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Conserved domains on  [gi|505180648|ref|WP_015367750|]
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MULTISPECIES: LysR family transcriptional regulator [Klebsiella]

Protein Classification

LysR family transcriptional regulator( domain architecture ID 11426483)

LysR family transcriptional regulator containing an N-terminal HTH (helix-turn-helix) DNA-binding domain and a C-terminal substrate binding domain, which is structurally homologous to the type 2 periplasmic-binding (PBP2) fold proteins

CATH:  3.40.190.10
Gene Ontology:  GO:0003700|GO:0003677|GO:0006355
PubMed:  19047729|8257110|15808743
SCOP:  4000316

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LysR COG0583
DNA-binding transcriptional regulator, LysR family [Transcription];
10-293 3.50e-40

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


:

Pssm-ID: 440348 [Multi-domain]  Cd Length: 256  Bit Score: 140.77  E-value: 3.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  10 FDLNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVGMNLHHHLEKNLNQLEKTIN 89
Cdd:COG0583    1 MDLRQLRAFVAVAEEGSFTAAAERLGVSQPAVSRQIRRLEEELGVPLFERTGRGLRLTEAGERLLERARRILAELEEAEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  90 IAN--HSELSKRFVIYSPQLLISPATMDLINKLHMD-PNLQIDHRdlLLSPESVEDLMAYRKADLIYSITPLSNHSTICQ 166
Cdd:COG0583   81 ELRalRGGPRGTLRIGAPPSLARYLLPPLLARFRARhPGVRLELR--EGNSDRLVDALLEGELDLAIRLGPPPDPGLVAR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 167 PFQELEIALVCREGHPRADHlnsfeevsregftlytssdpnvkafqqhgsdlmperriAFRSNSLIAILTMINQSDLIGF 246
Cdd:COG0583  159 PLGEERLVLVASPDHPLARR--------------------------------------APLVNSLEALLAAVAAGLGIAL 200

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 505180648 247 VPKHALSYFSASFKFREIILPDPIPPVMAYMIYNRSSLNNPKFSEFI 293
Cdd:COG0583  201 LPRFLAADELAAGRLVALPLPDPPPPRPLYLVWRRRRHLSPAVRAFL 247
 
Name Accession Description Interval E-value
LysR COG0583
DNA-binding transcriptional regulator, LysR family [Transcription];
10-293 3.50e-40

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


Pssm-ID: 440348 [Multi-domain]  Cd Length: 256  Bit Score: 140.77  E-value: 3.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  10 FDLNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVGMNLHHHLEKNLNQLEKTIN 89
Cdd:COG0583    1 MDLRQLRAFVAVAEEGSFTAAAERLGVSQPAVSRQIRRLEEELGVPLFERTGRGLRLTEAGERLLERARRILAELEEAEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  90 IAN--HSELSKRFVIYSPQLLISPATMDLINKLHMD-PNLQIDHRdlLLSPESVEDLMAYRKADLIYSITPLSNHSTICQ 166
Cdd:COG0583   81 ELRalRGGPRGTLRIGAPPSLARYLLPPLLARFRARhPGVRLELR--EGNSDRLVDALLEGELDLAIRLGPPPDPGLVAR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 167 PFQELEIALVCREGHPRADHlnsfeevsregftlytssdpnvkafqqhgsdlmperriAFRSNSLIAILTMINQSDLIGF 246
Cdd:COG0583  159 PLGEERLVLVASPDHPLARR--------------------------------------APLVNSLEALLAAVAAGLGIAL 200

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 505180648 247 VPKHALSYFSASFKFREIILPDPIPPVMAYMIYNRSSLNNPKFSEFI 293
Cdd:COG0583  201 LPRFLAADELAAGRLVALPLPDPPPPRPLYLVWRRRRHLSPAVRAFL 247
PRK11482 PRK11482
DNA-binding transcriptional regulator;
7-294 1.71e-36

DNA-binding transcriptional regulator;


Pssm-ID: 183159 [Multi-domain]  Cd Length: 317  Bit Score: 132.54  E-value: 1.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648   7 LKKFDLNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVGMNLHHHLEKNLNQLEK 86
Cdd:PRK11482  26 LRNIDLNLLTIFEAVYVHKGIVNAAKILNLTPSAISQSIQKLRVIFPDPLFIRKGQGVTPTAYATHLHEYISQGLESILG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  87 TINIANHSELSKRFVI-YSPQL--LISPATMDLINKLHmdPNLQIdhRDLLLSpeSVEDLMAYRKADLI-----YSITPL 158
Cdd:PRK11482 106 ALDITGSYDKQRTITIaTTPSVgaLVMPVIYQAIKTHY--PQLLL--RNIPIS--DAENQLSQFQTDLIidthsCSNRTI 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 159 SNHSTicqpFQElEIALVCREGHPRADHLNSFEEVSREGFTLYTSSDPNVKAFQQHGSDLMPERRIAFRSNSLIAILTMI 238
Cdd:PRK11482 180 QHHVL----FTD-NVVLVCRQGHPLLSLEDDEETLDNAEHTLLLPEGQNFSGLRQRLQEMFPDRQISFSSYNILTIAALI 254

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505180648 239 NQSDLIGFVPKHALSYFSASFKFREIilpdPIPPVMAYMI-----YNRSSLNNPKFSEFIT 294
Cdd:PRK11482 255 ASSDMLGIMPSRFYNLFSRCWPLEKL----PFPSLNEEQIdfslhYNKLSLRDPVLENVID 311
HTH_1 pfam00126
Bacterial regulatory helix-turn-helix protein, lysR family;
12-67 1.89e-20

