|
Name |
Accession |
Description |
Interval |
E-value |
| ccpA |
TIGR01481 |
catabolite control protein A; Catabolite control protein A is a LacI family global ... |
2-332 |
0e+00 |
|
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: 538.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 2 NVTIYDVAREANVSMATVSRVVNGNPNVKPTTRKKVLEAIDRLGYRPNAVARGLASKKTTTVGVIIPDISNTFYAELARG 81
Cdd:TIGR01481 1 TVTIYDVAREAGVSMATVSRVVNGNPNVKPATRKKVLEVIKRLDYRPNAVARGLASKRTTTVGVIIPDISNIYYAELARG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 82 IEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPVPIVLAASFDEQNETPSVNIDY 161
Cdd:TIGR01481 81 IEDIATMYKYNIILSNSDEDPEKEVQVLNTLLSKQVDGIIFMGGTITEKLREEFSRSPVPVVLAGTVDKENELPSVNIDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 162 TQAAYDAMKHFIEQGHKRIGFVSGPFIDKAGSAKKLQGYKKALEEAGISYDENLVIDGDYTYDSGIEAFEKLWSNdeKPT 241
Cdd:TIGR01481 161 KQATKEAVGELIAKGHKSIAFVGGPLSDSINGEDRLEGYKEALNKAGIQFGEDLVCEGKYSYDAGYKAFAELKGS--LPT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 242 AIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVAMRLLTKYMNKEKVEDHTVIL 321
Cdd:TIGR01481 239 AVFVASDEMAAGILNAAMDAGIKVPEDLEVITSNNTRLTEMVRPQLSTIIQPLYDIGAVAMRLLTKYMNDEELEEKTVVL 318
|
330
....*....|.
gi 2437085935 322 PHRIQFRDSTK 332
Cdd:TIGR01481 319 PHGIELRGSTK 329
|
|
| PurR |
COG1609 |
DNA-binding transcriptional regulator, LacI/PurR family [Transcription]; |
1-332 |
2.94e-151 |
|
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
Pssm-ID: 441217 [Multi-domain] Cd Length: 335 Bit Score: 428.08 E-value: 2.94e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 1 MNVTIYDVAREANVSMATVSRVVNGNPNVKPTTRKKVLEAIDRLGYRPNAVARGLASKKTTTVGVIIPDISNTFYAELAR 80
Cdd:COG1609 2 KRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 81 GIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPVPIVLAASFDEQNETPSVNID 160
Cdd:COG1609 82 GIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRPLPDPGVPSVGVD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 161 YTQAAYDAMKHFIEQGHKRIGFVSGPfIDKAGSAKKLQGYKKALEEAGISYDENLVIDGDYTYDSGIEAFEKLWSNDEKP 240
Cdd:COG1609 162 NRAGARLATEHLIELGHRRIAFIGGP-ADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEAARRLLARGPRP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 241 TAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVAMRLLTKYMNKEKVEDHTVI 320
Cdd:COG1609 241 TAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERVL 320
|
330
....*....|..
gi 2437085935 321 LPHRIQFRDSTK 332
Cdd:COG1609 321 LPPELVVRESTA 332
|
|
| PBP1_CcpA |
cd06298 |
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ... |
62-330 |
1.97e-147 |
|
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: 415.92 E-value: 1.97e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPVP 141
Cdd:cd06298 1 TVGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMGDELTEEIREEFKRSPVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 142 IVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFIDKAGSAKKLQGYKKALEEAGISYDENLVIDGDY 221
Cdd:cd06298 81 VVLAGTVDSDHEIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSGPLKEYINNDKKLQGYKRALEEAGLEFNEPLIFEGDY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 222 TYDSGIEAFEKLwSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVA 301
Cdd:cd06298 161 DYDSGYELYEEL-LESGEPDAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPLYDIGAVA 239
|
250 260
....*....|....*....|....*....
gi 2437085935 302 MRLLTKYMNKEKVEDHTVILPHRIQFRDS 330
Cdd:cd06298 240 MRLLTKLMNKEEVEETIVKLPHSIIWRQS 268
|
|
| PBP1_CcpA-like |
cd19975 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
62-330 |
1.36e-116 |
|
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: 337.61 E-value: 1.36e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPVP 141
Cdd:cd19975 1 TIGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFASGTLTEENKQLLKNMNIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 142 IVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFIDKAGSAKKLQGYKKALEEAGISYDENLVIDGDY 221
Cdd:cd19975 81 VVLVSTESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISGPLDDPNAGYPRYEGYKKALKDAGLPIKENLIVEGDF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 222 TYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVA 301
Cdd:cd19975 161 SFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQPFYEMGKKA 240
|
250 260
....*....|....*....|....*....
gi 2437085935 302 MRLLTKYMNKEKVEDHTVILPHRIQFRDS 330
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 ... |
62-325 |
2.13e-109 |
|
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: 319.08 E-value: 2.13e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPVP 141
Cdd:cd06267 1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLAAGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 142 IVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPfIDKAGSAKKLQGYKKALEEAGISYDENLVIDGDY 221
Cdd:cd06267 81 VVLIDRRLDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGP-LDLSTSRERLEGYRDALAEAGLPVDPELVVEGDF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 222 TYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVA 301
Cdd:cd06267 160 SEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEMGRAA 239
|
250 260
....*....|....*....|....
gi 2437085935 302 MRLLTKYMNKEKVEDHTVILPHRI 325
Cdd:cd06267 240 AELLLERIEGEEEPPRRIVLPTEL 263
|
|
| PBP1_LacI-like |
cd06284 |
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ... |
62-330 |
5.48e-98 |
|
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: 290.21 E-value: 5.48e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPvP 141
Cdd:cd06284 1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILLSGRLDAELLSELSKRY-P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 142 IVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPfiDKAGSAKK-LQGYKKALEEAGISYDENLVIDGD 220
Cdd:cd06284 80 IVQCCEYIPDSGVPSVSIDNEAAAYDATEYLISLGHRRIAHINGP--LDNVYARErLEGYRRALAEAGLPVDEDLIIEGD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 221 YTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAV 300
Cdd:cd06284 158 FSFEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIGET 237
|
250 260 270
....*....|....*....|....*....|
gi 2437085935 301 AMRLLTKYMNKEKVEDHTVILPHRIQFRDS 330
Cdd:cd06284 238 AAELLLEKIEGEGVPPEHIILPHELIVRES 267
|
|
| PRK11041 |
PRK11041 |
DNA-binding transcriptional regulator CytR; Provisional |
29-331 |
2.21e-85 |
|
DNA-binding transcriptional regulator CytR; Provisional
Pssm-ID: 182923 [Multi-domain] Cd Length: 309 Bit Score: 259.54 E-value: 2.21e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 29 VKPTTRKKVLEAIDRLGYRPNAVARGLASKKTTTVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHL 108
Cdd:PRK11041 4 VSQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKTF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 109 LNTMLGKQVDGIVFMGEDIT-DIHIEEFKKSPvPIVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPf 187
Cdd:PRK11041 84 VNLIITKQIDGMLLLGSRLPfDASKEEQRNLP-PMVMANEFAPELELPTVHIDNLTAAFEAVNYLHELGHKRIACIAGP- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 188 IDKAGSAKKLQGYKKALEEAGISYDENLVIDGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPT 267
Cdd:PRK11041 162 EEMPLCHYRLQGYVQALRRCGITVDPQYIARGDFTFEAGAKALKQLLDLPQPPTAVFCHSDVMALGALSQAKRMGLRVPQ 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2437085935 268 DVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVAMRLLTKYMNKEKVEDHTVILPHRIQFRDST 331
Cdd:PRK11041 242 DLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHVSSGSRLLDCELIIRGST 305
|
|
| PBP1_LacI-like |
cd06285 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-331 |
1.04e-83 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380508 [Multi-domain] Cd Length: 269 Bit Score: 254.07 E-value: 1.04e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPVP 141
Cdd:cd06285 1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQELAARGVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 142 IVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPfiDKAGSAK-KLQGYKKALEEAGISYDENLVIDGD 220
Cdd:cd06285 81 VVLVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGP--LNASTGRdRLRGYRRALAEAGLPVPDERIVPGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 221 YTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAV 300
Cdd:cd06285 159 FTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEMGRR 238
|
250 260 270
....*....|....*....|....*....|.
gi 2437085935 301 AMRLLTKYMNKEKVEDHTVILPHRIQFRDST 331
Cdd:cd06285 239 AAELLLQLIEGGGRPPRSITLPPELVVREST 269
|
|
| PBP1_PurR |
cd06275 |
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ... |
62-330 |
3.81e-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: 247.55 E-value: 3.81e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKK-SPV 140
Cdd:cd06275 1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAELLAAlRSI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 141 PIVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPfIDKAGSAKKLQGYKKALEEAGISYDENLVIDGD 220
Cdd:cd06275 81 PVVVLDREIAGDNADAVLDDSFQGGYLATRHLIELGHRRIGCITGP-LEHSVSRERLAGFRRALAEAGIEVPPSWIVEGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 221 YTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAV 300
Cdd:cd06275 160 FEPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQPKDELGEL 239
|
250 260 270
....*....|....*....|....*....|.
gi 2437085935 301 AMRLLTKYM-NKEKVEDHTVILPHRIQfRDS 330
Cdd:cd06275 240 AVELLLDRIeNKREEPQSIVLEPELIE-RES 269
|
|
| PBP1_sucrose_transcription_regulator |
cd06288 |
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ... |
62-330 |
1.80e-79 |
|
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: 243.22 E-value: 1.80e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYA-ELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSpV 140
Cdd:cd06288 1 TIGLITDDIATTPFAgDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYASMHHREVTLPPELTD-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 141 PIVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPfIDKAGSAKKLQGYKKALEEAGISYDENLVIDGD 220
Cdd:cd06288 80 PLVLLNCFDDDPSLPSVVPDDEQGGYLATRHLIEAGHRRIAFIGGP-EDSLATRLRLAGYRAALAEAGIPYDPSLVVHGD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 221 YTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAV 300
Cdd:cd06288 159 WGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVALPYYEMGRR 238
|
250 260 270
....*....|....*....|....*....|
gi 2437085935 301 AMRLLTKYMNKEKVEDHTVILPHRIQFRDS 330
Cdd:cd06288 239 AAELLLDGIEGEPPEPGVIRVPCPLIERES 268
|
|
| PBP1_DegA_Like |
cd19976 |
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ... |
62-330 |
2.08e-79 |
|
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: 242.93 E-value: 2.08e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDI-TDIHIEEFKKSPV 140
Cdd:cd19976 1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNIsDEAIIKLLKEEKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 141 PIVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPfIDKAGSAKKLQGYKKALEEAGISYDENLVIDGD 220
Cdd:cd19976 81 PVVVLDRYIEDNDSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGP-PSTYNEHERIEGYKNALQDHNLPIDESWIYSGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 221 YTYDSGIEAFEKLWSNdEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAV 300
Cdd:cd19976 160 SSLEGGYKAAEELLKS-KNPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQPIFEMGQE 238
|
250 260 270
....*....|....*....|....*....|
gi 2437085935 301 AMRLLTKYMNKEKVEDHTVILPHRIQFRDS 330
Cdd:cd19976 239 AAKLLLKIIKNPAKKKEEIVLPPELIKRDS 268
|
|
| PBP1_LacI-like |
cd06280 |
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ... |
62-328 |
5.80e-79 |
|
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria; This group includes the ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus saprophyticus and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.
Pssm-ID: 380503 [Multi-domain] Cd Length: 266 Bit Score: 241.78 E-value: 5.80e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPVP 141
Cdd:cd06280 1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGPSRELKRLLKHGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 142 IVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPfIDKAGSAKKLQGYKKALEEAGISYDENLVIDGDY 221
Cdd:cd06280 81 IVLIDREVEGLELDLVAGDNREGAYKAVKHLIELGHRRIGLITGP-LEISTTRERLAGYREALAEAGIPVDESLIFEGDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 222 TYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVA 301
Cdd:cd06280 160 TIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQPAYEIGRIA 239
|
250 260
....*....|....*....|....*..
gi 2437085935 302 MRLLTKYMNKEKVEDHTVILPHRIQFR 328
Cdd:cd06280 240 AQLLLERIEGQGEEPRRIVLPTELIIR 266
|
|
| PBP1_Qymf-like |
cd06291 |
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ... |
62-330 |
2.54e-78 |
|
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: 240.11 E-value: 2.54e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVfMGEDITDIhiEEFKKSPVP 141
Cdd:cd06291 1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGII-LGSHSLDI--EEYKKLNIP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 142 IVlaaSFD--EQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFIDKAgSAKKLQGYKKALEEAGISYDENLVIDG 219
Cdd:cd06291 78 IV---SIDryLSEGIPSVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSP-ANERYRGFEDALKEAGIEYEIIEIDEN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 220 DYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGA 299
Cdd:cd06291 154 DFSEEDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIEEMAK 233
|
250 260 270
....*....|....*....|....*....|.
gi 2437085935 300 VAMRLLTKYMNKEKVEDHTVILPHRIQFRDS 330
Cdd:cd06291 234 EAVELLLKLIEGEEIEESRIVLPVELIERET 264
|
|
| PBP1_LacI-like |
cd06290 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-330 |
6.49e-77 |
|
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: 236.74 E-value: 6.49e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSpVP 141
Cdd:cd06290 1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEELLKLLAEG-IP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 142 IVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPfIDKAGSAKKLQGYKKALEEAGISYDENLVIDGDY 221
Cdd:cd06290 80 VVLVDRELEGLNLPVVNVDNEQGGYNATNHLIDLGHRRIVHISGP-EDHPDAQERYAGYRRALEDAGLEVDPRLIVEGDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 222 TYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVA 301
Cdd:cd06290 159 TEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYEMGKTA 238
|
250 260
....*....|....*....|....*....
gi 2437085935 302 MRLLTKYMNKEKVEDHTVILPHRIQFRDS 330
Cdd:cd06290 239 AEILLELIEGKGRPPRRIILPTELVIRES 267
|
|
| PBP1_EndR-like |
cd19977 |
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ... |
62-320 |
2.91e-75 |
|
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: 232.42 E-value: 2.91e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFM--GEDITDIhiEEFKKSP 139
Cdd:cd19977 1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAptGGNEDLI--EKLVKSG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 140 VPIVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFIDKAGSaKKLQGYKKALEEAGISYDENLvIDG 219
Cdd:cd19977 79 IPVVFVDRYIPGLDVDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLELSTRQ-ERLEGYKAALADHGLPVDEEL-IKH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 220 DYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGA 299
Cdd:cd19977 157 VDRQDDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQPTYEIGR 236
|
250 260
....*....|....*....|.
