12682  29 SQPGVSKAIIELEEELGIEIFIRHGKRlKGLTEPGKAVLDVIERILReVGNIKRIGDDFSNQDsGTLTIATTHTQARYVL 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 654546228 115 PFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHR 157
Cdd:PRK12682 109 PRVVAAFRKRYPKVNLSLHQGSPDEIARMVISGEADIGIATES 151
PRK10086 PRK10086
DNA-binding transcriptional regulator DsdC;
5-203 1.82e-07

DNA-binding transcriptional regulator DsdC;


Pssm-ID: 182231 [Multi-domain]  Cd Length: 311  Bit Score: 51.54  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228   5 NRPIMNLDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILRF 84
Cdd:PRK10086   8 NRLLNGWQLSKLHTFEVAARHQSFALAADELSLTPSAVSHRINQLEEELGIKLFVRSHRKVELTEEGKRVFWALKSSLDT 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  85 NDEACMSLMFSNLQGVLTLGASDESADTILPFLLNRISSVYPKLALDVSVKrnafmvemlNEN------KVDLVV--TTH 156
Cdd:PRK10086  88 LNQEILDIKNQELSGTLTVYSRPSIAQCWLVPRLADFTRRYPSISLTILTG---------NENvnfqraGIDLAIyfDDA 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 654546228 157 RPGQFDCLTLRTSPTHWYCAAEYVLQKGepvplvLLDDPSPFRDMVL 203
Cdd:PRK10086 159 PSAQLTHHFLMDEEILPVCSPEYAERHA------LTGNPDNLRHCTL 199
PRK12684 PRK12684
CysB family HTH-type transcriptional regulator;
38-164 2.28e-07

CysB family HTH-type transcriptional regulator;


Pssm-ID: 237173 [Multi-domain]  Cd Length: 313  Bit Score: 51.52  E-value: 2.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  38 TQSAVSQQMQRLEQLVGKELFARHG-RNKLLTEHGIQLLGYARKILR-----------FNDEAcmslmfsnlQGVLTLGA 105
Cdd:PRK12684  29 SQPGVSKAIIELEDELGVEIFTRHGkRLRGLTEPGRIILASVERILQevenlkrvgkeFAAQD---------QGNLTIAT 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 654546228 106 SDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHRPGQFDCL 164
Cdd:PRK12684 100 THTQARYALPAAIKEFKKRYPKVRLSILQGSPTQIAEMVLHGQADLAIATEAIADYKEL 158
PRK12683 PRK12683
transcriptional regulator CysB-like protein; Reviewed
 38-165 3.64e-07

transcriptional regulator CysB-like protein; Reviewed


Pssm-ID: 237172 [Multi-domain]  Cd Length: 309  Bit Score: 50.81  E-value: 3.64e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  38 TQSAVSQQMQRLEQLVGKELFARHGRNKL-LTEHGIQLLGYARKIL-------RFNDEacmslmFSNL-QGVLTLGASDE 108
Cdd:PRK12683  29 SQSGVSKQIKDLEDELGVEIFIRRGKRLTgLTEPGKELLQIVERMLldaenlrRLAEQ------FADRdSGHLTVATTHT 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 654546228 109 SADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHRPGQFDCLT 165
Cdd:PRK12683 103 QARYALPKVVRQFKEVFPKVHLALRQGSPQEIAEMLLNGEADIGIATEALDREPDLV 159
PBP2_LysR_opines_like cd08415
The C-terminal substrate-domain of LysR-type transcriptional regulators involved in the ...
 101-236 5.28e-07