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


Pssm-ID: 459683 [Multi-domain]  Cd Length: 60  Bit Score: 82.82  E-value: 1.89e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 505180648   12 LNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPT 67
Cdd:pfam00126   1 LRQLRLFVAVAETGSFTAAAERLGLSQPAVSRQIKRLEEELGVPLFERTTRGVRLT 56
PBP2_LeuO cd08466
The C-terminal substrate binding domain of LysR-type transcriptional regulator LeuO, an ...
 100-287 5.78e-18

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: 80.37  E-value: 5.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 100 FVIYSPQ---LLISPATMDLINKLhmDPNLQidhrdLLLSPESVEDLMA---YRKADLIYSITPLSNHSTICQPFQELEI 173
Cdd:cd08466    2 FNIAANEtldLLLLPRLLARLKQL--APNIS-----LRESPSSEEDLFEdlrLQEVDLVIDYVPFRDPSFKSELLFEDEL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 174 ALVCREGHPRADHLNSFEEVSREGFTLYTSSDPNVKAFQQHGSDLMPERRIAFRSNSLIAILTMINQSDLIGFVPKHALS 253
Cdd:cd08466   75 VCVARKDHPRIQGSLSLEQYLAEKHVVLSLRRGNLSALDLLTEEVLPQRNIAYEVSSLLSMLAVVSQTDLIAIAPRWLAD 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 505180648 254 YFSASFKFREIILPDPIPPVMAYMIYNRSSLNNP 287
Cdd:cd08466  155 QYAEQLNLQILPLPFKTKPIPLYMVWHKSRERDP 188
LysR_Sec_metab NF040786
selenium metabolism-associated LysR family transcriptional regulator; LysR family ...
 11-194 5.19e-10

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: 59.17  E-value: 5.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  11 DLNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVG----------MNLHHHLEKN 80
Cdd:NF040786   2 NLKQLEAFVNVAEYKSFSKAAKKLFLTQPTISAHISSLEKELGVRLFVRNTKEVSLTEDGkllyeyakemLDLWEKLEEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  81 LNQLEK----TINIANHSELSKRFViysPQLLISpatmdlINKLHMDPNLQIDHRDlllsPESVEDLMAYRKADLIYSIT 156
Cdd:NF040786  82 FDRYGKeskgVLRIGASTIPGQYLL---PELLKK------FKEKYPNVRFKLMISD----SIKVIELLLEGEVDIGFTGT 148

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 505180648 157 PLSNHSTICQPFQELEIALVCREGHPRADHLNSFEEVS 194
Cdd:NF040786 149 KLEKKRLVYTPFYKDRLVLITPNGTEKYRMLKEEISIS 186
argP TIGR03298
transcriptional regulator, ArgP family; ArgP used to be known as IciA. ArgP is a positive ...
 10-85 1.22e-07

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


Pssm-ID: 274509 [Multi-domain]  Cd Length: 292  Bit Score: 51.84  E-value: 1.22e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505180648   10 FDLNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRsGKGITPTIVGMNLHHHLEKnLNQLE 85
Cdd:TIGR03298   1 LDYRQLAALAAVVEEGSFERAAAALSVTPSAVSQRIKALEERLGQPLLVR-TQPCRATEAGQRLLRHARQ-VRLLE 74
decaheme_TF NF041036
multiheme cytochrome-associated LysR family transcriptional regulator; Members of this family, ...
 26-70 3.68e-05

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


Pssm-ID: 468965 [Multi-domain]  Cd Length: 301  Bit Score: 44.34  E-value: 3.68e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 505180648  26 SISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVG 70
Cdd:NF041036  17 SFSKAAEKLHLTQSAVSQRIKFLEECYGYQLFDRSGPSLEPTAAG 61
 
Name Accession Description Interval E-value
LysR COG0583
DNA-binding transcriptional regulator, LysR family [Transcription];
10-293 3.50e-40

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


Pssm-ID: 440348 [Multi-domain]  Cd Length: 256  Bit Score: 140.77  E-value: 3.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  10 FDLNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVGMNLHHHLEKNLNQLEKTIN 89
Cdd:COG0583    1 MDLRQLRAFVAVAEEGSFTAAAERLGVSQPAVSRQIRRLEEELGVPLFERTGRGLRLTEAGERLLERARRILAELEEAEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  90 IAN--HSELSKRFVIYSPQLLISPATMDLINKLHMD-PNLQIDHRdlLLSPESVEDLMAYRKADLIYSITPLSNHSTICQ 166
Cdd:COG0583   81 ELRalRGGPRGTLRIGAPPSLARYLLPPLLARFRARhPGVRLELR--EGNSDRLVDALLEGELDLAIRLGPPPDPGLVAR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 167 PFQELEIALVCREGHPRADHlnsfeevsregftlytssdpnvkafqqhgsdlmperriAFRSNSLIAILTMINQSDLIGF 246
Cdd:COG0583  159 PLGEERLVLVASPDHPLARR--------------------------------------APLVNSLEALLAAVAAGLGIAL 200

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 505180648 247 VPKHALSYFSASFKFREIILPDPIPPVMAYMIYNRSSLNNPKFSEFI 293
Cdd:COG0583  201 LPRFLAADELAAGRLVALPLPDPPPPRPLYLVWRRRRHLSPAVRAFL 247
PRK11482 PRK11482
DNA-binding transcriptional regulator;
7-294 1.71e-36

