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Conserved domains on  [gi|495004537|ref|WP_007730551|]
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gluconate operon transcriptional repressor GntR [Cronobacter dublinensis]

Protein Classification

HTH-type transcriptional regulator GntR( domain architecture ID 11487547)

HTH-type transcriptional regulator GntR functions as a negative regulator for the gluconate utilization system GNT-I, the gntUKR operon

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK14987 PRK14987
HTH-type transcriptional regulator GntR;
1-331 0e+00

HTH-type transcriptional regulator GntR;


:

Pssm-ID: 184949 [Multi-domain]  Cd Length: 331  Bit Score: 648.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537   1 MKKRRPVLQDVADRVGVTKMTISRYLRNPEQVSLALRSKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAE 80
Cdd:PRK14987   1 MKKKRPVLQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  81 VLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPVVELMDSVSPCLDIAV 160
Cdd:PRK14987  81 VLRGIESVTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIEVAGIPVVELMDSQSPCLDIAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 161 GFDNFDAARQMTAEIIARGHRHVAYLGARLDERTIMKQKGYEQAMLDAGLTPYSVMVEHSSSFSTGSELLRQARREYPQL 240
Cdd:PRK14987 161 GFDNFEAARQMTTAIIARGHRHIAYLGARLDERTIIKQKGYEQAMLDAGLVPYSVMVEQSSSYSSGIELIRQARREYPQL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 241 DSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGAERLLARIRGESVTPQRLD 320
Cdd:PRK14987 241 DGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARIRGESVTPKMLD 320
                        330
                 ....*....|.
gi 495004537 321 LGFTLSPGGSI 331
Cdd:PRK14987 321 LGFTLSPGGSI 331
 
Name Accession Description Interval E-value
PRK14987 PRK14987
HTH-type transcriptional regulator GntR;
1-331 0e+00

HTH-type transcriptional regulator GntR;


Pssm-ID: 184949 [Multi-domain]  Cd Length: 331  Bit Score: 648.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537   1 MKKRRPVLQDVADRVGVTKMTISRYLRNPEQVSLALRSKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAE 80
Cdd:PRK14987   1 MKKKRPVLQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  81 VLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPVVELMDSVSPCLDIAV 160
Cdd:PRK14987  81 VLRGIESVTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIEVAGIPVVELMDSQSPCLDIAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 161 GFDNFDAARQMTAEIIARGHRHVAYLGARLDERTIMKQKGYEQAMLDAGLTPYSVMVEHSSSFSTGSELLRQARREYPQL 240
Cdd:PRK14987 161 GFDNFEAARQMTTAIIARGHRHIAYLGARLDERTIIKQKGYEQAMLDAGLVPYSVMVEQSSSYSSGIELIRQARREYPQL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 241 DSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGAERLLARIRGESVTPQRLD 320
Cdd:PRK14987 241 DGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARIRGESVTPKMLD 320
                        330
                 ....*....|.
gi 495004537 321 LGFTLSPGGSI 331
Cdd:PRK14987 321 LGFTLSPGGSI 331
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
66-330 1.12e-125

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: 360.66  E-value: 1.12e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPV 145
Cdd:cd01575    2 VAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEHTPATRKLLRAAGIPV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 146 VELMDSVSPCLDIAVGFDNFDAARQMTAEIIARGHRHVAYLGARL--DERTIMKQKGYEQAMLDAGL-TPYSVMVEHSSS 222
Cdd:cd01575   82 VETWDLPDDPIDMAVGFSNFAAGRAMARHLIERGYRRIAFVGARLdgDSRARQRLEGFRDALAEAGLpLPLVLLVELPSS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 223 FSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGA 302
Cdd:cd01575  162 FALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVRVPRYEIGRKAA 241
                        250       260
                 ....*....|....*....|....*...
gi 495004537 303 ERLLARIRGESVTPQRLDLGFTLSPGGS 330
Cdd:cd01575  242 ELLLARLEGEEPEPRVVDLGFELVRRES 269
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
3-330 1.01e-105

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 312.52  E-value: 1.01e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537   3 KRRPVLQDVADRVGVTKMTISRYLRNPEQVSLALRSKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVL 82
Cdd:COG1609    1 RKRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  83 RGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPVVELMDSVSPCLDIAVGF 162
Cdd:COG1609   81 RGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRPLPDPGVPSVGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 163 DNFDAARQMTAEIIARGHRHVAYLGARLD-ERTIMKQKGYEQAMLDAGLTPYSVMVEHSS-SFSTGSELLRQARREYPQL 240
Cdd:COG1609  161 DNRAGARLATEHLIELGHRRIAFIGGPADsSSARERLAGYREALAEAGLPPDPELVVEGDfSAESGYEAARRLLARGPRP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 241 DSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGAERLLARIRGESVTPQRLD 320
Cdd:COG1609  241 TAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERVL 320
                        330
                 ....*....|
gi 495004537 321 LGFTLSPGGS 330
Cdd:COG1609  321 LPPELVVRES 330
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
65-319 1.98e-30

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


Pssm-ID: 395423 [Multi-domain]  Cd Length: 281  Bit Score: 116.46  E-value: 1.98e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537   65 AIGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTER-NHTPRTLKMIEVAGI 143
Cdd:pfam00532   3 KLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPaPSGDDITAKAEGYGI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  144 PVVELMD-SVSPCLDIAVGFDNFDAARQMTAEIIARGH-RHVAYLGARLDERTIMKQ-KGYEQAMLDAGLTPYSV-MVEH 219
Cdd:pfam00532  83 PVIAADDaFDNPDGVPCVMPDDTQAGYESTQYLIAEGHkRPIAVMAGPASALTARERvQGFMAALAAAGREVKIYhVATG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  220 SSSFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLG-LRIPDD--------MAIAGFHGHDIGQVMEPQLASV 290
Cdd:pfam00532 163 DNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGrVKIPDIvgiginsvVGFDGLSKAQDTGLYLSPLTVI 242
                         250       260
                  ....*....|....*....|....*....
gi 495004537  291 LTPRERMGRIGAERLLARIRGESVTPQRL 319
Cdd:pfam00532 243 QLPRQLLGIKASDMVYQWIPKFREHPRVL 271
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
6-75 2.16e-24

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 94.19  E-value: 2.16e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537     6 PVLQDVADRVGVTKMTISRYLRNPEQVSLALRSKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTN 75
Cdd:smart00354   1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
 
Name Accession Description Interval E-value
PRK14987 PRK14987
HTH-type transcriptional regulator GntR;
1-331 0e+00

HTH-type transcriptional regulator GntR;


Pssm-ID: 184949 [Multi-domain]  Cd Length: 331  Bit Score: 648.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537   1 MKKRRPVLQDVADRVGVTKMTISRYLRNPEQVSLALRSKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAE 80
Cdd:PRK14987   1 MKKKRPVLQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  81 VLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPVVELMDSVSPCLDIAV 160
Cdd:PRK14987  81 VLRGIESVTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIEVAGIPVVELMDSQSPCLDIAV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 161 GFDNFDAARQMTAEIIARGHRHVAYLGARLDERTIMKQKGYEQAMLDAGLTPYSVMVEHSSSFSTGSELLRQARREYPQL 240
Cdd:PRK14987 161 GFDNFEAARQMTTAIIARGHRHIAYLGARLDERTIIKQKGYEQAMLDAGLVPYSVMVEQSSSYSSGIELIRQARREYPQL 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 241 DSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGAERLLARIRGESVTPQRLD 320
Cdd:PRK14987 241 DGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARIRGESVTPKMLD 320
                        330
                 ....*....|.
gi 495004537 321 LGFTLSPGGSI 331
Cdd:PRK14987 321 LGFTLSPGGSI 331
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
66-330 1.12e-125

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: 360.66  E-value: 1.12e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPV 145
Cdd:cd01575    2 VAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEHTPATRKLLRAAGIPV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 146 VELMDSVSPCLDIAVGFDNFDAARQMTAEIIARGHRHVAYLGARL--DERTIMKQKGYEQAMLDAGL-TPYSVMVEHSSS 222
Cdd:cd01575   82 VETWDLPDDPIDMAVGFSNFAAGRAMARHLIERGYRRIAFVGARLdgDSRARQRLEGFRDALAEAGLpLPLVLLVELPSS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 223 FSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGA 302
Cdd:cd01575  162 FALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRVPGDIAIAGFGDLDIAAALPPALTTVRVPRYEIGRKAA 241
                        250       260
                 ....*....|....*....|....*...
gi 495004537 303 ERLLARIRGESVTPQRLDLGFTLSPGGS 330
Cdd:cd01575  242 ELLLARLEGEEPEPRVVDLGFELVRRES 269
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
3-330 1.01e-105

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 312.52  E-value: 1.01e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537   3 KRRPVLQDVADRVGVTKMTISRYLRNPEQVSLALRSKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVL 82
Cdd:COG1609    1 RKRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  83 RGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPVVELMDSVSPCLDIAVGF 162
Cdd:COG1609   81 RGIEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRPLPDPGVPSVGV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 163 DNFDAARQMTAEIIARGHRHVAYLGARLD-ERTIMKQKGYEQAMLDAGLTPYSVMVEHSS-SFSTGSELLRQARREYPQL 240
Cdd:COG1609  161 DNRAGARLATEHLIELGHRRIAFIGGPADsSSARERLAGYREALAEAGLPPDPELVVEGDfSAESGYEAARRLLARGPRP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 241 DSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGAERLLARIRGESVTPQRLD 320
Cdd:COG1609  241 TAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERVL 320
                        330
                 ....*....|
gi 495004537 321 LGFTLSPGGS 330
Cdd:COG1609  321 LPPELVVRES 330
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
66-325 8.28e-72

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: 223.55  E-value: 8.28e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPV 145
Cdd:cd06267    2 IGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLAAGIPV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 146 VeLMDSVSPCLDI-AVGFDNFDAARQMTAEIIARGHRHVAYLGARLDERTIMK-QKGYEQAMLDAGLTPYSVMVEHS-SS 222
Cdd:cd06267   82 V-LIDRRLDGLGVdSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLSTSRErLEGYRDALAEAGLPVDPELVVEGdFS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 223 FSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGA 302
Cdd:cd06267  161 EESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVGFDDIPLAALLTPPLTTVRQPAYEMGRAAA 240
                        250       260
                 ....*....|....*....|...
gi 495004537 303 ERLLARIRGESVTPQRLDLGFTL 325
Cdd:cd06267  241 ELLLERIEGEEEPPRRIVLPTEL 263
PBP1_LacI-like cd06273
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
66-330 8.52e-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: 380497 [Multi-domain]  Cd Length: 268  Bit Score: 203.12  E-value: 8.52e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPV 145
Cdd:cd06273    2 IGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVGSDHDPELFELLEQRQVPY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 146 VeLMDSVSPCLDI-AVGFDNFDAARQMTAEIIARGHRHVAYLGARLD--ERTIMKQKGYEQAMLDAGLT-PYSVMVEHSS 221
Cdd:cd06273   82 V-LTWSYDEDSPHpSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAgnDRARARLAGIRDALAERGLElPEERVVEAPY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 222 SFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIG 301
Cdd:cd06273  161 SIEEGREALRRLLARPPRPTAIICGNDVLALGALAECRRLGISVPEDLSITGFDDLELAAHLSPPLTTVRVPAREIGELA 240
                        250       260
                 ....*....|....*....|....*....
gi 495004537 302 AERLLARIRGESVtPQRLDLGFTLSPGGS 330
Cdd:cd06273  241 ARYLLALLEGGPP-PKSVELETELIVRES 268
PBP1_LacI-like cd06282
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
65-330 9.08e-64

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


Pssm-ID: 380505 [Multi-domain]  Cd Length: 267  Bit Score: 202.90  E-value: 9.08e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  65 AIGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERN-HTPRTLKMIEVAGI 143
Cdd:cd06282    1 TIGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTVGDaQGSEALELLEEEGV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 144 PVV----ELMDSVSPCldiaVGFDNFDAARQMTAEIIARGHRHVAYLGARL--DERTIMKQKGYEQAMLDAGLTPYSVmV 217
Cdd:cd06282   81 PYVllfnQTENSSHPF----VSVDNRLASYDVAEYLIALGHRRIAMVAGDFsaSDRARLRYQGYRDALKEAGLKPIPI-V 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 218 EHSSSFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERM 297
Cdd:cd06282  156 EVDFPTNGLEEALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVIGFDGIAIGELLTPTLATVVQPSRDM 235
                        250       260       270
                 ....*....|....*....|....*....|...
gi 495004537 298 GRIGAERLLARIRGESVTPQRLdLGFTLSPGGS 330
Cdd:cd06282  236 GRAAADLLLAEIEGESPPTSIR-LPHHLREGGS 267
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
65-318 1.23e-54

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: 179.27  E-value: 1.23e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  65 AIGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEvAGIP 144
Cdd:cd06284    1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILLSGRLDAELLSELS-KRYP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 145 VVELMDSVSPClDIA-VGFDNFDAARQMTAEIIARGHRHVAYLGARLDER-TIMKQKGYEQAMLDAGLTPYSVMVEHSS- 221
Cdd:cd06284   80 IVQCCEYIPDS-GVPsVSIDNEAAAYDATEYLISLGHRRIAHINGPLDNVyARERLEGYRRALAEAGLPVDEDLIIEGDf 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 222 SFSTGSELLRQ--ARREYPqlDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGR 299
Cdd:cd06284  159 SFEAGYAAARAllALPERP--TAIFCASDELAIGAIKALRRAGLRVPEDVSVIGFDDIEFAEMFSPSLTTIRQPRYEIGE 236
                        250
                 ....*....|....*....
gi 495004537 300 IGAERLLARIRGESVTPQR 318
Cdd:cd06284  237 TAAELLLEKIEGEGVPPEH 255
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
65-316 3.36e-54

