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Conserved domains on  [gi|502820249|ref|WP_013055225|]
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MULTISPECIES: LacI family DNA-binding transcriptional regulator [Priestia]

Protein Classification

LacI family DNA-binding transcriptional regulator( domain architecture ID 11446715)

LacI family DNA-binding transcriptional regulator functions as an activator or repressor by binding a specific effector ligand that either decreases (induction) or increases DNA-binding affinity (co-repression)

CATH:  3.40.50.2300
Gene Ontology:  GO:0003677|GO:0003700|GO:0006355
PubMed:  8543068|12598694

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
1-332 3.47e-138

DNA-binding transcriptional regulator, LacI/PurR family [Transcription];


:

Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 395.34  E-value: 3.47e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249   1 MKPTIYSVAEEAGVSISTVSKVINQTGHISERTRQKVIEVMAQLNYHPSVVASALTGKPTKTIGLLVPDISNPFFADLAR 80
Cdd:COG1609    2 KRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  81 SIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDIPISVIASEIPHISVNTVTVD 160
Cdd:COG1609   82 GIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRPLPDPGVPSVGVD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 161 DYKGSYLATDYLLSLHHKKIAIITENAKSNHA--RLDAFREVMQENGIIVPPQHVITTEASIQKGYESAKQIFSMKEKVT 238
Cdd:COG1609  162 NRAGARLATEHLIELGHRRIAFIGGPADSSSAreRLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGPRPT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 239 AIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVVDLLVREMKYPAMHKEHLLL 318
Cdd:COG1609  242 AIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERVLL 321

                        330
                 ....*....|....
gi 502820249 319 EPKLIVRKSTAPLR 332
Cdd:COG1609  322 PPELVVRESTAPAP 335
 
Name Accession Description Interval E-value
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
1-332 3.47e-138

DNA-binding transcriptional regulator, LacI/PurR family [Transcription];


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 395.34  E-value: 3.47e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249   1 MKPTIYSVAEEAGVSISTVSKVINQTGHISERTRQKVIEVMAQLNYHPSVVASALTGKPTKTIGLLVPDISNPFFADLAR 80
Cdd:COG1609    2 KRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  81 SIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDIPISVIASEIPHISVNTVTVD 160
Cdd:COG1609   82 GIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRPLPDPGVPSVGVD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 161 DYKGSYLATDYLLSLHHKKIAIITENAKSNHA--RLDAFREVMQENGIIVPPQHVITTEASIQKGYESAKQIFSMKEKVT 238
Cdd:COG1609  162 NRAGARLATEHLIELGHRRIAFIGGPADSSSAreRLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGPRPT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 239 AIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVVDLLVREMKYPAMHKEHLLL 318
Cdd:COG1609  242 AIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERVLL 321

                        330
                 ....*....|....
gi 502820249 319 EPKLIVRKSTAPLR 332
Cdd:COG1609  322 PPELVVRESTAPAP 335
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
 62-323 1.96e-106

ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily; Ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily. In most cases, ligands are monosaccharide including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the domain sugar binding changes the DNA binding activity of the repressor domain.


Pssm-ID: 380491 [Multi-domain]  Cd Length: 264  Bit Score: 312.14  E-value: 1.96e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDIP 141
Cdd:cd06267    1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLAAGIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 ISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIIT--ENAKSNHARLDAFREVMQENGIIVPPQHVITTEAS 219
Cdd:cd06267   81 VVLIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGgpLDLSTSRERLEGYRDALAEAGLPVDPELVVEGDFS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 220 IQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVV 299
Cdd:cd06267  161 EESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEMGRAAA 240

                        250       260
                 ....*....|....*....|....
gi 502820249 300 DLLVREMKYPAMHKEHLLLEPKLI 323
Cdd:cd06267  241 ELLLERIEGEEEPPRRIVLPTELV 264
PRK10703 PRK10703
HTH-type transcriptional repressor PurR;
4-329 5.33e-82

HTH-type transcriptional repressor PurR;


Pssm-ID: 236739 [Multi-domain]  Cd Length: 341  Bit Score: 252.72  E-value: 5.33e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249   4 TIYSVAEEAGVSISTVSKVINQTGHISERTRQKVIEVMAQLNYHPSVVASALTGKPTKTIGLLVPDISNPFFADLARSIE 83
Cdd:PRK10703   3 TIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEAVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  84 DRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLkNMLK--QDIPIsVIASEIPHISVNTVTVDD 161
Cdd:PRK10703  83 KNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLL-AMLEeyRHIPM-VVMDWGEAKADFTDAIID 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 162 --YKGSYLATDYLLSLHHKKIAIITENAKSNHA--RLDAFREVMQENGIIVPPQHVITTEASIQKGYESAKQIFSMKEKV 237
Cdd:PRK10703 161 naFEGGYLAGRYLIERGHRDIGVIPGPLERNTGagRLAGFMKAMEEANIKVPEEWIVQGDFEPESGYEAMQQILSQKHRP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 238 TAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVVDLLVREMKYPAMHKEHLL 317
Cdd:PRK10703 241 TAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRIVNKREEPQTIE 320

                        330
                 ....*....|..
gi 502820249 318 LEPKLIVRKSTA 329
Cdd:PRK10703 321 VHPRLVERRSVA 332
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
 171-328 2.32e-40

Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional regulatory proteins. It is related to bacterial periplasmic binding proteins, although this domain is unlikely to be found in the periplasm. This domain acts as a sensor binding small molecule ligands that the DNA-binding domain responds to. This domain recognizes Sugars, sugar phosphates, sugar acids and purines (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433159 [Multi-domain]  Cd Length: 160  Bit Score: 139.40  E-value: 2.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  171 YLLSLHHKKIAIITEN----AKSNHARLDAFREVMQENGIIVPPQHVITTEASIQKGYESAKQifSMKEKVTAIFACNDL 246
Cdd:pfam13377   1 HLAELGHRRIALIGPEgdrdDPYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARERLR--WLGALPTAVFVANDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  247 LAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVVDLLVREMKYPAMHKEHLLLEPKLIVRK 326
Cdd:pfam13377  79 VALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVERE 158


                  ..
gi 502820249  327 ST 328
Cdd:pfam13377 159 ST 160
fruct_sucro_rep TIGR02417
D-fructose-responsive transcription factor; Members of this family belong the lacI ...
 4-304 2.18e-32

D-fructose-responsive transcription factor; Members of this family belong the lacI helix-turn-helix family (pfam00356) of DNA-binding transcriptional regulators. All members are from the proteobacteria. Characterized members act as positive and negative transcriptional regulators of fructose and sucrose transport and metabolism. Sucrose is a disaccharide composed of fructose and glucose; D-fructose-1-phosphate rather than an intact sucrose moiety has been shown to act as the inducer. [Regulatory functions, DNA interactions]


Pssm-ID: 131470 [Multi-domain]  Cd Length: 327  Bit Score: 122.94  E-value: 2.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249    4 TIYSVAEEAGVSISTVSKVINQTGH---ISERTRQKVIEVMAQLNYHPSVVASALTGKPTKTIGLLVPDISNPFFADLAR 80
Cdd:TIGR02417   1 TLSDIAKLAGVSKTTASYVINGKAKeyrISQETVERVMAVVREQGYQPNIHAASLRAGRSRTIGLVIPDLENYSYARIAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249   81 SIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQD-IPISVIASEIPHISVNTVTV 159
Cdd:TIGR02417  81 ELEQQCREAGYQLLIACSDDNPDQEKVVIENLLARQVDALIVASCMPPEDAYYQKLQNEgLPVVALDRSLDDEHFCSVIS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  160 DDYKGSYLATDYLLSLHHKKIAII--TENAKSNHARLDAFREVMQengiivppQHVITTEASIQKGY--ESAKQIFSMKE 235
Cdd:TIGR02417 161 DDVDAAAELIERLLSQHADEFWYLgaQPELSVSRDRLAGFRQALK--------QATLEVEWVYGGNYsrESGYQMFAKLC 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502820249  236 KV-----TAIFACNDLLAIGVMQAAKELKIDvPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVVDLLVR 304
Cdd:TIGR02417 233 ARlgrlpQALFTTSYTLLEGVLDYMLERPLL-DSQLHLATFGDNYLLDFLPLPINSVAQQHRQLAWHALELALA 305
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
3-72 3.93e-28

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 104.21  E-value: 3.93e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249     3 PTIYSVAEEAGVSISTVSKVINQTGHISERTRQKVIEVMAQLNYHPSVVASALTGKPTKTIGLLVPDISN 72
Cdd:smart00354   1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
 
Name Accession Description Interval E-value
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
1-332 3.47e-138

DNA-binding transcriptional regulator, LacI/PurR family [Transcription];


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 395.34  E-value: 3.47e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249   1 MKPTIYSVAEEAGVSISTVSKVINQTGHISERTRQKVIEVMAQLNYHPSVVASALTGKPTKTIGLLVPDISNPFFADLAR 80
Cdd:COG1609    2 KRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  81 SIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDIPISVIASEIPHISVNTVTVD 160
Cdd:COG1609   82 GIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRPLPDPGVPSVGVD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 161 DYKGSYLATDYLLSLHHKKIAIITENAKSNHA--RLDAFREVMQENGIIVPPQHVITTEASIQKGYESAKQIFSMKEKVT 238
Cdd:COG1609  162 NRAGARLATEHLIELGHRRIAFIGGPADSSSAreRLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGPRPT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 239 AIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVVDLLVREMKYPAMHKEHLLL 318
Cdd:COG1609  242 AIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERVLL 321

                        330
                 ....*....|....
gi 502820249 319 EPKLIVRKSTAPLR 332
Cdd:COG1609  322 PPELVVRESTAPAP 335
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
 62-323 1.96e-106

ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily; Ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily. In most cases, ligands are monosaccharide including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the domain sugar binding changes the DNA binding activity of the repressor domain.


Pssm-ID: 380491 [Multi-domain]  Cd Length: 264  Bit Score: 312.14  E-value: 1.96e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDIP 141
Cdd:cd06267    1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLAAGIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 ISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIIT--ENAKSNHARLDAFREVMQENGIIVPPQHVITTEAS 219
Cdd:cd06267   81 VVLIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGgpLDLSTSRERLEGYRDALAEAGLPVDPELVVEGDFS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 220 IQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVV 299
Cdd:cd06267  161 EESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEMGRAAA 240

                        250       260
                 ....*....|....*....|....
gi 502820249 300 DLLVREMKYPAMHKEHLLLEPKLI 323
Cdd:cd06267  241 ELLLERIEGEEEPPRRIVLPTELV 264
PBP1_DegA_Like cd19976
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
 62-327 1.07e-103

ligand-binding domain of putative DNA transcription regulators highly similar to that of the transcription regulator DegA; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the transcription regulator DegA, which is involved in the control of degradation of Bacillus subtilis amidophosphoribosyltransferase (purF). This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380631 [Multi-domain]  Cd Length: 268  Bit Score: 305.33  E-value: 1.07e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVAS-AFRNANLLKNMLKQDI 140
Cdd:cd19976    1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASsNISDEAIIKLLKEEKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 141 PISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIITENAKSN--HARLDAFREVMQENGIIVPPQHVITTEA 218
Cdd:cd19976   81 PVVVLDRYIEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPSTYneHERIEGYKNALQDHNLPIDESWIYSGES 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 219 SIQKGYESAKQIFSmKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNV 298
Cdd:cd19976  161 SLEGGYKAAEELLK-SKNPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQPIFEMGQEA 239

                        250       260
                 ....*....|....*....|....*....
gi 502820249 299 VDLLVREMKYPAMHKEHLLLEPKLIVRKS 327
Cdd:cd19976  240 AKLLLKIIKNPAKKKEEIVLPPELIKRDS 268
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 62-328 6.71e-94

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380508 [Multi-domain]  Cd Length: 269  Bit Score: 280.27  E-value: 6.71e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDIP 141
Cdd:cd06285    1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQELAARGVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 ISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIIT--ENAKSNHARLDAFREVMQENGIIVPPQHVITTEAS 219
Cdd:cd06285   81 VVLVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAgpLNASTGRDRLRGYRRALAEAGLPVPDERIVPGGFT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 220 IQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVV 299
Cdd:cd06285  161 IEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEMGRRAA 240

                        250       260
                 ....*....|....*....|....*....
gi 502820249 300 DLLVREMKYPAMHKEHLLLEPKLIVRKST 328
Cdd:cd06285  241 ELLLQLIEGGGRPPRSITLPPELVVREST 269
PBP1_PurR cd06275
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ...
 62-327 2.40e-91

ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli; Ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli. This dimeric PurR belongs to the LacI-GalR family of transcription regulators and is activated to bind to DNA operator sites by initially binding either of high affinity corepressors, hypoxanthine or guanine. PurR is composed of two functional domains: aan N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the purine transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380499 [Multi-domain]  Cd Length: 269  Bit Score: 273.75  E-value: 2.40e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRN---ANLLKNMLkq 138
Cdd:cd06275    1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTdddAELLAALR-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 139 DIPISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIITENAKSNHA--RLDAFREVMQENGIIVPPQHVITT 216
Cdd:cd06275   79 SIPVVVLDREIAGDNADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSVSreRLAGFRRALAEAGIEVPPSWIVEG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 217 EASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAV 296
Cdd:cd06275  159 DFEPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQPKDELGE 238

                        250       260       270
                 ....*....|....*....|....*....|.
gi 502820249 297 NVVDLLVREMKYPAMHKEHLLLEPKLIVRKS 327
Cdd:cd06275  239 LAVELLLDRIENKREEPQSIVLEPELIERES 269
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
 62-327 1.86e-90

ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus succinogenes and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380507 [Multi-domain]  Cd Length: 267  Bit Score: 271.33  E-value: 1.86e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLkNMLKQDIP 141
Cdd:cd06284    1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILLSGRLDAELL-SELSKRYP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 IsVIASE-IPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIIT--ENAKSNHARLDAFREVMQENGIIVPPQHVITTEA 218
Cdd:cd06284   80 I-VQCCEyIPDSGVPSVSIDNEAAAYDATEYLISLGHRRIAHINgpLDNVYARERLEGYRRALAEAGLPVDEDLIIEGDF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 219 SIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNV 298
Cdd:cd06284  159 SFEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIGETA 238

                        250       260
                 ....*....|....*....|....*....
gi 502820249 299 VDLLVREMKYPAMHKEHLLLEPKLIVRKS 327
Cdd:cd06284  239 AELLLEKIEGEGVPPEHIILPHELIVRES 267
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
 62-327 3.39e-90

ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus Metalliredigens (strain Qymf) and its close homologs; This group includes the ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus metalliredigens (strain Qymf) and its close homologs. Qymf is a strict anaerobe that could be grown in the presence of borax and its cells are straight rods that produce endospores. This group is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380514 [Multi-domain]  Cd Length: 264  Bit Score: 270.55  E-value: 3.39e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKnmlKQDIP 141
Cdd:cd06291    1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILGSHSLDIEEYK---KLNIP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 ISVIASEIPHiSVNTVTVDDYKGSYLATDYLLSLHHKKIAIIT--ENAKSNHARLDAFREVMQENGIIVPPQHVITTEAS 219
Cdd:cd06291   78 IVSIDRYLSE-GIPSVSSDNYQGGRLAAEHLIEKGCKKILHIGgpSNNSPANERYRGFEDALKEAGIEYEIIEIDENDFS 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 220 IQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVV 299
Cdd:cd06291  157 EEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIEEMAKEAV 236

                        250       260
                 ....*....|....*....|....*...
gi 502820249 300 DLLVREMKYPAMHKEHLLLEPKLIVRKS 327
Cdd:cd06291  237 ELLLKLIEGEEIEESRIVLPVELIERET 264
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
 62-323 1.13e-88

periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its close homologs; This group includes the ligand-binding domain of putative repressor of the endoglucanase operon from Paenibacillus polymyxa and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380632 [Multi-domain]  Cd Length: 264  Bit Score: 266.70  E-value: 1.13e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDIP 141
Cdd:cd19977    1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNEDLIEKLVKSGIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 ISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIITE--NAKSNHARLDAFREVMQENGIIVpPQHVITTEAS 219
Cdd:cd19977   81 VVFVDRYIPGLDVDTVVVDNFKGAYQATEHLIELGHKRIAFITYplELSTRQERLEGYKAALADHGLPV-DEELIKHVDR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 220 IQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVV 299
Cdd:cd19977  160 QDDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQPTYEIGRKAA 239

                        250       260
                 ....*....|....*....|....*
gi 502820249 300 DLLVREMK-YPAMHKEHLLLEPKLI 323
Cdd:cd19977  240 ELLLDRIEnKPKGPPRQIVLPTELI 264
PBP1_CcpA-like cd19975
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
 62-327 8.71e-85

ligand-binding domain of putative DNA transcription regulators highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.