DNA-binding transcriptional regulator;


Pssm-ID: 183159 [Multi-domain]  Cd Length: 317  Bit Score: 132.54  E-value: 1.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648   7 LKKFDLNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVGMNLHHHLEKNLNQLEK 86
Cdd:PRK11482  26 LRNIDLNLLTIFEAVYVHKGIVNAAKILNLTPSAISQSIQKLRVIFPDPLFIRKGQGVTPTAYATHLHEYISQGLESILG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  87 TINIANHSELSKRFVI-YSPQL--LISPATMDLINKLHmdPNLQIdhRDLLLSpeSVEDLMAYRKADLI-----YSITPL 158
Cdd:PRK11482 106 ALDITGSYDKQRTITIaTTPSVgaLVMPVIYQAIKTHY--PQLLL--RNIPIS--DAENQLSQFQTDLIidthsCSNRTI 179

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 159 SNHSTicqpFQElEIALVCREGHPRADHLNSFEEVSREGFTLYTSSDPNVKAFQQHGSDLMPERRIAFRSNSLIAILTMI 238
Cdd:PRK11482 180 QHHVL----FTD-NVVLVCRQGHPLLSLEDDEETLDNAEHTLLLPEGQNFSGLRQRLQEMFPDRQISFSSYNILTIAALI 254

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505180648 239 NQSDLIGFVPKHALSYFSASFKFREIilpdPIPPVMAYMI-----YNRSSLNNPKFSEFIT 294
Cdd:PRK11482 255 ASSDMLGIMPSRFYNLFSRCWPLEKL----PFPSLNEEQIdfslhYNKLSLRDPVLENVID 311
HTH_1 pfam00126
Bacterial regulatory helix-turn-helix protein, lysR family;
12-67 1.89e-20

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


Pssm-ID: 459683 [Multi-domain]  Cd Length: 60  Bit Score: 82.82  E-value: 1.89e-20
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 505180648   12 LNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPT 67
Cdd:pfam00126   1 LRQLRLFVAVAETGSFTAAAERLGLSQPAVSRQIKRLEEELGVPLFERTTRGVRLT 56
leuO PRK09508
leucine transcriptional activator; Reviewed
 7-283 9.52e-19

leucine transcriptional activator; Reviewed


Pssm-ID: 181918 [Multi-domain]  Cd Length: 314  Bit Score: 84.69  E-value: 9.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648   7 LKKFDLNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVGMNLHHHLEKNL----N 82
Cdd:PRK09508  19 LRMVDLNLLTVFDAVMQEQNITRAAHNLGMSQPAVSNAVARLKVMFNDELFVRYGRGIQPTARARQLFGPVRQALqlvqN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  83 QLEKTINIANHSELSKRFVIYSP-QLLISPATMDLINKLhmDPNLQIDHRDLLlsPESVEDLMAYRKADLIYSITPLSNH 161
Cdd:PRK09508  99 ELPGSGFEPESSERVFNLCICSPlDIRLTSQIYNRIEQI--APNIHVVFKSSL--NQNIEHQLRYQETEFVISYEEFDRP 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 162 STICQPFQELEIALVCREGHPRADHLNSFEEVSREGFTLYtsSDPNVKAFQQHG-SDLMPERRIAFRSNSLIAILTMINQ 240
Cdd:PRK09508 175 EFTSVPLFKDELVLVASKNHPRIKGPITEEQLYNEQHAVV--SLDRFASFSQPWyDTVDKQASIAYQGTALSSVLNVVSQ 252

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 505180648 241 SDLIGFVPKHALSYFSASFKFREIILPDPIPPVMAYMIYNRSS 283
Cdd:PRK09508 253 THLVAIAPRWLAEEFAESLELQILPLPLKNNSRTCYLSWHESA 295
PBP2_LeuO cd08466
The C-terminal substrate binding domain of LysR-type transcriptional regulator LeuO, an ...
 100-287 5.78e-18

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: 80.37  E-value: 5.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 100 FVIYSPQ---LLISPATMDLINKLhmDPNLQidhrdLLLSPESVEDLMA---YRKADLIYSITPLSNHSTICQPFQELEI 173
Cdd:cd08466    2 FNIAANEtldLLLLPRLLARLKQL--APNIS-----LRESPSSEEDLFEdlrLQEVDLVIDYVPFRDPSFKSELLFEDEL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 174 ALVCREGHPRADHLNSFEEVSREGFTLYTSSDPNVKAFQQHGSDLMPERRIAFRSNSLIAILTMINQSDLIGFVPKHALS 253
Cdd:cd08466   75 VCVARKDHPRIQGSLSLEQYLAEKHVVLSLRRGNLSALDLLTEEVLPQRNIAYEVSSLLSMLAVVSQTDLIAIAPRWLAD 154

                        170       180       190
                 ....*....|....*....|....*....|....
gi 505180648 254 YFSASFKFREIILPDPIPPVMAYMIYNRSSLNNP 287
Cdd:cd08466  155 QYAEQLNLQILPLPFKTKPIPLYMVWHKSRERDP 188
LysR_substrate pfam03466
LysR substrate binding domain; The structure of this domain is known and is similar to the ...
 124-293 2.53e-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: 75.79  E-value: 2.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  124 PNLQIDhrdLLL-SPESVEDLMAYRKADLIYSITPLSNHSTICQPFQELEIALVCREGHPRADHLN-SFEEVSREGFTLY 201
Cdd:pfam03466  29 PDVELE---LTEgNSEELLDLLLEGELDLAIRRGPPDDPGLEARPLGEEPLVLVAPPDHPLARGEPvSLEDLADEPLILL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  202 TSSDPNVKAFQQHGSDLMPERRIAFRSNSLIAILTMINQSDLIGFVPKHALSYFSASFKFREIILPDPIPPVMAYMIYNR 281
Cdd:pfam03466 106 PPGSGLRDLLDRALRAAGLRPRVVLEVNSLEALLQLVAAGLGIALLPRSAVARELADGRLVALPLPEPPLPRELYLVWRK 185

