|
Name |
Accession |
Description |
Interval |
E-value |
| ccpA |
TIGR01481 |
catabolite control protein A; Catabolite control protein A is a LacI family global ... |
2-331 |
2.78e-176 |
|
catabolite control protein A; Catabolite control protein A is a LacI family global transcriptional regulator found in Gram-positive bacteria. CcpA is involved in repressing carbohydrate utilization genes [ex: alpha-amylase (amyE), acetyl-coenzyme A synthase (acsA)] and in activating genes involved in transporting excess carbon from the cell [ex: acetate kinase (ackA), alpha-acetolactate synthase (alsS)]. Additionally, disruption of CcpA in Bacillus megaterium, Staphylococcus xylosus, Lactobacillus casei and Lactocacillus pentosus also decreases growth rate, which suggests CcpA is involved in the regulation of other metabolic pathways. [Regulatory functions, DNA interactions]
Pssm-ID: 130546 [Multi-domain] Cd Length: 329 Bit Score: 491.61 E-value: 2.78e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 2 SVTIYDVAREAGVSMATVSRVVNGNPNVKPATRKKVLEVIERLGYRPNAVARGLASKKTTTVGVIIPDIASAFYAELARG 81
Cdd:TIGR01481 1 TVTIYDVAREAGVSMATVSRVVNGNPNVKPATRKKVLEVIKRLDYRPNAVARGLASKRTTTVGVIIPDISNIYYAELARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 82 IEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVPVVLATTIDPGCQLPSVNIDQ 161
Cdd:TIGR01481 81 IEDIATMYKYNIILSNSDEDPEKEVQVLNTLLSKQVDGIIFMGGTITEKLREEFSRSPVPVVLAGTVDKENELPSVNIDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 162 RQAAYDATRLLLNHGHTRIAFLGGPLEEFA-GLSRFQGYRQALEDAGVPFREELVQIADYRYETALKRMAHFLTLpeRPT 240
Cdd:TIGR01481 161 KQATKEAVGELIAKGHKSIAFVGGPLSDSInGEDRLEGYKEALNKAGIQFGEDLVCEGKYSYDAGYKAFAELKGS--LPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 241 AVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVSMRLLTKYMHNEKVTDSLVFL 320
Cdd:TIGR01481 239 AVFVASDEMAAGILNAAMDAGIKVPEDLEVITSNNTRLTEMVRPQLSTIIQPLYDIGAVAMRLLTKYMNDEELEEKTVVL 318
|
330
....*....|.
gi 1900939922 321 PHTIEIRGSTR 331
Cdd:TIGR01481 319 PHGIELRGSTK 329
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
3-332 |
1.02e-146 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 416.91 E-value: 1.02e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 3 VTIYDVAREAGVSMATVSRVVNGNPNVKPATRKKVLEVIERLGYRPNAVARGLASKKTTTVGVIIPDIASAFYAELARGI 82
Cdd:COG1609 4 VTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLRGI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 83 EDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVPVVLATTIDPGCQLPSVNIDQR 162
Cdd:COG1609 84 EEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRPLPDPGVPSVGVDNR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 163 QAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIADYRYETALKRMAHFLTLPERPTAV 242
Cdd:COG1609 164 AGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGPRPTAI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 243 FATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVSMRLLTKYMHNEKVTDSLVFLPH 322
Cdd:COG1609 244 FCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERVLLPP 323
|
330
....*....|
gi 1900939922 323 TIEIRGSTRA 332
Cdd:COG1609 324 ELVVRESTAP 333
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
62-329 |
7.15e-129 |
|
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: 369.31 E-value: 7.15e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVP 141
Cdd:cd06298 1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMGDELTEEIREEFKRSPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFA-GLSRFQGYRQALEDAGVPFREELVQIADY 220
Cdd:cd06298 81 VVLAGTVDSDHEIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSGPLKEYInNDKKLQGYKRALEEAGLEFNEPLIFEGDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 221 RYETALKRMAHFLTLpERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVS 300
Cdd:cd06298 161 DYDSGYELYEELLES-GEPDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPLYDIGAVA 239
|
250 260
....*....|....*....|....*....
gi 1900939922 301 MRLLTKYMHNEKVTDSLVFLPHTIEIRGS 329
Cdd:cd06298 240 MRLLTKLMNKEEVEETIVKLPHSIIWRQS 268
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
62-329 |
1.19e-118 |
|
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: 343.38 E-value: 1.19e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVP 141
Cdd:cd19975 1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFASGTLTEENKQLLKNMNIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEF-AGLSRFQGYRQALEDAGVPFREELVQIADY 220
Cdd:cd19975 81 VVLVSTESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISGPLDDPnAGYPRYEGYKKALKDAGLPIKENLIVEGDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 221 RYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVS 300
Cdd:cd19975 161 SFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQPFYEMGKKA 240
|
250 260
....*....|....*....|....*....
gi 1900939922 301 MRLLTKYMHNEKVTDSLVFLPHTIEIRGS 329
Cdd:cd19975 241 VELLLDLIKNEKKEEKSIVLPHQIIERES 269
|
|
| PBP1_LacI_sugar_binding-like |
cd06267 |
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ... |
62-324 |
1.76e-106 |
|
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily; Ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily. In most cases, ligands are monosaccharide including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the domain sugar binding changes the DNA binding activity of the repressor domain.
Pssm-ID: 380491 [Multi-domain] Cd Length: 264 Bit Score: 312.14 E-value: 1.76e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVP 141
Cdd:cd06267 1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLAAGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIADYR 221
Cdd:cd06267 81 VVLIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLSTSRERLEGYRDALAEAGLPVDPELVVEGDFS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 222 YETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVSM 301
Cdd:cd06267 161 EESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEMGRAAA 240
|
250 260
....*....|....*....|...
gi 1900939922 302 RLLTKYMHNEKVTDSLVFLPHTI 324
Cdd:cd06267 241 ELLLERIEGEEEPPRRIVLPTEL 263
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
62-329 |
2.06e-103 |
|
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: 304.46 E-value: 2.06e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLfRSASVP 141
Cdd:cd06284 1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILLSGRLDAELLSE-LSKRYP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIADYR 221
Cdd:cd06284 80 IVQCCEYIPDSGVPSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDNVYARERLEGYRRALAEAGLPVDEDLIIEGDFS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 222 YETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVSM 301
Cdd:cd06284 160 FEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIGETAA 239
|
250 260
....*....|....*....|....*...
gi 1900939922 302 RLLTKYMHNEKVTDSLVFLPHTIEIRGS 329
Cdd:cd06284 240 ELLLEKIEGEGVPPEHIILPHELIVRES 267
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-330 |
3.96e-85 |
|
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: 257.92 E-value: 3.96e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVP 141
Cdd:cd06285 1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQELAARGVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIADYR 221
Cdd:cd06285 81 VVLVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDERIVPGGFT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 222 YETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVSM 301
Cdd:cd06285 161 IEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEMGRRAA 240
|
250 260
....*....|....*....|....*....
gi 1900939922 302 RLLTKYMHNEKVTDSLVFLPHTIEIRGST 330
Cdd:cd06285 241 ELLLQLIEGGGRPPRSITLPPELVVREST 269
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
62-327 |
8.75e-82 |
|
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: 249.48 E-value: 8.75e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVP 141
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGPSRELKRLLKHGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIADYR 221
Cdd:cd06280 81 IVLIDREVEGLELDLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEISTTRERLAGYREALAEAGIPVDESLIFEGDST 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 222 YETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVSM 301
Cdd:cd06280 161 IEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQPAYEIGRIAA 240
|
250 260
....*....|....*....|....*.
gi 1900939922 302 RLLTKYMHNEKVTDSLVFLPHTIEIR 327
Cdd:cd06280 241 QLLLERIEGQGEEPRRIVLPTELIIR 266
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
62-329 |
1.02e-81 |
|
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: 249.10 E-value: 1.02e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRS-ASV 140
Cdd:cd06275 1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAELLAAlRSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 141 PVVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIADY 220
Cdd:cd06275 81 PVVVLDREIAGDNADAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSVSRERLAGFRRALAEAGIEVPPSWIVEGDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 221 RYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVS 300
Cdd:cd06275 161 EPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQPKDELGELA 240
|
250 260 270
....*....|....*....|....*....|
gi 1900939922 301 MRLLTKYM-HNEKVTDSLVFLPHTIEiRGS 329
Cdd:cd06275 241 VELLLDRIeNKREEPQSIVLEPELIE-RES 269
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
62-312 |
4.43e-81 |
|
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: 247.44 E-value: 4.43e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLfMGPrvTDEHLDLFRS---A 138
Cdd:cd19977 1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGII-IAP--TGGNEDLIEKlvkS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 139 SVPVVLattID---PGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELV 215
Cdd:cd19977 78 GIPVVF---VDryiPGLDVDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLELSTRQERLEGYKAALADHGLPVDEELI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 216 QIADYRyETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYD 295
Cdd:cd19977 155 KHVDRQ-DDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQPTYE 233
|
250
....*....|....*..
gi 1900939922 296 IGAVSMRLLTKYMHNEK 312
Cdd:cd19977 234 IGRKAAELLLDRIENKP 250
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
62-329 |
5.31e-81 |
|
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: 247.46 E-value: 5.31e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYA-ELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLF--MGPRVTDEHLDLfrsA 138
Cdd:cd06288 1 TIGLITDDIATTPFAgDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYasMHHREVTLPPEL---T 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 139 SVPVVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIA 218
Cdd:cd06288 78 DIPLVLLNCFDDDPSLPSVVPDDEQGGYLATRHLIEAGHRRIAFIGGPEDSLATRLRLAGYRAALAEAGIPYDPSLVVHG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 219 DYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGA 298
Cdd:cd06288 158 DWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVALPYYEMGR 237
|
250 260 270
....*....|....*....|....*....|.
gi 1900939922 299 VSMRLLTKYMHNEKVTDSLVFLPHTIEIRGS 329
Cdd:cd06288 238 RAAELLLDGIEGEPPEPGVIRVPCPLIERES 268
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
62-329 |
5.05e-80 |
|
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: 244.85 E-value: 5.05e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLD-LFRSASV 140
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNISDEAIIkLLKEEKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 141 PVV-LATTIDPGcQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIAD 219
Cdd:cd19976 81 PVVvLDRYIEDN-DSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGPPSTYNEHERIEGYKNALQDHNLPIDESWIYSGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 220 YRYETAlKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAV 299
Cdd:cd19976 160 SSLEGG-YKAAEELLKSKNPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQPIFEMGQE 238
|
250 260 270
....*....|....*....|....*....|
gi 1900939922 300 SMRLLTKYMHNEKVTDSLVFLPHTIEIRGS 329
Cdd:cd19976 239 AAKLLLKIIKNPAKKKEEIVLPPELIKRDS 268
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
29-332 |
6.27e-80 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 246.06 E-value: 6.27e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 29 VKPATRKKVLEVIERLGYRPNAVARGLASKKTTTVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTL 108
Cdd:PRK11041 4 VSQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 109 IETLLEKQVDGLLFMGPRV-----TDEHLDLfrsasVPVVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFL 183
Cdd:PRK11041 84 VNLIITKQIDGMLLLGSRLpfdasKEEQRNL-----PPMVMANEFAPELELPTVHIDNLTAAFEAVNYLHELGHKRIACI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 184 GGPleEFAGLSRF--QGYRQALEDAGVPFREELVQIADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAG 261
Cdd:PRK11041 159 AGP--EEMPLCHYrlQGYVQALRRCGITVDPQYIARGDFTFEAGAKALKQLLDLPQPPTAVFCHSDVMALGALSQAKRMG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1900939922 262 FRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVSMRLLTKYMHNEKVTDSLVFLPHTIEIRGSTRA 332
Cdd:PRK11041 237 LRVPQDLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSSGSRLLDCELIIRGSTAA 307
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
62-321 |
7.26e-80 |
|
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: 244.35 E-value: 7.26e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLfMGPRVTDEhlDLFRSASVP 141
Cdd:cd06291 1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGII-LGSHSLDI--EEYKKLNIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VVlatTID--PGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIAD 219
Cdd:cd06291 78 IV---SIDryLSEGIPSVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIEIDEND 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 220 YRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAV 299
Cdd:cd06291 155 FSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIEEMAKE 234
|
250 260
....*....|....*....|..