Pssm-ID: 380630 [Multi-domain]  Cd Length: 269  Bit Score: 257.10  E-value: 8.71e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAF---RNANLLKNMlkq 138
Cdd:cd19975    1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFASGTlteENKQLLKNM--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 139 DIPISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIIT---ENAKSNHARLDAFREVMQENGIIVPPQHVIT 215
Cdd:cd19975   78 NIPVVLVSTESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISgplDDPNAGYPRYEGYKKALKDAGLPIKENLIVE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 216 TEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMA 295
Cdd:cd19975  158 GDFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQPFYEMG 237

                        250       260       270
                 ....*....|....*....|....*....|..
gi 502820249 296 VNVVDLLVREMKYPAMHKEHLLLEPKLIVRKS 327
Cdd:cd19975  238 KKAVELLLDLIKNEKKEEKSIVLPHQIIERES 269
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
 62-325 1.51e-83

ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380503 [Multi-domain]  Cd Length: 266  Bit Score: 253.72  E-value: 1.51e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDIP 141
Cdd:cd06280    1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGPSRELKRLLKHGIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 ISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIIT--ENAKSNHARLDAFREVMQENGIIVPPQHVITTEAS 219
Cdd:cd06280   81 IVLIDREVEGLELDLVAGDNREGAYKAVKHLIELGHRRIGLITgpLEISTTRERLAGYREALAEAGIPVDESLIFEGDST 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 220 IQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVV 299
Cdd:cd06280  161 IEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQPAYEIGRIAA 240

                        250       260
                 ....*....|....*....|....*.
gi 502820249 300 DLLVREMKYPAMHKEHLLLEPKLIVR 325
Cdd:cd06280  241 QLLLERIEGQGEEPRRIVLPTELIIR 266
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 62-327 6.33e-83

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380516 [Multi-domain]  Cd Length: 270  Bit Score: 252.58  E-value: 6.33e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDIP 141
Cdd:cd06293    1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSHLARLRARGTA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 ISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIIT--ENAKSNHARLDAFREVMQENGiIVPPQHVI---TT 216
Cdd:cd06293   81 VVLLDRPAPGPAGCSVSVDDVQGGALAVDHLLELGHRRIAFVSgpLRTRQVAERLAGARAAVAEAG-LDPDEVVRelsAP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 217 EASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAV 296
Cdd:cd06293  160 DANAELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQPSYELGR 239

                        250       260       270
                 ....*....|....*....|....*....|.
gi 502820249 297 NVVDLLVREMKYPAMHKEHLLLEPKLIVRKS 327
Cdd:cd06293  240 AAADLLLDEIEGPGHPHEHVVFQPELVVRSS 270
PRK10703 PRK10703
HTH-type transcriptional repressor PurR;
4-329 5.33e-82

HTH-type transcriptional repressor PurR;


Pssm-ID: 236739 [Multi-domain]  Cd Length: 341  Bit Score: 252.72  E-value: 5.33e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249   4 TIYSVAEEAGVSISTVSKVINQTGHISERTRQKVIEVMAQLNYHPSVVASALTGKPTKTIGLLVPDISNPFFADLARSIE 83
Cdd:PRK10703   3 TIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEAVE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  84 DRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLkNMLK--QDIPIsVIASEIPHISVNTVTVDD 161
Cdd:PRK10703  83 KNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLL-AMLEeyRHIPM-VVMDWGEAKADFTDAIID 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 162 --YKGSYLATDYLLSLHHKKIAIITENAKSNHA--RLDAFREVMQENGIIVPPQHVITTEASIQKGYESAKQIFSMKEKV 237
Cdd:PRK10703 161 naFEGGYLAGRYLIERGHRDIGVIPGPLERNTGagRLAGFMKAMEEANIKVPEEWIVQGDFEPESGYEAMQQILSQKHRP 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 238 TAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVVDLLVREMKYPAMHKEHLL 317
Cdd:PRK10703 241 TAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRIVNKREEPQTIE 320

                        330
                 ....*....|..
gi 502820249 318 LEPKLIVRKSTA 329
Cdd:PRK10703 321 VHPRLVERRSVA 332
PBP1_GalS-like cd06270
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ...
 62-325 3.10e-79

ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalS is a dimeric protein like GalR,and its major role is in regulating expression of the high-affinity galactose transporter encoded by the mgl operon, whereas GalR is the exclusive regulator of galactose permease, the low-affinity galactose transporter. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are homologous to the periplasmic sugar binding of ABC-type transport systems.


Pssm-ID: 380494 [Multi-domain]  Cd Length: 266  Bit Score: 242.81  E-value: 3.10e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDIP 141
Cdd:cd06270    1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEELILIAEKIPP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 ISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIITENAKS--NHARLDAFREVMQENGIIVPPQHVITTEAS 219
Cdd:cd06270   81 LVVINRYIPGLADRCVWLDNEQGGRLAAEHLLDLGHRRIACITGPLDIpdARERLAGYRDALAEAGIPLDPSLIIEGDFT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 220 IQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVV 299
Cdd:cd06270  161 IEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHYPIEEMAQAAA 240

                        250       260
                 ....*....|....*....|....*.
gi 502820249 300 DLLVReMKYPAMHKEHLLLEPKLIVR 325
Cdd:cd06270  241 ELALN-LAYGEPLPISHEFTPTLIER 265
PBP1_sucrose_transcription_regulator cd06288
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ...
 62-327 1.22e-77

ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380511 [Multi-domain]  Cd Length: 268  Bit Score: 238.99  E-value: 1.22e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDI-SNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRnanllknmlkQDI 140
Cdd:cd06288    1 TIGLITDDIaTTPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYASMHH----------REV 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 141 PISVIASEIPHISVN---------TVTVDDYKGSYLATDYLLSLHHKKIAIITENAKSNHA--RLDAFREVMQENGIIVP 209
Cdd:cd06288   71 TLPPELTDIPLVLLNcfdddpslpSVVPDDEQGGYLATRHLIEAGHRRIAFIGGPEDSLATrlRLAGYRAALAEAGIPYD 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 210 PQHVITTEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQ 289
Cdd:cd06288  151 PSLVVHGDWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVAL 230

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 502820249 290 PTKEMAVNVVDLLVREMKYPAMHKEHLLLEPKLIVRKS 327
Cdd:cd06288  231 PYYEMGRRAAELLLDGIEGEPPEPGVIRVPCPLIERES 268
PRK10423 PRK10423
transcriptional repressor RbsR; Provisional
 8-327 5.58e-77

transcriptional repressor RbsR; Provisional


Pssm-ID: 182448 [Multi-domain]  Cd Length: 327  Bit Score: 239.22  E-value: 5.58e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249   8 VAEEAGVSISTVSKVINQTGHISERTRQKVIEVMAQLNYHPSVVASALTGKPTKTIGLLVPDISNPFFADLARSIEDRSH 87
Cdd:PRK10423   4 VARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVERSCF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  88 ERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAfRNANLLKNMLKQ--DIPIsVIASEIPHISVNTVTVDD-YKG 164
Cdd:PRK10423  84 ERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCT-ETHQPSREIMQRypSVPT-VMMDWAPFDGDSDLIQDNsLLG 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 165 SYLATDYLLSLHHKKIAIIT--ENAKSNHARLDAFREVMQENGIIVPPQHVITTEASIQKGYESAKQIFSMKEKVTAIFA 242
Cdd:PRK10423 162 GDLATQYLIDKGYTRIACITgpLDKTPARLRLEGYRAAMKRAGLNIPDGYEVTGDFEFNGGFDAMQQLLALPLRPQAVFT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 243 CNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVVDLLVREMKYPAMHKEHLLLEPKL 322
Cdd:PRK10423 242 GNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQRLQLTPEL 321


                 ....*
gi 502820249 323 IVRKS 327
Cdd:PRK10423 322 MERGS 326
PBP1_LacI-like cd06290
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 62-327 5.36e-73

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380513 [Multi-domain]  Cd Length: 267  Bit Score: 226.73  E-value: 5.36e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKnMLKQDIP 141
Cdd:cd06290    1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEELLK-LLAEGIP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 ISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIIT--ENAKSNHARLDAFREVMQENGIIVPPQHVITTEAS 219
Cdd:cd06290   80 VVLVDRELEGLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHISgpEDHPDAQERYAGYRRALEDAGLEVDPRLIVEGDFT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 220 IQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVV 299
Cdd:cd06290  160 EESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYEMGKTAA 239

                        250       260
                 ....*....|....*....|....*...
gi 502820249 300 DLLVREMKYPAMHKEHLLLEPKLIVRKS 327
Cdd:cd06290  240 EILLELIEGKGRPPRRIILPTELVIRES 267
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
 62-326 2.02e-71

ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria; This group includes the ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia coli and its close homologs from other bacteria. They are members of the LacI-GalR family of repressor proteins which are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380512 [Multi-domain]  Cd Length: 268  Bit Score: 222.83  E-value: 2.02e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRN-ANLLKNMLKQDI 140
Cdd:cd06289    1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPAAGTtAELLRRLKAWGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 141 PISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAII--TENAKSNHARLDAFREVMQENGIIVPPQHVITTEA 218
Cdd:cd06289   81 PVVLALRDVPGSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLggLSDSSTRRERLAGFRAALAEAGLPLDESLIVPGPA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 219 SIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNV 298
Cdd:cd06289  161 TREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHPREIGRRA 240

                        250       260
                 ....*....|....*....|....*...
gi 502820249 299 VDLLVREMKYPAMHKEHLLLEPKLIVRK 326
Cdd:cd06289  241 ARLLLRRIEGPDTPPERIIIEPRLVVRE 268
PBP1_LacI-like cd06299
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ...
 62-327 4.24e-71

ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum produces significant amounts of L-glutamate directly from cheap sugar and ammonia; This group includes the ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum which has a unique ability to produce significant amounts of L-glutamate directly from cheap sugar and ammonia. This regulatory protein is a member of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380522 [Multi-domain]  Cd Length: 268  Bit Score: 222.15  E-value: 4.24e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDIP 141
Cdd:cd06299    1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGENSEGLQALIAQGLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 ISVIASEIPHIS-VNTVTVDDYKGSYLATDYLLSLHHKKIAIIT--ENAKSNHARLDAFREVMQENGIIVPPQHVITTEA 218
Cdd:cd06299   81 VVFVDREVEGLGgVPVVTSDNRPGAREAVEYLVSLGHRRIGYISgpLSTSTGRERLAAFRAALTAAGIPIDEELVAFGDF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 219 SIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNV 298
Cdd:cd06299  161 RQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVERIGRRA 240

                        250       260
                 ....*....|....*....|....*....
gi 502820249 299 VDLLVREMKYPAMHKEHlLLEPKLIVRKS 327
Cdd:cd06299  241 VELLLALIENGGRATSI-RVPTELIPRES 268
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 62-327 5.85e-70

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380501 [Multi-domain]  Cd Length: 266  Bit Score: 218.94  E-value: 5.85e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEkEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDIP 141
Cdd:cd06278    1 LVGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDD-VDDALRQLLQYRVDGVIVTSATLSSELAEECARRGIP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 ISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIIT--ENAKSNHARLDAFREVMQENGIivPPQHVITTEAS 219
Cdd:cd06278   80 VVLFNRVVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGgpEGTSTSRERERGFRAALAELGL--PPPAVEAGDYS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 220 IQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAK-ELKIDVPQDLSVIGFDNtvlsttiTPM-------LTTVAQPT 291
Cdd:cd06278  158 YEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAARqEGGLVVPEDISVVGFDD-------IPMaawpsydLTTVRQPI 230

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 502820249 292 KEMAVNVVDLLVREMKYPAMHKEHLLLEPKLIVRKS 327
Cdd:cd06278  231 EEMAEAAVDLLLERIENPETPPERRVLPGELVERGS 266
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
 62-327 9.87e-70

ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of AraR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380483 [Multi-domain]  Cd Length: 274  Bit Score: 218.97  E-value: 9.87e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVA---SAFRNAN--LLKNML 136
Cdd:cd01541    1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEptkSALPNPNldLYEELQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 137 KQDIPISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIITenaKSN----HARLDAFREVMQENGIIVPPQH 212
Cdd:cd01541   81 KKGIPVVFINSYYPELDAPSVSLDDEKGGYLATKHLIDLGHRRIAGIF---KSDdlqgVERYQGFIKALREAGLPIDDDR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 213 VI---TTEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQ 289
Cdd:cd01541  158 ILwysTEDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEPPLTSVVH 237

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 502820249 290 PTKEMAVNVVDLLVREMKYPaMHKEHLLLEPKLIVRKS 327
Cdd:cd01541  238 PKEELGRKAAELLLRMIEEG-RKPESVIFPPELIERES 274
PBP1_SalR cd01545
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ...
 62-327 4.93e-69

ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. The SalR binds to glucose based compound Salicin which is chemically related to aspirin. The ligand-binding of SalR is structurally homologous to the periplasmic sugar-binding domain of ABC-transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380487 [Multi-domain]  Cd Length: 270  Bit Score: 217.04  E-value: 4.93e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVM--CNTDNDAEKEKkYLSLLIRQRIDGLIVASAFRNANLLKNML-KQ 138
Cdd:cd01545    1 LIGLLYDNPSASYVSALQVGALRACREAGYHLVVepCDSDDEDLADR-LRRFLSRSRPDGVILTPPLSDDPALLDALdEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 139 DIPISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIIT--ENAKSNHARLDAFREVMQENGIIVPPQHVITT 216
Cdd:cd01545   80 GIPYVRIAPGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAgpPDHGASAERLEGFRDALAEAGLPLDPDLVVQG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 217 EASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAV 296
Cdd:cd01545  160 DFTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTTVRQPIAEMAR 239

                        250       260       270
                 ....*....|....*....|....*....|.
gi 502820249 297 NVVDLLVREMKYPAMHKEHLLLEPKLIVRKS 327
Cdd:cd01545  240 RAVELLIAAIRGAPAGPERETLPHELVIRES 270
PBP1_AglR_RafR-like cd06292
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ...
 62-328 2.97e-68

Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the repressors specific raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins highly similar to DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR). Members of this group belong to the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380515 [Multi-domain]  Cd Length: 273  Bit Score: 214.82  E-value: 2.97e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDI----SNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRN---ANLLKn 134
Cdd:cd06292    1 LIGYVVPELpggfSDPFFDEFLAALGHAAAARGYDVLLFTASGDEDEIDYYRDLVRSRRVDGFVLASTRHDdprVRYLH- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 135 mlKQDIPISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIIT--ENAKSNHARLDAFREVMQENGIIVPPQH 212
Cdd:cd06292   80 --EAGVPFVAFGRANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGgpEGSVPSDDRLAGYRAALEEAGLPFDPGL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 213 VITTEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTK 292
Cdd:cd06292  158 VVEGENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTVRQPID 237

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 502820249 293 EMAVNVVDLLVREMKYPAMHKEHLLLEPKLIVRKST 328
Cdd:cd06292  238 EIGRAVVDLLLAAIEGNPSEPREILLQPELVVRESS 273
lacI PRK09526
lac repressor; Reviewed
 1-338 3.09e-68

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 217.17  E-value: 3.09e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249   1 MKP-TIYSVAEEAGVSISTVSKVINQTGHISERTRQKVIEVMAQLNYHPSVVASALTGKPTKTIGLLVPDISNPFFADLA 79
Cdd:PRK09526   3 SKPvTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTSLALHAPSQIA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  80 RSIEDRSHERGFHVVMCNTD-NDAEKEKKYLSLLIRQRIDGLIVasafrnanllkNM-LKQD--IPISVIASEI------ 149
Cdd:PRK09526  83 AAIKSRADQLGYSVVISMVErSGVEACQAAVNELLAQRVSGVII-----------NVpLEDAdaEKIVADCADVpclfld 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 150 --PHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIIT--ENAKSNHARLDAFREVMQENGIivPPQHVITTEASIQKGYE 225
Cdd:PRK09526 152 vsPQSPVNSVSFDPEDGTRLGVEHLVELGHQRIALLAgpESSVSARLRLAGWLEYLTDYQL--QPIAVREGDWSAMSGYQ 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 226 SAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVVDLLVRE 305
Cdd:PRK09526 230 QTLQMLREGPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLLAL 309

                        330       340       350
                 ....*....|....*....|....*....|...
gi 502820249 306 MKYPAmHKEHLLLEPKLIVRKSTAPlRREATAS 338
Cdd:PRK09526 310 SQGQA-VKGSQLLPTSLVVRKSTAP-PNTQTAS 340
PBP1_LacI cd01574
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ...
 62-327 1.73e-67

ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of LacI is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380488 [Multi-domain]  Cd Length: 265  Bit Score: 212.83  E-value: 1.73e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKE-KKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDI 140
Cdd:cd01574    1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATVDEDDPASvREALDRLLSQRVDGIIVIAPDEAVLEALRRLPPGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 141 PIsVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIIT--ENAKSNHARLDAFREVMQENGIIVPPqhVITTEA 218
Cdd:cd01574   81 PV-VIVGSGPSPGVPTVSIDQEEGARLATRHLLELGHRRIAHIAgpLDWVDARARLRGWREALEEAGLPPPP--VVEGDW 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 219 SIQKGYESAKQIFSMKEkVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNV 298
Cdd:cd01574  158 SAASGYRAGRRLLDDGP-VTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDFAELGRRA 236

                        250       260
                 ....*....|....*....|....*....
gi 502820249 299 VDLLVREMKYPAMHKEHLLLEPKLIVRKS 327
Cdd:cd01574  237 VELLLALIEGPAPPPESVLLPPELVVRES 265
PBP1_LacI-like cd06273
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 62-327 6.45e-66

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380497 [Multi-domain]  Cd Length: 268  Bit Score: 208.90  E-value: 6.45e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDIP 141
Cdd:cd06273    1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVGSDHDPELFELLEQRQVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 ISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIITENAKSN---HARLDAFREVMQENGIIVPPQHVITTEA 218
Cdd:cd06273   81 YVLTWSYDEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGNdraRARLAGIRDALAERGLELPEERVVEAPY 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 219 SIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNV 298
Cdd:cd06273  161 SIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPAREIGELA 240

                        250       260
                 ....*....|....*....|....*....
gi 502820249 299 VDLLVREMKYPAMHKeHLLLEPKLIVRKS 327
Cdd:cd06273  241 ARYLLALLEGGPPPK-SVELETELIVRES 268
PRK11041 PRK11041
DNA-binding transcriptional regulator CytR; Provisional
 29-332 2.12e-64

DNA-binding transcriptional regulator CytR; Provisional


Pssm-ID: 182923 [Multi-domain]  Cd Length: 309  Bit Score: 206.39  E-value: 2.12e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  29 ISERTRQKVIEVMAQLNYHPSVVASALTGKPTKTIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKY 108
Cdd:PRK11041   4 VSQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 109 LSLLIRQRIDGLIVASAfrnaNLLKNMLKQD---IPISVIASEI-PHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIIT 184
Cdd:PRK11041  84 VNLIITKQIDGMLLLGS----RLPFDASKEEqrnLPPMVMANEFaPELELPTVHIDNLTAAFEAVNYLHELGHKRIACIA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 185 --ENAKSNHARLDAFREVMQENGIIVPPQHVITTEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDV 262
Cdd:PRK11041 160 gpEEMPLCHYRLQGYVQALRRCGITVDPQYIARGDFTFEAGAKALKQLLDLPQPPTAVFCHSDVMALGALSQAKRMGLRV 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 263 PQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVVDLLVREMKYPAMHKEHLLLEPKLIVRKSTAPLR 332
Cdd:PRK11041 240 PQDLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSSGSRLLDCELIIRGSTAAPP 309
PBP1_CcpB-like cd06286
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ...
 62-325 7.27e-64

ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species; This group includes the ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species. Catabolite control protein B (CcpB) is 30% identical in sequence to CcpA which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. Like CcpA, the DNA-binding protein CcpB exerts its catabolite-repressing effect by a mechanism dependent on the presence of HPr(Ser-P), the small phosphocarrier proteins of the phosphoenolpyruvate-sugar phosphotransferase system, but with a less significant degree.


Pssm-ID: 380509 [Multi-domain]  Cd Length: 262  Bit Score: 203.16  E-value: 7.27e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKqDIP 141
Cdd:cd06286    1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLIITSRENDWEVIEPYAK-YGP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 IsVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIIT--ENAKSNH--ARLDAFREVMQENGIIVPPQHVITTE 217
Cdd:cd06286   80 I-VLCEETDSPDIPSVYIDRYEAYLEALEYLKEKGHRKIGYCLgrPESSSAStqARLKAYQDVLGEHGLSLREEWIFTNC 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 218 ASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITpmLTTVAQPTKEMAVN 297
Cdd:cd06286  159 HTIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISELLN--LTTIDQPLEEMGKE 236

                        250       260
                 ....*....|....*....|....*....
gi 502820249 298 VVDLLVREM-KYPAMHKEhllLEPKLIVR 325
Cdd:cd06286  237 AFELLLSQLeSKEPTKKE---LPSKLIER 262
PBP1_GalR cd01544
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ...
 70-327 9.89e-59

ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalR is a dimeric protein like GalS and is exclusively involved in the regulation of galactose permease, the low-affinity galactose transporter. GalS is involved in regulating expression of the high-affinity galactose transporter encoded by the mgl operon. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are structurally homologous to the periplasmic sugar binding of ABC-type transport systems.


Pssm-ID: 380486 [Multi-domain]  Cd Length: 269  Bit Score: 190.43  E-value: 9.89e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  70 ISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEkkylsllIRQRIDGLIVASAFrNANLLKNMLKQDIPISVIASEI 149
Cdd:cd01544   14 LEDPYYLSIRLGIEKEAKKLGYEIKTIFRDDEDLES-------LLEKVDGIIAIGKF-SKEEIEKLKKLNPNIVFVDSNP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 150 PHISVNTVTVDDYKGSYLATDYLLSLHHKKIAII--TENAKSNHA-----RLDAFREVMQENGIIVPPqHVITTEASIQK 222
Cdd:cd01544   86 DPDGFDSVVPDFEQAVRQALDYLIELGHRRIGFIggKEYTSDDGEeiedpRLRAFREYMKEKGLYNEE-YIYIGEFSVES 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 223 GYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVVDLL 302
Cdd:cd01544  165 GYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTPPLTTVHIPTEEMGRTAVRLL 244

                        250       260
                 ....*....|....*....|....*
gi 502820249 303 VREMKYPAMHKEHLLLEPKLIVRKS 327
Cdd:cd01544  245 LERINGGRTIPKKVLLPTKLIERES 269
PBP1_LacI-like cd19974
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 62-327 1.39e-58

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380629 [Multi-domain]  Cd Length: 270  Bit Score: 190.07  E-value: 1.39e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDI---SNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFrNANLLKNMLKQ 138
Cdd:cd19974    1 NIAVLIPERffgDNSFYGKIYQGIEKELSELGYNLVLEIISDEDEEELNLPSIISEEKVDGIIILGEI-SKEYLEKLKEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 139 DIPISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAII--TENAKSNHARLDAFREVMQENGIIVPPQHVITT 216
Cdd:cd19974   80 GIPVVLVDHYDEELNADSVLSDNYYGAYKLTSYLIEKGHKKIGFVgdINYTSSFMDRYLGYRKALLEAGLPPEKEEWLLE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 217 EASIQKG-YESAKQIFSMkEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMA 295
Cdd:cd19974  160 DRDDGYGlTEEIELPLKL-MLPTAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLTTVEVDKEAMG 238

                        250       260       270
                 ....*....|....*....|....*....|..
gi 502820249 296 VNVVDLLVREMKYPAMHKEHLLLEPKLIVRKS 327
Cdd:cd19974  239 RRAVEQLLWRIENPDRPFEKILVSGKLIERDS 270
PBP1_CatR-like cd06296
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ...
 62-328 1.63e-57

ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation; This group includes the ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in catechol degradation. This group belongs to the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380519 [Multi-domain]  Cd Length: 270  Bit Score: 187.10  E-value: 1.63e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDIP 141
Cdd:cd06296    1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQLRLLRSAGIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 ISVI--ASEIPHiSVNTVTVDDYKGSYLATDYLLSLHHKKIAIIT--ENAKSNHARLDAFREVMQENGIIVPPQHVITTE 217
Cdd:cd06296   81 FVLIdpVGEPDP-DLPSVGATNWAGGRLATEHLLDLGHRRIAVITgpPRSVSGRARLAGYRAALAEAGIAVDPDLVREGD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 218 ASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVN 297
Cdd:cd06296  160 FTYEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVHQPLREMGAV 239

                        250       260       270
                 ....*....|....*....|....*....|.
gi 502820249 298 VVDLLVREMKYPAMHKEHLLLEPKLIVRKST 328
Cdd:cd06296  240 AVRLLLRLLEGGPPDARRIELATELVVRGST 270
PRK10727 PRK10727
HTH-type transcriptional regulator GalR;
3-341 7.54e-57

HTH-type transcriptional regulator GalR;


Pssm-ID: 182681 [Multi-domain]  Cd Length: 343  Bit Score: 188.04  E-value: 7.54e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249   3 PTIYSVAEEAGVSISTVSKVINQTGHISERTRQKVIEVMAQLNYHPSVVASALTGKPTKTIGLLVPDISNPFFADLARSI 82
Cdd:PRK10727   2 ATIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKAV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  83 EDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQdIPISVIASEI-PHISVNTVTVDD 161
Cdd:PRK10727  82 EQVAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVVHAKMIPDAELASLMKQ-IPGMVLINRIlPGFENRCIALDD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 162 YKGSYLATDYLLSLHHKKIAIITenakSNHA------RLDAFREVMQENGIIVPPQHVITTEASIQKGYESAKQIFSMKE 235
Cdd:PRK10727 161 RYGAWLATRHLIQQGHTRIGYLC----SNHSisdaedRLQGYYDALAESGIPANDRLVTFGEPDESGGEQAMTELLGRGR 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 236 KVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVVDL-LVREMKYPAMHKE 314
Cdd:PRK10727 237 NFTAVACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELaLALADNRPLPEIT 316

                        330       340
                 ....*....|....*....|....*..
gi 502820249 315 HlLLEPKLIVRKSTAPLRREATASTNN 341
Cdd:PRK10727 317 N-VFSPTLVRRHSVSTPSLEASHHATS 342
PBP1_LacI-like cd06281
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 62-327 4.08e-56

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380504 [Multi-domain]  Cd Length: 270  Bit Score: 183.59  E-value: 4.08e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAF-RNANLLKNMLKQDI 140
Cdd:cd06281    1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILTPGDeDDPELAAALARLDI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 141 PISVIASEIPhISVNTVTVDDYKGSYLATDYLLSLHHKKIAIITENAKS--NHARLDAFREVMQENGIIVPPQHVITTEA 218
Cdd:cd06281   81 PVVLIDRDLP-GDIDSVLVDHRSGVRQATEYLLSLGHRRIALLTGGPDIrpGRERIAGFKAAFAAAGLPPDPDLVRLGSF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 219 SIQKGYESAKQIFSMKEKVTAIFAC-NDLLAiGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVN 297
Cdd:cd06281  160 SADSGFREAMALLRQPRPPTAIIALgTQLLA-GVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDLDAVGRA 238

                        250       260       270
                 ....*....|....*....|....*....|.
gi 502820249 298 VVDLLVREMKYPAMHK-EHLLLEPKLIVRKS 327
Cdd:cd06281  239 AAELLLDRIEGPPAGPpRRIVVPTELILRDS 269
PBP1_RegR_EndR_KdgR-like cd06283
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ...
 62-325 1.02e-54

ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR; Ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR, all of which are members of the LacI-GalR family of bacterial transcription regulators. RegR regulates bacterial competence and the expression of virulence factors, including hyaluronidase. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380506 [Multi-domain]  Cd Length: 266  Bit Score: 180.05  E-value: 1.02e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDIP 141
Cdd:cd06283    1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPTGNNNDAYLELAQKGLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 ISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIITENAK---SNHARLDAFREVMQENGiIVPPQHVI---T 215
Cdd:cd06283   81 VVLVDRQIEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPIKgisTRRERLQGFLDALARYN-IEGDVYVIeieD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 216 TEASIQKGYESAKQIFSMKekvTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMA 295
Cdd:cd06283  160 TEDLQQALAAFLSQHDGGK---TAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQPTYEIG 236

                        250       260       270
                 ....*....|....*....|....*....|
gi 502820249 296 VNVVDLLVREMKYPAMHKEHLLLEPKLIVR 325
Cdd:cd06283  237 KAAAEILLERIEGDSGEPKEIELPSELIIR 266
PBP1_LacI-like cd06282
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 62-307 2.38e-54

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380505 [Multi-domain]  Cd Length: 267  Bit Score: 179.02  E-value: 2.38e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQ-DI 140
Cdd:cd06282    1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTVGDAQGSEALELLEEeGV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 141 PISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIITEN-AKSNHA--RLDAFREVMQENGI-IVPPQHVITT 216
Cdd:cd06282   81 PYVLLFNQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAGDfSASDRArlRYQGYRDALKEAGLkPIPIVEVDFP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 217 EASIQKGYESakqIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAV 296
Cdd:cd06282  161 TNGLEEALTS---LLSGPNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQPSRDMGR 237

                        250
                 ....*....|.
gi 502820249 297 NVVDLLVREMK 307
Cdd:cd06282  238 AAADLLLAEIE 248
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
 62-327 5.71e-54

ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators; This group represents the ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of GntR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding, which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380489 [Multi-domain]  Cd Length: 269  Bit Score: 178.07  E-value: 5.71e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKnMLKQ-DI 140
Cdd:cd01575    1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEHTPATRK-LLRAaGI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 141 PIsVIASEIP--HISVNtVTVDDYKGSYLATDYLLSLHHKKIAIITENAKSNH---ARLDAFREVMQENGIIVPPQHVIT 215
Cdd:cd01575   80 PV-VETWDLPddPIDMA-VGFSNFAAGRAMARHLIERGYRRIAFVGARLDGDSrarQRLEGFRDALAEAGLPLPLVLLVE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 216 TEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMA 295
Cdd:cd01575  158 LPSSFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVRVPRYEIG 237

                        250       260       270
                 ....*....|....*....|....*....|..
gi 502820249 296 VNVVDLLVREMKYPAMHKEHLLLEPKLIVRKS 327
Cdd:cd01575  238 RKAAELLLARLEGEEPEPRVVDLGFELVRRES 269
PRK10401 PRK10401
HTH-type transcriptional regulator GalS;
4-340 1.59e-53

HTH-type transcriptional regulator GalS;


Pssm-ID: 236681 [Multi-domain]  Cd Length: 346  Bit Score: 179.20  E-value: 1.59e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249   4 TIYSVAEEAGVSISTVSKVINQTGHISERTRQKVIEVMAQLNYHPSVVASALTGKPTKTIGLLVPDISNPFFADLARSIE 83
Cdd:PRK10401   3 TIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAVD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  84 DRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIV-ASAFRNANLLKNMlkQDIPISVIASEI-PHISVNTVTVDD 161
Cdd:PRK10401  83 LVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVhSKALSDDELAQFM--DQIPGMVLINRVvPGYAHRCVCLDN 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 162 YKGSYLATDYLLSLHHKKIAIITenakSNHA------RLDAFREVMQENGIIVPPQHVITTEASIQKGYESAKQIFSMKE 235
Cdd:PRK10401 161 VSGARMATRMLLNNGHQRIGYLS----SSHGieddamRRAGWMSALKEQGIIPPESWIGTGTPDMQGGEAAMVELLGRNL 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 236 KVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVVDLLVREMKYPAMHKEH 315
Cdd:PRK10401 237 QLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQGAAGNLDPRAS 316

                        330       340
                 ....*....|....*....|....*
gi 502820249 316 LLLEPKLIVRKSTAPlRREATASTN 340
Cdd:PRK10401 317 HCFMPTLVRRHSVAT-RQNAAAITN 340
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
 62-304 1.04e-52

ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of TreR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380484 [Multi-domain]  Cd Length: 259  Bit Score: 174.61  E-value: 1.04e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVaSAFRNANLLKNMLKQ-DI 140
Cdd:cd01542    1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIIL-FATEITDEHRKALKKlKI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 141 PISVIASEIPHISvnTVTVDDYKGSYLATDYLLSLHHKKIAIITENaKSNHA----RLDAFREVMQENGIIVPpqHVITT 216
Cdd:cd01542   80 PVVVLGQEHEGFS--CVYHDDYGAGKLLGEYLLKKGHKNIAYIGVD-EEDIAvgvaRKQGYLDALKEHGIDEV--EIVET 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 217 EASIQKGYESAKQIFSmKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAV 296
Cdd:cd01542  155 DFSMESGYEAAKELLK-ENKPDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEAGE 233


                 ....*...
gi 502820249 297 NVVDLLVR 304
Cdd:cd01542  234 KAAELLLD 241
PBP1_MalR-like cd06294
ligand-binding domain of maltose transcription regulator MalR which is a member of the ...
 62-323 4.33e-50

ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors; This group includes the ligand-binding domain of maltose transcription regulator MalR which is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380517 [Multi-domain]  Cd Length: 269  Bit Score: 168.15  E-value: 4.33e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDIS-----NPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNML 136
Cdd:cd06294    1 TIGLVLPSSAeelfqNPFFSEVLRGISQVANENGYSLLLATGNTEEELLEEVKRMVRGRRVDGFILLYSKEDDPLIEYLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 137 KQDIPISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIITENAKSNHA--RLDAFREVMQENGIIVPPQHVI 214
Cdd:cd06294   81 EEGFPFVVIGKPLDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVSidRLQGYKQALKEAGLPLDDDYIL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 215 TTEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEM 294
Cdd:cd06294  161 LLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSVDINPYEL 240

                        250       260
                 ....*....|....*....|....*....
gi 502820249 295 AVNVVDLLVREMKYPAMHKEHLLLEPKLI 323
Cdd:cd06294  241 GREAAKLLINLLEGPESLPKNVIVPHELI 269
PBP1_LacI-like cd06277
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 73-327 1.12e-49

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380500 [Multi-domain]  Cd Length: 275  Bit Score: 167.03  E-value: 1.12e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  73 PFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKkYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDIPISVIASEIPHI 152
Cdd:cd06277   19 PFFSELIDGIEREARKYGYNLLISSVDIGDDFDE-ILKELTDDQSSGIILLGTELEEKQIKLFQDVSIPVVVVDNYFEDL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 153 SVNTVTVDDYKGSYLATDYLLSLHHKKIAIITENAKSNH--ARLDAFREVMQENGIIVPPQHVITTEASIQKGYESAKQI 230
Cdd:cd06277   98 NFDCVVIDNEDGAYEAVKYLVELGHTRIGYLASSYRIKNfeERRRGFRKAMRELGLSEDPEPEFVVSVGPEGAYKDMKAL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 231 FSMKEKV-TAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVVDLLVREMKYP 309
Cdd:cd06277  178 LDTGPKLpTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRRLIEKIKDP 257

                        250
                 ....*....|....*...
gi 502820249 310 AMHKEHLLLEPKLIVRKS 327
Cdd:cd06277  258 DGGTLKILVSTKLVERGS 275
PBP1_LacI-like cd06279
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ...
 62-327 1.32e-47

ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium glutamicum and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380502 [Multi-domain]  Cd Length: 284  Bit Score: 161.99  E-value: 1.32e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPD-----ISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEkekkYLSLLIRQRIDGLIVASAFRNANLLKNML 136
Cdd:cd06279    1 AIGVLLPDdlsyaFSDPVAAQFLRGVAEVCEEEGLGLLLLPATDEGS----AAAAVRNAAVDGFIVYGLSDDDPAVAALR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 137 KQDIPISVIASEIP--HISVNtvtVDDYKGSYLATDYLLSLHHKKIAIIT----------------ENAKSN---HARLD 195
Cdd:cd06279   77 RRGLPLVVVDGPAPpgIPSVG---IDDRAAARAAARHLLDLGHRRIAILSlrldrgrergpvsaerLAAATNsvaRERLA 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 196 AFREVMQENGIIVPPQHVI-TTEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNT 274
Cdd:cd06279  154 GYRDALEEAGLDLDDVPVVeAPGNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRVPEDLSVTGFDDI 233

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 502820249 275 VLSTTITPMLTTVAQPTKEMAVNVVDLLVREMkyPAMHKEHLLLEPKLIVRKS 327
Cdd:cd06279  234 PEAAAADPGLTTVRQPAVEKGRAAARLLLGLL--PGAPPRPVILPTELVVRAS 284
PBP1_CcpA cd06298
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ...
 62-327 2.81e-47

ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; Ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.


Pssm-ID: 380521 [Multi-domain]  Cd Length: 268  Bit Score: 160.53  E-value: 2.81e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIvasaFRNANLLKNMLKQ--- 138
Cdd:cd06298    1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGII----FMGDELTEEIREEfkr 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 139 -DIPISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIIT---ENAKSNHARLDAFREVMQENGIIVPPQHVI 214
Cdd:cd06298   77 sPVPVVLAGTVDSDHEIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSgplKEYINNDKKLQGYKRALEEAGLEFNEPLIF 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 215 TTEASIQKGYESAKQIFSmKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEM 294
Cdd:cd06298  157 EGDYDYDSGYELYEELLE-SGEPDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPLYDI 235

                        250       260       270
                 ....*....|....*....|....*....|...
gi 502820249 295 AVNVVDLLVREMKYPAMHKEHLLLEPKLIVRKS 327
Cdd:cd06298  236 GAVAMRLLTKLMNKEEVEETIVKLPHSIIWRQS 268
PBP1_AglR-like cd20010
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ...
 62-323 3.61e-47

Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and similar proteins; Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380665 [Multi-domain]  Cd Length: 269  Bit Score: 160.41  E-value: 3.61e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVP----DISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLK 137
Cdd:cd20010    1 AIGLVLPldpgDLGDPFFLEFLAGLSEALAERGLDLLLAPAPSGEDELATYRRLVERGRVDGFILARTRVNDPRIAYLLE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 138 QDIPISV---IASEIPHisvNTVTVDDYKGSYLATDYLLSLHHKKIAIITENAKSN--HARLDAFREVMQENGIIVPPQH 212
Cdd:cd20010   81 RGIPFVVhgrSESGAPY---AWVDIDNEGAFRRATRRLLALGHRRIALLNGPEELNfaHQRRDGYRAALAEAGLPVDPAL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 213 VITTEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTI-TPMLTTVAQPT 291
Cdd:cd20010  158 VREGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLLPALEYfSPPLTTTRSSL 237

                        250       260       270
                 ....*....|....*....|....*....|..
gi 502820249 292 KEMAVNVVDLLVREMKYPAMHKEHLLLEPKLI 323
Cdd:cd20010  238 RDAGRRLAEMLLALIDGEPAAELQELWPPELI 269
PRK10014 PRK10014
DNA-binding transcriptional repressor MalI; Provisional
 2-326 1.09e-44

DNA-binding transcriptional repressor MalI; Provisional


Pssm-ID: 182193 [Multi-domain]  Cd Length: 342  Bit Score: 156.02  E-value: 1.09e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249   2 KPTIYSVAEEAGVSISTVSKVINQTGHISERTRQKVIEVMAQLNYHPSVVASALTGKPTKTIGLLVPDISNPFFADLARS 81
Cdd:PRK10014   6 KITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAELTAG 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  82 IEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLK-QDIPIsVIASEIPHI-SVNTVTV 159
Cdd:PRK10014  86 LTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAGSSDDLREMAEeKGIPV-VFASRASYLdDVDTVRP 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 160 DDYKGSYLATDYLLSLHHKKIAIITENAKS--NHARLDAFREVMQENGIIVPPQHVITTEASIQKGYESAKQIFSMKEKV 237
Cdd:PRK10014 165 DNMQAAQLLTEHLIRNGHQRIAWLGGQSSSltRAERVGGYCATLLKFGLPFHSEWVLECTSSQKQAAEAITALLRHNPTI 244

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 238 TAIFACNDLLAI----GVMQAAK---ELKID--VPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVVDLLVREMKY 308
Cdd:PRK10014 245 SAVVCYNETIAMgawfGLLRAGRqsgESGVDryFEQQVALAAFTDVPEAELDDPPLTWASTPAREIGRTLADRMMQRITH 324

                        330
                 ....*....|....*...
gi 502820249 309 PAMHKEHLLLEPKLIVRK 326
Cdd:PRK10014 325 EETHSRNLIIPPRLIARK 342
PBP1_CelR cd06295
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ...
 60-327 1.43e-40

ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators; This group includes the ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly homologous to the LacI-GalR family of bacterial transcription regulators. The binding of CelR to the celE promoter is inhibited specifically by cellobiose. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380518 [Multi-domain]  Cd Length: 273  Bit Score: 143.16  E-value: 1.43e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  60 TKTIGLLVP-------DISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKekkYLSLLIRQRIDGLIVASAFRNANLL 132
Cdd:cd06295    3 SRTIAVVVPmdphgdqSITDPFFLELLGGISEALTDRGYDMLLSTQDEDANQ---LARLLDSGRADGLIVLGQGLDHDAL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 133 KNMLKQDIPISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAII-----TENAksnhARLDAFREVMQENGII 207
Cdd:cd06295   80 RELAQQGLPMVVWGAPEDGQSYCSVGSDNVKGGALATEHLIEIGRRRIAFLgdpphPEVA----DRLQGYRDALAEAGLE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 208 VPPQHVITTEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTV 287
Cdd:cd06295  156 ADPSLLLSCDFTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFRPPLTTV 235

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 502820249 288 AQPTKEMAVNVVDLLVREmkypaMHKEH---LLLEPKLIVRKS 327
Cdd:cd06295  236 RQDLALAGRLLVEKLLAL-----IAGEPvtsSMLPVELVVRES 273
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
 171-328 2.32e-40

Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional regulatory proteins. It is related to bacterial periplasmic binding proteins, although this domain is unlikely to be found in the periplasm. This domain acts as a sensor binding small molecule ligands that the DNA-binding domain responds to. This domain recognizes Sugars, sugar phosphates, sugar acids and purines (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433159 [Multi-domain]  Cd Length: 160  Bit Score: 139.40  E-value: 2.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  171 YLLSLHHKKIAIITEN----AKSNHARLDAFREVMQENGIIVPPQHVITTEASIQKGYESAKQifSMKEKVTAIFACNDL 246
Cdd:pfam13377   1 HLAELGHRRIALIGPEgdrdDPYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARERLR--WLGALPTAVFVANDE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  247 LAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVVDLLVREMKYPAMHKEHLLLEPKLIVRK 326
Cdd:pfam13377  79 VALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVERE 158


                  ..
gi 502820249  327 ST 328
Cdd:pfam13377 159 ST 160
PBP1_CcpA_TTHA0807 cd06297
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ...
 62-327 1.38e-38

ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its close homologs; Ligand-binding domain of the uncharacterized transcription regulator TTHA0807 from the extremely thermophilic organism Thermus thermophilus HB8 and close homologs from other bacteria. Although its exact biological function is not known, the TTHA0807 belongs to the catabolite control protein A (CcpA)family of regulatory proteins. The CcpA functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.


Pssm-ID: 380520 [Multi-domain]  Cd Length: 268  Bit Score: 137.98  E-value: 1.38e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDIP 141
Cdd:cd06297    1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLLSEYRLEKYLRNSTLAYQCDGLVMASLDLTELFEEVIVPTEKP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 ISVIASEIPhiSVNTVTVDDYKGSYLATDYLLSLHHKKIAIITENAKSNH------ARLDAFREVMQENGIIVPPQHVIT 215
Cdd:cd06297   81 VVLIDANSM--GYDCVYVDNVKGGFMATEYLAGLGEREYVFFGIEEDTVFtetvfrEREQGFLEALNKAGRPISSSRMFR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 216 TEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLstTITPMLTTVAQPTKEMA 295
Cdd:cd06297  159 IDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPW--AASPGLTTVRQPVEEMG 236

                        250       260       270
                 ....*....|....*....|....*....|..
gi 502820249 296 VNVVDLLVREMKYPAMHKEHLLLEPKLIVRKS 327
Cdd:cd06297  237 EAAAKLLLKRLNEYGGPPRSLKFEPELIVRES 268
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
 63-302 1.58e-38

Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems; Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems, all of which contain the type 1 periplasmic binding protein-like fold. Their specific ligands include lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor; in general the sugar binding domain in this family binds a sugar, which in turn changes the DNA binding activity of the repressor domain. The core structure of the periplasmic binding proteins is classified into two types and they differ in number and order of beta strands in each domain: type 1, which has six beta strands, and type 2, which has five beta strands. These two distinct structural arrangements may have originated from a common ancestor.


Pssm-ID: 380479 [Multi-domain]  Cd Length: 265  Bit Score: 137.76  E-value: 1.58e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  63 IGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLK-QDIP 141
Cdd:cd01537    2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAGVAEKARgQNVP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 ISVI-ASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIITENAKSNHA--RLDAFREVMQENGIIVPPQHVITTEA 218
Cdd:cd01537   82 VVFFdKEPSRYDKAYYVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHPDAeaRLAGVIKELNDKGIKTEQLQLDTGDW 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 219 SIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNV 298
Cdd:cd01537  162 DTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDANNLGKTT 241


                 ....
gi 502820249 299 VDLL 302
Cdd:cd01537  242 FDLL 245
fruct_sucro_rep TIGR02417
D-fructose-responsive transcription factor; Members of this family belong the lacI ...
 4-304 2.18e-32

D-fructose-responsive transcription factor; Members of this family belong the lacI helix-turn-helix family (pfam00356) of DNA-binding transcriptional regulators. All members are from the proteobacteria. Characterized members act as positive and negative transcriptional regulators of fructose and sucrose transport and metabolism. Sucrose is a disaccharide composed of fructose and glucose; D-fructose-1-phosphate rather than an intact sucrose moiety has been shown to act as the inducer. [Regulatory functions, DNA interactions]


Pssm-ID: 131470 [Multi-domain]  Cd Length: 327  Bit Score: 122.94  E-value: 2.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249    4 TIYSVAEEAGVSISTVSKVINQTGH---ISERTRQKVIEVMAQLNYHPSVVASALTGKPTKTIGLLVPDISNPFFADLAR 80
Cdd:TIGR02417   1 TLSDIAKLAGVSKTTASYVINGKAKeyrISQETVERVMAVVREQGYQPNIHAASLRAGRSRTIGLVIPDLENYSYARIAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249   81 SIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQD-IPISVIASEIPHISVNTVTV 159
Cdd:TIGR02417  81 ELEQQCREAGYQLLIACSDDNPDQEKVVIENLLARQVDALIVASCMPPEDAYYQKLQNEgLPVVALDRSLDDEHFCSVIS 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  160 DDYKGSYLATDYLLSLHHKKIAII--TENAKSNHARLDAFREVMQengiivppQHVITTEASIQKGY--ESAKQIFSMKE 235
Cdd:TIGR02417 161 DDVDAAAELIERLLSQHADEFWYLgaQPELSVSRDRLAGFRQALK--------QATLEVEWVYGGNYsrESGYQMFAKLC 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502820249  236 KV-----TAIFACNDLLAIGVMQAAKELKIDvPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVVDLLVR 304
Cdd:TIGR02417 233 ARlgrlpQALFTTSYTLLEGVLDYMLERPLL-DSQLHLATFGDNYLLDFLPLPINSVAQQHRQLAWHALELALA 305
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
 62-304 1.22e-30

periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic sugar-binding domain of active transport systems that are members of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this family function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea. The sugar binding domain is also homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR. Moreover, this periplasmic binding domain, also known as Venus flytrap domain, undergoes transition from an open to a closed conformational state upon the binding of ligands such as lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. This family also includes the periplasmic binding domain of autoinducer-2 (AI-2) receptors such as LsrB and LuxP which are highly homologous to periplasmic pentose/hexose sugar-binding proteins.