                         170
                  ....*....|..
gi 505180648  282 SSLNNPKFSEFI 293
Cdd:pfam03466 186 GRPLSPAVRAFI 197
PBP2_Nitroaromatics_like cd08417
The C-terminal substrate binding domain of LysR-type transcriptional regulators that involved ...
 99-287 1.29e-14

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: 71.09  E-value: 1.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  99 RFVIYSP---QLLISPAtmdLINKLHMD-PNLQIDHRDLllSPESVEDLMAYRKADLIYSITPLSNHSTICQPFQELEIA 174
Cdd:cd08417    1 TFRIAASdylEALLLPP---LLARLRQEaPGVRLRFVPL--DRDDLEEALESGEIDLAIGVFPELPPGLRSQPLFEDRFV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 175 LVCREGHPRADHLNSFEEVSREGFTLYTSSDPNVKAFQQHGSDLMPERRIAFRSNSLIAILTMINQSDLIGFVPKHALSY 254
Cdd:cd08417   76 CVARKDHPLAGGPLTLEDYLAAPHVLVSPRGRGHGLVDDALAELGLSRRVALTVPHFLAAPALVAGTDLIATVPRRLAEA 155

                        170       180       190
                 ....*....|....*....|....*....|...
gi 505180648 255 FSASFKFREIILPDPIPPVMAYMIYNRSSLNNP 287
Cdd:cd08417  156 LAERLGLRVLPLPFELPPFTVSLYWHPRRDRDP 188
PRK10216 PRK10216
HTH-type transcriptional regulator YidZ;
7-77 9.09e-14

HTH-type transcriptional regulator YidZ;


Pssm-ID: 182312 [Multi-domain]  Cd Length: 319  Bit Score: 70.23  E-value: 9.09e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505180648   7 LKKFDLNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVGMNLHHHL 77
Cdd:PRK10216   5 LTTLDLNLLLCLQLLMQERSVTKAAKRMNVTPSAVSKSLAKLRAWFDDPLFVNTPLGLSPTPLMVSMEQNL 75
PRK10086 PRK10086
DNA-binding transcriptional regulator DsdC;
7-177 7.32e-13

DNA-binding transcriptional regulator DsdC;


Pssm-ID: 182231 [Multi-domain]  Cd Length: 311  Bit Score: 67.72  E-value: 7.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648   7 LKKFDLNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVGMNLHHHLEKNLNQLEK 86
Cdd:PRK10086  11 LNGWQLSKLHTFEVAARHQSFALAADELSLTPSAVSHRINQLEEELGIKLFVRSHRKVELTEEGKRVFWALKSSLDTLNQ 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  87 TINIANHSELSKRFVIYSP----QLLISPATMDLINKLhmdPNLQIdhrDLLLSPESVEdlMAYRKADLI--YSITPLSN 160
Cdd:PRK10086  91 EILDIKNQELSGTLTVYSRpsiaQCWLVPRLADFTRRY---PSISL---TILTGNENVN--FQRAGIDLAiyFDDAPSAQ 162

                        170
                 ....*....|....*..
gi 505180648 161 HStiCQPFQELEIALVC 177
Cdd:PRK10086 163 LT--HHFLMDEEILPVC 177
PBP2_LTTR_substrate cd05466
The substrate binding domain of LysR-type transcriptional regulators (LTTRs), a member of the ...
 115-293 7.38e-13

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: 66.08  E-value: 7.38e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 115 DLINKLHMD-PNLQIDHRDLllSPESVEDLMAYRKADLIYSITPLSNHSTICQPFQELEIALVCREGHPRADHLN-SFEE 192
Cdd:cd05466   17 PLLAAFRQRyPGVELSLVEG--GSSELLEALLEGELDLAIVALPVDDPGLESEPLFEEPLVLVVPPDHPLAKRKSvTLAD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 193 VSREGFTLYTSSDPN----VKAFQQHGsdlmPERRIAFRSNSLIAILTMINQSDLIGFVPKHALSyFSASFKFREIILPD 268
Cdd:cd05466   95 LADEPLILFERGSGLrrllDRAFAEAG----FTPNIALEVDSLEAIKALVAAGLGIALLPESAVE-ELADGGLVVLPLED 169

                        170       180
                 ....*....|....*....|....*
gi 505180648 269 PIPPVMAYMIYNRSSLNNPKFSEFI 293
Cdd:cd05466  170 PPLSRTIGLVWRKGRYLSPAARAFL 194
PRK09791 PRK09791
LysR family transcriptional regulator;
12-295 2.20e-10

LysR family transcriptional regulator;