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


Pssm-ID: 380508 [Multi-domain]  Cd Length: 269  Bit Score: 178.19  E-value: 3.36e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  65 AIGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTE-RNHTPRTLKMIEvAGI 143
Cdd:cd06285    1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPaRDDAPDLQELAA-RGV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 144 PVVELMDSVSPCLDIAVGFDNFDAARQMTAEIIARGHRHVAYLGARLDERTIM-KQKGYEQAMLDAGLTPYSVMVEHS-S 221
Cdd:cd06285   80 PVVLVDRRIGDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPLNASTGRdRLRGYRRALAEAGLPVPDERIVPGgF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 222 SFSTGSELLRQ--ARREYPQldSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGR 299
Cdd:cd06285  160 TIEAGREAAYRllSRPERPT--AVFAANDLMAIGVLRAARDLGLRVPEDLSVVGFDDIPLAAFLPPPLTTVRQPKYEMGR 237
                        250
                 ....*....|....*..
gi 495004537 300 IGAERLLARIRGESVTP 316
Cdd:cd06285  238 RAAELLLQLIEGGGRPP 254
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
66-330 3.49e-54

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: 178.10  E-value: 3.49e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIevaGIPV 145
Cdd:cd06291    2 IGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILGSHSLDIEEYKKL---NIPI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 146 VeLMDSVSPCLDIAVGFDNFDAARQMTAEIIARGHRHVAYLGARLDERTIMK-QKGYEQAMLDAGLTPYSV-MVEHSSSF 223
Cdd:cd06291   79 V-SIDRYLSEGIPSVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSPANErYRGFEDALKEAGIEYEIIeIDENDFSE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 224 STGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGAE 303
Cdd:cd06291  158 EDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIGFDGIEISELLYPELTTIRQPIEEMAKEAVE 237
                        250       260
                 ....*....|....*....|....*..
gi 495004537 304 RLLARIRGESVTPQRLDLGFTLSPGGS 330
Cdd:cd06291  238 LLLKLIEGEEIEESRIVLPVELIERET 264
PBP1_CcpA-like cd19975
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
66-312 3.62e-53

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: 175.82  E-value: 3.62e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPV 145
Cdd:cd19975    2 IGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFASGTLTEENKQLLKNMNIPV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 146 V----ELMDSVSPCLDIavgfDNFDAARQMTAEIIARGHRHVAYLGARLDERTIMKQ--KGYEQAMLDAGLTPYS-VMVE 218
Cdd:cd19975   82 VlvstESEDPDIPSVKI----DDYQAAYDATNYLIKKGHRKIAMISGPLDDPNAGYPryEGYKKALKDAGLPIKEnLIVE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 219 HSSSFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMG 298
Cdd:cd19975  158 GDFSFKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPEDISVIGFDNTEIAEMSIPPLTTVSQPFYEMG 237
                        250
                 ....*....|....
gi 495004537 299 RIGAERLLARIRGE 312
Cdd:cd19975  238 KKAVELLLDLIKNE 251
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
66-319 2.03e-52

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: 173.52  E-value: 2.03e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRT-LKMIEVAGIP 144
Cdd:cd06289    2 VGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSPAAGTTAElLRRLKAWGIP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 145 VVELMDSVSPC-LDIaVGFDNFDAARQMTAEIIARGHRHVAYLGARLD-----ERtimkQKGYEQAMLDAGLTPYSVMVE 218
Cdd:cd06289   82 VVLALRDVPGSdLDY-VGIDNRLGAQLATEHLIALGHRRIAFLGGLSDsstrrER----LAGFRAALAEAGLPLDESLIV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 219 HS-SSFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFhgHDI--GQVMEPQLASVLTPRE 295
Cdd:cd06289  157 PGpATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGRDIAVVGF--DDVpeAALWTPPLTTVSVHPR 234
                        250       260
                 ....*....|....*....|....
gi 495004537 296 RMGRIGAERLLARIRGESVTPQRL 319
Cdd:cd06289  235 EIGRRAARLLLRRIEGPDTPPERI 258
PBP1_sucrose_transcription_regulator cd06288
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ...
65-330 6.61e-51

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: 169.65  E-value: 6.61e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  65 AIGVLLPSLTNQVFA-EVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLkMIEVAGI 143
Cdd:cd06288    1 TIGLITDDIATTPFAgDIIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYASMHHREVTL-PPELTDI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 144 PVVeLMDSVSPCLDI-AVGFDNFDAARQMTAEIIARGHRHVAYLGarLDER---TIMKQKGYEQAMLDAGLTPYSVMVEH 219
Cdd:cd06288   80 PLV-LLNCFDDDPSLpSVVPDDEQGGYLATRHLIEAGHRRIAFIG--GPEDslaTRLRLAGYRAALAEAGIPYDPSLVVH 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 220 -----SSSFSTGSELLRQARReypqLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPR 294
Cdd:cd06288  157 gdwgrESGYEAAKRLLSAPDR----PTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVVGFDNQELAAYLRPPLTTVALPY 232
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 495004537 295 ERMGRIGAERLLARIRGESVTPQRLDLGFTLSPGGS 330
Cdd:cd06288  233 YEMGRRAAELLLDGIEGEPPEPGVIRVPCPLIERES 268
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
66-321 9.90e-48

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: 161.66  E-value: 9.90e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPV 145
Cdd:cd06280    2 IGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGPSRELKRLLKHGIPI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 146 VeLMDSVSPCLDI-AVGFDNFDAARQMTAEIIARGHRHVAYLGARLDERTIMKQK-GYEQAMLDAGLTP-YSVMVEHSSS 222
Cdd:cd06280   82 V-LIDREVEGLELdLVAGDNREGAYKAVKHLIELGHRRIGLITGPLEISTTRERLaGYREALAEAGIPVdESLIFEGDST 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 223 FSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGA 302
Cdd:cd06280  161 IEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVGFDDSDWFEIVDPPLTVVAQPAYEIGRIAA 240
                        250
                 ....*....|....*....
gi 495004537 303 ERLLARIRGESVTPQRLDL 321
Cdd:cd06280  241 QLLLERIEGQGEEPRRIVL 259
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
66-321 2.74e-47

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


Pssm-ID: 380516 [Multi-domain]  Cd Length: 270  Bit Score: 160.52  E-value: 2.74e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPV 145
Cdd:cd06293    2 IGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSHLARLRARGTAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 146 VeLMDSVSPCLDIA-VGFDNFDAARQMTAEIIARGHRHVAYLGARLDERTIM-KQKGYEQAMLDAGLTPYSVMVEHSSsF 223
Cdd:cd06293   82 V-LLDRPAPGPAGCsVSVDDVQGGALAVDHLLELGHRRIAFVSGPLRTRQVAeRLAGARAAVAEAGLDPDEVVRELSA-P 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 224 STGSELLRQARRE----YPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGR 299
Cdd:cd06293  160 DANAELGRAAAAQllamPPRPTAVFAANDLLALGLLAGLRRAGLRVPDDVSVVGYDDLPFAAAANPPLTTVRQPSYELGR 239
                        250       260
                 ....*....|....*....|..
gi 495004537 300 IGAERLLARIRGESVTPQRLDL 321
Cdd:cd06293  240 AAADLLLDEIEGPGHPHEHVVF 261
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
66-326 1.47e-46

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: 158.04  E-value: 1.47e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPV 145
Cdd:cd01542    2 IGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEITDEHRKALKKLKIPV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 146 VEL---MDSVSpcldiAVGFDNFDAARQMTAEIIARGHRHVAYLGARLDERTIMKQ--KGYEQAMLDAGLTPYSvMVEHS 220
Cdd:cd01542   82 VVLgqeHEGFS-----CVYHDDYGAGKLLGEYLLKKGHKNIAYIGVDEEDIAVGVArkQGYLDALKEHGIDEVE-IVETD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 221 SSFSTGSELLRQARREYPqLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRI 300
Cdd:cd01542  156 FSMESGYEAAKELLKENK-PDAIICATDNIALGAIKALRELGIKIPEDISVAGFGGYDLSEFVSPSLTTVKFDYEEAGEK 234
                        250       260
                 ....*....|....*....|....*.
gi 495004537 301 GAERLLARIRGESVtPQRLDLGFTLS 326
Cdd:cd01542  235 AAELLLDMIEGEKV-PKKQKLPYELI 259
PBP1_LacI-like cd06299
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ...
66-320 5.23e-45

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: 154.36  E-value: 5.23e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLIL--TERNHtPRTLKMIEvAGI 143
Cdd:cd06299    2 IGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNSDEDPEREDESLEMLLSQRVDGIIAvpTGENS-EGLQALIA-QGL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 144 PVVELMDSVSPCLDI-AVGFDNFDAARQMTAEIIARGHRHVAYLGARLDERTIM-KQKGYEQAMLDAGLTPYSVMVE--- 218
Cdd:cd06299   80 PVVFVDREVEGLGGVpVVTSDNRPGAREAVEYLVSLGHRRIGYISGPLSTSTGReRLAAFRAALTAAGIPIDEELVAfgd 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 219 --HSSSFSTGSELLRQARReypqLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRER 296
Cdd:cd06299  160 frQDSGAAAAHRLLSRGDP----PTALIAGDSLMALGAIQALRELGLRIGDDVSLISFDDVPWFELLSPPLTVIAQPVER 235
                        250       260
                 ....*....|....*....|....*
gi 495004537 297 MGRIGAERLLARI-RGESVTPQRLD 320
Cdd:cd06299  236 IGRRAVELLLALIeNGGRATSIRVP 260
PBP1_DegA_Like cd19976
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
66-319 1.63e-44

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: 153.17  E-value: 1.63e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTL-KMIEVAGIP 144
Cdd:cd19976    2 IGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNISDEAIiKLLKEEKIP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 145 VVeLMDSVSPCLDIA-VGFDNFDAARQMTAEIIARGHRHVAYL-----GARLDERTimkqKGYEQAMLDAGLTPYSVMVE 218
Cdd:cd19976   82 VV-VLDRYIEDNDSDsVGVDDYRGGYEATKYLIELGHTRIGCIvgppsTYNEHERI----EGYKNALQDHNLPIDESWIY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 219 -HSSSFSTG----SELLRQArreypQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTP 293
Cdd:cd19976  157 sGESSLEGGykaaEELLKSK-----NPTAIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYITPALTTIAQP 231
                        250       260
                 ....*....|....*....|....*.
gi 495004537 294 RERMGRIGAERLLARIRGESVTPQRL 319
Cdd:cd19976  232 IFEMGQEAAKLLLKIIKNPAKKKEEI 257
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
66-313 2.27e-44

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: 153.10  E-value: 2.27e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLI-------LTERNHtpRTLKMI 138
Cdd:cd01541    2 IGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIieptksaLPNPNL--DLYEEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 139 EVAGIPVVeLMDSVSPCLDI-AVGFDNFDAARQMTAEIIARGHRHVAYLGARLDERTIMKQKGYEQAMLDAGLTPYSvmv 217
Cdd:cd01541   80 QKKGIPVV-FINSYYPELDApSVSLDDEKGGYLATKHLIDLGHRRIAGIFKSDDLQGVERYQGFIKALREAGLPIDD--- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 218 EHSSSFSTGSELLRQARREYPQL-------DSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASV 290
Cdd:cd01541  156 DRILWYSTEDLEDRFFAEELREFlrrlsrcTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDDSYLASLSEPPLTSV 235
                        250       260
                 ....*....|....*....|...
gi 495004537 291 LTPRERMGRIGAERLLARIRGES 313
Cdd:cd01541  236 VHPKEELGRKAAELLLRMIEEGR 258
PBP1_GalS-like cd06270
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ...
66-318 2.35e-44

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: 152.67  E-value: 2.35e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPV 145
Cdd:cd06270    2 IGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEELILIAEKIPPL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 146 VELMDSVSPCLDIAVGFDNFDAARQMTAEIIARGHRHVAYLGARLDERT-IMKQKGYEQAMLDAGLTP-YSVMVEHSSSF 223
Cdd:cd06270   82 VVINRYIPGLADRCVWLDNEQGGRLAAEHLLDLGHRRIACITGPLDIPDaRERLAGYRDALAEAGIPLdPSLIIEGDFTI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 224 STGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGAE 303
Cdd:cd06270  162 EGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVPEDVSVIGFDDVPLARYLSPKLTTVHYPIEEMAQAAAE 241
                        250
                 ....*....|....*
gi 495004537 304 RLLARIRGESVTPQR 318
Cdd:cd06270  242 LALNLAYGEPLPISH 256
PRK10014 PRK10014
DNA-binding transcriptional repressor MalI; Provisional
1-322 1.26e-43

DNA-binding transcriptional repressor MalI; Provisional


Pssm-ID: 182193 [Multi-domain]  Cd Length: 342  Bit Score: 152.94  E-value: 1.26e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537   1 MKKRRPVLQDVADRVGVTKMTISRYLRNPEQVSLALRSKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAE 80
Cdd:PRK10014   2 ATAKKITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  81 VLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILT-ERNHTPRTLKMIEVAGIPVV--------ELMDS 151
Cdd:PRK10014  82 LTAGLTEALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAgAAGSSDDLREMAEEKGIPVVfasrasylDDVDT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 152 VSPcldiavgfDNFDAARQMTAEIIARGHRHVAYLGARLDERTIMKQ-KGYEQAMLDAGLTPYSV-MVEHSSSFSTGSEL 229
Cdd:PRK10014 162 VRP--------DNMQAAQLLTEHLIRNGHQRIAWLGGQSSSLTRAERvGGYCATLLKFGLPFHSEwVLECTSSQKQAAEA 233
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 230 LRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDD---------MAIAGFHGHDIGQVMEPQLASVLTPRERMGRI 300
Cdd:PRK10014 234 ITALLRHNPTISAVVCYNETIAMGAWFGLLRAGRQSGESgvdryfeqqVALAAFTDVPEAELDDPPLTWASTPAREIGRT 313
                        330       340
                 ....*....|....*....|..
gi 495004537 301 GAERLLARIRGESVTPQRLDLG 322
Cdd:PRK10014 314 LADRMMQRITHEETHSRNLIIP 335
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
66-316 1.44e-43