gi 2437085935 300 VAMRLLTKYMNKEKVEDHTVI 320
Cdd:cd19977 237 KAAELLLDRIENKPKGPPRQI 257
|
|
| PBP1_GalS-like |
cd06270 |
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ... |
62-325 |
5.20e-73 |
|
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: 226.63 E-value: 5.20e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPVP 141
Cdd:cd06270 1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEELILIAEKIPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 142 IVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFiDKAGSAKKLQGYKKALEEAGISYDENLVIDGDY 221
Cdd:cd06270 81 LVVINRYIPGLADRCVWLDNEQGGRLAAEHLLDLGHRRIACITGPL-DIPDARERLAGYRDALAEAGIPLDPSLIIEGDF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 222 TYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVA 301
Cdd:cd06270 160 TIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHYPIEEMAQAA 239
|
250 260
....*....|....*....|....
gi 2437085935 302 MRLLTKYMNKEKVEDHTVILPHRI 325
Cdd:cd06270 240 AELALNLAYGEPLPISHEFTPTLI 263
|
|
| PRK10423 |
PRK10423 |
transcriptional repressor RbsR; Provisional |
7-330 |
3.08e-70 |
|
transcriptional repressor RbsR; Provisional
Pssm-ID: 182448 [Multi-domain] Cd Length: 327 Bit Score: 221.50 E-value: 3.08e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 7 DVAREANVSMATVSRVVNGNPNVKPTTRKKVLEAIDRLGYRPNAVARGLASKKTTTVGVIIPDISNTFYAELARGIEDIA 86
Cdd:PRK10423 3 DVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVERSC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 87 TMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMgedITDIHI---EEFKKSP-VPIVLA--ASFDEQNETPSVNid 160
Cdd:PRK10423 83 FERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLL---CTETHQpsrEIMQRYPsVPTVMMdwAPFDGDSDLIQDN-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 161 YTQAAYDAMKHFIEQGHKRIGFVSGPfIDKAGSAKKLQGYKKALEEAGISYDENLVIDGDYTYDSGIEAFEKLWSNDEKP 240
Cdd:PRK10423 158 SLLGGDLATQYLIDKGYTRIACITGP-LDKTPARLRLEGYRAAMKRAGLNIPDGYEVTGDFEFNGGFDAMQQLLALPLRP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 241 TAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVAMRLLTKYMNKEKVEDHTVI 320
Cdd:PRK10423 237 QAVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQRLQ 316
|
330
....*....|
gi 2437085935 321 LPHRIQFRDS 330
Cdd:PRK10423 317 LTPELMERGS 326
|
|
| PBP1_SalR |
cd01545 |
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ... |
62-330 |
4.16e-70 |
|
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: 219.35 E-value: 4.16e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNII---LSNSDQNKEKEfhLLNTMLGKQVDGIVF---MGEDiTDIhIEEF 135
Cdd:cd01545 1 LIGLLYDNPSASYVSALQVGALRACREAGYHLVvepCDSDDEDLADR--LRRFLSRSRPDGVILtppLSDD-PAL-LDAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 136 KKSPVPIVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPfIDKAGSAKKLQGYKKALEEAGISYDENL 215
Cdd:cd01545 77 DELGIPYVRIAPGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGP-PDHGASAERLEGFRDALAEAGLPLDPDL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 216 VIDGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMY 295
Cdd:cd01545 156 VVQGDFTFESGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTTVRQPIA 235
|
250 260 270
....*....|....*....|....*....|....*
gi 2437085935 296 DIGAVAMRLLTKYMNKEKVEDHTVILPHRIQFRDS 330
Cdd:cd01545 236 EMARRAVELLIAAIRGAPAGPERETLPHELVIRES 270
|
|
| PRK10703 |
PRK10703 |
HTH-type transcriptional repressor PurR; |
4-323 |
5.25e-69 |
|
HTH-type transcriptional repressor PurR;
Pssm-ID: 236739 [Multi-domain] Cd Length: 341 Bit Score: 218.83 E-value: 5.25e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 4 TIYDVAREANVSMATVSRVVNGNPNVKPTTRKKVLEAIDRLGYRPNAVARGLASKKTTTVGVIIPDISNTFYAELARGIE 83
Cdd:PRK10703 3 TIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEAVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 84 DIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKK-SPVPIVLAASFDEQNETPSVNIDYT 162
Cdd:PRK10703 83 KNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLLAMLEEyRHIPMVVMDWGEAKADFTDAIIDNA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 163 -QAAYDAMKHFIEQGHKRIGFVSGPfIDKAGSAKKLQGYKKALEEAGISYDENLVIDGDYTYDSGIEAFEKLWSNDEKPT 241
Cdd:PRK10703 163 fEGGYLAGRYLIERGHRDIGVIPGP-LERNTGAGRLAGFMKAMEEANIKVPEEWIVQGDFEPESGYEAMQQILSQKHRPT 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 242 AIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVAMRLLTKYMNkEKVEDHTVIL 321
Cdd:PRK10703 242 AVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRIV-NKREEPQTIE 320
|
..
gi 2437085935 322 PH 323
Cdd:PRK10703 321 VH 322
|
|
| PBP1_LacI-like |
cd06273 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-330 |
1.20e-67 |
|
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: 212.75 E-value: 1.20e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDitdiHIEEF----KK 137
Cdd:cd06273 1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVGSD----HDPELfellEQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 138 SPVPIVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFIDKAGSAKKLQGYKKALEEAGISYDENLVI 217
Cdd:cd06273 77 RQVPYVLTWSYDEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGNDRARARLAGIRDALAERGLELPEERVV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 218 DGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDI 297
Cdd:cd06273 157 EAPYSIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPAREI 236
|
250 260 270
....*....|....*....|....*....|...
gi 2437085935 298 GAVAMRLLTKYMNKEKVEDHTViLPHRIQFRDS 330
Cdd:cd06273 237 GELAARYLLALLEGGPPPKSVE-LETELIVRES 268
|
|
| PBP1_GntR |
cd01575 |
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ... |
62-330 |
1.56e-65 |
|
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: 207.35 E-value: 1.56e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPVP 141
Cdd:cd01575 1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEHTPATRKLLRAAGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 142 IVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFIDKAGSAKKLQGYKKALEEAGISYDENLVIDGDY 221
Cdd:cd01575 81 VVETWDLPDDPIDMAVGFSNFAAGRAMARHLIERGYRRIAFVGARLDGDSRARQRLEGFRDALAEAGLPLPLVLLVELPS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 222 TYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVA 301
Cdd:cd01575 161 SFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVRVPRYEIGRKA 240
|
250 260
....*....|....*....|....*....
gi 2437085935 302 MRLLTKYMNKEKVEDHTVILPHRIQFRDS 330
Cdd:cd01575 241 AELLLARLEGEEPEPRVVDLGFELVRRES 269
|
|
| PBP1_CcpB-like |
cd06286 |
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ... |
62-328 |
2.86e-65 |
|
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: 206.63 E-value: 2.86e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPvP 141
Cdd:cd06286 1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLIITSRENDWEVIEPYAKYG-P 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 142 IVLAASfDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSG-PFIDKAGSAKKLQGYKKALEEAGISYDENLVIDGD 220
Cdd:cd06286 80 IVLCEE-TDSPDIPSVYIDRYEAYLEALEYLKEKGHRKIGYCLGrPESSSASTQARLKAYQDVLGEHGLSLREEWIFTNC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 221 YTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMvrPQLSTVVQPMYDIGAV 300
Cdd:cd06286 159 HTIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISEL--LNLTTIDQPLEEMGKE 236
|
250 260
....*....|....*....|....*...
gi 2437085935 301 AMRLLTKYMNKEKVEDHtvILPHRIQFR 328
Cdd:cd06286 237 AFELLLSQLESKEPTKK--ELPSKLIER 262
|
|
| PBP1_MalR-like |
cd06294 |
ligand-binding domain of maltose transcription regulator MalR which is a member of the ... |
62-325 |
5.03e-65 |
|
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: 206.28 E-value: 5.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDIS-----NTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFK 136
Cdd:cd06294 1 TIGLVLPSSAeelfqNPFFSEVLRGISQVANENGYSLLLATGNTEEELLEEVKRMVRGRRVDGFILLYSKEDDPLIEYLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 137 KSPVPIVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFiDKAGSAKKLQGYKKALEEAGISYDENLV 216
Cdd:cd06294 81 EEGFPFVVIGKPLDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDK-NLVVSIDRLQGYKQALKEAGLPLDDDYI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 217 IDGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTV-VQPmY 295
Cdd:cd06294 160 LLLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSVdINP-Y 238
|
250 260 270
....*....|....*....|....*....|
gi 2437085935 296 DIGAVAMRLLTKYMNKEKVEDHTVILPHRI 325
Cdd:cd06294 239 ELGREAAKLLINLLEGPESLPKNVIVPHEL 268
|
|
| PBP1_LacI-like |
cd06293 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-330 |
2.71e-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: 380516 [Multi-domain] Cd Length: 270 Bit Score: 204.43 E-value: 2.71e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPVP 141
Cdd:cd06293 1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSHLARLRARGTA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 142 IVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFiDKAGSAKKLQGYKKALEEAGISYDENLVID--G 219
Cdd:cd06293 81 VVLLDRPAPGPAGCSVSVDDVQGGALAVDHLLELGHRRIAFVSGPL-RTRQVAERLAGARAAVAEAGLDPDEVVRELsaP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 220 DYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGA 299
Cdd:cd06293 160 DANAELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQPSYELGR 239
|
250 260 270
....*....|....*....|....*....|.
gi 2437085935 300 VAMRLLTKYMNKEKVEDHTVILPHRIQFRDS 330
Cdd:cd06293 240 AAADLLLDEIEGPGHPHEHVVFQPELVVRSS 270
|
|
| PBP1_LacI-like |
cd06299 |
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ... |
62-310 |
3.43e-63 |
|
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: 201.35 E-value: 3.43e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFM--GEDITdiHIEEFKKSP 139
Cdd:cd06299 1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAVptGENSE--GLQALIAQG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 140 VPIVLAA-SFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPfIDKAGSAKKLQGYKKALEEAGISYDENLVID 218
Cdd:cd06299 79 LPVVFVDrEVEGLGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYISGP-LSTSTGRERLAAFRAALTAAGIPIDEELVAF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 219 GDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIG 298
Cdd:cd06299 158 GDFRQDSGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVERIG 237
|
250
....*....|..
gi 2437085935 299 AVAMRLLTKYMN 310
Cdd:cd06299 238 RRAVELLLALIE 249
|
|
| PBP1_TreR-like |
cd01542 |
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ... |
62-320 |
3.72e-63 |
|
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: 201.18 E-value: 3.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPVP 141
Cdd:cd01542 1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEITDEHRKALKKLKIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 142 IVLAASfdEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFIDKAGSAKKLQGYKKALEEAGIsyDENLVIDGDY 221
Cdd:cd01542 81 VVVLGQ--EHEGFSCVYHDDYGAGKLLGEYLLKKGHKNIAYIGVDEEDIAVGVARKQGYLDALKEHGI--DEVEIVETDF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 222 TYDSGIEAFEKLWSNdEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVA 301
Cdd:cd01542 157 SMESGYEAAKELLKE-NKPDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEAGEKA 235
|
250
....*....|....*....
gi 2437085935 302 MRLLTKYMNKEKVEDHTVI 320
Cdd:cd01542 236 AELLLDMIEGEKVPKKQKL 254
|
|
| PBP1_AglR_RafR-like |
cd06292 |
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ... |
62-331 |
8.63e-63 |
|
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: 200.57 E-value: 8.63e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDI----SNTFYAELARGIEDIATMYKYNIILSNS--DQNKEKEFHLLntMLGKQVDGIVFMGEDITDIHIEEF 135
Cdd:cd06292 1 LIGYVVPELpggfSDPFFDEFLAALGHAAAARGYDVLLFTAsgDEDEIDYYRDL--VRSRRVDGFVLASTRHDDPRVRYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 136 KKSPVPIVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFiDKAGSAKKLQGYKKALEEAGISYDENL 215
Cdd:cd06292 79 HEAGVPFVAFGRANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPE-GSVPSDDRLAGYRAALEEAGLPFDPGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 216 VIDGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMY 295
Cdd:cd06292 158 VVEGENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTVRQPID 237
|
250 260 270
....*....|....*....|....*....|....*.
gi 2437085935 296 DIGAVAMRLLTKYMNKEKVEDHTVILPHRIQFRDST 331
Cdd:cd06292 238 EIGRAVVDLLLAAIEGNPSEPREILLQPELVVRESS 273
|
|
| PBP1_LacI-like |
cd06282 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-326 |
2.55e-62 |
|
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: 199.05 E-value: 2.55e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVF-MGEDITDIHIEEFKKSPV 140
Cdd:cd06282 1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILtVGDAQGSEALELLEEEGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 141 PIVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFIDKAGSAKKLQGYKKALEEAGisYDENLVIDGD 220
Cdd:cd06282 81 PYVLLFNQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAGDFSASDRARLRYQGYRDALKEAG--LKPIPIVEVD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 221 YTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAV 300
Cdd:cd06282 159 FPTNGLEEALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQPSRDMGRA 238
|
250 260
....*....|....*....|....*.
gi 2437085935 301 AMRLLTKYMNKEKvEDHTVILPHRIQ 326
Cdd:cd06282 239 AADLLLAEIEGES-PPTSIRLPHHLR 263
|
|
| PBP1_LacI |
cd01574 |
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ... |
62-330 |
6.79e-62 |
|
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: 198.19 E-value: 6.79e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFH-LLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPV 140
Cdd:cd01574 1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIATVDEDDPASVReALDRLLSQRVDGIIVIAPDEAVLEALRRLPPGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 141 PIVLAASFDEQNeTPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFiDKAGSAKKLQGYKKALEEAGISYDEnlVIDGD 220
Cdd:cd01574 81 PVVIVGSGPSPG-VPTVSIDQEEGARLATRHLLELGHRRIAHIAGPL-DWVDARARLRGWREALEEAGLPPPP--VVEGD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 221 YTYDSGIEAFEKLwSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAV 300
Cdd:cd01574 157 WSAASGYRAGRRL-LDDGPVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDFAELGRR 235
|
250 260 270
....*....|....*....|....*....|
gi 2437085935 301 AMRLLTKYMNKEKVEDHTVILPHRIQFRDS 330
Cdd:cd01574 236 AVELLLALIEGPAPPPESVLLPPELVVRES 265
|
|
| PBP1_CatR-like |
cd06296 |
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ... |
62-331 |
1.18e-59 |
|
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: 192.49 E-value: 1.18e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPVP 141
Cdd:cd06296 1 LIDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQLRLLRSAGIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 142 IVLAASFDEQN-ETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPfIDKAGSAKKLQGYKKALEEAGISYDENLVIDGD 220
Cdd:cd06296 81 FVLIDPVGEPDpDLPSVGATNWAGGRLATEHLLDLGHRRIAVITGP-PRSVSGRARLAGYRAALAEAGIAVDPDLVREGD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 221 YTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAV 300
Cdd:cd06296 160 FTYEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVHQPLREMGAV 239
|
250 260 270
....*....|....*....|....*....|.