Pssm-ID: 380478 [Multi-domain]  Cd Length: 268  Bit Score: 116.90  E-value: 1.22e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAfrNANLLKNMLKQ--- 138
Cdd:cd01536    1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPV--DSEALVPAVKKana 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 139 -DIPISVIASEIPHIS--VNTVTVDDYKGSYLATDYLLSLHHK--KIAIITENAKSNHA--RLDAFREVMQENG--IIVP 209
Cdd:cd01536   79 aGIPVVAVDTDIDGGGdvVAFVGTDNYEAGKLAGEYLAEALGGkgKVAILEGPPGSSTAidRTKGFKEALKKYPdiEIVA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 210 PQhviTTEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDvpQDLSVIGFDNT------VLSTTITPm 283
Cdd:cd01536  159 EQ---PANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRT--GDIKIVGVDGTpealkaIKDGELDA- 232

                        250       260
                 ....*....|....*....|.
gi 502820249 284 ltTVAQPTKEMAVNVVDLLVR 304
Cdd:cd01536  233 --TVAQDPYLQGYLAVEAAVK 251
PBP1_FruR cd06274
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ...
 62-323 1.91e-30

ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs; Ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to members of the type 1 periplasmic binding protein superfamily. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor


Pssm-ID: 380498 [Multi-domain]  Cd Length: 264  Bit Score: 116.15  E-value: 1.91e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDIP 141
Cdd:cd06274    1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAPSTPPDDIYYLCQAAGLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 ISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIITENAK--SNHARLDAFREVMQENGIIVPPQHVITTEAS 219
Cdd:cd06274   81 VVFLDRPFSGSDAPSVVSDNRAGARALTEKLLAAGPGEIYFLGGRPElpSTAERIRGFRAALAEAGITEGDDWILAEGYD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 220 IQKGYESAKQIF-SMKEKVTAIFaCNDLLAI-GVMQAAKELKIDVPQDLSVIGFD---------NTVLSttitpmlttVA 288
Cdd:cd06274  161 RESGYQLMAELLaRLGGLPQALF-TSSLTLLeGVLRFLRERLGAIPSDLVLGTFDdhplldflpNPVDS---------VR 230

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 502820249 289 QPTKEMAVNVVDLLVREMKYPAMHKEHlLLEPKLI 323
Cdd:cd06274  231 QDHDEIAEHAFELLDALIEGQPEPGVI-IIPPELI 264
PRK11303 PRK11303
catabolite repressor/activator;
8-276 3.91e-30

catabolite repressor/activator;


Pssm-ID: 236897 [Multi-domain]  Cd Length: 328  Bit Score: 116.90  E-value: 3.91e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249   8 VAEEAGVSISTVSKVIN---QTGHISERTRQKVIEVMAQLNYHPSVVASALTGKPTKTIGLLVPDISNPFFADLARSIED 84
Cdd:PRK11303   6 IARLAGVSRTTASYVINgkaKQYRVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSYARIAKYLER 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  85 RSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNAN-LLKNMLKQDIPISVI--ASEIPHISvnTVTVDD 161
Cdd:PRK11303  86 QARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVSTSLPPEHpFYQRLQNDGLPIIALdrALDREHFT--SVVSDD 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 162 YKGSYLATDYLLSLHHKKIAIITENAKSN--HARLDAFREVMQENGIIVppqHVITTEA-SIQKGYESAKQIFSMKEKVT 238
Cdd:PRK11303 164 QDDAEMLAESLLKFPAESILLLGALPELSvsFEREQGFRQALKDDPREV---HYLYANSfEREAGAQLFEKWLETHPMPD 240

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 502820249 239 AIFACNDLLAIGVMQAAKELKIDVPQDLSVIGF-DNTVL 276
Cdd:PRK11303 241 ALFTTSYTLLQGVLDVLLERPGELPSDLAIATFgDNELL 279
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 48-304 1.20e-29

ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH domain [Carbohydrate transport and metabolism];


Pssm-ID: 441483 [Multi-domain]  Cd Length: 307  Bit Score: 115.41  E-value: 1.20e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  48 PSVVASALTGKPTKTIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAfr 127
Cdd:COG1879   21 SAAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVSPV-- 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 128 NANLLKNMLKQ----DIPISVIASEIPHISVNT-VTVDDYKGSYLATDYLLSLHHK--KIAIIT--ENAKSNHARLDAFR 198
Cdd:COG1879   99 DPDALAPALKKakaaGIPVVTVDSDVDGSDRVAyVGSDNYAAGRLAAEYLAKALGGkgKVAILTgsPGAPAANERTDGFK 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 199 EVMQEN-GI-IVPPQhviTTEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDvpQDLSVIGFDNTvl 276
Cdd:COG1879  179 EALKEYpGIkVVAEQ---YADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRK--GDVKVVGFDGS-- 251

                        250       260       270
                 ....*....|....*....|....*....|...
gi 502820249 277 STTIT-----PMLTTVAQPTKEMAVNVVDLLVR 304
Cdd:COG1879  252 PEALQaikdgTIDATVAQDPYLQGYLAVDAALK 284
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
3-72 3.93e-28

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 104.21  E-value: 3.93e-28
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249     3 PTIYSVAEEAGVSISTVSKVINQTGHISERTRQKVIEVMAQLNYHPSVVASALTGKPTKTIGLLVPDISN 72
Cdd:smart00354   1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
PRK14987 PRK14987
HTH-type transcriptional regulator GntR;
2-295 5.15e-27

HTH-type transcriptional regulator GntR;


Pssm-ID: 184949 [Multi-domain]  Cd Length: 331  Bit Score: 108.57  E-value: 5.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249   2 KPTIYSVAEEAGVSISTVSKVINQTGHISERTRQKVIEVMAQLNYHPSVVASALTGKPTKTIGLLVPDISNPFFADLARS 81
Cdd:PRK14987   5 RPVLQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  82 IEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDIP-ISVIASEIPHISVnTVTVD 160
Cdd:PRK14987  85 IESVTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIEVAGIPvVELMDSQSPCLDI-AVGFD 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 161 DYKGSYLATDYLLSLHHKKIAIITenaksnhARLDAfREVMQENGI--------IVPPQHVITTEASIQKGYESAKQIFS 232
Cdd:PRK14987 164 NFEAARQMTTAIIARGHRHIAYLG-------ARLDE-RTIIKQKGYeqamldagLVPYSVMVEQSSSYSSGIELIRQARR 235

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502820249 233 MKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMA 295
Cdd:PRK14987 236 EYPQLDGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMG 298
PBP1_hexuronate_repressor-like cd06272
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ...
 62-325 2.15e-26

ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and close homologs, all members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and its close homologs from other bacteria, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380496 [Multi-domain]  Cd Length: 266  Bit Score: 105.53  E-value: 2.15e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDI-SNPFFADLARSIEDRSHERGFH--VVMCNTDNDAEKEKKYLSLliRQRIDGLIVASAFRNANLLKNMLKQ 138
Cdd:cd06272    1 TIGLYWPSVgERVALTRLLSGINEAISKQGYNinLSICPYKVGHLCTAKGLFS--ENRFDGVIVFGISDSDIEYLNKNKP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 139 DIPISVIASEIPHISvnTVTVDDYKGSYLATDYLLSLHHKKIAII-TENAKSNH-ARLDAFREVMQENGIIVPPQHVITT 216
Cdd:cd06272   79 KIPIVLYNRESPKYS--TVNVDNEKAGRLAVLLLIQKGHKSIAYIgNPNSNRNQtLRGKGFIETCEKHGIHLSDSIIDSR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 217 EASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAV 296
Cdd:cd06272  157 GLSIEGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLTVVGVPIEKIAE 236

                        250       260
                 ....*....|....*....|....*....
gi 502820249 297 NVVDLLVREMKYPAMHKEHLLLEPKLIVR 325
Cdd:cd06272  237 ESLRLILKLIEGRENEIQQLILYPELIFR 265
PBP1_XylR cd01543
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ...
 63-328 1.09e-25

ligand-binding domain of DNA transcription repressor specific for xylose (XylR); Ligand-binding domain of DNA transcription repressor specific for xylose (XylR), a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of XylR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380485 [Multi-domain]  Cd Length: 265  Bit Score: 103.44  E-value: 1.09e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  63 IGLLVpDISNPFFADLARSIEDRSHERG---FHVVMcnTDNDAEkekkyLSLLIRQRIDGLIVAsaFRNANLLKNMLKQD 139
Cdd:cd01543    2 VALLL-ETSRGYGRRLLRGIARYAREHGpwsLYLEP--PGYEEL-----LDLLKGWKGDGIIAR--LDDPELAEALRRLG 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 140 IPISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIA-IITENAKSNHARLDAFREVMQENGIivpPQHVITTEA 218
Cdd:cd01543   72 IPVVNVSGSRPEPGFPRVTTDNEAIGRMAAEHLLERGFRHFAfCGFRNAAWSRERGEGFREALREAGY---ECHVYESPP 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 219 SIQKGYESAKQIFSMK-----EKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDN-TVLSTTITPMLTTVAQPTK 292
Cdd:cd01543  149 SGSSRSWEEEREELADwlkslPKPVGIFACNDDRARQVLEACREAGIRVPEEVAVLGVDNdELICELSSPPLSSIALDAE 228

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 502820249 293 EMAVNVVDLLVREMKYPAMHKEHLLLEPK-LIVRKST 328
Cdd:cd01543  229 QIGYEAAELLDRLMRGERVPPEPILIPPLgVVTRQST 265
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 62-304 2.92e-25

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380542 [Multi-domain]  Cd Length: 278  Bit Score: 102.82  E-value: 2.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNA--NLLKNMLKQD 139
Cdd:cd06319    1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAapTVLDLANEAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 140 IPIsVIASeiphISVNT------VTVDDYKGSYLATDYL------LSLHHKKIAIIT--ENAKSNHARLDAFREVMQENG 205
Cdd:cd06319   81 IPV-VIAD----IGTGGgdyvsyIISDNYDGGYQAGEYLaealkeNGWGGGSVGIIAipQSRVNGQARTAGFEDALEEAG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 206 iIVPPQHVITTEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDvpQDLSVIGFDNTVLSTTITP--- 282
Cdd:cd06319  156 -VEEVALRQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRT--GDILVVGFDGDPEALDLIKdgk 232

                        250       260
                 ....*....|....*....|..
gi 502820249 283 MLTTVAQPTKEMAVNVVDLLVR 304
Cdd:cd06319  233 LDGTVAQQPFGMGARAVELAIQ 254
PBP1_AglR_RafR-like cd06271
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ...
 72-323 5.19e-24

ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380495 [Multi-domain]  Cd Length: 264  Bit Score: 99.04  E-value: 5.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  72 NPFFADLARSIEDRSHERGFHVVMCnTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNMLKQDIPISVIASEIPH 151
Cdd:cd06271   14 NGTVSE*VSGITEEAGTTGYHLLVW-PFEEAES*VPIRDLVETGSADGVILSEIEPNDPRVQFLTKQNFPFVAHGRSD*P 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 152 ISVNTVTVDDYKGSYLATDYLLSLHHKKIAIITENAKSNHA--RLDAFREVMQENGIIVPPQHvitTEASIQKGYESAKQ 229
Cdd:cd06271   93 IGHAWVDIDNEAGAYEAVERLAGLGHRRIAFIVPPARYSPHdrRLQGYVRA*RDAGLTGYPLD---ADTTLEAGRAAAQR 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 230 IFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNT-VLSTTITPMLTTVAQPTKEMAVNVVDLLVREMKY 308
Cdd:cd06271  170 LLALSPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSApFLGAMITPPLTTVHAPIAEAGRELAKALLARIDG 249

                        250
                 ....*....|....*
gi 502820249 309 PAMHKEHLLLEPKLI 323
Cdd:cd06271  250 EDPETLQVLVQPSLS 264
PRK10339 PRK10339
DNA-binding transcriptional repressor EbgR; Provisional
 4-303 3.08e-23

DNA-binding transcriptional repressor EbgR; Provisional


Pssm-ID: 182389 [Multi-domain]  Cd Length: 327  Bit Score: 98.29  E-value: 3.08e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249   4 TIYSVAEEAGVSISTVSKVINQ--TGHISERTRQKVIEVMAQLNYHPSVVASALTGKPTKTIGLLV------PDISNPFF 75
Cdd:PRK10339   3 TLKDIAIEAGVSLATVSRVLNDdpTLNVKEETKHRILEIAEKLEYKTSSARKLQTGAVNQHHILAIysyqqeLEINDPYY 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  76 ADLARSIEDRSHERGFHVVMCNtdnDAEKEKKYlsllirQRIDGLIVASAFRNAnLLKNMLKQDIPISVIASEIPHISVN 155
Cdd:PRK10339  83 LAIRHGIETQCEKLGIELTNCY---EHSGLPDI------KNVTGILIVGKPTPA-LRAAASALTDNICFIDFHEPGSGYD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 156 TVTVDDYKGSYLATDYLLSLHHKKIAIITENAKSNHA--RLDAFREVMQENGIiVPPQHVITTEASIQKGYESAKQIFSM 233
Cdd:PRK10339 153 AVDIDLARISKEIIDFYINQGVNRIGFIGGEDEPGKAdiREVAFAEYGRLKQV-VREEDIWRGGFSSSSGYELAKQMLAR 231

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 234 KEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVVDLLV 303
Cdd:PRK10339 232 EDYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNLLY 301
Periplasmic_Binding_Protein_type1 cd01391
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
 70-303 1.66e-22

Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This model and hierarchy represent the ligand binding domains of the LacI family of transcriptional regulators, periplasmic binding proteins of the ABC-type transport systems, the family C G-protein couples receptors (GPCRs), membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal leucine-isoleucine-valine binding protein (LIVBP)-like domains of the ionotropic glutamate receptors (iGluRs). In LacI-like transcriptional regulator and the bacterial periplasmic binding proteins, the ligands are monosaccharides, including lactose, ribose, fructose, xylose, arabinose, galactose/glucose and other sugars, with a few exceptions. Periplasmic sugar binding proteins are one of the components of ABC transporters and are involved in the active transport of water-soluble ligands. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The core structures of periplasmic binding proteins are classified into two types, and they differ in number and order of beta strands: type 1 has six beta strands while type 2 has five beta strands per sub-domain. These two structural folds are thought to be distantly related via a common ancestor. Notably, while the N-terminal LIVBP-like domain of iGluRs belongs to the type 1 periplasmic-binding fold protein superfamily, the glutamate-binding domain of the iGluR is structurally similar to the type 2 periplasmic-binding fold.


Pssm-ID: 380477 [Multi-domain]  Cd Length: 280  Bit Score: 95.41  E-value: 1.66e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  70 ISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANLLKNML-KQDIPISVIASE 148
Cdd:cd01391   12 IREQFGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGPGSSSVAIVIQNLAqLFDIPQLALDAT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 149 IPHIS-------VNTVTVDDYKGSYLATDYLLSLHHKKIAII-TENAKSNHARLDAFREVMQENGIIVPPQHVITTEAsI 220
Cdd:cd01391   92 SQDLSdktlykyFLSVVFSDTLGARLGLDIVKRKNWTYVAAIhGEGLNSGELRMAGFKELAKQEGICIVASDKADWNA-G 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 221 QKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKidVPQDLSVIGFDNT-----VLSTTITPMLTTVAQPTKEMA 295
Cdd:cd01391  171 EKGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLG--LVGDVSVIGSDGWadrdeVGYEVEANGLTTIKQQKMGFG 248


                 ....*...
gi 502820249 296 VNVVDLLV 303
Cdd:cd01391  249 ITAIKAMA 256
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
 60-326 2.11e-22

Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the periplasmic binding proteins, and the LacI family transcriptional regulators. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The LacI family of proteins consist of transcriptional regulators related to the lac repressor. In this case, generally the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain (pfam00356).


Pssm-ID: 395423 [Multi-domain]  Cd Length: 281  Bit Score: 94.88  E-value: 2.11e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249   60 TKTIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVAS-AFRNANLLKNMLKQ 138
Cdd:pfam00532   1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTpAPSGDDITAKAEGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  139 DIPI--SVIASEIPhISVNTVTVDDYKGSYLATDYLLSLHHKK-IAI--ITENAKSNHARLDAFREVMQENGIIVPPQHV 213
Cdd:pfam00532  81 GIPViaADDAFDNP-DGVPCVMPDDTQAGYESTQYLIAEGHKRpIAVmaGPASALTARERVQGFMAALAAAGREVKIYHV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  214 ITTEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAA-KELKIDVPQD-----LSVIGFDN--TVLSTTITPMLT 285
Cdd:pfam00532 160 ATGDNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALlKQGRVKIPDIvgigiNSVVGFDGlsKAQDTGLYLSPL 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 502820249  286 TVAQ-PTKEMAVNVVDLLVREMKYPAMHKEHLLLEPKLIVRK 326
Cdd:pfam00532 240 TVIQlPRQLLGIKASDMVYQWIPKFREHPRVLLIPRDFFKET 281
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
 62-310 1.99e-21

periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs; Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis D-ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group belong to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.