gi 1900939922 300 SMRLLTKYMHNEKVTDSLVFLP 321
Cdd:cd06291 235 AVELLLKLIEGEEIEESRIVLP 256
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
7-329 |
2.39e-79 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 245.38 E-value: 2.39e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 7 DVAREAGVSMATVSRVVNGNPNVKPATRKKVLEVIERLGYRPNAVARGLASKKTTTVGVIIPDIASAFYAELARGIEDIA 86
Cdd:PRK10423 3 DVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVERSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 87 NMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMgprVTDEHLD----LFRSASVPVVLA--TTIDPGCQLPSVNid 160
Cdd:PRK10423 83 FERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLL---CTETHQPsreiMQRYPSVPTVMMdwAPFDGDSDLIQDN-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 161 QRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIADYRYETALKRMAHFLTLPERPT 240
Cdd:PRK10423 158 SLLGGDLATQYLIDKGYTRIACITGPLDKTPARLRLEGYRAAMKRAGLNIPDGYEVTGDFEFNGGFDAMQQLLALPLRPQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 241 AVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVSMRLLTKYMHN-EKVTDSLVF 319
Cdd:PRK10423 238 AVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQpTLQQQRLQL 317
|
330
....*....|
gi 1900939922 320 LPHTIEiRGS 329
Cdd:PRK10423 318 TPELME-RGS 326
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
62-325 |
3.08e-77 |
|
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: 237.80 E-value: 3.08e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVP 141
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEELILIAEKIPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIADYR 221
Cdd:cd06270 81 LVVINRYIPGLADRCVWLDNEQGGRLAAEHLLDLGHRRIACITGPLDIPDARERLAGYRDALAEAGIPLDPSLIIEGDFT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 222 YETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVSM 301
Cdd:cd06270 161 IEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHYPIEEMAQAAA 240
|
250 260
....*....|....*....|....
gi 1900939922 302 RLLTKYMHNEKVTDSLVFLPHTIE 325
Cdd:cd06270 241 ELALNLAYGEPLPISHEFTPTLIE 264
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-329 |
2.08e-76 |
|
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: 235.59 E-value: 2.08e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFrSASVP 141
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEELLKLL-AEGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIADYR 221
Cdd:cd06290 80 VVLVDRELEGLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDHPDAQERYAGYRRALEDAGLEVDPRLIVEGDFT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 222 YETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVSM 301
Cdd:cd06290 160 EESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYEMGKTAA 239
|
250 260
....*....|....*....|....*...
gi 1900939922 302 RLLTKYMHNEKVTDSLVFLPHTIEIRGS 329
Cdd:cd06290 240 EILLELIEGKGRPPRRIILPTELVIRES 267
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
4-326 |
5.63e-72 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 226.91 E-value: 5.63e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 4 TIYDVAREAGVSMATVSRVVNGNPNVKPATRKKVLEVIERLGYRPNAVARGLASKKTTTVGVIIPDIASAFYAELARGIE 83
Cdd:PRK10703 3 TIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEAVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 84 DIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRS-ASVPVVLattIDPGCQLPSVN---I 159
Cdd:PRK10703 83 KNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLLAMLEEyRHIPMVV---MDWGEAKADFTdaiI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 160 DQR-QAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIADYRYETALKRMAHFLTLPER 238
Cdd:PRK10703 160 DNAfEGGYLAGRYLIERGHRDIGVIPGPLERNTGAGRLAGFMKAMEEANIKVPEEWIVQGDFEPESGYEAMQQILSQKHR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 239 PTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVSMRLLTKYMhNEKVTDslv 318
Cdd:PRK10703 240 PTAVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRI-VNKREE--- 315
|
....*...
gi 1900939922 319 flPHTIEI 326
Cdd:PRK10703 316 --PQTIEV 321
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
62-329 |
2.12e-69 |
|
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. The SalR binds to glucose based compound Salicin which is chemically related to aspirin. The ligand-binding of SalR is structurally homologous to the periplasmic sugar-binding domain of ABC-transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380487 [Multi-domain] Cd Length: 270 Bit Score: 217.81 E-value: 2.12e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIIL--CNSDkQPKKELTLIETLLEKQVDGLLFMgPRVTDEH--LDLFRS 137
Cdd:cd01545 1 LIGLLYDNPSASYVSALQVGALRACREAGYHLVVepCDSD-DEDLADRLRRFLSRSRPDGVILT-PPLSDDPalLDALDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 138 ASVPVVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQI 217
Cdd:cd01545 79 LGIPYVRIAPGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGPPDHGASAERLEGFRDALAEAGLPLDPDLVVQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 218 ADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIG 297
Cdd:cd01545 159 GDFTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTTVRQPIAEMA 238
|
250 260 270
....*....|....*....|....*....|..
gi 1900939922 298 AVSMRLLTKYMHNEKVTDSLVFLPHTIEIRGS 329
Cdd:cd01545 239 RRAVELLIAAIRGAPAGPERETLPHELVIRES 270
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-329 |
2.25e-69 |
|
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: 217.91 E-value: 2.25e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVP 141
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSHLARLRARGTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIADYR 221
Cdd:cd06293 81 VVLLDRPAPGPAGCSVSVDDVQGGALAVDHLLELGHRRIAFVSGPLRTRQVAERLAGARAAVAEAGLDPDEVVRELSAPD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 222 YETALKR--MAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAV 299
Cdd:cd06293 161 ANAELGRaaAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQPSYELGRA 240
|
250 260 270
....*....|....*....|....*....|
gi 1900939922 300 SMRLLTKYMHNEKVTDSLVFLPHTIEIRGS 329
Cdd:cd06293 241 AADLLLDEIEGPGHPHEHVVFQPELVVRSS 270
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-329 |
3.33e-65 |
|
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: 206.98 E-value: 3.33e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVP 141
Cdd:cd06273 1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVGSDHDPELFELLEQRQVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEE-FAGLSRFQGYRQALEDAGVPFREELVQIADY 220
Cdd:cd06273 81 YVLTWSYDEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGnDRARARLAGIRDALAERGLELPEERVVEAPY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 221 RYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVS 300
Cdd:cd06273 161 SIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPAREIGELA 240
|
250 260
....*....|....*....|....*....
gi 1900939922 301 MRLLTKYMHNEKVTDSLVfLPHTIEIRGS 329
Cdd:cd06273 241 ARYLLALLEGGPPPKSVE-LETELIVRES 268
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-324 |
1.81e-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: 380505 [Multi-domain] Cd Length: 267 Bit Score: 205.21 E-value: 1.81e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGL-LFMGPRVTDEHLDLFRSASV 140
Cdd:cd06282 1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLiLTVGDAQGSEALELLEEEGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 141 PVVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEefagLS-----RFQGYRQALEDAGVPFREeLV 215
Cdd:cd06282 81 PYVLLFNQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAGDFS----ASdrarlRYQGYRDALKEAGLKPIP-IV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 216 QIADYRYETALKRMAHFLTlPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYD 295
Cdd:cd06282 156 EVDFPTNGLEEALTSLLSG-PNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQPSRD 234
|
250 260
....*....|....*....|....*....
gi 1900939922 296 IGAVSMRLLTKYMHNEKVTDSLVfLPHTI 324
Cdd:cd06282 235 MGRAAADLLLAEIEGESPPTSIR-LPHHL 262
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
62-330 |
4.41e-63 |
|
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: 201.74 E-value: 4.41e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVP 141
Cdd:cd06296 1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQLRLLRSAGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VVL---ATTIDPGcqLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIA 218
Cdd:cd06296 81 FVLidpVGEPDPD--LPSVGATNWAGGRLATEHLLDLGHRRIAVITGPPRSVSGRARLAGYRAALAEAGIAVDPDLVREG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 219 DYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGA 298
Cdd:cd06296 159 DFTYEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVHQPLREMGA 238
|
250 260 270
....*....|....*....|....*....|..
gi 1900939922 299 VSMRLLTKYMHNEKVTDSLVFLPHTIEIRGST 330
Cdd:cd06296 239 VAVRLLLRLLEGGPPDARRIELATELVVRGST 270
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
62-329 |
4.12e-62 |
|
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: 199.04 E-value: 4.12e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVP 141
Cdd:cd06299 1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVPTGENSEGLQALIAQGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VVLAT-TIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIADY 220
Cdd:cd06299 81 VVFVDrEVEGLGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYISGPLSTSTGRERLAAFRAALTAAGIPIDEELVAFGDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 221 RYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVS 300
Cdd:cd06299 161 RQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVERIGRRA 240
|
250 260
....*....|....*....|....*....
gi 1900939922 301 MRLLTKYMHNEKVTDSLVfLPHTIEIRGS 329
Cdd:cd06299 241 VELLLALIENGGRATSIR-VPTELIPRES 268
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
62-324 |
1.55e-61 |
|
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: 197.42 E-value: 1.55e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASA-----FYAELARGIEDIANMYKYNIIL--CNSDKQPKKE-LTLIEtllEKQVDGLLFMGPRVTDEHLD 133
Cdd:cd06294 1 TIGLVLPSSAEElfqnpFFSEVLRGISQVANENGYSLLLatGNTEEELLEEvKRMVR---GRRVDGFILLYSKEDDPLIE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 134 LFRSASVPVVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREE 213
Cdd:cd06294 78 YLKEEGFPFVVIGKPLDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVSIDRLQGYKQALKEAGLPLDDD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 214 LVQIADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPM 293
Cdd:cd06294 158 YILLLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSVDINP 237
|
250 260 270
....*....|....*....|....*....|.
gi 1900939922 294 YDIGAVSMRLLTKYMHNEKVTDSLVFLPHTI 324
Cdd:cd06294 238 YELGREAAKLLINLLEGPESLPKNVIVPHEL 268
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
62-330 |
2.40e-61 |
|
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: 197.11 E-value: 2.40e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDI----ASAFYAELARGIEDIANMYKYNIILCNSDKQPKkELTLIETLLE-KQVDGLLFMGPRVTDEHLDLFR 136
Cdd:cd06292 1 LIGYVVPELpggfSDPFFDEFLAALGHAAAARGYDVLLFTASGDED-EIDYYRDLVRsRRVDGFVLASTRHDDPRVRYLH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 137 SASVPVVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQ 216
Cdd:cd06292 80 EAGVPFVAFGRANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPEGSVPSDDRLAGYRAALEEAGLPFDPGLVV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 217 IADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDI 296
Cdd:cd06292 160 EGENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTVRQPIDEI 239
|
250 260 270
....*....|....*....|....*....|....
gi 1900939922 297 GAVSMRLLTKYMHNEKVTDSLVFLPHTIEIRGST 330
Cdd:cd06292 240 GRAVVDLLLAAIEGNPSEPREILLQPELVVRESS 273
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
3-301 |
7.46e-61 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 198.46 E-value: 7.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 3 VTIYDVAREAGVSMATVSRVVNGNPNVKPATRKKVLEVIERLGYRPNAVARGLASKKTTTVGVIIPDIASAFYAELARGI 82
Cdd:PRK10401 2 ITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 83 EDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVPVVLATTIDPGCQLPSVNIDQR 162
Cdd:PRK10401 82 DLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDQIPGMVLINRVVPGYAHRCVCLDNV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 163 QAAYDATRLLLNHGHTRIAFLGG--PLEEFAglSRFQGYRQALEDAGVPFREELVQIADYRYETALKRMAHFLTLPERPT 240
Cdd:PRK10401 162 SGARMATRMLLNNGHQRIGYLSSshGIEDDA--MRRAGWMSALKEQGIIPPESWIGTGTPDMQGGEAAMVELLGRNLQLT 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1900939922 241 AVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMydigaVSM 301
Cdd:PRK10401 240 AVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPI-----ASM 295
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
62-313 |
1.66e-60 |
|
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: 194.64 E-value: 1.66e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVP 141
Cdd:cd01542 1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEITDEHRKALKKLKIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VVLATTIDPGCqlPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFA-GLSRFQGYRQALEDAGVPfrEELVQIADY 220
Cdd:cd01542 81 VVVLGQEHEGF--SCVYHDDYGAGKLLGEYLLKKGHKNIAYIGVDEEDIAvGVARKQGYLDALKEHGID--EVEIVETDF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 221 RYETALKRMAHFLTlPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVS 300
Cdd:cd01542 157 SMESGYEAAKELLK-ENKPDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEAGEKA 235
|
250
....*....|...
