|
Name |
Accession |
Description |
Interval |
E-value |
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
1-331 |
9.99e-128 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 368.76 E-value: 9.99e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 1 MGKITMADVAKKAGVSKSTVSQFLNKRyEYMREDTRKRIEAAIEELHYQPNYLARSLKQKRTSTVGIIVANIMHRFSTEV 80
Cdd:COG1609 1 RKRVTIKDVARLAGVSVATVSRVLNGP-PRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 81 SRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMMKEGYPIVFMDRKVPDLIAPSVV 160
Cdd:COG1609 80 LRGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRPLPDPGVPSVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 161 SNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMISAN--IKKIKKELEELFALDDP 238
Cdd:COG1609 160 VDNRAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEGDfsAESGYEAARRLLARGPR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 239 PSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKASELLLKQINKEEIENHEL 318
Cdd:COG1609 240 PTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERV 319
|
330
....*....|...
gi 1816548106 319 TFPCELIIRDSSK 331
Cdd:COG1609 320 LLPPELVVRESTA 332
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
64-325 |
2.27e-121 |
|
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: 349.91 E-value: 2.27e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMMKEGYP 143
Cdd:cd19977 1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNEDLIEKLVKSGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 144 IVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMISANI- 222
Cdd:cd19977 81 VVFVDRYIPGLDVDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLELSTRQERLEGYKAALADHGLPVDEELIKHVDRq 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 223 KKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKASE 302
Cdd:cd19977 161 DDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQPTYEIGRKAAE 240
|
250 260
....*....|....*....|....
gi 1816548106 303 LLLKQI-NKEEIENHELTFPCELI 325
Cdd:cd19977 241 LLLDRIeNKPKGPPRQIVLPTELI 264
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
64-325 |
2.26e-90 |
|
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: 270.93 E-value: 2.26e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMMKEGYP 143
Cdd:cd06267 1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLAAGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 144 IVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMISAN-- 221
Cdd:cd06267 81 VVLIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLSTSRERLEGYRDALAEAGLPVDPELVVEGDfs 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 222 IKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKAS 301
Cdd:cd06267 161 EESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEMGRAAA 240
|
250 260
....*....|....*....|....
gi 1816548106 302 ELLLKQINKEEIENHELTFPCELI 325
Cdd:cd06267 241 ELLLERIEGEEEPPRRIVLPTELV 264
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
64-327 |
6.81e-82 |
|
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: 249.39 E-value: 6.81e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMMKEGYP 143
Cdd:cd06283 1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPTGNNNDAYLELAQKGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 144 IVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPL-TISTRVERQEGYKKALQDNGIEIRQPFMISANI 222
Cdd:cd06283 81 VVLVDRQIEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPIkGISTRRERLQGFLDALARYNIEGDVYVIEIEDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 223 KKIKKELEELFAL-DDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKAS 301
Cdd:cd06283 161 EDLQQALAAFLSQhDGGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQPTYEIGKAAA 240
|
250 260
....*....|....*....|....*.
gi 1816548106 302 ELLLKQINKEEIENHELTFPCELIIR 327
Cdd:cd06283 241 EILLERIEGDSGEPKEIELPSELIIR 266
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
64-327 |
3.10e-79 |
|
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: 242.93 E-value: 3.10e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMMKEGYP 143
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGPSRELKRLLKHGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 144 IVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMISAN-- 221
Cdd:cd06280 81 IVLIDREVEGLELDLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEISTTRERLAGYREALAEAGIPVDESLIFEGDst 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 222 IKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKAS 301
Cdd:cd06280 161 IEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQPAYEIGRIAA 240
|
250 260
....*....|....*....|....*.
gi 1816548106 302 ELLLKQINKEEIENHELTFPCELIIR 327
Cdd:cd06280 241 QLLLERIEGQGEEPRRIVLPTELIIR 266
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
64-329 |
1.24e-74 |
|
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: 230.87 E-value: 1.24e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKrmmKEGYP 143
Cdd:cd06291 1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILGSHSLDIEEYK---KLNIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 144 IVFMDRKVPDLIaPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMIS--AN 221
Cdd:cd06291 78 IVSIDRYLSEGI-PSVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIEIDEndFS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 222 IKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKAS 301
Cdd:cd06291 157 EEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIEEMAKEAV 236
|
250 260
....*....|....*....|....*...
gi 1816548106 302 ELLLKQINKEEIENHELTFPCELIIRDS 329
Cdd:cd06291 237 ELLLKLIEGEEIEESRIVLPVELIERET 264
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
64-330 |
1.20e-71 |
|
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: 223.64 E-value: 1.20e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMMKEGYP 143
Cdd:cd06285 1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQELAARGVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 144 IVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMISA--N 221
Cdd:cd06285 81 VVLVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDERIVPGgfT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 222 IKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKAS 301
Cdd:cd06285 161 IEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEMGRRAA 240
|
250 260
....*....|....*....|....*....
gi 1816548106 302 ELLLKQINKEEIENHELTFPCELIIRDSS 330
Cdd:cd06285 241 ELLLQLIEGGGRPPRSITLPPELVVREST 269
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
64-329 |
5.68e-71 |
|
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: 221.74 E-value: 5.68e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPT-GENFDLYKRMMKEGY 142
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSnISDEAIIKLLKEEKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 143 PIVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMISANI 222
Cdd:cd19976 81 PVVVLDRYIEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPSTYNEHERIEGYKNALQDHNLPIDESWIYSGES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 223 KKI--KKELEELFAlDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKA 300
Cdd:cd19976 161 SLEggYKAAEELLK-SKNPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQPIFEMGQEA 239
|
250 260
....*....|....*....|....*....
gi 1816548106 301 SELLLKQINKEEIENHELTFPCELIIRDS 329
Cdd:cd19976 240 AKLLLKIIKNPAKKKEEIVLPPELIKRDS 268
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
64-329 |
3.11e-70 |
|
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: 219.72 E-value: 3.11e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFpTGENFDLYKRMMKEGYP 143
Cdd:cd06284 1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILL-SGRLDAELLSELSKRYP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 144 IVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMISA--N 221
Cdd:cd06284 80 IVQCCEYIPDSGVPSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDNVYARERLEGYRRALAEAGLPVDEDLIIEGdfS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 222 IKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKAS 301
Cdd:cd06284 160 FEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIGETAA 239
|
250 260
....*....|....*....|....*...
gi 1816548106 302 ELLLKQINKEEIENHELTFPCELIIRDS 329
Cdd:cd06284 240 ELLLEKIEGEGVPPEHIILPHELIVRES 267
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
64-329 |
1.31e-65 |
|
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: 207.90 E-value: 1.31e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMMKEGYP 143
Cdd:cd06299 1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGENSEGLQALIAQGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 144 IVFMDRKVPDLI-APSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMISANI 222
Cdd:cd06299 81 VVFVDREVEGLGgVPVVTSDNRPGAREAVEYLVSLGHRRIGYISGPLSTSTGRERLAAFRAALTAAGIPIDEELVAFGDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 223 KKIKKE--LEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKA 300
Cdd:cd06299 161 RQDSGAaaAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVERIGRRA 240
|
250 260 270
....*....|....*....|....*....|
gi 1816548106 301 SELLLKQI-NKEEIENHELtfPCELIIRDS 329
Cdd:cd06299 241 VELLLALIeNGGRATSIRV--PTELIPRES 268
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
64-329 |
6.69e-64 |
|
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: 203.56 E-value: 6.69e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGlIIFPTGENFDLYKRMMKE-GY 142
Cdd:cd19975 1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDG-IIFASGTLTEENKQLLKNmNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 143 PIVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLT-ISTRVERQEGYKKALQDNGIEIRQPFMISAN 221
Cdd:cd19975 80 PVVLVSTESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISGPLDdPNAGYPRYEGYKKALKDAGLPIKENLIVEGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 222 --IKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEK 299
Cdd:cd19975 160 fsFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQPFYEMGKK 239
|
250 260 270
....*....|....*....|....*....|
gi 1816548106 300 ASELLLKQINKEEIENHELTFPCELIIRDS 329
Cdd:cd19975 240 AVELLLDLIKNEKKEEKSIVLPHQIIERES 269
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
5-334 |
2.63e-62 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 201.88 E-value: 2.63e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 5 TMADVAKKAGVSKSTVSQFLNKRyEYMREDTRKRIEAAIEELHYQPNYLARSLKQKRTSTVGIIVANIMHRFSTEVSRSI 84
Cdd:PRK10703 3 TIKDVAKRAGVSTTTVSHVINKT-RFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 85 EDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLykRMMKEGY---PIVFMD-RKVPDLIAPSVV 160
Cdd:PRK10703 82 EKNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPL--LAMLEEYrhiPMVVMDwGEAKADFTDAII 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 161 SNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMISANIKKIK--KELEELFALDDP 238
Cdd:PRK10703 160 DNAFEGGYLAGRYLIERGHRDIGVIPGPLERNTGAGRLAGFMKAMEEANIKVPEEWIVQGDFEPESgyEAMQQILSQKHR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 239 PSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKASELLLKQINKEEIENHEL 318
Cdd:PRK10703 240 PTAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRIVNKREEPQTI 319
|
330
....*....|....*.
gi 1816548106 319 TFPCELIIRDSSKELN 334
Cdd:PRK10703 320 EVHPRLVERRSVADGP 335
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
64-329 |
4.91e-60 |
|
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: 193.93 E-value: 4.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTG-----ENFDLYKRMM 138
Cdd:cd01541 1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEPTKsalpnPNLDLYEELQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 139 KEGYPIVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATepLTISTR-VERQEGYKKALQDNGIEIRQPFM 217
Cdd:cd01541 81 KKGIPVVFINSYYPELDAPSVSLDDEKGGYLATKHLIDLGHRRIAGIF--KSDDLQgVERYQGFIKALREAGLPIDDDRI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 218 I-----SANIKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQP 292
Cdd:cd01541 159 LwysteDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEPPLTSVVHP 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 1816548106 293 SYHMGEKASELLLKQINKEEiENHELTFPCELIIRDS 329
Cdd:cd01541 239 KEELGRKAAELLLRMIEEGR-KPESVIFPPELIERES 274
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
64-329 |
6.07e-60 |
|
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: 193.24 E-value: 6.07e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRM-MKEGY 142
Cdd:cd06275 1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAELLaALRSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 143 PIVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMISANI 222
Cdd:cd06275 81 PVVVLDREIAGDNADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSVSRERLAGFRRALAEAGIEVPPSWIVEGDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 223 KKIKKEL--EELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKA 300
Cdd:cd06275 161 EPEGGYEamQRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQPKDELGELA 240
|
250 260
....*....|....*....|....*....