Pssm-ID: 182077 [Multi-domain]  Cd Length: 302  Bit Score: 60.16  E-value: 2.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  12 LNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVGMNLHHH--------------L 77
Cdd:PRK09791   7 IHQIRAFVEVARQGSIRGASRMLNMSQPALTKSIQELEEGLAAQLFFRRSKGVTLTDAGESFYQHaslileelraaqedI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  78 EKNLNQLEKTINIANHSELSKRfviyspqllISPATMDLINKLHMDPNLQIDHRDLL-LSPEsvedlmaYRKADLIYSI- 155
Cdd:PRK09791  87 RQRQGQLAGQINIGMGASIARS---------LMPAVISRFHQQHPQVKVRIMEGQLVsMINE-------LRQGELDFTIn 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 156 ----TPLSNHSTIcQPFQELEIALVCREGHPrADHLNSFEEVSREGFTLYTSSDPNVKAFQQHGSDLMPERRIAFRSNSL 231
Cdd:PRK09791 151 tyyqGPYDHEFTF-EKLLEKQFAVFCRPGHP-AIGARSLKQLLDYSWTMPTPHGSYYKQLSELLDDQAQTPQVGVVCETF 228

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505180648 232 IAILTMINQSDLIGFVPKHALSYFSASFKFREIILPDPIPPVMAYMIYNRSSLNNPKFSEFITQ 295
Cdd:PRK09791 229 SACISLVAKSDFLSILPEEMGCDPLHGQGLVMLPVSEILPKATYYLIQRRDTRQTPLTASLITL 292
LysR_Sec_metab NF040786
selenium metabolism-associated LysR family transcriptional regulator; LysR family ...
 11-194 5.19e-10

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: 59.17  E-value: 5.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  11 DLNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVG----------MNLHHHLEKN 80
Cdd:NF040786   2 NLKQLEAFVNVAEYKSFSKAAKKLFLTQPTISAHISSLEKELGVRLFVRNTKEVSLTEDGkllyeyakemLDLWEKLEEE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  81 LNQLEK----TINIANHSELSKRFViysPQLLISpatmdlINKLHMDPNLQIDHRDlllsPESVEDLMAYRKADLIYSIT 156
Cdd:NF040786  82 FDRYGKeskgVLRIGASTIPGQYLL---PELLKK------FKEKYPNVRFKLMISD----SIKVIELLLEGEVDIGFTGT 148

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 505180648 157 PLSNHSTICQPFQELEIALVCREGHPRADHLNSFEEVS 194
Cdd:NF040786 149 KLEKKRLVYTPFYKDRLVLITPNGTEKYRMLKEEISIS 186
PRK11242 PRK11242
DNA-binding transcriptional regulator CynR; Provisional
 23-248 9.41e-09

DNA-binding transcriptional regulator CynR; Provisional


Pssm-ID: 183051 [Multi-domain]  Cd Length: 296  Bit Score: 55.35  E-value: 9.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  23 QHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVGMNLHHHLEKNLNQLE---KTIN-IANHSELSK 98
Cdd:PRK11242  14 EHGNFTRAAEALHVSQPTLSQQIRQLEESLGVQLFDRSGRTVRLTDAGEVYLRYARRALQDLEagrRAIHdVADLSRGSL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  99 R------FVIYspqlLISPatmdLINKLHMD-PNLQIDHRDllLSPESVEDLMAYRKADLIYSITPLSNHSTICQPFQEL 171
Cdd:PRK11242  94 RlamtptFTAY----LIGP----LIDAFHARyPGITLTIRE--MSQERIEALLADDELDVGIAFAPVHSPEIEAQPLFTE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 172 EIALVCREGHPRADHLNSF--EEVSREGFTLYTSS-------DpnvKAFQQHGsdLMPerRIAFRSNSLIAILTMINQSD 242
Cdd:PRK11242 164 TLALVVGRHHPLAARRKALtlDELADEPLVLLSAEfatreqiD---RYFRRHG--VTP--RVAIEANSISAVLEIVRRGR 236


                 ....*.
gi 505180648 243 LIGFVP 248
Cdd:PRK11242 237 LATLLP 242
PRK11139 PRK11139
DNA-binding transcriptional activator GcvA; Provisional
 12-62 5.18e-08

DNA-binding transcriptional activator GcvA; Provisional


Pssm-ID: 182990 [Multi-domain]  Cd Length: 297  Bit Score: 53.31  E-value: 5.18e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 505180648  12 LNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGK 62
Cdd:PRK11139   8 LNALRAFEAAARHLSFTRAAEELFVTQAAVSHQIKALEDFLGLKLFRRRNR 58
argP TIGR03298
transcriptional regulator, ArgP family; ArgP used to be known as IciA. ArgP is a positive ...
 10-85 1.22e-07

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


Pssm-ID: 274509 [Multi-domain]  Cd Length: 292  Bit Score: 51.84  E-value: 1.22e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505180648   10 FDLNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRsGKGITPTIVGMNLHHHLEKnLNQLE 85
Cdd:TIGR03298   1 LDYRQLAALAAVVEEGSFERAAAALSVTPSAVSQRIKALEERLGQPLLVR-TQPCRATEAGQRLLRHARQ-VRLLE 74
PBP2_TdcA cd08418
The C-terminal substrate binding domain of LysR-type transcriptional regulator TdcA, which is ...
 115-295 2.05e-07