The C-terminal substrate-domain of LysR-type transcriptional regulators involved in the catabolism of opines and that of related regulators, contains the type 2 periplasmic binding fold; This CD includes the C-terminal substrate-domain of LysR-type transcriptional regulators, OccR and NocR, involved in the catabolism of opines and that of LysR for lysine biosynthesis which clustered together in phylogenetic trees. Opines, such as octopine and nopaline, are low molecular weight compounds found in plant crown gall tumors that are produced by the parasitic bacterium Agrobacterium. There are at least 30 different opines identified so far. Opines are utilized by tumor-colonizing bacteria as a source of carbon, nitrogen, and energy. NocR and OccR belong to the family of LysR-type transcriptional regulators that positively regulates the catabolism of nopaline and octopine, respectively. Both nopaline and octopalin are arginine derivatives. In Agrobacterium tumefaciens, NocR regulates expression of the divergently transcribed nocB and nocR genes of the nopaline catabolism (noc) region. OccR protein activates the occQ operon of the Ti plasmid in response to octopine. This operon encodes proteins required for the uptake and catabolism of octopine. The occ operon also encodes the TraR protein, which is a quorum-sensing transcriptional regulator of the Ti plasmid tra regulon. LysR is the transcriptional activator of lysA gene encoding diaminopimelate decarboxylase, an enzyme that catalyses the decarboxylation of diaminopimelate to produce lysine. 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: 176107 [Multi-domain]  Cd Length: 196  Bit Score: 49.10  E-value: 5.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 101 LTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTT---HRPGqFDCLTLRTSP------- 170
Cdd:cd08415    2 LRIAALPALALSLLPRAIARFRARHPDVRISLHTLSSSTVVEAVLSGQADLGLASlplDHPG-LESEPLASGRavcvlpp 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 654546228 171 THWYCAAEYV-LQKGEPVPLVLLDDPSPFRDMVLTALNEANIPWRLAYVASTLPAVRAAVKAGLGVT 236
Cdd:cd08415   81 GHPLARKDVVtPADLAGEPLISLGRGDPLRQRVDAAFERAGVEPRIVIETQLSHTACALVAAGLGVA 147
cbl PRK12679
HTH-type transcriptional regulator Cbl;
38-157 9.72e-07

HTH-type transcriptional regulator Cbl;


Pssm-ID: 183676 [Multi-domain]  Cd Length: 316  Bit Score: 49.42  E-value: 9.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  38 TQSAVSQQMQRLEQLVGKELFARHGRNKL-LTEHGIQLLGYARKILrfnDEAC----MSLMFSN-LQGVLTLGASDESAD 111
Cdd:PRK12679  29 SQSGVSRHIRELEDELGIEIFIRRGKRLLgMTEPGKALLVIAERIL---NEASnvrrLADLFTNdTSGVLTIATTHTQAR 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 654546228 112 TILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHR 157
Cdd:PRK12679 106 YSLPEVIKAFRELFPEVRLELIQGTPQEIATLLQNGEADIGIASER 151
PBP2_LTTR_like_4 cd08440
TThe C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional ...
 101-250 3.92e-06

TThe C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator, contains the type 2 periplasmic binding fold; LysR-transcriptional regulators comprise 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, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to a name a few. 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: 176131 [Multi-domain]  Cd Length: 197  Bit Score: 46.75  E-value: 3.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 101 LTLGASDESADTILPFLLNRISSVYPKLAL---DVSVKRnafMVEMLNENKVDLVVTTHRPGQ--FDCLTLRTSPTHWYC 175
Cdd:cd08440    2 VRVAALPSLAATLLPPVLAAFRRRHPGIRVrlrDVSAEQ---VIEAVRSGEVDFGIGSEPEADpdLEFEPLLRDPFVLVC 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 176 AAEYVLQKGEPV--------PLVLLDDPSPFRDMVLTALNEANIPWRLAYVASTLPAVRAAVKAGLGVTARP----VEMM 243
Cdd:cd08440   79 PKDHPLARRRSVtwaelagyPLIALGRGSGVRALIDRALAAAGLTLRPAYEVSHMSTALGMVAAGLGVAVLPalalPLAD 158


                 ....*..
gi 654546228 244 SPDLRVL 250
Cdd:cd08440  159 HPGLVAR 165
PRK11242 PRK11242
DNA-binding transcriptional regulator CynR; Provisional
 16-260 4.90e-06