gi 1900939922 301 MRLLTKYMHNEKV 313
Cdd:cd01542 236 AELLLDMIEGEKV 248
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
62-304 |
5.68e-60 |
|
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: 193.55 E-value: 5.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMG-PRVTDEHLDLFRSASV 140
Cdd:cd06289 1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPaAGTTAELLRRLKAWGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 141 PVVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIADY 220
Cdd:cd06289 81 PVVLALRDVPGSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLSDSSTRRERLAGFRAALAEAGLPLDESLIVPGPA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 221 RYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVS 300
Cdd:cd06289 161 TREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHPREIGRRA 240
|
....
gi 1900939922 301 MRLL 304
Cdd:cd06289 241 ARLL 244
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
1-337 |
2.83e-58 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 191.36 E-value: 2.83e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 1 MSVTIYDVAREAGVSMATVSRVVNGNPNVKPATRKKVLEVIERLGYRPNAVARGLASKKTTTVGVIIPDIASAFYAELAR 80
Cdd:PRK09526 4 KPVTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTSLALHAPSQIAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 81 GIEDIANMYKYNIILCNSDKQPKKELTL-IETLLEKQVDGLLFMGPRVTDEHLDLFRSASVPVVLATTIDPGCQLPSVNI 159
Cdd:PRK09526 84 AIKSRADQLGYSVVISMVERSGVEACQAaVNELLAQRVSGVIINVPLEDADAEKIVADCADVPCLFLDVSPQSPVNSVSF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 160 DQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVpfreELVQIA--DYRYETALKRMAHFLTLPE 237
Cdd:PRK09526 164 DPEDGTRLGVEHLVELGHQRIALLAGPESSVSARLRLAGWLEYLTDYQL----QPIAVRegDWSAMSGYQQTLQMLREGP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 238 RPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVSMRLLTKYMHNEKVTDSL 317
Cdd:PRK09526 240 VPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLLALSQGQAVKGSQ 319
|
330 340
....*....|....*....|
gi 1900939922 318 VfLPHTIEIRGSTRAESKTA 337
Cdd:PRK09526 320 L-LPTSLVVRKSTAPPNTQT 338
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
62-329 |
3.31e-58 |
|
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: 188.94 E-value: 3.31e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCN-SDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASV 140
Cdd:cd01574 1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATvDEDDPASVREALDRLLSQRVDGIIVIAPDEAVLEALRRLPPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 141 PVVLATTiDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPfrEELVQIADY 220
Cdd:cd01574 81 PVVIVGS-GPSPGVPTVSIDQEEGARLATRHLLELGHRRIAHIAGPLDWVDARARLRGWREALEEAGLP--PPPVVEGDW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 221 RYETALKRMAHFLTLPeRPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVS 300
Cdd:cd01574 158 SAASGYRAGRRLLDDG-PVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDFAELGRRA 236
|
250 260
....*....|....*....|....*....
gi 1900939922 301 MRLLTKYMHNEKVTDSLVFLPHTIEIRGS 329
Cdd:cd01574 237 VELLLALIEGPAPPPESVLLPPELVVRES 265
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
62-329 |
6.76e-58 |
|
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: 188.09 E-value: 6.76e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVP 141
Cdd:cd01575 1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEHTPATRKLLRAAGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VV-----LATTIDPgcqlpSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFA-GLSRFQGYRQALEDAGVPFREELV 215
Cdd:cd01575 81 VVetwdlPDDPIDM-----AVGFSNFAAGRAMARHLIERGYRRIAFVGARLDGDSrARQRLEGFRDALAEAGLPLPLVLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 216 QIADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYD 295
Cdd:cd01575 156 VELPSSFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVRVPRYE 235
|
250 260 270
....*....|....*....|....*....|....
gi 1900939922 296 IGAVSMRLLTKYMHNEKVTDSLVFLPHTIEIRGS 329
Cdd:cd01575 236 IGRKAAELLLARLEGEEPEPRVVDLGFELVRRES 269
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
62-329 |
1.12e-56 |
|
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: 185.07 E-value: 1.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVT--DEHLDLFR--- 136
Cdd:cd01541 1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEPTKSAlpNPNLDLYEelq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 137 SASVPVVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLggpleeFA-----GLSRFQGYRQALEDAGVPFR 211
Cdd:cd01541 81 KKGIPVVFINSYYPELDAPSVSLDDEKGGYLATKHLIDLGHRRIAGI------FKsddlqGVERYQGFIKALREAGLPID 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 212 EELV---QIADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTT 288
Cdd:cd01541 155 DDRIlwySTEDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEPPLTS 234
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1900939922 289 VAQPMYDIGAVSMRLLTKYMHNEKVTDSLVFLPhTIEIRGS 329
Cdd:cd01541 235 VVHPKEELGRKAAELLLRMIEEGRKPESVIFPP-ELIERES 274
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
62-327 |
2.43e-55 |
|
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: 181.20 E-value: 2.43e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLlFMGPRVTDEHLDLFRSASVP 141
Cdd:cd06286 1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGL-IITSRENDWEVIEPYAKYGP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VVL-ATTIDPgcQLPSVNIDQRQAAYDATRLLLNHGHTRIAF-LGGPLEE-FAGLSRFQGYRQALEDAGVPFREELVQIA 218
Cdd:cd06286 80 IVLcEETDSP--DIPSVYIDRYEAYLEALEYLKEKGHRKIGYcLGRPESSsASTQARLKAYQDVLGEHGLSLREEWIFTN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 219 DYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMvrPTLTTVAQPMYDIGA 298
Cdd:cd06286 158 CHTIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISEL--LNLTTIDQPLEEMGK 235
|
250 260
....*....|....*....|....*....
gi 1900939922 299 VSMRLLTKYMHNEKVTDslVFLPHTIEIR 327
Cdd:cd06286 236 EAFELLLSQLESKEPTK--KELPSKLIER 262
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-329 |
3.27e-55 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380501 [Multi-domain] Cd Length: 266 Bit Score: 181.19 E-value: 3.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDkQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVP 141
Cdd:cd06278 1 LVGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVD-DEDDVDDALRQLLQYRVDGVIVTSATLSSELAEECARRGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVqiADYR 221
Cdd:cd06278 80 VVLFNRVVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPEGTSTSRERERGFRAALAELGLPPPAVEA--GDYS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 222 YETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAY-QDAGFRVPEDVEVIGFDNIRLASmvRPT--LTTVAQPMYDIGA 298
Cdd:cd06278 158 YEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAArQEGGLVVPEDISVVGFDDIPMAA--WPSydLTTVRQPIEEMAE 235
|
250 260 270
....*....|....*....|....*....|.
gi 1900939922 299 VSMRLLTKYMHNEKVTDSLVFLPHTIEIRGS 329
Cdd:cd06278 236 AAVDLLLERIENPETPPERRVLPGELVERGS 266
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
73-329 |
9.40e-53 |
|
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: 175.02 E-value: 9.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 73 AFYAELARGIEDIANMYKYNIILCNSDKQpkkeltlIETLLEKQVDGLLFMGpRVTDEHLDLFRSASVPVVLATTIDPGC 152
Cdd:cd01544 17 PYYLSIRLGIEKEAKKLGYEIKTIFRDDE-------DLESLLEKVDGIIAIG-KFSKEEIEKLKKLNPNIVFVDSNPDPD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 153 QLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGG---------PLEEfaglSRFQGYRQALEDAGvPFREELVQIADYRYE 223
Cdd:cd01544 89 GFDSVVPDFEQAVRQALDYLIELGHRRIGFIGGkeytsddgeEIED----PRLRAFREYMKEKG-LYNEEYIYIGEFSVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 224 TALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVSMRL 303
Cdd:cd01544 164 SGYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTPPLTTVHIPTEEMGRTAVRL 243
|
250 260
....*....|....*....|....*.
gi 1900939922 304 LTKYMHNEKVTDSLVFLPHTIEIRGS 329
Cdd:cd01544 244 LLERINGGRTIPKKVLLPTKLIERES 269
|
|
| PRK10727 |
PRK10727 |
HTH-type transcriptional regulator GalR; |
4-293 |
4.79e-52 |
|
HTH-type transcriptional regulator GalR;
Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 175.33 E-value: 4.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 4 TIYDVAREAGVSMATVSRVVNGNPNVKPATRKKVLEVIERLGYRPNAVARGLASKKTTTVGVIIPDIASAFYAELARGIE 83
Cdd:PRK10727 3 TIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKAVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 84 DIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVPVVLATTIDPGCQLPSVNIDQRQ 163
Cdd:PRK10727 83 QVAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVVHAKMIPDAELASLMKQIPGMVLINRILPGFENRCIALDDRY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 164 AAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIADYRYETALKRMAHFLTLPERPTAVF 243
Cdd:PRK10727 163 GAWLATRHLIQQGHTRIGYLCSNHSISDAEDRLQGYYDALAESGIPANDRLVTFGEPDESGGEQAMTELLGRGRNFTAVA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1900939922 244 ATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPM 293
Cdd:PRK10727 243 CYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPI 292
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
74-329 |
1.22e-51 |
|
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: 172.42 E-value: 1.22e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 74 FYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIEtLLEKQVDGLLFMGPRVTDEHLDLFRSASVPVVLATTIDPGCQ 153
Cdd:cd06277 20 FFSELIDGIEREARKYGYNLLISSVDIGDDFDEILKE-LTDDQSSGIILLGTELEEKQIKLFQDVSIPVVVVDNYFEDLN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 154 LPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIADYRYETALKRMAHFL 233
Cdd:cd06277 99 FDCVVIDNEDGAYEAVKYLVELGHTRIGYLASSYRIKNFEERRRGFRKAMRELGLSEDPEPEFVVSVGPEGAYKDMKALL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 234 -TLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVSMRLLTKYMHNEK 312
Cdd:cd06277 179 dTGPKLPTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRRLIEKIKDPD 258
|
250
....*....|....*..
gi 1900939922 313 VTDSLVFLPHTIEIRGS 329
Cdd:cd06277 259 GGTLKILVSTKLVERGS 275
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
62-329 |
2.49e-50 |
|
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: 168.93 E-value: 2.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPD-IASAF----YAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLlekqVDGLLFMGPRVTDEHLDLFR 136
Cdd:cd06279 1 AIGVLLPDdLSYAFsdpvAAQFLRGVAEVCEEEGLGLLLLPATDEGSAAAAVRNAA----VDGFIVYGLSDDDPAVAALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 137 SASVPVVlatTID--PGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAG-----------------LSRFQ 197
Cdd:cd06279 77 RRGLPLV---VVDgpAPPGIPSVGIDDRAAARAAARHLLDLGHRRIAILSLRLDRGRErgpvsaerlaaatnsvaRERLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 198 GYRQALEDAGVPF-REELVQIADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNI 276
Cdd:cd06279 154 GYRDALEEAGLDLdDVPVVEAPGNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRVPEDLSVTGFDDI 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1900939922 277 RLASMVRPTLTTVAQPMYDIGAVSMRLLTKYMHNEKVTDslVFLPHTIEIRGS 329
Cdd:cd06279 234 PEAAAADPGLTTVRQPAVEKGRAAARLLLGLLPGAPPRP--VILPTELVVRAS 284
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
3-325 |
1.03e-48 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 166.81 E-value: 1.03e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 3 VTIYDVAREAGVSMATVSRVVNGNPNVKPATRKKVLEVIERLGYRPNAVARGLASKKTTTVGVIIPDIASAFYAELARGI 82
Cdd:PRK10014 7 ITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAELTAGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 83 EDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHL-DLFRSASVPVVLATTIDPGCQLPSVNIDQ 161
Cdd:PRK10014 87 TEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGAAGSSDDLrEMAEEKGIPVVFASRASYLDDVDTVRPDN 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 162 RQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIADYRYETALKRMAHFLTLPERPTA 241
Cdd:PRK10014 167 MQAAQLLTEHLIRNGHQRIAWLGGQSSSLTRAERVGGYCATLLKFGLPFHSEWVLECTSSQKQAAEAITALLRHNPTISA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 242 VFATSDEMAVAAIHAYQDAGFRVPED---------VEVIGFDNIRLASMVRPTLTTVAQPMYDIG-AVSMRLLTKYMHNE 311
Cdd:PRK10014 247 VVCYNETIAMGAWFGLLRAGRQSGESgvdryfeqqVALAAFTDVPEAELDDPPLTWASTPAREIGrTLADRMMQRITHEE 326
|
330
....*....|....