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


Pssm-ID: 176110 [Multi-domain]  Cd Length: 201  Bit Score: 50.43  E-value: 2.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 115 DLINKLH-MDPNLQIDhrdlLLSPESVEDLMAYRKADLIYSITPLSN----HSTICQPFQELEIALVCREGHPrADHLNS 189
Cdd:cd08418   17 AVINRFKeQFPDVQIS----IYEGQLSSLLPELRDGRLDFAIGTLPDemylKELISEPLFESDFVVVARKDHP-LQGARS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 190 FEEVSREGFTLYTSSDPNVKAFQQHGSDLMPERRIAFRSNSLIAILTMINQSDLIGFVPKHALSYFSASFKFREIILPDP 269
Cdd:cd08418   92 LEELLDASWVLPGTRMGYYNNLLEALRRLGYNPRVAVRTDSIVSIINLVEKADFLTILSRDMGRGPLDSFRLITIPVEEP 171

                        170       180
                 ....*....|....*....|....*.
gi 505180648 270 IPPVMAYMIYNRSSLNNPKFSEFITQ 295
Cdd:cd08418  172 LPSADYYLIYRKKSRLTPLAEQLVEL 197
PRK13348 PRK13348
HTH-type transcriptional regulator ArgP;
10-78 2.18e-07

HTH-type transcriptional regulator ArgP;


Pssm-ID: 237357 [Multi-domain]  Cd Length: 294  Bit Score: 51.13  E-value: 2.18e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505180648  10 FDLNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRsGKGITPTIVGMNLHHHLE 78
Cdd:PRK13348   2 LDYKQLEALAAVVETGSFERAARRLHVTPSAVSQRIKALEESLGQPLLVR-GRPCRPTPAGQRLLRHLR 69
PRK11233 PRK11233
nitrogen assimilation transcriptional regulator; Provisional
 26-86 8.34e-07

nitrogen assimilation transcriptional regulator; Provisional


Pssm-ID: 183045 [Multi-domain]  Cd Length: 305  Bit Score: 49.68  E-value: 8.34e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505180648  26 SISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVGMNLHHHLEKNLNQLEK 86
Cdd:PRK11233  17 SLTQAAEVLHIAQPALSQQVATLEGELNQQLLIRTKRGVTPTEAGKILYTHARAILRQCEQ 77
PBP2_DntR_like_1 cd08460
The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional ...
 133-277 1.29e-06

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: 47.97  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 133 LLLSPESVEDLMAYR--KADLIYSITPLSNHSTICQP-FQELEIALVcREGHP------------RADHLNsfeeVSREG 197
Cdd:cd08460   31 LRFVPESDKDVDALRegRIDLEIGVLGPTGPEIRVQTlFRDRFVGVV-RAGHPlargpitperyaAAPHVS----VSRRG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 198 ftlyTSSDPNVKAFQQHGSdlmpERRIAFRSNSLIAILTMINQSDLIGFVPKHALSYFSASFKFREIILPDPIPPVMAYM 277
Cdd:cd08460  106 ----RLHGPIDDALAALGL----TRRVVAVVPTFAAALFLARGSDLIALVPERVTAAARAGLGLRTFPLPLELPAVTVSQ 177
rbcR CHL00180
LysR transcriptional regulator; Provisional
 10-67 2.05e-06

LysR transcriptional regulator; Provisional


Pssm-ID: 177082 [Multi-domain]  Cd Length: 305  Bit Score: 48.48  E-value: 2.05e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 505180648  10 FDLNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPT 67
Cdd:CHL00180   5 FTLDQLRILKAIATEGSFKKAAESLYISQPAVSLQIKNLEKQLNIPLFDRSKNKASLT 62
PBP2_DntR_like_3 cd08461
The C-terminal substrate binding domain of an uncharacterized LysR-type transcriptional ...
 124-287 5.23e-06

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: 46.12  E-value: 5.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 124 PNLQIDHRDLllSPESVEDLMAYRKADLIYSITPLSNHSTICQPFQELEIALVCREGHPRADHLNSFEE--------VSR 195
Cdd:cd08461   27 PGVRVAIRDL--ESDNLEAQLERGEVDLALTTPEYAPDGLRSRPLFEERYVCVTRRGHPLLQGPLSLDQfcaldhivVSP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 196 EGFTLYTSSDpnvKAFQQHGSdlmpERRIAFRSNSLIAILTMINQSDLIGFVPKHALSYFSasfKFREIILPDPIPPVMA 275
Cdd:cd08461  105 SGGGFAGSTD---EALAALGL----TRNVVLSVPSFLVVPEILAATDMVAFVPSRLVPNLE---GLQEVELPLEPPGFDV 174

                        170
                 ....*....|..
gi 505180648 276 YMIYNRSSLNNP 287
Cdd:cd08461  175 VMAWHERTHRDP 186
PRK10094 PRK10094
HTH-type transcriptional activator AllS;
10-186 6.48e-06

HTH-type transcriptional activator AllS;


Pssm-ID: 182237 [Multi-domain]  Cd Length: 308  Bit Score: 46.72  E-value: 6.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  10 FDLNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVGMNLHHHLEKNLNQLE---- 85
Cdd:PRK10094   2 FDPETLRTFIAVAETGSFSKAAERLCKTTATISYRIKLLEENTGVALFFRTTRSVTLTAAGEHLLSQARDWLSWLEsmps 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  86 --KTINianhSELSKRFVIYSPQLLISP-ATMDLINKLHMD-PNLQID-HRDLLLspeSVEDLMAYRKADLIYSIT---P 157
Cdd:PRK10094  82 elQQVN----DGVERQVNIVINNLLYNPqAVAQLLAWLNERyPFTQFHiSRQIYM---GVWDSLLYEGFSLAIGVTgteA 154

