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Conserved domains on  [gi|754692769|ref|WP_042070252|]
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MULTISPECIES: LysR substrate-binding domain-containing protein [Aeromonas]

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;
6-306 2.10e-53

HTH-type transcriptional regulator YidZ;


The actual alignment was detected with superfamily member PRK10216:

Pssm-ID: 182312 [Multi-domain]  Cd Length: 319  Bit Score: 177.70  E-value: 2.10e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769   6 LARIDLNLLIILQVLLEERNGSKAARRLHLSQSAVSKALGRLRETFDDPLFIRSAYGLEPTARAQTLQQQLQPILLSLDN 85
Cdd:PRK10216   5 LTTLDLNLLLCLQLLMQERSVTKAAKRMNVTPSAVSKSLAKLRAWFDDPLFVNTPLGLSPTPLMVSMEQNLAEWMQMGNQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769  86 LIQPPAFDPASSEReFVIASMdsaftlfAPLYLSELKRQAPRIRLRYEE-------WTENSLTEMSQGQVDIAFTVRENC 158
Cdd:PRK10216  85 LLDKPHHQTPRGLK-FELAAE-------SPLMMIMLNALSKRIYQRYPQatiklrnWDYDSLDAITRGEVDIGFTGRESH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 159 INSDYRLDTLPSSICQRLLAIDGLTCLVQKHHPALREPgWDLDHYLRYPHVQTYCEGRDRWMLDYKLAEQDLYRRIEATV 238
Cdd:PRK10216 157 PRSRELLSLLPLAIDFEVLFSDLPCVWLRKDHPALHEE-WNLDTFLRYPHISICWEQSDTWALDDVLQELGRERTIALSL 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754692769 239 PSFEAALRMGM--HSDMIVTlSSLYARHATQVY--PLMQLPLPIELDSISHL-----LIWHQRHDEDPGHRWLRETL 306
Cdd:PRK10216 236 PEFEQSLFMAAqpDHLLLAT-APRYCQYYNQLHqlPLVALPLPFDESQQKKLevpftLLWHKRNSHNPKIVWLRETI 311
 
Name Accession Description Interval E-value
PRK10216 PRK10216
HTH-type transcriptional regulator YidZ;
6-306 2.10e-53

HTH-type transcriptional regulator YidZ;


Pssm-ID: 182312 [Multi-domain]  Cd Length: 319  Bit Score: 177.70  E-value: 2.10e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769   6 LARIDLNLLIILQVLLEERNGSKAARRLHLSQSAVSKALGRLRETFDDPLFIRSAYGLEPTARAQTLQQQLQPILLSLDN 85
Cdd:PRK10216   5 LTTLDLNLLLCLQLLMQERSVTKAAKRMNVTPSAVSKSLAKLRAWFDDPLFVNTPLGLSPTPLMVSMEQNLAEWMQMGNQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769  86 LIQPPAFDPASSEReFVIASMdsaftlfAPLYLSELKRQAPRIRLRYEE-------WTENSLTEMSQGQVDIAFTVRENC 158
Cdd:PRK10216  85 LLDKPHHQTPRGLK-FELAAE-------SPLMMIMLNALSKRIYQRYPQatiklrnWDYDSLDAITRGEVDIGFTGRESH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 159 INSDYRLDTLPSSICQRLLAIDGLTCLVQKHHPALREPgWDLDHYLRYPHVQTYCEGRDRWMLDYKLAEQDLYRRIEATV 238
Cdd:PRK10216 157 PRSRELLSLLPLAIDFEVLFSDLPCVWLRKDHPALHEE-WNLDTFLRYPHISICWEQSDTWALDDVLQELGRERTIALSL 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754692769 239 PSFEAALRMGM--HSDMIVTlSSLYARHATQVY--PLMQLPLPIELDSISHL-----LIWHQRHDEDPGHRWLRETL 306
Cdd:PRK10216 236 PEFEQSLFMAAqpDHLLLAT-APRYCQYYNQLHqlPLVALPLPFDESQQKKLevpftLLWHKRNSHNPKIVWLRETI 311
PBP2_Nitroaromatics_like cd08417
The C-terminal substrate binding domain of LysR-type transcriptional regulators that involved ...
100-307 6.48e-53

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: 172.78  E-value: 6.48e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 100 EFVIASMDSAFTLFAPLYLSELKRQAPRIRLRYEEWT-ENSLTEMSQGQVDIAFTVrencinsdyrLDTLPSSICQRLLA 178
Cdd:cd08417    1 TFRIAASDYLEALLLPPLLARLRQEAPGVRLRFVPLDrDDLEEALESGEIDLAIGV----------FPELPPGLRSQPLF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 179 IDGLTCLVQKHHPALREPgWDLDHYLRYPHVQTYCEGRDRWMLDYKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTLS 258
Cdd:cd08417   71 EDRFVCVARKDHPLAGGP-LTLEDYLAAPHVLVSPRGRGHGLVDDALAELGLSRRVALTVPHFLAAPALVAGTDLIATVP 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 754692769 259 SLYARHATQVYPLMQLPLPIELDSISHLLIWHQRHDEDPGHRWLRETLL 307
Cdd:cd08417  150 RRLAEALAERLGLRVLPLPFELPPFTVSLYWHPRRDRDPAHRWLRELIA 198
LysR COG0583
DNA-binding transcriptional regulator, LysR family [Transcription];
9-310 4.26e-29