gi 1816548106 301 SELLLKQINKEEIENHELTFPCELIIRDS 329
Cdd:cd06275 241 VELLLDRIENKREEPQSIVLEPELIERES 269
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
64-329 |
1.47e-58 |
|
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: 189.68 E-value: 1.47e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANI-MHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGlIIFPTGENFDLYKRMMKEGY 142
Cdd:cd06288 1 TIGLITDDIaTTPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDG-IIYASMHHREVTLPPELTDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 143 PIVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIA-IATEPLTISTRvERQEGYKKALQDNGIEIRQPFMISAN 221
Cdd:cd06288 80 PLVLLNCFDDDPSLPSVVPDDEQGGYLATRHLIEAGHRRIAfIGGPEDSLATR-LRLAGYRAALAEAGIPYDPSLVVHGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 222 --IKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEK 299
Cdd:cd06288 159 wgRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVALPYYEMGRR 238
|
250 260 270
....*....|....*....|....*....|
gi 1816548106 300 ASELLLKQINKEEIENHELTFPCELIIRDS 329
Cdd:cd06288 239 AAELLLDGIEGEPPEPGVIRVPCPLIERES 268
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
6-329 |
3.61e-58 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 190.68 E-value: 3.61e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 6 MADVAKKAGVSKSTVSQFLNKRyEYMREDTRKRIEAAIEELHYQPNYLARSLKQKRTSTVGIIVANIMHRFSTEVSRSIE 85
Cdd:PRK10423 1 MKDVARLAGVSTSTVSHVINKD-RFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 86 DFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTgENFDLYKRMMKE--GYPIVFMDRKVPDLIAPSVVSNN 163
Cdd:PRK10423 80 RSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCT-ETHQPSREIMQRypSVPTVMMDWAPFDGDSDLIQDNS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 164 IEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMISANIKKIK--KELEELFALDDPPSA 241
Cdd:PRK10423 159 LLGGDLATQYLIDKGYTRIACITGPLDKTPARLRLEGYRAAMKRAGLNIPDGYEVTGDFEFNGgfDAMQQLLALPLRPQA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 242 ILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKASELLLKQINKEEIENHELTFP 321
Cdd:PRK10423 239 VFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQRLQLT 318
|
....*...
gi 1816548106 322 CELIIRDS 329
Cdd:PRK10423 319 PELMERGS 326
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
64-329 |
9.66e-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: 380516 [Multi-domain] Cd Length: 270 Bit Score: 182.47 E-value: 9.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMMKEGYP 143
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSHLARLRARGTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 144 IVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGI----EIRQPFMIS 219
Cdd:cd06293 81 VVLLDRPAPGPAGCSVSVDDVQGGALAVDHLLELGHRRIAFVSGPLRTRQVAERLAGARAAVAEAGLdpdeVVRELSAPD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 220 ANIKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEK 299
Cdd:cd06293 161 ANAELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQPSYELGRA 240
|
250 260 270
....*....|....*....|....*....|
gi 1816548106 300 ASELLLKQINKEEIENHELTFPCELIIRDS 329
Cdd:cd06293 241 AADLLLDEIEGPGHPHEHVVFQPELVVRSS 270
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
64-328 |
1.00e-55 |
|
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: 182.38 E-value: 1.00e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPT-GENFDLYKRMMKEGY 142
Cdd:cd06289 1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPAaGTTAELLRRLKAWGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 143 PIVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMISANI 222
Cdd:cd06289 81 PVVLALRDVPGSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSSTRRERLAGFRAALAEAGLPLDESLIVPGPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 223 KKI--KKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKA 300
Cdd:cd06289 161 TREagAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHPREIGRRA 240
|
250 260
....*....|....*....|....*...
gi 1816548106 301 SELLLKQINKEEIENHELTFPCELIIRD 328
Cdd:cd06289 241 ARLLLRRIEGPDTPPERIIIEPRLVVRE 268
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
64-328 |
1.80e-55 |
|
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: 181.95 E-value: 1.80e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMMKEGYP 143
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEELILIAEKIPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 144 IVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMISA--N 221
Cdd:cd06270 81 LVVINRYIPGLADRCVWLDNEQGGRLAAEHLLDLGHRRIACITGPLDIPDARERLAGYRDALAEAGIPLDPSLIIEGdfT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 222 IKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKAS 301
Cdd:cd06270 161 IEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHYPIEEMAQAAA 240
|
250 260
....*....|....*....|....*..
gi 1816548106 302 ELLLKQINKEEiENHELTFPCELIIRD 328
Cdd:cd06270 241 ELALNLAYGEP-LPISHEFTPTLIERD 266
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
64-329 |
4.06e-55 |
|
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: 180.89 E-value: 4.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFpTGENFDLYKRMMKEGYP 143
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVV-GGFGDEELLKLLAEGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 144 IVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMISAN-- 221
Cdd:cd06290 80 VVLVDRELEGLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDHPDAQERYAGYRRALEDAGLEVDPRLIVEGDft 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 222 IKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKAS 301
Cdd:cd06290 160 EESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYEMGKTAA 239
|
250 260
....*....|....*....|....*...
gi 1816548106 302 ELLLKQINKEEIENHELTFPCELIIRDS 329
Cdd:cd06290 240 EILLELIEGKGRPPRRIILPTELVIRES 267
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
64-330 |
1.10e-53 |
|
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: 177.46 E-value: 1.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHR----FSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMMK 139
Cdd:cd06292 1 LIGYVVPELPGGfsdpFFDEFLAALGHAAAARGYDVLLFTASGDEDEIDYYRDLVRSRRVDGFVLASTRHDDPRVRYLHE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 140 EGYPIVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMIS 219
Cdd:cd06292 81 AGVPFVAFGRANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPEGSVPSDDRLAGYRAALEEAGLPFDPGLVVE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 220 A--NIKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMG 297
Cdd:cd06292 161 GenTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTVRQPIDEIG 240
|
250 260 270
....*....|....*....|....*....|...
gi 1816548106 298 EKASELLLKQINKEEIENHELTFPCELIIRDSS 330
Cdd:cd06292 241 RAVVDLLLAAIEGNPSEPREILLQPELVVRESS 273
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
35-330 |
1.01e-51 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 173.26 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 35 TRKRIEAAIEELHYQPNYLARSLKQKRTSTVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEML 114
Cdd:PRK11041 8 TRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTFVNLI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 115 RAKQVDGLIIFPTGENFDLYKRMMKEGYPIVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTR 194
Cdd:PRK11041 88 ITKQIDGMLLLGSRLPFDASKEEQRNLPPMVMANEFAPELELPTVHIDNLTAAFEAVNYLHELGHKRIACIAGPEEMPLC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 195 VERQEGYKKALQDNGIEIRQPFMISANI--KKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAV 272
Cdd:PRK11041 168 HYRLQGYVQALRRCGITVDPQYIARGDFtfEAGAKALKQLLDLPQPPTAVFCHSDVMALGALSQAKRMGLRVPQDLSIIG 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1816548106 273 FDNIPFAHLVHPPVTTIAQPSYHMGEKASELLLKQINKEEIENHELTFPCELIIRDSS 330
Cdd:PRK11041 248 FDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSSGSRLLDCELIIRGST 305
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
64-327 |
1.96e-51 |
|
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: 171.19 E-value: 1.96e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMMKEGyP 143
Cdd:cd06286 1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLIITSRENDWEVIEPYAKYG-P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 144 IVFMDRKVPDLIaPSVVSNNIEATKTTIEHFMENGHKQIAIAT--EPLTISTRVERQEGYKKALQDNGIEIRQPFMIS-- 219
Cdd:cd06286 80 IVLCEETDSPDI-PSVYIDRYEAYLEALEYLKEKGHRKIGYCLgrPESSSASTQARLKAYQDVLGEHGLSLREEWIFTnc 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 220 ANIKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLvhPPVTTIAQPSYHMGEK 299
Cdd:cd06286 159 HTIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISEL--LNLTTIDQPLEEMGKE 236
|
250 260
....*....|....*....|....*...
gi 1816548106 300 ASELLLKQINKEEIENHELTFpcELIIR 327
Cdd:cd06286 237 AFELLLSQLESKEPTKKELPS--KLIER 262
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
64-329 |
8.93e-49 |
|
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: 164.39 E-value: 8.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGlIIFPTGE-NFDLYKRMMKEGY 142
Cdd:cd06298 1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDG-IIFMGDElTEEIREEFKRSPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 143 PIVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTIST-RVERQEGYKKALQDNGIEIRQPFMISAN 221
Cdd:cd06298 80 PVVLAGTVDSDHEIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSGPLKEYInNDKKLQGYKRALEEAGLEFNEPLIFEGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 222 IK-KIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKA 300
Cdd:cd06298 160 YDyDSGYELYEELLESGEPDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPLYDIGAVA 239
|
250 260
....*....|....*....|....*....
gi 1816548106 301 SELLLKQINKEEIENHELTFPCELIIRDS 329
Cdd:cd06298 240 MRLLTKLMNKEEVEETIVKLPHSIIWRQS 268
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
64-325 |
5.56e-48 |
|
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: 162.28 E-value: 5.56e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTgENFDLYKRMMKE-GY 142
Cdd:cd01542 1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFAT-EITDEHRKALKKlKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 143 PIVFMDRKVPDLiaPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLT-ISTRVERQEGYKKALQDNGIEIRQ----PFM 217
Cdd:cd01542 80 PVVVLGQEHEGF--SCVYHDDYGAGKLLGEYLLKKGHKNIAYIGVDEEdIAVGVARKQGYLDALKEHGIDEVEivetDFS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 218 ISANIKKIKKELEElfaldDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMG 297
Cdd:cd01542 158 MESGYEAAKELLKE-----NKPDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEAG 232
|
250 260
....*....|....*....|....*...
gi 1816548106 298 EKASELLLKQINKEEIENHELtFPCELI 325
Cdd:cd01542 233 EKAAELLLDMIEGEKVPKKQK-LPYELI 259
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
64-329 |
2.41e-44 |
|
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: 153.16 E-value: 2.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENF-DLYKRMMKEGY 142
Cdd:cd06281 1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILTPGDEDDpELAAALARLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 143 PIVFMDRKVPDLIaPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMISAN- 221
Cdd:cd06281 81 PVVLIDRDLPGDI-DSVLVDHRSGVRQATEYLLSLGHRRIALLTGGPDIRPGRERIAGFKAAFAAAGLPPDPDLVRLGSf 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 222 -IKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKA 300
Cdd:cd06281 160 sADSGFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDLDAVGRAA 239
|
250 260 270
....*....|....*....|....*....|
gi 1816548106 301 SELLLKQINKEEI-ENHELTFPCELIIRDS 329
Cdd:cd06281 240 AELLLDRIEGPPAgPPRRIVVPTELILRDS 269
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
64-324 |
7.88e-44 |
|
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: 151.67 E-value: 7.88e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMMKE-GY 142
Cdd:cd06282 1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTVGDAQGSEALELLEEeGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 143 PIVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTR-VERQEGYKKALQDNGIEIRQPFMISAN 221
Cdd:cd06282 81 PYVLLFNQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAGDFSASDRaRLRYQGYRDALKEAGLKPIPIVEVDFP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 222 IKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKAS 301
Cdd:cd06282 161 TNGLEEALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQPSRDMGRAAA 240
|
250 260
....*....|....*....|...