gi 1900939922 312 KVTDSLVFLPHTIE 325
Cdd:PRK10014 327 THSRNLIIPPRLIA 340
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
58-329 |
1.32e-47 |
|
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: 161.65 E-value: 1.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 58 KKTTTVGVIIP-------DIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETlleKQVDGLLFMGPRVTDE 130
Cdd:cd06295 1 QRSRTIAVVVPmdphgdqSITDPFFLELLGGISEALTDRGYDMLLSTQDEDANQLARLLDS---GRADGLIVLGQGLDHD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 131 HLDLFRSASVPVVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLE-EFAglSRFQGYRQALEDAGVP 209
Cdd:cd06295 78 ALRELAQQGLPMVVWGAPEDGQSYCSVGSDNVKGGALATEHLIEIGRRRIAFLGDPPHpEVA--DRLQGYRDALAEAGLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 210 FREELVQIADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTV 289
Cdd:cd06295 156 ADPSLLLSCDFTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFRPPLTTV 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1900939922 290 AQPMYDIGAVSMRLLTKYMHNEKVTDSLvfLPHTIEIRGS 329
Cdd:cd06295 236 RQDLALAGRLLVEKLLALIAGEPVTSSM--LPVELVVRES 273
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-310 |
2.64e-47 |
|
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: 160.79 E-value: 2.64e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIA---SAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPrVTDEHLDLFRSA 138
Cdd:cd19974 1 NIAVLIPERFfgdNSFYGKIYQGIEKELSELGYNLVLEIISDEDEEELNLPSIISEEKVDGIIILGE-ISKEYLEKLKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 139 SVPVVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPleeFAGLS---RFQGYRQALEDAGVPFREELV 215
Cdd:cd19974 80 GIPVVLVDHYDEELNADSVLSDNYYGAYKLTSYLIEKGHKKIGFVGDI---NYTSSfmdRYLGYRKALLEAGLPPEKEEW 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 216 QIADYRY--------ETALKRMahfltlpeRPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLT 287
Cdd:cd19974 157 LLEDRDDgyglteeiELPLKLM--------LPTAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLT 228
|
250 260
....*....|....*....|...
gi 1900939922 288 TVAQPMYDIGAVSMRLLTKYMHN 310
Cdd:cd19974 229 TVEVDKEAMGRRAVEQLLWRIEN 251
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
62-327 |
1.48e-46 |
|
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: 158.87 E-value: 1.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVP 141
Cdd:cd06283 1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPTGNNNDAYLELAQKGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VVLattID---PGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEefaGLS----RFQGYRQALEDAGVPFREEL 214
Cdd:cd06283 81 VVL---VDrqiEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPIK---GIStrreRLQGFLDALARYNIEGDVYV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 215 VQIADyrYETALKRMAHFLTL-PERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPM 293
Cdd:cd06283 155 IEIED--TEDLQQALAAFLSQhDGGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQPT 232
|
250 260 270
....*....|....*....|....*....|....
gi 1900939922 294 YDIGAVSMRLLTKYMHNEKVTDSLVFLPHTIEIR 327
Cdd:cd06283 233 YEIGKAAAEILLERIEGDSGEPKEIELPSELIIR 266
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
62-298 |
3.73e-44 |
|
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: 152.71 E-value: 3.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIP----DIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRS 137
Cdd:cd20010 1 AIGLVLPldpgDLGDPFFLEFLAGLSEALAERGLDLLLAPAPSGEDELATYRRLVERGRVDGFILARTRVNDPRIAYLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 138 ASVP-VVLATTIDPGcQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQ 216
Cdd:cd20010 81 RGIPfVVHGRSESGA-PYAWVDIDNEGAFRRATRRLLALGHRRIALLNGPEELNFAHQRRDGYRAALAEAGLPVDPALVR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 217 IADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNI-RLASMVRPTLTTVAQPMYD 295
Cdd:cd20010 160 EGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLlPALEYFSPPLTTTRSSLRD 239
|
...
gi 1900939922 296 IGA 298
Cdd:cd20010 240 AGR 242
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-329 |
6.00e-42 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380504 [Multi-domain] Cd Length: 270 Bit Score: 147.00 E-value: 6.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHL-DLFRSASV 140
Cdd:cd06281 1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILTPGDEDDPELaAALARLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 141 PVVLattID--PGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIA 218
Cdd:cd06281 81 PVVL---IDrdLPGDIDSVLVDHRSGVRQATEYLLSLGHRRIALLTGGPDIRPGRERIAGFKAAFAAAGLPPDPDLVRLG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 219 DYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGA 298
Cdd:cd06281 158 SFSADSGFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDLDAVGR 237
|
250 260 270
....*....|....*....|....*....|..
gi 1900939922 299 VSMRLLTKYMHNEKVTDSL-VFLPHTIEIRGS 329
Cdd:cd06281 238 AAAELLLDRIEGPPAGPPRrIVVPTELILRDS 269
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
7-329 |
2.09e-40 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 144.78 E-value: 2.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 7 DVAREAGVSMATVSRVVNGNPNVKPATRKKVLEVIERLGYRPNAVARGLASKKTTTVGVIIPDIASAFYAELARGIEDIA 86
Cdd:PRK14987 10 DVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGIESVT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 87 NMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVPVVLATTIDPGCQLPSVNIDQRQAAY 166
Cdd:PRK14987 90 DAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIEVAGIPVVELMDSQSPCLDIAVGFDNFEAAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 167 DATRLLLNHGHTRIAFLGGPLEEFAGLSRfQGYRQALEDAG-VPFREELVQIADYRYETALKRMAHfltlPERPT--AVF 243
Cdd:PRK14987 170 QMTTAIIARGHRHIAYLGARLDERTIIKQ-KGYEQAMLDAGlVPYSVMVEQSSSYSSGIELIRQAR----REYPQldGVF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 244 ATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVSMRLLTKYMHNEKVTDSLVFLPHT 323
Cdd:PRK14987 245 CTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARIRGESVTPKMLDLGFT 324
|
....*.
gi 1900939922 324 IEIRGS 329
Cdd:PRK14987 325 LSPGGS 330
|
|
| fruct_sucro_rep |
TIGR02417 |
D-fructose-responsive transcription factor; Members of this family belong the lacI ... |
4-328 |
9.26e-38 |
|
D-fructose-responsive transcription factor; Members of this family belong the lacI helix-turn-helix family (pfam00356) of DNA-binding transcriptional regulators. All members are from the proteobacteria. Characterized members act as positive and negative transcriptional regulators of fructose and sucrose transport and metabolism. Sucrose is a disaccharide composed of fructose and glucose; D-fructose-1-phosphate rather than an intact sucrose moiety has been shown to act as the inducer. [Regulatory functions, DNA interactions]
Pssm-ID: 131470 [Multi-domain] Cd Length: 327 Bit Score: 137.57 E-value: 9.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 4 TIYDVAREAGVSMATVSRVVNGNPN---VKPATRKKVLEVIERLGYRPNAVARGLASKKTTTVGVIIPDIASAFYAELAR 80
Cdd:TIGR02417 1 TLSDIAKLAGVSKTTASYVINGKAKeyrISQETVERVMAVVREQGYQPNIHAASLRAGRSRTIGLVIPDLENYSYARIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 81 GIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGlLFMGPRVTDEHLDLFRSAS--VPVVLATTIDPGCQLPSVN 158
Cdd:TIGR02417 81 ELEQQCREAGYQLLIACSDDNPDQEKVVIENLLARQVDA-LIVASCMPPEDAYYQKLQNegLPVVALDRSLDDEHFCSVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 159 IDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAgvPFREELVQIADYRYETALKRMAHFL-TLPE 237
Cdd:TIGR02417 160 SDDVDAAAELIERLLSQHADEFWYLGAQPELSVSRDRLAGFRQALKQA--TLEVEWVYGGNYSRESGYQMFAKLCaRLGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 238 RPTAVFATSDEMaVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVSMRLLTKYMHNEKVTDSL 317
Cdd:TIGR02417 238 LPQALFTTSYTL-LEGVLDYMLERPLLDSQLHLATFGDNYLLDFLPLPINSVAQQHRQLAWHALELALAAIDGKKPEPGQ 316
|
330
....*....|.
gi 1900939922 318 VFLPHTIEIRG 328
Cdd:TIGR02417 317 RYIPRTLQIRH 327
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
63-321 |
2.37e-36 |
|
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: 131.98 E-value: 2.37e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 63 VGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHL-DLFRSASVP 141
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAGVaEKARGQNVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VVL-------ATTIDpgcqlpSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREEL 214
Cdd:cd01537 82 VVFfdkepsrYDKAY------YVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKTEQLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 215 VQIADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMY 294
Cdd:cd01537 156 LDTGDWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDAN 235
|
250 260
....*....|....*....|....*..
gi 1900939922 295 DIGAVSMRLLTKYMHNEKVTDSLVFLP 321
Cdd:cd01537 236 NLGKTTFDLLLNLADNWKIDNKVVRVP 262
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
172-330 |
3.52e-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: 3.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 172 LLNHGHTRIAFLGGPLEEFAGLS--RFQGYRQALEDAGVPFREELVQIADYRYETALKRMahFLTLPERPTAVFATSDEM 249
Cdd:pfam13377 2 LAELGHRRIALIGPEGDRDDPYSdlRERGFREAARELGLDVEPTLYAGDDEAEAAAARER--LRWLGALPTAVFVANDEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 250 AVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVSMRLLTKYMHNEKVTDSLVFLPHTIEIRGS 329
Cdd:pfam13377 80 ALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVERES 159
|
.
gi 1900939922 330 T 330
Cdd:pfam13377 160 T 160
|
|
| HTH_LACI |
smart00354 |
helix_turn _helix lactose operon repressor; |
3-72 |
9.56e-36 |
|
helix_turn _helix lactose operon repressor;
Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 124.24 E-value: 9.56e-36
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 3 VTIYDVAREAGVSMATVSRVVNGNPNVKPATRKKVLEVIERLGYRPNAVARGLASKKTTTVGVIIPDIAS 72
Cdd:smart00354 1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
7-246 |
5.45e-35 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 130.00 E-value: 5.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 7 DVAREAGVSMATVSRVVNGNPN---VKPATRKKVLEVIERLGYRPNAVARGLASKKTTTVGVIIPDIASAFYAELARGIE 83
Cdd:PRK11303 5 EIARLAGVSRTTASYVINGKAKqyrVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSYARIAKYLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 84 DIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMG--PRVTDEHLDLfRSASVPVV-LATTIDPGCqLPSVNID 160
Cdd:PRK11303 85 RQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVSTslPPEHPFYQRL-QNDGLPIIaLDRALDREH-FTSVVSD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 161 QRQAAYDATRLLLNHGHTRIAFLGGpLEEFaGLS--RFQGYRQALEDAGVPfreelVQI---ADYRYETALKRMAHFLTL 235
Cdd:PRK11303 163 DQDDAEMLAESLLKFPAESILLLGA-LPEL-SVSfeREQGFRQALKDDPRE-----VHYlyaNSFEREAGAQLFEKWLET 235
|
250
....*....|.