                        170       180
                 ....*....|....*....|....*....
gi 505180648 158 LSNHSTICqPFQELEIALVCREGHPRADH 186
Cdd:PRK10094 155 LANTFSLD-PLGSVQWRFVMAADHPLANV 182
PRK12682 PRK12682
transcriptional regulator CysB-like protein; Reviewed
 17-215 1.56e-05

transcriptional regulator CysB-like protein; Reviewed


Pssm-ID: 183679 [Multi-domain]  Cd Length: 309  Bit Score: 45.75  E-value: 1.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  17 IFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGK---GITPtiVGMNLHHHLEKNLNQLEKTINIANh 93
Cdd:PRK12682   9 VREAVRRNLNLTEAAKALHTSQPGVSKAIIELEEELGIEIFIRHGKrlkGLTE--PGKAVLDVIERILREVGNIKRIGD- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  94 sELSKRfviYSPQLLIS----------PATMDLINKLHMDPNLQIDHRdlllSPESVEDLMAYRKADLIYSITPLSNH-S 162
Cdd:PRK12682  86 -DFSNQ---DSGTLTIAtthtqaryvlPRVVAAFRKRYPKVNLSLHQG----SPDEIARMVISGEADIGIATESLADDpD 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505180648 163 TICQPFQELEIALVCREGHPRA-------DHLNSFEEVS-REGFTLYTSSDpnvKAFQQHG 215
Cdd:PRK12682 158 LATLPCYDWQHAVIVPPDHPLAqeeritlEDLAEYPLITyHPGFTGRSRID---RAFAAAG 215
PRK03635 PRK03635
ArgP/LysG family DNA-binding transcriptional regulator;
29-85 1.79e-05

ArgP/LysG family DNA-binding transcriptional regulator;


Pssm-ID: 235144 [Multi-domain]  Cd Length: 294  Bit Score: 45.53  E-value: 1.79e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 505180648  29 KAAETLFITPSAVSQSLQRLRNQLNDPLFVRsGKGITPTIVGMNLHHHLEKnLNQLE 85
Cdd:PRK03635  21 RAAQKLHITQSAVSQRIKALEERVGQVLLVR-TQPCRPTEAGQRLLRHARQ-VRLLE 75
nhaR PRK11062
transcriptional activator NhaR; Provisional
 13-70 2.56e-05

transcriptional activator NhaR; Provisional


Pssm-ID: 182938 [Multi-domain]  Cd Length: 296  Bit Score: 45.00  E-value: 2.56e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 505180648  13 NLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVG 70
Cdd:PRK11062   7 NHLYYFWMVCKEGSVVGAAEALFLTPQTITGQIKALEERLQGKLFKRKGRGLEPTELG 64
decaheme_TF NF041036
multiheme cytochrome-associated LysR family transcriptional regulator; Members of this family, ...
 26-70 3.68e-05

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


Pssm-ID: 468965 [Multi-domain]  Cd Length: 301  Bit Score: 44.34  E-value: 3.68e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 505180648  26 SISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVG 70
Cdd:NF041036  17 SFSKAAEKLHLTQSAVSQRIKFLEECYGYQLFDRSGPSLEPTAAG 61
PRK10341 PRK10341
transcriptional regulator TdcA;
15-281 4.18e-05

transcriptional regulator TdcA;


Pssm-ID: 182391 [Multi-domain]  Cd Length: 312  Bit Score: 44.47  E-value: 4.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  15 LVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVGMNLHHHLEKNLNQLEKTINIANhS 94
Cdd:PRK10341  12 LVVFQEVIRSGSIGSAAKELGLTQPAVSKIINDIEDYFGVELIVRKNTGVTLTPAGQVLLSRSESITREMKNMVNEIN-G 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648  95 ELSKRFVIYS---PQLLISPATMDLINKLHM-DPNLQIDHRDLLLSpesvEDLMAYRKADLIYSITPLSNHSTI----CQ 166
Cdd:PRK10341  91 MSSEAVVDVSfgfPSLIGFTFMSDMINKFKEvFPKAQVSMYEAQLS----SFLPAIRDGRLDFAIGTLSNEMKLqdlhVE 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 167 PFQELEIALVCREGHP--RADHLNSFEE----VSREGFTLYTSSdpnVKAFQQHGSDlmpeRRIAFRSNSLIAILTMINQ 240
Cdd:PRK10341 167 PLFESEFVLVASKSRTctGTTTLESLKNeqwvLPQTNMGYYSEL---LTTLQRNGIS----IENIVKTDSVVTIYNLVLN 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 505180648 241 SDLIGFVPKHALSYFsASFKFREIILPDPIPPVMAYMIYNR 281
Cdd:PRK10341 240 ADFLTVIPCDMTSPF-GSNQFITIPIEETLPVAQYAAVWSK 279
PRK09801 PRK09801
LysR family transcriptional regulator;
1-89 5.58e-05

LysR family transcriptional regulator;


Pssm-ID: 182085 [Multi-domain]  Cd Length: 310  Bit Score: 43.87  E-value: 5.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648   1 MANLYDLKKfDLNLLVifECIYQHlSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVGMNLHHHLEKN 80
Cdd:PRK09801   1 MLNSWPLAK-DLQVLV--EIVHSG-SFSAAAATLGQTPAFVTKRIQILENTLATTLLNRSARGVALTESGQRCYEHALEI 76


                 ....*....
gi 505180648  81 LNQLEKTIN 89
Cdd:PRK09801  77 LTQYQRLVD 85
PBP2_GbpR cd08435
The C-terminal substrate binding domain of galactose-binding protein regulator contains the ...
 125-272 8.09e-05