gi 1816548106 302 ELLLKQInKEEIENHELTFPCEL 324
Cdd:cd06282 241 DLLLAEI-EGESPPTSIRLPHHL 262
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
64-325 |
2.61e-43 |
|
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: 150.43 E-value: 2.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFST-----EVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMM 138
Cdd:cd06294 1 TIGLVLPSSAEELFQnpffsEVLRGISQVANENGYSLLLATGNTEEELLEEVKRMVRGRRVDGFILLYSKEDDPLIEYLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 139 KEGYPIVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQP--F 216
Cdd:cd06294 81 EEGFPFVVIGKPLDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVSIDRLQGYKQALKEAGLPLDDDyiL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 217 MISANIKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHM 296
Cdd:cd06294 161 LLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSVDINPYEL 240
|
250 260
....*....|....*....|....*....
gi 1816548106 297 GEKASELLLKQINKEEIENHELTFPCELI 325
Cdd:cd06294 241 GREAAKLLINLLEGPESLPKNVIVPHELI 269
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
64-329 |
5.86e-42 |
|
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: 146.89 E-value: 5.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHR-FSTEVSrSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIfpTGENFD--LYKRMMKE 140
Cdd:cd06273 1 TIGAIVPTLDNAiFARAIQ-ALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLIL--VGSDHDpeLFELLEQR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 141 GYPIVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRV-ERQEGYKKALQDNGIEIRQPFMIS 219
Cdd:cd06273 78 QVPYVLTWSYDEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGNDRArARLAGIRDALAERGLELPEERVVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 220 A--NIKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMG 297
Cdd:cd06273 158 ApySIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPAREIG 237
|
250 260 270
....*....|....*....|....*....|...
gi 1816548106 298 EKASELLLKQI-NKEEIENHELtfPCELIIRDS 329
Cdd:cd06273 238 ELAARYLLALLeGGPPPKSVEL--ETELIVRES 268
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
103-329 |
1.56e-40 |
|
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: 143.08 E-value: 1.56e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 103 DPEKEKKYIEMLRAKQVDGLIIF-PTGENFDLYKRMMKEGYPIVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQ 181
Cdd:cd01545 41 DEDLADRLRRFLSRSRPDGVILTpPLSDDPALLDALDELGIPYVRIAPGTDDDRSPSVRIDDRAAAREMTRHLIALGHRR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 182 IAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMI-------SAnikkiKKELEELFALDDPPSAILAGNDLVFLEVL 254
Cdd:cd01545 121 IGFIAGPPDHGASAERLEGFRDALAEAGLPLDPDLVVqgdftfeSG-----LEAAEALLDLPDRPTAIFASNDEMAAGVL 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816548106 255 EFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKASELLLKQINKEEIENHELTFPCELIIRDS 329
Cdd:cd01545 196 AAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTTVRQPIAEMARRAVELLIAAIRGAPAGPERETLPHELVIRES 270
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
4-330 |
4.24e-40 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 143.98 E-value: 4.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 4 ITMADVAKKAGVSKSTVSQFLNKRyEYMREDTRKRIEAAIEELHYQPNYLARSLKQKRTSTVGIIVANI-MHRFStEVSR 82
Cdd:PRK09526 6 VTLYDVARYAGVSYQTVSRVLNQA-SHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTSLaLHAPS-QIAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 83 SIEDFFNKHDIHTIVCN-ADNDPEKEKKYIEMLRAKQVDGLII-FPTGENFDLYKRMMKEGYPIVFMDRKvPDLIAPSVV 160
Cdd:PRK09526 84 AIKSRADQLGYSVVISMvERSGVEACQAAVNELLAQRVSGVIInVPLEDADAEKIVADCADVPCLFLDVS-PQSPVNSVS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 161 SNNIEATKTTIEHFMENGHKQIAIATEPLT-ISTRVeRQEGYKKALQDNGIEI--------------RQPFmisanikki 225
Cdd:PRK09526 163 FDPEDGTRLGVEHLVELGHQRIALLAGPESsVSARL-RLAGWLEYLTDYQLQPiavregdwsamsgyQQTL--------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 226 kkeleELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKASELLL 305
Cdd:PRK09526 233 -----QMLREGPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLL 307
|
330 340
....*....|....*....|....*
gi 1816548106 306 KQINKEEIENHELtFPCELIIRDSS 330
Cdd:PRK09526 308 ALSQGQAVKGSQL-LPTSLVVRKST 331
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
64-329 |
3.10e-38 |
|
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: 136.91 E-value: 3.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANI----MHrFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFptGENFDLYKRMMK 139
Cdd:cd19974 1 NIAVLIPERffgdNS-FYGKIYQGIEKELSELGYNLVLEIISDEDEEELNLPSIISEEKVDGIIIL--GEISKEYLEKLK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 140 E-GYPIVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMI 218
Cdd:cd19974 78 ElGIPVVLVDHYDEELNADSVLSDNYYGAYKLTSYLIEKGHKKIGFVGDINYTSSFMDRYLGYRKALLEAGLPPEKEEWL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 219 SANIKKIKKELEELFALDD--PPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHM 296
Cdd:cd19974 158 LEDRDDGYGLTEEIELPLKlmLPTAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLTTVEVDKEAM 237
|
250 260 270
....*....|....*....|....*....|....*
gi 1816548106 297 GEKASELLLKQINKEE--IENHELtfPCELIIRDS 329
Cdd:cd19974 238 GRRAVEQLLWRIENPDrpFEKILV--SGKLIERDS 270
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
64-329 |
3.29e-37 |
|
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: 134.16 E-value: 3.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMMKEGYP 143
Cdd:cd01575 1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEHTPATRKLLRAAGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 144 IV-FMDRKvPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRV-ERQEGYKKALQDNGIEIRQPFMIS-- 219
Cdd:cd01575 81 VVeTWDLP-DDPIDMAVGFSNFAAGRAMARHLIERGYRRIAFVGARLDGDSRArQRLEGFRDALAEAGLPLPLVLLVElp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 220 ANIKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEK 299
Cdd:cd01575 160 SSFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVRVPRYEIGRK 239
|
250 260 270
....*....|....*....|....*....|
gi 1816548106 300 ASELLLKQINKEEIENHELTFPCELIIRDS 329
Cdd:cd01575 240 AAELLLARLEGEEPEPRVVDLGFELVRRES 269
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
76-329 |
5.64e-36 |
|
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: 131.21 E-value: 5.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 76 FSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKkYIEMLRAKQVDGLIIFPTGENFDLYKRMMKEGYPIVFMDRKVPDLI 155
Cdd:cd06277 20 FFSELIDGIEREARKYGYNLLISSVDIGDDFDE-ILKELTDDQSSGIILLGTELEEKQIKLFQDVSIPVVVVDNYFEDLN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 156 APSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQP--FMISANIKKIKKELEELF 233
Cdd:cd06277 99 FDCVVIDNEDGAYEAVKYLVELGHTRIGYLASSYRIKNFEERRRGFRKAMRELGLSEDPEpeFVVSVGPEGAYKDMKALL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 234 A-LDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKASELLLKQINKEE 312
Cdd:cd06277 179 DtGPKLPTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRRLIEKIKDPD 258
|
250
....*....|....*..
gi 1816548106 313 IENHELTFPCELIIRDS 329
Cdd:cd06277 259 GGTLKILVSTKLVERGS 275
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
64-325 |
2.45e-35 |
|
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: 129.25 E-value: 2.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMMKEGYP 143
Cdd:cd06274 1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAPSTPPDDIYYLCQAAGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 144 IVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIA-IATEPlTISTRVERQEGYKKALQDNGIEIRQPFMISANI 222
Cdd:cd06274 81 VVFLDRPFSGSDAPSVVSDNRAGARALTEKLLAAGPGEIYfLGGRP-ELPSTAERIRGFRAALAEAGITEGDDWILAEGY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 223 KKI--KKELEELFA-LDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEK 299
Cdd:cd06274 160 DREsgYQLMAELLArLGGLPQALFTSSLTLLEGVLRFLRERLGAIPSDLVLGTFDDHPLLDFLPNPVDSVRQDHDEIAEH 239
|
250 260
....*....|....*....|....*.
gi 1816548106 300 ASELLLKQINKEEiENHELTFPCELI 325
Cdd:cd06274 240 AFELLDALIEGQP-EPGVIIIPPELI 264
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
64-329 |
3.03e-35 |
|
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: 129.19 E-value: 3.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEkEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMMKEGYP 143
Cdd:cd06278 1 LVGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDD-VDDALRQLLQYRVDGVIVTSATLSSELAEECARRGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 144 IVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIrqPFMISA--N 221
Cdd:cd06278 80 VVLFNRVVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPEGTSTSRERERGFRAALAELGLPP--PAVEAGdyS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 222 IKKIKKELEELFALDDPPSAILAGNDLV---FLEVLefAKEHKLKVGKDFALAVFDNIPFAHlvHPPV--TTIAQPSYHM 296
Cdd:cd06278 158 YEGGYEAARRLLAAPDRPDAIFCANDLMalgALDAA--RQEGGLVVPEDISVVGFDDIPMAA--WPSYdlTTVRQPIEEM 233
|
250 260 270
....*....|....*....|....*....|...
gi 1816548106 297 GEKASELLLKQINKEEIENHELTFPCELIIRDS 329
Cdd:cd06278 234 AEAAVDLLLERIENPETPPERRVLPGELVERGS 266
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
3-328 |
3.62e-35 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 130.99 E-value: 3.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 3 KITMADVAKKAGVSKSTVSQFLNKRYEyMREDTRKRIEAAIEELHYQPNYLARSLKQKRTSTVGIIVANIMHRFSTEVSR 82
Cdd:PRK10014 6 KITIHDVALAAGVSVSTVSLVLSGKGR-ISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAELTA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 83 SIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFP-TGENFDLYKRMMKEGYPIVFMDRKV----PDLIAP 157
Cdd:PRK10014 85 GLTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGaAGSSDDLREMAEEKGIPVVFASRASylddVDTVRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 158 svvsNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMI--SANIKKIKKELEELFAL 235
Cdd:PRK10014 165 ----DNMQAAQLLTEHLIRNGHQRIAWLGGQSSSLTRAERVGGYCATLLKFGLPFHSEWVLecTSSQKQAAEAITALLRH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 236 DDPPSAILAGNDLVFLEV---LEFAKEHKLKVGKD------FALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKASELLLK 306
Cdd:PRK10014 241 NPTISAVVCYNETIAMGAwfgLLRAGRQSGESGVDryfeqqVALAAFTDVPEAELDDPPLTWASTPAREIGRTLADRMMQ 320
|
330 340
....*....|....*....|..