gi 1900939922 236 PERPTAVFATS 246
Cdd:PRK11303 236 HPMPDALFTTS 246
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
62-325 |
1.18e-33 |
|
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: 124.89 E-value: 1.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVP 141
Cdd:cd06297 1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLLSEYRLEKYLRNSTLAYQCDGLVMASLDLTELFEEVIVPTEKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VVLATTIDPGcqLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLS----RFQGYRQALEDAGVPFREELVQI 217
Cdd:cd06297 81 VVLIDANSMG--YDCVYVDNVKGGFMATEYLAGLGEREYVFFGIEEDTVFTETvfreREQGFLEALNKAGRPISSSRMFR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 218 ADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMvrPTLTTVAQPMYDIG 297
Cdd:cd06297 159 IDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAAS--PGLTTVRQPVEEMG 236
|
250 260 270
....*....|....*....|....*....|
gi 1900939922 298 AVSMRLLTKYMhNEKVT--DSLVFLPHTIE 325
Cdd:cd06297 237 EAAAKLLLKRL-NEYGGppRSLKFEPELIV 265
|
|
| PRK10339 |
PRK10339 |
DNA-binding transcriptional repressor EbgR; Provisional |
4-331 |
1.56e-33 |
|
DNA-binding transcriptional repressor EbgR; Provisional
Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 126.03 E-value: 1.56e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 4 TIYDVAREAGVSMATVSRVVNGNP--NVKPATRKKVLEVIERLGYRPNAVARGL-ASKKTTTVGVIIP-----DIASAFY 75
Cdd:PRK10339 3 TLKDIAIEAGVSLATVSRVLNDDPtlNVKEETKHRILEIAEKLEYKTSSARKLQtGAVNQHHILAIYSyqqelEINDPYY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 76 AELARGIEdiANMYKYNIILCNS-DKQPKKELtlietlleKQVDGLLFMGpRVTDEHLDLFRSASVPVVLATTIDPGCQL 154
Cdd:PRK10339 83 LAIRHGIE--TQCEKLGIELTNCyEHSGLPDI--------KNVTGILIVG-KPTPALRAAASALTDNICFIDFHEPGSGY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 155 PSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVpFREELVQIADYRYETALKRMAHFLT 234
Cdd:PRK10339 152 DAVDIDLARISKEIIDFYINQGVNRIGFIGGEDEPGKADIREVAFAEYGRLKQV-VREEDIWRGGFSSSSGYELAKQMLA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 235 LPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVSMRLLTKYMHNEKVT 314
Cdd:PRK10339 231 REDYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNLLYEKARDGRAL 310
|
330
....*....|....*..
gi 1900939922 315 DSLVFLPHTIEIRGSTR 331
Cdd:PRK10339 311 PLLVFVPSKLKLRGTTR 327
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
108-330 |
6.31e-31 |
|
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: 117.69 E-value: 6.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 108 LIETLLEKQVDGLLFmgpRVTDEHL-DLFRSASVPVVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGP 186
Cdd:cd01543 42 LLDLLKGWKGDGIIA---RLDDPELaEALRRLGIPVVNVSGSRPEPGFPRVTTDNEAIGRMAAEHLLERGFRHFAFCGFR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 187 LEEFAGLsRFQGYRQALEDAGVPFR--EELVQIADYRYETALKRMAHFL-TLPeRPTAVFATSDEMAVAAIHAYQDAGFR 263
Cdd:cd01543 119 NAAWSRE-RGEGFREALREAGYECHvyESPPSGSSRSWEEEREELADWLkSLP-KPVGIFACNDDRARQVLEACREAGIR 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1900939922 264 VPEDVEVIGFDN---IRLASmvRPTLTTVAQPMYDIGAVSMRLLTKYMHNEKVTDSLVFLPHT-IEIRGST 330
Cdd:cd01543 197 VPEEVAVLGVDNdelICELS--SPPLSSIALDAEQIGYEAAELLDRLMRGERVPPEPILIPPLgVVTRQST 265
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
44-324 |
2.98e-30 |
|
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: 116.95 E-value: 2.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 44 LGYRPNAVARGLASKKTTTVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFM 123
Cdd:COG1879 17 AACGSAAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 124 G--PRVTDEHLDLFRSASVPVV-LATTIDPGCQLPSVNIDQRQAAYDATRLLLNH--GHTRIAFLGGPLEEFAGLSRFQG 198
Cdd:COG1879 97 PvdPDALAPALKKAKAAGIPVVtVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKAlgGKGKVAILTGSPGAPAANERTDG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 199 YRQALEDAGvpfREELV--QIADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGfrVPEDVEVIGFDNI 276
Cdd:COG1879 177 FKEALKEYP---GIKVVaeQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAG--RKGDVKVVGFDGS 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1900939922 277 R--LASMVRPTLT-TVAQPMYDIGAVSMRLLTKYMHNEKVtDSLVFLPHTI 324
Cdd:COG1879 252 PeaLQAIKDGTIDaTVAQDPYLQGYLAVDAALKLLKGKEV-PKEILTPPVL 301
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
62-308 |
1.05e-28 |
|
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: 111.53 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGlLFMGPRVTDEHLDLF-RSASV 140
Cdd:cd06274 1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDG-LIVAPSTPPDDIYYLcQAAGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 141 PVVLATTIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIADY 220
Cdd:cd06274 80 PVVFLDRPFSGSDAPSVVSDNRAGARALTEKLLAAGPGEIYFLGGRPELPSTAERIRGFRAALAEAGITEGDDWILAEGY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 221 RYETALKRMAHFL-TLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVeVIG-FDNIRLASMVRPTLTTVAQPMYDIGA 298
Cdd:cd06274 160 DRESGYQLMAELLaRLGGLPQALFTSSLTLLEGVLRFLRERLGAIPSDL-VLGtFDDHPLLDFLPNPVDSVRQDHDEIAE 238
|
250
....*....|
gi 1900939922 299 VSMRLLTKYM 308
Cdd:cd06274 239 HAFELLDALI 248
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
62-313 |
1.20e-28 |
|
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: 111.50 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLF--MGPRVTDEHLDLFRSAS 139
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIapVDSEALVPAVKKANAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 140 VPVVLATT-IDPGCQLPS-VNIDQRQAAYDATRLLLNH--GHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGvpfREELV 215
Cdd:cd01536 81 IPVVAVDTdIDGGGDVVAfVGTDNYEAGKLAGEYLAEAlgGKGKVAILEGPPGSSTAIDRTKGFKEALKKYP---DIEIV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 216 --QIADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGfrVPEDVEVIGFDNIR--LASMVRPTLT-TVA 290
Cdd:cd01536 158 aeQPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAG--RTGDIKIVGVDGTPeaLKAIKDGELDaTVA 235
|
250 260
....*....|....*....|...
gi 1900939922 291 QPMYDIGAVSMRLLTKYMHNEKV 313
Cdd:cd01536 236 QDPYLQGYLAVEAAVKLLNGEKV 258
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
62-320 |
2.79e-28 |
|
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: 110.54 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFY-AELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASV 140
Cdd:cd06272 1 TIGLYWPSVGERVAlTRLLSGINEAISKQGYNINLSICPYKVGHLCTAKGLFSENRFDGVIVFGISDSDIEYLNKNKPKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 141 PVVLATTidPGCQLPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIADY 220
Cdd:cd06272 81 PIVLYNR--ESPKYSTVNVDNEKAGRLAVLLLIQKGHKSIAYIGNPNSNRNQTLRGKGFIETCEKHGIHLSDSIIDSRGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 221 RYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVS 300
Cdd:cd06272 159 SIEGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLTVVGVPIEKIAEES 238
|
250 260
....*....|....*....|
gi 1900939922 301 MRLLTKYMHNEKVTDSLVFL 320
Cdd:cd06272 239 LRLILKLIEGRENEIQQLIL 258
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
60-317 |
4.27e-26 |
|
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: 104.90 E-value: 4.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 60 TTTVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLF-RSA 138
Cdd:pfam00532 1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPAPSGDDITAKaEGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 139 SVPVVLAT-TIDPGCQLPSVNIDQRQAAYDATRLLLNHGHTR-IAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQ 216
Cdd:pfam00532 81 GIPVIAADdAFDNPDGVPCVMPDDTQAGYESTQYLIAEGHKRpIAVMAGPASALTARERVQGFMAALAAAGREVKIYHVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 217 IADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAG-FRVPEDVE-----VIGFDNIRLAS--MVRPTLTT 288
Cdd:pfam00532 161 TGDNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGrVKIPDIVGiginsVVGFDGLSKAQdtGLYLSPLT 240
|
250 260 270
....*....|....*....|....*....|.
gi 1900939922 289 VAQ-PMYDIG-AVSMRLLTKYMHNEKVTDSL 317
Cdd:pfam00532 241 VIQlPRQLLGiKASDMVYQWIPKFREHPRVL 271
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
74-304 |
7.71e-24 |
|
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and alpha-glucosides (AglR) which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380495 [Multi-domain] Cd Length: 264 Bit Score: 98.65 E-value: 7.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 74 FYAELARGIEDIANMYKYNIILCnSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRSASVPVVLATTIDPGCQ 153
Cdd:cd06271 16 TVSE*VSGITEEAGTTGYHLLVW-PFEEAES*VPIRDLVETGSADGVILSEIEPNDPRVQFLTKQNFPFVAHGRSD*PIG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 154 LPSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPfreELVQIADYRYETALKRMAHFL 233
Cdd:cd06271 95 HAWVDIDNEAGAYEAVERLAGLGHRRIAFIVPPARYSPHDRRLQGYVRA*RDAGLT---GYPLDADTTLEAGRAAAQRLL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1900939922 234 TLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIR-LASMVRPTLTTVAQPMYDIGAVSMRLL 304
Cdd:cd06271 172 ALSPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSAPfLGAMITPPLTTVHAPIAEAGRELAKAL 243
|
|
| HTH_LacI |
cd01392 |
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
6-57 |
9.16e-23 |
|
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: 89.39 E-value: 9.16e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1900939922 6 YDVAREAGVSMATVSRVVNGNPNVKPATRKKVLEVIERLGYRPNAVARGLAS 57
Cdd:cd01392 1 KDIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
62-324 |
1.49e-21 |
|
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: 92.67 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMgPRVT---DEHLDLFRSA 138
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILIS-PIDAtgwDPVLKEAKDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 139 SVPVVL-ATTIDPGC---QLPSVNIDQRQAAYDATRLLLNH---GHTRIAFLGGPleefAGLS----RFQGYRQALEDAG 207
Cdd:cd06309 80 GIPVILvDRTIDGEDgslYVTFIGSDFVEEGRRAAEWLVKNykgGKGNVVELQGT----AGSSvaidRSKGFREVIKKHP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 208 vPFREELVQIADYRYETALKRMAHFL-TLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIR--LASMVRP 284
Cdd:cd06309 156 -NIKIVASQSGNFTREKGQKVMENLLqAGPGDIDVIYAHNDDMALGAIQALKEAGLKPGKDVLVVGIDGQKdaLEAIKAG 234
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1900939922 285 TLT-TVA-QPMYdiGAVSMRLLTKYMHNEKVtDSLVFLPHTI 324
Cdd:cd06309 235 ELNaTVEcNPLF--GPTAFDTIAKLLAGEKV-PKLIIVEERL 273
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
63-312 |
3.63e-21 |
|
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic binding proteins. This domain recognizes fructose (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433182 [Multi-domain] Cd Length: 259 Bit Score: 91.22 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 63 VGVIIPDIASAFYAELARGIEDIANMYKYN-IILCNSDKQPKKELTLIETLLEKQVDGLLF--MGPRVTDEHLDLFRSAS 139
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEvIVVGPAEADAAEQVAQIEDAIAQGVDAIIVapVDPTALAPVLKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 140 VPVVL-ATTIDPGCQLPSVNIDQRQAAYDATRLLLNH--GHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPF-REELV 215
Cdd:pfam13407 81 IPVVTfDSDAPSSPRLAYVGFDNEAAGEAAGELLAEAlgGKGKVAILSGSPGDPNANERIDGFKKVLKEKYPGIkVVAEV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 216 QIADYRYETALKRMAHFLTLPERPT-AVFATSDEMAVAAIHAYQDAGfrVPEDVEVIGFDNIR--LASMVRPTLT-TVAQ 291
Cdd:pfam13407 161 EGTNWDPEKAQQQMEALLTAYPNPLdGIISPNDGMAGGAAQALEAAG--LAGKVVVTGFDATPeaLEAIKDGTIDaTVLQ 238
|
250 260
....*....|....*....|.