gi 2437085935 301 AMRLLTKYMNKEKVEDHTVILPHRIQFRDST 331
Cdd:cd06296 240 AVRLLLRLLEGGPPDARRIELATELVVRGST 270
|
|
| lacI |
PRK09526 |
lac repressor; Reviewed |
1-331 |
3.15e-59 |
|
lac repressor; Reviewed
Pssm-ID: 181929 [Multi-domain] Cd Length: 342 Bit Score: 193.67 E-value: 3.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 1 MNVTIYDVAREANVSMATVSRVVNGNPNVKPTTRKKVLEAIDRLGYRPNAVARGLASKKTTTVGVIIPDISNTFYAELAR 80
Cdd:PRK09526 4 KPVTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTSLALHAPSQIAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 81 GIEDIATMYKYNIILSNSDQNKEKEF-HLLNTMLGKQVDGIV--FMGEDITDIHIEEfKKSPVPiVLAASFDEQNETPSV 157
Cdd:PRK09526 84 AIKSRADQLGYSVVISMVERSGVEACqAAVNELLAQRVSGVIinVPLEDADAEKIVA-DCADVP-CLFLDVSPQSPVNSV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 158 NIDYTQAAYDAMKHFIEQGHKRIGFVSGPfiDKAGSAK-KLQGYKKALEEAGISydENLVIDGDYTYDSGIEAFEKLWSN 236
Cdd:PRK09526 162 SFDPEDGTRLGVEHLVELGHQRIALLAGP--ESSVSARlRLAGWLEYLTDYQLQ--PIAVREGDWSAMSGYQQTLQMLRE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 237 DEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVAMRLLTKYMNKEKVED 316
Cdd:PRK09526 238 GPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLLALSQGQAVKG 317
|
330
....*....|....*
gi 2437085935 317 HTvILPHRIQFRDST 331
Cdd:PRK09526 318 SQ-LLPTSLVVRKST 331
|
|
| PBP1_MalI-like |
cd06289 |
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ... |
62-329 |
6.06e-59 |
|
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: 190.47 E-value: 6.06e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMG-EDITDIHIEEFKKSPV 140
Cdd:cd06289 1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPaAGTTAELLRRLKAWGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 141 PIVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGpFIDKAGSAKKLQGYKKALEEAGISYDENLVIDGD 220
Cdd:cd06289 81 PVVLALRDVPGSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLGG-LSDSSTRRERLAGFRAALAEAGLPLDESLIVPGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 221 YTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAV 300
Cdd:cd06289 160 ATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGFDDVPEAALWTPPLTTVSVHPREIGRR 239
|
250 260
....*....|....*....|....*....
gi 2437085935 301 AMRLLTKYMNKEKVEDHTVILPHRIQFRD 329
Cdd:cd06289 240 AARLLLRRIEGPDTPPERIIIEPRLVVRE 268
|
|
| PBP1_GalR |
cd01544 |
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ... |
70-330 |
3.12e-56 |
|
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: 183.49 E-value: 3.12e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 70 ISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEfhllntmLGKQVDGIVFMGEdITDIHIEEFKKSPVPIVLAASFD 149
Cdd:cd01544 14 LEDPYYLSIRLGIEKEAKKLGYEIKTIFRDDEDLES-------LLEKVDGIIAIGK-FSKEEIEKLKKLNPNIVFVDSNP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 150 EQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFIDKAGSAKK----LQGYKKALEEAGIsYDENLVIDGDYTYDS 225
Cdd:cd01544 86 DPDGFDSVVPDFEQAVRQALDYLIELGHRRIGFIGGKEYTSDDGEEIedprLRAFREYMKEKGL-YNEEYIYIGEFSVES 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 226 GIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVAMRLL 305
Cdd:cd01544 165 GYEAMKELLKEGDLPTAFFVASDPMAIGALRALQEAGIKVPEDISIISFNDIEVAKYVTPPLTTVHIPTEEMGRTAVRLL 244
|
250 260
....*....|....*....|....*
gi 2437085935 306 TKYMNKEKVEDHTVILPHRIQFRDS 330
Cdd:cd01544 245 LERINGGRTIPKKVLLPTKLIERES 269
|
|
| PBP1_AraR |
cd01541 |
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ... |
62-330 |
7.16e-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: 182.76 E-value: 7.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVF------MGEDITDIHiEEF 135
Cdd:cd01541 1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIeptksaLPNPNLDLY-EEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 136 KKSPVPIV-LAASFDEQNeTPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSgPFIDKAGsAKKLQGYKKALEEAGISYDEN 214
Cdd:cd01541 80 QKKGIPVVfINSYYPELD-APSVSLDDEKGGYLATKHLIDLGHRRIAGIF-KSDDLQG-VERYQGFIKALREAGLPIDDD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 215 LVI---DGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVV 291
Cdd:cd01541 157 RILwysTEDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEPPLTSVV 236
|
250 260 270
....*....|....*....|....*....|....*....
gi 2437085935 292 QPMYDIGAVAMRLLTKYMNKEKvEDHTVILPHRIQFRDS 330
Cdd:cd01541 237 HPKEELGRKAAELLLRMIEEGR-KPESVIFPPELIERES 274
|
|
| PRK10401 |
PRK10401 |
HTH-type transcriptional regulator GalS; |
3-304 |
8.50e-54 |
|
HTH-type transcriptional regulator GalS;
Pssm-ID: 236681 [Multi-domain] Cd Length: 346 Bit Score: 179.59 E-value: 8.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 3 VTIYDVAREANVSMATVSRVVNGNPNVKPTTRKKVLEAIDRLGYRPNAVARGLASKKTTTVGVIIPDISNTFYAELARGI 82
Cdd:PRK10401 2 ITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 83 EDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPVPIVLAASFDEQNETPSVNIDYT 162
Cdd:PRK10401 82 DLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQFMDQIPGMVLINRVVPGYAHRCVCLDNV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 163 QAAYDAMKHFIEQGHKRIGFV--SGPFIDkagSAKKLQGYKKALEEAGISYDENLVIDGDYTYDSGIEAFEKLWSNDEKP 240
Cdd:PRK10401 162 SGARMATRMLLNNGHQRIGYLssSHGIED---DAMRRAGWMSALKEQGIIPPESWIGTGTPDMQGGEAAMVELLGRNLQL 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2437085935 241 TAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVAMRL 304
Cdd:PRK10401 239 TAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATEL 302
|
|
| PBP1_LacI-like |
cd06278 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-330 |
3.03e-52 |
|
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: 173.10 E-value: 3.03e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEfHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPVP 141
Cdd:cd06278 1 LVGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDDVD-DALRQLLQYRVDGVIVTSATLSSELAEECARRGIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 142 IVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPfIDKAGSAKKLQGYKKALEEAGIsyDENLVIDGDY 221
Cdd:cd06278 80 VVLFNRVVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGP-EGTSTSRERERGFRAALAELGL--PPPAVEAGDY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 222 TYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAA-QDAGLNVPTDVEVLGFDNTRLAlmVRP--QLSTVVQPMYDIG 298
Cdd:cd06278 157 SYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAArQEGGLVVPEDISVVGFDDIPMA--AWPsyDLTTVRQPIEEMA 234
|
250 260 270
....*....|....*....|....*....|..
gi 2437085935 299 AVAMRLLTKYMNKEKVEDHTVILPHRIQFRDS 330
Cdd:cd06278 235 EAAVDLLLERIENPETPPERRVLPGELVERGS 266
|
|
| PBP1_LacI-like |
cd06279 |
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ... |
62-330 |
5.79e-52 |
|
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: 173.16 E-value: 5.79e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPD-----ISNTFYAELARGIEDIATMYKYNIILSnSDQNKEKEFHLLNTMLgkqVDGIVFMGEDITDIHIEEFK 136
Cdd:cd06279 1 AIGVLLPDdlsyaFSDPVAAQFLRGVAEVCEEEGLGLLLL-PATDEGSAAAAVRNAA---VDGFIVYGLSDDDPAVAALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 137 KSPVPIVlAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFIDKAG----------------SAKKLQGY 200
Cdd:cd06279 77 RRGLPLV-VVDGPAPPGIPSVGIDDRAAARAAARHLLDLGHRRIAILSLRLDRGRErgpvsaerlaaatnsvARERLAGY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 201 KKALEEAGISYDENLVID-GDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRL 279
Cdd:cd06279 156 RDALEEAGLDLDDVPVVEaPGNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRVPEDLSVTGFDDIPE 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2437085935 280 ALMVRPQLSTVVQPMYDIGAVAMRLLTKYMNKEKVEdhTVILPHRIQFRDS 330
Cdd:cd06279 236 AAAADPGLTTVRQPAVEKGRAAARLLLGLLPGAPPR--PVILPTELVVRAS 284
|
|
| PRK10727 |
PRK10727 |
HTH-type transcriptional regulator GalR; |
4-302 |
1.31e-50 |
|
HTH-type transcriptional regulator GalR;
Pssm-ID: 182681 [Multi-domain] Cd Length: 343 Bit Score: 171.48 E-value: 1.31e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 4 TIYDVAREANVSMATVSRVVNGNPNVKPTTRKKVLEAIDRLGYRPNAVARGLASKKTTTVGVIIPDISNTFYAELARGIE 83
Cdd:PRK10727 3 TIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKAVE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 84 DIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPVPIVLAASFDEQNETPSVNIDYTQ 163
Cdd:PRK10727 83 QVAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVVHAKMIPDAELASLMKQIPGMVLINRILPGFENRCIALDDRY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 164 AAYDAMKHFIEQGHKRIGFV-SGPFIDKAgsAKKLQGYKKALEEAGISYDENLVIDGDYTYDSGIEAFEKLWSNDEKPTA 242
Cdd:PRK10727 163 GAWLATRHLIQQGHTRIGYLcSNHSISDA--EDRLQGYYDALAESGIPANDRLVTFGEPDESGGEQAMTELLGRGRNFTA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 243 IFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMydigaVAM 302
Cdd:PRK10727 241 VACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPI-----VTM 295
|
|
| PBP1_LacI-like |
cd19974 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-330 |
5.21e-50 |
|
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: 167.73 E-value: 5.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDI---SNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEdITDIHIEEFKKS 138
Cdd:cd19974 1 NIAVLIPERffgDNSFYGKIYQGIEKELSELGYNLVLEIISDEDEEELNLPSIISEEKVDGIIILGE-ISKEYLEKLKEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 139 PVPIVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGP-----FIDKagsakkLQGYKKALEEAGISYDE 213
Cdd:cd19974 80 GIPVVLVDHYDEELNADSVLSDNYYGAYKLTSYLIEKGHKKIGFVGDInytssFMDR------YLGYRKALLEAGLPPEK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 214 NLVI----DGDYTYDSGIEAFEKLWsndeKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLST 289
Cdd:cd19974 154 EEWLledrDDGYGLTEEIELPLKLM----LPTAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLTT 229
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2437085935 290 VVQPMYDIGAVAMRLLTKYM-NKEKVEDHTVILPHRIqFRDS 330
Cdd:cd19974 230 VEVDKEAMGRRAVEQLLWRIeNPDRPFEKILVSGKLI-ERDS 270
|
|
| PRK10014 |
PRK10014 |
DNA-binding transcriptional repressor MalI; Provisional |
2-329 |
1.47e-48 |
|
DNA-binding transcriptional repressor MalI; Provisional
Pssm-ID: 182193 [Multi-domain] Cd Length: 342 Bit Score: 166.04 E-value: 1.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 2 NVTIYDVAREANVSMATVSRVVNGNPNVKPTTRKKVLEAIDRLGYRPNAVARGLASKKTTTVGVIIPDISNTFYAELARG 81
Cdd:PRK10014 6 KITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAELTAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 82 IEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMG-EDITDIHIEEFKKSPVPIVLAASFDEQNETPSVNID 160
Cdd:PRK10014 86 LTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAGaAGSSDDLREMAEEKGIPVVFASRASYLDDVDTVRPD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 161 YTQAAYDAMKHFIEQGHKRIGFVSGpfidKAGS---AKKLQGYKKALEEAGISYDENLVIDGDYTYDSGIEAFEKLWSND 237
Cdd:PRK10014 166 NMQAAQLLTEHLIRNGHQRIAWLGG----QSSSltrAERVGGYCATLLKFGLPFHSEWVLECTSSQKQAAEAITALLRHN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 238 EKPTAIFVSSDEMALGVIHAAQDAGLNVPTD---------VEVLGFDNTRLALMVRPQLSTVVQPMYDIG-AVAMRLLTK 307
Cdd:PRK10014 242 PTISAVVCYNETIAMGAWFGLLRAGRQSGESgvdryfeqqVALAAFTDVPEAELDDPPLTWASTPAREIGrTLADRMMQR 321
|
330 340
....*....|....*....|..