The C-terminal substrate binding domain of galactose-binding protein regulator contains the type 2 periplasmic binding fold; Galactose-binding protein regulator (GbpR), a member of the LysR family of bacterial transcriptional regulators, regulates the expression of chromosomal virulence gene chvE. The chvE gene is involved in the uptake of specific sugars, in chemotaxis to these sugars, and in the VirA-VirG two-component signal transduction system. In the presence of an inducing sugar such as L-arabinose, D-fucose, or D-galactose, GbpR activates chvE expression, while in the absence of an inducing sugar, GbpR represses expression. 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: 176126 [Multi-domain]  Cd Length: 201  Bit Score: 42.65  E-value: 8.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 125 NLQIDHRDLLLspesveDLMAYRKADLIYSITP---LSNHSTICQPFQElEIALVCREGHPRAD-HLNSFEEVSREGFTL 200
Cdd:cd08435   32 RVVEGTSDELL------EGLRAGELDLAIGRLAddeQPPDLASEELADE-PLVVVARPGHPLARrARLTLADLADYPWVL 104

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505180648 201 YTSSDPNVK----AFQQHGsdlMPERRIAFRSNSLIAILTMINQSDLIGFVPKHALSYFSASFKFREIILPDPIPP 272
Cdd:cd08435  105 PPPGTPLRQrleqLFAAAG---LPLPRNVVETASISALLALLARSDMLAVLPRSVAEDELRAGVLRELPLPLPTSR 177
PBP2_DntR_NahR_LinR_like cd08459
The C-terminal substrate binding domain of LysR-type transcriptional regulators that are ...
 135-273 8.41e-05

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: 42.56  E-value: 8.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 135 LSPESVEDLMAYRKADL-IYSITPLSnHSTICQPFQELEIALVCREGHPRADHLNSFEEVSREGFTLYTSSDPNVKAFQQ 213
Cdd:cd08459   36 LPVDELEEALESGEIDLaIGYLPDLG-AGFFQQRLFRERYVCLVRKDHPRIGSTLTLEQFLAARHVVVSASGTGHGLVEQ 114

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648 214 HGSDLMPERRIAFRSNSLIAILTMINQSDLIGFVPKHALSYFSASFKFREIILPDPIPPV 273
Cdd:cd08459  115 ALREAGIRRRIALRVPHFLALPLIVAQTDLVATVPERLARLFARAGGLRIVPLPFPLPPF 174
PRK15092 PRK15092
DNA-binding transcriptional repressor LrhA; Provisional
 11-73 3.15e-04

DNA-binding transcriptional repressor LrhA; Provisional


Pssm-ID: 237907 [Multi-domain]  Cd Length: 310  Bit Score: 41.55  E-value: 3.15e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505180648  11 DLNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVGMNL 73
Cdd:PRK15092  12 DLDLLRTFVAVADLNTFAAAAAAVCRTQSAVSQQMQRLEQLVGKELFARHGRNKLLTEHGIQL 74
PRK03601 PRK03601
HTH-type transcriptional regulator HdfR;
29-97 3.68e-04

HTH-type transcriptional regulator HdfR;


Pssm-ID: 235137 [Multi-domain]  Cd Length: 275  Bit Score: 41.16  E-value: 3.68e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505180648  29 KAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVGMNLHHHLEKNLN--QLEK--TINIANHSELS 97
Cdd:PRK03601  20 RAAESLYLTQSAVSFRIRQLENQLGVNLFTRHRNNIRLTAAGERLLPYAETLMNtwQAAKkeVAHTSQHNELS 92
PRK12683 PRK12683
transcriptional regulator CysB-like protein; Reviewed
 14-85 9.75e-04

transcriptional regulator CysB-like protein; Reviewed


Pssm-ID: 237172 [Multi-domain]  Cd Length: 309  Bit Score: 40.03  E-value: 9.75e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505180648  14 LLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGK---GITPTivGMNLHHHLEKNLNQLE 85
Cdd:PRK12683   6 LRIIREAVRQNFNLTEVANALYTSQSGVSKQIKDLEDELGVEIFIRRGKrltGLTEP--GKELLQIVERMLLDAE 78
PRK12684 PRK12684
CysB family HTH-type transcriptional regulator;
17-65 2.76e-03

CysB family HTH-type transcriptional regulator;


Pssm-ID: 237173 [Multi-domain]  Cd Length: 313  Bit Score: 38.80  E-value: 2.76e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 505180648  17 IFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGIT 65
Cdd:PRK12684   9 VREAVRQNFNLTEAAKALYTSQPGVSKAIIELEDELGVEIFTRHGKRLR 57
PRK09986 PRK09986
LysR family transcriptional regulator;
7-89 4.03e-03

LysR family transcriptional regulator;


Pssm-ID: 182183 [Multi-domain]  Cd Length: 294  Bit Score: 38.17  E-value: 4.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505180648   7 LKKFDLNLLVIFECIYQHLSISKAAETLFITPSAVSQSLQRLRNQLNDPLFVRSGKGITPTIVGMNLHHHLEKNLNQLEK 86
Cdd:PRK09986   4 LYRIDLKLLRYFLAVAEELHFGRAAARLNISQPPLSIHIKELEDQLGTPLFIRHSRSVVLTHAGKILMEESRRLLDNAEQ 83


                 ...
gi 505180648  87 TIN 89
Cdd:PRK09986  84 SLA 86
 
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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