DNA-binding transcriptional regulator CynR; Provisional


Pssm-ID: 183051 [Multi-domain]  Cd Length: 296  Bit Score: 47.26  E-value: 4.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  16 LRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILRFNDEACMSLM-F 94
Cdd:PRK11242   6 IRYFLAVAEHGNFTRAAEALHVSQPTLSQQIRQLEESLGVQLFDRSGRTVRLTDAGEVYLRYARRALQDLEAGRRAIHdV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  95 SNLQ-GVLTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHRPGQFDC---------L 164
Cdd:PRK11242  86 ADLSrGSLRLAMTPTFTAYLIGPLIDAFHARYPGITLTIREMSQERIEALLADDELDVGIAFAPVHSPEIeaqplftetL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 165 TLRTSPTHWYCAAEYVLQKGE--PVPLVLLDDPSPFRDMVLTALNEANIPWRLAYVASTLPAVRAAVKAGLGVTARP--V 240
Cdd:PRK11242 166 ALVVGRHHPLAARRKALTLDElaDEPLVLLSAEFATREQIDRYFRRHGVTPRVAIEANSISAVLEIVRRGRLATLLPaaI 245

                        250       260
                 ....*....|....*....|
gi 654546228 241 EMMSPDLRVLGKSdglPALP 260
Cdd:PRK11242 246 AREHDGLCAIPLD---PPLP 262
PRK11151 PRK11151
DNA-binding transcriptional regulator OxyR; Provisional
 9-153 5.17e-06

DNA-binding transcriptional regulator OxyR; Provisional


Pssm-ID: 182999 [Multi-domain]  Cd Length: 305  Bit Score: 47.33  E-value: 5.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228   9 MNL-DLDLLrtfVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILR---- 83
Cdd:PRK11151   1 MNIrDLEYL---VALAEHRHFRRAADSCHVSQPTLSGQIRKLEDELGVMLLERTSRKVLFTQAGLLLVDQARTVLRevkv 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  84 FNDEAcmSLMFSNLQGVLTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVV 153
Cdd:PRK11151  78 LKEMA--SQQGETMSGPLHIGLIPTVGPYLLPHIIPMLHQTFPKLEMYLHEAQTHQLLAQLDSGKLDCAI 145
PRK03635 PRK03635
ArgP/LysG family DNA-binding transcriptional regulator;
11-80 9.42e-06

ArgP/LysG family DNA-binding transcriptional regulator;


Pssm-ID: 235144 [Multi-domain]  Cd Length: 294  Bit Score: 46.31  E-value: 9.42e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  11 LDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARhGRNKLLTEHGIQLLGYARK 80
Cdd:PRK03635   2 LDYKQLEALAAVVREGSFERAAQKLHITQSAVSQRIKALEERVGQVLLVR-TQPCRPTEAGQRLLRHARQ 70
PBP2_CysL_like cd08420
C-terminal substrate binding domain of LysR-type transcriptional regulator CysL, which ...
 101-236 1.29e-05

C-terminal substrate binding domain of LysR-type transcriptional regulator CysL, which activates the transcription of the cysJI operon encoding sulfite reductase, contains the type 2 periplasmic binding fold; CysL, also known as YwfK, is a regular of sulfur metabolism in Bacillus subtilis. Sulfur is required for the synthesis of proteins and essential cofactors in all living organism. Sulfur can be assimilated either from inorganic sources (sulfate and thiosulfate), or from organic sources (sulfate esters, sulfamates, and sulfonates). CysL activates the transcription of the cysJI operon encoding sulfite reductase, which reduces sulfite to sulfide. Both cysL mutant and cysJI mutant are unable to grow using sulfate or sulfite as the sulfur source. Like other LysR-type regulators, CysL also negatively regulates its own transcription. In Escherichia coli, three LysR-type activators are involved in the regulation of sulfur metabolism: CysB, Cbl and MetR. 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: 176112 [Multi-domain]  Cd Length: 201  Bit Score: 45.18  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 101 LTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDL-VV--TTHRPG----QF--DCLTLRTSPT 171
Cdd:cd08420    2 LRIGASTTIGEYLLPRLLARFRKRYPEVRVSLTIGNTEEIAERVLDGEIDLgLVegPVDHPDlivePFaeDELVLVVPPD 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 172 H-WYCAAEYVLQKGEPVPLVLLDDPSPFRDMVLTALNEANI-PWRLAyVASTLP---AVRAAVKAGLGVT 236
Cdd:cd08420   82 HpLAGRKEVTAEELAAEPWILREPGSGTREVFERALAEAGLdGLDLN-IVMELGsteAIKEAVEAGLGIS 150
PRK09986 PRK09986
LysR family transcriptional regulator;
11-82 1.74e-05