gi 1816548106 307 QINKEEIENHELTFPCELIIRD 328
Cdd:PRK10014 321 RITHEETHSRNLIIPPRLIARK 342
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
92-330 |
4.65e-34 |
|
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: 126.24 E-value: 4.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 92 DIHTIVCNADNDPEKEkkYIEMLRAKQVDGLIIFPTGENFDLYKRMMKEGYPIVFMD-RKVPDLIAPSVVSNNIEATKTT 170
Cdd:cd06296 31 DLVVTATRAGRAPVDD--WVRRAVARGSAGVVLVTSDPTSRQLRLLRSAGIPFVLIDpVGEPDPDLPSVGATNWAGGRLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 171 IEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIrQPFMISA---NIKKIKKELEELFALDDPPSAILAGND 247
Cdd:cd06296 109 TEHLLDLGHRRIAVITGPPRSVSGRARLAGYRAALAEAGIAV-DPDLVREgdfTYEAGYRAARELLELPDPPTAVFAGND 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 248 LVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKASELLLKQINKEEIENHELTFPCELIIR 327
Cdd:cd06296 188 EQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVHQPLREMGAVAVRLLLRLLEGGPPDARRIELATELVVR 267
|
...
gi 1816548106 328 DSS 330
Cdd:cd06296 268 GST 270
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
119-329 |
6.07e-34 |
|
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: 126.17 E-value: 6.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 119 VDGLIIFPTGENFDLYKRMMKEGYPIVFMDRKVPDLIaPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRV--- 195
Cdd:cd06279 57 VDGFIVYGLSDDDPAVAALRRRGLPLVVVDGPAPPGI-PSVGIDDRAAARAAARHLLDLGHRRIAILSLRLDRGRERgpv 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 196 --------------ERQEGYKKALQDNGIEIRQPFMISA---NIKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAK 258
Cdd:cd06279 136 saerlaaatnsvarERLAGYRDALEEAGLDLDDVPVVEApgnTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAAR 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1816548106 259 EHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKASELLLKQINKEeiENHELTFPCELIIRDS 329
Cdd:cd06279 216 ERGLRVPEDLSVTGFDDIPEAAAADPGLTTVRQPAVEKGRAAARLLLGLLPGA--PPRPVILPTELVVRAS 284
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
4-306 |
1.80e-32 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 123.73 E-value: 1.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 4 ITMADVAKKAGVSKSTVSQFLNKRyEYMREDTRKRIEAAIEELHYQPNYLARSLKQKRTSTVGIIVANIMHRFSTEVSRS 83
Cdd:PRK10401 2 ITIRDVARQAGVSVATVSRVLNNS-ALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 84 IEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMMKEGYPIVFMDRKVPDLIAPSVVSNN 163
Cdd:PRK10401 81 VDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDQIPGMVLINRVVPGYAHRCVCLDN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 164 IEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMISA--NIKKIKKELEELFALDDPPSA 241
Cdd:PRK10401 161 VSGARMATRMLLNNGHQRIGYLSSSHGIEDDAMRRAGWMSALKEQGIIPPESWIGTGtpDMQGGEAAMVELLGRNLQLTA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816548106 242 ILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKASELLLK 306
Cdd:PRK10401 241 VFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATELALQ 305
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
64-325 |
1.20e-31 |
|
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: 119.58 E-value: 1.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIV---ANIMHR-FSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMMK 139
Cdd:cd20010 1 AIGLVLpldPGDLGDpFFLEFLAGLSEALAERGLDLLLAPAPSGEDELATYRRLVERGRVDGFILARTRVNDPRIAYLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 140 EGYPIVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMIS 219
Cdd:cd20010 81 RGIPFVVHGRSESGAPYAWVDIDNEGAFRRATRRLLALGHRRIALLNGPEELNFAHQRRDGYRAALAEAGLPVDPALVRE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 220 AnikkikkELEE---------LFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPF-AHLVHPPVTTI 289
Cdd:cd20010 161 G-------PLTEeggyqaarrLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLLPaLEYFSPPLTTT 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 1816548106 290 AQPSYHMGEKASELLLKQINKEEIENHELTFPCELI 325
Cdd:cd20010 234 RSSLRDAGRRLAEMLLALIDGEPAAELQELWPPELI 269
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
82-329 |
5.18e-31 |
|
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: 118.01 E-value: 5.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 82 RSIEDFFNKHDIHTIVCNADNDPEKEkkyiemlRAKQVDGLII---FPTGENFDLYKRMMkegyPIVFMDRKVPDLIAPS 158
Cdd:cd01544 24 LGIEKEAKKLGYEIKTIFRDDEDLES-------LLEKVDGIIAigkFSKEEIEKLKKLNP----NIVFVDSNPDPDGFDS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 159 VVSNNIEATKTTIEHFMENGHKQIAI--ATEPLTISTRVE---RQEGYKKALQDNGIeIRQPFMISANI------KKIKK 227
Cdd:cd01544 93 VVPDFEQAVRQALDYLIELGHRRIGFigGKEYTSDDGEEIedpRLRAFREYMKEKGL-YNEEYIYIGEFsvesgyEAMKE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 228 ELEELfaldDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKASELLLKQ 307
Cdd:cd01544 172 LLKEG----DLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTPPLTTVHIPTEEMGRTAVRLLLER 247
|
250 260
....*....|....*....|..
gi 1816548106 308 INKEEIENHELTFPCELIIRDS 329
Cdd:cd01544 248 INGGRTIPKKVLLPTKLIERES 269
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
65-321 |
6.21e-31 |
|
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: 117.73 E-value: 6.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 65 VGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIfptgeNFDLYKR---MMKEG 141
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAI-----NLVDPAAagvAEKAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 142 Y---PIVFMDrKVPDLIAP--SVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPF 216
Cdd:cd01537 77 GqnvPVVFFD-KEPSRYDKayYVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKTEQLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 217 MISANIKKI--KKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSY 294
Cdd:cd01537 156 LDTGDWDTAsgKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDAN 235
|
250 260
....*....|....*....|....*..
gi 1816548106 295 HMGEKASELLLKQINKEEIENHELTFP 321
Cdd:cd01537 236 NLGKTTFDLLLNLADNWKIDNKVVRVP 262
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
64-329 |
2.57e-30 |
|
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: 115.76 E-value: 2.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADN-DPEKEKKYIEMLRAKQVDGLIIF-PTGENFDLyKRMMKEG 141
Cdd:cd01574 1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATVDEdDPASVREALDRLLSQRVDGIIVIaPDEAVLEA-LRRLPPG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 142 YPIVFMDRkVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPF----M 217
Cdd:cd01574 80 LPVVIVGS-GPSPGVPTVSIDQEEGARLATRHLLELGHRRIAHIAGPLDWVDARARLRGWREALEEAGLPPPPVVegdwS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 218 ISANIKKIKkeleeLFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMG 297
Cdd:cd01574 159 AASGYRAGR-----RLLDDGPVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDFAELG 233
|
250 260 270
....*....|....*....|....*....|..
gi 1816548106 298 EKASELLLKQINKEEIENHELTFPCELIIRDS 329
Cdd:cd01574 234 RRAVELLLALIEGPAPPPESVLLPPELVVRES 265
|
|
| HTH_LACI |
smart00354 |
helix_turn _helix lactose operon repressor; |
4-74 |
3.81e-30 |
|
helix_turn _helix lactose operon repressor;
Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 109.60 E-value: 3.81e-30
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1816548106 4 ITMADVAKKAGVSKSTVSQFLNKrYEYMREDTRKRIEAAIEELHYQPNYLARSLKQKRTSTVGIIVANIMH 74
Cdd:smart00354 1 ATIKDVARLAGVSKATVSRVLNG-KGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
173-330 |
1.03e-28 |
|
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: 108.58 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 173 HFMENGHKQIAIATE--PLTISTRVERQEGYKKALQDNGIEIrQPFMISANIKKIKKELEE-LFALDDPPSAILAGNDLV 249
Cdd:pfam13377 1 HLAELGHRRIALIGPegDRDDPYSDLRERGFREAARELGLDV-EPTLYAGDDEAEAAAARErLRWLGALPTAVFVANDEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 250 FLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKASELLLKQINKEEIENHELTFPCELIIRDS 329
Cdd:pfam13377 80 ALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVERES 159
|
.
gi 1816548106 330 S 330
Cdd:pfam13377 160 T 160
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
5-311 |
4.57e-28 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 111.51 E-value: 4.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 5 TMADVAKKAGVSKSTVSQFLNKRYEYMR--EDTRKRIEAAIEELHYQPNYLARSLKQKRTSTVGIIVANIMHRFSTEVSR 82
Cdd:PRK11303 2 KLDEIARLAGVSRTTASYVINGKAKQYRvsDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSYARIAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 83 SIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLII---FPTGENFdlYKRMMKEGYPIVFMDRKVPDLIAPSV 159
Cdd:PRK11303 82 YLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVstsLPPEHPF--YQRLQNDGLPIIALDRALDREHFTSV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 160 VSNNIEATKTTIEHFMENGHKQIAI--ATEPLTIStrVERQEGYKKALQDNGIEIRQPFMISANIKKIKKELEELFALDD 237
Cdd:PRK11303 160 VSDDQDDAEMLAESLLKFPAESILLlgALPELSVS--FEREQGFRQALKDDPREVHYLYANSFEREAGAQLFEKWLETHP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 238 PPSAILAgNDLVFLE-VLEFAKEHKLKVGKDFALAVF------DNIPFahlvhpPVTTIAQPSYHMGEKASELLLKQINK 310
Cdd:PRK11303 238 MPDALFT-TSYTLLQgVLDVLLERPGELPSDLAIATFgdnellDFLPC------PVNAVAQQHRLIAERALELALAALDE 310
|
.
gi 1816548106 311 E 311
Cdd:PRK11303 311 P 311
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
64-329 |
4.63e-28 |
|
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: 109.86 E-value: 4.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIfptgENFDLYKRMmKEGY- 142
Cdd:cd06297 1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLLSEYRLEKYLRNSTLAYQCDGLVM----ASLDLTELF-EEVIv 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 143 ----PIVFMDRKVPDLiaPSVVSNNIEATKTTIEHFMENGHKQIA-IATEPLTISTRV---ERQEGYKKALQDNG--IEI 212
Cdd:cd06297 76 ptekPVVLIDANSMGY--DCVYVDNVKGGFMATEYLAGLGEREYVfFGIEEDTVFTETvfrEREQGFLEALNKAGrpISS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 213 RQPFMISANIKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLvhPPVTTIAQP 292
Cdd:cd06297 154 SRMFRIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAAS--PGLTTVRQP 231
|
250 260 270
....*....|....*....|....*....|....*..