gi 2437085935 308 yMNKEKVEDHTVILPHRIQFRD 329
Cdd:PRK10014 322 -ITHEETHSRNLIIPPRLIARK 342
|
|
| PBP1_CelR |
cd06295 |
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ... |
58-330 |
2.43e-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: 160.88 E-value: 2.43e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 58 KKTTTVGVIIP-------DISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTmlgKQVDGIVFMGEDITDI 130
Cdd:cd06295 1 QRSRTIAVVVPmdphgdqSITDPFFLELLGGISEALTDRGYDMLLSTQDEDANQLARLLDS---GRADGLIVLGQGLDHD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 131 HIEEFKKSPVPIVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPfiDKAGSAKKLQGYKKALEEAGIS 210
Cdd:cd06295 78 ALRELAQQGLPMVVWGAPEDGQSYCSVGSDNVKGGALATEHLIEIGRRRIAFLGDP--PHPEVADRLQGYRDALAEAGLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 211 YDENLVIDGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTV 290
Cdd:cd06295 156 ADPSLLLSCDFTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFRPPLTTV 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2437085935 291 VQPMYDIGAVAMRLLTKYMNKEKVEdhTVILPHRIQFRDS 330
Cdd:cd06295 236 RQDLALAGRLLVEKLLALIAGEPVT--SSMLPVELVVRES 273
|
|
| PBP1_RegR_EndR_KdgR-like |
cd06283 |
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ... |
62-328 |
4.35e-47 |
|
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: 160.02 E-value: 4.35e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPVP 141
Cdd:cd06283 1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPTGNNNDAYLELAQKGLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 142 IVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFidKAGSAKK--LQGYKKALEEAGISYDEnLVIDG 219
Cdd:cd06283 81 VVLVDRQIEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPI--KGISTRRerLQGFLDALARYNIEGDV-YVIEI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 220 DYT--YDSGIEAFekLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDI 297
Cdd:cd06283 158 EDTedLQQALAAF--LSQHDGGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQPTYEI 235
|
250 260 270
....*....|....*....|....*....|.
gi 2437085935 298 GAVAMRLLTKYMNKEKVEDHTVILPHRIQFR 328
Cdd:cd06283 236 GKAAAEILLERIEGDSGEPKEIELPSELIIR 266
|
|
| PBP1_LacI-like |
cd06277 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
73-321 |
8.80e-46 |
|
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: 156.63 E-value: 8.80e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 73 TFYAELARGIEDIATMYKYNIILSNSDQNKEKEfHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPVPIVLAASFDEQN 152
Cdd:cd06277 19 PFFSELIDGIEREARKYGYNLLISSVDIGDDFD-EILKELTDDQSSGIILLGTELEEKQIKLFQDVSIPVVVVDNYFEDL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 153 ETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFiDKAGSAKKLQGYKKALEEAGISYDENLVidgdYTYDSGIEAFEK 232
Cdd:cd06277 98 NFDCVVIDNEDGAYEAVKYLVELGHTRIGYLASSY-RIKNFEERRRGFRKAMRELGLSEDPEPE----FVVSVGPEGAYK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 233 -----LWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVAMRLLTK 307
Cdd:cd06277 173 dmkalLDTGPKLPTAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRRLIE 252
|
250
....*....|....
gi 2437085935 308 YMNKEKVEdHTVIL 321
Cdd:cd06277 253 KIKDPDGG-TLKIL 265
|
|
| PBP1_LacI-like |
cd06281 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
62-330 |
2.77e-45 |
|
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: 155.47 E-value: 2.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEE-FKKSPV 140
Cdd:cd06281 1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILTPGDEDDPELAAaLARLDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 141 PIVLaasFDE--QNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFIDKAGSAKkLQGYKKALEEAGISYDENLVID 218
Cdd:cd06281 81 PVVL---IDRdlPGDIDSVLVDHRSGVRQATEYLLSLGHRRIALLTGGPDIRPGRER-IAGFKAAFAAAGLPPDPDLVRL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 219 GDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIG 298
Cdd:cd06281 157 GSFSADSGFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDLDAVG 236
|
250 260 270
....*....|....*....|....*....|...
gi 2437085935 299 AVAMRLLTKYMNKEKVED-HTVILPHRIQFRDS 330
Cdd:cd06281 237 RAAAELLLDRIEGPPAGPpRRIVVPTELILRDS 269
|
|
| PBP1_AglR-like |
cd20010 |
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ... |
62-322 |
4.92e-45 |
|
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: 154.63 E-value: 4.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIP----DISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKK 137
Cdd:cd20010 1 AIGLVLPldpgDLGDPFFLEFLAGLSEALAERGLDLLLAPAPSGEDELATYRRLVERGRVDGFILARTRVNDPRIAYLLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 138 SPVPIVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPfIDKAGSAKKLQGYKKALEEAGISYDENLVI 217
Cdd:cd20010 81 RGIPFVVHGRSESGAPYAWVDIDNEGAFRRATRRLLALGHRRIALLNGP-EELNFAHQRRDGYRAALAEAGLPVDPALVR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 218 DGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNT-RLALMVRPQLSTVVQPMYD 296
Cdd:cd20010 160 EGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLlPALEYFSPPLTTTRSSLRD 239
|
250 260
....*....|....*....|....*.
gi 2437085935 297 IGAVAMRLLTKYMNKEKVEDHTVILP 322
Cdd:cd20010 240 AGRRLAEMLLALIDGEPAAELQELWP 265
|
|
| Peripla_BP_3 |
pfam13377 |
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ... |
171-331 |
1.74e-40 |
|
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional regulatory proteins. It is related to bacterial periplasmic binding proteins, although this domain is unlikely to be found in the periplasm. This domain acts as a sensor binding small molecule ligands that the DNA-binding domain responds to. This domain recognizes Sugars, sugar phosphates, sugar acids and purines (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).
Pssm-ID: 433159 [Multi-domain] Cd Length: 160 Bit Score: 139.40 E-value: 1.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 171 HFIEQGHKRIGFV-SGPFIDKAGSAKKLQGYKKALEEAGISYDENLVIDGDYTYDSGIEAfEKLWSNDeKPTAIFVSSDE 249
Cdd:pfam13377 1 HLAELGHRRIALIgPEGDRDDPYSDLRERGFREAARELGLDVEPTLYAGDDEAEAAAARE-RLRWLGA-LPTAVFVANDE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 250 MALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVAMRLLTKYMNKEKVEDHTVILPHRIQFRD 329
Cdd:pfam13377 79 VALGVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVERE 158
|
..
gi 2437085935 330 ST 331
Cdd:pfam13377 159 ST 160
|
|
| HTH_LACI |
smart00354 |
helix_turn _helix lactose operon repressor; |
3-72 |
4.45e-37 |
|
helix_turn _helix lactose operon repressor;
Pssm-ID: 197675 [Multi-domain] Cd Length: 70 Bit Score: 127.32 E-value: 4.45e-37
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 3 VTIYDVAREANVSMATVSRVVNGNPNVKPTTRKKVLEAIDRLGYRPNAVARGLASKKTTTVGVIIPDISN 72
Cdd:smart00354 1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
|
|
| PRK10339 |
PRK10339 |
DNA-binding transcriptional repressor EbgR; Provisional |
4-332 |
7.41e-36 |
|
DNA-binding transcriptional repressor EbgR; Provisional
Pssm-ID: 182389 [Multi-domain] Cd Length: 327 Bit Score: 132.19 E-value: 7.41e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 4 TIYDVAREANVSMATVSRVVNGNP--NVKPTTRKKVLEAIDRLGYRPNAVARGL-ASKKTTTVGVIIP-----DISNTFY 75
Cdd:PRK10339 3 TLKDIAIEAGVSLATVSRVLNDDPtlNVKEETKHRILEIAEKLEYKTSSARKLQtGAVNQHHILAIYSyqqelEINDPYY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 76 AELARGIEdiATMYKYNIILSNS-DQNKEKEFhllntmlgKQVDGIVFMGEDITDIHiEEFKKSPVPIVLAASFDEQNET 154
Cdd:PRK10339 83 LAIRHGIE--TQCEKLGIELTNCyEHSGLPDI--------KNVTGILIVGKPTPALR-AAASALTDNICFIDFHEPGSGY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 155 PSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPfIDKAGSAKKLQGYKKALEEAGISYDENLVIdGDYTYDSGIEAFEKLW 234
Cdd:PRK10339 152 DAVDIDLARISKEIIDFYINQGVNRIGFIGGE-DEPGKADIREVAFAEYGRLKQVVREEDIWR-GGFSSSSGYELAKQML 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 235 SNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVAMRLLTKYMNKEKV 314
Cdd:PRK10339 230 AREDYPKALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNLLYEKARDGRA 309
|
330
....*....|....*...
gi 2437085935 315 EDHTVILPHRIQFRDSTK 332
Cdd:PRK10339 310 LPLLVFVPSKLKLRGTTR 327
|
|
| PBP1_repressor_sugar_binding-like |
cd01537 |
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ... |
63-324 |
1.08e-35 |
|
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: 130.06 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 63 VGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFM-GEDITDIHIEEFKKSPVP 141
Cdd:cd01537 2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINlVDPAAAGVAEKARGQNVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 142 IVLAaSFDEQNETP--SVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPfIDKAGSAKKLQGYKKALEEAGISYDENLVIDG 219
Cdd:cd01537 82 VVFF-DKEPSRYDKayYVITDSKEGGIIQGDLLAKHGHIQIVLLKGP-LGHPDAEARLAGVIKELNDKGIKTEQLQLDTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 220 DYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGA 299
Cdd:cd01537 160 DWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDANNLGK 239
|
250 260
....*....|....*....|....*
gi 2437085935 300 VAMRLLTKYMNKEKVEDHTVILPHR 324
Cdd:cd01537 240 TTFDLLLNLADNWKIDNKVVRVPYV 264
|
|
| PBP1_XylR |
cd01543 |
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ... |
116-331 |
3.22e-35 |
|
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: 128.86 E-value: 3.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 116 QVDGIVfmGEDITDIHIEEFKKSPVPIVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSgpFIDKAGSAK 195
Cdd:cd01543 50 KGDGII--ARLDDPELAEALRRLGIPVVNVSGSRPEPGFPRVTTDNEAIGRMAAEHLLERGFRHFAFCG--FRNAAWSRE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 196 KLQGYKKALEEAGISYDenlvidgdyTYDSGIEAFEKLWSNDE-----------KPTAIFVSSDEMALGVIHAAQDAGLN 264
Cdd:cd01543 126 RGEGFREALREAGYECH---------VYESPPSGSSRSWEEEReeladwlkslpKPVGIFACNDDRARQVLEACREAGIR 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2437085935 265 VPTDVEVLGFDNTRL-ALMVRPQLSTVVQPMYDIGAVAMRLLTKYMNKEKVEDHTVIL-PHRIQFRDST 331
Cdd:cd01543 197 VPEEVAVLGVDNDELiCELSSPPLSSIALDAEQIGYEAAELLDRLMRGERVPPEPILIpPLGVVTRQST 265
|
|
| PRK14987 |
PRK14987 |
HTH-type transcriptional regulator GntR; |
7-307 |
1.27e-34 |
|
HTH-type transcriptional regulator GntR;
Pssm-ID: 184949 [Multi-domain] Cd Length: 331 Bit Score: 128.99 E-value: 1.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 7 DVAREANVSMATVSRVVNGNPNVKPTTRKKVLEAIDRLGYRPNAVARGLASKKTTTVGVIIPDISNTFYAELARGIEDIA 86
Cdd:PRK14987 10 DVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGIESVT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 87 TMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPVPIVLAASFDEQNETPSVNIDYTQAAY 166
Cdd:PRK14987 90 DAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIEVAGIPVVELMDSQSPCLDIAVGFDNFEAAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 167 DAMKHFIEQGHKRIGFVsGPFIDKAGSAKKlQGYKKALEEAGISyDENLVIDGDYTYDSGIEAFEKLWSNDEKPTAIFVS 246
Cdd:PRK14987 170 QMTTAIIARGHRHIAYL-GARLDERTIIKQ-KGYEQAMLDAGLV-PYSVMVEQSSSYSSGIELIRQARREYPQLDGVFCT 246
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2437085935 247 SDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAV-AMRLLTK 307
Cdd:PRK14987 247 NDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIgAERLLAR 308
|
|
| PBP1_hexuronate_repressor-like |
cd06272 |
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ... |
62-329 |
6.47e-34 |
|
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: 125.56 E-value: 6.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFY-AELARGIEDIATMYKYNIILS-----NSDQNKEKEFHLLNtmlgkQVDGIVFMGEDITDIHIEEF 135
Cdd:cd06272 1 TIGLYWPSVGERVAlTRLLSGINEAISKQGYNINLSicpykVGHLCTAKGLFSEN-----RFDGVIVFGISDSDIEYLNK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 136 KKSPVPIVLAASfdEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFIDKAGSAKKlQGYKKALEEAGISYDENL 215
Cdd:cd06272 76 NKPKIPIVLYNR--ESPKYSTVNVDNEKAGRLAVLLLIQKGHKSIAYIGNPNSNRNQTLRG-KGFIETCEKHGIHLSDSI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 216 VIDGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMY 295
Cdd:cd06272 153 IDSRGLSIEGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLTVVGVPIE 232
|
250 260 270
....*....|....*....|....*....|....
gi 2437085935 296 DIGAVAMRLLTKYMNKEKVEDHTVILPHRIQFRD 329
Cdd:cd06272 233 KIAEESLRLILKLIEGRENEIQQLILYPELIFRE 266
|
|
| PBP1_CcpA_TTHA0807 |
cd06297 |
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ... |
62-310 |
6.77e-34 |
|
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: 125.27 E-value: 6.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPVP 141
Cdd:cd06297 1 TISLLVPEVMTPFYMRLLTGVERALDENRYDLAIFPLLSEYRLEKYLRNSTLAYQCDGLVMASLDLTELFEEVIVPTEKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 142 IVLaasFDEQNET-PSVNIDYTQAAYDAMKHFIEQGHKRIGFvsgPFIDKAGS------AKKLQGYKKALEEAGISYDEN 214
Cdd:cd06297 81 VVL---IDANSMGyDCVYVDNVKGGFMATEYLAGLGEREYVF---FGIEEDTVftetvfREREQGFLEALNKAGRPISSS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 215 LVIDGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLAlmVRPQLSTVVQPM 294
Cdd:cd06297 155 RMFRIDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWA--ASPGLTTVRQPV 232
|
250
....*....|....*.
