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Conserved domains on  [gi|504341065|ref|WP_014528167|]
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LacI family DNA-binding transcriptional regulator [Sinorhizobium meliloti]

Protein Classification

LacI family DNA-binding transcriptional regulator( domain architecture ID 10105133)

LacI family DNA-binding transcriptional regulator functions as an activator or repressor by binding a specific effector ligand that either decreases (induction) or increases DNA-binding affinity (co-repression)

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
61-332 8.44e-106

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: 310.65  E-value: 8.44e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  61 RLDFVLPAGTNTFVANLLRQLQTQATARPDLDVRVHS--IEGFNPDTLAGTLQELRGETMGVGVIALDHPTVREAMRSLA 138
Cdd:cd06307    1 RFGFLLPSPENPFYELLRRAIEAAAAALRDRRVRLRIhfVDSLDPEALAAALRRLAAGCDGVALVAPDHPLVRAAIDELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 139 SSGVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGRgSKGKIALFAGSLSYRGHEEREMGFRHIIADEFPALE 218
Cdd:cd06307   81 ARGIPVVTLVSDLPGSRRLAYVGIDNRAAGRTAAWLMGRFLGR-RPGKVLVILGSHRFRGHEEREAGFRSVLRERFPDLT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 219 IVELREIRDDRERAFEEAAALLKRHPDLAGIYNIGAGNSGIGQALAEAGKADSIIFVGHELTEHSKRLLLSGVMDAVIDQ 298
Cdd:cd06307  160 VLEVLEGLDDDELAYELLRELLARHPDLVGIYNAGGGNEGIARALREAGRARRVVFIGHELTPETRRLLRDGTIDAVIDQ 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 504341065 299 NPRVEAREALSML--DCAVRGKPIDYHPPRLQVIFR 332
Cdd:cd06307  240 DPELQARRAIEVLlaHLGGKGPAPPQPPIPIEIITR 275
HTH_LacI cd01392
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ...
7-46 2.49e-14

Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; HTH-DNA binding domain of the LacI (lactose operon repressor) family of bacterial transcriptional regulators and their putative homologs found in plants. The LacI family has more than 500 members distributed among almost all bacterial species. The monomeric proteins of the LacI family contain common structural features that include a small DNA-binding domain with a helix-turn-helix motif in the N-terminus, a regulatory ligand-binding domain which exhibits the type I periplasmic binding protein fold in the C-terminus for oligomerization and for effector binding, and an approximately 18-amino acid linker connecting these two functional domains. In LacI-like transcriptional regulators, the ligands are monosaccharides including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars, with a few exceptions. When the C-terminal domain of the LacI family repressor binds its ligand, it undergoes a conformational change which affects the DNA-binding affinity of the repressor. In Escherichia coli, LacI represses transcription by binding with high affinity to the lac operon at a specific operator DNA sequence until it interacts with the physiological inducer allolactose or a non-degradable analog IPTG (isopropyl-beta-D-thiogalactopyranoside). Induction of the repressor lowers its affinity for the operator sequence, thereby allowing transcription of the lac operon structural genes (lacZ, lacY, and LacA). The lac repressor occurs as a tetramer made up of two functional dimers. Thus, two DNA binding domains of a dimer are required to bind the inverted repeat sequences of the operator DNA binding sites.


:

Pssm-ID: 143331 [Multi-domain]  Cd Length: 52  Bit Score: 66.28  E-value: 2.49e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 504341065   7 DIAREAGVSSATVDRVLNNRSGVKDRTREIVMNAARRLGY 46
Cdd:cd01392    2 DIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGY 41
 
Name Accession Description Interval E-value
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
61-332 8.44e-106