gi 1816548106 293 SYHMGEKASELLLKQINKEEIENHELTFPCELIIRDS 329
Cdd:cd06297 232 VEEMGEAAAKLLLKRLNEYGGPPRSLKFEPELIVRES 268
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
6-313 |
9.68e-28 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 110.50 E-value: 9.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 6 MADVAKKAGVSKSTVSQFLnKRYEYMREDTRKRIEAAIEELHYQPNYLARSLKQKRTSTVGIIVANIMHRFSTEVSRSIE 85
Cdd:PRK14987 8 LQDVADRVGVTKMTVSRFL-RNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGIE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 86 DFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMMKEGYPIV-FMDRKVPDLIApSVVSNNI 164
Cdd:PRK14987 87 SVTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIEVAGIPVVeLMDSQSPCLDI-AVGFDNF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 165 EATKTTIEHFMENGHKQIAIATEPLTISTrVERQEGYKKALQDNG-----IEIRQPFMISANIKKIKKELEELFALDdpp 239
Cdd:PRK14987 166 EAARQMTTAIIARGHRHIAYLGARLDERT-IIKQKGYEQAMLDAGlvpysVMVEQSSSYSSGIELIRQARREYPQLD--- 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1816548106 240 sAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKASELLLKQINKEEI 313
Cdd:PRK14987 242 -GVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARIRGESV 314
|
|
| PRK10727 |
PRK10727 |
HTH-type transcriptional regulator GalR; |
5-329 |
2.16e-26 |
|
HTH-type transcriptional regulator GalR;
Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 107.15 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 5 TMADVAKKAGVSKSTVSQFLNKRYEyMREDTRKRIEAAIEELHYQPNYLARSLKQKRTSTVGIIVANIMHRFSTEVSRSI 84
Cdd:PRK10727 3 TIKDVARLAGVSVATVSRVINNSPK-ASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 85 EDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLII----FPTGEnfdlYKRMMKEGYPIVFMDRKVPDLIAPSVV 160
Cdd:PRK10727 82 EQVAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVVhakmIPDAE----LASLMKQIPGMVLINRILPGFENRCIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 161 SNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMISANIKKIKKE--LEELFALDDP 238
Cdd:PRK10727 158 LDDRYGAWLATRHLIQQGHTRIGYLCSNHSISDAEDRLQGYYDALAESGIPANDRLVTFGEPDESGGEqaMTELLGRGRN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 239 PSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKASELLLKQINKEEIENHEL 318
Cdd:PRK10727 238 FTAVACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELALALADNRPLPEITN 317
|
330
....*....|.
gi 1816548106 319 TFPCELIIRDS 329
Cdd:PRK10727 318 VFSPTLVRRHS 328
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
60-329 |
7.04e-25 |
|
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: 101.56 E-value: 7.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 60 KRTSTVGIIVANIMHR-------FSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAkqvDGLIIFPTGENFD 132
Cdd:cd06295 1 QRSRTIAVVVPMDPHGdqsitdpFFLELLGGISEALTDRGYDMLLSTQDEDANQLARLLDSGRA---DGLIVLGQGLDHD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 133 LYKRMMKEGYPIVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRvERQEGYKKALQDNGIEI 212
Cdd:cd06295 78 ALRELAQQGLPMVVWGAPEDGQSYCSVGSDNVKGGALATEHLIEIGRRRIAFLGDPPHPEVA-DRLQGYRDALAEAGLEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 213 RQPFMISANIK--KIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIA 290
Cdd:cd06295 157 DPSLLLSCDFTeeSGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFRPPLTTVR 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 1816548106 291 QPSYHMGEKASELLLKQINKEEIENHELtfPCELIIRDS 329
Cdd:cd06295 237 QDLALAGRLLVEKLLALIAGEPVTSSML--PVELVVRES 273
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
62-327 |
9.48e-25 |
|
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: 101.43 E-value: 9.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 62 TSTVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMMKE- 140
Cdd:pfam00532 1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPAPSGDDITAKAEGy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 141 GYPIVFMDRK-VPDLIAPSVVSNNIEATKTTIEHFMENGHKQ-IAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMI 218
Cdd:pfam00532 81 GIPVIAADDAfDNPDGVPCVMPDDTQAGYESTQYLIAEGHKRpIAVMAGPASALTARERVQGFMAALAAAGREVKIYHVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 219 --SANIKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAK-----EHKLKVGKDF-ALAVFDNIPFA---HLVHPPVT 287
Cdd:pfam00532 161 tgDNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLkqgrvKIPDIVGIGInSVVGFDGLSKAqdtGLYLSPLT 240
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1816548106 288 TIAQPSYHMGEKASELLLKQINKEEIENHELTFPCELIIR 327
Cdd:pfam00532 241 VIQLPRQLLGIKASDMVYQWIPKFREHPRVLLIPRDFFKE 280
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
64-328 |
1.13e-24 |
|
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: 101.54 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENF--DLYKRMMKEG 141
Cdd:COG1879 35 TIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDAlaPALKKAKAAG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 142 YPIVFMDRKVP-DLIAPSVVSNNIEATKTTIEHFME--NGHKQIAIATEPLTISTRVERQEGYKKALQDN-GIEIRQPFM 217
Cdd:COG1879 115 IPVVTVDSDVDgSDRVAYVGSDNYAAGRLAAEYLAKalGGKGKVAILTGSPGAPAANERTDGFKEALKEYpGIKVVAEQY 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 218 ISANIKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKvgKDFALAVFDNIP--FAHLVHPPVT-TIAQPSY 294
Cdd:COG1879 195 ADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRK--GDVKVVGFDGSPeaLQAIKDGTIDaTVAQDPY 272
|
250 260 270
....*....|....*....|....*....|....
gi 1816548106 295 HMGEKASELLLKQINKEEIENHELTfPCELIIRD 328
Cdd:COG1879 273 LQGYLAVDAALKLLKGKEVPKEILT-PPVLVTKE 305
|
|
| HTH_LacI |
cd01392 |
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
7-59 |
4.89e-20 |
|
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: 82.07 E-value: 4.89e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1816548106 7 ADVAKKAGVSKSTVSQFLNKRyEYMREDTRKRIEAAIEELHYQPNYLARSLKQ 59
Cdd:cd01392 1 KDIARAAGVSVATVSRVLNGK-PRVSEETRERVLAAAEELGYRPNAAARSLRT 52
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
105-325 |
5.79e-20 |
|
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: 87.87 E-value: 5.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 105 EKEKKYIEMLRAKQVDGLIIFPTGENFDLYKRMMKEGYPIVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAI 184
Cdd:cd06271 44 ES*VPIRDLVETGSADGVILSEIEPNDPRVQFLTKQNFPFVAHGRSD*PIGHAWVDIDNEAGAYEAVERLAGLGHRRIAF 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 185 ATEPLTISTRVERQEGYKKALQDNGIEIRqPFMISANIKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKV 264
Cdd:cd06271 124 IVPPARYSPHDRRLQGYVRA*RDAGLTGY-PLDADTTLEAGRAAAQRLLALSPRPTAIVTMNDSATIGLVAGLQAAGLKI 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816548106 265 GKDFALAVFDNIPF-AHLVHPPVTTIAQPSYHMGEKASELLLKQINKEEIENHELTFPCELI 325
Cdd:cd06271 203 GEDVSIIGKDSAPFlGAMITPPLTTVHAPIAEAGRELAKALLARIDGEDPETLQVLVQPSLS 264
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
111-330 |
9.46e-20 |
|
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: 87.26 E-value: 9.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 111 IEMLRAKQVDGLIIFptGENFDLYKRMMKEGYPIVFMDRKVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLT 190
Cdd:cd01543 43 LDLLKGWKGDGIIAR--LDDPELAEALRRLGIPVVNVSGSRPEPGFPRVTTDNEAIGRMAAEHLLERGFRHFAFCGFRNA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 191 ISTRvERQEGYKKALQDNGIEIRQpFMI---------SANIKKIKKELEELfalddP-PSAILAGNDLVFLEVLEFAKEH 260
Cdd:cd01543 121 AWSR-ERGEGFREALREAGYECHV-YESppsgssrswEEEREELADWLKSL-----PkPVGIFACNDDRARQVLEACREA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816548106 261 KLKVGKDFA-LAVFDNIPFAHLVHPPVTTIAQPSYHMGEKASELLLKQINKEEIENHELTFPC-ELIIRDSS 330
Cdd:cd01543 194 GIRVPEEVAvLGVDNDELICELSSPPLSSIALDAEQIGYEAAELLDRLMRGERVPPEPILIPPlGVVTRQST 265
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
64-324 |
1.98e-17 |
|
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: 80.69 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENF--DLYKRMMKEG 141
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEAlvPAVKKANAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 142 YPIVFMDRKVPDL--IAPSVVSNNIEATKTTIEHFME--NGHKQIAIATEPLTISTRVERQEGYKKALQDN-GIEI--RQ 214
Cdd:cd01536 81 IPVVAVDTDIDGGgdVVAFVGTDNYEAGKLAGEYLAEalGGKGKVAILEGPPGSSTAIDRTKGFKEALKKYpDIEIvaEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 215 PfmisAN--IKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKvgKDFALAVFDNIPFAhlvhppVT----- 287
Cdd:cd01536 161 P----ANwdRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRT--GDIKIVGVDGTPEA------LKaikdg 228
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1816548106 288 ----TIAQPSYHMGEKASELLLKQINKEEIENHELTfPCEL 324
Cdd:cd01536 229 eldaTVAQDPYLQGYLAVEAAVKLLNGEKVPKEILT-PVTL 268
|
|
| LacI |
pfam00356 |
Bacterial regulatory proteins, lacI family; |
5-51 |
4.66e-17 |
|
Bacterial regulatory proteins, lacI family;
Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 73.83 E-value: 4.66e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1816548106 5 TMADVAKKAGVSKSTVSQFLNKRyEYMREDTRKRIEAAIEELHYQPN 51
Cdd:pfam00356 1 TIKDVARLAGVSKSTVSRVLNNP-GRVSEETRERVEAAMEELNYIPN 46
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
65-312 |
9.33e-17 |
|
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: 78.89 E-value: 9.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 65 VGIIVANIMHRFSTEVSRSIEDFFNK-HDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENF--DLYKRMMKEG 141
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKElGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTAlaPVLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 142 YPIVFMDR-KVPDLIAPSVVSNNIEATKTTIEHFME--NGHKQIAIATEPLTISTRVERQEGYKKALQDN--GIEI---R 213
Cdd:pfam13407 81 IPVVTFDSdAPSSPRLAYVGFDNEAAGEAAGELLAEalGGKGKVAILSGSPGDPNANERIDGFKKVLKEKypGIKVvaeV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 214 QPFMISANikKIKKELEELF-ALDDPPSAILAGNDLVFLEVLEFAKEHKLKvgKDFALAVFDNIPFA------HLVHppv 286
Cdd:pfam13407 161 EGTNWDPE--KAQQQMEALLtAYPNPLDGIISPNDGMAGGAAQALEAAGLA--GKVVVTGFDATPEAleaikdGTID--- 233
|
250 260
....*....|....*....|....*.
gi 1816548106 287 TTIAQPSYHMGEKASELLLKQINKEE 312
Cdd:pfam13407 234 ATVLQDPYGQGYAAVELAAALLKGKK 259
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
90-328 |
3.41e-16 |
|
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: 77.41 E-value: 3.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 90 KHDIHTIVCNADNDPEKEKKYIemLRAKQVDGLIIFPTGENFDLYKRMMKEGYPIVFMDRKVPDLiaPSVVSNNIEATKT 169
Cdd:cd06272 30 GYNINLSICPYKVGHLCTAKGL--FSENRFDGVIVFGISDSDIEYLNKNKPKIPIVLYNRESPKY--STVNVDNEKAGRL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 170 TIEHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIEIRQPFMISAN--IKKIKKELEELFALDDPPSAILAGND 247
Cdd:cd06272 106 AVLLLIQKGHKSIAYIGNPNSNRNQTLRGKGFIETCEKHGIHLSDSIIDSRGlsIEGGDNAAKKLLKKKTLPKAIFCNSD 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 248 LVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKASELLLKQINKEEIENHELTFPCELIIR 327
Cdd:cd06272 186 DIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLTVVGVPIEKIAEESLRLILKLIEGRENEIQQLILYPELIFR 265
|
.