Pssm-ID: 380546 [Multi-domain]  Cd Length: 268  Bit Score: 91.97  E-value: 1.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIV----ASAFRNAnlLKNMLK 137
Cdd:cd06323    1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLInptdSDAVSPA--VEEANE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 138 QDIPI-----SVIASEI-PHISVNTVtvddyKGSYLATDYLLSLHHKKIAII----TENAKSNHARLDAFREVMQENGII 207
Cdd:cd06323   79 AGIPVitvdrSVTGGKVvSHIASDNV-----AGGEMAAEYIAKKLGGKGKVVelqgIPGTSAARERGKGFHNAIAKYPKI 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 208 vppqHVITTEA---SIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKidvPQDLSVIGFDNT---VLSTTIT 281
Cdd:cd06323  154 ----NVVASQTadfDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAG---RKDVIVVGFDGTpdaVKAVKDG 226

                        250       260       270
                 ....*....|....*....|....*....|..
gi 502820249 282 PMLTTVAQPTKEM---AVNVVDLLVREMKYPA 310
Cdd:cd06323  227 KLAATVAQQPEEMgakAVETADKYLKGEKVPK 258
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 63-307 2.15e-21

Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins. This domain recognizes fructose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433182 [Multi-domain]  Cd Length: 259  Bit Score: 91.60  E-value: 2.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249   63 IGLLVPDISNPFFADLARSIEDRSHERGF-HVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNAnlLKNMLKQ--- 138
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGeVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTA--LAPVLKKakd 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  139 -DIPISVIASEIPHIS-VNTVTVDDYKGSYLATDYLLSL--HHKKIAIITENAKSNHA--RLDAFREVMQEN--GIIVPP 210
Cdd:pfam13407  79 aGIPVVTFDSDAPSSPrLAYVGFDNEAAGEAAGELLAEAlgGKGKVAILSGSPGDPNAneRIDGFKKVLKEKypGIKVVA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  211 QhVITTEASIQKGYESAKQIFS-MKEKVTAIFACNDLLAIGVMQAAKELKIDvpQDLSVIGFDNT------VLSTTITpm 283
Cdd:pfam13407 159 E-VEGTNWDPEKAQQQMEALLTaYPNPLDGIISPNDGMAGGAAQALEAAGLA--GKVVVTGFDATpealeaIKDGTID-- 233

                         250       260
                  ....*....|....*....|....
gi 502820249  284 lTTVAQPTKEMAVNVVDLLVREMK 307
Cdd:pfam13407 234 -ATVLQDPYGQGYAAVELAAALLK 256
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 62-307 1.85e-19

monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380625 [Multi-domain]  Cd Length: 275  Bit Score: 86.53  E-value: 1.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHER-GFH--VVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANL--LKNML 136
Cdd:cd19970    1 KVALVMKSLANEFFIEMEKGARKHAKEAnGYEllVKGIKQETDIEQQIAIVENLIAQKVDAIVIAPADSKALVpvLKKAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 137 KQDIPISVI-------ASEIPHISVNTVTVDDYKGSYLATDYLLSLHHK--KIAII-----TENAKsnhARLDAFREVMQ 202
Cdd:cd19970   81 DAGIAVINIdnrldadALKEGGINVPFVGPDNRQGAYLAGDYLAKKLGKggKVAIIegipgADNAQ---QRKAGFLKAFE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 203 ENGI-IVPPQhviTTEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDvpQDLSVIGFDNTvlsTTIT 281
Cdd:cd19970  158 EAGMkIVASQ---SANWEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKA--GKVLVVGFDNI---PAVR 229

                        250       260       270
                 ....*....|....*....|....*....|..
gi 502820249 282 P------MLTTVAQPTKEMAVNVVDLLVREMK 307
Cdd:cd19970  230 PllkdgkMLATIDQHPAKQAVYGIEYALKMLN 261
PBP1_RafR-like cd20009
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ...
 159-323 2.46e-18

Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar proteins; Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) which is a member of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type I periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380664 [Multi-domain]  Cd Length: 266  Bit Score: 83.36  E-value: 2.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 159 VDDYKGSYLATDYLLSLHHKKIAIITENAK---SNHaRLDAFREVMQENGIIVPPQHVITTEASIQKGYESAKQIFSMKE 235
Cdd:cd20009  100 FDNEAFAYEAVRRLAARGRRRIALVAPPREltyAQH-RLRGFRRALAEAGLEVEPLLIVTLDSSAEAIRAAARRLLRQPP 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 236 KVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVVDLLVREMKYPAMHKEH 315
Cdd:cd20009  179 RPDGIICASEIAALGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPIDTLYEDIEEAGRFLAEALLRRIEGEPAEPLQ 258


                 ....*...
gi 502820249 316 LLLEPKLI 323
Cdd:cd20009  259 TLERPELI 266
HTH_LacI cd01392
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ...
 8-55 2.95e-17

Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; HTH-DNA binding domain of the LacI (lactose operon repressor) family of bacterial transcriptional regulators and their putative homologs found in plants. The LacI family has more than 500 members distributed among almost all bacterial species. The monomeric proteins of the LacI family contain common structural features that include a small DNA-binding domain with a helix-turn-helix motif in the N-terminus, a regulatory ligand-binding domain which exhibits the type I periplasmic binding protein fold in the C-terminus for oligomerization and for effector binding, and an approximately 18-amino acid linker connecting these two functional domains. In LacI-like transcriptional regulators, the ligands are monosaccharides including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars, with a few exceptions. When the C-terminal domain of the LacI family repressor binds its ligand, it undergoes a conformational change which affects the DNA-binding affinity of the repressor. In Escherichia coli, LacI represses transcription by binding with high affinity to the lac operon at a specific operator DNA sequence until it interacts with the physiological inducer allolactose or a non-degradable analog IPTG (isopropyl-beta-D-thiogalactopyranoside). Induction of the repressor lowers its affinity for the operator sequence, thereby allowing transcription of the lac operon structural genes (lacZ, lacY, and LacA). The lac repressor occurs as a tetramer made up of two functional dimers. Thus, two DNA binding domains of a dimer are required to bind the inverted repeat sequences of the operator DNA binding sites.


Pssm-ID: 143331 [Multi-domain]  Cd Length: 52  Bit Score: 74.37  E-value: 2.95e-17
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 502820249   8 VAEEAGVSISTVSKVINQTGHISERTRQKVIEVMAQLNYHPSVVASAL 55
Cdd:cd01392    3 IARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSL 50
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
 62-272 6.63e-17

periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; Periplasmic binding domain of ABC-type YtfQ-like transport systems. The YtfQ protein from Escherichia coli is up-regulated under glucose-limited conditions and shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their ligand specificity is not determined experimentally.


Pssm-ID: 380532 [Multi-domain]  Cd Length: 285  Bit Score: 79.57  E-value: 6.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAfrNANLLKNMLKQdip 141
Cdd:cd06309    1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPI--DATGWDPVLKE--- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 isVIASEIPHISVNTvTVDDYKGS----YLATDYL-------------LSLHHKKIAIITENAKSNHA--RLDAFREVMQ 202
Cdd:cd06309   76 --AKDAGIPVILVDR-TIDGEDGSlyvtFIGSDFVeegrraaewlvknYKGGKGNVVELQGTAGSSVAidRSKGFREVIK 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502820249 203 E--NGIIVPPQhviTTEASIQKGYESAKQIFSM-KEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFD 272
Cdd:cd06309  153 KhpNIKIVASQ---SGNFTREKGQKVMENLLQAgPGDIDVIYAHNDDMALGAIQALKEAGLKPGKDVLVVGID 222
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
 62-300 1.68e-16

D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ribose binding protein (ttRBP); Periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose binding protein (ttRBP) and its mesophilic homologs. Members of this group are belonging to the type 1 periplasmic binding protein superfamily, whose members are involved in chemotaxis, ATP-binding cassette transport, and intercellular communication in central nervous system. The thermophilic and mesophilic ribose-binding proteins are structurally very similar, but differ substantially in thermal stability.


Pssm-ID: 380622 [Multi-domain]  Cd Length: 272  Bit Score: 78.13  E-value: 1.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIvasaFRNANL------LKNM 135
Cdd:cd19967    1 LVAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAII----LDPADAdasiaaVKKA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 136 LKQDIPISVIASEIPH--ISVNTVTVDDYKGSYLATDYLLSLHHKKIAIIT----ENAKSNHARLDAFREVMQENGIIVP 209
Cdd:cd19967   77 KDAGIPVFLIDREINAegVAVAQIVSDNYQGAVLLAQYFVKLMGEKGLYVEllgkESDTNAQLRSQGFHSVIDQYPELKM 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 210 PQHVITTEASiQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIdvPQDLSVIGFDNT---VLSTTITPMLTT 286
Cdd:cd19967  157 VAQQSADWDR-TEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGR--AGDVIIVGFDGSndvRDAIKEGKISAT 233

                        250
                 ....*....|....
gi 502820249 287 VAQPTKEMAVNVVD 300
Cdd:cd19967  234 VLQPAKLIARLAVE 247
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 62-323 5.93e-16

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380544 [Multi-domain]  Cd Length: 270  Bit Score: 76.56  E-value: 5.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIED--RSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAfrNANLLKNMLKQ- 138
Cdd:cd06321    1 VIGVTVQDLGNPFFVAMVRGAEEaaAEINPGAKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAA--DSAGIEPAIKRa 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 139 -DIPISVIASEIPHISVN-TVTVDDYKGSYLATDYLL-SLHHK-KIAIIteNAKSNHA---RLDAFREVMQEN-GIIVPP 210
Cdd:cd06321   79 kDAGIIVVAVDVAAEGADaTVTTDNVQAGYLACEYLVeQLGGKgKVAII--DGPPVSAvidRVNGCKEALAEYpGIKLVD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 211 QHviTTEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDvpqDLSVIGFDNT-----VLSTTITPMLT 285
Cdd:cd06321  157 DQ--NGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRD---DIVITSVDGSpeavaALKREGSPFIA 231

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 502820249 286 TVAQPTKEMAVNVVDLLVREMKYPAMHKEHLLLEPKLI 323
Cdd:cd06321  232 TAAQDPYDMARKAVELALKILNGQEPAPELVLIPSTLV 269
LacI pfam00356
Bacterial regulatory proteins, lacI family;
4-49 3.88e-15

Bacterial regulatory proteins, lacI family;


Pssm-ID: 306791 [Multi-domain]  Cd Length: 46  Bit Score: 68.43  E-value: 3.88e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 502820249    4 TIYSVAEEAGVSISTVSKVINQTGHISERTRQKVIEVMAQLNYHPS 49
Cdd:pfam00356   1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 62-257 6.59e-14

monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380626 [Multi-domain]  Cd Length: 267  Bit Score: 70.69  E-value: 6.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVA----SAFRNAnlLKNMLK 137
Cdd:cd19971    1 KFGFSYMTMNNPFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNpvdsEGIRPA--LEAAKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 138 QDIPISVIASEIPHIS-VN-TVTVDDYKGSYLATDYLLSLHHK--KIAIIT-ENAKSNHARLDAFREVMQEN-GIIVPPQ 211
Cdd:cd19971   79 AGIPVINVDTPVKDTDlVDsTIASDNYNAGKLCGEDMVKKLPEgaKIAVLDhPTAESCVDRIDGFLDAIKKNpKFEVVAQ 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 502820249 212 hvITTEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKE 257
Cdd:cd19971  159 --QDGKGQLEVAMPIMEDILQAHPDLDAVFALNDPSALGALAALKA 202
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 62-302 8.21e-14

monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380627 [Multi-domain]  Cd Length: 269  Bit Score: 70.55  E-value: 8.21e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANL--LKNMLKQD 139
Cdd:cd19972    1 TIGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAvpVKAARAAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 140 IPISVIASEIPHISVNT-VTVDDYKGSYLATDYLLSLHHKK--IAII--TENAKSNHARLDAFREVMQEN-GIIVPPQHv 213
Cdd:cd19972   81 IPVIAVDRNPEDAPGDTfIATDSVAAAKELGEWVIKQTGGKgeIAILhgQLGTTPEVDRTKGFQEALAEApGIKVVAEQ- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 214 iTTEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDvpQDLSVIGFD------NTVLSTTITPMLTTV 287
Cdd:cd19972  160 -TADWDQDEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGLD--HKIWVVGFDgdvaglKAVKDGVLDATMTQQ 236

                        250
                 ....*....|....*.
gi 502820249 288 AQPTKEMAV-NVVDLL 302
Cdd:cd19972  237 TQKMGRLAVdSAIDLL 252
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 62-324 1.18e-13

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380545 [Multi-domain]  Cd Length: 270  Bit Score: 70.00  E-value: 1.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLI--------VASAFRNANllk 133
Cdd:cd06322    1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIIlapvdsggIVPAIEAAN--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 134 nmlKQDIPISVIASEIPHISVNT-VTVDDYKGSYLATDYLLSLHHK---KIAIIT-ENAKSNHARLDAFREVM-QENGI- 206
Cdd:cd06322   78 ---EAGIPVFTVDVKADGAKVVThVGTDNYAGGKLAGEYALKALLGgggKIAIIDyPEVESVVLRVNGFKEAIkKYPNIe 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 207 IVPPQHVITteaSIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKidVPQDLSVIGFDNTVLSTTIT----P 282
Cdd:cd06322  155 IVAEQPGDG---RREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAG--KEDKIKVIGFDGNPEAIKAIakggK 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 502820249 283 MLTTVAQPTKEMAVNVVDLLVREMKYPAMHKEhLLLEPKLIV 324
Cdd:cd06322  230 IKADIAQQPDKIGQETVEAIVKYLAGETVEKE-ILIPPKLYT 270
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
 62-274 4.80e-13

periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The periplasmic binding protein (PBP) IbpA mediates the uptake of myo-inositol by an ABC transporter that consists of the PBP IbpA, the transmembrane permease IatP, and the ABC IatA. IbpA shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.


Pssm-ID: 380623 [Multi-domain]  Cd Length: 271  Bit Score: 68.18  E-value: 4.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNA--NLLKNMLKQD 139
Cdd:cd19968    1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKAlvPAIEAAIKAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 140 IPISVI------ASEIPHisvntVTVDDYKGSYLATDYLLSLHHKKIAII----TENAKSNHARLDAFREVMQ--ENGII 207
Cdd:cd19968   81 IPVVTVdrraegAAPVPH-----VGADNVAGGREVAKFVVDKLPNGAKVIeltgTPGSSPAIDRTKGFHEELAagPKIKV 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502820249 208 VPPQhviTTEASIQKGYESAKQIF-SMKEKVTAIFACNDLLAIGVMQAAKELKIDVpQDLSVIGFDNT 274
Cdd:cd19968  156 VFEQ---TGNFERDEGLTVMENILtSLPGPPDAIICANDDMALGAIEAMRAAGLDL-KKVKVIGFDAV 219
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 97-275 2.07e-12

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380661 [Multi-domain]  Cd Length: 274  Bit Score: 66.47  E-value: 2.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  97 NTDNDAEKEKKYLSLLIRQRIDGLIVASA--FRNANLLKNMLKQDIPISVIASEIPHISVNT-VTVDDYKGSYLATDYLL 173
Cdd:cd20006   40 ESEEDIDGQIELIEEAIAQKPDAIVLAASdyDRLVEAVERAKKAGIPVITIDSPVNSKKADSfVATDNYEAGKKAGEKLA 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 174 SLHHK--KIAIIT--ENAKSNHARLDAFREVMQENGIIvppqHVITTE---ASIQKGYESAKQIFSMKEKVTAIFACNDL 246
Cdd:cd20006  120 SLLGEkgKVAIVSfvKGSSTAIEREEGFKQALAEYPNI----KIVETEycdSDEEKAYEITKELLSKYPDINGIVALNEQ 195

                        170       180
                 ....*....|....*....|....*....
gi 502820249 247 LAIGVMQAAKELKIDvpQDLSVIGFDNTV 275
Cdd:cd20006  196 STLGAARALKELGLG--GKVKVVGFDSSV 222
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
 62-272 2.70e-12

periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic binding domain of two-component sensor kinase signaling systems, some of which are fused with a C-terminal histidine kinase A domain (HisK) and/or a signal receiver domain (REC). Members of this group share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily and are predicted to be involved in sensing of environmental stimuli; their substrate specificities, however, are not known in detail.


Pssm-ID: 380531 [Multi-domain]  Cd Length: 268  Bit Score: 66.03  E-value: 2.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHE-RGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNA--NLLKNMLKQ 138
Cdd:cd06308    1 VIGFSQCSLNDPWRAAMNEEIKAEAAKyPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADAltPVVKKAYDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 139 DIPISVIASEIPHISVNT-VTVDDYKGSYLATDYLLSLHHKKIAII----TENAKSNHARLDAFREVMQENgiivPPQHV 213
Cdd:cd06308   81 GIPVIVLDRKVSGDDYTAfIGADNVEIGRQAGEYIAELLNGKGNVVeiqgLPGSSPAIDRHKGFLEAIAKY----PGIKI 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502820249 214 ITTEA---SIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDvpQDLSVIGFD 272
Cdd:cd06308  157 VASQDgdwLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGRE--KEIKIIGVD 216
PBP1_LacI-like cd06287
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 117-327 9.92e-12

ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380510 [Multi-domain]  Cd Length: 268  Bit Score: 64.36  E-value: 9.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 117 IDGLIVASAFRNANLLKNMLKQDIPISVIA------SEIPHIsvntvtvdDYKGSYLATDYLLSLH---HKKIAIITENA 187
Cdd:cd06287   57 VDGAIVVEPTVEDPILARLRQRGVPVVSIGrapgtdEPVPYV--------DLQSAATARLLLEHLHgagARQVALLTGSS 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 188 KSNhARLDAFR---EVMQENGIivpPQHVITTEASI--QKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDV 262
Cdd:cd06287  129 RRN-SSLESEAaylRFAQEYGT---TPVVYKVPESEgeRAGYEAAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSV 204

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502820249 263 PQDLSVIGFDNTVLSTTITPMLTTVAQPTKEMAVNVVDLLVREMKyPAMHKEHLLLEPKLIVRKS 327
Cdd:cd06287  205 PEDLMVVTRYDGIRARTADPPLTAVDLHLDRVARTAIDLLFASLS-GEERSVEVGPAPELVVRAS 268
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
 63-310 1.16e-11

periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis; Periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis. The members of this group are belonging to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Like other periplasmic receptors of the ABC-type transport systems, the allose-binding protein consists of two alpha/beta domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding.