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: 310.65  E-value: 8.44e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  61 RLDFVLPAGTNTFVANLLRQLQTQATARPDLDVRVHS--IEGFNPDTLAGTLQELRGETMGVGVIALDHPTVREAMRSLA 138
Cdd:cd06307    1 RFGFLLPSPENPFYELLRRAIEAAAAALRDRRVRLRIhfVDSLDPEALAAALRRLAAGCDGVALVAPDHPLVRAAIDELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 139 SSGVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGRgSKGKIALFAGSLSYRGHEEREMGFRHIIADEFPALE 218
Cdd:cd06307   81 ARGIPVVTLVSDLPGSRRLAYVGIDNRAAGRTAAWLMGRFLGR-RPGKVLVILGSHRFRGHEEREAGFRSVLRERFPDLT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 219 IVELREIRDDRERAFEEAAALLKRHPDLAGIYNIGAGNSGIGQALAEAGKADSIIFVGHELTEHSKRLLLSGVMDAVIDQ 298
Cdd:cd06307  160 VLEVLEGLDDDELAYELLRELLARHPDLVGIYNAGGGNEGIARALREAGRARRVVFIGHELTPETRRLLRDGTIDAVIDQ 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 504341065 299 NPRVEAREALSML--DCAVRGKPIDYHPPRLQVIFR 332
Cdd:cd06307  240 DPELQARRAIEVLlaHLGGKGPAPPQPPIPIEIITR 275
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
48-335 2.56e-58

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: 190.52  E-value: 2.56e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  48 SPAAHNASAEGRVRLDFVLPAGTNTFVANLLRQLQTQAtARPDLDVRVHSiEGFNPDTLAGTLQELRgeTMGVGVIAL-- 125
Cdd:COG1879   22 AAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAA-KELGVELIVVD-AEGDAAKQISQIEDLI--AQGVDAIIVsp 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 126 -DHPTVREAMRSLASSGVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGRgsKGKIALFAGSLSYRGHEEREM 204
Cdd:COG1879   98 vDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGG--KGKVAILTGSPGAPAANERTD 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 205 GFRHIIAdEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYNI-GAGNSGIGQALAEAGKADSIIFVGHELTEHS 283
Cdd:COG1879  176 GFKEALK-EYPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAAnDGMALGAAQALKAAGRKGDVKVVGFDGSPEA 254
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504341065 284 KRLLLSGVMDAVIDQNPRVEAREALSMLDCAVRGKPI-DYHPPRLQVIFRENI 335
Cdd:COG1879  255 LQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEVpKEILTPPVLVTKENV 307
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
64-319 3.18e-44

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: 152.46  E-value: 3.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065   64 FVLPAGTNTFVANLLRQLQTQATARPDlDVRVHSIEGFNPDTLAGTLQELRgeTMGVGVIAL---DHPTVREAMRSLASS 140
Cdd:pfam13407   3 VVPKSTGNPFFQAAEEGAEEAAKELGG-EVIVVGPAEADAAEQVAQIEDAI--AQGVDAIIVapvDPTALAPVLKKAKDA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  141 GVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGrgSKGKIALFAGSLSYRGHEEREMGFRHIIADEFPALEIV 220
Cdd:pfam13407  80 GIPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEALG--GKGKVAILSGSPGDPNANERIDGFKKVLKEKYPGIKVV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  221 ELRE-IRDDRERAFEEAAALLKRHPD-LAGIYNIGAGNS-GIGQALAEAGKADSIIFVGHELTEHSKRLLLSGVMDAVID 297
Cdd:pfam13407 158 AEVEgTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMAgGAAQALEAAGLAGKVVVTGFDATPEALEAIKDGTIDATVL 237
                         250       260
                  ....*....|....*....|..
gi 504341065  298 QNPRVEAREALSMLDCAVRGKP 319
Cdd:pfam13407 238 QDPYGQGYAAVELAAALLKGKK 259
HTH_LacI cd01392
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ...
7-46 2.49e-14

Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; HTH-DNA binding domain of the LacI (lactose operon repressor) family of bacterial transcriptional regulators and their putative homologs found in plants. The LacI family has more than 500 members distributed among almost all bacterial species. The monomeric proteins of the LacI family contain common structural features that include a small DNA-binding domain with a helix-turn-helix motif in the N-terminus, a regulatory ligand-binding domain which exhibits the type I periplasmic binding protein fold in the C-terminus for oligomerization and for effector binding, and an approximately 18-amino acid linker connecting these two functional domains. In LacI-like transcriptional regulators, the ligands are monosaccharides including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars, with a few exceptions. When the C-terminal domain of the LacI family repressor binds its ligand, it undergoes a conformational change which affects the DNA-binding affinity of the repressor. In Escherichia coli, LacI represses transcription by binding with high affinity to the lac operon at a specific operator DNA sequence until it interacts with the physiological inducer allolactose or a non-degradable analog IPTG (isopropyl-beta-D-thiogalactopyranoside). Induction of the repressor lowers its affinity for the operator sequence, thereby allowing transcription of the lac operon structural genes (lacZ, lacY, and LacA). The lac repressor occurs as a tetramer made up of two functional dimers. Thus, two DNA binding domains of a dimer are required to bind the inverted repeat sequences of the operator DNA binding sites.