gi 1816548106 328 D 328
Cdd:cd06272 266 E 266
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
172-314 |
1.22e-15 |
|
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: 75.65 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 172 EHFMENGHKQIAIATEPLTISTRVERQEGYKKALQDNGIE--IRQPFMISANIKKIKKELEELFALDDPPSAILAGNDLV 249
Cdd:cd20009 111 RRLAARGRRRIALVAPPRELTYAQHRLRGFRRALAEAGLEvePLLIVTLDSSAEAIRAAARRLLRQPPRPDGIICASEIA 190
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816548106 250 FLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKASELLLKQINKEEIE 314
Cdd:cd20009 191 ALGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPIDTLYEDIEEAGRFLAEALLRRIEGEPAE 255
|
|
| PRK10339 |
PRK10339 |
DNA-binding transcriptional repressor EbgR; Provisional |
5-331 |
1.36e-13 |
|
DNA-binding transcriptional repressor EbgR; Provisional
Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 70.56 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 5 TMADVAKKAGVSKSTVSQFLNKRYEY-MREDTRKRIEAAIEELHYQPN---YLARSLKQKRTstvgiIVANIMHRFSTEV 80
Cdd:PRK10339 3 TLKDIAIEAGVSLATVSRVLNDDPTLnVKEETKHRILEIAEKLEYKTSsarKLQTGAVNQHH-----ILAIYSYQQELEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 81 S--------RSIEDFFNKHDIHTIVC-NADNDPEkekkyiemlrAKQVDGLIIF--PTGENFDLYKRMMKegyPIVFMDR 149
Cdd:PRK10339 78 NdpyylairHGIETQCEKLGIELTNCyEHSGLPD----------IKNVTGILIVgkPTPALRAAASALTD---NICFIDF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 150 KVPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAI---ATEPLTISTRVERQEGY---KKALQDNGIeIRQPFMISANIK 223
Cdd:PRK10339 145 HEPGSGYDAVDIDLARISKEIIDFYINQGVNRIGFiggEDEPGKADIREVAFAEYgrlKQVVREEDI-WRGGFSSSSGYE 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 224 KIKKELEElfalDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIPFAHLVHPPVTTIAQPSYHMGEKASEL 303
Cdd:PRK10339 224 LAKQMLAR----EDYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNL 299
|
330 340
....*....|....*....|....*...
gi 1816548106 304 LLKQINKEEIENHELTFPCELIIRDSSK 331
Cdd:PRK10339 300 LYEKARDGRALPLLVFVPSKLKLRGTTR 327
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
64-313 |
6.56e-12 |
|
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: 64.77 E-value: 6.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDL--YKRMMKEG 141
Cdd:cd19972 1 TIGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAvpVKAARAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 142 YPIVFMDRKVPDliAPS---VVSNNIEATKTTIEHFME--NGHKQIAIATEPLTISTRVERQEGYKKAL----------- 205
Cdd:cd19972 81 IPVIAVDRNPED--APGdtfIATDSVAAAKELGEWVIKqtGGKGEIAILHGQLGTTPEVDRTKGFQEALaeapgikvvae 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 206 ------QDNGIEIRQPfMISANikkikkeleelfalddpPS--AILAGNDLVFLEVLEFAKE----HKL-KVGKDFALAV 272
Cdd:cd19972 159 qtadwdQDEGFKVAQD-MLQAN-----------------PNitVFFGQSDAMALGAAQAVKVagldHKIwVVGFDGDVAG 220
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1816548106 273 FDNIPFAHLvhppVTTIAQPSYHMGEKASELLLKQINKEEI 313
Cdd:cd19972 221 LKAVKDGVL----DATMTQQTQKMGRLAVDSAIDLLNGKAV 257
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
64-212 |
2.51e-09 |
|
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: 57.24 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFF-NKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFP--TGENFDLYKRMMKE 140
Cdd:cd06301 2 KIGVSMQNFSDEFLTYLRDAIEAYAkEYPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPvdTDASAPAVDAAADA 81
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816548106 141 GYPIVFMDRKVPDLIAPSVV--SNNIEATKTTIEHFME--NGHKQIAIATEPLTISTRVERQEGYKKALQDN-GIEI 212
Cdd:cd06301 82 GIPLVYVNREPDSKPKGVAFvgSDDIESGELQMEYLAKllGGKGNIAILDGVLGHEAQILRTEGNKDVLAKYpGMKI 158
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
100-328 |
5.42e-09 |
|
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: 56.21 E-value: 5.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 100 ADNDPEKEKKYIEMLRAKQVDGLIIFPT-----GENFDLYKRmmkEGYPIVfmdrkVPDLIAPS------VVSNNIE--- 165
Cdd:cd06319 37 QKNSANEQVTNANDLIAQGVDGIIISPTnssaaPTVLDLANE---AKIPVV-----IADIGTGGgdyvsyIISDNYDggy 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 166 -ATKTTIEHFMENG--HKQIAIATEPLTISTRVERQEGYKKALQDNGIE---IRQpfMISANIKKIKKELEELFALDDPP 239
Cdd:cd06319 109 qAGEYLAEALKENGwgGGSVGIIAIPQSRVNGQARTAGFEDALEEAGVEevaLRQ--TPNSTVEETYSAAQDLLAANPDI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 240 SAILAGNDLVFLEVLEFAKEhkLKVGKDFALAVFDNIP-FAHLVHPP--VTTIAQPSYHMGEKASELLLKQINKEEIENH 316
Cdd:cd06319 187 KGIFAQNDQMAQGALQAIEE--AGRTGDILVVGFDGDPeALDLIKDGklDGTVAQQPFGMGARAVELAIQALNGDNTVEK 264
|
250
....*....|..
gi 1816548106 317 ELTFPCELIIRD 328
Cdd:cd06319 265 EIYLPVLLVTSE 276
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
64-314 |
5.73e-09 |
|
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: 56.23 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENfdLYKRMMKE--- 140
Cdd:cd06317 1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVN--GSIPAIKRase 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 141 -GYPIVFMDRKVP-DLIAPSVVSNNIEATKTTIEHFME------NGHKQIAI-ATEPLTIStrVERQEGYKKALQDN-GI 210
Cdd:cd06317 79 aGIPVIAYDAVIPsDFQAAQVGVDNLEGGKEIGKYAADyikaelGGQAKIGVvGALSSLIQ--NQRQKGFEEALKANpGV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 211 EI--------RQPFMISA--NIKKIKKELEELFALDDPP--SAILAGNDLvflevlefAKEHKLKV-GKD-----FALAV 272
Cdd:cd06317 157 EIvatvdgqnVQEKALSAaeNLLTANPDLDAIYATGEPAllGAVAAVRSQ--------GRQGKIKVfGWDltkqaIFLGI 228
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1816548106 273 FDNIPFAhlvhppvtTIAQPSYHMGEKASELLLKQINKEEIE 314
Cdd:cd06317 229 DEGVLQA--------VVQQDPEKMGYEAVKAAVKAIKGEDVE 262
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
64-314 |
5.99e-09 |
|
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: 56.02 E-value: 5.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKH-DIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFP-TGENF-DLYKRMMKE 140
Cdd:cd06308 1 VIGFSQCSLNDPWRAAMNEEIKAEAAKYpNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPnEADALtPVVKKAYDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 141 GYPIVFMDRKVP-DLIAPSVVSNNIEATKTTIEHFME--NGHKQIAIATEPLTISTRVERQEGYKKALQDN-GIEIRQPf 216
Cdd:cd06308 81 GIPVIVLDRKVSgDDYTAFIGADNVEIGRQAGEYIAEllNGKGNVVEIQGLPGSSPAIDRHKGFLEAIAKYpGIKIVAS- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 217 mISANIKKIK--KELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLK-----VGKD-----FALAVFDNIPFAHLVHP 284
Cdd:cd06308 160 -QDGDWLRDKaiKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGREkeikiIGVDglpeaGEKAVKDGILAATFLYP 238
|
250 260 270
....*....|....*....|....*....|
gi 1816548106 285 PvttiaqpsyhMGEKASELLLKQINKEEIE 314
Cdd:cd06308 239 T----------GGKEAIEAALKILNGEKVP 258
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
64-277 |
9.93e-09 |
|
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: 55.69 E-value: 9.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGEN--FDLYKRMMKEG 141
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATgwDPVLKEAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 142 YPIVFMDRKVPD----LIAPSVVSNNIEATKT----TIEHFmENGHKQIAIATEPLTISTRVERQEGYKKALQDNG---I 210
Cdd:cd06309 81 IPVILVDRTIDGedgsLYVTFIGSDFVEEGRRaaewLVKNY-KGGKGNVVELQGTAGSSVAIDRSKGFREVIKKHPnikI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 211 EIRQpfmiSANIKKIK-KELEELFALDDPPS--AILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIP 277
Cdd:cd06309 160 VASQ----SGNFTREKgQKVMENLLQAGPGDidVIYAHNDDMALGAIQALKEAGLKPGKDVLVVGIDGQK 225
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
64-212 |
1.83e-08 |
|
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: 54.58 E-value: 1.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGEN--FDLYKRMMKEG 141
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADalAPAVEKAKEAG 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1816548106 142 YPIVFMDRKV-PDLIAPSVVSNNIEATKTTIEHFME--NGHKQIAIATEPLTISTRVERQEGYKKALQDN-GIEI 212
Cdd:cd06313 81 IPLVGVNALIeNEDLTAYVGSDDVVAGELEGQAVADrlGGKGNVVILEGPIGQSAQIDRGKGIENVLKKYpDIKV 155
|
|
| PBP1_ABC_sugar_binding-like |
cd06316 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
69-229 |
1.93e-08 |
|
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: 380539 [Multi-domain] Cd Length: 294 Bit Score: 54.94 E-value: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 69 VANIMHR----FSTEVSRSIEDFFNKHDIHTI-VCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGEN--FDLYKRMMKEG 141
Cdd:cd06316 2 VAIAMHTtgsdWSRLQVAGIKDTFEELGIEVVaVTDANFDPAKQITDLETLIALKPDIIISIPVDPVatAAAYKKVADAG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 142 YPIVFMDRKVPDLIAP----SVVS-NNIE----ATKTTIEHFMENGhkQIAIAT--EPLTISTrvERQEGYKKALQDN-- 208
Cdd:cd06316 82 IKLVFMDNVPDGLEAGkdyvSVVSsDNRGngqiAAELLAEAIGGKG--KVGIIYhdADFYATN--QRDKAFKDTLKEKyp 157
|
170 180
....*....|....*....|...