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: 150.76  E-value: 1.44e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPV 145
Cdd:cd19977    2 IGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNEDLIEKLVKSGIPV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 146 VeLMDSVSPCLDI-AVGFDNFDAARQMTAEIIARGHRHVAYLGARLdERTIMKQK--GYEQAMLDAGLTPYSVMVEHSSS 222
Cdd:cd19977   82 V-FVDRYIPGLDVdTVVVDNFKGAYQATEHLIELGHKRIAFITYPL-ELSTRQERleGYKAALADHGLPVDEELIKHVDR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 223 FSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGA 302
Cdd:cd19977  160 QDDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALIGFDDIPWADLFNPPLTVIAQPTYEIGRKAA 239
                        250
                 ....*....|....
gi 495004537 303 ERLLARIRGESVTP 316
Cdd:cd19977  240 ELLLDRIENKPKGP 253
PBP1_LacI-like cd06290
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
65-325 5.39e-43

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: 149.30  E-value: 5.39e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  65 AIGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEvAGIP 144
Cdd:cd06290    1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEELLKLLA-EGIP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 145 VVeLMDSVSPCLDI-AVGFDNFDAARQMTAEIIARGHRHVAYLGARLDER-TIMKQKGYEQAMLDAGLTPYSVMVEHSS- 221
Cdd:cd06290   80 VV-LVDRELEGLNLpVVNVDNEQGGYNATNHLIDLGHRRIVHISGPEDHPdAQERYAGYRRALEDAGLEVDPRLIVEGDf 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 222 SFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIG 301
Cdd:cd06290  159 TEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVSVIGFDDLPFSKYTTPPLTTVRQPLYEMGKTA 238
                        250       260
                 ....*....|....*....|....
gi 495004537 302 AERLLARIRGESVTPQRLDLGFTL 325
Cdd:cd06290  239 AEILLELIEGKGRPPRRIILPTEL 262
PBP1_PurR cd06275
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ...
66-321 7.19e-43

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: 148.94  E-value: 7.19e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEV-AGIP 144
Cdd:cd06275    2 IGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAELLAAlRSIP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 145 VVeLMDSVSPCLDI-AVGFDNFDAARQMTAEIIARGHRHVAYLGARLDERTIMKQ-KGYEQAMLDAGLT-PYSVMVEHSS 221
Cdd:cd06275   82 VV-VLDREIAGDNAdAVLDDSFQGGYLATRHLIELGHRRIGCITGPLEHSVSRERlAGFRRALAEAGIEvPPSWIVEGDF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 222 SFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIG 301
Cdd:cd06275  161 EPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIGYDDIELARYFSPALTTIHQPKDELGELA 240
                        250       260
                 ....*....|....*....|
gi 495004537 302 AERLLARIRGESVTPQRLDL 321
Cdd:cd06275  241 VELLLDRIENKREEPQSIVL 260
PRK10423 PRK10423
transcriptional repressor RbsR; Provisional
8-331 7.47e-40

transcriptional repressor RbsR; Provisional


Pssm-ID: 182448 [Multi-domain]  Cd Length: 327  Bit Score: 142.53  E-value: 7.47e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537   8 LQDVADRVGVTKMTISRYLRNPEQVSLALRSKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGIES 87
Cdd:PRK10423   1 MKDVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRGVER 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  88 VIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLIL--TErNHTPRTLKMIEVAGIPVVeLMDSvSPcLDIA--VGFD 163
Cdd:PRK10423  81 SCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLlcTE-THQPSREIMQRYPSVPTV-MMDW-AP-FDGDsdLIQD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 164 NFDAARQM-TAEIIARGHRHVAYLGARLDERTI-MKQKGYEQAMLDAGLT-PYSVMVEHSSSFSTGSELLRQ--ARREYP 238
Cdd:PRK10423 157 NSLLGGDLaTQYLIDKGYTRIACITGPLDKTPArLRLEGYRAAMKRAGLNiPDGYEVTGDFEFNGGFDAMQQllALPLRP 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 239 QldSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGAERLLARIRGESVTPQR 318
Cdd:PRK10423 237 Q--AVFTGNDAMAVGVYQALYQAGLSVPQDIAVIGYDDIELARYMTPPLTTIHQPKDELGELAIDVLIHRMAQPTLQQQR 314
                        330
                 ....*....|...
gi 495004537 319 LDLGFTLSPGGSI 331
Cdd:PRK10423 315 LQLTPELMERGSV 327
PBP1_SalR cd01545
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ...
66-330 1.78e-39

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: 140.00  E-value: 1.78e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLS-WNIDGLILTER-NHTPRTLKMIEVAGI 143
Cdd:cd01545    2 IGLLYDNPSASYVSALQVGALRACREAGYHLVVEPCDSDDEDLADRLRRFLSrSRPDGVILTPPlSDDPALLDALDELGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 144 PVVelmdSVSPCLD----IAVGFDNFDAARQMTAEIIARGHRHVAYLGARLDER-TIMKQKGYEQAMLDAGLTPYSVMVE 218
Cdd:cd01545   82 PYV----RIAPGTDddrsPSVRIDDRAAAREMTRHLIALGHRRIGFIAGPPDHGaSAERLEGFRDALAEAGLPLDPDLVV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 219 H-----SSSFSTGSELLRQARReyPqlDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTP 293
Cdd:cd01545  158 QgdftfESGLEAAEALLDLPDR--P--TAIFASNDEMAAGVLAAAHRLGLRVPDDLSVAGFDDSPIARLVWPPLTTVRQP 233
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 495004537 294 RERMGRIGAERLLARIRGESVTPQRLDLGFTLSPGGS 330
Cdd:cd01545  234 IAEMARRAVELLIAAIRGAPAGPERETLPHELVIRES 270
PBP1_LacI-like cd19974
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
66-311 9.67e-39

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: 138.07  E-value: 9.67e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPS---LTNQVFAEVLRGIESVIDAHGYQTMLahYGYKPELEQE-RLESMLS-WNIDGLILTErnHTPRT-LKMIE 139
Cdd:cd19974    2 IAVLIPErffGDNSFYGKIYQGIEKELSELGYNLVL--EIISDEDEEElNLPSIISeEKVDGIIILG--EISKEyLEKLK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 140 VAGIPVVeLMDSVSPCLDI-AVGFDNFDAARQMTAEIIARGHRHVAYLGARLDERTIM-KQKGYEQAMLDAGLTP---YS 214
Cdd:cd19974   78 ELGIPVV-LVDHYDEELNAdSVLSDNYYGAYKLTSYLIEKGHKKIGFVGDINYTSSFMdRYLGYRKALLEAGLPPekeEW 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 215 VMVEHSSSFSTGSELLRQARREYPqlDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPR 294
Cdd:cd19974  157 LLEDRDDGYGLTEEIELPLKLMLP--TAFVCANDSIAIQLIKALKEKGYRVPEDISVVGFDNIELAELSTPPLTTVEVDK 234
                        250
                 ....*....|....*..
gi 495004537 295 ERMGRIGAERLLARIRG 311
Cdd:cd19974  235 EAMGRRAVEQLLWRIEN 251
PBP1_RegR_EndR_KdgR-like cd06283
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ...
66-321 5.15e-38

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: 136.14  E-value: 5.15e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPV 145
Cdd:cd06283    2 IGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPTGNNNDAYLELAQKGLPV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 146 VeLMD-SVSPC-LDIaVGFDNFDAARQMTAEIIARGHRHVAYLGARLDE-RT-IMKQKGYEQAMLDAGLTPYSVMVEHSS 221
Cdd:cd06283   82 V-LVDrQIEPLnWDT-VVTDNYDATYEATEHLKEQGYERIVFVTEPIKGiSTrRERLQGFLDALARYNIEGDVYVIEIED 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 222 SFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIG 301
Cdd:cd06283  160 TEDLQQALAAFLSQHDGGKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCGFDDWDWADLIGPGITTIRQPTYEIGKAA 239
                        250       260
                 ....*....|....*....|
gi 495004537 302 AERLLARIRGESVTPQRLDL 321
Cdd:cd06283  240 AEILLERIEGDSGEPKEIEL 259
PBP1_CcpB-like cd06286
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ...
66-323 1.81e-37

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: 134.60  E-value: 1.81e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGiPV 145
Cdd:cd06286    2 IGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLIITSRENDWEVIEPYAKYG-PI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 146 VELMDSVSPCLDiAVGFDNFDAARQMTAEIIARGHRHVAYLGARLDER---TIMKQKGYEQAMLDAGLTPYSVMV-EHSS 221
Cdd:cd06286   81 VLCEETDSPDIP-SVYIDRYEAYLEALEYLKEKGHRKIGYCLGRPESSsasTQARLKAYQDVLGEHGLSLREEWIfTNCH 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 222 SFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMepQLASVLTPRERMGRIG 301
Cdd:cd06286  160 TIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRVPEDLAVIGFDNQPISELL--NLTTIDQPLEEMGKEA 237
                        250       260
                 ....*....|....*....|..
gi 495004537 302 AERLLARIRGESVTPQRLDLGF 323
Cdd:cd06286  238 FELLLSQLESKEPTKKELPSKL 259
PBP1_MalR-like cd06294
ligand-binding domain of maltose transcription regulator MalR which is a member of the ...
65-318 4.29e-37

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: 133.86  E-value: 4.29e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  65 AIGVLLPSLT-----NQVFAEVLRGIESVIDAHGYQTMLAhYGykpELEQERLESMLSW----NIDGLILTERNHTPRTL 135
Cdd:cd06294    1 TIGLVLPSSAeelfqNPFFSEVLRGISQVANENGYSLLLA-TG---NTEEELLEEVKRMvrgrRVDGFILLYSKEDDPLI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 136 KMIEVAGIPVVELMDSVSPCLDIAVGFDNFDAARQMTAEIIARGHRHVAYLGARLDER-TIMKQKGYEQAMLDAGLT-PY 213
Cdd:cd06294   77 EYLKEEGFPFVVIGKPLDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVvSIDRLQGYKQALKEAGLPlDD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 214 SVMVEHSSSFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTP 293
Cdd:cd06294  157 DYILLLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFNNSPLAELASPPLTSVDIN 236
                        250       260
                 ....*....|....*....|....*
gi 495004537 294 RERMGRIGAERLLARIRGESVTPQR 318
Cdd:cd06294  237 PYELGREAAKLLINLLEGPESLPKN 261
lacI PRK09526
lac repressor; Reviewed
1-319 8.27e-37

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 135.12  E-value: 8.27e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537   1 MKKRRPVLQDVADRVGVTKMTISRYLRNPEQVSLALRSKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAE 80
Cdd:PRK09526   1 MKSKPVTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTSLALHAPSQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  81 VLRGIESVIDAHGYQT---MLAHygykPELE--QERLESMLSWNIDGLILTERNHTPRTLKMIEVAG-IPVVeLMDsVSP 154
Cdd:PRK09526  81 IAAAIKSRADQLGYSVvisMVER----SGVEacQAAVNELLAQRVSGVIINVPLEDADAEKIVADCAdVPCL-FLD-VSP 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 155 CLDI-AVGFDNFDAARQMTAEIIARGHRHVAYLG-------ARLdertimKQKGYEQAMLDAGLTPYSVMvEHSSSFSTG 226
Cdd:PRK09526 155 QSPVnSVSFDPEDGTRLGVEHLVELGHQRIALLAgpessvsARL------RLAGWLEYLTDYQLQPIAVR-EGDWSAMSG 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 227 SELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGAERLL 306
Cdd:PRK09526 228 YQQTLQMLREGPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRLL 307
                        330
                 ....*....|...
gi 495004537 307 ARIRGESVTPQRL 319
Cdd:PRK09526 308 ALSQGQAVKGSQL 320
PBP1_LacI cd01574
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ...
66-321 8.75e-37

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: 132.71  E-value: 8.75e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHY-GYKPELEQERLESMLSWNIDGLILTE-RNHTPRTLKMIEvAGI 143
Cdd:cd01574    2 IGVIATGLSLYGPASTLAGIERAARERGYSVSIATVdEDDPASVREALDRLLSQRVDGIIVIApDEAVLEALRRLP-PGL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 144 PVVeLMDSVSPCLDIAVGFDNFDAARQMTAEIIARGHRHVAYLGARLDER-TIMKQKGYEQAMLDAGLTPYSVMV---EH 219
Cdd:cd01574   81 PVV-IVGSGPSPGVPTVSIDQEEGARLATRHLLELGHRRIAHIAGPLDWVdARARLRGWREALEEAGLPPPPVVEgdwSA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 220 SSSFSTGSELLRQarreyPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGR 299
Cdd:cd01574  160 ASGYRAGRRLLDD-----GPVTAVFAANDQMALGALRALHERGLRVPEDVSVVGFDDIPEAAYFVPPLTTVRQDFAELGR 234
                        250       260
                 ....*....|....*....|..
gi 495004537 300 IGAERLLARIRGESVTPQRLDL 321
Cdd:cd01574  235 RAVELLLALIEGPAPPPESVLL 256
PBP1_CcpA cd06298
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ...
66-330 1.30e-36

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: 132.41  E-value: 1.30e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPV 145
Cdd:cd06298    2 VGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMGDELTEEIREEFKRSPVPV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 146 VeLMDSVSPCLDI-AVGFDNFDAARQMTAEIIARGHRHVAYLGARLDERTI--MKQKGYEQAMLDAGL---TPYsvMVEH 219
Cdd:cd06298   82 V-LAGTVDSDHEIpSVNIDYEQAAYDATKSLIDKGHKKIAFVSGPLKEYINndKKLQGYKRALEEAGLefnEPL--IFEG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 220 SSSFSTGSELL-RQARREYPqlDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMG 298
Cdd:cd06298  159 DYDYDSGYELYeELLESGEP--DAAIVVRDEIAVGLLNAAQDRGLKVPEDLEIIGFDNTRYATMSRPQLTSINQPLYDIG 236
                        250       260       270
                 ....*....|....*....|....*....|...
gi 495004537 299 RIgAERLLARI-RGESVTPQRLDLGFTLSPGGS 330
Cdd:cd06298  237 AV-AMRLLTKLmNKEEVEETIVKLPHSIIWRQS 268
PBP1_LacI-like cd06279
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ...
65-320 1.33e-36