Pssm-ID: 380543 [Multi-domain]  Cd Length: 283  Bit Score: 64.21  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  63 IGLLVPDISNPFFADLARSIEDRSHERGFHV-VMC-NTDNDAEKEKKYLSLLIRQRIDGLIVA--SAFrnaNL---LKNM 135
Cdd:cd06320    2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVdVQAaPSETDTQGQLNLLETMLNKGYDAILVSpiSDT---NLippIEKA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 136 LKQDIPI-----SVIASEIPHISVNT---VTVDDYKGSYLATDYLLSLHHK--KIAIITENAKSNHA--RLDAFREVMQE 203
Cdd:cd06320   79 NKKGIPVinlddAVDADALKKAGGKVtsfIGTDNVAAGALAAEYIAEKLPGggKVAIIEGLPGNAAAeaRTKGFKETFKK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 204 NGIIvppQHVITTEAS--IQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELkiDVPQDLSVIGFDNTV------ 275
Cdd:cd06320  159 APGL---KLVASQPADwdRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAA--GKTGKVLVVGTDGIPeakksi 233

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 502820249 276 ----LSTTITPMLTTVAQptkeMAVNVVDLLVREMKYPA 310
Cdd:cd06320  234 kageLTATVAQYPYLEGA----MAVEAALRLLQGQKVPA 268
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 97-272 1.68e-11

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380659 [Multi-domain]  Cd Length: 273  Bit Score: 63.79  E-value: 1.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  97 NTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNA--NLLKNMLKQDIPISVIASEIP---HISVntVTVDDYKGSYLATDY 171
Cdd:cd20004   38 SREDDVEAQIQIIEYFIDQGVDGIVLAPLDRKAlvAPVERARAQGIPVVIIDSDLGgdaVISF--VATDNYAAGRLAAKR 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 172 LLSLHHKKIAII----TENAKSNHARLDAFREVMQE--NGIIVPPQHVITTeaSIQKGYESAKQIFSMKEKVTAIFACND 245
Cdd:cd20004  116 MAKLLNGKGKVAllrlAKGSASTTDRERGFLEALKKlaPGLKVVDDQYAGG--TVGEARSSAENLLNQYPDVDGIFTPNE 193

                        170       180
                 ....*....|....*....|....*..
gi 502820249 246 LLAIGVMQAAKELKidVPQDLSVIGFD 272
Cdd:cd20004  194 STTIGALRALRRLG--LAGKVKFIGFD 218
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
 62-274 3.33e-11

periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs; Periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs from other bacteria. They are members of the type 1 periplasmic binding protein superfamily which consists of two domains connected by a three-stranded hinge. TmGBP is specific for glucose and its binding pocket is buried at the interface of the two domains. TmGBP also exhibits high thermostability and the highest structural similarity to E. coli glucose binding protein (ecGBP).


Pssm-ID: 380537 [Multi-domain]  Cd Length: 271  Bit Score: 62.98  E-value: 3.33e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMC-NTDNDAEKEKKYLSLLIRQRIDGLIVASAfrNANLLKNMLKQdi 140
Cdd:cd06314    1 TFALVPKGLNNPFWDLAEAGAEKAAKELGVNVEFVgPQKSDAAEQVQLIEDLIARGVDGIAISPN--DPEAVTPVINK-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 141 pisVIASEIPHISVNT----------VTVDDYKGSYLATDYLLSLHHK--KIAIIT-----ENAKsnhARLDAFREVMQE 203
Cdd:cd06314   77 ---AADKGIPVITFDSdapdskrlayIGTDNYEAGREAGELMKKALPGggKVAIITgglgaDNLN---ERIQGFKDALKG 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502820249 204 -NGIIVPPqhVITTEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIdvPQDLSVIGFDNT 274
Cdd:cd06314  151 sPGIEIVD--PLSDNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGK--VGKVKIVGFDTL 218
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 62-274 2.54e-09

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380547 [Multi-domain]  Cd Length: 317  Bit Score: 57.61  E-value: 2.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDIS-NPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQ--RIDGLIVASAFRNANLLKNMLKQ 138
Cdd:cd06324    1 RVVFINPGKEdEPFWQNVTRFMQAAAKDLGIELEVLYANRNRFKMLELAEELLARppKPDYLILVNEKGVAPELLELAEQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 139 -DIPI-----SVIASEIPHISVN---------TVTVDDYKGSYLATDYLLSLHHKK--------IAIitENAKSNHA--- 192
Cdd:cd06324   81 aKIPVflinnDLTDEERALLGKPrekfkywlgSIVPDNEQAGYLLAKALIKAARKKsddgkirvLAI--SGDKSTPAsil 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 193 RLDAFREVMQENGIIVPPQHVITTEaSIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGFD 272
Cdd:cd06324  159 REQGLRDALAEHPDVTLLQIVYANW-SEDEAYQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGLKPGKDVLVGGID 237


                 ..
gi 502820249 273 NT 274
Cdd:cd06324  238 WS 239
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 62-274 1.54e-08

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380663 [Multi-domain]  Cd Length: 277  Bit Score: 54.93  E-value: 1.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMC--NTDNDAEKEKKYLSLLIRQRIDGLIVA-SAFRNANLLKNMLKQ 138
Cdd:cd20008    1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLgpATEADIAGQVNLVENAISRKPDAIVLApNDTAALVPAVEAADA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 139 DIPISVIASEI-PHISVNTVTVDDYKGSYLATDYLLSLHHK------KIAIITENA--KSNHARLDAFREVMQENG---I 206
Cdd:cd20008   81 GIPVVLVDSGAnTDDYDAFLATDNVAAGALAADELAELLKAsgggkgKVAIISFQAgsQTLVDREEGFRDYIKEKYpdiE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502820249 207 IVPPQHvitTEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKidVPQDLSVIGFDNT 274
Cdd:cd20008  161 IVDVQY---SDGDIAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAG--KAGKIVLVGFDSS 223
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 96-272 2.28e-08

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380660 [Multi-domain]  Cd Length: 274  Bit Score: 54.56  E-value: 2.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  96 CNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNA--NLLKNMLKQDIPISVIASEIPH-ISVNTVTVDDYKGSYLATDYL 172
Cdd:cd20005   37 PDTESDVDKQIEMLDNAIAKKPDAIALAALDTNAllPQLEKAKEKGIPVVTFDSGVPSdLPLATVATDNYAAGALAADHL 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 173 LSLHHK--KIAII--TENAKSNHARLDAFREVMQEN--GI-IVPPQHVITTEASIQkgyESAKQIFSMKEKVTAIFACND 245
Cdd:cd20005  117 AELIGGkgKVAIVahDATSETGIDRRDGFKDEIKEKypDIkVVNVQYGVGDHAKAA---DIAKAILQANPDLKGIYATNE 193

                        170       180
                 ....*....|....*....|....*..
gi 502820249 246 LLAIGVMQAAKELKidVPQDLSVIGFD 272
Cdd:cd20005  194 GAAIGVANALKEMG--KLGKIKVVGFD 218
PBP1_ABC_xylose_binding-like cd01538
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ...
 62-310 3.41e-08

periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380480 [Multi-domain]  Cd Length: 283  Bit Score: 53.97  E-value: 3.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAfrNANLLKNMLK--QD 139
Cdd:cd01538    1 KIGVSLPNLREARWQTDRDIMVEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPV--DGQALSPVVAeaKA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 140 IPISVIASE--IPHISVN-TVTVDDYK-GSYLATDYLLSLHHKKIAIITENAKSNHARL--DAFREVMQ---ENGIIVPP 210
Cdd:cd01538   79 EGIKVIAYDrlILNADVDyYISFDNEKvGELQAQALLDAKPEGNYVLIGGSPTDNNAKLfrDGQMKVLQpaiDSGKIKVV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 211 QHVITTEASIQKGYESAKQIF-SMKEKVTAIFACNDLLAIGVMQAAKE--LKIDVP---QDLSVIGFdNTVLSTTITpml 284
Cdd:cd01538  159 GDQWVDDWLPANAQQIMENALtANGNNVDAVVASNDGTAGGAIAALKAqgLSGGVPvsgQDADLAAI-KRILAGTQT--- 234

                        250       260
                 ....*....|....*....|....*....
gi 502820249 285 TTVAQPTKEM---AVNVVDLLVREMKYPA 310
Cdd:cd01538  235 MTVYKDIRLLadaAAEVAVALMRGEKPPI 263
XylF COG4213
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ...
 62-301 4.90e-08

ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 443359 [Multi-domain]  Cd Length: 310  Bit Score: 53.60  E-value: 4.90e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDisnpffADLARSIEDRSH------ERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASafRNANLLKNM 135
Cdd:COG4213    4 KIGVSLPT------KTSERWIRDGDNfkaalkELGYEVDVQNANGDVATQLSQIENMITKGADVLVIAP--IDGTALAAV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 136 L----KQDIPisVIASEipHISVNT-----VTVDDYK-----GSYLAtDYLLSLHHKKIAIITENAKSNHARL--DAFRE 199
Cdd:COG4213   76 LekakAAGIP--VIAYD--RLILNSdvdyyVSFDNVKvgelqGQYLV-DGLPLKGKGNIELFGGSPTDNNATLffEGAMS 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 200 VMQ---ENGIIVPPQHVITTEASIQKGYESAKQIF-SMKEKVTAIFACNDLLAIGVMQAAKELKID--VPqdlsVIGFDN 273
Cdd:COG4213  151 VLQpyiDSGKLVVVSGQWTLGWDPETAQKRMENLLtANGNKVDAVLAPNDGLAGGIIQALKAQGLAgkVV----VTGQDA 226

                        250       260       270
                 ....*....|....*....|....*....|...
gi 502820249 274 TVLSttITPMLT-----TVAQPTKEMAVNVVDL 301
Cdd:COG4213  227 ELAA--VQRILAgtqymTVYKDTRELAEAAAEL 257
PBP1_ABC_xylose_binding-like cd19992
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
 63-307 5.18e-08

periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380647 [Multi-domain]  Cd Length: 284  Bit Score: 53.36  E-value: 5.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  63 IGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASafRNANLLKNML----KQ 138
Cdd:cd19992    2 IGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAP--VDAGAAANIVdkakAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 139 DIPISVIASEIPHISVN-TVTVDDYKGSYLATDYLLSLHHK-KIAIITENAKSNHARL--DAFREVMQEN----GI-IVP 209
Cdd:cd19992   80 GVPVISYDRLILNADVDlYVGRDNYKVGQLQAEYALEAVPKgNYVILSGDPGDNNAQLitAGAMDVLQPAidsgDIkIVL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 210 PQHVITTEASIQKGY-ESAkqIFSMKEKVTAIFACNDLLAIGVMQAAKELKID--VP---QDLSVIGFDNTVLSTtitpM 283
Cdd:cd19992  160 DQYVKGWSPDEAMKLvENA--LTANNNNIDAVLAPNDGMAGGAIQALKAQGLAgkVFvtgQDAELAALKRIVEGT----Q 233

                        250       260
                 ....*....|....*....|....
gi 502820249 284 LTTVAQPTKEMAVNVVDLLVREMK 307
Cdd:cd19992  234 TMTVWKDLKELARAAADAAVKLAK 257
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
 62-272 5.51e-08

periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380541 [Multi-domain]  Cd Length: 282  Bit Score: 53.18  E-value: 5.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNA--NLLKNMLKQD 139
Cdd:cd06318    1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGltPAVKAAKAAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 140 IPISVIASEI-PHISVNT-VTVDDYKGSYLATDYLLSLHHK---KIAIITENA--KSNHARLDAFREVMQENGIIVPPQH 212
Cdd:cd06318   81 IPVITVDSALdPSANVATqVGRDNKQNGVLVGKEAAKALGGdpgKIIELSGDKgnEVSRDRRDGFLAGVNEYQLRKYGKS 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502820249 213 VITTEASIQKGYESAKQIFSMKEKVTA------IFACNDLLAIGVMQAAKELKIDvpQDLSVIGFD 272
Cdd:cd06318  161 NIKVVAQPYGNWIRSGAVAAMEDLLQAhpdinvVYAENDDMALGAMKALKAAGML--DKVKVAGAD 224
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
 73-294 7.31e-08

monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380624 [Multi-domain]  Cd Length: 278  Bit Score: 53.11  E-value: 7.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  73 PFFADLARSIEDRSHERGFHVVMC-NTDNDAEKEKKYLSLLIRQRIDGLIVA----SAFRNAnlLKNMLKQDIPISVIAS 147
Cdd:cd19969   12 PYWDDVKEGFEDAGAELGVKTEYTgPATADVNEQITAIEQAIAKNPDGIAVSaidpEALTPT--INKAVDAGIPVVTFDS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 148 EIP---HISVntVTVDDYKGSYLATDYLLSLHHK--KIAIITENAKSNHA-RLDAFREVMQEN-GIIVppQHVITTEASI 220
Cdd:cd19969   90 DAPeskRISY--VGTDNYEAGYAAAEKLAELLGGkgKVAVLTGPGQPNHEeRVEGFKEAFAEYpGIEV--VAVGDDNDDP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 221 QKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKE--LKIDVPqdlsVIGFD--NTVLST----TITpmlTTVAQPTK 292
Cdd:cd19969  166 EKAAQNTSALLQAHPDLVGIFGVDASGGVGAAQAVREagKTGKVK----IVAFDddPETLDLikdgVID---ASIAQRPW 238


                 ..
gi 502820249 293 EM 294
Cdd:cd19969  239 MM 240
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
 62-304 3.59e-07

similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Proteins similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. The sugar-binding domain of the periplasmic proteins in this group is also homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR), DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380528 [Multi-domain]  Cd Length: 273  Bit Score: 50.76  E-value: 3.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIV--ASAFRNANLLKNMLKQD 139
Cdd:cd06305    1 TIAVVRNGTSGDWDQQALQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIIshGDADALDPKLKKALDAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 140 IPISVIASEIPHISVNTVTVDDYKGSYLATDYLLSLHHKKIAIITENAkSNHA----RLDAFREVMQEN--GIIVPPQHV 213
Cdd:cd06305   81 IPVVTFDTDSQVPGVNNITQDDYALGTLSLGQLVKDLNGEGNIAVFNV-FGVPpldkRYDIYKAVLKANpgIKKIVAELG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 214 ITTEASIQKGYESAKQIFSM--KEKVTAIFACNDLLAIGVMQAAKEL-KIDVPqdlsVIGFD--NTVLSTTIT---PMLT 285
Cdd:cd06305  160 DVTPNTAADAQTQVEALLKKypEGGIDAIWAAWDEPAKGAVQALEEAgRTDIK----VYGVDisNQDLELMADegsPWVA 235

                        250
                 ....*....|....*....
gi 502820249 286 TVAQPTKEMAVNVVDLLVR 304
Cdd:cd06305  236 TAAQDPALIGTVAVRNVAR 254
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 62-259 2.01e-06

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380534 [Multi-domain]  Cd Length: 270  Bit Score: 48.52  E-value: 2.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGlIVASAFRNANL---LKNMLKQ 138
Cdd:cd06311    1 TIGISIPSADHGWTAGVAYYAEKQAKELADLEYKLVTSSNANEQVSQLEDLIAQKVDA-IVILPQDSEELtvaAQKAKDA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 139 DIPISVIASEIP-HISVNTVTVDDYKGSYLATDYLL-SLHHKKIAIITENAKS---NHARLDAFREVMQENgiivPPQHV 213
Cdd:cd06311   80 GIPVVNFDRGLNvLIYDLYVAGDNPGMGVVSAEYIGkKLGGKGNVVVLEVPSSgsvNEERVAGFKEVIKGN----PGIKI 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 502820249 214 ITTEAS---IQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELK 259
Cdd:cd06311  156 LAMQAGdwtREDGLKVAQDILTKNKKIDAVWAADDDMAIGVLQAIKEAG 204
PBP1_GGBP cd01539
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ...
 62-301 2.30e-06

periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species; Periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species. GGBP is a member of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic GGBP is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380481 [Multi-domain]  Cd Length: 302  Bit Score: 48.35  E-value: 2.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERG-FHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNA--NLLKNMLKQ 138
Cdd:cd01539    2 KIGVFIYNYDDTFISSVRKALEKAAKAGGkIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAaqTIIDKAKAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 139 DIPIsVIASEIPHISVntvtVDDYKGSY---------------LATDYLLSlhHKKIA---------IITENAKSNH--- 191
Cdd:cd01539   82 NIPV-IFFNREPSRED----LKSYDKAYyvgtdaeesgimqgeIIADYWKA--NPEIDkngdgkiqyVMLKGEPGHQdai 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 192 ARLDAFREVMQENGIIVPPQHVITTEASIQKGYESAKQIFSMKE-KVTAIFACNDLLAIGVMQAAKEL---KIDVPQDLS 267
Cdd:cd01539  155 ARTKYSVKTLNDAGIKTEQLAEDTANWDRAQAKDKMDAWLSKYGdKIELVIANNDDMALGAIEALKAAgynTGDGDKYIP 234