Pssm-ID: 143331 [Multi-domain]  Cd Length: 52  Bit Score: 66.28  E-value: 2.49e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 504341065   7 DIAREAGVSSATVDRVLNNRSGVKDRTREIVMNAARRLGY 46
Cdd:cd01392    2 DIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGY 41
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
4-46 7.73e-14

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 65.69  E-value: 7.73e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 504341065     4 TLIDIAREAGVSSATVDRVLNNRSGVKDRTREIVMNAARRLGY 46
Cdd:smart00354   2 TIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGY 44
PRK09701 PRK09701
D-allose transporter substrate-binding protein;
158-320 1.05e-12

D-allose transporter substrate-binding protein;


Pssm-ID: 182037 [Multi-domain]  Cd Length: 311  Bit Score: 67.59  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 158 GYIGIDNRAAGRL-AGYLLGRFLGRGskGKIALFAGSLSYRGHEEREMGFRHIIADEfPALEIVELREIRDDRERAFEEA 236
Cdd:PRK09701 131 AFVTTDNVAVGAKgASFIIDKLGAEG--GEVAIIEGKAGNASGEARRNGATEAFKKA-SQIKLVASQPADWDRIKALDVA 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 237 AALLKRHPDLAGIYnigAGNS----GIGQALAEAGKADSIIFVGHELTEHSKRLLLSGVMDAVIDQNPRVEAREALSMLD 312
Cdd:PRK09701 208 TNVLQRNPNIKAIY---CANDtmamGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTATVAQNPADIGATGLKLMV 284

                 ....*...
gi 504341065 313 CAVRGKPI 320
Cdd:PRK09701 285 DAEKSGKV 292
LacI pfam00356
Bacterial regulatory proteins, lacI family;
4-46 1.30e-12

Bacterial regulatory proteins, lacI family;


Pssm-ID: 306791 [Multi-domain]  Cd Length: 46  Bit Score: 61.50  E-value: 1.30e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 504341065    4 TLIDIAREAGVSSATVDRVLNNRSGVKDRTREIVMNAARRLGY 46
Cdd:pfam00356   1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNY 43
PRK10401 PRK10401
HTH-type transcriptional regulator GalS;
4-56 3.39e-10

HTH-type transcriptional regulator GalS;


Pssm-ID: 236681 [Multi-domain]  Cd Length: 346  Bit Score: 60.56  E-value: 3.39e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504341065   4 TLIDIAREAGVSSATVDRVLNNRSGVKDRTREIVMNAARRLGYlSPAAhNASA 56
Cdd:PRK10401   3 TIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGY-RPNA-NAQA 53
 
Name Accession Description Interval E-value
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
61-332 8.44e-106

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: 310.65  E-value: 8.44e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  61 RLDFVLPAGTNTFVANLLRQLQTQATARPDLDVRVHS--IEGFNPDTLAGTLQELRGETMGVGVIALDHPTVREAMRSLA 138
Cdd:cd06307    1 RFGFLLPSPENPFYELLRRAIEAAAAALRDRRVRLRIhfVDSLDPEALAAALRRLAAGCDGVALVAPDHPLVRAAIDELA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 139 SSGVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGRgSKGKIALFAGSLSYRGHEEREMGFRHIIADEFPALE 218
Cdd:cd06307   81 ARGIPVVTLVSDLPGSRRLAYVGIDNRAAGRTAAWLMGRFLGR-RPGKVLVILGSHRFRGHEEREAGFRSVLRERFPDLT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 219 IVELREIRDDRERAFEEAAALLKRHPDLAGIYNIGAGNSGIGQALAEAGKADSIIFVGHELTEHSKRLLLSGVMDAVIDQ 298
Cdd:cd06307  160 VLEVLEGLDDDELAYELLRELLARHPDLVGIYNAGGGNEGIARALREAGRARRVVFIGHELTPETRRLLRDGTIDAVIDQ 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 504341065 299 NPRVEAREALSML--DCAVRGKPIDYHPPRLQVIFR 332
Cdd:cd06307  240 DPELQARRAIEVLlaHLGGKGPAPPQPPIPIEIITR 275
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
48-335 2.56e-58