LysR family transcriptional regulator;


Pssm-ID: 182183 [Multi-domain]  Cd Length: 294  Bit Score: 45.48  E-value: 1.74e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654546228  11 LDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKIL 82
Cdd:PRK09986   7 IDLKLLRYFLAVAEELHFGRAAARLNISQPPLSIHIKELEDQLGTPLFIRHSRSVVLTHAGKILMEESRRLL 78
PBP2_OxyR cd08411
The C-terminal substrate-binding domain of the LysR-type transcriptional regulator OxyR, a ...
 99-236 3.45e-05

The C-terminal substrate-binding domain of the LysR-type transcriptional regulator OxyR, a member of the type 2 periplasmic binding fold protein superfamily; OxyR senses hydrogen peroxide and is activated through the formation of an intramolecular disulfide bond. The OxyR activation induces the transcription of genes necessary for the bacterial defense against oxidative stress. The OxyR of LysR-type transcriptional regulator family is 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 C-terminal domain also contains the redox-active cysteines that mediate the redox-dependent conformational switch. Thus, the interaction between the OxyR-tetramer and DNA is notably different between the oxidized and reduced forms. 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: 176103 [Multi-domain]  Cd Length: 200  Bit Score: 44.05  E-value: 3.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  99 GVLTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVT---THRPGqFDCLTLRTSPTHWYC 175
Cdd:cd08411    1 GPLRLGVIPTIAPYLLPRLLPALRQAYPKLRLYLREDQTERLLEKLRSGELDAALLalpVDEPG-LEEEPLFDEPFLLAV 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 654546228 176 AAEYVLQKGEPV--------PLVLLDDPSPFRDMVLTALNEANIPWRLAYVASTLPAVRAAVKAGLGVT 236
Cdd:cd08411   80 PKDHPLAKRKSVtpedlageRLLLLEEGHCLRDQALELCRLAGAREQTDFEATSLETLRQMVAAGLGIT 148
PRK13348 PRK13348
HTH-type transcriptional regulator ArgP;
10-81 3.80e-05

HTH-type transcriptional regulator ArgP;


Pssm-ID: 237357 [Multi-domain]  Cd Length: 294  Bit Score: 44.58  E-value: 3.80e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654546228  10 NLDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARhGRNKLLTEHGIQLLGYARKI 81
Cdd:PRK13348   1 MLDYKQLEALAAVVETGSFERAARRLHVTPSAVSQRIKALEESLGQPLLVR-GRPCRPTPAGQRLLRHLRQV 71
PBP2_LTTR_like_6 cd08423
The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional ...
 101-260 4.05e-04

The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator, contains the type 2 periplasmic binding fold; LysR-transcriptional regulators comprise 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, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to a name a few. 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: 176115 [Multi-domain]  Cd Length: 200  Bit Score: 40.66  E-value: 4.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 101 LTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTH-------RPGQFDCLTLRTSPTHW 173
Cdd:cd08423    2 LRVGAFPTAAAALLPPALAALRARHPGLEVRLREAEPPESLDALRAGELDLAVVFDypvtpppDDPGLTRVPLLDDPLDL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 174 YCAAEYVLQKGEPVPLV-LLDDP-------SPFRDMVLTALNEANIPWRLAYVASTLPAVRAAVKAGLGVTarpvemMSP 245
Cdd:cd08423   82 VLPADHPLAGREEVALAdLADEPwiagcpgSPCHRWLVRACRAAGFTPRIAHEADDYATVLALVAAGLGVA------LVP 155