gi 1816548106 209 GIEI--RQPFMISANIKKIKKEL 229
Cdd:cd06316 158 DIKIvaEQGFADPNDAEEVASAM 180
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
76-314 |
1.98e-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: 380626 [Multi-domain] Cd Length: 267 Bit Score: 54.51 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 76 FSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFP---TGENFDLyKRMMKEGYPIVFMDRKV- 151
Cdd:cd19971 13 FFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPvdsEGIRPAL-EAAKEAGIPVINVDTPVk 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 152 -PDLIAPSVVSNNIEATKTT----IEHFMENGhkQIAIATEPLTISTrVERQEGYKKALQDN-GIEIRQPFMISANIKKI 225
Cdd:cd19971 92 dTDLVDSTIASDNYNAGKLCgedmVKKLPEGA--KIAVLDHPTAESC-VDRIDGFLDAIKKNpKFEVVAQQDGKGQLEVA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 226 KKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLK-----VGKD---FALAVFDNIPFAhlvhppvTTIAQPSYHMG 297
Cdd:cd19971 169 MPIMEDILQAHPDLDAVFALNDPSALGALAALKAAGKLgdilvYGVDgspDAKAAIKDGKMT-------ATAAQSPIEIG 241
|
250
....*....|....*..
gi 1816548106 298 EKASELLLKQINKEEIE 314
Cdd:cd19971 242 KKAVETAYKILNGEKVE 258
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
64-314 |
4.92e-08 |
|
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: 53.45 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTgeNFDLYKRMMKE--- 140
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPT--DSDAVSPAVEEane 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 141 -GYPIVFMDRKVPD-LIAPSVVSNNIEATKTTIEHFME--NGHKQIAIATE-PLTISTRvERQEGYKKALQDN-GIEI-- 212
Cdd:cd06323 79 aGIPVITVDRSVTGgKVVSHIASDNVAGGEMAAEYIAKklGGKGKVVELQGiPGTSAAR-ERGKGFHNAIAKYpKINVva 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 213 RQPfmisANIKKIK--KELEELFALDDPPSAILAGNDLVFLEVLEFAKEhklkVGKDFALAV-FDNIPFAhlvhppVT-- 287
Cdd:cd06323 158 SQT----ADFDRTKglNVMENLLQAHPDIDAVFAHNDEMALGAIQALKA----AGRKDVIVVgFDGTPDA------VKav 223
|
250 260 270
....*....|....*....|....*....|....
gi 1816548106 288 -------TIAQPSYHMGEKASELLLKQINKEEIE 314
Cdd:cd06323 224 kdgklaaTVAQQPEEMGAKAVETADKYLKGEKVP 257
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
64-314 |
9.79e-08 |
|
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: 52.28 E-value: 9.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGEN--FDLYKRMMKEG 141
Cdd:cd06322 1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGgiVPAIEAANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 142 YPIVFMDRKVP-DLIAPSVVSNNIEATKTTIEHFME---NGHKQIAIATEPLTISTrVERQEGYKKALQDN-GIEI--RQ 214
Cdd:cd06322 81 IPVFTVDVKADgAKVVTHVGTDNYAGGKLAGEYALKallGGGGKIAIIDYPEVESV-VLRVNGFKEAIKKYpNIEIvaEQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 215 P--------FMISANIKKIKKELEELFALDDpPSAILAgndlvfLEVLEFA-KEHKLKV-GKDFAL----AVFDNIPFah 280
Cdd:cd06322 160 PgdgrreeaLAATEDMLQANPDLDGIFAIGD-PAALGA------LTAIESAgKEDKIKViGFDGNPeaikAIAKGGKI-- 230
|
250 260 270
....*....|....*....|....*....|....
gi 1816548106 281 lvhppVTTIAQPSYHMGEKASELLLKQINKEEIE 314
Cdd:cd06322 231 -----KADIAQQPDKIGQETVEAIVKYLAGETVE 259
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
64-237 |
2.08e-07 |
|
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: 51.60 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFP-TGENFD-LYKRMMKEG 141
Cdd:cd06311 1 TIGISIPSADHGWTAGVAYYAEKQAKELADLEYKLVTSSNANEQVSQLEDLIAQKVDAIVILPqDSEELTvAAQKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 142 YPIVFMDRKVPDLIAPSVVSNN-----IEATKTTIEHFmeNGHKQIAIATEPLTISTRVERQEGYKKALQDN-GIEI--R 213
Cdd:cd06311 81 IPVVNFDRGLNVLIYDLYVAGDnpgmgVVSAEYIGKKL--GGKGNVVVLEVPSSGSVNEERVAGFKEVIKGNpGIKIlaM 158
|
170 180 190
....*....|....*....|....*....|..
gi 1816548106 214 QP--------FMISANIKKIKKELEELFALDD 237
Cdd:cd06311 159 QAgdwtredgLKVAQDILTKNKKIDAVWAADD 190
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
64-325 |
3.14e-07 |
|
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: 50.75 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDI--HTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGENfDL---YKRMM 138
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINPgaKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSA-GIepaIKRAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 139 KEGYPIVFMDrkVP-DLIAPSVVSNNIEATKTTIEHFME--NGHKQIAIATEPlTISTRVERQEGYKKALQDN-GIEI-- 212
Cdd:cd06321 80 DAGIIVVAVD--VAaEGADATVTTDNVQAGYLACEYLVEqlGGKGKVAIIDGP-PVSAVIDRVNGCKEALAEYpGIKLvd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 213 RQ--------PFMISANIKKIKKELEELFALDDpPSAIlaGNDLVflevlefAKEHKLkvgKDFALAVFDNIPFAHLV-- 282
Cdd:cd06321 157 DQngkgsragGLSVMTRMLTAHPDVDGVFAIND-PGAI--GALLA-------AQQAGR---DDIVITSVDGSPEAVAAlk 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1816548106 283 ---HPPVTTIAQPSYHMGEKASELLLKQINKEEIENHELTFPCELI 325
Cdd:cd06321 224 regSPFIATAAQDPYDMARKAVELALKILNGQEPAPELVLIPSTLV 269
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
101-319 |
4.60e-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: 380659 [Multi-domain] Cd Length: 273 Bit Score: 47.23 E-value: 4.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 101 DNDPEKEKKYIEMLRAKQVDGLIIFPTGENfDL---YKRMMKEGYPIVFMDRKVP-DLIAPSVVSNNIEATKTTIEHFME 176
Cdd:cd20004 40 EDDVEAQIQIIEYFIDQGVDGIVLAPLDRK-ALvapVERARAQGIPVVIIDSDLGgDAVISFVATDNYAAGRLAAKRMAK 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 177 --NGHKQIA-IATEPLTISTRvERQEGYKKALQ--DNGIEIRQPFMISANIKKIKKELEELFALDDPPSAILAGNDLVF- 250
Cdd:cd20004 119 llNGKGKVAlLRLAKGSASTT-DRERGFLEALKklAPGLKVVDDQYAGGTVGEARSSAENLLNQYPDVDGIFTPNESTTi 197
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1816548106 251 --LEVLEfakehKLKVGKDFALAVFDNIPF------AHLVHppvTTIAQPSYHMGEKASELLLKQINKEEIENHELT 319
Cdd:cd20004 198 gaLRALR-----RLGLAGKVKFIGFDASDLlldalrAGEIS---ALVVQDPYRMGYLGVKTAVAALRGKPVPKRIDT 266
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
104-275 |
5.94e-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: 380661 [Multi-domain] Cd Length: 274 Bit Score: 47.21 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 104 PEKEKKY---IEMLR---AKQVDGLIIFPTG--ENFDLYKRMMKEGYPIVFMDRKVPDLIAPSVVS-NNIEA----TKTT 170
Cdd:cd20006 39 PESEEDIdgqIELIEeaiAQKPDAIVLAASDydRLVEAVERAKKAGIPVITIDSPVNSKKADSFVAtDNYEAgkkaGEKL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 171 IEHFMENGhkQIAIATEPLTISTRVERQEGYKKALQDNG-IEIRQPFMISANIKKIKKELEELFALDDPPSAILAGNDLV 249
Cdd:cd20006 119 ASLLGEKG--KVAIVSFVKGSSTAIEREEGFKQALAEYPnIKIVETEYCDSDEEKAYEITKELLSKYPDINGIVALNEQS 196
|
170 180
....*....|....*....|....*.
gi 1816548106 250 FLEVLEFAKEhkLKVGKDFALAVFDN 275
Cdd:cd20006 197 TLGAARALKE--LGLGGKVKVVGFDS 220
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
76-305 |
7.36e-06 |
|
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: 46.88 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 76 FSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLII-FPTGENFDLYKRMMKEGYPIVFMDRKVPDL 154
Cdd:cd01391 16 FGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGpGSSSVAIVIQNLAQLFDIPQLALDATSQDL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 155 IAP-------SVVSNNIEATKTTIEHFMENGHKQIAIATEPLTISTRVeRQEGYKKALQDNGIEI--RQPfmisANIKKI 225
Cdd:cd01391 96 SDKtlykyflSVVFSDTLGARLGLDIVKRKNWTYVAAIHGEGLNSGEL-RMAGFKELAKQEGICIvaSDK----ADWNAG 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 226 KKELEELFALDD---PPSAILAGNDLVFLEVLEFAKEhkLKVGKDFALAVFDNIPFAHLVH-----PPVTTIAQPSYHMG 297
Cdd:cd01391 171 EKGFDRALRKLReglKARVIVCANDMTARGVLSAMRR--LGLVGDVSVIGSDGWADRDEVGyeveaNGLTTIKQQKMGFG 248
|
....*...
gi 1816548106 298 EKASELLL 305
Cdd:cd01391 249 ITAIKAMA 256
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
111-324 |
8.53e-06 |
|
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: 46.47 E-value: 8.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 111 IEMLRAKQVDGLIIFPTG--ENFDLYKRMMKEGYPIVFMDRKV-PDLIA------PSVVSNNIEATKTTIEHFMEN--GH 179
Cdd:cd19970 51 VENLIAQKVDAIVIAPADskALVPVLKKAVDAGIAVINIDNRLdADALKegginvPFVGPDNRQGAYLAGDYLAKKlgKG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 180 KQIAIATEPLTISTRVERQEGYKKALQDNGI----------EIRQPFMISANIKKIKKELEelfalddppsAILAGNDLV 249
Cdd:cd19970 131 GKVAIIEGIPGADNAQQRKAGFLKAFEEAGMkivasqsanwEIDEANTVAANLLTAHPDIR----------GILCANDNM 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 250 FLEVLEFAKEHKLKvgKDFALAVFDNIPfahLVHPPVT------TIAQPSYHMGEKASELLLKQINKEEIENHELTfPCE 323
Cdd:cd19970 201 ALGAIKAVDAAGKA--GKVLVVGFDNIP---AVRPLLKdgkmlaTIDQHPAKQAVYGIEYALKMLNGEEVPGWVKT-PVE 274
|
.