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: 190.52  E-value: 2.56e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  48 SPAAHNASAEGRVRLDFVLPAGTNTFVANLLRQLQTQAtARPDLDVRVHSiEGFNPDTLAGTLQELRgeTMGVGVIAL-- 125
Cdd:COG1879   22 AAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAA-KELGVELIVVD-AEGDAAKQISQIEDLI--AQGVDAIIVsp 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 126 -DHPTVREAMRSLASSGVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGRgsKGKIALFAGSLSYRGHEEREM 204
Cdd:COG1879   98 vDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGG--KGKVAILTGSPGAPAANERTD 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 205 GFRHIIAdEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYNI-GAGNSGIGQALAEAGKADSIIFVGHELTEHS 283
Cdd:COG1879  176 GFKEALK-EYPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAAnDGMALGAAQALKAAGRKGDVKVVGFDGSPEA 254
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504341065 284 KRLLLSGVMDAVIDQNPRVEAREALSMLDCAVRGKPI-DYHPPRLQVIFRENI 335
Cdd:COG1879  255 LQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKEVpKEILTPPVLVTKENV 307
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
64-319 3.18e-44

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: 152.46  E-value: 3.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065   64 FVLPAGTNTFVANLLRQLQTQATARPDlDVRVHSIEGFNPDTLAGTLQELRgeTMGVGVIAL---DHPTVREAMRSLASS 140
Cdd:pfam13407   3 VVPKSTGNPFFQAAEEGAEEAAKELGG-EVIVVGPAEADAAEQVAQIEDAI--AQGVDAIIVapvDPTALAPVLKKAKDA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  141 GVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGrgSKGKIALFAGSLSYRGHEEREMGFRHIIADEFPALEIV 220
Cdd:pfam13407  80 GIPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEALG--GKGKVAILSGSPGDPNANERIDGFKKVLKEKYPGIKVV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  221 ELRE-IRDDRERAFEEAAALLKRHPD-LAGIYNIGAGNS-GIGQALAEAGKADSIIFVGHELTEHSKRLLLSGVMDAVID 297
Cdd:pfam13407 158 AEVEgTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMAgGAAQALEAAGLAGKVVVTGFDATPEALEAIKDGTIDATVL 237
                         250       260
                  ....*....|....*....|..
gi 504341065  298 QNPRVEAREALSMLDCAVRGKP 319
Cdd:pfam13407 238 QDPYGQGYAAVELAAALLKGKK 259
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
64-321 5.08e-33

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: 123.06  E-value: 5.08e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  64 FVLPAGTNTFVANLLRQLQTQAtARPDLDVRVHSIEGfNPDTLAGTLQELRgeTMGVGVIAL---DHPTVREAMRSLASS 140
Cdd:cd01536    4 VVVKDLTNPFWVAVKKGAEAAA-KELGVELVVLDAQG-DVAKQISQIEDLI--AQGVDAIIIapvDSEALVPAVKKANAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 141 GVPIVTLVSDI-LHVPRTGYIGIDNRAAGRLAGYLLGRFLGrgSKGKIALFAGSLSYRGHEEREMGFRHIIAdEFPALEI 219
Cdd:cd01536   80 GIPVVAVDTDIdGGGDVVAFVGTDNYEAGKLAGEYLAEALG--GKGKVAILEGPPGSSTAIDRTKGFKEALK-KYPDIEI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 220 VELREIRDDRERAFEEAAALLKRHPDLAGIYNIGAGN-SGIGQALAEAGKADSIIFVGHELTEHSKRLLLSGVMDAVIDQ 298
Cdd:cd01536  157 VAEQPANWDRAKALTVTENLLQANPDIDAVFAANDDMaLGAAEALKAAGRTGDIKIVGVDGTPEALKAIKDGELDATVAQ 236
                        250       260
                 ....*....|....*....|...
gi 504341065 299 NPRVEAREALSMLDCAVRGKPID 321
Cdd:cd01536  237 DPYLQGYLAVEAAVKLLNGEKVP 259
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
119-300 6.70e-32