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: 133.10  E-value: 1.33e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  65 AIGVLLP-----SLTNQVFAEVLRGIESVIDAHGYQTMLAHygykPELEQERLESMLSWNIDGLILterNHTPRTLKMIE 139
Cdd:cd06279    1 AIGVLLPddlsyAFSDPVAAQFLRGVAEVCEEEGLGLLLLP----ATDEGSAAAAVRNAAVDGFIV---YGLSDDDPAVA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 140 VA---GIPVVeLMDSVSPCLDIAVGFDNFDAARQMTAEIIARGHRHVAYLGARLDE----------------RTIMKQ-- 198
Cdd:cd06279   74 ALrrrGLPLV-VVDGPAPPGIPSVGIDDRAAARAAARHLLDLGHRRIAILSLRLDRgrergpvsaerlaaatNSVARErl 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 199 KGYEQAMLDAGLTPYSVMVEHS--SSFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHG 276
Cdd:cd06279  153 AGYRDALEEAGLDLDDVPVVEApgNTEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRVPEDLSVTGFDD 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 495004537 277 HDIGQVMEPQLASVLTPRERMGRIGAERLLARIRGESVTPQRLD 320
Cdd:cd06279  233 IPEAAAADPGLTTVRQPAVEKGRAAARLLLGLLPGAPPRPVILP 276
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
66-319 5.84e-35

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


Pssm-ID: 380501 [Multi-domain]  Cd Length: 266  Bit Score: 128.04  E-value: 5.84e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEqERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPV 145
Cdd:cd06278    2 VGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDDVD-DALRQLLQYRVDGVIVTSATLSSELAEECARRGIPV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 146 VeLMDSVSPCLDI-AVGFDNFDAARQMTAEIIARGHRHVAYLGARLDERT-IMKQKGYEQAMLDAGLTPYSVMVEHSS-- 221
Cdd:cd06278   81 V-LFNRVVEDPGVdSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPEGTSTsRERERGFRAALAELGLPPPAVEAGDYSye 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 222 -SFSTGSELLRQARReypqLDSIFCTNDDLAIGA--AFEcQRLGLRIPDDMAIAGFhgHDIGQVMEP--QLASVLTPRER 296
Cdd:cd06278  160 gGYEAARRLLAAPDR----PDAIFCANDLMALGAldAAR-QEGGLVVPEDISVVGF--DDIPMAAWPsyDLTTVRQPIEE 232
                        250       260
                 ....*....|....*....|...
gi 495004537 297 MGRIGAERLLARIRGESVTPQRL 319
Cdd:cd06278  233 MAEAAVDLLLERIENPETPPERR 255
PRK11041 PRK11041
DNA-binding transcriptional regulator CytR; Provisional
29-314 7.87e-35

DNA-binding transcriptional regulator CytR; Provisional


Pssm-ID: 182923 [Multi-domain]  Cd Length: 309  Bit Score: 128.96  E-value: 7.87e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  29 PEQVSLALRSKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELE 108
Cdd:PRK11041   1 PEKVSQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIVPDICDPFFSEIIRGIEVTAAEHGYLVLIGDCAHQNQQE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 109 QERLESMLSWNIDGLILTERNHtPRTLKMIEVAGIPVVELMDSVSPCLDI-AVGFDNFDAARQMTAEIIARGHRHVAYLg 187
Cdd:PRK11041  81 KTFVNLIITKQIDGMLLLGSRL-PFDASKEEQRNLPPMVMANEFAPELELpTVHIDNLTAAFEAVNYLHELGHKRIACI- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 188 ARLDERTI--MKQKGYEQAMLDAGLTPYSVMVEHSS-SFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLR 264
Cdd:PRK11041 159 AGPEEMPLchYRLQGYVQALRRCGITVDPQYIARGDfTFEAGAKALKQLLDLPQPPTAVFCHSDVMALGALSQAKRMGLR 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 495004537 265 IPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGAERLLARIRGESV 314
Cdd:PRK11041 239 VPQDLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQGHHV 288
PBP1_LacI-like cd06281
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
65-330 1.71e-33

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: 124.27  E-value: 1.71e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  65 AIGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHT-PRTLKMIEVAGI 143
Cdd:cd06281    1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILTPGDEDdPELAAALARLDI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 144 PVVeLMDSVSPCLDIAVGFDNFDAARQMTAEIIARGHRHVAYLGARLDERTIMKQ-KGYEQAMLDAGLTPYSVMVEH--- 219
Cdd:cd06281   81 PVV-LIDRDLPGDIDSVLVDHRSGVRQATEYLLSLGHRRIALLTGGPDIRPGRERiAGFKAAFAAAGLPPDPDLVRLgsf 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 220 --SSSFSTGSELLRQARReyPQldSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERM 297
Cdd:cd06281  160 saDSGFREAMALLRQPRP--PT--AIIALGTQLLAGVLRAVRAAGLRIPGDLSVVSIGDSDLAELHDPPITAIRWDLDAV 235
                        250       260       270
                 ....*....|....*....|....*....|....
gi 495004537 298 GRIGAERLLARIRGESVT-PQRLDLGFTLSPGGS 330
Cdd:cd06281  236 GRAAAELLLDRIEGPPAGpPRRIVVPTELILRDS 269
PBP1_AglR_RafR-like cd06292
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ...
65-317 5.05e-33

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: 123.15  E-value: 5.05e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  65 AIGVLLPSL----TNQVFAEVLRGIESVIDAHGYQTMLAhYGYKPELEQERLESML-SWNIDGLILTERNHT-PRTLKMI 138
Cdd:cd06292    1 LIGYVVPELpggfSDPFFDEFLAALGHAAAARGYDVLLF-TASGDEDEIDYYRDLVrSRRVDGFVLASTRHDdPRVRYLH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 139 EvAGIPVVEL----MDSVSPCLDIavgfDNFDAARQMTAEIIARGHRHVAYLGARLDERTIM-KQKGYEQAMLDAGLTPY 213
Cdd:cd06292   80 E-AGVPFVAFgranPDLDFPWVDV----DGAAGMRQAVRHLIALGHRRIGLIGGPEGSVPSDdRLAGYRAALEEAGLPFD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 214 SVMVEHSS-SFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLT 292
Cdd:cd06292  155 PGLVVEGEnTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVSVVGFDDSPLAAFTHPPLTTVRQ 234
                        250       260
                 ....*....|....*....|....*
gi 495004537 293 PRERMGRIGAERLLARIRGESVTPQ 317
Cdd:cd06292  235 PIDEIGRAVVDLLLAAIEGNPSEPR 259
PRK10703 PRK10703
HTH-type transcriptional repressor PurR;
8-321 3.95e-32

HTH-type transcriptional repressor PurR;


Pssm-ID: 236739 [Multi-domain]  Cd Length: 341  Bit Score: 122.53  E-value: 3.95e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537   8 LQDVADRVGVTKMTISRYLRNPEQVSLALRSKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGIES 87
Cdd:PRK10703   4 IKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEAVEK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  88 VIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEV-AGIPVVeLMD---SVSPCLDIAVgfD 163
Cdd:PRK10703  84 NCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLLAMLEEyRHIPMV-VMDwgeAKADFTDAII--D 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 164 N-FDAARQMTAEIIARGHRHVAYLGARLdERTIMKQK--GYEQAMLDAGLTPYSVMV-----EHSSSFSTGSELLRQARR 235
Cdd:PRK10703 161 NaFEGGYLAGRYLIERGHRDIGVIPGPL-ERNTGAGRlaGFMKAMEEANIKVPEEWIvqgdfEPESGYEAMQQILSQKHR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 236 eyPQldSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGAERLLARIRGESVT 315
Cdd:PRK10703 240 --PT--AVFCGGDIMAMGAICAADEMGLRVPQDISVIGYDNVRNARYFTPALTTIHQPKDRLGETAFNMLLDRIVNKREE 315

                 ....*.
gi 495004537 316 PQRLDL 321
Cdd:PRK10703 316 PQTIEV 321
PBP1_LacI-like cd06277
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
78-325 1.28e-31

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: 119.65  E-value: 1.28e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  78 FAEVLRGIESVIDAHGYQTMLAHYGYKPELEqERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPVVeLMDSVSPCLD 157
Cdd:cd06277   21 FSELIDGIEREARKYGYNLLISSVDIGDDFD-EILKELTDDQSSGIILLGTELEEKQIKLFQDVSIPVV-VVDNYFEDLN 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 158 I-AVGFDNFDAARQMTAEIIARGHRHVAYLGARLDERTI-MKQKGYEQAMLDAGLtpySVMVEHSSSFSTGSELLRQ--- 232
Cdd:cd06277   99 FdCVVIDNEDGAYEAVKYLVELGHTRIGYLASSYRIKNFeERRRGFRKAMRELGL---SEDPEPEFVVSVGPEGAYKdmk 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 233 ----ARREYPQldSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGAERLLAR 308
Cdd:cd06277  176 alldTGPKLPT--AFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQMGKLAVRRLIEK 253
                        250
                 ....*....|....*..
gi 495004537 309 IRGESVTPQRLDLGFTL 325
Cdd:cd06277  254 IKDPDGGTLKILVSTKL 270
PBP1_CatR-like cd06296
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ...
66-330 1.31e-31

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: 119.30  E-value: 1.31e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPV 145
Cdd:cd06296    2 IDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQLRLLRSAGIPF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 146 VeLMD--SVSPCLDIAVGFDNFDAARQMTAEIIARGHRHVAYLGARLDER-TIMKQKGYEQAMLDAGLTPYSVMVEHS-- 220
Cdd:cd06296   82 V-LIDpvGEPDPDLPSVGATNWAGGRLATEHLLDLGHRRIAVITGPPRSVsGRARLAGYRAALAEAGIAVDPDLVREGdf 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 221 ---SSFSTGSELLRQARReyPQldSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERM 297
Cdd:cd06296  161 tyeAGYRAARELLELPDP--PT--AVFAGNDEQALGVYRAARALGLRVPDDLSVIGFDDTPPARWTSPPLTTVHQPLREM 236
                        250       260       270
                 ....*....|....*....|....*....|...
gi 495004537 298 GRIGAERLLARIRGESVTPQRLDLGFTLSPGGS 330
Cdd:cd06296  237 GAVAVRLLLRLLEGGPPDARRIELATELVVRGS 269
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
65-319 1.98e-30

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


Pssm-ID: 395423 [Multi-domain]  Cd Length: 281  Bit Score: 116.46  E-value: 1.98e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537   65 AIGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTER-NHTPRTLKMIEVAGI 143
Cdd:pfam00532   3 KLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIITTPaPSGDDITAKAEGYGI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  144 PVVELMD-SVSPCLDIAVGFDNFDAARQMTAEIIARGH-RHVAYLGARLDERTIMKQ-KGYEQAMLDAGLTPYSV-MVEH 219
Cdd:pfam00532  83 PVIAADDaFDNPDGVPCVMPDDTQAGYESTQYLIAEGHkRPIAVMAGPASALTARERvQGFMAALAAAGREVKIYhVATG 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  220 SSSFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLG-LRIPDD--------MAIAGFHGHDIGQVMEPQLASV 290
Cdd:pfam00532 163 DNDIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGrVKIPDIvgiginsvVGFDGLSKAQDTGLYLSPLTVI 242
                         250       260
                  ....*....|....*....|....*....
gi 495004537  291 LTPRERMGRIGAERLLARIRGESVTPQRL 319
Cdd:pfam00532 243 QLPRQLLGIKASDMVYQWIPKFREHPRVL 271
PBP1_CcpA_TTHA0807 cd06297
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ...
66-319 4.39e-30

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: 115.26  E-value: 4.39e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYqtmlaHYGYKPELEQERLE-----SMLSWNIDGLILTERNHTPRTLKMIEV 140
Cdd:cd06297    2 ISLLVPEVMTPFYMRLLTGVERALDENRY-----DLAIFPLLSEYRLEkylrnSTLAYQCDGLVMASLDLTELFEEVIVP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 141 AGIPVVeLMDSVSPCLDiAVGFDNFDAARQMTAEIIARGHRHVAYLGARLDE---RTIMKQ--KGYEQAMLDAGLtPYSV 215
Cdd:cd06297   77 TEKPVV-LIDANSMGYD-CVYVDNVKGGFMATEYLAGLGEREYVFFGIEEDTvftETVFREreQGFLEALNKAGR-PISS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 216 MVEHSSSFST--GSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQvmEPQLASVLTP 293
Cdd:cd06297  154 SRMFRIDNSSkkAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRVGEDVAVIGFDGQPWAA--SPGLTTVRQP 231
                        250       260
                 ....*....|....*....|....*.
gi 495004537 294 RERMGRIGAERLLARIRGESVTPQRL 319
Cdd:cd06297  232 VEEMGEAAAKLLLKRLNEYGGPPRSL 257
PBP1_GalR cd01544
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ...
78-325 1.35e-29

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: 113.77  E-value: 1.35e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  78 FAEVLRGIESVIDAHGYQTMLaHYGYKPELEQerlesmLSWNIDGLILTERnHTPRTLKMIEVAGIPVVeLMDSVSPCLD 157
Cdd:cd01544   19 YLSIRLGIEKEAKKLGYEIKT-IFRDDEDLES------LLEKVDGIIAIGK-FSKEEIEKLKKLNPNIV-FVDSNPDPDG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 158 I-AVGFDNFDAARQMTAEIIARGHRHVAYLGAR----------LDERTimkqKGYEQAMLDAGLTPYSVMVEHSSSFSTG 226
Cdd:cd01544   90 FdSVVPDFEQAVRQALDYLIELGHRRIGFIGGKeytsddgeeiEDPRL----RAFREYMKEKGLYNEEYIYIGEFSVESG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 227 SELLRQARREYPQLDSIFCTNDDLAIGA--AFecQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGAER 304
Cdd:cd01544  166 YEAMKELLKEGDLPTAFFVASDPMAIGAlrAL--QEAGIKVPEDISIISFNDIEVAKYVTPPLTTVHIPTEEMGRTAVRL 243
                        250       260
                 ....*....|....*....|.
gi 495004537 305 LLARIRGESVTPQRLDLGFTL 325
Cdd:cd01544  244 LLERINGGRTIPKKVLLPTKL 264
PBP1_CelR cd06295
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ...
62-320 2.82e-26