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


Pssm-ID: 440348 [Multi-domain]  Cd Length: 256  Bit Score: 112.27  E-value: 4.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769   9 IDLNLLIILQVLLEERNGSKAARRLHLSQSAVSKALGRLRETFDDPLFIRSAYGLEPTARAQTLQQQLQPILLSLDNLIQ 88
Cdd:COG0583    1 MDLRQLRAFVAVAEEGSFTAAAERLGVSQPAVSRQIRRLEEELGVPLFERTGRGLRLTEAGERLLERARRILAELEEAEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769  89 PPAFDPASSEREFVIASMDSAFTLFAPLYLSELKRQAPRIRLRYEEWTENSLTEM-SQGQVDIAFTVRENcinsdyrldt 167
Cdd:COG0583   81 ELRALRGGPRGTLRIGAPPSLARYLLPPLLARFRARHPGVRLELREGNSDRLVDAlLEGELDLAIRLGPP---------- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 168 LPSSICQRLLAIDGLTCLVQKHHPalrepgwdldhylryphvqtycegrdrwmldykLAEQdlyrriEATVPSFEAALRM 247
Cdd:COG0583  151 PDPGLVARPLGEERLVLVASPDHP---------------------------------LARR------APLVNSLEALLAA 191
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754692769 248 GMHSDMIVTLSSLYARHATQVYPLMQLPLPIELDSISHLLIWHQRHDEDPGHRWLRETLLTQI 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 ...
98-309 4.47e-16

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: 75.40  E-value: 4.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769   98 EREFVIASMDSAFTLFAPLYLSELKRQAPRIRLR-YEEWTENSLTEMSQGQVDIAFTvrencinsdyRLDTLPSSICQRL 176
Cdd:pfam03466   1 SGRLRIGAPPTLASYLLPPLLARFRERYPDVELElTEGNSEELLDLLLEGELDLAIR----------RGPPDDPGLEARP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769  177 LAIDGLTCLVQKHHPALREPGWDLDHYLRYPHVQTYCEGRDRWMLDYKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVT 256
Cdd:pfam03466  71 LGEEPLVLVAPPDHPLARGEPVSLEDLADEPLILLPPGSGLRDLLDRALRAAGLRPRVVLEVNSLEALLQLVAAGLGIAL 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 754692769  257 LSSLYARHATQVYPLMQLPLPIELDSISHLLIWHQRHDEDPGHRWLRETLLTQ 309
Cdd:pfam03466 151 LPRSAVARELADGRLVALPLPEPPLPRELYLVWRKGRPLSPAVRAFIEFLREA 203
LysR_Sec_metab NF040786
selenium metabolism-associated LysR family transcriptional regulator; LysR family ...
9-153 1.94e-07

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: 51.85  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769   9 IDLNLLIILQVLLEERNGSKAARRLHLSQSAVSKALGRLRETFDDPLFIRSAYGLEPTARAQTLQQQLQPILLSLDNLIQ 88
Cdd:NF040786   1 MNLKQLEAFVNVAEYKSFSKAAKKLFLTQPTISAHISSLEKELGVRLFVRNTKEVSLTEDGKLLYEYAKEMLDLWEKLEE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754692769  89 ppAFDPASSEREFVI---ASMDSAfTLFAPLYLSELKRQAPRIRLR-YEEWTENSLTEMSQGQVDIAFT 153
Cdd:NF040786  81 --EFDRYGKESKGVLrigASTIPG-QYLLPELLKKFKEKYPNVRFKlMISDSIKVIELLLEGEVDIGFT 146
decaheme_TF NF041036
multiheme cytochrome-associated LysR family transcriptional regulator; Members of this family, ...
17-67 7.52e-06

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: 47.04  E-value: 7.52e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 754692769  17 LQVLLEERNGSKAARRLHLSQSAVSKALGRLRETFDDPLFIRSAYGLEPTA 67
Cdd:NF041036   9 LVIVAEEGSFSKAAEKLHLTQSAVSQRIKFLEECYGYQLFDRSGPSLEPTA 59
 
Name Accession Description Interval E-value
PRK10216 PRK10216
HTH-type transcriptional regulator YidZ;
6-306 2.10e-53

HTH-type transcriptional regulator YidZ;