                        170
                 ....*....|....*
gi 654546228 246 DLRVLGKSDGLPALP 260
Cdd:cd08423  156 RLALGARPPGVVVRP 170
PRK11482 PRK11482
DNA-binding transcriptional regulator;
6-156 4.39e-04

DNA-binding transcriptional regulator;


Pssm-ID: 183159 [Multi-domain]  Cd Length: 317  Bit Score: 41.25  E-value: 4.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228   6 RPIMNLDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILrfn 85
Cdd:PRK11482  24 RTLRNIDLNLLTIFEAVYVHKGIVNAAKILNLTPSAISQSIQKLRVIFPDPLFIRKGQGVTPTAYATHLHEYISQGL--- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  86 dEACMSLMfsNLQG------VLTLGASDESADTILPFLLNRISSVYPKLALdvsvkRNAFMVE---MLNENKVDLVVTTH 156
Cdd:PRK11482 101 -ESILGAL--DITGsydkqrTITIATTPSVGALVMPVIYQAIKTHYPQLLL-----RNIPISDaenQLSQFQTDLIIDTH 172
PBP2_Nitroaromatics_like cd08417
The C-terminal substrate binding domain of LysR-type transcriptional regulators that involved ...
 100-158 5.86e-04

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: 40.28  E-value: 5.86e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 654546228 100 VLTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHRP 158
Cdd:cd08417    1 TFRIAASDYLEALLLPPLLARLRQEAPGVRLRFVPLDRDDLEEALESGEIDLAIGVFPE 59
PBP2_GltC_like cd08434
The substrate binding domain of LysR-type transcriptional regulator GltC, which activates gltA ...
 102-236 6.16e-04

The substrate binding domain of LysR-type transcriptional regulator GltC, which activates gltA expression of glutamate synthase operon, contains type 2 periplasmic binding fold; GltC, a member of the LysR family of bacterial transcriptional factors, activates the expression of gltA gene of glutamate synthase operon and is essential for cell growth in the absence of glutamate. Glutamate synthase is a heterodimeric protein that encoded by gltA and gltB, whose expression is subject to nutritional regulation. GltC also negatively auto-regulates its own expression. This substrate-binding domain has strong 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: 176125 [Multi-domain]  Cd Length: 195  Bit Score: 40.21  E-value: 6.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 102 TLGASdesadtILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHRP--GQFDCLTLRTSPthwYCAA-- 177
Cdd:cd08434    9 SLGTS------LVPDLIRAFRKEYPNVTFELHQGSTDELLDDLKNGELDLALCSPVPdePDIEWIPLFTEE---LVLVvp 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654546228 178 -EYVLQKGEPV--------PLVLLDDPSPFRDMVLTALNEANIPWRLAYVASTLPAVRAAVKAGLGVT 236
Cdd:cd08434   80 kDHPLAGRDSVdlaeladePFVLLSPGFGLRPIVDELCAAAGFTPKIAFEGEEDSTIAGLVAAGLGVA 147
cysB PRK12681
HTH-type transcriptional regulator CysB;
39-155 6.93e-04

HTH-type transcriptional regulator CysB;


Pssm-ID: 183678 [Multi-domain]  Cd Length: 324  Bit Score: 40.65  E-value: 6.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  39 QSAVSQQMQRLEQLVGKELFARHGRN-KLLTEHGIQLLGYARKILRfNDEACMSLM--FSNL-QGVLTLGASDESADTIL 114
Cdd:PRK12681  30 QPGISKQVRMLEDELGIQIFARSGKHlTQVTPAGEEIIRIAREILS-KVESIKSVAgeHTWPdKGSLYIATTHTQARYAL 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 654546228 115 PFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTT 155
Cdd:PRK12681 109 PPVIKGFIERYPRVSLHMHQGSPTQIAEAAAKGNADFAIAT 149
PRK10341 PRK10341
transcriptional regulator TdcA;
38-155 6.98e-04

transcriptional regulator TdcA;