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 502820249 268 VIGFDNtvlsttiTP----------MLTTVAQPTKEMAVNVVDL 301
Cdd:cd01539  235 VFGVDA-------TPealeaikegkMLGTVLNDAKAQAKAIYEL 271
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 68-280 3.13e-06

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380535 [Multi-domain]  Cd Length: 272  Bit Score: 48.00  E-value: 3.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  68 PDISNPFFADLARSIEDRSHERGFHVVMCN-TDNDAEKEKKYLSLLIRQRIDGLIVASAFRNAnlLKNMLKQdipisVIA 146
Cdd:cd06312    8 GSPSDPFWSVVKKGAKDAAKDLGVTVQYLGpQNNDIADQARLIEQAIAAKPDGIIVTIPDPDA--LEPALKR-----AVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 147 SEIPHISVNTVTV--------------DDYKGSYLATDYLLSLHHKKIAII-TENAKSNH-ARLDAFREVMQENGIIVPP 210
Cdd:cd06312   81 AGIPVIAINSGDDrskerlgaltyvgqDEYLAGQAAGERALEAGPKNALCVnHEPGNPGLeARCKGFADAFKGAGILVEL 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 211 QHVITTEASIQKGYESAKQIFSmkeKVTAIFACNDLLAIGVMQAAKELKIDvpQDLSVIGFDntvLSTTI 280
Cdd:cd06312  161 LDVGGDPTEAQEAIKAYLQADP---DTDAVLTLGPVGADPALKAVKEAGLK--GKVKIGTFD---LSPET 222
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 62-272 3.99e-06

monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380533 [Multi-domain]  Cd Length: 272  Bit Score: 47.72  E-value: 3.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVV--MCNTDNDAEKEKKYLSLLIRQRIDGLIVASAfrNANLLKNMLKQd 139
Cdd:cd06310    1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIfvGPESEEDVAGQNSLLEELINKKPDAIVVAPL--DSEDLVDPLKD- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 140 ipisVIASEIPHISVNTVTVDDYKGSYLATD-----------YLLSLHHK-KIAII--TENAKSNHARLDAFREVMQEN- 204
Cdd:cd06310   78 ----AKDKGIPVIVIDSGIKGDAYLSYIATDnyaagrlaaqkLAEALGGKgKVAVLslTAGNSTTDQREEGFKEYLKKHp 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502820249 205 -GIIVPPQHVITTEAsiQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDvpQDLSVIGFD 272
Cdd:cd06310  154 gGIKVLASQYAGSDY--AKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLS--GQIKIVGFD 218
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 62-307 4.75e-06

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380540 [Multi-domain]  Cd Length: 281  Bit Score: 47.37  E-value: 4.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNANL--LKNMLKQD 139
Cdd:cd06317    1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIpaIKRASEAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 140 IPISVIASEIPHISVNT-VTVDDYKGSY----LATDYLLSLHHKKIAIITENAKSN---HARLDAFREVMQENGIIvppQ 211
Cdd:cd06317   81 IPVIAYDAVIPSDFQAAqVGVDNLEGGKeigkYAADYIKAELGGQAKIGVVGALSSliqNQRQKGFEEALKANPGV---E 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 212 HVITTEASI--QKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQA------AKELKI---DVPQDLSVIGFDNTVLstti 280
Cdd:cd06317  158 IVATVDGQNvqEKALSAAENLLTANPDLDAIYATGEPALLGAVAAvrsqgrQGKIKVfgwDLTKQAIFLGIDEGVL---- 233

                        250       260
                 ....*....|....*....|....*..
gi 502820249 281 tpmLTTVAQPTKEMAVNVVDLLVREMK 307
Cdd:cd06317  234 ---QAVVQQDPEKMGYEAVKAAVKAIK 257
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
 61-274 6.43e-06

periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to rhizopines, which are simple sugar-like compounds produced in the nodules induced by the symbiotic root nodule bacteria, such as Rhizobium and Sinorhizobium. Rhizopine-binding-like proteins from other bacteria are also included. Two inositol based rhizopine compounds are known to date: L-3-O-methly-scyllo-inosamine (3-O-MSI) and scyllo-inosamine. Bacterial strains that can metabolize rhizopine have a greater competitive advantage in nodulation and rhizopine synthesis is regulated by NifA/NtrA regulatory transcription activators which are maximally expressed at the onset of nitrogen fixation in bacteroids. The members of this group belong to the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily.


Pssm-ID: 380524 [Multi-domain]  Cd Length: 272  Bit Score: 46.84  E-value: 6.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  61 KTIGLLVPDISNPFFADLARSIEDRSHE-RGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAFRNAnlLKNMLKqd 139
Cdd:cd06301    1 IKIGVSMQNFSDEFLTYLRDAIEAYAKEyPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDA--SAPAVD-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 140 ipiSVIASEIPHISVNTVTVDDYKGSY-----------LATDYLLSLHHKK--IAIITENAkSNHA---RLDAFREVMQE 203
Cdd:cd06301   77 ---AAADAGIPLVYVNREPDSKPKGVAfvgsddiesgeLQMEYLAKLLGGKgnIAILDGVL-GHEAqilRTEGNKDVLAK 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502820249 204 N-GI-IVPPQhviTTEASIQKGYESAKQIFSMKEKVTAIFACNDLLAIGVMQAAKELKIDVpqDLSVIGFDNT 274
Cdd:cd06301  153 YpGMkIVAEQ---TANWSREKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKKD--DILVAGIDAT 220
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
 63-325 7.84e-06

periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic sugar-binding domain of uncharacterized transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes.


Pssm-ID: 380530 [Multi-domain]  Cd Length: 275  Bit Score: 46.79  E-value: 7.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  63 IGLLVPDISNPFFADLARSIE---DRSHERGFHV-VMCNTDNDAEKekkyLSLLIRQ---RIDGLIVASAF--RNANLLK 133
Cdd:cd06307    2 FGFLLPSPENPFYELLRRAIEaaaAALRDRRVRLrIHFVDSLDPEA----LAAALRRlaaGCDGVALVAPDhpLVRAAID 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 134 NMLKQDIPISVIASEIPHI-SVNTVTVDDYKGSYLATdYLLSLHHK----KIAIITENAKS-NHA-RLDAFREVMQENGi 206
Cdd:cd06307   78 ELAARGIPVVTLVSDLPGSrRLAYVGIDNRAAGRTAA-WLMGRFLGrrpgKVLVILGSHRFrGHEeREAGFRSVLRERF- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 207 ivpPQHVItteASIQKGYESAKQIFsmkEKVTAIFACN-DLLAI--------GVMQAAKELkiDVPQDLSVIGFDntvLS 277
Cdd:cd06307  156 ---PDLTV---LEVLEGLDDDELAY---ELLRELLARHpDLVGIynagggneGIARALREA--GRARRVVFIGHE---LT 221

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502820249 278 TTITPML------TTVAQPTKEMAVNVVDLLVREMKYPAMHKEHLLLEPKLIVR 325
Cdd:cd06307  222 PETRRLLrdgtidAVIDQDPELQARRAIEVLLAHLGGKGPAPPQPPIPIEIITR 275
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
 62-307 9.45e-05

periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group includes periplasmic D-threitol-binding protein ThpA and xylitol/L-sorbitol-binding protein XypA, which are part of sugar ABC-type transport systems. Both ThpA and XypA share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.


Pssm-ID: 380536 [Multi-domain]  Cd Length: 277  Bit Score: 43.41  E-value: 9.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAfrNANLLKNMLKqdip 141
Cdd:cd06313    1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPV--DADALAPAVE---- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 142 iSVIASEIPHISVNTVTVDDYKGSYLATDYLLS-----------LHHK-KIAIItENAKSNHA---RLDAFREVMQEN-G 205
Cdd:cd06313   75 -KAKEAGIPLVGVNALIENEDLTAYVGSDDVVAgelegqavadrLGGKgNVVIL-EGPIGQSAqidRGKGIENVLKKYpD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 206 IIVPPQHviTTEASIQKGYESAKQ-IFSMKEKVTAIFACNDLLAIGVMQAAKELKIDvpqDLSVIGFD------NTVLST 278
Cdd:cd06313  153 IKVLAEQ--TANWSRDEAMSLMENwLQAYGDEIDGIIAQNDDMALGALQAVKAAGRD---DIPVVGIDgiedalQAVKSG 227

                        250       260
                 ....*....|....*....|....*....
gi 502820249 279 TitpMLTTVAQPTKEMAVNVVDLLVREMK 307
Cdd:cd06313  228 E---LIATVLQDAEAQGKGAVEVAVDAVK 253
PBP1_ABC_transporter_LIVBP-like cd06268
periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the ...
 62-280 4.94e-04

periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily; Periplasmic binding domain of ATP-binding cassette transporter-like systems that belong to the type 1 periplasmic binding fold protein superfamily. They are mostly present in archaea and eubacteria, and are primarily involved in scavenging solutes from the environment. ABC-type transporters couple ATP hydrolysis with the uptake and efflux of a wide range of substrates across bacterial membranes, including amino acids, peptides, lipids and sterols, and various drugs. These systems are comprised of transmembrane domains, nucleotide binding domains, and in most bacterial uptake systems, periplasmic binding proteins (PBPs) which transfer the ligand to the extracellular gate of the transmembrane domains. These PBPs bind their substrates selectively and with high affinity. Members of this group include ABC-type Leucine-Isoleucine-Valine-Binding Proteins (LIVBP), which are homologous to the aliphatic amidase transcriptional repressor, AmiC, of Pseudomonas aeruginosa. The uncharacterized periplasmic components of various ABC-type transport systems are included in this group.


Pssm-ID: 380492 [Multi-domain]  Cd Length: 298  Bit Score: 41.16  E-value: 4.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPdISNPFfADLARSI--------EDRSHERG-----FHVVMCNTDNDAEKEKKYLSLLI-RQRIDGLI--VASA 125
Cdd:cd06268    1 KIGVVVP-LTGPY-ADYGEEIlrgvalavEEINAAGGingrkLELVIADDQGDPETAVAVARKLVdDDKVLAVVghYSSS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 126 frnanllknMLKQDIPISVIAsEIPHISVNT---------------VTVDDYKGSYLATDYLLS-LHHKKIAIITENAKS 189
Cdd:cd06268   79 ---------VTLAAAPIYQEA-GIPLISPGStapeltegggpyvfrTVPSDAMQAAALADYLAKkLKGKKVAILYDDYDY 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 190 NHARLDAFREVMQENGIIvppqhvITTEASIQKGYESAKQIFS--MKEKVTAIFACNDLLAIG-VMQAAKELKIDVPqdl 266
Cdd:cd06268  149 GKSLADAFKKALKALGGE------IVAEEDFPLGTTDFSAQLTkiKAAGPDVLFLAGYGADAAnALKQARELGLKLP--- 219

                        250
                 ....*....|....
gi 502820249 267 sVIGFDNTVLSTTI 280
Cdd:cd06268  220 -ILGGDGLYSPELL 232
PBP1_arabinose_binding cd01540
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ...
 63-270 8.64e-04

periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily; Periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. ABP is only involved in transport contrary to other related sugar-binding proteins such as the glucose/galactose-binding protein (GGBP) and the ribose-binding protein (RBP), both of which are involved in chemotaxis as well as transport. The periplasmic ABP consists of two alpha/beta globular domains connected by a three-stranded hinge, a Venus flytrap-like domain, which undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, ABP is homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380482 [Multi-domain]  Cd Length: 294  Bit Score: 40.74  E-value: 8.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  63 IGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLI-----------VASAFRNANl 131
Cdd:cd01540    2 IGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKIDAKMDGEKVLSAIDNLIAQGAQGIVictpdqklgpaIAAKAKAAG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 132 lknmlkqdipISVIAS-----------EIPHISVNT----VTVDDYKGSYLATDYLLSLHHKKIAIITENAKSN-HARLD 195
Cdd:cd01540   81 ----------IPVIAVddqlvdadpmkIVPFVGIDAykigEAVGEWLAKEMKKRGWDDVKEVGVLAITMDTLSVcVDRTD 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 196 AFREVMQENG-----IIVPPQHVITTEasiqKGYESAKQIFSMKEKVT--AIFACNDLLAIGVMQAAKELKIDvPQDLSV 268
Cdd:cd01540  151 GAKDALKAAGfpedqIFQAPYKGTDTE----GAFNAANAVITAHPEVKhwLVVGCNDEGVLGAVRALEQAGFD-AEDIIG 225


                 ..
gi 502820249 269 IG 270
Cdd:cd01540  226 VG 227
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
 62-307 1.57e-03

periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling system; Periplasmic aldose-monosaccharides binding protein ChvE that belongs to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380649 [Multi-domain]  Cd Length: 304  Bit Score: 39.92  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249  62 TIGLLVPDISNPFFADLARSIEDRSHERGFHVVMCNTDNDAEKEKKYLSLLIRQRIDGLIVASAfrNANLLKNMLKQ--D 139
Cdd:cd19994    1 KIGISLPTKSEERWIKDGENLKSELEEAGYTVDLQYADDDVATQNSQIENMINKGAKVLVIAPV--DGSALGDVLEEakD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 140 IPISVIASEipHISVNT------VTVDDYKGSYLATDYLLS---LHHKK----IAIITENAKSNHARL------DAFREV 200
Cdd:cd19994   79 AGIPVIAYD--RLIMNTdavdyyVTFDNEKVGELQGQYLVDklgLKDGKgpfnIELFAGSPDDNNAQLffkgamEVLQPY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 201 MQENGIIVP-----PQHVITTEASIQKGYESAKQI----FSMKEKVTAIFACNDLLAIGVMQAAKELKIDVPQDLSVIGF 271
Cdd:cd19994  157 IDDGTLVVRsgqttFEQVATPDWDTETAQARMETLlsayYTGGKKLDAVLSPNDGIARGVIEALKAAGYDTGPWPVVTGQ 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 502820249 272 DNTVLSttITPMLT-----TVAQPTKEMAVNVVDLLVREMK 307
Cdd:cd19994  237 DAEDAS--VKSILDgeqsmTVFKDTRLLAKATVELVDALLE 275
PBP1_PrnA-like cd06354
periplasmic binding domain of basic membrane lipoprotein, PnrA, in Treponema pallidum and its ...
 112-272 8.46e-03

periplasmic binding domain of basic membrane lipoprotein, PnrA, in Treponema pallidum and its homologs from other bacteria and Archaea; Periplasmic binding domain of basic membrane lipoprotein, PnrA, in Treponema pallidum and its homologs from other bacteria and Archaea. The PnrA lipoprotein, also known as Tp0319 or TmpC, represents a novel family of bacterial purine nucleoside receptor encoded within an ATP-binding cassette (ABC) transport system (pnrABCDE). It shows a striking structural similarity to another basic membrane lipoprotein Med which regulates the competence transcription factor gene, comK, in Bacillus subtilis. The members of PnrA-like subgroup are likely to have similar nucleoside-binding functions and a similar type 1 periplasmic sugar-binding protein-like fold.


Pssm-ID: 380577  Cd Length: 268  Bit Score: 37.55  E-value: 8.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 112 LIRQRIDgLIVASAFRNANLLKNMLKQ--DIPISVI--ASEIPHISVNTVTVDDYKGSYLAtDYLLSL--HHKKIAIIT- 184
Cdd:cd06354   53 LADEGYD-LIITVGFAMADAVEEAAKAnpDTKFIIIdaTVDETPPNVRSIVFREEEAAFLA-GYLAALmtKTGKVGFIGg 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502820249 185 ENAKSNHARLDAFRE-VMQENGIIVPPQHVITTEA----SIQKGYESAKQIfsMKEKVTAIFACNDLLAIGVMQAAKELK 259
Cdd:cd06354  131 MDIPPVRRFEDGFAAgAKYANPDIVVDVTVIGTYAgsfnDPAKGKAIAQEM--IDQGADVIFAAAGGTGLGVIEAAKEAG 208

                        170
                 ....*....|...
gi 502820249 260 IdvpqdlSVIGFD 272
Cdd:cd06354  209 K------YAIGVD 215
 
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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