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: 105.03  E-value: 2.82e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  62 TSRAIGVLLP-------SLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSwniDGLILTERNHTPRT 134
Cdd:cd06295    2 RSRTIAVVVPmdphgdqSITDPFFLELLGGISEALTDRGYDMLLSTQDEDANQLARLLDSGRA---DGLIVLGQGLDHDA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 135 LKMIEVAGIPVV---ELMDSVSPCldiAVGFDNFDAARQMTAEIIARGHRHVAYLGARLDERTIMKQKGYEQAMLDAGLT 211
Cdd:cd06295   79 LRELAQQGLPMVvwgAPEDGQSYC---SVGSDNVKGGALATEHLIEIGRRRIAFLGDPPHPEVADRLQGYRDALAEAGLE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 212 PYSVMVEHSS-SFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASV 290
Cdd:cd06295  156 ADPSLLLSCDfTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVGYDDIPLAAYFRPPLTTV 235
                        250       260       270
                 ....*....|....*....|....*....|
gi 495004537 291 LTPRERMGRIGAERLLARIRGESVTPQRLD 320
Cdd:cd06295  236 RQDLALAGRLLVEKLLALIAGEPVTSSMLP 265
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
176-330 1.75e-25

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: 100.11  E-value: 1.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  176 IARGHRHVAYLG---ARLDERTIMKQKGYEQAMLDAGLTPYSVMVeHSSSFSTGSELLRQARREYPQLDSIFCTNDDLAI 252
Cdd:pfam13377   3 AELGHRRIALIGpegDRDDPYSDLRERGFREAARELGLDVEPTLY-AGDDEAEAAAARERLRWLGALPTAVFVANDEVAL 81
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495004537  253 GAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGAERLLARIRGESVTPQRLDLGFTLSPGGS 330
Cdd:pfam13377  82 GVLQALREAGLRVPEDLSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLPPELVERES 159
PRK10401 PRK10401
HTH-type transcriptional regulator GalS;
8-303 1.22e-24

HTH-type transcriptional regulator GalS;


Pssm-ID: 236681 [Multi-domain]  Cd Length: 346  Bit Score: 102.16  E-value: 1.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537   8 LQDVADRVGVTKMTISRYLRNPEQVSLALRSKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGIES 87
Cdd:PRK10401   4 IRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKAVDL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  88 VIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIeVAGIPVVELMDSVSP-----CldiaVGF 162
Cdd:PRK10401  84 VAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDELAQF-MDQIPGMVLINRVVPgyahrC----VCL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 163 DNFDAARQMTAEIIARGHRHVAYLGARLD-ERTIMKQKGYEQAMLDAGLTPYSVMVEHSSSFSTGSEllrQARREY---- 237
Cdd:PRK10401 159 DNVSGARMATRMLLNNGHQRIGYLSSSHGiEDDAMRRAGWMSALKEQGIIPPESWIGTGTPDMQGGE---AAMVELlgrn 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495004537 238 PQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGAE 303
Cdd:PRK10401 236 LQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIGFDDIPIARYTDPQLTTVRYPIASMAKLATE 301
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
6-75 2.16e-24

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 94.19  E-value: 2.16e-24
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537     6 PVLQDVADRVGVTKMTISRYLRNPEQVSLALRSKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTN 75
Cdd:smart00354   1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
PBP1_AglR-like cd20010
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ...
65-318 2.77e-24

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: 99.55  E-value: 2.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  65 AIGVLLPS----LTNQVFAEVLRGIESVIDAHGYQtMLAHYGYKPELEQERLESMLSWN-IDGLILTE-RNHTPRtLKMI 138
Cdd:cd20010    1 AIGLVLPLdpgdLGDPFFLEFLAGLSEALAERGLD-LLLAPAPSGEDELATYRRLVERGrVDGFILARtRVNDPR-IAYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 139 EVAGIPVV-----ELMDSVsPCLDIavgfDNFDAARQMTAEIIARGHRHVAYLGArlDERT---IMKQKGYEQAMLDAGL 210
Cdd:cd20010   79 LERGIPFVvhgrsESGAPY-AWVDI----DNEGAFRRATRRLLALGHRRIALLNG--PEELnfaHQRRDGYRAALAEAGL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 211 T-PYSVMVEHSSSFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGH-DIGQVMEPQLA 288
Cdd:cd20010  152 PvDPALVREGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLlPALEYFSPPLT 231
                        250       260       270
                 ....*....|....*....|....*....|
gi 495004537 289 SVLTPRERMGRIGAERLLARIRGESVTPQR 318
Cdd:cd20010  232 TTRSSLRDAGRRLAEMLLALIDGEPAAELQ 261
PBP1_XylR cd01543
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ...
66-318 4.36e-23

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: 96.12  E-value: 4.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPslTNQVFA-EVLRGIESVIDAHGYQTMLahygYKPELEQERLESMLSWNIDGLILteRNHTPRTLKMIEVAGIP 144
Cdd:cd01543    2 VALLLE--TSRGYGrRLLRGIARYAREHGPWSLY----LEPPGYEELLDLLKGWKGDGIIA--RLDDPELAEALRRLGIP 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 145 VVELmDSVSPCLDIA-VGFDNfDAARQMTAE-IIARGHRHVAYLGARLDERTIMKQKGYEQAMLDAGLTPYSVMVEHSSS 222
Cdd:cd01543   74 VVNV-SGSRPEPGFPrVTTDN-EAIGRMAAEhLLERGFRHFAFCGFRNAAWSRERGEGFREALREAGYECHVYESPPSGS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 223 FSTGSELLRQARReypQLDS------IFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHD-IGQVMEPQLASVLTPRE 295
Cdd:cd01543  152 SRSWEEEREELAD---WLKSlpkpvgIFACNDDRARQVLEACREAGIRVPEEVAVLGVDNDElICELSSPPLSSIALDAE 228
                        250       260
                 ....*....|....*....|...
gi 495004537 296 RMGRIGAERLLARIRGESVTPQR 318
Cdd:cd01543  229 QIGYEAAELLDRLMRGERVPPEP 251
PBP1_AglR_RafR-like cd06271
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ...
65-312 3.92e-22

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: 93.64  E-value: 3.92e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  65 AIGVLLPS---LTNQVFAEVLRGIESVIDAHGYQTMLAhygykPELEQERLESML----SWNIDGLILTERNHTPRTLKM 137
Cdd:cd06271    1 VIALVFPVtetELNGTVSE*VSGITEEAGTTGYHLLVW-----PFEEAES*VPIRdlveTGSADGVILSEIEPNDPRVQF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 138 IEVAGIPVVELMDSVSPCLDIAVGFDNFDAARQMTAEIIARGHRHVAYLGARLDER-TIMKQKGYEQAMLDAGLTPYSVM 216
Cdd:cd06271   76 LTKQNFPFVAHGRSD*PIGHAWVDIDNEAGAYEAVERLAGLGHRRIAFIVPPARYSpHDRRLQGYVRA*RDAGLTGYPLD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 217 VEHS--SSFSTGSELLRQArreyPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGH-DIGQVMEPQLASVLTP 293
Cdd:cd06271  156 ADTTleAGRAAAQRLLALS----PRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSApFLGAMITPPLTTVHAP 231
                        250
                 ....*....|....*....
gi 495004537 294 RERMGRIGAERLLARIRGE 312
Cdd:cd06271  232 IAEAGRELAKALLARIDGE 250
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
34-325 1.07e-19

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: 87.67  E-value: 1.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  34 LALRSKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLE 113
Cdd:COG1879    4 ALLAAVLALALALAACGSAAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 114 SMLSWNIDGLIL--TERNHTPRTLKMIEVAGIPVVeLMDSVSPCLDIA--VGFDNFDAARqMTAEIIAR---GHRHVAYL 186
Cdd:COG1879   84 DLIAQGVDAIIVspVDPDALAPALKKAKAAGIPVV-TVDSDVDGSDRVayVGSDNYAAGR-LAAEYLAKalgGKGKVAIL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 187 GARLDER-TIMKQKGYEQAMLDAG----LTPYSVMVEHSSSFSTGSELLRQarreYPQLDSIFCTNDDLAIGAAFECQRL 261
Cdd:COG1879  162 TGSPGAPaANERTDGFKEALKEYPgikvVAEQYADWDREKALEVMEDLLQA----HPDIDGIFAANDGMALGAAQALKAA 237
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 262 GLriPDDMAIAGFhghDIGQVMEPQL------ASVLTPRERMGRIGAERLLARIRGESVtPQRLDLGFTL 325
Cdd:COG1879  238 GR--KGDVKVVGF---DGSPEALQAIkdgtidATVAQDPYLQGYLAVDAALKLLKGKEV-PKEILTPPVL 301
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
66-325 6.50e-18

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: 81.84  E-value: 6.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILT---ERNHTPrTLKMIEVAG 142
Cdd:cd01536    2 IGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIApvdSEALVP-AVKKANAAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 143 IPVVeLMDS-VSPCLDIA--VGFDNFDAARQMtAEIIAR---GHRHVAYL-GARLDERTIMKQKGYEQAMLDAG----LT 211
Cdd:cd01536   81 IPVV-AVDTdIDGGGDVVafVGTDNYEAGKLA-GEYLAEalgGKGKVAILeGPPGSSTAIDRTKGFKEALKKYPdieiVA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 212 PYSVMVEHSSSFSTGSELLRQarreYPQLDSIFCTNDDLAIGAAFECQRLGLriPDDMAIAGFHG-HDIGQVME--PQLA 288
Cdd:cd01536  159 EQPANWDRAKALTVTENLLQA----NPDIDAVFAANDDMALGAAEALKAAGR--TGDIKIVGVDGtPEALKAIKdgELDA 232
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 495004537 289 SVLTPRERMGRIGAERLLARIRGESVtPQRLDLGFTL 325
Cdd:cd01536  233 TVAQDPYLQGYLAVEAAVKLLNGEKV-PKEILTPVTL 268
PBP1_FruR cd06274
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ...
66-274 1.78e-17

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: 80.71  E-value: 1.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGIPV 145
Cdd:cd06274    2 IGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERRLVENLIARQVDGLIVAPSTPPDDIYYLCQAAGLPV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 146 VELMDSVSPCLDIAVGFDNFDAARQMTAEIIARGHRHVAYLGARLDERTI-MKQKGYEQAMLDAGLTPYSVMVEHSS-SF 223
Cdd:cd06274   82 VFLDRPFSGSDAPSVVSDNRAGARALTEKLLAAGPGEIYFLGGRPELPSTaERIRGFRAALAEAGITEGDDWILAEGyDR 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 495004537 224 STGSELLR---QARREYPQldSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGF 274
Cdd:cd06274  162 ESGYQLMAellARLGGLPQ--ALFTSSLTLLEGVLRFLRERLGAIPSDLVLGTF 213
LacI pfam00356
Bacterial regulatory proteins, lacI family;
8-52 2.41e-15

Bacterial regulatory proteins, lacI family;


Pssm-ID: 306791 [Multi-domain]  Cd Length: 46  Bit Score: 69.20  E-value: 2.41e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 495004537    8 LQDVADRVGVTKMTISRYLRNPEQVSLALRSKIAAALDELGYIPN 52
Cdd:pfam00356   2 IKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
PRK11303 PRK11303
catabolite repressor/activator;
8-278 2.63e-15

catabolite repressor/activator;


Pssm-ID: 236897 [Multi-domain]  Cd Length: 328  Bit Score: 75.30  E-value: 2.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537   8 LQDVADRVGVTKMTISrYLRN--PEQ--VSLALRSKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLR 83
Cdd:PRK11303   3 LDEIARLAGVSRTTAS-YVINgkAKQyrVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDLENTSYARIAK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  84 GIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTER--NHTPRTLKMIEvAGIPVVEL---MDSvsPCLDI 158
Cdd:PRK11303  82 YLERQARQRGYQLLIACSDDQPDNEMRCAEHLLQRQVDALIVSTSlpPEHPFYQRLQN-DGLPIIALdraLDR--EHFTS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 159 AVGfDNFDAARQMTAEIIARGHRHVAYLGArLDERTIMKQK--GYEQAMLDAGLtpySVMVEHSSSFS--TGSELLRQAR 234
Cdd:PRK11303 159 VVS-DDQDDAEMLAESLLKFPAESILLLGA-LPELSVSFEReqGFRQALKDDPR---EVHYLYANSFEreAGAQLFEKWL 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 495004537 235 REYPQLDSIFCTNDDLAIGaAFEC--QRLGlRIPDDMAIAGFhGHD 278
Cdd:PRK11303 234 ETHPMPDALFTTSYTLLQG-VLDVllERPG-ELPSDLAIATF-GDN 276
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
66-325 3.05e-15

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: 74.59  E-value: 3.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHtPRTLKMIEVAG--I 143
Cdd:cd01537    2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDP-AAAGVAEKARGqnV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 144 PVVeLMDSVSPCLDI--AVGFDNFDAARQMTAEIIARGHRHVAYLGARLDERTI-MKQKGYEQAMLDAGL-TPYSVMVEH 219
Cdd:cd01537   81 PVV-FFDKEPSRYDKayYVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHPDAeARLAGVIKELNDKGIkTEQLQLDTG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 220 SSSFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGR 299
Cdd:cd01537  160 DWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYDALPEALKSGPLLTTILQDANNLGK 239
                        250       260
                 ....*....|....*....|....*.
gi 495004537 300 IGAERLLARIRGESVTPQRLDLGFTL 325
Cdd:cd01537  240 TTFDLLLNLADNWKIDNKVVRVPYVL 265
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
66-317 3.78e-15

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: 74.24  E-value: 3.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAhygyKPELEQER----LESMLSWNIDGLIL--TERNHTPRTLKMIE 139
Cdd:cd06322    2 IGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVA----DANGDLAKqlsqIEDFIQQGVDAIILapVDSGGIVPAIEAAN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 140 VAGIPVVELmDSVSPCLDIA--VGFDNFDAARQM---TAEIIARGHRHVAYLGARLDERTIMKQKGYEQAMLD------- 207
Cdd:cd06322   78 EAGIPVFTV-DVKADGAKVVthVGTDNYAGGKLAgeyALKALLGGGGKIAIIDYPEVESVVLRVNGFKEAIKKypnieiv 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 208 AGLTPYSVMVEhssSFSTGSELLrQArreYPQLDSIFCTNDDLAIGAAFECQRLGLriPDDMAIAGFHGHDigqvmEPQ- 286
Cdd:cd06322  157 AEQPGDGRREE---ALAATEDML-QA---NPDLDGIFAIGDPAALGALTAIESAGK--EDKIKVIGFDGNP-----EAIk 222
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 495004537 287 --------LASVLTPRERMGRIGAERLLARIRGESVTPQ 317
Cdd:cd06322  223 aiakggkiKADIAQQPDKIGQETVEAIVKYLAGETVEKE 261
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
66-325 8.59e-15

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: 73.15  E-value: 8.59e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQtmLAHYGYKPE----LEQERLESMLSWNIDGLIL--TERNHTPRTLKMIE 139
Cdd:cd06310    2 IGVVLKGTTSAFWRTVREGAEAAAKDLGVK--IIFVGPESEedvaGQNSLLEELINKKPDAIVVapLDSEDLVDPLKDAK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 140 VAGIPVVeLMDS--VSPCLDIAVGFDNFDAARQMTAEIIA--RGHRHVAYLGARLDERTIM-KQKGYEQAMLDAGLTPYS 214
Cdd:cd06310   80 DKGIPVI-VIDSgiKGDAYLSYIATDNYAAGRLAAQKLAEalGGKGKVAVLSLTAGNSTTDqREEGFKEYLKKHPGGIKV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 215 VMVEHSSS-FSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRipDDMAIAGFhghDIGQVMEPQL------ 287
Cdd:cd06310  159 LASQYAGSdYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLS--GQIKIVGF---DSQEELLDALkngkid 233
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 495004537 288 ASVLTPRERMGRIGAERLLARIRGESVtPQRLDLGFTL 325
Cdd:cd06310  234 ALVVQNPYEIGYEGIKLALKLLKGEEV-PKNIDTGAEL 270
PBP1_RafR-like cd20009
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ...
121-320 2.58e-13

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: 68.72  E-value: 2.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 121 DGLILterNHT----PRTLKMIEvAGIPVVEL----MDSVSPCLDiavgFDNFDAARQMTAEIIARGHRHVAYLGARLD- 191
Cdd:cd20009   59 DGIII---SHTepqdPRVRYLLE-RGFPFVTHgrteLSTPHAYFD----FDNEAFAYEAVRRLAARGRRRIALVAPPREl 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 192 ----ERtimkQKGYEQAMLDAGLTpysVMVEHSSSFSTGSELLRQA----RREYPQLDSIFCTNDDLAIGAAFECQRLGL 263
Cdd:cd20009  131 tyaqHR----LRGFRRALAEAGLE---VEPLLIVTLDSSAEAIRAAarrlLRQPPRPDGIICASEIAALGALAGLEDAGL 203
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495004537 264 RIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGAERLLARIRGESVTP-QRLD 320
Cdd:cd20009  204 VVGRDVDVVAKETSPILDYFRPPIDTLYEDIEEAGRFLAEALLRRIEGEPAEPlQTLE 261
PRK10727 PRK10727
HTH-type transcriptional regulator GalR;
6-307 6.53e-13

HTH-type transcriptional regulator GalR;


Pssm-ID: 182681 [Multi-domain]  Cd Length: 343  Bit Score: 68.63  E-value: 6.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537   6 PVLQDVADRVGVTKMTISRYLRNPEQVSLALRSKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGI 85
Cdd:PRK10727   2 ATIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKAV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  86 ESVidahGYQT---MLAHYGYKPElEQER--LESMLSWNIDGLILTERNHTPRTLKMIeVAGIPVVELMDSVSPCLDI-A 159
Cdd:PRK10727  82 EQV----AYHTgnfLLIGNGYHNE-QKERqaIEQLIRHRCAALVVHAKMIPDAELASL-MKQIPGMVLINRILPGFENrC 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 160 VGFDNFDAARQMTAEIIARGHRHVAYLGA---------RLdertimkqKGYEQAMLDAGLTPYSVMVEHSSSFSTG---- 226
Cdd:PRK10727 156 IALDDRYGAWLATRHLIQQGHTRIGYLCSnhsisdaedRL--------QGYYDALAESGIPANDRLVTFGEPDESGgeqa 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 227 -SELLRQARreypQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGAERL 305
Cdd:PRK10727 228 mTELLGRGR----NFTAVACYNDSMAAGAMGVLNDNGIDVPGEISLIGFDDVLVSRYVRPRLTTVRYPIVTMATQAAELA 303

                 ..
gi 495004537 306 LA 307
Cdd:PRK10727 304 LA 305
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
66-312 8.54e-13

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: 67.39  E-value: 8.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQtMLAHYGYKPELEQ-ERLESMLSWNIDGLILTERNHT--PRTLKMIEVAG 142
Cdd:cd06319    2 IGYSVYDLDNPFWQIMERGVQAAAEELGYE-FVTYDQKNSANEQvTNANDLIAQGVDGIIISPTNSSaaPTVLDLANEAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 143 IPVVelmdsvspCLDIAVGFDNFDAarQMTAEIIARGHRHVAYLGARLDERTI------------------MKQKGYEQA 204
Cdd:cd06319   81 IPVV--------IADIGTGGGDYVS--YIISDNYDGGYQAGEYLAEALKENGWgggsvgiiaipqsrvngqARTAGFEDA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 205 MLDAGLTPYSVMVEHSSSFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRipDDMAIAGFHGHDIGQVME 284
Cdd:cd06319  151 LEEAGVEEVALRQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRT--GDILVVGFDGDPEALDLI 228
                        250       260       270
                 ....*....|....*....|....*....|.
gi 495004537 285 PQ---LASVLTPRERMGRIGAERLLARIRGE 312
Cdd:cd06319  229 KDgklDGTVAQQPFGMGARAVELAIQALNGD 259
HTH_LacI cd01392
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ...
9-54 2.45e-12

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: 60.88  E-value: 2.45e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 495004537   9 QDVADRVGVTKMTISRYLRNPEQVSLALRSKIAAALDELGYIPNRA 54
Cdd:cd01392    1 KDIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAA 46
PBP1_hexuronate_repressor-like cd06272
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ...
65-322 2.59e-12

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: 65.86  E-value: 2.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  65 AIGVLLPSLTNQV-FAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRTLKMIEVAGI 143
Cdd:cd06272    1 TIGLYWPSVGERVaLTRLLSGINEAISKQGYNINLSICPYKVGHLCTAKGLFSENRFDGVIVFGISDSDIEYLNKNKPKI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 144 PVVeLMDSVSPCLDIaVGFDNFDAARQMTAEIIARGHRHVAYLG-ARLDERTIMKQKGYEQAMLDAGLT-PYSVMVEHSS 221
Cdd:cd06272   81 PIV-LYNRESPKYST-VNVDNEKAGRLAVLLLIQKGHKSIAYIGnPNSNRNQTLRGKGFIETCEKHGIHlSDSIIDSRGL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 222 SFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIG 301
Cdd:cd06272  159 SIEGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISIPEDISIVSYDNIPQEARSDPPLTVVGVPIEKIAEES 238
                        250       260
                 ....*....|....*....|.
gi 495004537 302 AERLLARIRGESVTPQRLDLG 322
Cdd:cd06272  239 LRLILKLIEGRENEIQQLILY 259
PBP1_LacI-like cd06287
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
119-316 5.12e-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: 65.13  E-value: 5.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 119 NIDGLILTERNHTPRTLKMIEVAGIPVVEL-----MDSVSPCLDIAVGfdnfDAARQMTAEIIARGHRHVAYL-GARLDE 192
Cdd:cd06287   56 DVDGAIVVEPTVEDPILARLRQRGVPVVSIgrapgTDEPVPYVDLQSA----ATARLLLEHLHGAGARQVALLtGSSRRN 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 193 RTIMKQKGYEQAMLDAGLTPYSVMVEHSSSFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIA 272
Cdd:cd06287  132 SSLESEAAYLRFAQEYGTTPVVYKVPESEGERAGYEAAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPEDLMVV 211
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 495004537 273 GFHGHDIGQVMEPQLASVLTPRERMGRIGAERLLARIRGESVTP 316
Cdd:cd06287  212 TRYDGIRARTADPPLTAVDLHLDRVARTAIDLLFASLSGEERSV 255
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
66-313 1.21e-11

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: 63.87  E-value: 1.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537   66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYG-YKPELEQERLESMLSWNIDGLILTeRNHTPRTLKMIEVA--- 141
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAeADAAEQVAQIEDAIAQGVDAIIVA-PVDPTALAPVLKKAkda 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  142 GIPVVeLMDSV---SPCLDIaVGFDNFDAARQMtAEIIAR---GHRHVAYLGARL-DERTIMKQKGYEQAM--LDAGLTP 212
Cdd:pfam13407  80 GIPVV-TFDSDapsSPRLAY-VGFDNEAAGEAA-GELLAEalgGKGKVAILSGSPgDPNANERIDGFKKVLkeKYPGIKV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  213 YSVMVEHSSSFSTGSELLRQARREYP-QLDSIFCTNDDLAIGAAFECQRLGLRipDDMAIAGFhghDIGQVMEPQL---- 287
Cdd:pfam13407 157 VAEVEGTNWDPEKAQQQMEALLTAYPnPLDGIISPNDGMAGGAAQALEAAGLA--GKVVVTGF---DATPEALEAIkdgt 231
                         250       260
                  ....*....|....*....|....*...
gi 495004537  288 --ASVLTPRERMGRIGAERLLARIRGES 313
Cdd:pfam13407 232 idATVLQDPYGQGYAAVELAAALLKGKK 259
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
66-314 3.56e-10

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


Pssm-ID: 380546 [Multi-domain]  Cd Length: 268  Bit Score: 59.62  E-value: 3.56e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLIL--TERNHTPRTLKMIEVAGI 143
Cdd:cd06323    2 IGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLInpTDSDAVSPAVEEANEAGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 144 PVVELMDSVSPCLDIA-VGFDNFDAARQMTAEIIARGHR--HVAYL----GArldERTIMKQKGYEQAMLDAGltPYSVM 216
Cdd:cd06323   82 PVITVDRSVTGGKVVShIASDNVAGGEMAAEYIAKKLGGkgKVVELqgipGT---SAARERGKGFHNAIAKYP--KINVV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 217 VEHSSSFS--TGSELLRQARREYPQLDSIFCTNDDLAIGAAfecQRLGLRIPDDMAIAGFHGHDIGQ--VMEPQL-ASVL 291
Cdd:cd06323  157 ASQTADFDrtKGLNVMENLLQAHPDIDAVFAHNDEMALGAI---QALKAAGRKDVIVVGFDGTPDAVkaVKDGKLaATVA 233
                        250       260
                 ....*....|....*....|...
gi 495004537 292 TPRERMGRIGAERLLARIRGESV 314
Cdd:cd06323  234 QQPEEMGAKAVETADKYLKGEKV 256
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
66-313 5.01e-10

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


Pssm-ID: 380622 [Multi-domain]  Cd Length: 272  Bit Score: 59.26  E-value: 5.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLIL--TERNHTPRTLKMIEVAGI 143
Cdd:cd19967    2 VAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILdpADADASIAAVKKAKDAGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 144 PVVeLMDSVSPCLDIAVG---FDNFDAAR---QMTAEIIARGHRHVAYLGARLDERTIMKQKGYEQaMLDAglTPYSVMV 217
Cdd:cd19967   82 PVF-LIDREINAEGVAVAqivSDNYQGAVllaQYFVKLMGEKGLYVELLGKESDTNAQLRSQGFHS-VIDQ--YPELKMV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 218 -EHSSSFS--TGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGlrIPDDMAIAGFHGHD--IGQVMEPQL-ASVL 291
Cdd:cd19967  158 aQQSADWDrtEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAG--RAGDVIIVGFDGSNdvRDAIKEGKIsATVL 235
                        250       260
                 ....*....|....*....|..
gi 495004537 292 TPRERMGRIGAERLLARIRGES 313
Cdd:cd19967  236 QPAKLIARLAVEQADQYLKGGS 257
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
66-316 8.27e-10

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: 58.75  E-value: 8.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILT--ERNHTPRTLKMIEVAGI 143
Cdd:cd19971    2 FGFSYMTMNNPFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNpvDSEGIRPALEAAKEAGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 144 PVV---------ELMDSVspcldiaVGFDNFDAARQMTAEIIAR---GHRhVAYLGARLDERTIMKQKGYEQAMldAGLT 211
Cdd:cd19971   82 PVInvdtpvkdtDLVDST-------IASDNYNAGKLCGEDMVKKlpeGAK-IAVLDHPTAESCVDRIDGFLDAI--KKNP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 212 PYSVM--VEHSSSFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLriPDDMAIAGFHGHDIGQVM--EPQL 287
Cdd:cd19971  152 KFEVVaqQDGKGQLEVAMPIMEDILQAHPDLDAVFALNDPSALGALAALKAAGK--LGDILVYGVDGSPDAKAAikDGKM 229
                        250       260       270
                 ....*....|....*....|....*....|.
gi 495004537 288 ASVL--TPRErMGRIGAERLLARIRGESVTP 316
Cdd:cd19971  230 TATAaqSPIE-IGKKAVETAYKILNGEKVEK 259
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
66-316 9.12e-09

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


Pssm-ID: 380540 [Multi-domain]  Cd Length: 281  Bit Score: 55.46  E-value: 9.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILT--ERNHTPRTLKMIEVAGI 143
Cdd:cd06317    2 IALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDaiDVNGSIPAIKRASEAGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 144 PVVeLMDSVSPCLDIA--VGFDNFDAARQM---TAEIIAR---GHRHVAYLGARLDERTIMKQKGYEQAMLD-AGLTPYS 214
Cdd:cd06317   82 PVI-AYDAVIPSDFQAaqVGVDNLEGGKEIgkyAADYIKAelgGQAKIGVVGALSSLIQNQRQKGFEEALKAnPGVEIVA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 215 VM---VEHSSSFSTGSELLrQARreyPQLDSIFCTNDDLAIGA--AFECQRLGLRIP----DDMAIAGFHGHDIGQVmep 285
Cdd:cd06317  161 TVdgqNVQEKALSAAENLL-TAN---PDLDAIYATGEPALLGAvaAVRSQGRQGKIKvfgwDLTKQAIFLGIDEGVL--- 233
                        250       260       270
                 ....*....|....*....|....*....|.
gi 495004537 286 qLASVLTPRERMGRIGAERLLARIRGESVTP 316
Cdd:cd06317  234 -QAVVQQDPEKMGYEAVKAAVKAIKGEDVEK 263
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
120-274 2.74e-08

periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group includes the periplasmic sugar-binding domain of uncharacterized ABC-type transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which 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: 54.53  E-value: 2.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 120 IDGLILT-ERNHTPRTLKMIEVAGIPVVELMDSVSPCLDIAVGF--------------DNFDAARQMTAEIIARGHRH-- 182
Cdd:cd06324   59 PDYLILVnEKGVAPELLELAEQAKIPVFLINNDLTDEERALLGKprekfkywlgsivpDNEQAGYLLAKALIKAARKKsd 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 183 ------VAYLGARLDERTIMKQKGYEQAMLDAG-LTPYSVMV---EHSSSFSTGSELLRQarreYPQLDSIFCTNDDLAI 252
Cdd:cd06324  139 dgkirvLAISGDKSTPASILREQGLRDALAEHPdVTLLQIVYanwSEDEAYQKTEKLLQR----YPDIDIVWAANDAMAL 214
                        170       180
                 ....*....|....*....|..
gi 495004537 253 GAAFECQRLGLRIPDDMAIAGF 274
Cdd:cd06324  215 GAIDALEEAGLKPGKDVLVGGI 236
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
66-274 4.71e-08

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


Pssm-ID: 380625 [Multi-domain]  Cd Length: 275  Bit Score: 53.41  E-value: 4.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIES-VIDAHGYQtmLAHYGYKPEL---EQERL-ESMLSWNIDGLILTERNHT---PRTLKM 137
Cdd:cd19970    2 VALVMKSLANEFFIEMEKGARKhAKEANGYE--LLVKGIKQETdieQQIAIvENLIAQKVDAIVIAPADSKalvPVLKKA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 138 IEvAGIPVVEL---MD---SVSPCLDIA-VGFDNFDAARqMTAEIIARG---HRHVAYL-GARLDERTIMKQKGYEQAML 206
Cdd:cd19970   80 VD-AGIAVINIdnrLDadaLKEGGINVPfVGPDNRQGAY-LAGDYLAKKlgkGGKVAIIeGIPGADNAQQRKAGFLKAFE 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495004537 207 DAGLTPYSVMVEH---SSSFSTGSELLRQarreYPQLDSIFCTNDDLAIGAAFECQRLGLRipDDMAIAGF 274
Cdd:cd19970  158 EAGMKIVASQSANweiDEANTVAANLLTA----HPDIRGILCANDNMALGAIKAVDAAGKA--GKVLVVGF 222
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
66-319 9.51e-08

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


Pssm-ID: 380627 [Multi-domain]  Cd Length: 269  Bit Score: 52.44  E-value: 9.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRT--LKMIEVAGI 143
Cdd:cd19972    2 IGLAVANLQADFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAvpVKAARAAGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 144 PVVELmDSVSPC--LDIAVGFDNFDAARQMTAEIIAR--GHRHVAYL-GARLDERTIMKQKGYEQAMldAGLTPYSVMVE 218
Cdd:cd19972   82 PVIAV-DRNPEDapGDTFIATDSVAAAKELGEWVIKQtgGKGEIAILhGQLGTTPEVDRTKGFQEAL--AEAPGIKVVAE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 219 HSSSFS--TGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLriPDDMAIAGFHG--HDIGQVMEPQLASVLTPR 294
Cdd:cd19972  159 QTADWDqdEGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGL--DHKIWVVGFDGdvAGLKAVKDGVLDATMTQQ 236
                        250       260
                 ....*....|....*....|....*.
gi 495004537 295 -ERMGRIGAERLLARIRGESVTPQRL 319
Cdd:cd19972  237 tQKMGRLAVDSAIDLLNGKAVPKEQL 262
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
66-317 3.35e-07

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


Pssm-ID: 380544 [Multi-domain]  Cd Length: 270  Bit Score: 50.75  E-value: 3.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGY--QTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHT---PRTLKMIEv 140
Cdd:cd06321    2 IGVTVQDLGNPFFVAMVRGAEEAAAEINPgaKVTVVDARYDLAKQFSQIDDFIAQGVDLILLNAADSAgiePAIKRAKD- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 141 AGIPVVElMDSVSPCLDIAVGFDNFDAArQMTAEiiarghrhvaYLGARLDER-------------TIMKQKGYEQAMLD 207
Cdd:cd06321   81 AGIIVVA-VDVAAEGADATVTTDNVQAG-YLACE----------YLVEQLGGKgkvaiidgppvsaVIDRVNGCKEALAE 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 208 AGLTPYSVMVEHSSSFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLripDDMAIAGFHGH-DIGQVMEPQ 286
Cdd:cd06321  149 YPGIKLVDDQNGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGR---DDIVITSVDGSpEAVAALKRE 225
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 495004537 287 LASVLT-----PRErMGRIGAERLLARIRGESVTPQ 317
Cdd:cd06321  226 GSPFIAtaaqdPYD-MARKAVELALKILNGQEPAPE 260
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
103-317 5.94e-07

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


Pssm-ID: 380662 [Multi-domain]  Cd Length: 271  Bit Score: 49.93  E-value: 5.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 103 YKPELEQERLESMLSWNIDGLIL--TERNHTPRTLKMIEVAGIPVVeLMDSVSPCLDIAVGF---DNFD----AARQMtA 173
Cdd:cd20007   40 FDPTLQTPIVNAVIAKKPDALLIapTDPQALIAPLKRAADAGIKVV-TVDTTLGDPSFVLSQiasDNVAggalAAEAL-A 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 174 EIIArGHRHVAYLGARLDERTI-MKQKGYEQAMLDA-GLTpySVMVEHS-SSFSTGSELLRQARREYPQLDSIFCTNDDL 250
Cdd:cd20007  118 ELIG-GKGKVLVINSTPGVSTTdARVKGFAEEMKKYpGIK--VLGVQYSeNDPAKAASIVAAALQANPDLAGIFGTNTFS 194
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495004537 251 AIGAAFECQRLGLRipDDMAIAGFhghDIGQVMEPQLAS-------VLTPRErMGRIGAERLLARIRGESVTPQ 317
Cdd:cd20007  195 AEGAAAALRNAGKT--GKVKVVGF---DASPAQVEQLKAgtidaliAQKPAE-IGYLAVEQAVAALTGKPVPKD 262
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
66-322 1.69e-06

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: 48.95  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRT--LKMIEVAGI 143
Cdd:cd06318    2 IGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTpaVKAAKAAGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 144 PVVELMDSVSPCLDIA--VGFDNFD---AARQMTAEIIARGHRHVAYL-----GARLDERTIMKQKGYEQAML----DAG 209
Cdd:cd06318   82 PVITVDSALDPSANVAtqVGRDNKQngvLVGKEAAKALGGDPGKIIELsgdkgNEVSRDRRDGFLAGVNEYQLrkygKSN 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 210 LT----PYSVMVeHSSSFSTGSELLrQArreYPQLDSIFCTNDDLAIGAAFECQRLGLRipDDMAIAGFHGHD--IGQVM 283
Cdd:cd06318  162 IKvvaqPYGNWI-RSGAVAAMEDLL-QA---HPDINVVYAENDDMALGAMKALKAAGML--DKVKVAGADGQKeaLKLIK 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 495004537 284 EPQL-ASVLTPRERMGRIGAERLLARIRGESVTPQRLDLG 322
Cdd:cd06318  235 DGKYvATGLNDPDLLGKTAVDTAAKVVKGEESFPEFTYTP 274
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
141-274 1.77e-06

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


Pssm-ID: 380661 [Multi-domain]  Cd Length: 274  Bit Score: 48.75  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 141 AGIPVVeLMDS-----VSPCLdiaVGFDNFDAARQMTAEIIARGHR--HVAYLGARLDERTIMK-QKGYEQAMLDAGLTp 212
Cdd:cd20006   83 AGIPVI-TIDSpvnskKADSF---VATDNYEAGKKAGEKLASLLGEkgKVAIVSFVKGSSTAIErEEGFKQALAEYPNI- 157
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495004537 213 YSVMVEHSSSFSTGSELL-RQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRipDDMAIAGF 274
Cdd:cd20006  158 KIVETEYCDSDEEKAYEItKELLSKYPDINGIVALNEQSTLGAARALKELGLG--GKVKVVGF 218
PRK10339 PRK10339
DNA-binding transcriptional repressor EbgR; Provisional
8-318 2.59e-06

DNA-binding transcriptional repressor EbgR; Provisional


Pssm-ID: 182389 [Multi-domain]  Cd Length: 327  Bit Score: 48.60  E-value: 2.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537   8 LQDVADRVGVTKMTISRYLRNPEQVSLA--LRSKIAAALDELGYIPNRAPDILSNATSR----AIGVLLPSL-TNQVFAE 80
Cdd:PRK10339   4 LKDIAIEAGVSLATVSRVLNDDPTLNVKeeTKHRILEIAEKLEYKTSSARKLQTGAVNQhhilAIYSYQQELeINDPYYL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  81 VLR-GIESVIDAHGYqTMLAHYGYKPELEQERlesmlswnIDGLILTERNhTPRTLKMIEVAGIPVVeLMDSVSPCLDI- 158
Cdd:PRK10339  84 AIRhGIETQCEKLGI-ELTNCYEHSGLPDIKN--------VTGILIVGKP-TPALRAAASALTDNIC-FIDFHEPGSGYd 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 159 AVGFDNFDAARQMTAEIIARGHRHVAYLGARlDERTIMKQKgyEQAMLDAGLTPYSVMVE--HSSSFST--GSELLRQ-- 232
Cdd:PRK10339 153 AVDIDLARISKEIIDFYINQGVNRIGFIGGE-DEPGKADIR--EVAFAEYGRLKQVVREEdiWRGGFSSssGYELAKQml 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 233 ARREYPQldSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHGHDIGQVMEPQLASVLTPRERMGRIGAERLLARIRGE 312
Cdd:PRK10339 230 AREDYPK--ALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNLLYEKARDG 307

                 ....*.
gi 495004537 313 SVTPQR 318
Cdd:PRK10339 308 RALPLL 313
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
66-273 2.97e-06

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


Pssm-ID: 380524 [Multi-domain]  Cd Length: 272  Bit Score: 48.00  E-value: 2.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQvFAEVLR-GIESVIDAH-GYQTMLAHYGYKPELEQERLESMLSWNIDGLILT--ERNHTPRTLKMIEVA 141
Cdd:cd06301    3 IGVSMQNFSDE-FLTYLRdAIEAYAKEYpGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNpvDTDASAPAVDAAADA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 142 GIPVVELMDSV--SPCLDIAVGFDNFDAARqMTAEIIAR---GHRHVAYL-GARLDERTIMKQKGYEQAMLD-AGLtpyS 214
Cdd:cd06301   82 GIPLVYVNREPdsKPKGVAFVGSDDIESGE-LQMEYLAKllgGKGNIAILdGVLGHEAQILRTEGNKDVLAKyPGM---K 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495004537 215 VMVEHSSSFST--GSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLRipDDMAIAG 273
Cdd:cd06301  158 IVAEQTANWSRekAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKK--DDILVAG 216
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
65-316 4.92e-06

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


Pssm-ID: 380649 [Multi-domain]  Cd Length: 304  Bit Score: 47.62  E-value: 4.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  65 AIGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRT--LKMIEVAG 142
Cdd:cd19994    1 KIGISLPTKSEERWIKDGENLKSELEEAGYTVDLQYADDDVATQNSQIENMINKGAKVLVIAPVDGSALGdvLEEAKDAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 143 IPVVE----LMDsvSPCLDIAVGFDNFdAARQMTAEIIARGhrhvAYLGARLDERTIM----------KQKGYEQAM--- 205
Cdd:cd19994   81 IPVIAydrlIMN--TDAVDYYVTFDNE-KVGELQGQYLVDK----LGLKDGKGPFNIElfagspddnnAQLFFKGAMevl 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 206 ---LDAG-LTPYSVMVE------HSSSFSTG----SELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLrIPDDMAI 271
Cdd:cd19994  154 qpyIDDGtLVVRSGQTTfeqvatPDWDTETAqarmETLLSAYYTGGKKLDAVLSPNDGIARGVIEALKAAGY-DTGPWPV 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495004537 272 AGfhghdiGQVMEP----------QLASVLTPRERMGRIGAERLLARIRGESVTP 316
Cdd:cd19994  233 VT------GQDAEDasvksildgeQSMTVFKDTRLLAKATVELVDALLEGEEVEV 281
Periplasmic_Binding_Protein_type1 cd01391
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
66-264 9.25e-06