Pssm-ID: 182391 [Multi-domain]  Cd Length: 312  Bit Score: 40.62  E-value: 6.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  38 TQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILR--FNDEACMSLMFSNLQGVLTLGASDESADTILP 115
Cdd:PRK10341  34 TQPAVSKIINDIEDYFGVELIVRKNTGVTLTPAGQVLLSRSESITRemKNMVNEINGMSSEAVVDVSFGFPSLIGFTFMS 113

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 654546228 116 FLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTT 155
Cdd:PRK10341 114 DMINKFKEVFPKAQVSMYEAQLSSFLPAIRDGRLDFAIGT 153
PBP2_Nac cd08433
The C-teminal substrate binding domain of LysR-like nitrogen assimilation control (NAC) ...
 101-236 8.23e-04

The C-teminal substrate binding domain of LysR-like nitrogen assimilation control (NAC) protein, contains the type 2 periplasmic binding fold; The NAC is a LysR-type transcription regulator that activates expression of operons such as hut (histidine utilization) and ure (urea utilization), allowing use of non-preferred (poor) nitrogen sources, and represses expression of operons, such as glutamate dehydrogenase (gdh), allowing assimilation of the preferred nitrogen source. The expression of the nac gene is fully dependent on the nitrogen regulatory system (NTR) and the sigma54-containing RNA polymerase (sigma54-RNAP). In response to nitrogen starvation, NTR system activates the expression of nac, and NAC activates the expression of hut, ure, and put (proline utilization). NAC is not involved in the transcription of Sigma70-RNAP operons such as glnA, which directly respond by the NTR system, but activates the transcription of sigma70-RNAP dependent operons such as hut. Hence, NAC allows the coupling of sigma70-RNAP dependent operons to the sigma54-RNAP dependent NTR system. 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: 176124  Cd Length: 198  Bit Score: 39.89  E-value: 8.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 101 LTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVV--TTHRPGQFDCLTLRTSPTHWYCAAE 178
Cdd:cd08433    2 VSVGLPPSAASVLAVPLLRAVRRRYPGIRLRIVEGLSGHLLEWLLNGRLDLALlyGPPPIPGLSTEPLLEEDLFLVGPAD 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 654546228 179 YVLQKGEPV--------PLVLLDDPSPFRDMVLTALNEANIPWRLAYVASTLPAVRAAVKAGLGVT 236
Cdd:cd08433   82 APLPRGAPVplaelarlPLILPSRGHGLRRLVDEAAARAGLTLNVVVEIDSVATLKALVAAGLGYT 147
PBP2_LTTR_like_5 cd08426
The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional ...
 102-236 8.43e-04

The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional regulator, contains the type 2 periplasmic binding fold; LysR-transcriptional regulators comprise 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, nodule formation of nitrogen-fixing bacteria, and synthesis of virulence factors, to a name a few. 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: 176117 [Multi-domain]  Cd Length: 199  Bit Score: 39.60  E-value: 8.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 102 TLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHRPGQFDcltLRTSPTHW--YCAaey 179
Cdd:cd08426    3 RVATGEGLAAELLPSLIARFRQRYPGVFFTVDVASTADVLEAVLSGEADIGLAFSPPPEPG---IRVHSRQPapIGA--- 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 654546228 180 VLQKGEPV--------------PLVLLDDPSPFRDMVLTALNEANIPWRLAYVASTLPAVRAAVKAGLGVT 236
Cdd:cd08426   77 VVPPGHPLarqpsvtlaqlagyPLALPPPSFSLRQILDAAFARAGVQLEPVLISNSIETLKQLVAAGGGIS 147
PRK15421 PRK15421
HTH-type transcriptional regulator MetR;
11-82 2.34e-03

HTH-type transcriptional regulator MetR;