gi 1900939922 292 PMYDIGAVSMRLLTKYMHNEK 312
Cdd:pfam13407 239 DPYGQGYAAVELAAALLKGKK 259
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
155-306 |
4.10e-21 |
|
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: 91.06 E-value: 4.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 155 PSVNIDQRQAAYDATRLLLNHGHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVPFREELVQIADYRYETALKRMAHFLT 234
Cdd:cd20009 96 AYFDFDNEAFAYEAVRRLAARGRRRIALVAPPRELTYAQHRLRGFRRALAEAGLEVEPLLIVTLDSSAEAIRAAARRLLR 175
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1900939922 235 LPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGFDNIRLASMVRPTLTTVAQPMYDIGAVSMRLLTK 306
Cdd:cd20009 176 QPPRPDGIICASEIAALGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPIDTLYEDIEEAGRFLAEALLR 247
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
62-321 |
9.73e-20 |
|
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: 87.42 E-value: 9.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLF--MGPRVTDEHLDLFRSAS 139
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIIspTNSSAAPTVLDLANEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 140 VPVVLATT-IDPGCQLPSVNIDQRQAAYDATRLLLNH------GHTRIAFLGGPLEEFAGLSRFQGYRQALEDAGVpfrE 212
Cdd:cd06319 81 IPVVIADIgTGGGDYVSYIISDNYDGGYQAGEYLAEAlkengwGGGSVGIIAIPQSRVNGQARTAGFEDALEEAGV---E 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 213 ELV--QIADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGfrVPEDVEVIGFDNIRLAS-MVR--PTLT 287
Cdd:cd06319 158 EVAlrQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAG--RTGDILVVGFDGDPEALdLIKdgKLDG 235
|
250 260 270
....*....|....*....|....*....|....
gi 1900939922 288 TVAQPMYDIGAVSMRLLTKYMHNEKVTDSLVFLP 321
Cdd:cd06319 236 TVAQQPFGMGARAVELAIQALNGDNTVEKEIYLP 269
|
|
| LacI |
pfam00356 |
Bacterial regulatory proteins, lacI family; |
4-49 |
3.96e-18 |
|
Bacterial regulatory proteins, lacI family;
Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 76.91 E-value: 3.96e-18
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1900939922 4 TIYDVAREAGVSMATVSRVVNGNPNVKPATRKKVLEVIERLGYRPN 49
Cdd:pfam00356 1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
62-317 |
3.40e-16 |
|
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: 77.34 E-value: 3.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLF-------MGPRVTDEHldl 134
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLInptdsdaVSPAVEEAN--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 135 frSASVPVVlatTID----PGCQLPSVNIDQRQAAYDATRLLLNhghtriaFLGGP-----LEEFAGLS----RFQGYRQ 201
Cdd:cd06323 78 --EAGIPVI---TVDrsvtGGKVVSHIASDNVAGGEMAAEYIAK-------KLGGKgkvveLQGIPGTSaareRGKGFHN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 202 ALEDAGvPFREELVQIADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGfrvPEDVEVIGFDNIRLASM 281
Cdd:cd06323 146 AIAKYP-KINVVASQTADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAG---RKDVIVVGFDGTPDAVK 221
|
250 260 270
....*....|....*....|....*....|....*....
gi 1900939922 282 V---RPTLTTVAQPMYDIGAVSMRLLTKYMHNEKVTDSL 317
Cdd:cd06323 222 AvkdGKLAATVAQQPEEMGAKAVETADKYLKGEKVPKKI 260
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
62-313 |
1.06e-14 |
|
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: 73.08 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDG--LLFMGPRVTDEHLDLFRSAS 139
Cdd:cd06322 1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAiiLAPVDSGGIVPAIEAANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 140 VPV----VLATTIDPGCQLPSVNIDQ-RQAAYDATRLLLNHGhTRIAFLGGPlEEFAGLSRFQGYRQALED-AGVpfreE 213
Cdd:cd06322 81 IPVftvdVKADGAKVVTHVGTDNYAGgKLAGEYALKALLGGG-GKIAIIDYP-EVESVVLRVNGFKEAIKKyPNI----E 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 214 LVQIADY--RYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGfrVPEDVEVIGFD----NIRLASMVRPTLT 287
Cdd:cd06322 155 IVAEQPGdgRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAG--KEDKIKVIGFDgnpeAIKAIAKGGKIKA 232
|
250 260
....*....|....*....|....*.
gi 1900939922 288 TVAQPMYDIGAVSMRLLTKYMHNEKV 313
Cdd:cd06322 233 DIAQQPDKIGQETVEAIVKYLAGETV 258
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
62-274 |
4.79e-13 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380627 [Multi-domain] Cd Length: 269 Bit Score: 68.24 E-value: 4.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTdehldlfrSASVP 141
Cdd:cd19972 1 TIGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGAT--------AAAVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 142 VVLATTidpgCQLPSVNIDQR---------------QAAYDATRLLLNH--GHTRIAFLGGPLEEFAGLSRFQGYRQALE 204
Cdd:cd19972 73 VKAARA----AGIPVIAVDRNpedapgdtfiatdsvAAAKELGEWVIKQtgGKGEIAILHGQLGTTPEVDRTKGFQEALA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1900939922 205 DA-GVPFREElvQIADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGfrVPEDVEVIGFD 274
Cdd:cd19972 149 EApGIKVVAE--QTADWDQDEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAG--LDHKIWVVGFD 215
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
63-324 |
2.49e-12 |
|
periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis; Periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis. The members of this group are belonging to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Like other periplasmic receptors of the ABC-type transport systems, the allose-binding protein consists of two alpha/beta domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding.
Pssm-ID: 380543 [Multi-domain] Cd Length: 283 Bit Score: 66.13 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 63 VGVIIPDIASAFYAELARGIEDIANMY--KYNIILCNSDKQPKKELTLIETLLEKQVDGLLFmGPrVTDEHLDL-FRSAS 139
Cdd:cd06320 2 IGVVLKTLSNPFWVAMKDGIEAEAKKLgvKVDVQAAPSETDTQGQLNLLETMLNKGYDAILV-SP-ISDTNLIPpIEKAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 140 ---VPVV-LATTIDP------GCQLPS-VNIDQRQAAYDATRLLLN--HGHTRIAFLGGPLEEFAGLSRFQGYRQALEDA 206
Cdd:cd06320 80 kkgIPVInLDDAVDAdalkkaGGKVTSfIGTDNVAAGALAAEYIAEklPGGGKVAIIEGLPGNAAAEARTKGFKETFKKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 207 GvpfREELV--QIADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRvpEDVEVIGFDNIRLA--SMV 282
Cdd:cd06320 160 P---GLKLVasQPADWDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAGKT--GKVLVVGTDGIPEAkkSIK 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1900939922 283 RPTLT-TVAQPMYDIGAVSMRLLTKYMHNEKVTDSlVFLPHTI 324
Cdd:cd06320 235 AGELTaTVAQYPYLEGAMAVEAALRLLQGQKVPAV-VATPQAL 276
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
62-313 |
2.60e-12 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380533 [Multi-domain] Cd Length: 272 Bit Score: 66.21 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQ--PKKELTLIETLLEKQVDGLLF--MGPRVTDEHLDLFRS 137
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFVGPESEedVAGQNSLLEELINKKPDAIVVapLDSEDLVDPLKDAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 138 ASVPVVLATT-IDPGCQLPSVNIDQRQAAYDATRLLLN--HGHTRIAFLGGPLEEFAGLSRFQGYRQAL--EDAGVPFRE 212
Cdd:cd06310 81 KGIPVIVIDSgIKGDAYLSYIATDNYAAGRLAAQKLAEalGGKGKVAVLSLTAGNSTTDQREEGFKEYLkkHPGGIKVLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 213 ElvQIADYRYETALKRMAHFLTlpERPTA--VFATSDEMAVAAIHAYQDAGfrVPEDVEVIGFD----------NIRLAS 280
Cdd:cd06310 161 S--QYAGSDYAKAANETEDLLG--KYPDIdgIFATNEITALGAAVAIKSRK--LSGQIKIVGFDsqeelldalkNGKIDA 234
|
250 260 270
....*....|....*....|....*....|...
gi 1900939922 281 MvrptlttVAQPMYDIGAVSMRLLTKYMHNEKV 313
Cdd:cd06310 235 L-------VVQNPYEIGYEGIKLALKLLKGEEV 260
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
62-274 |
2.95e-12 |
|
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: 66.47 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIAS-AFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLL--EKQVDGLLFMG-PRVTDEHLDLFRS 137
Cdd:cd06324 1 RVVFINPGKEDePFWQNVTRFMQAAAKDLGIELEVLYANRNRFKMLELAEELLarPPKPDYLILVNeKGVAPELLELAEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 138 ASVPVVLA-TTIDPGCQ-------------LPSVNIDQRQAAYDATRLLLNHGHTR--------IAFLGGPLEeFAGLSR 195
Cdd:cd06324 81 AKIPVFLInNDLTDEERallgkprekfkywLGSIVPDNEQAGYLLAKALIKAARKKsddgkirvLAISGDKST-PASILR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 196 FQGYRQALEDAGvpfREELVQI--ADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVPEDVEVIGF 273
Cdd:cd06324 160 EQGLRDALAEHP---DVTLLQIvyANWSEDEAYQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGLKPGKDVLVGGI 236
|
.
gi 1900939922 274 D 274
Cdd:cd06324 237 D 237
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
62-274 |
6.06e-12 |
|
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: 65.10 E-value: 6.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLfMGPRVTDE---HLDLFRSA 138
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGII-VSPIDVKAlvpAIEAAIKA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 139 SVPVVlatTIDPGCQ----LPSVNIDQR---QAAYDATRLLLNHGhTRIAFLGGPLEEFAGLSRFQGYRQALeDAGVPFR 211
Cdd:cd19968 80 GIPVV---TVDRRAEgaapVPHVGADNVaggREVAKFVVDKLPNG-AKVIELTGTPGSSPAIDRTKGFHEEL-AAGPKIK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1900939922 212 EELVQIADYRYETALKRMAHFLT-LPERPTAVFATSDEMAVAAIHAYQDAGFRVpEDVEVIGFD 274
Cdd:cd19968 155 VVFEQTGNFERDEGLTVMENILTsLPGPPDAIICANDDMALGAIEAMRAAGLDL-KKVKVIGFD 217
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
117-329 |
3.22e-11 |
|
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: 62.82 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 117 VDGLLFMGPRVTDEHLDLFRSASVPVV-LATTIDPGCQLPSVNIDQRQAAydatRLLLNHGHT----RIAFLGGPLEEFA 191
Cdd:cd06287 57 VDGAIVVEPTVEDPILARLRQRGVPVVsIGRAPGTDEPVPYVDLQSAATA----RLLLEHLHGagarQVALLTGSSRRNS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 192 GLSRFQGYRQALEDAGvpFREELVQIADYRYETALKRMAHFLtLPERPT--AVFATSDEMAVAAIHAYQDAGFRVPEDVE 269
Cdd:cd06287 133 SLESEAAYLRFAQEYG--TTPVVYKVPESEGERAGYEAAAAL-LAAHPDidAVCVPVDAFAVGAMRAARDSGRSVPEDLM 209
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1900939922 270 VIG-FDNIRlASMVRPTLTTVAQPMYDIGAVSMRLLTKYMHNEKVTDSLVFLPHTIEiRGS 329
Cdd:cd06287 210 VVTrYDGIR-ARTADPPLTAVDLHLDRVARTAIDLLFASLSGEERSVEVGPAPELVV-RAS 268
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
62-313 |
9.68e-11 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 61.64 E-value: 9.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLfMGPRVTDEHLDLFRSAS-- 139
Cdd:PRK10653 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKELANVQDLTVRGTKILL-INPTDSDAVGNAVKMANqa 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 140 -VPVVlatTIDPGC-------QLPSVNIDQRQAAYDATRLLLNHGHTRIAflggpLEEFAGLS----RFQGYRQALEDAG 207
Cdd:PRK10653 107 nIPVI---TLDRGAtkgevvsHIASDNVAGGKMAGDFIAKKLGEGAKVIQ-----LEGIAGTSaareRGEGFKQAVAAHK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 208 vpFREELVQIADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGfrvPEDVEVIGFDNIR--LASMVRPT 285
Cdd:PRK10653 179 --FNVLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KSDVMVVGFDGTPdgIKAVNRGK 253
|
250 260
....*....|....*....|....*....
gi 1900939922 286 L-TTVAQPMYDIGAVSMRLLTKYMHNEKV 313
Cdd:PRK10653 254 LaATIAQQPDQIGAIGVETADKVLKGEKV 282
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
62-321 |
2.92e-10 |
|
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to rhizopines, which are simple sugar-like compounds produced in the nodules induced by the symbiotic root nodule bacteria, such as Rhizobium and Sinorhizobium. Rhizopine-binding-like proteins from other bacteria are also included. Two inositol based rhizopine compounds are known to date: L-3-O-methly-scyllo-inosamine (3-O-MSI) and scyllo-inosamine. Bacterial strains that can metabolize rhizopine have a greater competitive advantage in nodulation and rhizopine synthesis is regulated by NifA/NtrA regulatory transcription activators which are maximally expressed at the onset of nitrogen fixation in bacteroids. The members of this group belong to the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily.
Pssm-ID: 380524 [Multi-domain] Cd Length: 272 Bit Score: 59.94 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYK-YNIILCNSDKQPKKELTLIETLLEKQVDGLLFMgPRVTDE---HLDLFRS 137
Cdd:cd06301 2 KIGVSMQNFSDEFLTYLRDAIEAYAKEYPgVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVN-PVDTDAsapAVDAAAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 138 ASVPVVL--ATTIDPGCQLPSVNIDQRQAA-YDATRLL-LNHGHTRIAFLGGPLEEFAGLSRFQGYRQALED-AGVpfre 212
Cdd:cd06301 81 AGIPLVYvnREPDSKPKGVAFVGSDDIESGeLQMEYLAkLLGGKGNIAILDGVLGHEAQILRTEGNKDVLAKyPGM---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 213 ELV--QIADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGfrVPEDVEVIGFDNIR--LASMVRPTL-T 287
Cdd:cd06301 157 KIVaeQTANWSREKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAG--KKDDILVAGIDATPdaLKAMKAGRLdA 234
|
250 260 270
....*....|....*....|....*....|....
gi 1900939922 288 TVAQPMYDIGAVSMRLLTKYMHNEKVtDSLVFLP 321
Cdd:cd06301 235 TVFQDAAGQGETAVDVAVKAAKGEEV-ESDIWIP 267
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
62-312 |
4.09e-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: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLF--MGPRVTDEHLDLFRSAS 139
Cdd:cd19967 1 LVAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILdpADADASIAAVKKAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 140 VPVVLattIDPgcQLPSVNIDQRQAA---YDATRLLLNH------GHTRIAFLGGPLEEFAGLSRFQGYRQALEdaGVPF 210
Cdd:cd19967 81 IPVFL---IDR--EINAEGVAVAQIVsdnYQGAVLLAQYfvklmgEKGLYVELLGKESDTNAQLRSQGFHSVID--QYPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 211 REELV-QIADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGfrVPEDVEVIGFD---NIRLASMVRPTL 286
Cdd:cd19967 154 LKMVAqQSADWDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAG--RAGDVIIVGFDgsnDVRDAIKEGKIS 231
|
250 260
....*....|....*....|....*.
gi 1900939922 287 TTVAQPMYDIGAVSMRLLTKYMHNEK 312
Cdd:cd19967 232 ATVLQPAKLIARLAVEQADQYLKGGS 257
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
62-287 |
1.28e-09 |
|
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: 58.03 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIA---NMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLF-------MGPRVTDEH 131
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKGARKHAkeaNGYELLVKGIKQETDIEQQIAIVENLIAQKVDAIVIapadskaLVPVLKKAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 132 ldlfrSASVPVV-LATTIDP------GCQLPSVNIDQRQAAYDATRLLLNH--GHTRIAFLGGPLEEFAGLSRFQGYRQA 202
Cdd:cd19970 81 -----DAGIAVInIDNRLDAdalkegGINVPFVGPDNRQGAYLAGDYLAKKlgKGGKVAIIEGIPGADNAQQRKAGFLKA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 203 LEDAGVpfreELV--QIADYRYETALKRMAHFLTlpERP--TAVFATSDEMAVAAIHAYQDAGFRvpEDVEVIGFDNIrl 278
Cdd:cd19970 156 FEEAGM----KIVasQSANWEIDEANTVAANLLT--AHPdiRGILCANDNMALGAIKAVDAAGKA--GKVLVVGFDNI-- 225
|
....*....
gi 1900939922 279 aSMVRPTLT 287
Cdd:cd19970 226 -PAVRPLLK 233
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
62-325 |
2.38e-09 |
|
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Proteins similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. The sugar-binding domain of the periplasmic proteins in this group is also homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR), DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380528 [Multi-domain] Cd Length: 273 Bit Score: 57.31 E-value: 2.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLF-MGP-RVTDEHLDLFRSAS 139
Cdd:cd06305 1 TIAVVRNGTSGDWDQQALQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIIsHGDaDALDPKLKKALDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 140 VPVVlatTIDPGCQLPSVNIDQrQAAYDATRLLLN------HGHTRIAFLGG----PLEefaglSRFQGYrQALEDAGVP 209
Cdd:cd06305 81 IPVV---TFDTDSQVPGVNNIT-QDDYALGTLSLGqlvkdlNGEGNIAVFNVfgvpPLD-----KRYDIY-KAVLKANPG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 210 FREELVQIADYRYETALKRMAHFLT-LPERP----TAVFATSDEMAVAAIHAYQDAGfRvpEDVEVIGFD--NIRLASMV 282
Cdd:cd06305 151 IKKIVAELGDVTPNTAADAQTQVEAlLKKYPeggiDAIWAAWDEPAKGAVQALEEAG-R--TDIKVYGVDisNQDLELMA 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1900939922 283 RPTLT---TVAQPMYDIGAVSMRLLTKYMHNEKVTDSLVFLPHTIE 325
Cdd:cd06305 228 DEGSPwvaTAAQDPALIGTVAVRNVARKLAGEDLPDKYSLVPVLIT 273
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
62-276 |
3.27e-09 |
|
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group includes periplasmic D-threitol-binding protein ThpA and xylitol/L-sorbitol-binding protein XypA, which are part of sugar ABC-type transport systems. Both ThpA and XypA share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.
Pssm-ID: 380536 [Multi-domain] Cd Length: 277 Bit Score: 56.89 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLF-------MGPRVTDEhldl 134
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVvpvdadaLAPAVEKA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 135 fRSASVPVV-LATTIDPGCQLPSVNIDQRQAAYDATRLLLNH--GHTRIAFLGGPLEEFAGLSRFQGYRQALEDA-GVPF 210
Cdd:cd06313 77 -KEAGIPLVgVNALIENEDLTAYVGSDDVVAGELEGQAVADRlgGKGNVVILEGPIGQSAQIDRGKGIENVLKKYpDIKV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1900939922 211 REElvQIADYRYETALKRMAHFLTL-PERPTAVFATSDEMAVAAIHAYQDAGFrvpEDVEVIGFDNI 276
Cdd:cd06313 156 LAE--QTANWSRDEAMSLMENWLQAyGDEIDGIIAQNDDMALGALQAVKAAGR---DDIPVVGIDGI 217
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
62-324 |
8.63e-09 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consist of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380544 [Multi-domain] Cd Length: 270 Bit Score: 55.76 E-value: 8.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYN--IILCNSDKQPKKELTLIETLLEKQVDGLLF-------MGPRVTDEHl 132
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINPGakVTVVDARYDLAKQFSQIDDFIAQGVDLILLnaadsagIEPAIKRAK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 133 dlfrSASVPVVLATTIDPGCQlPSVNIDQRQAAYDATRLLLNH--GHTRIAFLGGPlEEFAGLSRFQGYRQAL-EDAGVp 209
Cdd:cd06321 80 ----DAGIIVVAVDVAAEGAD-ATVTTDNVQAGYLACEYLVEQlgGKGKVAIIDGP-PVSAVIDRVNGCKEALaEYPGI- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 210 freELV--QIADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRvpeDVEVIGFDN-----IRLASMV 282
Cdd:cd06321 153 ---KLVddQNGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRD---DIVITSVDGspeavAALKREG 226
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1900939922 283 RPTLTTVAQPMYDIGAVSMRLLTKYMHNEKVTDSLVFLPHTI 324
Cdd:cd06321 227 SPFIATAAQDPYDMARKAVELALKILNGQEPAPELVLIPSTL 268
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
62-313 |
1.98e-08 |
|
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: 54.48 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKY-NIILCNSDKQPKKELTLIETLLEKQVDGLLfMGPRVTDEHLDLFRSA-- 138
Cdd:cd06308 1 VIGFSQCSLNDPWRAAMNEEIKAEAAKYPNvELIVTDAQGDAAKQIADIEDLIAQGVDLLI-VSPNEADALTPVVKKAyd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 139 -SVPVVLattID---PGCQLPS-VNIDQRQAAYDATRLL--LNHGHTRIAFLGGPLEEFAGLSRFQGYRQALedAGVPfR 211
Cdd:cd06308 80 aGIPVIV---LDrkvSGDDYTAfIGADNVEIGRQAGEYIaeLLNGKGNVVEIQGLPGSSPAIDRHKGFLEAI--AKYP-G 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 212 EELV--QIADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRvpEDVEVIGFDNIR--LASMVRP-TL 286
Cdd:cd06308 154 IKIVasQDGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGRE--KEIKIIGVDGLPeaGEKAVKDgIL 231
|
250 260
....*....|....*....|....*...
gi 1900939922 287 T-TVAQPmyDIGAVSMRLLTKYMHNEKV 313
Cdd:cd06308 232 AaTFLYP--TGGKEAIEAALKILNGEKV 257
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
62-274 |
4.80e-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: 380540 [Multi-domain] Cd Length: 281 Bit Score: 53.53 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVTDEHLDLFRS--AS 139
Cdd:cd06317 1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRAseAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 140 VPVV-LATTIDPGCQLPSVNIDQRQAAYDATRLLL------NHGHTRIAFLGGpLEEFAGLSRFQGYRQALED-AGVpfr 211
Cdd:cd06317 81 IPVIaYDAVIPSDFQAAQVGVDNLEGGKEIGKYAAdyikaeLGGQAKIGVVGA-LSSLIQNQRQKGFEEALKAnPGV--- 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1900939922 212 eELVQIADYR--YETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGfrVPEDVEVIGFD 274
Cdd:cd06317 157 -EIVATVDGQnvQEKALSAAENLLTANPDLDAIYATGEPALLGAVAAVRSQG--RQGKIKVFGWD 218
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
62-319 |
1.42e-07 |
|
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species; Periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species. GGBP is a member of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic GGBP is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380481 [Multi-domain] Cd Length: 302 Bit Score: 52.20 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIAN-MYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPRVT--DEHLDLFRSA 138
Cdd:cd01539 2 KIGVFIYNYDDTFISSVRKALEKAAKaGGKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTaaQTIIDKAKAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 139 SVPVVLATTIdpgcqlPSVNIDQR--QAAY---DAT-------RLLLNH------------GHTRIAFLGGPLEEFAGLS 194
Cdd:cd01539 82 NIPVIFFNRE------PSREDLKSydKAYYvgtDAEesgimqgEIIADYwkanpeidkngdGKIQYVMLKGEPGHQDAIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 195 RFQGYRQALEDAGVPFREELVQIADYRYETALKRMAHFLT-LPERPTAVFATSDEMAVAAIHAYQDAGF---RVPEDVEV 270
Cdd:cd01539 156 RTKYSVKTLNDAGIKTEQLAEDTANWDRAQAKDKMDAWLSkYGDKIELVIANNDDMALGAIEALKAAGYntgDGDKYIPV 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1900939922 271 IGFDNIR--LASMVRPTLT-TVAQPMYDIGAVSMRLLTKYMHNEKVTDSLVF 319
Cdd:cd01539 236 FGVDATPeaLEAIKEGKMLgTVLNDAKAQAKAIYELAKNLANGKEPLETGYK 287
|
|
| PRK09701 |
PRK09701 |
D-allose transporter substrate-binding protein; |
65-315 |
3.23e-07 |
|
D-allose transporter substrate-binding protein;
Pssm-ID: 182037 [Multi-domain] Cd Length: 311 Bit Score: 51.03 E-value: 3.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 65 VIIPDIASAFYAELARGIEDIANM--YKYNIILCNSDKQPKKELTLIETLLEKQVDGLLF-------MGPRVT------- 128
Cdd:PRK09701 29 VVLKTLSNPFWVDMKKGIEDEAKTlgVSVDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFaplssvnLVMPVArawkkgi 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 129 -----DEHLDL--FRSASVPVVLATTIDpgcqlpSVNIDQRQAAYDATRLLLNHGhtRIAFLGGPLEEFAGLSRFQGYRQ 201
Cdd:PRK09701 109 ylvnlDEKIDMdnLKKAGGNVEAFVTTD------NVAVGAKGASFIIDKLGAEGG--EVAIIEGKAGNASGEARRNGATE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 202 ALEDAGvpfREELV--QIADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRvpEDVEVIGFDNIRLA 279
Cdd:PRK09701 181 AFKKAS---QIKLVasQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKT--GKVLVVGTDGIPEA 255
|
250 260 270
....*....|....*....|....*....|....*....
gi 1900939922 280 -SMV--RPTLTTVAQPMYDIGAVSMRLLTKYMHNEKVTD 315
Cdd:PRK09701 256 rKMVeaGQMTATVAQNPADIGATGLKLMVDAEKSGKVIP 294
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
70-313 |
4.16e-07 |
|
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: 50.73 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 70 IASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLFMGPrvtdehldlFRSASVPVVLATTID 149
Cdd:cd01391 12 IREQFGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGPGS---------SSVAIVIQNLAQLFD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 150 -PGCQLPSVNIDQRQAAY------------DATRLLLNH----GHTRIAFLGGPLEEFaGLSRFQGYRQALEDAGVpfRE 212
Cdd:cd01391 83 iPQLALDATSQDLSDKTLykyflsvvfsdtLGARLGLDIvkrkNWTYVAAIHGEGLNS-GELRMAGFKELAKQEGI--CI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 213 ELVQIADY-RYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRvpEDVEVIGFDNIRLASMVR-----PTL 286
Cdd:cd01391 160 VASDKADWnAGEKGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLV--GDVSVIGSDGWADRDEVGyeveaNGL 237
|
250 260
....*....|....*....|....*..
gi 1900939922 287 TTVAQPMYDIGAVSMRLLTKYMHNEKV 313
Cdd:cd01391 238 TTIKQQKMGFGITAIKAMADGSQNMHE 264
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
82-265 |
1.60e-06 |
|
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.
Pssm-ID: 380651 [Multi-domain] Cd Length: 302 Bit Score: 49.16 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 82 IEDIANMYKYNI---ILCNSDKQPKKELTLIETLLEKQVDGLLfMGPRVTDEHLDLFRSAS---VPVVLATTIDPGCQLP 155
Cdd:cd19996 21 FEAEAAKLKKLIkelIYTDAQGDTQKQIADIQDLIAQGVDAII-VSPNSPTALLPAIEKAAaagIPVVLFDSGVGSDKYT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 156 S-VNIDQ-----RQAAYDATRLllnHGHTRIAFLGGPleefAGLS----RFQGYRQALEDAgvPFREEL-VQIADYRYET 224
Cdd:cd19996 100 AfVGVDDaafgrVGAEWLVKQL---GGKGNIIALRGI----AGVSvsedRWAGAKEVFKEY--PGIKIVgEVYADWDYAK 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1900939922 225 ALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRVP 265
Cdd:cd19996 171 AKQAVESLLAAYPDIDGVWSDGGAMTLGAIEAFEEAGRPLV 211
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
65-324 |
4.59e-06 |
|
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs; Periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs from other bacteria. They are members of the type 1 periplasmic binding protein superfamily which consists of two domains connected by a three-stranded hinge. TmGBP is specific for glucose and its binding pocket is buried at the interface of the two domains. TmGBP also exhibits high thermostability and the highest structural similarity to E. coli glucose binding protein (ecGBP).
Pssm-ID: 380537 [Multi-domain] Cd Length: 271 Bit Score: 47.58 E-value: 4.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 65 VIIPDIASAFYAELAR-GIEDIANMYKYNIILCNSDK-QPKKELTLIETLLEKQVDGLLFMG---PRVTDEhLDLFRSAS 139
Cdd:cd06314 3 ALVPKGLNNPFWDLAEaGAEKAAKELGVNVEFVGPQKsDAAEQVQLIEDLIARGVDGIAISPndpEAVTPV-INKAADKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 140 VPVVlatTID---PGCQ-LPSVNIDQRQAAYDATRL---LLNHGHTRIAFLGGPLEEFAgLSRFQGYRQALEDAgvpFRE 212
Cdd:cd06314 82 IPVI---TFDsdaPDSKrLAYIGTDNYEAGREAGELmkkALPGGGKVAIITGGLGADNL-NERIQGFKDALKGS---PGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 213 ELVQI---ADYRyETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRvpEDVEVIGFDNirlasmVRPTLT-- 287
Cdd:cd06314 155 EIVDPlsdNDDI-AKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKV--GKVKIVGFDT------LPETLQgi 225
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1900939922 288 -------TVAQPMYDIGAVSMRLLTKYMHNEKVTDSLVFLPHTI 324
Cdd:cd06314 226 kdgviaaTVGQRPYEMGYLSVKLLYKLLKGGKPVPDVIDTGVDV 269
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
74-275 |
1.28e-05 |
|
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr 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: 380621 [Multi-domain] Cd Length: 278 Bit Score: 46.16 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 74 FYAELARGIEDIANMY--KYNIILCNSDkqPKKELTLIETLLEKQVDGLLFMGP---RVTDEHLDLFRSASVPVVLATTI 148
Cdd:cd19966 14 FWTVVYNGAKDAAADLgvDLDYVFSSWD--PEKMVEQFKEAIAAKPDGIAIMGHpgdGAYTPLIEAAKKAGIIVTSFNTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 149 DPGCQLPS-----VNIDQRQAAYD-ATRLLLNH----GHTRIAFLGGPLEEFAGLsRFQGYRQALEDAGVPFREELVQIA 218
Cdd:cd19966 92 LPKLEYGDcglgyVGADLYAAGYTlAKELVKRGglktGDRVFVPGLLPGQPYRVL-RTKGVIDALKEAGIKVDYLEISLE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1900939922 219 DYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGFRvPEDVEVIGFDN 275
Cdd:cd19966 171 PNKPAEGIPVMTGYLAANPDVKAIVGDGGGLTANVAKYLKAAGKK-PGEIPVAGFDL 226
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
63-201 |
1.09e-04 |
|
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: 43.32 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 63 VGVIIPDIASAFYAELARGIEDIANMYK-YNI---ILCNSDKQPKKELTLIETLLEkQVDGLLFMG---PRVTDEhLDLF 135
Cdd:cd06307 2 FGFLLPSPENPFYELLRRAIEAAAAALRdRRVrlrIHFVDSLDPEALAAALRRLAA-GCDGVALVApdhPLVRAA-IDEL 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1900939922 136 RSASVPVV-LATTIDPGCQLPSVNIDQRQ----AAYDATRLLLNHGHtRIAFlggpleeFAGLSRFQGYRQ 201
Cdd:cd06307 80 AARGIPVVtLVSDLPGSRRLAYVGIDNRAagrtAAWLMGRFLGRRPG-KVLV-------ILGSHRFRGHEE 142
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
62-274 |
3.50e-04 |
|
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: 41.63 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLF--MGPRVTDEHLDLFRSAS 139
Cdd:cd06318 1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILnpVDPEGLTPAVKAAKAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 140 VPVV-LATTIDPGCQLPS-VNIDQRQAAYDATRLLLNH-GHTR--IAFLGGPLEEFAGLSRFQGYRQALEDA-GVPFREE 213
Cdd:cd06318 81 IPVItVDSALDPSANVATqVGRDNKQNGVLVGKEAAKAlGGDPgkIIELSGDKGNEVSRDRRDGFLAGVNEYqLRKYGKS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1900939922 214 LVQIADYRY-----ETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAGfrVPEDVEVIGFD 274
Cdd:cd06318 161 NIKVVAQPYgnwirSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAG--MLDKVKVAGAD 224
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
62-261 |
5.99e-04 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380534 [Multi-domain] Cd Length: 270 Bit Score: 40.81 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 62 TVGVIIPDI------ASAFYAELArgIEDIANMyKYNIILCNSdkqPKKELTLIETLLEKQVDGLLFMGprvtdehldlF 135
Cdd:cd06311 1 TIGISIPSAdhgwtaGVAYYAEKQ--AKELADL-EYKLVTSSN---ANEQVSQLEDLIAQKVDAIVILP----------Q 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 136 RSASVPVVLATTIDPGcqLPSVNIDQRQAAYDATRLL------------------LNhGHTRIAFLGGPLEEFAGLSRFQ 197
Cdd:cd06311 65 DSEELTVAAQKAKDAG--IPVVNFDRGLNVLIYDLYVagdnpgmgvvsaeyigkkLG-GKGNVVVLEVPSSGSVNEERVA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1900939922 198 GYRQALEDAgVPFREELVQIADYRYETALKRMAHFLTLPERPTAVFATSDEMAVAAIHAYQDAG 261
Cdd:cd06311 142 GFKEVIKGN-PGIKILAMQAGDWTREDGLKVAQDILTKNKKIDAVWAADDDMAIGVLQAIKEAG 204
|
|
| PBP1_arabinose_binding |
cd01540 |
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ... |
63-272 |
3.52e-03 |
|
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily; Periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. ABP is only involved in transport contrary to other related sugar-binding proteins such as the glucose/galactose-binding protein (GGBP) and the ribose-binding protein (RBP), both of which are involved in chemotaxis as well as transport. The periplasmic ABP consists of two alpha/beta globular domains connected by a three-stranded hinge, a Venus flytrap-like domain, which undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, ABP is homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380482 [Multi-domain] Cd Length: 294 Bit Score: 38.81 E-value: 3.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 63 VGVIIPDIASAFYAELARGIEDIANMYKYNIILCNSDKQPKKELTLIETLLEKQVDGLLF------MGPRVtdehLDLFR 136
Cdd:cd01540 2 IGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKIDAKMDGEKVLSAIDNLIAQGAQGIVIctpdqkLGPAI----AAKAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1900939922 137 SASVPVVLA----TTIDPGCQLPSVNIDQRQ---------AAYDATRLLLNHGHTRIAFLggpleEFAGLS----RFQGY 199
Cdd:cd01540 78 AAGIPVIAVddqlVDADPMKIVPFVGIDAYKigeavgewlAKEMKKRGWDDVKEVGVLAI-----TMDTLSvcvdRTDGA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1900939922 200 RQALEDAGVPfREELVQI--ADYRYETALKRMAHFLTL-PE-RPTAVFATSDEMAVAAIHAYQDAGFRvPEDVEVIG 272
Cdd:cd01540 153 KDALKAAGFP-EDQIFQApyKGTDTEGAFNAANAVITAhPEvKHWLVVGCNDEGVLGAVRALEQAGFD-AEDIIGVG 227
|
|
| |