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


Pssm-ID: 380477 [Multi-domain]  Cd Length: 280  Bit Score: 46.49  E-value: 9.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSL---TNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLI---LTERNHTPRT---LK 136
Cdd:cd01391    2 IGVVTSSLhqiREQFGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIgpgSSSVAIVIQNlaqLF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 137 MIEVAGIPVVELMDSVSPCLD--IAVGFDNFDAARQMTAEIIARGHRHVAYLGARLDERTIMKQKGYEQAMLDAGLTPYS 214
Cdd:cd01391   82 DIPQLALDATSQDLSDKTLYKyfLSVVFSDTLGARLGLDIVKRKNWTYVAAIHGEGLNSGELRMAGFKELAKQEGICIVA 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 495004537 215 VMVEHSSSFSTGSELLRQARREYPQLDSIFCTNDDLAIGAAFECQRLGLR 264
Cdd:cd01391  162 SDKADWNAGEKGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLV 211
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
66-325 1.06e-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: 380659 [Multi-domain]  Cd Length: 273  Bit Score: 46.07  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQtmLAHYGykPELEQER------LESMLSWNIDGLILTErNHTPRTLKMIE 139
Cdd:cd20004    2 IAVIPKGTTHDFWKSVKAGAEKAAQELGVE--IYWRG--PSREDDVeaqiqiIEYFIDQGVDGIVLAP-LDRKALVAPVE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 140 VA---GIPVVeLMDSVSPCLDI--AVGFDNFdAARQMTAEIIAR---GHRHVAYLgaRLDE---RTIMKQKGYEQAM--L 206
Cdd:cd20004   77 RAraqGIPVV-IIDSDLGGDAVisFVATDNY-AAGRLAAKRMAKllnGKGKVALL--RLAKgsaSTTDRERGFLEALkkL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 207 DAGLT----PYsVMVEHSSSFSTGSELLRQarreYPQLDSIFCTNDDLAIGAAFECQRLGL--RIPddmaiagFHGHDIG 280
Cdd:cd20004  153 APGLKvvddQY-AGGTVGEARSSAENLLNQ----YPDVDGIFTPNESTTIGALRALRRLGLagKVK-------FIGFDAS 220
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495004537 281 QVMEPQL------ASVLTPRERMGRIGAERLLARIRGESVtPQRLDLGFTL 325
Cdd:cd20004  221 DLLLDALrageisALVVQDPYRMGYLGVKTAVAALRGKPV-PKRIDTGVVL 270
PBP1_ABC_xylose_binding-like cd19992
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
66-263 1.28e-05

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: 46.04  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHT--PRTLKMIEVAGI 143
Cdd:cd19992    2 IGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGaaANIVDKAKAAGV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 144 PVVElMDSV--SPCLDIAVGFDNFDAARQMTAEIIARGHR-HVAYL-GARLDERTIMKQKGYE---QAMLDAG-LTpySV 215
Cdd:cd19992   82 PVIS-YDRLilNADVDLYVGRDNYKVGQLQAEYALEAVPKgNYVILsGDPGDNNAQLITAGAMdvlQPAIDSGdIK--IV 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495004537 216 MVEHSSSFSTgSELLRQAR----REYPQLDSIFCTNDDLAIGAAFECQRLGL 263
Cdd:cd19992  159 LDQYVKGWSP-DEAMKLVEnaltANNNNIDAVLAPNDGMAGGAIQALKAQGL 209
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
112-254 6.34e-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: 43.89  E-value: 6.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 112 LESMLSWNIDGLILTERNHTPRT--LKMIEVAGIPVVELmDSVSPCL--DIAVGFDNFDAARQmTAEIIAR---GHRHVA 184
Cdd:cd06311   48 LEDLIAQKVDAIVILPQDSEELTvaAQKAKDAGIPVVNF-DRGLNVLiyDLYVAGDNPGMGVV-SAEYIGKklgGKGNVV 125
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495004537 185 YL-----GARLDERTimkqKGYEQAMldAGLTPYSVMVEHSSSFST--GSELLRQARREYPQLDSIFCTNDDLAIGA 254
Cdd:cd06311  126 VLevpssGSVNEERV----AGFKEVI--KGNPGIKILAMQAGDWTRedGLKVAQDILTKNKKIDAVWAADDDMAIGV 196
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
104-322 1.35e-04

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: 42.92  E-value: 1.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 104 KPELEQERLESMLSWNIDGLILTERNHTPRT--LKMIEVAGIPVVeLMDS-VSPCLDIA-VGFDNFDAARQMtAEIIAR- 178
Cdd:cd06308   41 DAAKQIADIEDLIAQGVDLLIVSPNEADALTpvVKKAYDAGIPVI-VLDRkVSGDDYTAfIGADNVEIGRQA-GEYIAEl 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 179 --GHRHVAYL-GARLDERTIMKQKGYEQAMldAGLTPYSVMVEHSSSFSTGS--ELLRQARREYPQLDSIFCTNDDLAIG 253
Cdd:cd06308  119 lnGKGNVVEIqGLPGSSPAIDRHKGFLEAI--AKYPGIKIVASQDGDWLRDKaiKVMEDLLQAHPDIDAVYAHNDEMALG 196
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495004537 254 AAFECQRLGLRipDDMAIAGFHG--HDIGQ-VMEPQL-ASVLTPreRMGRIGAERLLARIRGESVtPQRLDLG 322
Cdd:cd06308  197 AYQALKKAGRE--KEIKIIGVDGlpEAGEKaVKDGILaATFLYP--TGGKEAIEAALKILNGEKV-PKEIVLP 264
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
108-274 3.55e-04

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


Pssm-ID: 380624 [Multi-domain]  Cd Length: 278  Bit Score: 41.55  E-value: 3.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 108 EQERLESMLSWNIDGLILT---ERNHTPRTLKMIEvAGIPVVeLMDSVSPCLD--IAVGFDNFDAARqMTAEIIAR---G 179
Cdd:cd19969   45 QITAIEQAIAKNPDGIAVSaidPEALTPTINKAVD-AGIPVV-TFDSDAPESKriSYVGTDNYEAGY-AAAEKLAEllgG 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 180 HRHVAYL----GARLDERTimkqKGYEQAMldAGLTPYSVMVEHSS--SFSTGSELLRQARREYPQLDSIFCTNDDLAIG 253
Cdd:cd19969  122 KGKVAVLtgpgQPNHEERV----EGFKEAF--AEYPGIEVVAVGDDndDPEKAAQNTSALLQAHPDLVGIFGVDASGGVG 195
                        170       180
                 ....*....|....*....|.
gi 495004537 254 AAFECQRLGLRipDDMAIAGF 274
Cdd:cd19969  196 AAQAVREAGKT--GKVKIVAF 214
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
105-325 3.78e-04

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: 41.41  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 105 PELEQERLESMLSWNIDGLILT--ERNHTPRTLKMIEVAGIPVVeLMDSVSP-CLDIA-VGFDNFDAARQMtAEIIARGH 180
Cdd:cd06314   42 AAEQVQLIEDLIARGVDGIAISpnDPEAVTPVINKAADKGIPVI-TFDSDAPdSKRLAyIGTDNYEAGREA-GELMKKAL 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 181 RH-------VAYLGA-RLDERTimkqKGYEQAMLDAG----LTPYSVmvehSSSFSTGSELLRQARREYPQLDSIFCTN- 247
Cdd:cd06314  120 PGggkvaiiTGGLGAdNLNERI----QGFKDALKGSPgieiVDPLSD----NDDIAKAVQNVEDILKANPDLDAIFGVGa 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 248 -DDLAIGAAFEcqrlGLRIPDDMAIAGFhghDIgqvMEPQL---------ASVLTPRERMGRIGAERLLARIRGESVTPQ 317
Cdd:cd06314  192 yNGPAIAAALK----DAGKVGKVKIVGF---DT---LPETLqgikdgviaATVGQRPYEMGYLSVKLLYKLLKGGKPVPD 261

                 ....*...
gi 495004537 318 RLDLGFTL 325
Cdd:cd06314  262 VIDTGVDV 269
PBP1_LuxPQ_Quorum_Sensing cd06303
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi ...
53-276 5.73e-04

periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs; Periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs from other bacteria. The members of this group are highly homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea, and that are members of the type 1 periplasmic binding protein superfamily. The Vibrio harveyi AI-2 receptor consists of two polypeptides, LuxP and LuxQ: LuxP is a periplasmic binding protein that binds AI-2 by clamping it between two domains, LuxQ is an integral membrane protein belonging to the two-component sensor kinase family. Unlike AI-2 bound to the LsrB receptor in Salmonella typhimurium, the Vibrio harveyi AI-2 signaling molecule has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LuxPQ to control light production as well as its motility behavior.


Pssm-ID: 380526 [Multi-domain]  Cd Length: 320  Bit Score: 41.20  E-value: 5.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  53 RAPDILSNATSRA---IGVLLPSLtnQVFAEVLRGIESV---IDAHGYQTMLAHYGYKPELEQER----LESMLSWNIDG 122
Cdd:cd06303   14 RAPPVPAEVTQKRpvkIAVVYPGL--QVSDYWRRSIVSFrkrLDELGIKYQLDEFFTRPGAEIRLqalqIREMLKSDPDY 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 123 LILTErnHTPRTLKMIEVA---GIPVVELMDSVSPCLD-------IAVGFDNFDAARQMTAEIIARGHRHVAYLGARLDE 192
Cdd:cd06303   92 LIFTL--DALRHRRFVEILldsGKPKLILQNITTPLRDwdnhqplLYVGFDHAEGSRMLAKHFIKIFPEEGKYAILYLTE 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 193 RTIMKQKGyeQAMLDAgLTPYSVMvEHSSSFSTG--SELLRQARRE----YPQLDSIFCTNDDLAIGAAFECQRLGLRip 266
Cdd:cd06303  170 GYVSDQRG--DTFIDE-VARHSNL-ELVSAYYTDfdRESAREAARAllarHPDLDFIYACSTDIALGAIDALQELGRE-- 243
                        250
                 ....*....|
gi 495004537 267 DDMAIAGFHG 276
Cdd:cd06303  244 TDIMINGWGG 253
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
83-317 6.08e-04

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: 41.05  E-value: 6.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  83 RGIESVIDAHGYQTMLAHYGYKPELEQERLESMLSWNIDGLILTERNHTPRT--LKMIEVAGIPVVeLMD---SVSPCLD 157
Cdd:cd06309   19 KSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDpvLKEAKDAGIPVI-LVDrtiDGEDGSL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 158 IA--VGFDNFDAARQM---TAEIIARGHRHVAYL-GARLDERTIMKQKGYEQAMLDAGltPYSVMVEHSSSFS--TGSEL 229
Cdd:cd06309   98 YVtfIGSDFVEEGRRAaewLVKNYKGGKGNVVELqGTAGSSVAIDRSKGFREVIKKHP--NIKIVASQSGNFTreKGQKV 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537 230 LRQARREYPQ-LDSIFCTNDDLAIGAAFECQRLGLRIPDDMAIAGFHG-HD-IGQVMEPQLASVLTPRERMGRIGAERLL 306
Cdd:cd06309  176 MENLLQAGPGdIDVIYAHNDDMALGAIQALKEAGLKPGKDVLVVGIDGqKDaLEAIKAGELNATVECNPLFGPTAFDTIA 255
                        250
                 ....*....|.
gi 495004537 307 ARIRGESVTPQ 317
Cdd:cd06309  256 KLLAGEKVPKL 266
HipB COG1396
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
8-45 1.29e-03

Transcriptional regulator, contains XRE-family HTH domain [Transcription];


Pssm-ID: 441006 [Multi-domain]  Cd Length: 83  Bit Score: 37.28  E-value: 1.29e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 495004537   8 LQDVADRVGVTKMTISRYLRNPEQVSLALRSKIAAALD 45
Cdd:COG1396   23 QEELAERLGVSRSTISRIERGRRNPSLETLLKLAKALG 60
XRE COG1476
DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription];
9-45 1.51e-03

DNA-binding transcriptional regulator, XRE-family HTH domain [Transcription];


Pssm-ID: 441085 [Multi-domain]  Cd Length: 68  Bit Score: 36.75  E-value: 1.51e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 495004537   9 QDVADRVGVTKMTISRYLRNPEQVSLALRSKIAAALD 45
Cdd:COG1476   21 EELAELLGVSRQTISAIENGKYNPSLELALKIARALG 57
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
66-182 4.31e-03

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: 38.31  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495004537  66 IGVLLPSLTNQVFAEVLRGIESVIDAHGYQTMLAHYGYKPELEQERLES---MLSWNIDGLILTERNHtPRTLKMIE--- 139
Cdd:cd06307    2 FGFLLPSPENPFYELLRRAIEAAAAALRDRRVRLRIHFVDSLDPEALAAalrRLAAGCDGVALVAPDH-PLVRAAIDela 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 495004537 140 VAGIPVVELMDSVSPCLDIA-VGFDNFDAARqmTA-EIIARGHRH 182
Cdd:cd06307   81 ARGIPVVTLVSDLPGSRRLAyVGIDNRAAGR--TAaWLMGRFLGR 123
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
8-45 4.88e-03

Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.


Pssm-ID: 238045 [Multi-domain]  Cd Length: 58  Bit Score: 34.84  E-value: 4.88e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 495004537   8 LQDVADRVGVTKMTISRYLRNPEQVSLALRSKIAAALD 45
Cdd:cd00093   15 QEELAEKLGVSRSTISRIENGKRNPSLETLEKLAKALG 52
AF2118 COG3620
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ...
10-46 7.53e-03

Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain CBS pair) [Transcription];


Pssm-ID: 442838 [Multi-domain]  Cd Length: 95  Bit Score: 35.38  E-value: 7.53e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 495004537  10 DVADRVGVTKMTISRYLRNPEQVSLALRSKIAAALDE 46
Cdd:COG3620   35 PVAELVGVSQSDILRIESGKRDPTVSTLEKIAEALGK 71
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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