gi 2437085935 295 YDIGAVAMRLLTKYMN 310
Cdd:cd06297 233 EEMGEAAAKLLLKRLN 248
|
|
| fruct_sucro_rep |
TIGR02417 |
D-fructose-responsive transcription factor; Members of this family belong the lacI ... |
4-329 |
3.46e-33 |
|
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: 124.86 E-value: 3.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 4 TIYDVAREANVSMATVSRVVNGNPN---VKPTTRKKVLEAIDRLGYRPNAVARGLASKKTTTVGVIIPDISNTFYAELAR 80
Cdd:TIGR02417 1 TLSDIAKLAGVSKTTASYVINGKAKeyrISQETVERVMAVVREQGYQPNIHAASLRAGRSRTIGLVIPDLENYSYARIAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 81 GIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDG-IVFMGEDITDIHIEEFKKSPVPIVLAASFDEQNETPSVNI 159
Cdd:TIGR02417 81 ELEQQCREAGYQLLIACSDDNPDQEKVVIENLLARQVDAlIVASCMPPEDAYYQKLQNEGLPVVALDRSLDDEHFCSVIS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 160 DYTQAAYDAMKHFIEQGHKRIGFVsGPFIDKAGSAKKLQGYKKALEEAgiSYDENLVIDGDYTYDSGIEAFEKLWSNDEK 239
Cdd:TIGR02417 161 DDVDAAAELIERLLSQHADEFWYL-GAQPELSVSRDRLAGFRQALKQA--TLEVEWVYGGNYSRESGYQMFAKLCARLGR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 240 -PTAIFVSSDEMALGVIHAAQDAGLnVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVAMRLLTKYMNKEKVEDHT 318
Cdd:TIGR02417 238 lPQALFTTSYTLLEGVLDYMLERPL-LDSQLHLATFGDNYLLDFLPLPINSVAQQHRQLAWHALELALAAIDGKKPEPGQ 316
|
330
....*....|.
gi 2437085935 319 VILPHRIQFRD 329
Cdd:TIGR02417 317 RYIPRTLQIRH 327
|
|
| RbsB |
COG1879 |
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ... |
44-320 |
9.34e-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: 115.41 E-value: 9.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 44 LGYRPNAVARGLASKKTTTVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFM 123
Cdd:COG1879 17 AACGSAAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 124 GED---ITDIhIEEFKKSPVPIV-LAASFDEQNETPSVNIDYTQAAYDAMKHFIEQ--GHKRIGFVSGPFIDkAGSAKKL 197
Cdd:COG1879 97 PVDpdaLAPA-LKKAKAAGIPVVtVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKAlgGKGKVAILTGSPGA-PAANERT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 198 QGYKKALEEAGisyDENLV--IDGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLnvPTDVEVLGFD 275
Cdd:COG1879 175 DGFKEALKEYP---GIKVVaeQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGR--KGDVKVVGFD 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2437085935 276 NTRLAL-MVR--PQLSTVVQPMYDIGAVAMRLLTKYMNKEKVEDHTVI 320
Cdd:COG1879 250 GSPEALqAIKdgTIDATVAQDPYLQGYLAVDAALKLLKGKEVPKEILT 297
|
|
| PBP1_AglR_RafR-like |
cd06271 |
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ... |
72-321 |
3.06e-29 |
|
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: 112.90 E-value: 3.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 72 NTFYAELARGIEDIATMYKYNIILSnSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIEEFKKSPVPIVLAASFDEQ 151
Cdd:cd06271 14 NGTVSE*VSGITEEAGTTGYHLLVW-PFEEAES*VPIRDLVETGSADGVILSEIEPNDPRVQFLTKQNFPFVAHGRSD*P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 152 NETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGP----FIDKAgsakkLQGYKKALEEAGIsydENLVIDGDYTYDSGI 227
Cdd:cd06271 93 IGHAWVDIDNEAGAYEAVERLAGLGHRRIAFIVPParysPHDRR-----LQGYVRA*RDAGL---TGYPLDADTTLEAGR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 228 EAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTR-LALMVRPQLSTVVQPMYDIGAVAMRLLT 306
Cdd:cd06271 165 AAAQRLLALSPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSAPfLGAMITPPLTTVHAPIAEAGRELAKALL 244
|
250
....*....|....*
gi 2437085935 307 KYMNKEKVEDHTVIL 321
Cdd:cd06271 245 ARIDGEDPETLQVLV 259
|
|
| PRK11303 |
PRK11303 |
catabolite repressor/activator; |
7-313 |
1.36e-26 |
|
catabolite repressor/activator;
Pssm-ID: 236897 [Multi-domain] Cd Length: 328 Bit Score: 107.27 E-value: 1.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 7 DVAREANVSMATVSRVVNGNPN---VKPTTRKKVLEAIDRLGYRPNAVARGLASKKTTTVGVIIPDISNTFYAELARGIE 83
Cdd:PRK11303 5 EIARLAGVSRTTASYVINGKAKqyrVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSYARIAKYLE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 84 DIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVF---MGEDiTDIHiEEFKKSPVPIVlaaSFDEQNETP---SV 157
Cdd:PRK11303 85 RQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVstsLPPE-HPFY-QRLQNDGLPII---ALDRALDREhftSV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 158 NIDYTQAAYDAMKHFIEQGHKRIGFVsGPFIDKAGSAKKLQGYKKALEEAGISYDenlVIDGD-YTYDSGIEAFEKLWSN 236
Cdd:PRK11303 160 VSDDQDDAEMLAESLLKFPAESILLL-GALPELSVSFEREQGFRQALKDDPREVH---YLYANsFEREAGAQLFEKWLET 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2437085935 237 DEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVAMRLLTKYMNKEK 313
Cdd:PRK11303 236 HPMPDALFTTSYTLLQGVLDVLLERPGELPSDLAIATFGDNELLDFLPCPVNAVAQQHRLIAERALELALAALDEPR 312
|
|
| PBP1_galactofuranose_YtfQ-like |
cd06309 |
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ... |
62-325 |
2.59e-26 |
|
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: 105.38 E-value: 2.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDIT--DIHIEEFKKSP 139
Cdd:cd06309 1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATgwDPVLKEAKDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 140 VPIVLAA----SFDEQNETPSVNIDYT---QAAYDAMKHFIEQGHKRIGFVSGPfidkAGSAKKlQGYKKALEEAgISYD 212
Cdd:cd06309 81 IPVILVDrtidGEDGSLYVTFIGSDFVeegRRAAEWLVKNYKGGKGNVVELQGT----AGSSVA-IDRSKGFREV-IKKH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 213 ENLVI----DGDYTYDSGIEAFEK-LWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTR--LALMVRP 285
Cdd:cd06309 155 PNIKIvasqSGNFTREKGQKVMENlLQAGPGDIDVIYAHNDDMALGAIQALKEAGLKPGKDVLVVGIDGQKdaLEAIKAG 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2437085935 286 QLSTVVQPMYDIGAVAMRLLTKYMNKEKVEdHTVILPHRI 325
Cdd:cd06309 235 ELNATVECNPLFGPTAFDTIAKLLAGEKVP-KLIIVEERL 273
|
|
| PBP1_FruR |
cd06274 |
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ... |
62-326 |
2.66e-25 |
|
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: 102.28 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMG-EDITDIHiEEFKKSPV 140
Cdd:cd06274 1 TIGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAPsTPPDDIY-YLCQAAGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 141 PIVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFIDKAgSAKKLQGYKKALEEAGISYDENLVIDGD 220
Cdd:cd06274 80 PVVFLDRPFSGSDAPSVVSDNRAGARALTEKLLAAGPGEIYFLGGRPELPS-TAERIRGFRAALAEAGITEGDDWILAEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 221 YTYDSGIEAFEKLW-SNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGA 299
Cdd:cd06274 159 YDRESGYQLMAELLaRLGGLPQALFTSSLTLLEGVLRFLRERLGAIPSDLVLGTFDDHPLLDFLPNPVDSVRQDHDEIAE 238
|
250 260
....*....|....*....|....*..
gi 2437085935 300 VAMRLLTKYMNKEKvEDHTVILPHRIQ 326
Cdd:cd06274 239 HAFELLDALIEGQP-EPGVIIIPPELI 264
|
|
| PBP1_ABC_sugar_binding-like |
cd01536 |
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ... |
62-320 |
8.57e-25 |
|
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: 101.10 E-value: 8.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGED---ITDIhIEEFKKS 138
Cdd:cd01536 1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDseaLVPA-VKKANAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 139 PVPIVLAASF--DEQNETPSVNIDYTQAAYDAMKHFIEQ--GHKRIGFVSGPFIDKAGSAKKlQGYKKALEEAGisyDEN 214
Cdd:cd01536 80 GIPVVAVDTDidGGGDVVAFVGTDNYEAGKLAGEYLAEAlgGKGKVAILEGPPGSSTAIDRT-KGFKEALKKYP---DIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 215 LV--IDGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLnvPTDVEVLGFDNTRLAL-MVR--PQLST 289
Cdd:cd01536 156 IVaeQPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGR--TGDIKIVGVDGTPEALkAIKdgELDAT 233
|
250 260 270
....*....|....*....|....*....|.
gi 2437085935 290 VVQPMYDIGAVAMRLLTKYMNKEKVEDHTVI 320
Cdd:cd01536 234 VAQDPYLQGYLAVEAAVKLLNGEKVPKEILT 264
|
|
| PBP1_RafR-like |
cd20009 |
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ... |
155-323 |
1.20e-23 |
|
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: 97.99 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 155 PSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGP----FidkagSAKKLQGYKKALEEAGISYDENLVIDGDYTYDSGIEAF 230
Cdd:cd20009 96 AYFDFDNEAFAYEAVRRLAARGRRRIALVAPPreltY-----AQHRLRGFRRALAEAGLEVEPLLIVTLDSSAEAIRAAA 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 231 EKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVAMRLLTKYMN 310
Cdd:cd20009 171 RRLLRQPPRPDGIICASEIAALGALAGLEDAGLVVGRDVDVVAKETSPILDYFRPPIDTLYEDIEEAGRFLAEALLRRIE 250
|
170
....*....|....
gi 2437085935 311 KEKVED-HTVILPH 323
Cdd:cd20009 251 GEPAEPlQTLERPE 264
|
|
| HTH_LacI |
cd01392 |
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ... |
6-57 |
3.41e-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: 90.55 E-value: 3.41e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2437085935 6 YDVAREANVSMATVSRVVNGNPNVKPTTRKKVLEAIDRLGYRPNAVARGLAS 57
Cdd:cd01392 1 KDIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
|
|
| PBP1_ABC_sugar_binding-like |
cd06319 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
62-322 |
7.54e-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: 87.80 E-value: 7.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVF------MGEDITDIhieeF 135
Cdd:cd06319 1 KIGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIIsptnssAAPTVLDL----A 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 136 KKSPVPIVLAASFDEQNETPSVNI-DYTQAAYDAMKHFIEQ------GHKRIGFVSGPFIDKAGSAKKlQGYKKALEEAG 208
Cdd:cd06319 77 NEAKIPVVIADIGTGGGDYVSYIIsDNYDGGYQAGEYLAEAlkengwGGGSVGIIAIPQSRVNGQART-AGFEDALEEAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 209 ISyDENLVIDGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNvpTDVEVLGFDNTRLAL-MVRPQ- 286
Cdd:cd06319 156 VE-EVALRQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRT--GDILVVGFDGDPEALdLIKDGk 232
|
250 260 270
....*....|....*....|....*....|....*..
gi 2437085935 287 -LSTVVQPMYDIGAVAMRLLTKYMNKEKVEDHTVILP 322
Cdd:cd06319 233 lDGTVAQQPFGMGARAVELAIQALNGDNTVEKEIYLP 269
|
|
| Peripla_BP_1 |
pfam00532 |
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ... |
60-324 |
1.51e-19 |
|
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: 86.80 E-value: 1.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 60 TTTVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVF--MGEDITDI-HIEEFK 136
Cdd:pfam00532 1 TLKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIIttPAPSGDDItAKAEGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 137 KSPVpIVLAASFDEQNETPSVNIDYTQAAYDAMKHFIEQGHKR-IGFVSGPfiDKAGSAKK-LQGYKKALEEAGISYDEN 214
Cdd:pfam00532 81 GIPV-IAADDAFDNPDGVPCVMPDDTQAGYESTQYLIAEGHKRpIAVMAGP--ASALTARErVQGFMAALAAAGREVKIY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 215 LVIDGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAG-LNVPTDVE-----VLGFDNTRLA--LMVRPQ 286
Cdd:pfam00532 158 HVATGDNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGrVKIPDIVGiginsVVGFDGLSKAqdTGLYLS 237
|
250 260 270
....*....|....*....|....*....|....*....
gi 2437085935 287 LSTVVQ-PMYDIGAVAMRLLTKYMNKEKVEDHTVILPHR 324
Cdd:pfam00532 238 PLTVIQlPRQLLGIKASDMVYQWIPKFREHPRVLLIPRD 276
|
|
| Peripla_BP_4 |
pfam13407 |
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ... |
63-313 |
6.99e-19 |
|
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: 84.67 E-value: 6.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 63 VGVIIPDISNTFYAELARGIEDIATMYKYN-IILSNSDQNKEKEFHLLNTMLGKQVDGIVFM---GEDITDIhIEEFKKS 138
Cdd:pfam13407 1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEvIVVGPAEADAAEQVAQIEDAIAQGVDAIIVApvdPTALAPV-LKKAKDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 139 PVPIVLAASFDEQNE-TPSVNIDYTQAAYDAMKHFIEQ--GHKRIGFVSGpFIDKAGSAKKLQGYKKALEEAGISYdeNL 215
Cdd:pfam13407 80 GIPVVTFDSDAPSSPrLAYVGFDNEAAGEAAGELLAEAlgGKGKVAILSG-SPGDPNANERIDGFKKVLKEKYPGI--KV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 216 VIDGDYTYDSGIEAFEK----LWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNvpTDVEVLGFDNTR--LALMVRPQLS- 288
Cdd:pfam13407 157 VAEVEGTNWDPEKAQQQmealLTAYPNPLDGIISPNDGMAGGAAQALEAAGLA--GKVVVTGFDATPeaLEAIKDGTIDa 234
|
250 260
....*....|....*....|....*
gi 2437085935 289 TVVQPMYDIGAVAMRLLTKYMNKEK 313
Cdd:pfam13407 235 TVLQDPYGQGYAAVELAAALLKGKK 259
|
|
| LacI |
pfam00356 |
Bacterial regulatory proteins, lacI family; |
4-49 |
8.81e-17 |
|
Bacterial regulatory proteins, lacI family;
Pssm-ID: 306791 [Multi-domain] Cd Length: 46 Bit Score: 73.06 E-value: 8.81e-17
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 2437085935 4 TIYDVAREANVSMATVSRVVNGNPNVKPTTRKKVLEAIDRLGYRPN 49
Cdd:pfam00356 1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
|
|
| PBP1_ABC_sugar_binding-like |
cd06321 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
62-322 |
1.10e-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: 380544 [Multi-domain] Cd Length: 270 Bit Score: 72.71 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYN--IILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIH--IEEFKK 137
Cdd:cd06321 1 VIGVTVQDLGNPFFVAMVRGAEEAAAEINPGakVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEpaIKRAKD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 138 SPVPIVLAASFDEQNETpSVNIDYTQAAYDAMKHFIEQ--GHKRIGFVSGPFIdkAGSAKKLQGYKKALEEA-GI--SYD 212
Cdd:cd06321 81 AGIIVVAVDVAAEGADA-TVTTDNVQAGYLACEYLVEQlgGKGKVAIIDGPPV--SAVIDRVNGCKEALAEYpGIklVDD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 213 ENlvidGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLnvpTDVEVLGFDNT-----RLALMVRPQL 287
Cdd:cd06321 158 QN----GKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGR---DDIVITSVDGSpeavaALKREGSPFI 230
|
250 260 270
....*....|....*....|....*....|....*
gi 2437085935 288 STVVQPMYDIGAVAMRLLTKYMNKEKVEDHTVILP 322
Cdd:cd06321 231 ATAAQDPYDMARKAVELALKILNGQEPAPELVLIP 265
|
|
| PBP1_ABC_sugar_binding-like |
cd19972 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
62-314 |
5.10e-14 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380627 [Multi-domain] Cd Length: 269 Bit Score: 70.93 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDIT--DIHIEEFKKSP 139
Cdd:cd19972 1 TIGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATaaAVPVKAARAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 140 VPIVLAASFDEQNETPS-VNIDYTQAAYDAMKHFIEQ--GHKRIGFVSG-----PFIDKAgsakklQGYKKALEEAGisy 211
Cdd:cd19972 81 IPVIAVDRNPEDAPGDTfIATDSVAAAKELGEWVIKQtgGKGEIAILHGqlgttPEVDRT------KGFQEALAEAP--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 212 dENLVID---GDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNvpTDVEVLGFDNTRLAL-MVRPQL 287
Cdd:cd19972 152 -GIKVVAeqtADWDQDEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGLD--HKIWVVGFDGDVAGLkAVKDGV 228
|
250 260
....*....|....*....|....*....