Pssm-ID: 185319 [Multi-domain]  Cd Length: 317  Bit Score: 39.23  E-value: 2.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 654546228  11 LDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKIL 82
Cdd:PRK15421   2 IEVKHLKTLQALRNCGSLAAAAATLHQTQSALSHQFSDLEQRLGFRLFVRKSQPLRFTPQGEILLQLANQVL 73
PBP2_CysB cd08443
The C-terminal substrate domain of LysR-type transcriptional regulator CysB contains type 2 ...
 101-235 2.66e-03

The C-terminal substrate domain of LysR-type transcriptional regulator CysB contains type 2 periplasmic binding fold; CysB is a transcriptional activator of genes involved in sulfate and thiosulfate transport, sulfate reduction, and cysteine synthesis. In Escherichia coli, the regulation of transcription in response to sulfur source is attributed to two transcriptional regulators, CysB and Cbl. CysB, in association with Cbl, downregulates the expression of ssuEADCB operon which is required for the utilization of sulfur from aliphatic sulfonates, in the presence of cysteine. Also, Cbl and CysB together directly function as transcriptional activators of tauABCD genes, which are required for utilization of taurine as sulfur source for growth. Like many other members of the LTTR family, CysB is 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 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: 176134  Cd Length: 198  Bit Score: 38.31  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 101 LTLGASDESADTILPFLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHRPGQFDclTLRTSPT-HW----YC 175
Cdd:cd08443    2 LYVATTHTQARYVLPPVIKGFIERYPRVSLQMHQGSPTQIAEMVSKGLVDFAIATEALHDYD--DLITLPCyHWnrcvVV 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 654546228 176 AAEYVLQKGEPV--------PLVLLDDPSPFRDMVLTALNEANIPWRLAYVASTLPAVRAAVKAGLGV 235
Cdd:cd08443   80 KRDHPLADKQSIsieelatyPIVTYTFGFTGRSELDTAFNRAGLTPNIVLTATDADVIKTYVRLGLGV 147
PRK11233 PRK11233
nitrogen assimilation transcriptional regulator; Provisional
 9-239 2.95e-03

nitrogen assimilation transcriptional regulator; Provisional


Pssm-ID: 183045 [Multi-domain]  Cd Length: 305  Bit Score: 38.90  E-value: 2.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228   9 MNLDLdlLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKILRFNDEA 88
Cdd:PRK11233   1 MNFRR--LKYFVKIVDIGSLTQAAEVLHIAQPALSQQVATLEGELNQQLLIRTKRGVTPTEAGKILYTHARAILRQCEQA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228  89 CMSLMFSN--LQGVLTLG-ASDESADTI-LPfLLNRISSVYPKLALDVSVKRNAFMVEMLNENKVDLVVTTHR--PGQFD 162
Cdd:PRK11233  79 QLAVHNVGqaLSGQVSIGlAPGTAASSLtMP-LLQAVRAEFPGIVLYLHENSGATLNEKLMNGQLDMAVIYEHspVAGLS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 654546228 163 CLTLRTSPTHWYCAAEyvlQKGEPVPLVLLDD-----PSPFrDMVLTALNEANIPWRLAY-------VASTLpavRAAVK 230
Cdd:PRK11233 158 SQPLLKEDLFLVGTQD---CPGQSVDLAAVAQmnlflPRDY-SAVRLRVDEAFSLRRLTAkvigeieSIATL---TAAIA 230


                 ....*....
gi 654546228 231 AGLGVTARP 239
Cdd:PRK11233 231 SGMGVTVLP 239
leuO PRK09508
leucine transcriptional activator; Reviewed
 10-82 3.79e-03

leucine transcriptional activator; Reviewed


Pssm-ID: 181918 [Multi-domain]  Cd Length: 314  Bit Score: 38.47  E-value: 3.79e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 654546228  10 NLDLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQLLGYARKIL 82
Cdd:PRK09508  21 MVDLNLLTVFDAVMQEQNITRAAHNLGMSQPAVSNAVARLKVMFNDELFVRYGRGIQPTARARQLFGPVRQAL 93
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH