|
Name |
Accession |
Description |
Interval |
E-value |
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
8-336 |
3.80e-121 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 352.19 E-value: 3.80e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 8 KRVLLSDVAKLAGLSKATLSRYMNNSIVLPQDTIDRIETAIRELDYRGNSLARRLSKGGSETLGLVLPDITNPFFAELAD 87
Cdd:COG1609 2 KRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 88 AAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLRKEIQRHERIVLLDEDIPGSQVPKVFAD 167
Cdd:COG1609 82 GIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRPLPDPGVPSVGVD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 168 NVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDYQREFGQQALRHLFSQPVRPT 247
Cdd:COG1609 162 NRAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGPRPT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 248 AVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMMRLLNDDPDIPAETRL 327
Cdd:COG1609 242 AIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERVLL 321
|
....*....
gi 694083976 328 PVEWIGRDS 336
Cdd:COG1609 322 PPELVVRES 330
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
69-330 |
4.90e-95 |
|
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: 282.87 E-value: 4.90e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLRKEIQRHER 148
Cdd:cd06267 1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLAAGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 IVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDYQ 228
Cdd:cd06267 81 VVLIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLSTSRERLEGYRDALAEAGLPVDPELVVEGDFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 229 REFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAV 308
Cdd:cd06267 161 EESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEMGRAAA 240
|
250 260
....*....|....*....|..
gi 694083976 309 HIMMRLLNDDPDIPAETRLPVE 330
Cdd:cd06267 241 ELLLERIEGEEEPPRRIVLPTE 262
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
73-336 |
2.55e-81 |
|
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: 248.22 E-value: 2.55e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 73 VLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLrKEIQRHERIVLL 152
Cdd:cd06284 5 LVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILLSGRLDAELL-SELSKRYPIVQC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 153 DEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDYQREFG 232
Cdd:cd06284 84 CEYIPDSGVPSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDNVYARERLEGYRRALAEAGLPVDEDLIIEGDFSFEAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 233 QQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMM 312
Cdd:cd06284 164 YAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIGETAAELLL 243
|
250 260
....*....|....*....|....
gi 694083976 313 RLLNDDPDIPAETRLPVEWIGRDS 336
Cdd:cd06284 244 EKIEGEGVPPEHIILPHELIVRES 267
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
69-336 |
1.36e-76 |
|
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: 235.88 E-value: 1.36e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNgllrKEIQRHER 148
Cdd:cd06291 1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILGSHSLDI----EEYKKLNI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 -IVLLDEDIPGSqVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDY 227
Cdd:cd06291 77 pIVSIDRYLSEG-IPSVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIEIDENDF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 228 QREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTA 307
Cdd:cd06291 156 SEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIEEMAKEA 235
|
250 260
....*....|....*....|....*....
gi 694083976 308 VHIMMRLLNDDPDIPAETRLPVEWIGRDS 336
Cdd:cd06291 236 VELLLKLIEGEEIEESRIVLPVELIERET 264
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
69-336 |
2.96e-73 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380508 [Multi-domain] Cd Length: 269 Bit Score: 227.49 E-value: 2.96e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLRKEIQRHER 148
Cdd:cd06285 1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQELAARGVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 IVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDYQ 228
Cdd:cd06285 81 VVLVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDERIVPGGFT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 229 REFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAV 308
Cdd:cd06285 161 IEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEMGRRAA 240
|
250 260
....*....|....*....|....*...
gi 694083976 309 HIMMRLLNDDPDIPAETRLPVEWIGRDS 336
Cdd:cd06285 241 ELLLQLIEGGGRPPRSITLPPELVVRES 268
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
69-334 |
1.12e-72 |
|
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: 225.99 E-value: 1.12e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLRKEIQRHER 148
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGPSRELKRLLKHGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 IVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDYQ 228
Cdd:cd06280 81 IVLIDREVEGLELDLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEISTTRERLAGYREALAEAGIPVDESLIFEGDST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 229 REFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAV 308
Cdd:cd06280 161 IEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQPAYEIGRIAA 240
|
250 260
....*....|....*....|....*.
gi 694083976 309 HIMMRLLNDDPDIPAETRLPVEWIGR 334
Cdd:cd06280 241 QLLLERIEGQGEEPRRIVLPTELIIR 266
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
69-332 |
2.33e-72 |
|
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: 225.10 E-value: 2.33e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLRKEIQRHER 148
Cdd:cd19977 1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNEDLIEKLVKSGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 IVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDYQ 228
Cdd:cd19977 81 VVFVDRYIPGLDVDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLELSTRQERLEGYKAALADHGLPVDEELIKHVDRQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 229 REfGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAV 308
Cdd:cd19977 161 DD-VRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQPTYEIGRKAA 239
|
250 260
....*....|....*....|....*
gi 694083976 309 HIMMRLLNDDPDIPAET-RLPVEWI 332
Cdd:cd19977 240 ELLLDRIENKPKGPPRQiVLPTELI 264
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
69-336 |
1.89e-71 |
|
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: 222.90 E-value: 1.89e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLF---TTNRPDNGLLrkEIQR 145
Cdd:cd06275 1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLmcsEMTDDDAELL--AALR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 146 HERIVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYG 225
Cdd:cd06275 79 SIPVVVLDREIAGDNADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSVSRERLAGFRRALAEAGIEVPPSWIVEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 226 DYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGR 305
Cdd:cd06275 159 DFEPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQPKDELGE 238
|
250 260 270
....*....|....*....|....*....|..
gi 694083976 306 TAVHIMMRLLnDDPDIPAETR-LPVEWIGRDS 336
Cdd:cd06275 239 LAVELLLDRI-ENKREEPQSIvLEPELIERES 269
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
69-325 |
6.84e-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: 380516 [Multi-domain] Cd Length: 270 Bit Score: 221.76 E-value: 6.84e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLRKEIQRHER 148
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSHLARLRARGTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 IVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSwPPEWVM---YG 225
Cdd:cd06293 81 VVLLDRPAPGPAGCSVSVDDVQGGALAVDHLLELGHRRIAFVSGPLRTRQVAERLAGARAAVAEAGLD-PDEVVRelsAP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 226 DYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGR 305
Cdd:cd06293 160 DANAELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQPSYELGR 239
|
250 260
....*....|....*....|
gi 694083976 306 TAVhimmRLLNDDPDIPAET 325
Cdd:cd06293 240 AAA----DLLLDEIEGPGHP 255
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
69-336 |
5.75e-68 |
|
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: 214.04 E-value: 5.75e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLRKEIQRHER 148
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNISDEAIIKLLKEEKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 -IVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDY 227
Cdd:cd19976 81 pVVVLDRYIEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPSTYNEHERIEGYKNALQDHNLPIDESWIYSGES 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 228 QREFGQQALRHLFSQPvRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTA 307
Cdd:cd19976 161 SLEGGYKAAEELLKSK-NPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQPIFEMGQEA 239
|
250 260
....*....|....*....|....*....
gi 694083976 308 VHIMMRLLNDDPDIPAETRLPVEWIGRDS 336
Cdd:cd19976 240 AKLLLKIIKNPAKKKEEIVLPPELIKRDS 268
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
69-336 |
2.48e-67 |
|
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: 212.52 E-value: 2.48e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLRKEIQRHER 148
Cdd:cd06299 1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGENSEGLQALIAQGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 IVLLDEDIPG-SQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDY 227
Cdd:cd06299 81 VVFVDREVEGlGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYISGPLSTSTGRERLAAFRAALTAAGIPIDEELVAFGDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 228 QREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTA 307
Cdd:cd06299 161 RQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVERIGRRA 240
|
250 260
....*....|....*....|....*....
gi 694083976 308 VHIMMRLLNDDPDiPAETRLPVEWIGRDS 336
Cdd:cd06299 241 VELLLALIENGGR-ATSIRVPTELIPRES 268
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
69-322 |
4.45e-65 |
|
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: 206.60 E-value: 4.45e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLRKEIQRHER 148
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEELILIAEKIPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 IVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDYQ 228
Cdd:cd06270 81 LVVINRYIPGLADRCVWLDNEQGGRLAAEHLLDLGHRRIACITGPLDIPDARERLAGYRDALAEAGIPLDPSLIIEGDFT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 229 REFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAV 308
Cdd:cd06270 161 IEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHYPIEEMAQAAA 240
|
250
....*....|....
gi 694083976 309 HIMMRLLNDDPDIP 322
Cdd:cd06270 241 ELALNLAYGEPLPI 254
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
69-336 |
1.16e-64 |
|
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: 205.54 E-value: 1.16e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGL-LFTTNRPDNglLRKEIQRHE 147
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIiVVGGFGDEE--LLKLLAEGI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 148 RIVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDY 227
Cdd:cd06290 79 PVVLVDRELEGLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDHPDAQERYAGYRRALEDAGLEVDPRLIVEGDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 228 QREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTA 307
Cdd:cd06290 159 TEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYEMGKTA 238
|
250 260
....*....|....*....|....*....
gi 694083976 308 VHIMMRLLNDDPDIPAETRLPVEWIGRDS 336
Cdd:cd06290 239 AEILLELIEGKGRPPRRIILPTELVIRES 267
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
69-336 |
9.34e-64 |
|
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: 203.27 E-value: 9.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDI----TNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGllRKEIQ 144
Cdd:cd06292 1 LIGYVVPELpggfSDPFFDEFLAALGHAAAARGYDVLLFTASGDEDEIDYYRDLVRSRRVDGFVLASTRHDDP--RVRYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 145 RHERI--VLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWV 222
Cdd:cd06292 79 HEAGVpfVAFGRANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPEGSVPSDDRLAGYRAALEEAGLPFDPGLV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 223 MYGDYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARE 302
Cdd:cd06292 159 VEGENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTVRQPIDE 238
|
250 260 270
....*....|....*....|....*....|....
gi 694083976 303 LGRTAVHIMMRLLNDDPDIPAETRLPVEWIGRDS 336
Cdd:cd06292 239 IGRAVVDLLLAAIEGNPSEPREILLQPELVVRES 272
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
69-335 |
1.31e-63 |
|
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: 202.80 E-value: 1.31e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGL-LFTTNRPDNGLLRKEIQRHE 147
Cdd:cd06289 1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLiLSPAAGTTAELLRRLKAWGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 148 RIVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDY 227
Cdd:cd06289 81 PVVLALRDVPGSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSSTRRERLAGFRAALAEAGLPLDESLIVPGPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 228 QREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTA 307
Cdd:cd06289 161 TREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHPREIGRRA 240
|
250 260
....*....|....*....|....*...
gi 694083976 308 VHIMMRLLNDDPDIPAETRLPVEWIGRD 335
Cdd:cd06289 241 ARLLLRRIEGPDTPPERIIIEPRLVVRE 268
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
69-336 |
2.53e-62 |
|
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: 199.70 E-value: 2.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLRkEIQRHER 148
Cdd:cd19975 1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFASGTLTEENKQ-LLKNMNI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 -IVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSV-RERYQGFCTAMEQAGLSWPPEWVMYGD 226
Cdd:cd19975 80 pVVLVSTESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISGPLDDPNAgYPRYEGYKKALKDAGLPIKENLIVEGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 227 YQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRT 306
Cdd:cd19975 160 FSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQPFYEMGKK 239
|
250 260 270
....*....|....*....|....*....|
gi 694083976 307 AVHIMMRLLNDDPDIPAETRLPVEWIGRDS 336
Cdd:cd19975 240 AVELLLDLIKNEKKEEKSIVLPHQIIERES 269
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
14-337 |
9.22e-60 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 194.92 E-value: 9.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 14 DVAKLAGLSKATLSRYMNNSIVLPQDTIDRIETAIRELDYRGNSLARRLSKGGSETLGLVLPDITNPFFAELADAAEEAA 93
Cdd:PRK10423 3 DVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVERSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 94 SASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFT---TNRPDNGLLrkeiQRHERI--VLLDEDiPGSQVPKVFADN 168
Cdd:PRK10423 83 FERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLcteTHQPSREIM----QRYPSVptVMMDWA-PFDGDSDLIQDN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 169 -VQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDYQREFGQQALRHLFSQPVRPT 247
Cdd:PRK10423 158 sLLGGDLATQYLIDKGYTRIACITGPLDKTPARLRLEGYRAAMKRAGLNIPDGYEVTGDFEFNGGFDAMQQLLALPLRPQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 248 AVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMMRLLNDDPDIPAETRL 327
Cdd:PRK10423 238 AVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQRLQL 317
|
330
....*....|
gi 694083976 328 PVEWIGRDSI 337
Cdd:PRK10423 318 TPELMERGSV 327
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
14-338 |
2.91e-59 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 194.17 E-value: 2.91e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 14 DVAKLAGLSKATLSRYMNNSIVLPQDTIDRIETAIRELDYRGNSLARRLSKGGSETLGLVLPDITNPFFAELADAAEEAA 93
Cdd:PRK10703 6 DVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEAVEKNC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 94 SASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLL-FTTNRPDNGLLRKEIQRHERIVLLDEDIPGSQVPKVFADN-VQG 171
Cdd:PRK10703 86 YQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLvMCSEYPEPLLAMLEEYRHIPMVVMDWGEAKADFTDAIIDNaFEG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 172 GRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDYQREFGQQALRHLFSQPVRPTAVFA 251
Cdd:PRK10703 166 GYLAGRYLIERGHRDIGVIPGPLERNTGAGRLAGFMKAMEEANIKVPEEWIVQGDFEPESGYEAMQQILSQKHRPTAVFC 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 252 ASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMMRLLNDDPDIPAETRLPVEW 331
Cdd:PRK10703 246 GGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRIVNKREEPQTIEVHPRL 325
|
....*..
gi 694083976 332 IGRDSIK 338
Cdd:PRK10703 326 VERRSVA 332
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
69-336 |
6.70e-59 |
|
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: 190.84 E-value: 6.70e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDI-TNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTnrpdngllrkeiqRHE 147
Cdd:cd06288 1 TIGLITDDIaTTPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYAS-------------MHH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 148 RIV---LLDEDIP---------GSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGL 215
Cdd:cd06288 68 REVtlpPELTDIPlvllncfddDPSLPSVVPDDEQGGYLATRHLIEAGHRRIAFIGGPEDSLATRLRLAGYRAALAEAGI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 216 SWPPEWVMYGDYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRIST 295
Cdd:cd06288 148 PYDPSLVVHGDWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTT 227
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 694083976 296 IRQPARELGRTAVHIMMRLLNDDPDIPAETRLPVEWIGRDS 336
Cdd:cd06288 228 VALPYYEMGRRAAELLLDGIEGEPPEPGVIRVPCPLIERES 268
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
69-336 |
1.43e-56 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380504 [Multi-domain] Cd Length: 270 Bit Score: 184.75 E-value: 1.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLRkeiQRHER 148
Cdd:cd06281 1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILTPGDEDDPELA---AALAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 ----IVLLDEDIPGSqVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMY 224
Cdd:cd06281 78 ldipVVLIDRDLPGD-IDSVLVDHRSGVRQATEYLLSLGHRRIALLTGGPDIRPGRERIAGFKAAFAAAGLPPDPDLVRL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 225 GDYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELG 304
Cdd:cd06281 157 GSFSADSGFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDLDAVG 236
|
250 260 270
....*....|....*....|....*....|...
gi 694083976 305 RTAVHIMMRLLNDDPDIPAETR-LPVEWIGRDS 336
Cdd:cd06281 237 RAAAELLLDRIEGPPAGPPRRIvVPTELILRDS 269
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
71-336 |
1.71e-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: 380501 [Multi-domain] Cd Length: 266 Bit Score: 184.27 E-value: 1.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 71 GLVLPDITNPFFAELADAAEEAASASGYSLVLcITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLRKEIQRHERIV 150
Cdd:cd06278 3 GVVVGDLSNPFYAELLEELSRALQARGLRPLL-FNVDDEDDVDDALRQLLQYRVDGVIVTSATLSSELAEECARRGIPVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 151 LLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLswPPEWVMYGDYQRE 230
Cdd:cd06278 82 LFNRVVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPEGTSTSRERERGFRAALAELGL--PPPAVEAGDYSYE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 231 FGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRAS-GLQAPEALSLVGFDD---ANYADFtqpRISTIRQPARELGRT 306
Cdd:cd06278 160 GGYEAARRLLAAPDRPDAIFCANDLMALGALDAARQEgGLVVPEDISVVGFDDipmAAWPSY---DLTTVRQPIEEMAEA 236
|
250 260 270
....*....|....*....|....*....|
gi 694083976 307 AVHIMMRLLNDDPDIPAETRLPVEWIGRDS 336
Cdd:cd06278 237 AVDLLLERIENPETPPERRVLPGELVERGS 266
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
69-336 |
1.75e-55 |
|
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: 182.09 E-value: 1.75e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLRKEIQRHER 148
Cdd:cd06296 1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQLRLLRSAGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 IVLLDE-DIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDY 227
Cdd:cd06296 81 FVLIDPvGEPDPDLPSVGATNWAGGRLATEHLLDLGHRRIAVITGPPRSVSGRARLAGYRAALAEAGIAVDPDLVREGDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 228 QREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTA 307
Cdd:cd06296 161 TYEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVHQPLREMGAVA 240
|
250 260
....*....|....*....|....*....
gi 694083976 308 VHIMMRLLNDDPDIPAETRLPVEWIGRDS 336
Cdd:cd06296 241 VRLLLRLLEGGPPDARRIELATELVVRGS 269
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
96-336 |
2.17e-55 |
|
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: 181.60 E-value: 2.17e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 96 SGYSLVL-CITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLRKEIQRHE-RIVLLDEDIPGSQVPKVFADNVQGGR 173
Cdd:cd01545 28 AGYHLVVePCDSDDEDLADRLRRFLSRSRPDGVILTPPLSDDPALLDALDELGiPYVRIAPGTDDDRSPSVRIDDRAAAR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 174 IATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDYQREFGQQALRHLFSQPVRPTAVFAAS 253
Cdd:cd01545 108 EMTRHLIALGHRRIGFIAGPPDHGASAERLEGFRDALAEAGLPLDPDLVVQGDFTFESGLEAAEALLDLPDRPTAIFASN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 254 DYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMMRLLNDDPDIPAETRLPVEWIG 333
Cdd:cd01545 188 DEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTTVRQPIAEMARRAVELLIAAIRGAPAGPERETLPHELVI 267
|
...
gi 694083976 334 RDS 336
Cdd:cd01545 268 RES 270
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
97-336 |
2.22e-54 |
|
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: 178.93 E-value: 2.22e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 97 GYSLVLCITRNNPEKEC-QFIRWLDTCQVDGLLFTTnrPDNGLLRKEIQRHERI-VLLDEDIPGSQVPKVFADNVQGGRI 174
Cdd:cd01574 29 GYSVSIATVDEDDPASVrEALDRLLSQRVDGIIVIA--PDEAVLEALRRLPPGLpVVIVGSGPSPGVPTVSIDQEEGARL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 175 ATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLswPPEWVMYGDYQREFGQQALRHLFSQPvRPTAVFAASD 254
Cdd:cd01574 107 ATRHLLELGHRRIAHIAGPLDWVDARARLRGWREALEEAGL--PPPPVVEGDWSAASGYRAGRRLLDDG-PVTAVFAAND 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 255 YLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMMRLLNDDPDIPAETRLPVEWIGR 334
Cdd:cd01574 184 QMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDFAELGRRAVELLLALIEGPAPPPESVLLPPELVVR 263
|
..
gi 694083976 335 DS 336
Cdd:cd01574 264 ES 265
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
69-336 |
1.07e-53 |
|
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: 177.32 E-value: 1.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFT-TNRPDNglLRKEIQRHE 147
Cdd:cd06273 1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVgSDHDPE--LFELLEQRQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 148 R-IVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGP----DKlmsVRERYQGFCTAMEQAGLSWPPEWV 222
Cdd:cd06273 79 VpYVLTWSYDEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPtagnDR---ARARLAGIRDALAERGLELPEERV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 223 MYGDYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARE 302
Cdd:cd06273 156 VEAPYSIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPARE 235
|
250 260 270
....*....|....*....|....*....|....
gi 694083976 303 LGRTAVHIMMRLLNDDPdIPAETRLPVEWIGRDS 336
Cdd:cd06273 236 IGELAARYLLALLEGGP-PPKSVELETELIVRES 268
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
69-334 |
1.21e-51 |
|
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: 171.96 E-value: 1.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLRKEIQRHER 148
Cdd:cd06283 1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPTGNNNDAYLELAQKGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 IVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVR-ERYQGFCTAMEQAGLSWPPEWVMYGDY 227
Cdd:cd06283 81 VVLVDRQIEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPIKGISTRrERLQGFLDALARYNIEGDVYVIEIEDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 228 QREfgQQALRHLFSQ-PVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRT 306
Cdd:cd06283 161 EDL--QQALAAFLSQhDGGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQPTYEIGKA 238
|
250 260
....*....|....*....|....*...
gi 694083976 307 AVHIMMRLLNDDPDIPAETRLPVEWIGR 334
Cdd:cd06283 239 AAEILLERIEGDSGEPKEIELPSELIIR 266
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
69-319 |
3.30e-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: 170.80 E-value: 3.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLrKEIQRHER 148
Cdd:cd06286 1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLIITSRENDWEVI-EPYAKYGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 IVLLdEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSV--RERYQGFCTAMEQAGLSWPPEWVMYGD 226
Cdd:cd06286 80 IVLC-EETDSPDIPSVYIDRYEAYLEALEYLKEKGHRKIGYCLGRPESSSAstQARLKAYQDVLGEHGLSLREEWIFTNC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 227 YQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYAdfTQPRISTIRQPARELGRT 306
Cdd:cd06286 159 HTIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPIS--ELLNLTTIDQPLEEMGKE 236
|
250
....*....|...
gi 694083976 307 AVHIMMRLLNDDP 319
Cdd:cd06286 237 AFELLLSQLESKE 249
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
67-336 |
7.06e-51 |
|
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: 170.12 E-value: 7.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 67 SETLGLVLP-------DITNPFFAELADAAEEAASASGYSLVLCITRNNPEkecQFIRWLDTCQVDGLLFTTNRPDNGLL 139
Cdd:cd06295 3 SRTIAVVVPmdphgdqSITDPFFLELLGGISEALTDRGYDMLLSTQDEDAN---QLARLLDSGRADGLIVLGQGLDHDAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 140 RKEIQRHERIVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDkLMSVRERYQGFCTAMEQAGLSWPP 219
Cdd:cd06295 80 RELAQQGLPMVVWGAPEDGQSYCSVGSDNVKGGALATEHLIEIGRRRIAFLGDPP-HPEVADRLQGYRDALAEAGLEADP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 220 EWVMYGDYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQP 299
Cdd:cd06295 159 SLLLSCDFTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFRPPLTTVRQD 238
|
250 260 270
....*....|....*....|....*....|....*..
gi 694083976 300 ARELGRTAVHIMMRLLNDDPdiPAETRLPVEWIGRDS 336
Cdd:cd06295 239 LALAGRLLVEKLLALIAGEP--VTSSMLPVELVVRES 273
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
97-336 |
1.58e-49 |
|
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: 166.58 E-value: 1.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 97 GYSLVLCITRNNPEKECQFIRWLDTCQVDGLLF-----TTNRPDNGLLRKEIQRHERIVLLDEDIPGSQVPKVFADNVQG 171
Cdd:cd01541 29 GYSLLLALTNNDVEKEREILESLLDQNVDGLIIeptksALPNPNLDLYEELQKKGIPVVFINSYYPELDAPSVSLDDEKG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 172 GRIATEKLIAAGHRHIAFVGGPDKLMSVrERYQGFCTAMEQAGLSWPPEWV-MY--GDYQREFGQQALRHLFSQPVRPTA 248
Cdd:cd01541 109 GYLATKHLIDLGHRRIAGIFKSDDLQGV-ERYQGFIKALREAGLPIDDDRIlWYstEDLEDRFFAEELREFLRRLSRCTA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 249 VFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMMRLLNDDPDiPAETRLP 328
Cdd:cd01541 188 IVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEPPLTSVVHPKEELGRKAAELLLRMIEEGRK-PESVIFP 266
|
....*...
gi 694083976 329 VEWIGRDS 336
Cdd:cd01541 267 PELIERES 274
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
38-336 |
2.41e-49 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 167.48 E-value: 2.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 38 QDTIDRIETAIRELDYRGNSLARRLSKGGSETLGLVLPDITNPFFAELADAAEEAASASGYsLVL---CITRNNPEKecQ 114
Cdd:PRK11041 6 QATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGY-LVLigdCAHQNQQEK--T 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 115 FIRWLDTCQVDG-LLFTTNRP-DNGllrKEIQRH-ERIVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVG 191
Cdd:PRK11041 83 FVNLIITKQIDGmLLLGSRLPfDAS---KEEQRNlPPMVMANEFAPELELPTVHIDNLTAAFEAVNYLHELGHKRIACIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 192 GPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQA 271
Cdd:PRK11041 160 GPEEMPLCHYRLQGYVQALRRCGITVDPQYIARGDFTFEAGAKALKQLLDLPQPPTAVFCHSDVMALGALSQAKRMGLRV 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694083976 272 PEALSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMMRLLNDDpDIPAETRL-PVEWIGRDS 336
Cdd:PRK11041 240 PQDLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGH-HVSSGSRLlDCELIIRGS 304
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
69-332 |
3.06e-48 |
|
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: 163.11 E-value: 3.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLP----DITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNgllrkeiq 144
Cdd:cd20010 1 AIGLVLPldpgDLGDPFFLEFLAGLSEALAERGLDLLLAPAPSGEDELATYRRLVERGRVDGFILARTRVND-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 145 rhERI-VLLDEDIP---------GSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAG 214
Cdd:cd20010 73 --PRIaYLLERGIPfvvhgrsesGAPYAWVDIDNEGAFRRATRRLLALGHRRIALLNGPEELNFAHQRRDGYRAALAEAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 215 LSWPPEWVMYGDYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDA-NYADFTQPRI 293
Cdd:cd20010 151 LPVDPALVREGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLlPALEYFSPPL 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 694083976 294 STIRQPARELGRTAVHIMMRLLNDDPDIPAETRLPVEWI 332
Cdd:cd20010 231 TTTRSSLRDAGRRLAEMLLALIDGEPAAELQELWPPELI 269
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
5-336 |
3.32e-48 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 165.17 E-value: 3.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 5 MSIKRVLLSDVAKLAGLSKATLSRYMNNSIVLPQDTIDRIETAIRELDYRGNSLARRLSKGGSETLGLVLPDITNPFFAE 84
Cdd:PRK09526 1 MKSKPVTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTSLALHAPSQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 85 LADAAEEAASASGYSLVLCITRNNPEKECQF-IRWLDTCQVDGLLFttNRPdngllrKEIQRHERIVLLDEDI------- 156
Cdd:PRK09526 81 IAAAIKSRADQLGYSVVISMVERSGVEACQAaVNELLAQRVSGVII--NVP------LEDADAEKIVADCADVpclfldv 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 157 -PGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSwpPEWVMYGDYQREFGQQA 235
Cdd:PRK09526 153 sPQSPVNSVSFDPEDGTRLGVEHLVELGHQRIALLAGPESSVSARLRLAGWLEYLTDYQLQ--PIAVREGDWSAMSGYQQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 236 LRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMMRLL 315
Cdd:PRK09526 231 TLQMLREGPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLLALS 310
|
330 340
....*....|....*....|.
gi 694083976 316 nDDPDIPAETRLPVEWIGRDS 336
Cdd:PRK09526 311 -QGQAVKGSQLLPTSLVVRKS 330
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
69-328 |
6.00e-48 |
|
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: 162.45 E-value: 6.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLrKEIQRHER 148
Cdd:cd06282 1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTVGDAQGSEA-LELLEEEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 I--VLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPdkLMS---VRERYQGFCTAMEQAGLSwPPEWVM 223
Cdd:cd06282 80 VpyVLLFNQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAGD--FSAsdrARLRYQGYRDALKEAGLK-PIPIVE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 224 YGDYQREFgQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPAREL 303
Cdd:cd06282 157 VDFPTNGL-EEALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQPSRDM 235
|
250 260
....*....|....*....|....*
gi 694083976 304 GRTAVHIMMRLLNDDpDIPAETRLP 328
Cdd:cd06282 236 GRAAADLLLAEIEGE-SPPTSIRLP 259
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
5-335 |
1.45e-46 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 161.03 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 5 MSIKRVLLSDVAKLAGLSKATLSRYMNNSIVLPQDTIDRIETAIRELDYRGNSLARRLSKGGSETLGLVLPDITNPFFAE 84
Cdd:PRK10014 2 ATAKKITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 85 LADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLRKEIQrherivlldedipGSQVPKV 164
Cdd:PRK10014 82 LTAGLTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAGSSDDLREMAE-------------EKGIPVV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 165 FA--------------DNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDYQRE 230
Cdd:PRK10014 149 FAsrasylddvdtvrpDNMQAAQLLTEHLIRNGHQRIAWLGGQSSSLTRAERVGGYCATLLKFGLPFHSEWVLECTSSQK 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 231 FGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEA---------LSLVGFDDANYADFTQPRISTIRQPAR 301
Cdd:PRK10014 229 QAAEAITALLRHNPTISAVVCYNETIAMGAWFGLLRAGRQSGESgvdryfeqqVALAAFTDVPEAELDDPPLTWASTPAR 308
|
330 340 350
....*....|....*....|....*....|....
gi 694083976 302 ELGRTAVHIMMRLLNDDPDIPAETRLPVEWIGRD 335
Cdd:PRK10014 309 EIGRTLADRMMQRITHEETHSRNLIIPPRLIARK 342
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
97-336 |
2.13e-46 |
|
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: 158.45 E-value: 2.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 97 GYSLVLCITRNNpekecqfIRWLDTCQVDGLL----FTTNrpdngLLRKEIQRHERIVLLDEDIPGSQVPKVFADNVQGG 172
Cdd:cd01544 34 GYEIKTIFRDDE-------DLESLLEKVDGIIaigkFSKE-----EIEKLKKLNPNIVFVDSNPDPDGFDSVVPDFEQAV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 173 RIATEKLIAAGHRHIAFVGGPDKLMSVRE-----RYQGFCTAMEQAGLsWPPEWVMYGDYQREFGQQALRHLFSQPVRPT 247
Cdd:cd01544 102 RQALDYLIELGHRRIGFIGGKEYTSDDGEeiedpRLRAFREYMKEKGL-YNEEYIYIGEFSVESGYEAMKELLKEGDLPT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 248 AVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMMRLLNDDPDIPAETRL 327
Cdd:cd01544 181 AFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTPPLTTVHIPTEEMGRTAVRLLLERINGGRTIPKKVLL 260
|
....*....
gi 694083976 328 PVEWIGRDS 336
Cdd:cd01544 261 PTKLIERES 269
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
69-322 |
7.40e-46 |
|
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: 156.97 E-value: 7.40e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDIT-----NPFFAELADAAEEAASASGYSLVLcITRNNPEKECQFI-RWLDTCQVDGLLFTTNRPDNGLLrKE 142
Cdd:cd06294 1 TIGLVLPSSAeelfqNPFFSEVLRGISQVANENGYSLLL-ATGNTEEELLEEVkRMVRGRRVDGFILLYSKEDDPLI-EY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 143 IQRHE-RIVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEW 221
Cdd:cd06294 79 LKEEGfPFVVIGKPLDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVSIDRLQGYKQALKEAGLPLDDDY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 222 VMYGDYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPAR 301
Cdd:cd06294 159 ILLLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSVDINPY 238
|
250 260
....*....|....*....|.
gi 694083976 302 ELGRTAVHIMMRLLNDDPDIP 322
Cdd:cd06294 239 ELGREAAKLLINLLEGPESLP 259
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
69-336 |
8.87e-45 |
|
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: 153.99 E-value: 8.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLlRKEIQRHER 148
Cdd:cd06298 1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMGDELTEEI-REEFKRSPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 -IVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRE-RYQGFCTAMEQAGLSWPPEWVMYGD 226
Cdd:cd06298 80 pVVLAGTVDSDHEIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSGPLKEYINNDkKLQGYKRALEEAGLEFNEPLIFEGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 227 YQREFGQQALRHLFSQPVrPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRT 306
Cdd:cd06298 160 YDYDSGYELYEELLESGE-PDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPLYDIGAV 238
|
250 260 270
....*....|....*....|....*....|
gi 694083976 307 AVHIMMRLLNDDPDIPAETRLPVEWIGRDS 336
Cdd:cd06298 239 AMRLLTKLMNKEEVEETIVKLPHSIIWRQS 268
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
14-315 |
2.12e-44 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 155.32 E-value: 2.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 14 DVAKLAGLSKATLSRYMNNSIVLPQDTIDRIETAIRELDYRGNSLARRLSKGGSETLGLVLPDITNPFFAELADAAEEAA 93
Cdd:PRK10401 6 DVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAVDLVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 94 SASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLRKEIQRHERIVLLDEDIPGSQVPKVFADNVQGGR 173
Cdd:PRK10401 86 QQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDQIPGMVLINRVVPGYAHRCVCLDNVSGAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 174 IATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDYQREFGQQALRHLFSQPVRPTAVFAAS 253
Cdd:PRK10401 166 MATRMLLNNGHQRIGYLSSSHGIEDDAMRRAGWMSALKEQGIIPPESWIGTGTPDMQGGEAAMVELLGRNLQLTAVFAYN 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694083976 254 DYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQP----------------ARELGRTAVHIMMRLL 315
Cdd:PRK10401 246 DNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPiasmaklatelalqgaAGNLDPRASHCFMPTL 323
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
97-336 |
3.02e-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: 380629 [Multi-domain] Cd Length: 270 Bit Score: 152.70 E-value: 3.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 97 GYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTtnrpdnGLLRKEIQRHER-----IVLLDEDIPGSQVPKVFADNVQG 171
Cdd:cd19974 32 GYNLVLEIISDEDEEELNLPSIISEEKVDGIIIL------GEISKEYLEKLKelgipVVLVDHYDEELNADSVLSDNYYG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 172 GRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDYQREFGqqaLRHLFSQPV---RPTA 248
Cdd:cd19974 106 AYKLTSYLIEKGHKKIGFVGDINYTSSFMDRYLGYRKALLEAGLPPEKEEWLLEDRDDGYG---LTEEIELPLklmLPTA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 249 VFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMMRLLNdDPDIPAET-RL 327
Cdd:cd19974 183 FVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLTTVEVDKEAMGRRAVEQLLWRIE-NPDRPFEKiLV 261
|
....*....
gi 694083976 328 PVEWIGRDS 336
Cdd:cd19974 262 SGKLIERDS 270
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
69-332 |
5.56e-43 |
|
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: 149.28 E-value: 5.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLRKEIQRHER 148
Cdd:cd06274 1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAPSTPPDDIYYLCQAAGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 IVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDYQ 228
Cdd:cd06274 81 VVFLDRPFSGSDAPSVVSDNRAGARALTEKLLAAGPGEIYFLGGRPELPSTAERIRGFRAALAEAGITEGDDWILAEGYD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 229 REFGQQALRHLFSQPVR-PTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTA 307
Cdd:cd06274 161 RESGYQLMAELLARLGGlPQALFTSSLTLLEGVLRFLRERLGAIPSDLVLGTFDDHPLLDFLPNPVDSVRQDHDEIAEHA 240
|
250 260
....*....|....*....|....*
gi 694083976 308 VHIMMRLLNDDPDiPAETRLPVEWI 332
Cdd:cd06274 241 FELLDALIEGQPE-PGVIIIPPELI 264
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
69-336 |
5.82e-41 |
|
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: 144.17 E-value: 5.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTtnrpdnGLLRKEIQRHer 148
Cdd:cd01575 1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILT------GTEHTPATRK-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 ivLLDE---------DIPGSQVPKVFA-DNVQGGRIATEKLIAAGHRHIAFVGGPDKLMS-VRERYQGFCTAMEQAGLSW 217
Cdd:cd01575 73 --LLRAagipvvetwDLPDDPIDMAVGfSNFAAGRAMARHLIERGYRRIAFVGARLDGDSrARQRLEGFRDALAEAGLPL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 218 PPEWVMYGDYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIR 297
Cdd:cd01575 151 PLVLLVELPSSFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVR 230
|
250 260 270
....*....|....*....|....*....|....*....
gi 694083976 298 QPARELGRTAVHIMMRLLNDDPDIPAETRLPVEWIGRDS 336
Cdd:cd01575 231 VPRYEIGRKAAELLLARLEGEEPEPRVVDLGFELVRRES 269
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
124-336 |
4.94e-40 |
|
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: 142.35 E-value: 4.94e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 124 VDGLLFTTNRPDNGLLRKEIQRHERIVLLDEDiPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGP---------- 193
Cdd:cd06279 57 VDGFIVYGLSDDDPAVAALRRRGLPLVVVDGP-APPGIPSVGIDDRAAARAAARHLLDLGHRRIAILSLRldrgrergpv 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 194 ------DKLMSV-RERYQGFCTAMEQAGLSWPPEWVMYGDYQ-REFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLR 265
Cdd:cd06279 136 saerlaAATNSVaRERLAGYRDALEEAGLDLDDVPVVEAPGNtEEAGRAAARALLALDPRPTAILCMSDVLALGALRAAR 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694083976 266 ASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMMRLLNDDPdiPAETRLPVEWIGRDS 336
Cdd:cd06279 216 ERGLRVPEDLSVTGFDDIPEAAAADPGLTTVRQPAVEKGRAAARLLLGLLPGAP--PRPVILPTELVVRAS 284
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
96-330 |
7.43e-39 |
|
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: 138.40 E-value: 7.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 96 SGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLF--TTNRPDNGLLRKEIQRheRIVLLDEDIPGsqVPKVFADNVQGGR 173
Cdd:cd01542 28 NGYQPLIANTNLDEEREIEYLETLARQKVDGIILfaTEITDEHRKALKKLKI--PVVVLGQEHEG--FSCVYHDDYGAGK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 174 IATEKLIAAGHRHIAFVGGPDKLMSV-RERYQGFCTAMEQAGLswPPEWVMYGDYQREFGQQALRHLFSQPvRPTAVFAA 252
Cdd:cd01542 104 LLGEYLLKKGHKNIAYIGVDEEDIAVgVARKQGYLDALKEHGI--DEVEIVETDFSMESGYEAAKELLKEN-KPDAIICA 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694083976 253 SDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMMRLLNDDPdIPAETRLPVE 330
Cdd:cd01542 181 TDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEAGEKAAELLLDMIEGEK-VPKKQKLPYE 257
|
|
| PRK10727 |
PRK10727 |
HTH-type transcriptional regulator GalR; |
14-319 |
8.18e-38 |
|
HTH-type transcriptional regulator GalR;
Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 137.97 E-value: 8.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 14 DVAKLAGLSKATLSRYMNNSIVLPQDTIDRIETAIRELDYRGNSLARRLSKGGSETLGLVLPDITNPFFAELADAAEEAA 93
Cdd:PRK10727 6 DVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKAVEQVA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 94 SASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNR-PDNGL--LRKEIqrhERIVLLDEDIPGSQVPKVFADNVQ 170
Cdd:PRK10727 86 YHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVVHAKMiPDAELasLMKQI---PGMVLINRILPGFENRCIALDDRY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 171 GGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDYQREFGQQALRHLFSQPVRPTAVF 250
Cdd:PRK10727 163 GAWLATRHLIQQGHTRIGYLCSNHSISDAEDRLQGYYDALAESGIPANDRLVTFGEPDESGGEQAMTELLGRGRNFTAVA 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694083976 251 AASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMMRLLNDDP 319
Cdd:PRK10727 243 CYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELALALADNRP 311
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
97-329 |
1.46e-37 |
|
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: 135.45 E-value: 1.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 97 GYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPD-NGLLRKEIQRHERIVLLD-EDIPGSQVPKVFADNVQGGRI 174
Cdd:cd01537 29 GVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAaAGVAEKARGQNVPVVFFDkEPSRYDKAYYVITDSKEGGII 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 175 ATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDYQREFGQQALRHLFSQPVRPTAVFAASD 254
Cdd:cd01537 109 QGDLLAKHGHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKTEQLQLDTGDWDTASGKDKMDQWLSGPNKPTAVIANND 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694083976 255 YLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMMRLLNDDPDIPAETRLPV 329
Cdd:cd01537 189 AMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDANNLGKTTFDLLLNLADNWKIDNKVVRVPY 263
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
179-336 |
3.34e-36 |
|
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: 128.22 E-value: 3.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 179 LIAAGHRHIAFVG--GPDKLMSVRERYQGFCTAMEQAGLswPPEWVMYGDYQREFGQQALRHLFSQPVRPTAVFAASDYL 256
Cdd:pfam13377 2 LAELGHRRIALIGpeGDRDDPYSDLRERGFREAARELGL--DVEPTLYAGDDEAEAAAARERLRWLGALPTAVFVANDEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 257 VLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMMRLLNDDPDIPAETRLPVEWIGRDS 336
Cdd:pfam13377 80 ALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVERES 159
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
69-336 |
8.69e-36 |
|
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: 130.66 E-value: 8.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTnRPDNGLLRKEIQRHER 148
Cdd:cd06297 1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLLSEYRLEKYLRNSTLAYQCDGLVMAS-LDLTELFEEVIVPTEK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 -IVLLDEDIPGsqVPKVFADNVQGGRIATEKLIAAGHRHIAFVG---GPDKLMSV-RERYQGFCTAMEQAGLSWPPEWVM 223
Cdd:cd06297 80 pVVLIDANSMG--YDCVYVDNVKGGFMATEYLAGLGEREYVFFGieeDTVFTETVfREREQGFLEALNKAGRPISSSRMF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 224 YGDYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADftQPRISTIRQPAREL 303
Cdd:cd06297 158 RIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAA--SPGLTTVRQPVEEM 235
|
250 260 270
....*....|....*....|....*....|...
gi 694083976 304 GRTAVHIMMRLLNDDPDIPAETRLPVEWIGRDS 336
Cdd:cd06297 236 GEAAAKLLLKRLNEYGGPPRSLKFEPELIVRES 268
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
69-334 |
6.12e-30 |
|
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: 115.30 E-value: 6.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPD-NGLLRKEIQRHE 147
Cdd:pfam00532 3 KLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPAPSgDDITAKAEGYGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 148 RIVLLDE--DIPGSqVPKVFADNVQGGRIATEKLIAAGH-RHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMY 224
Cdd:pfam00532 83 PVIAADDafDNPDG-VPCVMPDDTQAGYESTQYLIAEGHkRPIAVMAGPASALTARERVQGFMAALAAAGREVKIYHVAT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 225 GDYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASG-LQAPEA-----LSLVGFD---DANYADFTQPRIST 295
Cdd:pfam00532 162 GDNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGrVKIPDIvgigiNSVVGFDglsKAQDTGLYLSPLTV 241
|
250 260 270
....*....|....*....|....*....|....*....
gi 694083976 296 IRQPARELGRTAVHIMMRLLNDDPDIPAETRLPVEWIGR 334
Cdd:pfam00532 242 IQLPRQLLGIKASDMVYQWIPKFREHPRVLLIPRDFFKE 280
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
125-332 |
6.18e-29 |
|
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: 112.25 E-value: 6.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 125 DGLLFTTNRPDNgllrkeiqrhERIVLLDE-DIP---------GSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPD 194
Cdd:cd20009 59 DGIIISHTEPQD----------PRVRYLLErGFPfvthgrtelSTPHAYFDFDNEAFAYEAVRRLAARGRRRIALVAPPR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 195 KLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEA 274
Cdd:cd20009 129 ELTYAQHRLRGFRRALAEAGLEVEPLLIVTLDSSAEAIRAAARRLLRQPPRPDGIICASEIAALGALAGLEDAGLVVGRD 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 694083976 275 LSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMMRLLNDDPDIPAETRLPVEWI 332
Cdd:cd20009 209 VDVVAKETSPILDYFRPPIDTLYEDIEEAGRFLAEALLRRIEGEPAEPLQTLERPELI 266
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
97-317 |
1.12e-27 |
|
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: 109.05 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 97 GYSLVLciTRNNPEKECQFIRWL-DTCQVDGLLFTTNRPDNGLLRKEIQRHERIVLLDEDIPGSQVPKVFADNVQGGRIA 175
Cdd:cd06271 32 GYHLLV--WPFEEAES*VPIRDLvETGSADGVILSEIEPNDPRVQFLTKQNFPFVAHGRSD*PIGHAWVDIDNEAGAYEA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 176 TEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLswpPEWVMYGDYQREFGQQALRHLFSQPVRPTAVFAASDY 255
Cdd:cd06271 110 VERLAGLGHRRIAFIVPPARYSPHDRRLQGYVRA*RDAGL---TGYPLDADTTLEAGRAAAQRLLALSPRPTAIVTMNDS 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694083976 256 LVLGLLDGLRASGLQAPEALSLVGFDDANY-ADFTQPRISTIRQPARELGRTAVHIMMRLLND 317
Cdd:cd06271 187 ATIGLVAGLQAAGLKIGEDVSIIGKDSAPFlGAMITPPLTTVHAPIAEAGRELAKALLARIDG 249
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
12-328 |
8.43e-27 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 108.04 E-value: 8.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 12 LSDVAKLAGLSKATLSRYMNN-------SivlpQDTIDRIETAIRELDYRGNSLARRLSKGGSETLGLVLPDITNPFFAE 84
Cdd:PRK11303 3 LDEIARLAGVSRTTASYVINGkakqyrvS----DKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSYAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 85 LADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRP-DNGLLRKEIQRHERIVLLDEDIPGSQVPK 163
Cdd:PRK11303 79 IAKYLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVSTSLPpEHPFYQRLQNDGLPIIALDRALDREHFTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 164 VFADNVQGGRIATEKLIAAGHRHIAFVGG-PDKLMSvRERYQGFCTAMEQAGLswpPEWVMYGD-YQREFGQQALRHLFS 241
Cdd:PRK11303 159 VVSDDQDDAEMLAESLLKFPAESILLLGAlPELSVS-FEREQGFRQALKDDPR---EVHYLYANsFEREAGAQLFEKWLE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 242 QPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMMRLLN-DDPD 320
Cdd:PRK11303 235 THPMPDALFTTSYTLLQGVLDVLLERPGELPSDLAIATFGDNELLDFLPCPVNAVAQQHRLIAERALELALAALDePRKP 314
|
....*...
gi 694083976 321 IPAETRLP 328
Cdd:PRK11303 315 KPGLTRIR 322
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
141-336 |
3.82e-26 |
|
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: 105.01 E-value: 3.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 141 KEIQRHER-IVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPP 219
Cdd:cd06277 78 KLFQDVSIpVVVVDNYFEDLNFDCVVIDNEDGAYEAVKYLVELGHTRIGYLASSYRIKNFEERRRGFRKAMRELGLSEDP 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 220 EWVMYGDYQREFGQQALRHLFSQPVR-PTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQ 298
Cdd:cd06277 158 EPEFVVSVGPEGAYKDMKALLDTGPKlPTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHV 237
|
170 180 190
....*....|....*....|....*....|....*...
gi 694083976 299 PARELGRTAVHIMMRLLNDDPDIPAETRLPVEWIGRDS 336
Cdd:cd06277 238 PKEQMGKLAVRRLIEKIKDPDGGTLKILVSTKLVERGS 275
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
5-305 |
3.68e-25 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 103.57 E-value: 3.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 5 MSIKRVLLSDVAKLAGLSKATLSRYMNNSIVLPQDTIDRIETAIRELDYRGNSLARRLSKGGSETLGLVLPDITNPFFAE 84
Cdd:PRK14987 1 MKKKRPVLQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 85 LADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTT-NRPDNGLLRKEIQRHERIVLLDEDIPGSQVPK 163
Cdd:PRK14987 81 VLRGIESVTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTErTHTPRTLKMIEVAGIPVVELMDSQSPCLDIAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 164 VFaDNVQGGRIATEKLIAAGHRHIAFVGGP-DKLMSVRERyqGFCTAMEQAGLSwPPEWVMYGDYQREFGQQALRHLFSQ 242
Cdd:PRK14987 161 GF-DNFEAARQMTTAIIARGHRHIAYLGARlDERTIIKQK--GYEQAMLDAGLV-PYSVMVEQSSSYSSGIELIRQARRE 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694083976 243 PVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGR 305
Cdd:PRK14987 237 YPQLDGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGS 299
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
114-336 |
2.73e-22 |
|
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: 94.19 E-value: 2.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 114 QFIRWLDTCQVDGLLFTTNRPDngLLRKEIQRHERIVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGP 193
Cdd:cd01543 41 ELLDLLKGWKGDGIIARLDDPE--LAEALRRLGIPVVNVSGSRPEPGFPRVTTDNEAIGRMAAEHLLERGFRHFAFCGFR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 194 DKLMSvRERYQGFCTAMEQAGL---SWPPEWVMYGDYQREFGQQALRHLFSQPvRPTAVFAASDYLVLGLLDGLRASGLQ 270
Cdd:cd01543 119 NAAWS-RERGEGFREALREAGYechVYESPPSGSSRSWEEEREELADWLKSLP-KPVGIFACNDDRARQVLEACREAGIR 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694083976 271 APEALSLVGFD-DANYADFTQPRISTIRQPARELGRTAVHIMMRLLNDDPdIPAETRL--PVEWIGRDS 336
Cdd:cd01543 197 VPEEVAVLGVDnDELICELSSPPLSSIALDAEQIGYEAAELLDRLMRGER-VPPEPILipPLGVVTRQS 264
|
|
| HTH_LACI |
smart00354 |
helix_turn _helix lactose operon repressor; |
12-79 |
1.05e-21 |
|
helix_turn _helix lactose operon repressor;
Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 87.26 E-value: 1.05e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694083976 12 LSDVAKLAGLSKATLSRYMNNSIVLPQDTIDRIETAIRELDYRGNSLARRLSKGGSETLGLVLPDITN 79
Cdd:smart00354 3 IKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
|
|
| PRK10339 |
PRK10339 |
DNA-binding transcriptional repressor EbgR; Provisional |
12-338 |
6.60e-21 |
|
DNA-binding transcriptional repressor EbgR; Provisional
Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 91.74 E-value: 6.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 12 LSDVAKLAGLSKATLSRYMNN--SIVLPQDTIDRIETAIRELDYRGNSlARRLSKGGSETLGLVL-------PDITNPFF 82
Cdd:PRK10339 4 LKDIAIEAGVSLATVSRVLNDdpTLNVKEETKHRILEIAEKLEYKTSS-ARKLQTGAVNQHHILAiysyqqeLEINDPYY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 83 AELADAAEEAASASGYSLVLCITRNNPekecqfirwLDTCQVDGLLFTtNRPDNGLLRKEIQRHERIVLLDEDIPGSQVP 162
Cdd:PRK10339 83 LAIRHGIETQCEKLGIELTNCYEHSGL---------PDIKNVTGILIV-GKPTPALRAAASALTDNICFIDFHEPGSGYD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 163 KVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEwVMYGDYQREFGQQALRHLFSQ 242
Cdd:PRK10339 153 AVDIDLARISKEIIDFYINQGVNRIGFIGGEDEPGKADIREVAFAEYGRLKQVVREED-IWRGGFSSSSGYELAKQMLAR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 243 PVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMMRLLNDDPDIP 322
Cdd:PRK10339 232 EDYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNLLYEKARDGRALP 311
|
330
....*....|....*.
gi 694083976 323 AETRLPVEWIGRDSIK 338
Cdd:PRK10339 312 LLVFVPSKLKLRGTTR 327
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
63-337 |
2.63e-20 |
|
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: 89.60 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 63 SKGGSETLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKEcqfIRWLDTC---QVDGLLFTTNRPDngLL 139
Cdd:COG1879 29 AAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQ---ISQIEDLiaqGVDAIIVSPVDPD--AL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 140 RKEIQR-HER---IVLLDEDIPGSQ-VPKVFADNVQGGRIATEKLIAA--GHRHIAFVGGPDKLMSVRERYQGFCTAMEQ 212
Cdd:COG1879 104 APALKKaKAAgipVVTVDSDVDGSDrVAYVGSDNYAAGRLAAEYLAKAlgGKGKVAILTGSPGAPAANERTDGFKEALKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 213 AglswpPEW----VMYGDYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPeaLSLVGFD--DANYA 286
Cdd:COG1879 184 Y-----PGIkvvaEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRKGD--VKVVGFDgsPEALQ 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 694083976 287 DFTQPRIS-TIRQPARELGRTAVHIMMRLLNDDPdIPAETRLPVEWIGRDSI 337
Cdd:COG1879 257 AIKDGTIDaTVAQDPYLQGYLAVDAALKLLKGKE-VPKEILTPPVLVTKENV 307
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
157-335 |
7.08e-18 |
|
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: 82.04 E-value: 7.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 157 PGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEWVMYGDYQREFGQQAL 236
Cdd:cd06272 88 ESPKYSTVNVDNEKAGRLAVLLLIQKGHKSIAYIGNPNSNRNQTLRGKGFIETCEKHGIHLSDSIIDSRGLSIEGGDNAA 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 237 RHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMMRLLN 316
Cdd:cd06272 168 KKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLTVVGVPIEKIAEESLRLILKLIE 247
|
170
....*....|....*....
gi 694083976 317 DDPDIPAETRLPVEWIGRD 335
Cdd:cd06272 248 GRENEIQQLILYPELIFRE 266
|
|
| HTH_LacI |
cd01392 |
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
14-64 |
3.44e-14 |
|
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: 65.89 E-value: 3.44e-14
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 694083976 14 DVAKLAGLSKATLSRYMNNSIVLPQDTIDRIETAIRELDYRGNSLARRLSK 64
Cdd:cd01392 2 DIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
69-330 |
1.22e-11 |
|
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: 64.12 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPD--NGLLRKEIQRH 146
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEalVPAVKKANAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 147 ERIVLLDEDIPGSQ--VPKVFADNVQGGRIATEKLIAA--GHRHIAFVGGPDKLMSVRERYQGFCTAMEQAglswPPEWV 222
Cdd:cd01536 81 IPVVAVDTDIDGGGdvVAFVGTDNYEAGKLAGEYLAEAlgGKGKVAILEGPPGSSTAIDRTKGFKEALKKY----PDIEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 223 M---YGDYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPeaLSLVGFDDANYA-------DFTqpr 292
Cdd:cd01536 157 VaeqPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRTGD--IKIVGVDGTPEAlkaikdgELD--- 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 694083976 293 iSTIRQPARELGRTAVHIMMRLLNDDPdIPAETRLPVE 330
Cdd:cd01536 232 -ATVAQDPYLQGYLAVEAAVKLLNGEK-VPKEILTPVT 267
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
147-322 |
3.94e-11 |
|
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: 62.67 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 147 ERIVLLDEDIPGSQVPKVFADNVQGGRIATEKLIAAGHRHIAFVGGPDkLMSVRERYQGFCTAMEQAGLSWPPEWVMYGD 226
Cdd:cd01391 90 ATSQDLSDKTLYKYFLSVVFSDTLGARLGLDIVKRKNWTYVAAIHGEG-LNSGELRMAGFKELAKQEGICIVASDKADWN 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 227 YQREFGQQALRHLFSQPVrPTAVFAASDYLVLGLLDGLRASGLQApeALSLVGFDDANYADFTQ-----PRISTIRQPAR 301
Cdd:cd01391 169 AGEKGFDRALRKLREGLK-ARVIVCANDMTARGVLSAMRRLGLVG--DVSVIGSDGWADRDEVGyeveaNGLTTIKQQKM 245
|
170 180
....*....|....*....|.
gi 694083976 302 ELGRTAVHIMMRLLNDDPDIP 322
Cdd:cd01391 246 GFGITAIKAMADGSQNMHEEV 266
|
|
| LacI |
pfam00356 |
Bacterial regulatory proteins, lacI family; |
12-56 |
8.29e-11 |
|
Bacterial regulatory proteins, lacI family;
Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 56.49 E-value: 8.29e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 694083976 12 LSDVAKLAGLSKATLSRYMNNSIVLPQDTIDRIETAIRELDYRGN 56
Cdd:pfam00356 2 IKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
69-327 |
2.63e-10 |
|
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: 60.00 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFttNRPDNGLLRKEIQRHER 148
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLI--NPTDSDAVSPAVEEANE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 ----IVLLDEDIPGSQVPKVFA-DNVQGGRIATEKLIAAGHR--HIAFVGGPDKLMSVRERYQGFCTAMEQ-------AG 214
Cdd:cd06323 79 agipVITVDRSVTGGKVVSHIAsDNVAGGEMAAEYIAKKLGGkgKVVELQGIPGTSAARERGKGFHNAIAKypkinvvAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 215 LSwppewvmyGDYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGlqaPEALSLVGFDDANYAdftQPRIS 294
Cdd:cd06323 159 QT--------ADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAG---RKDVIVVGFDGTPDA---VKAVK 224
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 694083976 295 ------TIRQPARELGRTAVHIMMRLLN-DDPD--IPAETRL 327
Cdd:cd06323 225 dgklaaTVAQQPEEMGAKAVETADKYLKgEKVPkkIPVPLKL 266
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
73-333 |
3.67e-10 |
|
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: 59.64 E-value: 3.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 73 VLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGL--LRKEIQRHERIV 150
Cdd:cd19967 5 IVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADADASIaaVKKAKDAGIPVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 151 LLDEDIP--GSQVPKVFADNVQGGRIATE---KLIAAGHRHIAFVGGPDKLMSvRERYQGFCTAMEQAglswpPEWVMYG 225
Cdd:cd19967 85 LIDREINaeGVAVAQIVSDNYQGAVLLAQyfvKLMGEKGLYVELLGKESDTNA-QLRSQGFHSVIDQY-----PELKMVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 226 DYQREFGQQ-ALR---HLFSQPVRPTAVFAASDYLVLGLLDGLRASGLqaPEALSLVGFDdanYADFTQPRIS------T 295
Cdd:cd19967 159 QQSADWDRTeAFEkmeSILQANPDIKGVICGNDEMALGAIAALKAAGR--AGDVIIVGFD---GSNDVRDAIKegkisaT 233
|
250 260 270
....*....|....*....|....*....|....*....
gi 694083976 296 IRQPARELGRTAVHIMMRLL-NDDPDIPAETRLPVEWIG 333
Cdd:cd19967 234 VLQPAKLIARLAVEQADQYLkGGSTGKEEKQLFDCVLIT 272
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
106-328 |
3.69e-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: 56.79 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 106 RNNPEKECQFIRWLDTCQVDGLLFTTNRPD--NGLLRKEIQRHERIVLLDEDIPGSQVpKVF--ADNVQGGRIATEKLIA 181
Cdd:cd06308 39 QGDAAKQIADIEDLIAQGVDLLIVSPNEADalTPVVKKAYDAGIPVIVLDRKVSGDDY-TAFigADNVEIGRQAGEYIAE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 182 A--GHRHIAFVGGPDKLMSVRERYQGFCTAMEQAglswPPEWVM---YGDYQREFGQQALRHLFSQPVRPTAVFAASDYL 256
Cdd:cd06308 118 LlnGKGNVVEIQGLPGSSPAIDRHKGFLEAIAKY----PGIKIVasqDGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEM 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 257 VLGLLDGLRASGLQAPeaLSLVGFD---DAN---------YADFTQPRIstirqparelGRTAVHIMMRLLNDDPdIPAE 324
Cdd:cd06308 194 ALGAYQALKKAGREKE--IKIIGVDglpEAGekavkdgilAATFLYPTG----------GKEAIEAALKILNGEK-VPKE 260
|
....
gi 694083976 325 TRLP 328
Cdd:cd06308 261 IVLP 264
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
97-327 |
4.70e-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: 56.46 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 97 GYSLVLCITRNNPEKECQFIRWLDTCQVDGLLF---TTNRPDNGLLR---KEIQrherIVLLDEDIPGS----QVPKVFA 166
Cdd:cd06309 29 GYELVYTDANQDQEKQINDIRDLIAQGVDAILIspiDATGWDPVLKEakdAGIP----VILVDRTIDGEdgslYVTFIGS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 167 DNVQGGRIATE---KLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQaglswPPEWVMY----GDYQREFGQQALRHL 239
Cdd:cd06309 105 DFVEEGRRAAEwlvKNYKGGKGNVVELQGTAGSSVAIDRSKGFREVIKK-----HPNIKIVasqsGNFTREKGQKVMENL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 240 F-SQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFD------------DANYADFTQPRistirqpareLGRT 306
Cdd:cd06309 180 LqAGPGDIDVIYAHNDDMALGAIQALKEAGLKPGKDVLVVGIDgqkdaleaikagELNATVECNPL----------FGPT 249
|
250 260
....*....|....*....|....
gi 694083976 307 AVHIMMRLLND---DPDIPAETRL 327
Cdd:cd06309 250 AFDTIAKLLAGekvPKLIIVEERL 273
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
70-330 |
1.06e-08 |
|
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic sugar-binding domain of uncharacterized transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes.
Pssm-ID: 380530 [Multi-domain] Cd Length: 275 Bit Score: 55.26 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 70 LGLVLPDITNPFFAELADAAEEAASASGY----SLVLCITRNNPEKECQFIRWLDTcQVDGLLFTTnrPDNGLLRKEIQR 145
Cdd:cd06307 2 FGFLLPSPENPFYELLRRAIEAAAAALRDrrvrLRIHFVDSLDPEALAAALRRLAA-GCDGVALVA--PDHPLVRAAIDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 146 -HER---IVLLDEDIPGS-QVPKVFADNVQGGRIATE---KLIAAGHRHIAFVGGPDKLMSVRERYQGFCTAMEQ--AGL 215
Cdd:cd06307 79 lAARgipVVTLVSDLPGSrRLAYVGIDNRAAGRTAAWlmgRFLGRRPGKVLVILGSHRFRGHEEREAGFRSVLRErfPDL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 216 SWPPEWVMYGDYQRefGQQALRHLFSQPVRPTAVFAASdYLVLGLLDGLRASGLQAPeaLSLVGFD--DANYADFTQPRI 293
Cdd:cd06307 159 TVLEVLEGLDDDEL--AYELLRELLARHPDLVGIYNAG-GGNEGIARALREAGRARR--VVFIGHEltPETRRLLRDGTI 233
|
250 260 270
....*....|....*....|....*....|....*...
gi 694083976 294 S-TIRQPARELGRTAVHIMMRLLNDDPDIPAETRLPVE 330
Cdd:cd06307 234 DaVIDQDPELQARRAIEVLLAHLGGKGPAPPQPPIPIE 271
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
69-337 |
1.10e-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: 380542 [Multi-domain] Cd Length: 278 Bit Score: 55.44 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGLLRKEIQRHER 148
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 IVLLDEDI---PGSQVPKVFADNVQGGRIATEKLIAA------GHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPP 219
Cdd:cd06319 81 IPVVIADIgtgGGDYVSYIISDNYDGGYQAGEYLAEAlkengwGGGSVGIIAIPQSRVNGQARTAGFEDALEEAGVEEVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 220 EWVMyGDYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQApeALSLVGFD--DANYADFTQPRIS-TI 296
Cdd:cd06319 161 LRQT-PNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRTG--DILVVGFDgdPEALDLIKDGKLDgTV 237
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 694083976 297 RQPARELGRTAVHIMMRLLNDDPDIPAETRLPVEWIGRDSI 337
Cdd:cd06319 238 AQQPFGMGARAVELAIQALNGDNTVEKEIYLPVLLVTSENV 278
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
164-327 |
2.50e-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: 54.20 E-value: 2.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 164 VFADNVQGGRIATE---KLIAAGHRHIAFVGGPDkLMSVRERYQGFCTAMEQAGlswPPEWVMYGDYQ--REFGQQALRH 238
Cdd:cd06322 99 VGTDNYAGGKLAGEyalKALLGGGGKIAIIDYPE-VESVVLRVNGFKEAIKKYP---NIEIVAEQPGDgrREEALAATED 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 239 LFSQPVRPTAVFAASDYLVLGLLDGLRASGLQ----------APEALSLVGFDDANYADFTQpristirQPAReLGRTAV 308
Cdd:cd06322 175 MLQANPDLDGIFAIGDPAALGALTAIESAGKEdkikvigfdgNPEAIKAIAKGGKIKADIAQ-------QPDK-IGQETV 246
|
170 180
....*....|....*....|..
gi 694083976 309 HIMMRLLN---DDPDIPAETRL 327
Cdd:cd06322 247 EAIVKYLAgetVEKEILIPPKL 268
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
68-327 |
4.65e-08 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 53.55 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 68 ETLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFttNRPDNGLLRKEIQRHE 147
Cdd:PRK10653 27 DTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILLI--NPTDSDAVGNAVKMAN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 148 R----IVLLDEDIP-GSQVPKVFADNVQGGRIA----TEKLiAAGHRHIAFVG--GPDklmSVRERYQGFCTAMEQAGL- 215
Cdd:PRK10653 105 QanipVITLDRGATkGEVVSHIASDNVAGGKMAgdfiAKKL-GEGAKVIQLEGiaGTS---AARERGEGFKQAVAAHKFn 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 216 ---SWPpewvmyGDYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGlqAPEALsLVGFD---DANYADFT 289
Cdd:PRK10653 181 vlaSQP------ADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG--KSDVM-VVGFDgtpDGIKAVNR 251
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 694083976 290 QPRISTIRQPARELGRTAVHIMMRLLND---DPDIPAETRL 327
Cdd:PRK10653 252 GKLAATIAQQPDQIGAIGVETADKVLKGekvEAKIPVDLKL 292
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
69-321 |
8.37e-08 |
|
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: 52.77 E-value: 8.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPD------NGLLRKE 142
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKalvpaiEAAIKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 143 IQrherIVLLDEDIPGSQ-VPKVFADNVQGGRIATEKLIA---AGHRhIAFVGGPDKLMSVRERYQGFCTAMEqAGLSWP 218
Cdd:cd19968 81 IP----VVTVDRRAEGAApVPHVGADNVAGGREVAKFVVDklpNGAK-VIELTGTPGSSPAIDRTKGFHEELA-AGPKIK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 219 PEWVMYGDYQREFGQQALRH-LFSQPVRPTAVFAASDYLVLGLLDGLRASGLQA-----------PEALSLVGFDDANya 286
Cdd:cd19968 155 VVFEQTGNFERDEGLTVMENiLTSLPGPPDAIICANDDMALGAIEAMRAAGLDLkkvkvigfdavPDALQAIKDGELY-- 232
|
250 260 270
....*....|....*....|....*....|....*
gi 694083976 287 dftqpriSTIRQPARELGRTAVHIMMRLLNDDPDI 321
Cdd:cd19968 233 -------ATVEQPPGGQARTALRILVDYLKDKKAP 260
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
71-316 |
1.76e-07 |
|
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: 51.54 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 71 GLVLPDITNPFFAELADAAEEAASASGY-SLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPD--NGLLRKEIQRHE 147
Cdd:pfam13407 2 GVVPKSTGNPFFQAAEEGAEEAAKELGGeVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTalAPVLKKAKDAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 148 RIVLLDEDIPGS-QVPKVFADNVQGGRIATEKLIAA--GHRHIAFVGGPDKLMSVRERYQGFctaMEQAGLSWP----PE 220
Cdd:pfam13407 82 PVVTFDSDAPSSpRLAYVGFDNEAAGEAAGELLAEAlgGKGKVAILSGSPGDPNANERIDGF---KKVLKEKYPgikvVA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 221 WVMYGDYQREFGQQALRHLFSQPVRPT-AVFAASDYLVLGLLDGLRASGLQAPEAlsLVGFDdanYADFTQPRI------ 293
Cdd:pfam13407 159 EVEGTNWDPEKAQQQMEALLTAYPNPLdGIISPNDGMAGGAAQALEAAGLAGKVV--VTGFD---ATPEALEAIkdgtid 233
|
250 260
....*....|....*....|...
gi 694083976 294 STIRQPARELGRTAVHIMMRLLN 316
Cdd:pfam13407 234 ATVLQDPYGQGYAAVELAAALLK 256
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
149-281 |
1.71e-06 |
|
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: 49.14 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 149 IVLLDEDIPGSQVPK--------------VFADNVQGGRIATEKLIAAGHRH--------IAFVGGPDKLMSVrERYQGF 206
Cdd:cd06324 85 VFLINNDLTDEERALlgkprekfkywlgsIVPDNEQAGYLLAKALIKAARKKsddgkirvLAISGDKSTPASI-LREQGL 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694083976 207 CTAMEQAG---LswppEWVMYGDYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQAPEALSLVGFD 281
Cdd:cd06324 164 RDALAEHPdvtL----LQIVYANWSEDEAYQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGLKPGKDVLVGGID 237
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
69-332 |
2.26e-06 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380533 [Multi-domain] Cd Length: 272 Bit Score: 48.49 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVL--CITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDN--GLLRKEIQ 144
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFvgPESEEDVAGQNSLLEELINKKPDAIVVAPLDSEDlvDPLKDAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 145 RHERIVLLDEDI-PGSQVPKVFADNVQGGRIATEKLIAA--GHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGLSWPPEW 221
Cdd:cd06310 81 KGIPVIVIDSGIkGDAYLSYIATDNYAAGRLAAQKLAEAlgGKGKVAVLSLTAGNSTTDQREEGFKEYLKKHPGGIKVLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 222 VMYGDYQREFGQQALRHLFSQpvRPTA--VFAASDYLVLGLLDGLRASGLQAPeaLSLVGFDDanyadfTQPRISTIR-- 297
Cdd:cd06310 161 SQYAGSDYAKAANETEDLLGK--YPDIdgIFATNEITALGAAVAIKSRKLSGQ--IKIVGFDS------QEELLDALKng 230
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 694083976 298 -------QPARELGRTAVHIMMRLLNDDPdIPAETRLPVEWI 332
Cdd:cd06310 231 kidalvvQNPYEIGYEGIKLALKLLKGEE-VPKNIDTGAELI 271
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
107-281 |
4.71e-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: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 107 NNPEKECQFIRWLDTCQVDGLLFT-TNRPD-NGLLRKEIQRHERIVLLDEDIPGSQVPKVFA-DNVQGGRIATEKLIAAG 183
Cdd:cd20004 41 DDVEAQIQIIEYFIDQGVDGIVLApLDRKAlVAPVERARAQGIPVVIIDSDLGGDAVISFVAtDNYAAGRLAAKRMAKLL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 184 H--------RHIAFVGgpdklmSVRERYQGFCTAMEQAGlswPPEWVM---YGDYQREFGQQALRHLFSQPVRPTAVFAA 252
Cdd:cd20004 121 NgkgkvallRLAKGSA------STTDRERGFLEALKKLA---PGLKVVddqYAGGTVGEARSSAENLLNQYPDVDGIFTP 191
|
170 180
....*....|....*....|....*....
gi 694083976 253 SDYLVLGLLDGLRASGLqaPEALSLVGFD 281
Cdd:cd20004 192 NESTTIGALRALRRLGL--AGKVKFIGFD 218
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
152-330 |
2.35e-05 |
|
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: 45.32 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 152 LDEDI---PGSQVPKVFADNVQGGRIATEKLIAA--GHRHIAFVGGPDKLMSVRERYQGFCTAMEQAGL----SWPPEWV 222
Cdd:cd19970 93 LDADAlkeGGINVPFVGPDNRQGAYLAGDYLAKKlgKGGKVAIIEGIPGADNAQQRKAGFLKAFEEAGMkivaSQSANWE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 223 MygdyqrEFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQapEALSLVGFDDANYAdftQPRI------STI 296
Cdd:cd19970 173 I------DEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKA--GKVLVVGFDNIPAV---RPLLkdgkmlATI 241
|
170 180 190
....*....|....*....|....*....|....
gi 694083976 297 RQPARELGRTAVHIMMRLLNDDpDIPAETRLPVE 330
Cdd:cd19970 242 DQHPAKQAVYGIEYALKMLNGE-EVPGWVKTPVE 274
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
97-316 |
1.47e-04 |
|
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: 42.79 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 97 GYSLVLC--ITRNNPekecqfirwLDTCQVDGLLFTTNRPDNGLLRKEIQRHERIVLLD-EDIPGSQVPKVFADNVQGGR 173
Cdd:cd06287 37 DLALVLVppLHHVSM---------LDALDVDGAIVVEPTVEDPILARLRQRGVPVVSIGrAPGTDEPVPYVDLQSAATAR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 174 IATEKLIAAGHRHIAFVGGPDKLMSVRER---YQGFCtameqAGLSWPPEWVMYGDYQREF-GQQALRHLFSQPVRPTAV 249
Cdd:cd06287 108 LLLEHLHGAGARQVALLTGSSRRNSSLESeaaYLRFA-----QEYGTTPVVYKVPESEGERaGYEAAAALLAAHPDIDAV 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694083976 250 FAASDYLVLGLLDGLRASGLQAPEALSLVGFDDANYADFTQPRISTIRQPARELGRTAVHIMMRLLN 316
Cdd:cd06287 183 CVPVDAFAVGAMRAARDSGRSVPEDLMVVTRYDGIRARTADPPLTAVDLHLDRVARTAIDLLFASLS 249
|
|
| PBP1_ABC_sugar_binding-like |
cd20007 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
69-328 |
2.67e-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: 380662 [Multi-domain] Cd Length: 271 Bit Score: 41.84 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRN-NPEKECQFIRWLDTCQVDGLLFTTNrpDNGLLRKEIQRHE 147
Cdd:cd20007 1 TIALVPGVTGDPFYITMQCGAEAAAKELGVELDVQGPPTfDPTLQTPIVNAVIAKKPDALLIAPT--DPQALIAPLKRAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 148 R----IV-----LLDEDIPGSQVPkvfADNVQGGRIATEKLIAAghrhiafVGGPDKLM---------SVRERYQGFCTA 209
Cdd:cd20007 79 DagikVVtvdttLGDPSFVLSQIA---SDNVAGGALAAEALAEL-------IGGKGKVLvinstpgvsTTDARVKGFAEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 210 MEQA-GLSWPPewVMYGDYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQapEALSLVGFD--DANYA 286
Cdd:cd20007 149 MKKYpGIKVLG--VQYSENDPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAGKT--GKVKVVGFDasPAQVE 224
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 694083976 287 DFTQPRIS-TIRQPARELGRTAVHIMMRLLNDDPdIPAETRLP 328
Cdd:cd20007 225 QLKAGTIDaLIAQKPAEIGYLAVEQAVAALTGKP-VPKDILTP 266
|
|
| HTH_XRE |
cd00093 |
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ... |
12-48 |
7.89e-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: 34.45 E-value: 7.89e-03
10 20 30
....*....|....*....|....*....|....*..
gi 694083976 12 LSDVAKLAGLSKATLSRYMNNSIVLPQDTIDRIETAI 48
Cdd:cd00093 15 QEELAEKLGVSRSTISRIENGKRNPSLETLEKLAKAL 51
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
69-328 |
8.20e-03 |
|
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380541 [Multi-domain] Cd Length: 282 Bit Score: 37.39 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 69 TLGLVLPDITNPFFAELADAAEEAASASGYSLVLCITRNNPEKECQFIRWLDTCQVDGLLFTTNRPDNGL--LRKEIQRH 146
Cdd:cd06318 1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTpaVKAAKAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 147 ERIVLLDEDIPGSQVPKVF--ADNVQGGRIATEKLIAA-GHRHIAFV---GGPDKLMSvRERYQGFCTAMEQAGLSWPPE 220
Cdd:cd06318 81 IPVITVDSALDPSANVATQvgRDNKQNGVLVGKEAAKAlGGDPGKIIelsGDKGNEVS-RDRRDGFLAGVNEYQLRKYGK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694083976 221 WVM------YGDYQREFGQQALRHLFSQPVRPTAVFAASDYLVLGLLDGLRASGLQapEALSLVGFD----------DAN 284
Cdd:cd06318 160 SNIkvvaqpYGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGML--DKVKVAGADgqkealklikDGK 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 694083976 285 YadftqprISTIRQPARELGRTAVHIMMRLLNDDPDIPAETRLP 328
Cdd:cd06318 238 Y-------VATGLNDPDLLGKTAVDTAAKVVKGEESFPEFTYTP 274
|
|
| |