gi 2437085935 288 --STVVQPMYDIGAVAMRLLTKYMNKEKV 314
Cdd:cd19972 229 ldATMTQQTQKMGRLAVDSAIDLLNGKAV 257
|
|
| PBP1_allose_binding |
cd06320 |
periplasmic allose-binding domain of bacterial transport systems that function as a primary ... |
63-325 |
9.24e-13 |
|
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: 67.67 E-value: 9.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 63 VGVIIPDISNTFYAELARGIEDIATMY--KYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIH--IEEFKKS 138
Cdd:cd06320 2 IGVVLKTLSNPFWVAMKDGIEAEAKKLgvKVDVQAAPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIppIEKANKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 139 PVPIV------LAASFDEQNETPSVNI--DYTQAAYDAMKHFIEQ--GHKRIGFVSGpfidKAGSA---KKLQGYKKALE 205
Cdd:cd06320 82 GIPVInlddavDADALKKAGGKVTSFIgtDNVAAGALAAEYIAEKlpGGGKVAIIEG----LPGNAaaeARTKGFKETFK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 206 EAGiSYDENLVIDGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNvpTDVEVLGFDNTRLAL-MVR 284
Cdd:cd06320 158 KAP-GLKLVASQPADWDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAGKT--GKVLVVGTDGIPEAKkSIK 234
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2437085935 285 P-QLS-TVVQPMYDIGAVAMRLLTKYMNKEKVEDHtVILPHRI 325
Cdd:cd06320 235 AgELTaTVAQYPYLEGAMAVEAALRLLQGQKVPAV-VATPQAL 276
|
|
| PBP1_TmRBP-like |
cd19967 |
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ... |
62-313 |
1.60e-12 |
|
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: 66.58 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATM--YKYNIILSNSDQNKEKEfhLLNTMLGKQVDGIVF--MGEDITDIHIEEFKK 137
Cdd:cd19967 1 LVAVIVSTPNNPFFVVEAEGAKEKAKElgYEVTVFDHQNDTAKEAE--LFDTAIASGAKAIILdpADADASIAAVKKAKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 138 SPVPIVLAASFDEQNETPSVNI--DYTQAAYDAMKHFIEQGHKRIGFVS--GPFIDKaGSAKKLQGYKKALEEagisYDE 213
Cdd:cd19967 79 AGIPVFLIDREINAEGVAVAQIvsDNYQGAVLLAQYFVKLMGEKGLYVEllGKESDT-NAQLRSQGFHSVIDQ----YPE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 214 NLVI---DGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLnvPTDVEVLGFDNT---RLALMVRPQL 287
Cdd:cd19967 154 LKMVaqqSADWDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGR--AGDVIIVGFDGSndvRDAIKEGKIS 231
|
250 260
....*....|....*....|....*.
gi 2437085935 288 STVVQPMYDIGAVAMRLLTKYMNKEK 313
Cdd:cd19967 232 ATVLQPAKLIARLAVEQADQYLKGGS 257
|
|
| PBP1_ribose_binding |
cd06323 |
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ... |
62-316 |
5.02e-12 |
|
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: 65.01 E-value: 5.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIH--IEEFKKSP 139
Cdd:cd06323 1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSpaVEEANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 140 VPIV---------LAASFdeqneTPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPfidkaGSA---KKLQGYKKALEEA 207
Cdd:cd06323 81 IPVItvdrsvtggKVVSH-----IASDNVAGGEMAAEYIAKKLGGKGKVVELQGIP-----GTSaarERGKGFHNAIAKY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 208 GisydeNLVI----DGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGlnvPTDVEVLGFDNTRLALMV 283
Cdd:cd06323 151 P-----KINVvasqTADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAG---RKDVIVVGFDGTPDAVKA 222
|
250 260 270
....*....|....*....|....*....|....*.
gi 2437085935 284 ---RPQLSTVVQPMYDIGAVAMRLLTKYMNKEKVED 316
Cdd:cd06323 223 vkdGKLAATVAQQPEEMGAKAVETADKYLKGEKVPK 258
|
|
| PBP1_LacI-like |
cd06287 |
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ... |
74-330 |
8.43e-12 |
|
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors; This group includes the ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.
Pssm-ID: 380510 [Multi-domain] Cd Length: 268 Bit Score: 64.36 E-value: 8.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 74 FYAELARGIEDIATMYKYNIILSNSDQNKEkefhLLNTMlgkQVDGIVFMGEDITDIHIEEFKKSPVPIV-LAASFDEQN 152
Cdd:cd06287 21 FMMEVAAAAAEEALEHDLALVLVPPLHHVS----MLDAL---DVDGAIVVEPTVEDPILARLRQRGVPVVsIGRAPGTDE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 153 ETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPfIDKAGSAKKLQGYKKALEEAG-----ISYDENLvidGDytyDSGI 227
Cdd:cd06287 94 PVPYVDLQSAATARLLLEHLHGAGARQVALLTGS-SRRNSSLESEAAYLRFAQEYGttpvvYKVPESE---GE---RAGY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 228 EAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVPTDVEVLGFDNTRLALMVRPQLSTVVQPMYDIGAVAMRLLTK 307
Cdd:cd06287 167 EAAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPEDLMVVTRYDGIRARTADPPLTAVDLHLDRVARTAIDLLFA 246
|
250 260
....*....|....*....|...
gi 2437085935 308 YMNKEKVEDHTVILPhRIQFRDS 330
Cdd:cd06287 247 SLSGEERSVEVGPAP-ELVVRAS 268
|
|
| PBP1_ABC_sugar_binding-like |
cd06322 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
62-322 |
2.68e-11 |
|
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: 63.06 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIH--IEEFKKSP 139
Cdd:cd06322 1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVpaIEAANEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 140 VPIVLA-ASFDEQNETPSVNIDYTQA---AYDAMKHFIEQGHKRIGFVSGPfiDKAGSAKKLQGYKKALEE-AGISYDEN 214
Cdd:cd06322 81 IPVFTVdVKADGAKVVTHVGTDNYAGgklAGEYALKALLGGGGKIAIIDYP--EVESVVLRVNGFKEAIKKyPNIEIVAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 215 LviDGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGlnVPTDVEVLGFDNTRLALMVRPQLST----V 290
Cdd:cd06322 159 Q--PGDGRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAG--KEDKIKVIGFDGNPEAIKAIAKGGKikadI 234
|
250 260 270
....*....|....*....|....*....|..
gi 2437085935 291 VQPMYDIGAVAMRLLTKYMNKEKVEDHTVILP 322
Cdd:cd06322 235 AQQPDKIGQETVEAIVKYLAGETVEKEILIPP 266
|
|
| PBP1_ABC_IbpA-like |
cd19968 |
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ... |
62-322 |
3.97e-11 |
|
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: 62.40 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDI--HIEEFKKSP 139
Cdd:cd19968 1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALvpAIEAAIKAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 140 VPIVlaaSFDEQNET----PSVNIDYTQAAyDAMKHFIEQ---GHKRIGFV-----SGPFIDKAgsakklQGYKKALEEA 207
Cdd:cd19968 81 IPVV---TVDRRAEGaapvPHVGADNVAGG-REVAKFVVDklpNGAKVIELtgtpgSSPAIDRT------KGFHEELAAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 208 GisyDENLVID--GDYTYDSGIEAFEK-LWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVpTDVEVLGFDNTRLAL--M 282
Cdd:cd19968 151 P---KIKVVFEqtGNFERDEGLTVMENiLTSLPGPPDAIICANDDMALGAIEAMRAAGLDL-KKVKVIGFDAVPDALqaI 226
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2437085935 283 VRPQLSTVVQ--PMYDIGAvAMRLLTKYMNKEKvEDHTVILP 322
Cdd:cd19968 227 KDGELYATVEqpPGGQART-ALRILVDYLKDKK-APKKVNLK 266
|
|
| PBP1_GGBP |
cd01539 |
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ... |
62-322 |
4.31e-11 |
|
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: 62.60 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIA-TMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIH--IEEFKKS 138
Cdd:cd01539 2 KIGVFIYNYDDTFISSVRKALEKAAkAGGKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQtiIDKAKAA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 139 PVPIVLAasfdeqNETPSVNI--DYTQAAY---DAMKHFIEQGHKRI-GFVSGPFIDKAGSaKKLQ-------------- 198
Cdd:cd01539 82 NIPVIFF------NREPSREDlkSYDKAYYvgtDAEESGIMQGEIIAdYWKANPEIDKNGD-GKIQyvmlkgepghqdai 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 199 ----GYKKALEEAGISYdENLVID-GDYTYDSGIEAFEKLWS-NDEKPTAIFVSSDEMALGVIHAAQDAGLN---VPTDV 269
Cdd:cd01539 155 artkYSVKTLNDAGIKT-EQLAEDtANWDRAQAKDKMDAWLSkYGDKIELVIANNDDMALGAIEALKAAGYNtgdGDKYI 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2437085935 270 EVLGFDNTRLAL-------MvrpqLSTVVQPMYDIGAVAMRL---------LTKYMNKEKVEDHTVILP 322
Cdd:cd01539 234 PVFGVDATPEALeaikegkM----LGTVLNDAKAQAKAIYELaknlangkePLETGYKFLVEGKYVRIP 298
|
|
| PBP1_sensor_kinase-like |
cd06308 |
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ... |
198-320 |
1.32e-10 |
|
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: 61.02 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 198 QGYKKALEEagisYDENLVI---DGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNvpTDVEVLGF 274
Cdd:cd06308 142 KGFLEAIAK----YPGIKIVasqDGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGRE--KEIKIIGV 215
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2437085935 275 D--NTRLALMVR--PQLSTVVQPmyDIGAVAMRLLTKYMNKEKVEDHTVI 320
Cdd:cd06308 216 DglPEAGEKAVKdgILAATFLYP--TGGKEAIEAALKILNGEKVPKEIVL 263
|
|
| Periplasmic_Binding_Protein_type1 |
cd01391 |
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ... |
70-305 |
1.45e-10 |
|
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: 61.13 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 70 ISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIHIE---EFKKSPVpIVLAA 146
Cdd:cd01391 12 IREQFGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGPGSSSVAIVIQnlaQLFDIPQ-LALDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 147 SFDEQNETP------SVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFIDKAGSakKLQGYKKALEEAGISYDENLVIDgd 220
Cdd:cd01391 91 TSQDLSDKTlykyflSVVFSDTLGARLGLDIVKRKNWTYVAAIHGEGLNSGEL--RMAGFKELAKQEGICIVASDKAD-- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 221 ytYDSGIEAFE---KLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNvpTDVEVLGFDNTRLALMVR-----PQLSTVVQ 292
Cdd:cd01391 167 --WNAGEKGFDralRKLREGLKARVIVCANDMTARGVLSAMRRLGLV--GDVSVIGSDGWADRDEVGyeveaNGLTTIKQ 242
|
250
....*....|...
gi 2437085935 293 PMYDIGAVAMRLL 305
Cdd:cd01391 243 QKMGFGITAIKAM 255
|
|
| PBP1_rhizopine_binding-like |
cd06301 |
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ... |
62-320 |
3.47e-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: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYK-YNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGED--ITDIHIEEFKKS 138
Cdd:cd06301 2 KIGVSMQNFSDEFLTYLRDAIEAYAKEYPgVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDtdASAPAVDAAADA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 139 PVPIVL--AASFDEQNETPSVNIDYTQAAYDAMKHFIEQ--GHKRIGFVSGPfIDKAGSAKKLQGYKKALEE-AGIsyde 213
Cdd:cd06301 82 GIPLVYvnREPDSKPKGVAFVGSDDIESGELQMEYLAKLlgGKGNIAILDGV-LGHEAQILRTEGNKDVLAKyPGM---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 214 NLVID--GDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNvpTDVEVLGFDNTRLAL--MVRPQLS- 288
Cdd:cd06301 157 KIVAEqtANWSREKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKK--DDILVAGIDATPDALkaMKAGRLDa 234
|
250 260 270
....*....|....*....|....*....|..
gi 2437085935 289 TVVQPMYDIGAVAMRLLTKYMNKEKVEDHTVI 320
Cdd:cd06301 235 TVFQDAAGQGETAVDVAVKAAKGEEVESDIWI 266
|
|
| PBP1_ABC_sugar_binding-like |
cd06324 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ... |
115-281 |
2.79e-09 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380547 [Multi-domain] Cd Length: 317 Bit Score: 57.61 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 115 KQVDGIVFMGED-ITDIHIEEFKKSPVPIVL---AASFDEQNET-----------PSVNIDYTQAAYDAMKHFIEQGHKR 179
Cdd:cd06324 57 PKPDYLILVNEKgVAPELLELAEQAKIPVFLinnDLTDEERALLgkprekfkywlGSIVPDNEQAGYLLAKALIKAARKK 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 180 IGFVSGPFI----DKAGSA--KKLQGYKKALEEAGisyDENLV--IDGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMA 251
Cdd:cd06324 137 SDDGKIRVLaisgDKSTPAsiLREQGLRDALAEHP---DVTLLqiVYANWSEDEAYQKTEKLLQRYPDIDIVWAANDAMA 213
|
170 180 190
....*....|....*....|....*....|
gi 2437085935 252 LGVIHAAQDAGLNVPTDVEVLGFDNTRLAL 281
Cdd:cd06324 214 LGAIDALEEAGLKPGKDVLVGGIDWSPEAL 243
|
|
| PBP1_ABC_sugar_binding-like |
cd06310 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
62-318 |
5.67e-09 |
|
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: 56.20 E-value: 5.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIIL----SNSD---QNKekefhLLNTMLGKQVDGIVFMGEDITDI--HI 132
Cdd:cd06310 1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFvgpeSEEDvagQNS-----LLEELINKKPDAIVVAPLDSEDLvdPL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 133 EEFKKSPVPIVLAASFDEQNE-TPSVNIDYTQAAYDAMKHFIEQ-GHK-RIGFVSGpfidKAGSAKKLQGYKKALEEAGI 209
Cdd:cd06310 76 KDAKDKGIPVIVIDSGIKGDAyLSYIATDNYAAGRLAAQKLAEAlGGKgKVAVLSL----TAGNSTTDQREEGFKEYLKK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 210 SYDENLVIDGDY---TYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNvpTDVEVLGFD---NTRLALMV 283
Cdd:cd06310 152 HPGGIKVLASQYagsDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLS--GQIKIVGFDsqeELLDALKN 229
|
250 260 270
....*....|....*....|....*....|....*
gi 2437085935 284 RPQLSTVVQPMYDIGAVAMRLLTKYMNKEKVEDHT 318
Cdd:cd06310 230 GKIDALVVQNPYEIGYEGIKLALKLLKGEEVPKNI 264
|
|
| PRK10653 |
PRK10653 |
ribose ABC transporter substrate-binding protein RbsB; |
62-315 |
7.35e-09 |
|
ribose ABC transporter substrate-binding protein RbsB;
Pssm-ID: 182620 [Multi-domain] Cd Length: 295 Bit Score: 55.87 E-value: 7.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEfhLLNtmlgkqVDGIVFMGEDITDIHIEEFKKSPVP 141
Cdd:PRK10653 28 TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNPAKE--LAN------VQDLTVRGTKILLINPTDSDAVGNA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 142 IVLAasfdEQNETPSVNIDYTQAAYDAMKHfIEQGHKRIGFVSGPFI-DKAGS-AKKLQ---------------GYKKAL 204
Cdd:PRK10653 100 VKMA----NQANIPVITLDRGATKGEVVSH-IASDNVAGGKMAGDFIaKKLGEgAKVIQlegiagtsaarergeGFKQAV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 205 EEAGISYDENLVIDGDYTydSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGlnvPTDVEVLGFDNTR--LALM 282
Cdd:PRK10653 175 AAHKFNVLASQPADFDRT--KGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAG---KSDVMVVGFDGTPdgIKAV 249
|
250 260 270
....*....|....*....|....*....|....
gi 2437085935 283 VRPQLS-TVVQPMYDIGAVAMRLLTKYMNKEKVE 315
Cdd:PRK10653 250 NRGKLAaTIAQQPDQIGAIGVETADKVLKGEKVE 283
|
|
| PBP1_ABC_sugar_binding-like |
cd19966 |
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ... |
74-277 |
1.26e-08 |
|
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: 55.02 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 74 FYAELARGIEDIA--TMYKYNIILSNSDQNKEKEfhLLNTMLGKQVDGIVFMG---EDITDIHIEEFKKSPVPIVLAASF 148
Cdd:cd19966 14 FWTVVYNGAKDAAadLGVDLDYVFSSWDPEKMVE--QFKEAIAAKPDGIAIMGhpgDGAYTPLIEAAKKAGIIVTSFNTD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 149 DEQNETPS-----VNIDYTQAAYDAMKHFIEQGHKRIG---FVSGPFIDKAGSAKKLQGYKKALEEAGISYDENLVIDGD 220
Cdd:cd19966 92 LPKLEYGDcglgyVGADLYAAGYTLAKELVKRGGLKTGdrvFVPGLLPGQPYRVLRTKGVIDALKEAGIKVDYLEISLEP 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2437085935 221 YTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNvPTDVEVLGFDNT 277
Cdd:cd19966 172 NKPAEGIPVMTGYLAANPDVKAIVGDGGGLTANVAKYLKAAGKK-PGEIPVAGFDLS 227
|
|
| PBP1_sugar_binding |
cd06307 |
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ... |
63-328 |
2.82e-08 |
|
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic sugar-binding domain of uncharacterized transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes.
Pssm-ID: 380530 [Multi-domain] Cd Length: 275 Bit Score: 54.10 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 63 VGVIIPDISNTFYAELARGIEDIATMYKY---NIILSNSDQNKEKEF-HLLNtMLGKQVDGIVFMGEDITDIH--IEEFK 136
Cdd:cd06307 2 FGFLLPSPENPFYELLRRAIEAAAAALRDrrvRLRIHFVDSLDPEALaAALR-RLAAGCDGVALVAPDHPLVRaaIDELA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 137 KSPVPIV-LAASFDEQNETPSVNIDYTQA---AYDAMKHFIEQGHKRIGFVSGPFIDKaGSAKKLQGYKKALEEAGisyd 212
Cdd:cd06307 81 ARGIPVVtLVSDLPGSRRLAYVGIDNRAAgrtAAWLMGRFLGRRPGKVLVILGSHRFR-GHEEREAGFRSVLRERF---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 213 ENL-VIDGDYTYDSGIEAFE---KLWSNDEKPTAIFVSSDEMAlGVIHAAQDAGLnvPTDVEVLGFD---NTRLALMVRp 285
Cdd:cd06307 156 PDLtVLEVLEGLDDDELAYEllrELLARHPDLVGIYNAGGGNE-GIARALREAGR--ARRVVFIGHEltpETRRLLRDG- 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2437085935 286 QLSTVV-QPMYDIGAVAMRLLTKYMNKEKVEDHTVILPHRIQFR 328
Cdd:cd06307 232 TIDAVIdQDPELQARRAIEVLLAHLGGKGPAPPQPPIPIEIITR 275
|
|
| PBP1_methylthioribose_binding-like |
cd06305 |
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ... |
237-316 |
4.02e-08 |
|
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: 53.45 E-value: 4.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 237 DEKPTAIFVSSDEMALGVIHAAQDAGLnvpTDVEVLGFD--NTRLALMVR---PQLSTVVQPMYDIGAVAMRLLTKYMNK 311
Cdd:cd06305 182 EGGIDAIWAAWDEPAKGAVQALEEAGR---TDIKVYGVDisNQDLELMADegsPWVATAAQDPALIGTVAVRNVARKLAG 258
|
....*
gi 2437085935 312 EKVED 316
Cdd:cd06305 259 EDLPD 263
|
|
| PBP1_ABC_ThpA_XypA |
cd06313 |
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ... |
62-320 |
5.58e-08 |
|
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group includes periplasmic D-threitol-binding protein ThpA and xylitol/L-sorbitol-binding protein XypA, which are part of sugar ABC-type transport systems. Both ThpA and XypA share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.
Pssm-ID: 380536 [Multi-domain] Cd Length: 277 Bit Score: 53.04 E-value: 5.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIH--IEEFKKSP 139
Cdd:cd06313 1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALApaVEKAKEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 140 VPIVLAASFDEQNE-TPSVNIDYTQAAYDAMKHFIEQ--GHKRIGFVSGPfIDKAGSAKKLQGYKKALEEAgisYDENLV 216
Cdd:cd06313 81 IPLVGVNALIENEDlTAYVGSDDVVAGELEGQAVADRlgGKGNVVILEGP-IGQSAQIDRGKGIENVLKKY---PDIKVL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 217 ID--GDYTYDSGIEAFE-KLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLnvpTDVEVLGFDNTRLAL-MVRP--QLSTV 290
Cdd:cd06313 157 AEqtANWSRDEAMSLMEnWLQAYGDEIDGIIAQNDDMALGALQAVKAAGR---DDIPVVGIDGIEDALqAVKSgeLIATV 233
|
250 260 270
....*....|....*....|....*....|
gi 2437085935 291 VQPMYDIGAVAMRLLTKYMNKEKVEDHTVI 320
Cdd:cd06313 234 LQDAEAQGKGAVEVAVDAVKGEGVEKKYYI 263
|
|
| PBP1_ABC_sugar_binding-like |
cd19971 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
62-320 |
2.10e-07 |
|
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380626 [Multi-domain] Cd Length: 267 Bit Score: 51.43 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFM---GEDITDIhIEEFKKS 138
Cdd:cd19971 1 KFGFSYMTMNNPFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNpvdSEGIRPA-LEAAKEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 139 PVPIVLaasFDeqneTPSVNIDYTQA-----AYDA--------MKHFIEQGhkRIGFVSGPFidkAGSAK-KLQGYKKAL 204
Cdd:cd19971 80 GIPVIN---VD----TPVKDTDLVDStiasdNYNAgklcgedmVKKLPEGA--KIAVLDHPT---AESCVdRIDGFLDAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 205 eEAGISYDENLVIDGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLnvPTDVEVLGFDNTRLA---- 280
Cdd:cd19971 148 -KKNPKFEVVAQQDGKGQLEVAMPIMEDILQAHPDLDAVFALNDPSALGALAALKAAGK--LGDILVYGVDGSPDAkaai 224
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2437085935 281 ---LMVrpqlSTVVQPMYDIGAVAMRLLTKYMNKEKVEDHTVI 320
Cdd:cd19971 225 kdgKMT----ATAAQSPIEIGKKAVETAYKILNGEKVEKEIVV 263
|
|
| PBP1_ABC_sugar_binding-like |
cd19970 |
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ... |
62-276 |
2.24e-07 |
|
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: 51.48 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIAT-MYKYNIILS--NSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIhIEEFKK- 137
Cdd:cd19970 1 KVALVMKSLANEFFIEMEKGARKHAKeANGYELLVKgiKQETDIEQQIAIVENLIAQKVDAIVIAPADSKAL-VPVLKKa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 138 --SPVPIV-----LAASFDEQN--ETPSVNIDYTQAAYDAMKHFIEQ--GHKRIGFVSGPFIDKAGSAKKLqGYKKALEE 206
Cdd:cd19970 80 vdAGIAVInidnrLDADALKEGgiNVPFVGPDNRQGAYLAGDYLAKKlgKGGKVAIIEGIPGADNAQQRKA-GFLKAFEE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2437085935 207 AGIsydeNLV--IDGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNvpTDVEVLGFDN 276
Cdd:cd19970 159 AGM----KIVasQSANWEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKA--GKVLVVGFDN 224
|
|
| PBP1_ABC_sugar_binding-like |
cd06317 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
62-322 |
4.48e-07 |
|
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380540 [Multi-domain] Cd Length: 281 Bit Score: 50.45 E-value: 4.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIH--IEEFKKSP 139
Cdd:cd06317 1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIpaIKRASEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 140 VPIV-LAASFDEQNETPSVNIDYTQAAYDAMKHFIE------QGHKRIGFVSgpFIDKAGSAKKLQGYKKALeEAGISYD 212
Cdd:cd06317 81 IPVIaYDAVIPSDFQAAQVGVDNLEGGKEIGKYAADyikaelGGQAKIGVVG--ALSSLIQNQRQKGFEEAL-KANPGVE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 213 ENLVIDGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNvpTDVEVLGFDNTRLALMVRPQ----LS 288
Cdd:cd06317 158 IVATVDGQNVQEKALSAAENLLTANPDLDAIYATGEPALLGAVAAVRSQGRQ--GKIKVFGWDLTKQAIFLGIDegvlQA 235
|
250 260 270
....*....|....*....|....*....|....
gi 2437085935 289 TVVQPMYDIGAVAMRLLTKYMNKEKVEDhTVILP 322
Cdd:cd06317 236 VVQQDPEKMGYEAVKAAVKAIKGEDVEK-TIDVP 268
|
|
| PBP1_ABC_sugar_binding-like |
cd20004 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
62-319 |
2.74e-06 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380659 [Multi-domain] Cd Length: 273 Bit Score: 48.00 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIIL-SNSDQNK-EKEFHLLNTMLGKQVDGIVFMGEDITDI--HIEEFKK 137
Cdd:cd20004 1 CIAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWrGPSREDDvEAQIQIIEYFIDQGVDGIVLAPLDRKALvaPVERARA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 138 SPVPIVLAAS-FDEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFIDKAGS-AKKLQGYKKALEEAgiSYDENL 215
Cdd:cd20004 81 QGIPVVIIDSdLGGDAVISFVATDNYAAGRLAAKRMAKLLNGKGKVALLRLAKGSAStTDRERGFLEALKKL--APGLKV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 216 VID--GDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLnvPTDVEVLGFDNTR--LALMVRPQLS-TV 290
Cdd:cd20004 159 VDDqyAGGTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGL--AGKVKFIGFDASDllLDALRAGEISaLV 236
|
250 260
....*....|....*....|....*....
gi 2437085935 291 VQPMYDIGAVAMRLLTKYMNKEKVEDHTV 319
Cdd:cd20004 237 VQDPYRMGYLGVKTAVAALRGKPVPKRID 265
|
|
| PBP1_ABC_sugar_binding-like |
cd19996 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
62-266 |
3.96e-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: 47.62 E-value: 3.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNI---ILSNSDQNKEKEFHLLNTMLGKQVDGIVF--MGEDITDIHIEEFK 136
Cdd:cd19996 1 TIGFSNAGLGNSWRVQMIAEFEAEAAKLKKLIkelIYTDAQGDTQKQIADIQDLIAQGVDAIIVspNSPTALLPAIEKAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 137 KSPVPIVLAASFDE-QNETPSVNIDYTQAAYDAMKHFIEQ--GHKRIGFVSGPfidkAG---SAKKLQGYKKALEEA-GI 209
Cdd:cd19996 81 AAGIPVVLFDSGVGsDKYTAFVGVDDAAFGRVGAEWLVKQlgGKGNIIALRGI----AGvsvSEDRWAGAKEVFKEYpGI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2437085935 210 S-YDENlviDGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNVP 266
Cdd:cd19996 157 KiVGEV---YADWDYAKAKQAVESLLAAYPDIDGVWSDGGAMTLGAIEAFEEAGRPLV 211
|
|
| PBP1_ABC_sugar_binding-like |
cd06311 |
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ... |
62-272 |
1.45e-05 |
|
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: 45.82 E-value: 1.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYK-YNIILSNSDqNKEKEFHLLNTMLGKQVDGIVFM---GEDITDIhIEEFKK 137
Cdd:cd06311 1 TIGISIPSADHGWTAGVAYYAEKQAKELAdLEYKLVTSS-NANEQVSQLEDLIAQKVDAIVILpqdSEELTVA-AQKAKD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 138 SPVPIVlaasfdeqnetpSVNIDYTQAAYDAmkhFIEQGHKRIGFVSGPFI-DKAGSAKKL----------------QGY 200
Cdd:cd06311 79 AGIPVV------------NFDRGLNVLIYDL---YVAGDNPGMGVVSAEYIgKKLGGKGNVvvlevpssgsvneervAGF 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2437085935 201 KKALEeaGISYDENLVI-DGDYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLnvpTDVEVL 272
Cdd:cd06311 144 KEVIK--GNPGIKILAMqAGDWTREDGLKVAQDILTKNKKIDAVWAADDDMAIGVLQAIKEAGR---TDIKVM 211
|
|
| PBP1_tmGBP |
cd06314 |
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ... |
62-325 |
4.65e-05 |
|
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs; Periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs from other bacteria. They are members of the type 1 periplasmic binding protein superfamily which consists of two domains connected by a three-stranded hinge. TmGBP is specific for glucose and its binding pocket is buried at the interface of the two domains. TmGBP also exhibits high thermostability and the highest structural similarity to E. coli glucose binding protein (ecGBP).
Pssm-ID: 380537 [Multi-domain] Cd Length: 271 Bit Score: 44.11 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIIL---SNSDQNKEKEfhLLNTMLGKQVDGIVFMGED---ITDIhIEEF 135
Cdd:cd06314 1 TFALVPKGLNNPFWDLAEAGAEKAAKELGVNVEFvgpQKSDAAEQVQ--LIEDLIARGVDGIAISPNDpeaVTPV-INKA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 136 KKSPVPIVlaaSFDeqneTPSV-----------NIDYTQAAYDAMKHFIEQGHKRIGFVSGPfiDKAGSAKKLQGYKKAL 204
Cdd:cd06314 78 ADKGIPVI---TFD----SDAPdskrlayigtdNYEAGREAGELMKKALPGGGKVAIITGGL--GADNLNERIQGFKDAL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 205 EEagisYDENLVIDGDYTYDS---GIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLnvPTDVEVLGFDNTRLAL 281
Cdd:cd06314 149 KG----SPGIEIVDPLSDNDDiakAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGK--VGKVKIVGFDTLPETL 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2437085935 282 -MVRPQL--STVVQPMYDIGAVAMRLLTKYMNKEKVEDHTVILPHRI 325
Cdd:cd06314 223 qGIKDGViaATVGQRPYEMGYLSVKLLYKLLKGGKPVPDVIDTGVDV 269
|
|
| PBP1_ABC_sugar_binding-like |
cd06300 |
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ... |
92-322 |
6.82e-05 |
|
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; 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: 380523 [Multi-domain] Cd Length: 302 Bit Score: 43.85 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 92 NIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIH--IEEFKKSPVPIVLAASFDEQNETPSVNIDYTQAAYDAM 169
Cdd:cd06300 36 ELIVANSNGDATEQIAQIRNLIDQGVDAIIINPSSPTALNavIEQAADAGIPVVAFDGAVTSPDAYNVSNDQVEWGRLGA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 170 KHFIEQ--GHKRIGFVSGpfIDKA-GSAKKLQGYKKALEEAGisyDENLV--IDGDYTYDSGIEAFEKLWSNDEKPTAIF 244
Cdd:cd06300 116 KWLFEAlgGKGNVLVVRG--IAGApASADRHAGVKEALAEYP---GIKVVgeVFGGWDEATAQTAMLDFLATHPQVDGVW 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 245 VSSDEmALGVIHAAQDAGLNVptdVEVLGFDNTRLALMVRPQL------STVVQPMYDIGA---VAMRLLTKYMNKEKve 315
Cdd:cd06300 191 TQGGE-DTGVLQAFQQAGRPP---VPIVGGDENGFAKQWWKHPkkgltgAAVWPPPAIGAAgleVALRLLEGQGPKPQ-- 264
|
....*..
gi 2437085935 316 dhTVILP 322
Cdd:cd06300 265 --SVLLP 269
|
|
| PBP1_ABC_sugar_binding-like |
cd20006 |
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ... |
69-316 |
8.18e-05 |
|
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380661 [Multi-domain] Cd Length: 274 Bit Score: 43.74 E-value: 8.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 69 DISNTFYAELARGIEDIATMYKYNIILS--NSDQNKEKEFHLLNTMLGKQVDGIVFMGED---ITDIhIEEFKKSPVPIV 143
Cdd:cd20006 10 DPNSDFWQTVKSGAEAAAKEYGVDLEFLgpESEEDIDGQIELIEEAIAQKPDAIVLAASDydrLVEA-VERAKKAGIPVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 144 LAASFDEQNETPS-VNIDYTQAAYDAMKHFIEQGHK--RIGFVSgpFIDKAGSAKKL-QGYKKALEEagisYDENLVIDG 219
Cdd:cd20006 89 TIDSPVNSKKADSfVATDNYEAGKKAGEKLASLLGEkgKVAIVS--FVKGSSTAIEReEGFKQALAE----YPNIKIVET 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 220 DYTYDSGIEAFE---KLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNvpTDVEVLGFDNT--RLALMVRPQL-STVVQP 293
Cdd:cd20006 163 EYCDSDEEKAYEitkELLSKYPDINGIVALNEQSTLGAARALKELGLG--GKVKVVGFDSSveEIQLLEEGIIdALVVQN 240
|
250 260
....*....|....*....|...
gi 2437085935 294 MYDIGAVAMRLLTKYMNKEKVED 316
Cdd:cd20006 241 PFNMGYLSVQAAVDLLNGKKIPK 263
|
|
| PBP1_ABC_D-talitol-like |
cd06318 |
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ... |
62-314 |
1.10e-03 |
|
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; Periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.
Pssm-ID: 380541 [Multi-domain] Cd Length: 282 Bit Score: 40.09 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIhieefkkspVP 141
Cdd:cd06318 1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGL---------TP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 142 IVLAAsfdEQNETPSVNIDYTQAAYDAMKHFIEQGHKRIGFVSGPFI-----DKAGSAKKLQGYKKALEE--------AG 208
Cdd:cd06318 72 AVKAA---KAAGIPVITVDSALDPSANVATQVGRDNKQNGVLVGKEAakalgGDPGKIIELSGDKGNEVSrdrrdgflAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 209 ISyDENLVIDG------------DYTYDSGIEAFEKLWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNvpTDVEVLGFDN 276
Cdd:cd06318 149 VN-EYQLRKYGksnikvvaqpygNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGML--DKVKVAGADG 225
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2437085935 277 TRLALMVRPQ---LSTVVQPMYDIGAVAMRLLTKYMNKEKV 314
Cdd:cd06318 226 QKEALKLIKDgkyVATGLNDPDLLGKTAVDTAAKVVKGEES 266
|
|
| PBP1_ABC_sugar_binding-like |
cd19999 |
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ... |
62-266 |
1.36e-03 |
|
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: 380654 [Multi-domain] Cd Length: 313 Bit Score: 39.98 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 62 TVGVIIPDISNTFYAELARGIEDIATMYKY-----NIILSNSDQNKEKEFHLLNTMLGKQVDGIVFMGEDITDIH--IEE 134
Cdd:cd19999 1 VIGVSNGYVGNEWRAQMIADFEEVAAEYKEegvisDLIVQNADADATGQISQIRNMINEGVDAILIDPVSATALNpvIEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 135 FKKSPVPIVlaaSFDEQNETP-SVNIDYTQAAYDAM--KHFIEQGHKR-----IGFVSGPFIDKAgsakKLQGYKKALEE 206
Cdd:cd19999 81 AQAAGILVV---SFDQPVSSPdAINVVIDQYKWAAIqaQWLAEQLGGKgnivaINGVAGNPANEA----RVKAADDVFAK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2437085935 207 AgisYDENLVID--GDYTYDSGIEAFEKLWSNDEKPTAIFVSsDEMALGVIHAAQDAGLNVP 266
Cdd:cd19999 154 Y---PGIKVLASvpGGWDQATAQQVMATLLATYPDIDGVLTQ-DGMAEGVLRAFQAAGKDPP 211
|
|
| PBP1_ABC_xylose_binding |
cd19991 |
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ... |
92-320 |
1.41e-03 |
|
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380646 [Multi-domain] Cd Length: 284 Bit Score: 39.91 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 92 NIILSNSDQNKEKEFHLLNTMLGKQVDGIVFM---GEDITDIhIEEFKKSPVPI------VLAASFDEQNETPSVNIDYT 162
Cdd:cd19991 31 EVIVQSANGDDEKQISQAEELIEQGVDVLVVVpnnGEALAPI-VKEAKKAGVPVlaydrlILNADVDLYVSFDNEKVGEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 163 QAAYdAMKHFIEQGHKRIGfvsGPFIDKagSAKKLQ-GYKKALEEAGISYDENLVID---GDYTYDSGIEAFEK-LWSND 237
Cdd:cd19991 110 QAEA-LVKAKPKGNYVLLG---GSPTDN--NAKLFReGQMKVLQPLIDSGDIKVVGDqwvDDWDPEEALKIMENaLTANN 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 238 EKPTAIFVSSDEMALGVIHAAQDAGLNvpTDVEVLGFDnTRLALMVR----PQLSTVVQPMYDIGAVAMRLLTKYMNKEK 313
Cdd:cd19991 184 NKIDAVIASNDGTAGGAIQALAEQGLA--GKVAVSGQD-ADLAACQRivegTQTMTIYKPIKELAEKAAELAVALAKGEK 260
|
....*..
gi 2437085935 314 VEDHTVI 320
Cdd:cd19991 261 NEANRTI 267
|
|
| PBP1_ABC_xylose_binding-like |
cd19992 |
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ... |
63-316 |
2.36e-03 |
|
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.
Pssm-ID: 380647 [Multi-domain] Cd Length: 284 Bit Score: 39.10 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 63 VGVIIPDISNTFYAELARGIEDIATMYKYNIILSNSDQNKEKEFHLLNTMLGKQVDGIVFM---GEDITDIhIEEFKKSP 139
Cdd:cd19992 2 IGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIApvdAGAAANI-VDKAKAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 140 VPIVlaaSFDeqNETPSVNIDYTqAAYDAMK----------HFIEQGHkrIGFVSGpfiDKAGSAKKL--QGYKKALEEA 207
Cdd:cd19992 81 VPVI---SYD--RLILNADVDLY-VGRDNYKvgqlqaeyalEAVPKGN--YVILSG---DPGDNNAQLitAGAMDVLQPA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 208 GISYDENLVIDgDYTYD-SGIEAFEK----LWSNDEKPTAIFVSSDEMALGVIHAAQDAGLNvpTDVEVLGFDNTRLAL- 281
Cdd:cd19992 150 IDSGDIKIVLD-QYVKGwSPDEAMKLvenaLTANNNNIDAVLAPNDGMAGGAIQALKAQGLA--GKVFVTGQDAELAALk 226
|
250 260 270
....*....|....*....|....*....|....*..
gi 2437085935 282 --MVRPQLSTVVQPMYDIGAVAMRLLTKYMNKEKVED 316
Cdd:cd19992 227 riVEGTQTMTVWKDLKELARAAADAAVKLAKGEKPQT 263
|
|
| LivK |
COG0683 |
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid ... |
7-224 |
4.24e-03 |
|
ABC-type branched-chain amino acid transport system, periplasmic component [Amino acid transport and metabolism];
Pssm-ID: 440447 [Multi-domain] Cd Length: 314 Bit Score: 38.37 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 7 DVAREANVSMATVSrvvNGNPNVkptTRKKVLEAIDRLGYRPNAVARGLAS-----KKTTTVGVIIPDisNTFYAELARG 81
Cdd:COG0683 89 PVAEEAGVPLISPS---ATAPAL---TGPECSPYVFRTAPSDAQQAEALADylakkLGAKKVALLYDD--YAYGQGLAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 82 IEDIATMYKYNIILSNSDQNKEKEFH-LLNTMLGKQVDGIVF--MGEDITDIhIEEFKKSPVPIVLAASF-----DEQNE 153
Cdd:COG0683 161 FKAALKAAGGEVVGEEYYPPGTTDFSaQLTKIKAAGPDAVFLagYGGDAALF-IKQAREAGLKGPLNKAFvkaykAKYGR 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2437085935 154 TPSvniDYTQAAYDAMKHFIEQghkrigfvsgpfIDKAGSAKKlQGYKKALEeaGISYDEnlvIDGDYTYD 224
Cdd:COG0683 240 EPS---SYAAAGYDAALLLAEA------------IEKAGSTDR-EAVRDALE--GLKFDG---VTGPITFD 289
|
|
| PBP1_ABC_ligand_binding-like |
cd19978 |
periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to ... |
161-281 |
4.50e-03 |
|
periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to be involved in the uptake of amino acids, peptides, or inorganic ions; This group includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type transport systems that are predicted to be involved in the uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); its ligand specificity has not been determined experimentally, however.
Pssm-ID: 380633 [Multi-domain] Cd Length: 341 Bit Score: 38.33 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2437085935 161 YTQAAYDAMKHFIEQG-HKRIGFvsgpFI--D---KAGsakkLQGYKKALEEAGIsydeNLVIDGDYTYDSGI--EAFEK 232
Cdd:cd19978 120 YADETEALVDYLVKTLgPKRIAI----FYqnDafgLAG----LEGAKKALKKRGL----TPVAEGSYTRNTLDveEALAK 187
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 2437085935 233 LwsNDEKPTAI-FVSSDEMALGVIHAAQDAGLNVP-TDVEVLGFDNTRLAL 281
Cdd:cd19978 188 I--LKAKPEAIiLVGTYAPAAEFIRLARAAGLNPLfANVSFVGSEALALEL 236
|
|
| |