Pssm-ID: 182312 [Multi-domain]  Cd Length: 319  Bit Score: 177.70  E-value: 2.10e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769   6 LARIDLNLLIILQVLLEERNGSKAARRLHLSQSAVSKALGRLRETFDDPLFIRSAYGLEPTARAQTLQQQLQPILLSLDN 85
Cdd:PRK10216   5 LTTLDLNLLLCLQLLMQERSVTKAAKRMNVTPSAVSKSLAKLRAWFDDPLFVNTPLGLSPTPLMVSMEQNLAEWMQMGNQ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769  86 LIQPPAFDPASSEReFVIASMdsaftlfAPLYLSELKRQAPRIRLRYEE-------WTENSLTEMSQGQVDIAFTVRENC 158
Cdd:PRK10216  85 LLDKPHHQTPRGLK-FELAAE-------SPLMMIMLNALSKRIYQRYPQatiklrnWDYDSLDAITRGEVDIGFTGRESH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 159 INSDYRLDTLPSSICQRLLAIDGLTCLVQKHHPALREPgWDLDHYLRYPHVQTYCEGRDRWMLDYKLAEQDLYRRIEATV 238
Cdd:PRK10216 157 PRSRELLSLLPLAIDFEVLFSDLPCVWLRKDHPALHEE-WNLDTFLRYPHISICWEQSDTWALDDVLQELGRERTIALSL 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754692769 239 PSFEAALRMGM--HSDMIVTlSSLYARHATQVY--PLMQLPLPIELDSISHL-----LIWHQRHDEDPGHRWLRETL 306
Cdd:PRK10216 236 PEFEQSLFMAAqpDHLLLAT-APRYCQYYNQLHqlPLVALPLPFDESQQKKLevpftLLWHKRNSHNPKIVWLRETI 311
PBP2_Nitroaromatics_like cd08417
The C-terminal substrate binding domain of LysR-type transcriptional regulators that involved ...
100-307 6.48e-53

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: 172.78  E-value: 6.48e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 100 EFVIASMDSAFTLFAPLYLSELKRQAPRIRLRYEEWT-ENSLTEMSQGQVDIAFTVrencinsdyrLDTLPSSICQRLLA 178
Cdd:cd08417    1 TFRIAASDYLEALLLPPLLARLRQEAPGVRLRFVPLDrDDLEEALESGEIDLAIGV----------FPELPPGLRSQPLF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 179 IDGLTCLVQKHHPALREPgWDLDHYLRYPHVQTYCEGRDRWMLDYKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTLS 258
Cdd:cd08417   71 EDRFVCVARKDHPLAGGP-LTLEDYLAAPHVLVSPRGRGHGLVDDALAELGLSRRVALTVPHFLAAPALVAGTDLIATVP 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 754692769 259 SLYARHATQVYPLMQLPLPIELDSISHLLIWHQRHDEDPGHRWLRETLL 307
Cdd:cd08417  150 RRLAEALAERLGLRVLPLPFELPPFTVSLYWHPRRDRDPAHRWLRELIA 198
PBP2_DntR_like_1 cd08460
The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional ...
101-310 8.35e-33

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: 120.39  E-value: 8.35e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 101 FVIASMDSAFTLFAPLYLSELKRQAPRIRLRYEEWTENSLTEMSQGQVDIAFTVrencinsdyrLDTLPSSICQRLLAID 180
Cdd:cd08460    2 FTIRANDGFVAAFGPALLAAVAAEAPGVRLRFVPESDKDVDALREGRIDLEIGV----------LGPTGPEIRVQTLFRD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 181 GLTCLVQKHHPALREPgWDLDHYLRYPHVQTYCEGRDRWMLDYKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTLSSL 260
Cdd:cd08460   72 RFVGVVRAGHPLARGP-ITPERYAAAPHVSVSRRGRLHGPIDDALAALGLTRRVVAVVPTFAAALFLARGSDLIALVPER 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 754692769 261 YARHATQVYPLMQLPLPIELDSISHLLIWHQRHDEDPGHRWLRETLLTQI 310
Cdd:cd08460  151 VTAAARAGLGLRTFPLPLELPAVTVSQAWHPRFDADPAHRWLRECVREVC 200
PBP2_SyrM cd08467
The C-terminal substrate binding of LysR-type symbiotic regulator SyrM, which activates ...
100-308 1.85e-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: 111.76  E-value: 1.85e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 100 EFVIASMDSAFTLFAPLYLSELKRQAPRIRLRYEEWTEN-SLTEMSQGQVDIAFTvrencinsdyRLDTLPSSICQRLLA 178
Cdd:cd08467    1 GFTLAMPDYAEVALLPRLAPRLRERAPGLDLRLCPIGDDlAERGLEQGTIDLAVG----------RFAVPPDGLVVRRLY 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 179 IDGLTCLVQKHHPALREPgWDLDHYLRYPHVQTYCEGRDRWMLDYKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTLS 258
Cdd:cd08467   71 DDGFACLVRHGHPALAQE-WTLDDFATLRHVAIAPPGRLFGGIYKRLENLGLKRNVAIAVSSFLTAAATVAATDLIATVP 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 754692769 259 SLYARHATQVYPLMQLPLPIELDSISHLLIWHQRHDEDPGHRWLRETLLT 308
Cdd:cd08467  150 RRVATQVAAMLPLRVVPPPVDLGTFPVMLIWHERYQHDPAHRWLRKLIAA 199
LysR COG0583
DNA-binding transcriptional regulator, LysR family [Transcription];
9-310 4.26e-29

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


Pssm-ID: 440348 [Multi-domain]  Cd Length: 256  Bit Score: 112.27  E-value: 4.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769   9 IDLNLLIILQVLLEERNGSKAARRLHLSQSAVSKALGRLRETFDDPLFIRSAYGLEPTARAQTLQQQLQPILLSLDNLIQ 88
Cdd:COG0583    1 MDLRQLRAFVAVAEEGSFTAAAERLGVSQPAVSRQIRRLEEELGVPLFERTGRGLRLTEAGERLLERARRILAELEEAEA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769  89 PPAFDPASSEREFVIASMDSAFTLFAPLYLSELKRQAPRIRLRYEEWTENSLTEM-SQGQVDIAFTVRENcinsdyrldt 167
Cdd:COG0583   81 ELRALRGGPRGTLRIGAPPSLARYLLPPLLARFRARHPGVRLELREGNSDRLVDAlLEGELDLAIRLGPP---------- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 168 LPSSICQRLLAIDGLTCLVQKHHPalrepgwdldhylryphvqtycegrdrwmldykLAEQdlyrriEATVPSFEAALRM 247
Cdd:COG0583  151 PDPGLVARPLGEERLVLVASPDHP---------------------------------LARR------APLVNSLEALLAA 191
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 754692769 248 GMHSDMIVTLSSLYARHATQVYPLMQLPLPIELDSISHLLIWHQRHDEDPGHRWLRETLLTQI 310
Cdd:COG0583  192 VAAGLGIALLPRFLAADELAAGRLVALPLPDPPPPRPLYLVWRRRRHLSPAVRAFLDFLREAL 254
PBP2_DntR_NahR_LinR_like cd08459
The C-terminal substrate binding domain of LysR-type transcriptional regulators that are ...
100-306 2.03e-27

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: 106.12  E-value: 2.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 100 EFVIASMDSAFTLFAPLYLSELKRQAPRIRLRYEEWTENSL-TEMSQGQVDIAFTVrencinsdyrLDTLPSSICQRLLA 178
Cdd:cd08459    1 TFRIAMSDIGEMYFLPRLLAALREVAPGVRIETVRLPVDELeEALESGEIDLAIGY----------LPDLGAGFFQQRLF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 179 IDGLTCLVQKHHPALREPgWDLDHYLRYPHVQTYCEGRDRWMLDYKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTLS 258
Cdd:cd08459   71 RERYVCLVRKDHPRIGST-LTLEQFLAARHVVVSASGTGHGLVEQALREAGIRRRIALRVPHFLALPLIVAQTDLVATVP 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 754692769 259 SLYARHATQVYPLMQLPLPIELDSISHLLIWHQRHDEDPGHRWLRETL 306
Cdd:cd08459  150 ERLARLFARAGGLRIVPLPFPLPPFEVKLYWHRRFHRDPGNRWLRQLV 197
PBP2_DntR_like_2 cd08464
The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional ...
101-306 2.49e-27

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: 106.16  E-value: 2.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 101 FVIASMDSAFTLFAPLYLSELKRQAPRIRLRYEewTENSLT--EM-SQGQVDIAFTVrencinsdyrLDTLPSSICQRLL 177
Cdd:cd08464    2 FRIGLSDDVESWLAPPLLAALRAEAPGVRLVFR--QVDPFNvgDMlDRGEIDLAIGV----------FGELPAWLKREVL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 178 AIDGLTCLVQKHHPALREPgWDLDHYLRYPHVQTYCEGRDRWMLDYKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTL 257
Cdd:cd08464   70 YTEGYACLFDPQQLSLSAP-LTLEDYVARPHVLVSYRGGLRGFVDDALAELGRSRRVVASTPHFAALPALLRGTPLIATV 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 754692769 258 SSLYARHATQVYPLMQLPLPIELDSISHLLIWHQRHDEDPGHRWLRETL 306
Cdd:cd08464  149 PARLARAWAAALGLRASPPPLDLPEFPISLLWHARTDNDPALVWLREQI 197
PBP2_DntR_like_4 cd08463
The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional ...
100-306 2.50e-26

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: 103.55  E-value: 2.50e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 100 EFVIASMDSAFTLFAPLYLSELKRQAPRIRLRYEEWT--ENSLTEMSQGQVDIAFTVRencinsdyrlDTLPSSICQRLL 177
Cdd:cd08463    1 TFRIAAPDYLNALFLPELVARFRREAPGARLEIHPLGpdFDYERALASGELDLVIGNW----------PEPPEHLHLSPL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 178 AIDGLTCLVQKHHPALREPGWDLDHYLRYPHV--QTYCEGRdRWMLDYKLAEQDLYRRIEATVPSFEAALRMGMHSDMIV 255
Cdd:cd08463   71 FSDEIVCLMRADHPLARRGLMTLDDYLEAPHLapTPYSVGQ-RGVIDSHLARLGLKRNIVVTVPYFGLAPYMLAQSDLVF 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 754692769 256 TLSSLYARHATQVYPLMQLPLPIELDSISHLLIWHQRHDEDPGHRWLRETL 306
Cdd:cd08463  150 TTGRHFAEHYAKLLPLAVVDAPIEFPRMRYYQLWHERSHRSPEHRWLRRLV 200
leuO PRK09508
leucine transcriptional activator; Reviewed
5-310 1.61e-24

leucine transcriptional activator; Reviewed


Pssm-ID: 181918 [Multi-domain]  Cd Length: 314  Bit Score: 101.25  E-value: 1.61e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769   5 QLARIDLNLLIILQVLLEERNGSKAARRLHLSQSAVSKALGRLRETFDDPLFIRSAYGLEPTARAQTLQQQLQPILLSLD 84
Cdd:PRK09508  18 QLRMVDLNLLTVFDAVMQEQNITRAAHNLGMSQPAVSNAVARLKVMFNDELFVRYGRGIQPTARARQLFGPVRQALQLVQ 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769  85 NLIQPPAFDPASSEREFVIASMDSAFTLFAPLYLSELKRQAPRIRLRYEEWTENSLTEMSQGQvDIAFTVrencinsDY- 163
Cdd:PRK09508  98 NELPGSGFEPESSERVFNLCICSPLDIRLTSQIYNRIEQIAPNIHVVFKSSLNQNIEHQLRYQ-ETEFVI-------SYe 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 164 RLDTlpSSICQRLLAIDGLTCLVQKHHPALREPgWDLDHYLRYPHVQTYCEGRDRWMLDYkLAEQDLYRRIEATVPSFEA 243
Cdd:PRK09508 170 EFDR--PEFTSVPLFKDELVLVASKNHPRIKGP-ITEEQLYNEQHAVVSLDRFASFSQPW-YDTVDKQASIAYQGTALSS 245
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 754692769 244 ALRMGMHSDMIVTLSSLYARHATQVYPLMQLPLPIELDSISHLLIWHQRHDEDPGHRWLREtLLTQI 310
Cdd:PRK09508 246 VLNVVSQTHLVAIAPRWLAEEFAESLELQILPLPLKNNSRTCYLSWHESAGRDKGHQWMEE-LLVSI 311
PBP2_LeuO cd08466
The C-terminal substrate binding domain of LysR-type transcriptional regulator LeuO, an ...
100-308 5.27e-23

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: 94.24  E-value: 5.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 100 EFVIASMDSAFTLFAPLYLSELKRQAPRIRLRYEEWTENSLTE-MSQGQVDIAFtvrencinsDYrLDTLPSSICQRLLA 178
Cdd:cd08466    1 TFNIAANETLDLLLLPRLLARLKQLAPNISLRESPSSEEDLFEdLRLQEVDLVI---------DY-VPFRDPSFKSELLF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 179 IDGLTCLVQKHHPALREPgWDLDHYLRYPHVqTYCEGRDRWMLDYKLAEQDLY-RRIEATVPSFEAALRMGMHSDMIVTL 257
Cdd:cd08466   71 EDELVCVARKDHPRIQGS-LSLEQYLAEKHV-VLSLRRGNLSALDLLTEEVLPqRNIAYEVSSLLSMLAVVSQTDLIAIA 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 754692769 258 SSLYARHATQVYPLMQLPLPIELDSISHLLIWHQRHDEDPGHRWLRETLLT 308
Cdd:cd08466  149 PRWLADQYAEQLNLQILPLPFKTKPIPLYMVWHKSRERDPAHQWLREQIKQ 199
PBP2_PnbR cd08469
The C-terminal substrate binding domain of LysR-type transcriptional regulator PnbR, which is ...
101-306 6.25e-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: 94.78  E-value: 6.25e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 101 FVIASMDSAFTLFAPLYLSELKRQAPRIRLRYEEWTENSLTE-MSQGQVDIAFTVRENcinsdyrldtLPSSICQRLLAI 179
Cdd:cd08469    2 FVIAANDYVTAVLLPALVRRLETEAPGIDLRIRPVTRLDLAEqLDLGRIDLVIGIFEQ----------IPPRFRRRTLFD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 180 DGLTCLVQKHHPALREPgWDLDHYLRYPHVQTYCEGR---------------------DRWMLDYKLAEQDLYRRIEATV 238
Cdd:cd08469   72 EDEVWVMRKDHPAARGA-LTIETLARYPHIVVSLGGEeegavsgfiserglarqtemfDRRALEEAFRESGLVPRVAVTV 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 754692769 239 PSFEAALRMGMHSDMIVTLSSLYARHATQVYPLMQLPLPIELDSISHLLIWHQRHDEDPGHRWLRETL 306
Cdd:cd08469  151 PHALAVPPLLADSDMLALLPRSLARAFAERGGLVMKEPPYPPPPVQIRAVWHERHDNDPAVAWLREMI 218
PBP2_DntR_like_3 cd08461
The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional ...
101-306 1.13e-22

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: 93.50  E-value: 1.13e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 101 FVIASMDSAFTLFAPLYLSELKRQAPRIRLRYEEWTENSLT-EMSQGQVDIAFTVREncinsdyrldTLPSSICQRLLAI 179
Cdd:cd08461    2 LVIAATDYAQKAILPPLLAALRQEAPGVRVAIRDLESDNLEaQLERGEVDLALTTPE----------YAPDGLRSRPLFE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 180 DGLTCLVQKHHPALREPgWDLDHYLRYPH-VQTYCEGRDRWMLDYKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTLS 258
Cdd:cd08461   72 ERYVCVTRRGHPLLQGP-LSLDQFCALDHiVVSPSGGGFAGSTDEALAALGLTRNVVLSVPSFLVVPEILAATDMVAFVP 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 754692769 259 SLYARHATQvypLMQLPLPIELDSISHLLIWHQRHDEDPGHRWLRETL 306
Cdd:cd08461  151 SRLVPNLEG---LQEVELPLEPPGFDVVMAWHERTHRDPAHRWLRELL 195
PBP2_ToxR cd08465
The C-terminal substrate binding domain of LysR-type transcriptional regulator ToxR regulates ...
101-306 2.94e-20

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: 86.98  E-value: 2.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 101 FVIASMDSAFTLFAPLYLSELKRQAPRIRLRYEEWT-ENSLTEMSQGQVDIAFTVrencinsdyrLDTLPSSICQRLLAI 179
Cdd:cd08465    2 FRLAMSDYGARLVLPALMRQLRAEAPGIDLAVSQASrEAMLAQVADGEIDLALGV----------FPELPEELHAETLFE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 180 DGLTCLVQKHHpaLREPG-WDLDHYLRYPHVQTYCEGRDRWMLDYKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTLS 258
Cdd:cd08465   72 ERFVCLADRAT--LPASGgLSLDAWLARPHVLVAMRGDAANEIDRALAARGLRRRVALTLPHWGVAPELIAGTDLILTVA 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 754692769 259 SLYARHATQVYPLMQLPLPIELDSISHLLIWHQRHDEDPGHRWLRETL 306
Cdd:cd08465  150 RRALDALRLDERLAVFAPPFPIPPFAFQQIWHQRREGDPAHRWLRERI 197
PBP2_NodD cd08462
The C-terminal substsrate binding domain of NodD family of LysR-type transcriptional ...
100-307 4.66e-20

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: 86.53  E-value: 4.66e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 100 EFVIASMDSAFTLFAPLYLSELKRQAPRIRLRYEEWTENSLTEMSQGQVDIAFTVrencinSDYRLDTLPSSIcqrlLAI 179
Cdd:cd08462    1 HFRIIASDYVITVLLPPVIERVAREAPGVRFELLPPDDQPHELLERGEVDLLIAP------ERFMSDGHPSEP----LFE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 180 DGLTCLVQKHHPALREPgWDLDHYLRYPHVQT-YCEGRDRWMLDYKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTLS 258
Cdd:cd08462   71 EEFVCVVWADNPLVGGE-LTAEQYFSAGHVVVrFGRNRRPSFEDWFLNEYGLKRRVEVVTPSFSSIPPLLVGTNRIATLH 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 754692769 259 SLYARHATQVYPLMQLPLPIELDSISHLLIWHQRHDEDPGHRWLRETLL 307
Cdd:cd08462  150 RRLAEQFARRLPLRILPLPFPLPPMREALQWHRYRNNDPGLIWLRELII 198
PBP2_Pa0477 cd08468
The C-terminal substrate biniding domain of an uncharacterized LysR-like transcriptional ...
100-306 7.21e-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: 85.95  E-value: 7.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 100 EFVIASMD-SAFTLFAPLyLSELKRQAPRIRLRYEEWTEN-SLTEMSQGQVDIAFtvrencinsDYRLDT--LPSSICQR 175
Cdd:cd08468    1 RFRFAVTDyTALAVMPRL-MARLEELAPSVRLNLVHAEQKlPLDALLAGEIDFAL---------GYSHDDgaEPRLIEER 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 176 LLAIDGLTCLVQKHHPALREPgwDLDHYLRYPHVQTYCEGRDRWMLDYKLAEQDLYRRIEATVPSFEAALRMGMHSDMIV 255
Cdd:cd08468   71 DWWEDTYVVIASRDHPRLSRL--TLDAFLAERHLVVTPWNEDRGVVDQVLEKQGLEREIALQLPNVLNAPFIVASSDLLM 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 754692769 256 TLSSLYARHATQVYPLMQLPLPIELDSISHLLIWHQRHDEDPGHRWLRETL 306
Cdd:cd08468  149 TLPRQAARALAEALPLELFDLPFDMPPYRLKLYSHRQHENSAANQWLIEQL 199
LysR_substrate pfam03466
LysR substrate binding domain; The structure of this domain is known and is similar to the ...
98-309 4.47e-16

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: 75.40  E-value: 4.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769   98 EREFVIASMDSAFTLFAPLYLSELKRQAPRIRLR-YEEWTENSLTEMSQGQVDIAFTvrencinsdyRLDTLPSSICQRL 176
Cdd:pfam03466   1 SGRLRIGAPPTLASYLLPPLLARFRERYPDVELElTEGNSEELLDLLLEGELDLAIR----------RGPPDDPGLEARP 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769  177 LAIDGLTCLVQKHHPALREPGWDLDHYLRYPHVQTYCEGRDRWMLDYKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVT 256
Cdd:pfam03466  71 LGEEPLVLVAPPDHPLARGEPVSLEDLADEPLILLPPGSGLRDLLDRALRAAGLRPRVVLEVNSLEALLQLVAAGLGIAL 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 754692769  257 LSSLYARHATQVYPLMQLPLPIELDSISHLLIWHQRHDEDPGHRWLRETLLTQ 309
Cdd:pfam03466 151 LPRSAVARELADGRLVALPLPEPPLPRELYLVWRKGRPLSPAVRAFIEFLREA 203
HTH_1 pfam00126
Bacterial regulatory helix-turn-helix protein, lysR family;
11-69 1.61e-15

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


Pssm-ID: 459683 [Multi-domain]  Cd Length: 60  Bit Score: 69.72  E-value: 1.61e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 754692769   11 LNLLIILQVLLEERNGSKAARRLHLSQSAVSKALGRLRETFDDPLFIRSAYGLEPTARA 69
Cdd:pfam00126   1 LRQLRLFVAVAETGSFTAAAERLGLSQPAVSRQIKRLEEELGVPLFERTTRGVRLTEAG 59
PRK11482 PRK11482
DNA-binding transcriptional regulator;
6-277 4.47e-14

DNA-binding transcriptional regulator;


Pssm-ID: 183159 [Multi-domain]  Cd Length: 317  Bit Score: 71.68  E-value: 4.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769   6 LARIDLNLLIILQVLLEERNGSKAARRLHLSQSAVSKALGRLRETFDDPLFIRSAYGLEPTARAQTLQQQLQPILLSLDN 85
Cdd:PRK11482  26 LRNIDLNLLTIFEAVYVHKGIVNAAKILNLTPSAISQSIQKLRVIFPDPLFIRKGQGVTPTAYATHLHEYISQGLESILG 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769  86 liqppAFDPASS---EREFVIASMDSAFTLFAPLYLSELKRQAPRIRLRYEEWTENSlTEMSQGQVDIaftVRENCINSD 162
Cdd:PRK11482 106 -----ALDITGSydkQRTITIATTPSVGALVMPVIYQAIKTHYPQLLLRNIPISDAE-NQLSQFQTDL---IIDTHSCSN 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 163 yrldtlpSSICQRLLAIDGLTCLVQKHHPALREPGwDLDHYLRYPHVQTYCEGRDRWMLDYKLAEQDLYRRIEATVPSFE 242
Cdd:PRK11482 177 -------RTIQHHVLFTDNVVLVCRQGHPLLSLED-DEETLDNAEHTLLLPEGQNFSGLRQRLQEMFPDRQISFSSYNIL 248
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 754692769 243 AALRMGMHSDMIVTLSSLYARHATQVYPLMQLPLP 277
Cdd:PRK11482 249 TIAALIASSDMLGIMPSRFYNLFSRCWPLEKLPFP 283
LysR_Sec_metab NF040786
selenium metabolism-associated LysR family transcriptional regulator; LysR family ...
9-153 1.94e-07

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: 51.85  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769   9 IDLNLLIILQVLLEERNGSKAARRLHLSQSAVSKALGRLRETFDDPLFIRSAYGLEPTARAQTLQQQLQPILLSLDNLIQ 88
Cdd:NF040786   1 MNLKQLEAFVNVAEYKSFSKAAKKLFLTQPTISAHISSLEKELGVRLFVRNTKEVSLTEDGKLLYEYAKEMLDLWEKLEE 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 754692769  89 ppAFDPASSEREFVI---ASMDSAfTLFAPLYLSELKRQAPRIRLR-YEEWTENSLTEMSQGQVDIAFT 153
Cdd:NF040786  81 --EFDRYGKESKGVLrigASTIPG-QYLLPELLKKFKEKYPNVRFKlMISDSIKVIELLLEGEVDIGFT 146
decaheme_TF NF041036
multiheme cytochrome-associated LysR family transcriptional regulator; Members of this family, ...
17-67 7.52e-06

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: 47.04  E-value: 7.52e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 754692769  17 LQVLLEERNGSKAARRLHLSQSAVSKALGRLRETFDDPLFIRSAYGLEPTA 67
Cdd:NF041036   9 LVIVAEEGSFSKAAEKLHLTQSAVSQRIKFLEECYGYQLFDRSGPSLEPTA 59
PBP2_LTTR_substrate cd05466
The substrate binding domain of LysR-type transcriptional regulators (LTTRs), a member of the ...
100-306 7.70e-06

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: 46.05  E-value: 7.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 100 EFVIASMDSAFTLFAPLYLSELKRQAPRIRLR-YEEWTENSLTEMSQGQVDIAFTvrencinsdyRLDTLPSSICQRLLA 178
Cdd:cd05466    1 TLRIGASPSIAAYLLPPLLAAFRQRYPGVELSlVEGGSSELLEALLEGELDLAIV----------ALPVDDPGLESEPLF 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769 179 IDGLTCLVQKHHPALREPGWDLDHYLRYPHVQTYCEGRDRWMLDYKLAEQDLYRRIEATVPSFEAALRMGMHSDMIVTLS 258
Cdd:cd05466   71 EEPLVLVVPPDHPLAKRKSVTLADLADEPLILFERGSGLRRLLDRAFAEAGFTPNIALEVDSLEAIKALVAAGLGIALLP 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 754692769 259 SLYARHAT----QVYPLMQLPLPIELdsishLLIWHQRHDEDPGHRWLRETL 306
Cdd:cd05466  151 ESAVEELAdgglVVLPLEDPPLSRTI-----GLVWRKGRYLSPAARAFLELL 197
PRK09986 PRK09986
LysR family transcriptional regulator;
3-60 9.26e-06

LysR family transcriptional regulator;


Pssm-ID: 182183 [Multi-domain]  Cd Length: 294  Bit Score: 46.64  E-value: 9.26e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 754692769   3 LEQLARIDLNLLIILQVLLEERNGSKAARRLHLSQSAVSKALGRLRETFDDPLFIRSA 60
Cdd:PRK09986   1 MERLYRIDLKLLRYFLAVAEELHFGRAAARLNISQPPLSIHIKELEDQLGTPLFIRHS 58
rbcR CHL00180
LysR transcriptional regulator; Provisional
11-59 5.85e-04

LysR transcriptional regulator; Provisional


Pssm-ID: 177082 [Multi-domain]  Cd Length: 305  Bit Score: 41.16  E-value: 5.85e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 754692769  11 LNLLIILQVLLEERNGSKAARRLHLSQSAVSKALGRLRETFDDPLFIRS 59
Cdd:CHL00180   7 LDQLRILKAIATEGSFKKAAESLYISQPAVSLQIKNLEKQLNIPLFDRS 55
PRK12684 PRK12684
CysB family HTH-type transcriptional regulator;
1-212 2.04e-03

CysB family HTH-type transcriptional regulator;


Pssm-ID: 237173 [Multi-domain]  Cd Length: 313  Bit Score: 39.57  E-value: 2.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769   1 MLLEQL------ARIDLNLliilqvlleerngSKAARRLHLSQSAVSKALGRLRETFDDPLFIRSA---YGLEPTARAqt 71
Cdd:PRK12684   1 MNLHQLrfvreaVRQNFNL-------------TEAAKALYTSQPGVSKAIIELEDELGVEIFTRHGkrlRGLTEPGRI-- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769  72 LQQQLQPILLSLDNLIQPPAFDPASSEREFVIASMDSAFTLFAPLYLSELKRQAPRIRLRYEEWTENSLTEM-SQGQVDI 150
Cdd:PRK12684  66 ILASVERILQEVENLKRVGKEFAAQDQGNLTIATTHTQARYALPAAIKEFKKRYPKVRLSILQGSPTQIAEMvLHGQADL 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 754692769 151 AftVRENCINSDYRLDTLPSSICQRLLaidgltcLVQKHHPALREPGWDLDHYLRYPHVqTY 212
Cdd:PRK12684 146 A--IATEAIADYKELVSLPCYQWNHCV-------VVPPDHPLLERKPLTLEDLAQYPLI-TY 197
PRK12680 PRK12680
LysR family transcriptional regulator;
23-151 8.33e-03

LysR family transcriptional regulator;


Pssm-ID: 183677 [Multi-domain]  Cd Length: 327  Bit Score: 37.68  E-value: 8.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754692769  23 ERNGSKAARRLHLSQSAVSKALGRLRETFDDPLFIRSAYGLEPTARAQTLQQQLQPILLSLDNLIQPPAfdpASSERE-- 100
Cdd:PRK12680  16 ELNITLAAARVHATQPGLSKQLKQLEDELGFLLFVRKGRSLESVTPAGVEVIERARAVLSEANNIRTYA---ANQRREsq 92
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 754692769 101 --FVIASMDSAFTLFAPLYLSELKRQAPRIRLRYEEWTENS-LTEMSQGQVDIA 151
Cdd:PRK12680  93 gqLTLTTTHTQARFVLPPAVAQIKQAYPQVSVHLQQAAESAaLDLLGQGDADIA 146
 
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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