gi 1816548106 324 L 324
Cdd:cd19970 275 L 275
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
64-277 |
2.66e-05 |
|
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: 45.07 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 64 TVGIIVANIMHRFSTEVSRSIEDFFNKHDIHTIVCNADNDPEKEKKYIEMLRAKQVDGLIIFPTGEN--FDLYKRMMKEG 141
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKalVPAIEAAIKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 142 YPIVFMDRKVP-DLIAPSVVSNNI---EATKTTIEHFMENGHKQIAIATEPLTiSTRVERQEGYKKALqDNGIEIRQPFM 217
Cdd:cd19968 81 IPVVTVDRRAEgAAPVPHVGADNVaggREVAKFVVDKLPNGAKVIELTGTPGS-SPAIDRTKGFHEEL-AAGPKIKVVFE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816548106 218 ISANIKKIK--KELEE-LFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAvFDNIP 277
Cdd:cd19968 159 QTGNFERDEglTVMENiLTSLPGPPDAIICANDDMALGAIEAMRAAGLDLKKVKVIG-FDAVP 220
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
101-325 |
4.06e-05 |
|
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: 44.50 E-value: 4.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 101 DNDPEKEKKYIEMLRAKQVDGLIIFPT-GENF-DLYKRMMKEGYPIVFMDRKVPDliapS-----VVSNNIEATKT---T 170
Cdd:cd06314 39 KSDAAEQVQLIEDLIARGVDGIAISPNdPEAVtPVINKAADKGIPVITFDSDAPD----SkrlayIGTDNYEAGREageL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 171 IEHFMENGHKqIAIATEPLTISTRVERQEGYKKALQD-NGIEIRQPF-----MISA--NIKKIKKELEELFALddppSAI 242
Cdd:cd06314 115 MKKALPGGGK-VAIITGGLGADNLNERIQGFKDALKGsPGIEIVDPLsdnddIAKAvqNVEDILKANPDLDAI----FGV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 243 LAGNDLVFLEVLEFAKehklKVGKdFALAVFDNIPF------AHLVHppvTTIAQPSYHMGEKASELLLKQINKEEIENH 316
Cdd:cd06314 190 GAYNGPAIAAALKDAG----KVGK-VKIVGFDTLPEtlqgikDGVIA---ATVGQRPYEMGYLSVKLLYKLLKGGKPVPD 261
|
....*....
gi 1816548106 317 ELTFPCELI 325
Cdd:cd06314 262 VIDTGVDVV 270
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
113-329 |
4.22e-05 |
|
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: 44.33 E-value: 4.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 113 MLRAKQVDGLIIFPTGENFDLYKRMMKEGYPIVFMDRK-VPDLIAPSVVSNNIEATKTTIEHFMENGHKQIAIATEPLTI 191
Cdd:cd06287 51 MLDALDVDGAIVVEPTVEDPILARLRQRGVPVVSIGRApGTDEPVPYVDLQSAATARLLLEHLHGAGARQVALLTGSSRR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 192 STRVERQEGYKKALQDNGIEirqPFMISANI----KKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKD 267
Cdd:cd06287 131 NSSLESEAAYLRFAQEYGTT---PVVYKVPEsegeRAGYEAAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPED 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1816548106 268 FALAV-FDNIPfAHLVHPPVTTIAQPSYHMGEKASELLLKQINKEEIENHELTFPcELIIRDS 329
Cdd:cd06287 208 LMVVTrYDGIR-ARTADPPLTAVDLHLDRVARTAIDLLFASLSGEERSVEVGPAP-ELVVRAS 268
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
101-325 |
1.32e-04 |
|
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: 43.08 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 101 DNDPEKEKKYIEMLRAKQVDGLIIFPTGENFDL--YKRMMKEGYPIVFMDRKVP--DLIAPSVVSNNIEATKTTIEHFME 176
Cdd:cd19967 38 QNDTAKEAELFDTAIASGAKAIILDPADADASIaaVKKAKDAGIPVFLIDREINaeGVAVAQIVSDNYQGAVLLAQYFVK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 177 --NGHKQIAIATEPLTISTRVERQEGYKKALqDNGIEIRQPFMISANIKKIK--KELEELFALDDPPSAILAGNDLVFL- 251
Cdd:cd19967 118 lmGEKGLYVELLGKESDTNAQLRSQGFHSVI-DQYPELKMVAQQSADWDRTEafEKMESILQANPDIKGVICGNDEMALg 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1816548106 252 --EVLEFA-KEHKLKV-GKDFALAVFDNIPFAHLvhppVTTIAQPSYHMGEKASELLLKQINKEEIENHELT-FPCELI 325
Cdd:cd19967 197 aiAALKAAgRAGDVIIvGFDGSNDVRDAIKEGKI----SATVLQPAKLIARLAVEQADQYLKGGSTGKEEKQlFDCVLI 271
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
100-325 |
3.06e-04 |
|
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: 41.94 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 100 ADNDPEKEKKYIEMLRAKQVDGLIIFPT-GENF-DLYKRMMKEGYPIVFMDRKV-PDLIAPSVVSNNIEATKTTIEHFME 176
Cdd:cd06310 39 SEEDVAGQNSLLEELINKKPDAIVVAPLdSEDLvDPLKDAKDKGIPVIVIDSGIkGDAYLSYIATDNYAAGRLAAQKLAE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 177 N-GHK-QIAIATEPLTISTRVERQEGYKKALQDN--GIEIRQPFMISANIKKIKKELEELFALDDPPSAILAGND---LV 249
Cdd:cd06310 119 AlGGKgKVAVLSLTAGNSTTDQREEGFKEYLKKHpgGIKVLASQYAGSDYAKAANETEDLLGKYPDIDGIFATNEitaLG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 250 FLEVLEFAK-EHKLKV-----GKDFALAVFDNIpFAHLVhppvttiAQPSYHMGEKASELLLKQINKEEIENHeLTFPCE 323
Cdd:cd06310 199 AAVAIKSRKlSGQIKIvgfdsQEELLDALKNGK-IDALV-------VQNPYEIGYEGIKLALKLLKGEEVPKN-IDTGAE 269
|
..
gi 1816548106 324 LI 325
Cdd:cd06310 270 LI 271
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
92-277 |
6.46e-04 |
|
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: 41.05 E-value: 6.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 92 DIHTIVCNADNDPEKEKKYIEML--RAKQVDGLIIFPtgenfdlYK----RMMK--EGYPIVFM---------------- 147
Cdd:cd06324 30 GIELEVLYANRNRFKMLELAEELlaRPPKPDYLILVN-------EKgvapELLElaEQAKIPVFlinndltdeerallgk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 148 -DRKVPDLIApSVVSNNIEATKTTIEHFMENGHKQ--------IAIATEPLTISTrVERQEGYKKALQDNG-IEIRQpfM 217
Cdd:cd06324 103 pREKFKYWLG-SIVPDNEQAGYLLAKALIKAARKKsddgkirvLAISGDKSTPAS-ILREQGLRDALAEHPdVTLLQ--I 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1816548106 218 ISAN--IKKIKKELEELFALDDPPSAILAGNDLVFLEVLEFAKEHKLKVGKDFALAVFDNIP 277
Cdd:cd06324 179 VYANwsEDEAYQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGLKPGKDVLVGGIDWSP 240
|
|
| PBP1_ABC_sugar_binding-like |
cd20008 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
100-315 |
1.61e-03 |
|
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: 39.52 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 100 ADNDPEKEKKYIEMLRAKQVDGLIIFPTgeNFDLY---KRMMKEGYPIVFMDRKV-PDLIAPSVVSNNI----EATKTTI 171
Cdd:cd20008 39 TEADIAGQVNLVENAISRKPDAIVLAPN--DTAALvpaVEAADAGIPVVLVDSGAnTDDYDAFLATDNVaagaLAADELA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 172 EHFMENGHK--QIAIATEPLTISTRVERQEGYKKALQDN--GIEIRQPF---------------MISANikkikKELEEL 232
Cdd:cd20008 117 ELLKASGGGkgKVAIISFQAGSQTLVDREEGFRDYIKEKypDIEIVDVQysdgdiakalnqttdLLTAN-----PDLVGI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 233 FALDDPpSAILAGNDLvflevlefaKEHKLkvGKDFALAVFDNIP---------FAHlvhppvTTIAQPSYHMGEKASEL 303
Cdd:cd20008 192 FGANNP-SAVGVAQAL---------AEAGK--AGKIVLVGFDSSPdevallksgVIK------ALVVQDPYQMGYEGVKT 253
|
250
....*....|..
gi 1816548106 304 LLKQINKEEIEN 315
Cdd:cd20008 254 AVKALKGEEIVE 265
|
|
| HTH_XRE |
cd00093 |
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ... |
3-44 |
2.74e-03 |
|
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.
Pssm-ID: 238045 [Multi-domain] Cd Length: 58 Bit Score: 35.61 E-value: 2.74e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1816548106 3 KITMADVAKKAGVSKSTVSQFLNKRYEyMREDTRKRIEAAIE 44
Cdd:cd00093 12 GLTQEELAEKLGVSRSTISRIENGKRN-PSLETLEKLAKALG 52
|
|
| HGD-D |
pfam06050 |
2-hydroxyglutaryl-CoA dehydratase, D-component; Degradation of glutamate via the ... |
95-176 |
7.30e-03 |
|
2-hydroxyglutaryl-CoA dehydratase, D-component; Degradation of glutamate via the hydroxyglutarate pathway involves the syn-elimination of water from 2-hydroxyglutaryl-CoA. This anaerobic process is catalyzed by 2-hydroxyglutaryl-CoA dehydratase, an enzyme with two components (A and D) that reversibly associate during reaction cycles. This component contains one non-reducible [4Fe-4S]2+ cluster and a reduced riboflavin 5'-monophosphate.
Pssm-ID: 461814 Cd Length: 339 Bit Score: 37.66 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816548106 95 TIVCNADNDPEKEKKYI-EMLRAKQVDGLIIFP-------TGENFDLYKRMMKEGYPIVFMDRkvpDLIAPSvvsnnIEA 166
Cdd:pfam06050 257 KIPCPCMTPNERRLELLlDLAKEYKADGVIYHTlkfckpySFESPLIRKALEEAGIPVLSIET---DYSDSD-----EGQ 328
|
90
....*....|
gi 1816548106 167 TKTTIEHFME 176
Cdd:pfam06050 329 LKTRVEAFLE 338
|
|
| HTH_XRE |
smart00530 |
Helix-turn-helix XRE-family like proteins; |
3-29 |
7.32e-03 |
|
Helix-turn-helix XRE-family like proteins;
Pssm-ID: 197775 [Multi-domain] Cd Length: 56 Bit Score: 34.42 E-value: 7.32e-03
|
| YozG |
COG3655 |
DNA-binding transcriptional regulator, XRE family [Transcription]; |
3-35 |
7.74e-03 |
|
DNA-binding transcriptional regulator, XRE family [Transcription];
Pssm-ID: 442872 [Multi-domain] Cd Length: 69 Bit Score: 34.73 E-value: 7.74e-03
10 20 30
....*....|....*....|....*....|...
gi 1816548106 3 KITMADVAKKAGVSKSTVSQFLNKRYEYMREDT 35
Cdd:COG3655 14 GMTKKELAEATGISRATLSRLKNGKAKAVRLDT 46
|
|
| |