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: 120.38  E-value: 6.70e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 119 GVGVIALDHPTVREAMRSLASSGVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGRGskGKIALFAGSLSYRG 198
Cdd:cd06314   59 GIAISPNDPEAVTPVINKAADKGIPVITFDSDAPDSKRLAYIGTDNYEAGREAGELMKKALPGG--GKVAIITGGLGADN 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 199 HEEREMGFRHIIADEfPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYNIGAGNS-GIGQALAEAGKADSIIFVGH 277
Cdd:cd06314  137 LNERIQGFKDALKGS-PGIEIVDPLSDNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGpAIAAALKDAGKVGKVKIVGF 215
                        170       180
                 ....*....|....*....|...
gi 504341065 278 ELTEHSKRLLLSGVMDAVIDQNP 300
Cdd:cd06314  216 DTLPETLQGIKDGVIAATVGQRP 238
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
1-329 8.11e-32

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 121.46  E-value: 8.11e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065   1 MRSTLIDIAREAGVSSATVDRVLNNRSGVKDRTREIVMNAARRLGYL-SPAAHN-ASAEGRVrLDFVLPAGTNTFVANLL 78
Cdd:COG1609    2 KRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRpNAAARSlRTGRTRT-IGVVVPDLSNPFFAELL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  79 RQLQTQATARpDLDVRVHSIEGfNPDTLAGTLQELRGetMGV-GVIALDHPTVREAMRSLASSGVPIVtLVSDILHVPRT 157
Cdd:COG1609   81 RGIEEAARER-GYQLLLANSDE-DPEREREALRLLLS--RRVdGLILAGSRLDDARLERLAEAGIPVV-LIDRPLPDPGV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 158 GYIGIDNRAAGRLAG-YLlgrfLGRGSKgKIALFAGSLSYRGHEEREMGFRHIIAD---EFPALEIVelrEIRDDRERAF 233
Cdd:COG1609  156 PSVGVDNRAGARLATeHL----IELGHR-RIAFIGGPADSSSARERLAGYREALAEaglPPDPELVV---EGDFSAESGY 227
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 234 EEAAALLKRHPDLAGIYnigAGNSGIG----QALAEAGKA---D-SII-FVGHELTEHSKRLLlsgvmdAVIDQNPRVEA 304
Cdd:COG1609  228 EAARRLLARGPRPTAIF---CANDLMAlgalRALREAGLRvpeDvSVVgFDDIPLARYLTPPL------TTVRQPIEEMG 298
                        330       340
                 ....*....|....*....|....*....
gi 504341065 305 REALSMLDCAVRGKPIDYH----PPRLQV 329
Cdd:COG1609  299 RRAAELLLDRIEGPDAPPErvllPPELVV 327
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
119-322 2.80e-26

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: 105.50  E-value: 2.80e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 119 GVGVIALDHPTVREAMRSLASSGVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLgrGSKGKIALFAGSLSYrG 198
Cdd:cd19969   59 GIAVSAIDPEALTPTINKAVDAGIPVVTFDSDAPESKRISYVGTDNYEAGYAAAEKLAELL--GGKGKVAVLTGPGQP-N 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 199 HEEREMGFRHIIAdEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIY-NIGAGNSGIGQALAEAGKADSIIFVGH 277
Cdd:cd19969  136 HEERVEGFKEAFA-EYPGIEVVAVGDDNDDPEKAAQNTSALLQAHPDLVGIFgVDASGGVGAAQAVREAGKTGKVKIVAF 214
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 504341065 278 ELTEHSKRLLLSGVMDAVIDQNPRVEAREALSMLDCAVRGKPIDY 322
Cdd:cd19969  215 DDDPETLDLIKDGVIDASIAQRPWMMGYWSLQFLYDLANGLVKDA 259
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
116-321 8.81e-25

periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis; Periplasmic allose-binding domain of bacterial transport systems that function as a primary receptor of active transport and chemotaxis. The members of this group are belonging to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Like other periplasmic receptors of the ABC-type transport systems, the allose-binding protein consists of two alpha/beta domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding.


Pssm-ID: 380543 [Multi-domain]  Cd Length: 283  Bit Score: 101.57  E-value: 8.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 116 ETM------GVGVIALDHPTVREAMRSLASSGVPIVTL-------VSDILHVPRTGYIGIDNRAAGRLAG-YLLGRFlgr 181
Cdd:cd06320   51 ETMlnkgydAILVSPISDTNLIPPIEKANKKGIPVINLddavdadALKKAGGKVTSFIGTDNVAAGALAAeYIAEKL--- 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 182 GSKGKIALFAG-SLSYRGhEEREMGFRHIIAdEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYnigAGNS--- 257
Cdd:cd06320  128 PGGGKVAIIEGlPGNAAA-EARTKGFKETFK-KAPGLKLVASQPADWDRTKALDAATAILQAHPDLKGIY---AANDtma 202
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504341065 258 -GIGQALAEAGKADSIIFVGHELTEHSKRLLLSGVMDAVIDQNPRVEAREALSMLDCAVRGKPID 321
Cdd:cd06320  203 lGAVEAVKAAGKTGKVLVVGTDGIPEAKKSIKAGELTATVAQYPYLEGAMAVEAALRLLQGQKVP 267
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
122-320 1.05e-24

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: 100.88  E-value: 1.05e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 122 VIALDHPTVREAMRSLASSGVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGRgsKGKIALFAGSLSYRGHEE 201
Cdd:cd06310   63 VAPLDSEDLVDPLKDAKDKGIPVIVIDSGIKGDAYLSYIATDNYAAGRLAAQKLAEALGG--KGKVAVLSLTAGNSTTDQ 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 202 REMGFRHIIADEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIY---NIGAgnSGIGQALAEAGKADSIIFVGHE 278
Cdd:cd06310  141 REEGFKEYLKKHPGGIKVLASQYAGSDYAKAANETEDLLGKYPDIDGIFatnEITA--LGAAVAIKSRKLSGQIKIVGFD 218
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 504341065 279 LTEHSKRLLLSGVMDAVIDQNPRVEAREALSMLDCAVRGKPI 320
Cdd:cd06310  219 SQEELLDALKNGKIDALVVQNPYEIGYEGIKLALKLLKGEEV 260
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
138-300 4.96e-24

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


Pssm-ID: 380663 [Multi-domain]  Cd Length: 277  Bit Score: 99.23  E-value: 4.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 138 ASSGVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGR--GSKGKIALFAGSLSYRGHEEREMGFRHIIADEFP 215
Cdd:cd20008   78 ADAGIPVVLVDSGANTDDYDAFLATDNVAAGALAADELAELLKAsgGGKGKVAIISFQAGSQTLVDREEGFRDYIKEKYP 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 216 ALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYniGAGNS---GIGQALAEAGKADSIIFVGHELTEHSKRLLLSGVM 292
Cdd:cd20008  158 DIEIVDVQYSDGDIAKALNQTTDLLTANPDLVGIF--GANNPsavGVAQALAEAGKAGKIVLVGFDSSPDEVALLKSGVI 235

                 ....*...
gi 504341065 293 DAVIDQNP 300
Cdd:cd20008  236 KALVVQDP 243
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
119-300 1.06e-23

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: 380660 [Multi-domain]  Cd Length: 274  Bit Score: 98.47  E-value: 1.06e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 119 GVGVIALDHPTVREAMRSLASSGVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGrgSKGKIALFAGSLSYRG 198
Cdd:cd20005   60 AIALAALDTNALLPQLEKAKEKGIPVVTFDSGVPSDLPLATVATDNYAAGALAADHLAELIG--GKGKVAIVAHDATSET 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 199 HEEREMGFRHIIADEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIY--NIGAGNsGIGQALAEAGKADSIIFVG 276
Cdd:cd20005  138 GIDRRDGFKDEIKEKYPDIKVVNVQYGVGDHAKAADIAKAILQANPDLKGIYatNEGAAI-GVANALKEMGKLGKIKVVG 216
                        170       180
                 ....*....|....*....|....
gi 504341065 277 HELTEHSKRLLLSGVMDAVIDQNP 300
Cdd:cd20005  217 FDSGEAQIDAIKNGVIAGSVTQNP 240
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
122-321 3.41e-22

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: 94.22  E-value: 3.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 122 VIA-LDHPTVREAMRSLASSGVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGRgsKGKIALF---AGSLSYR 197
Cdd:cd20004   62 VLApLDRKALVAPVERARAQGIPVVIIDSDLGGDAVISFVATDNYAAGRLAAKRMAKLLNG--KGKVALLrlaKGSASTT 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 198 gheEREMGFRHIIADEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYnigAGN--SGIG--QALAEAGKADSII 273
Cdd:cd20004  140 ---DRERGFLEALKKLAPGLKVVDDQYAGGTVGEARSSAENLLNQYPDVDGIF---TPNesTTIGalRALRRLGLAGKVK 213
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 504341065 274 FVGHELTEHSKRLLLSGVMDAVIDQNPRVEAREALSMLDCAVRGKPID 321
Cdd:cd20004  214 FIGFDASDLLLDALRAGEISALVVQDPYRMGYLGVKTAVAALRGKPVP 261
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
122-322 6.09e-21

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: 90.76  E-value: 6.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 122 VIAldhPTVREAM----RSLASSGVPIVTLVSDIL--HVPrTGYIGIDNRAAGRLAGYLLGRFLGRgsKGKIALFAGSLS 195
Cdd:cd20007   61 LIA---PTDPQALiaplKRAADAGIKVVTVDTTLGdpSFV-LSQIASDNVAGGALAAEALAELIGG--KGKVLVINSTPG 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 196 YRGHEEREMGFRHIIAdEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYNIgAGNSGIG--QALAEAGKADSII 273
Cdd:cd20007  135 VSTTDARVKGFAEEMK-KYPGIKVLGVQYSENDPAKAASIVAAALQANPDLAGIFGT-NTFSAEGaaAALRNAGKTGKVK 212
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 504341065 274 FVGHELTEHSKRLLLSGVMDAVIDQNPRVEAREALSMLDCAVRGKPIDY 322
Cdd:cd20007  213 VVGFDASPAQVEQLKAGTIDALIAQKPAEIGYLAVEQAVAALTGKPVPK 261
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
124-300 1.09e-18

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: 84.57  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 124 ALDHPTVREAMRSLASSGVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLgrGSKGKIALFAGSLSYRGHEERE 203
Cdd:cd20006   67 ASDYDRLVEAVERAKKAGIPVITIDSPVNSKKADSFVATDNYEAGKKAGEKLASLL--GEKGKVAIVSFVKGSSTAIERE 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 204 MGFRHIIAdEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIynIG---AGNSGIGQALAEAGKADSIIFVGHELT 280
Cdd:cd20006  145 EGFKQALA-EYPNIKIVETEYCDSDEEKAYEITKELLSKYPDINGI--VAlneQSTLGAARALKELGLGGKVKVVGFDSS 221
                        170       180
                 ....*....|....*....|
gi 504341065 281 EHSKRLLLSGVMDAVIDQNP 300
Cdd:cd20006  222 VEEIQLLEEGIIDALVVQNP 241
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
128-323 3.08e-18

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: 82.98  E-value: 3.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 128 PTVREAMRSlassGVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGRgsKGKIALFAGSLSYRGHEEREMGFR 207
Cdd:cd06308   72 PVVKKAYDA----GIPVIVLDRKVSGDDYTAFIGADNVEIGRQAGEYIAELLNG--KGNVVEIQGLPGSSPAIDRHKGFL 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 208 HIIAdEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYnigAGN----SGIGQALAEAGKADSIIFVGHE-LTEH 282
Cdd:cd06308  146 EAIA-KYPGIKIVASQDGDWLRDKAIKVMEDLLQAHPDIDAVY---AHNdemaLGAYQALKKAGREKEIKIIGVDgLPEA 221
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 504341065 283 SKRLLLSGVMDAVIdQNPrVEAREALSMLDCAVRGKPIDYH 323
Cdd:cd06308  222 GEKAVKDGILAATF-LYP-TGGKEAIEAALKILNGEKVPKE 260
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
119-320 1.83e-17

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: 80.78  E-value: 1.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 119 GVGVIAL---DHPTVREAMRSLASSGVPIVTLVSDILHVPRTGYIGIDNRAAGRLAG-YLLGRFLGRGSKGKIALFAGSL 194
Cdd:cd06322   55 GVDAIILapvDSGGIVPAIEAANEAGIPVFTVDVKADGAKVVTHVGTDNYAGGKLAGeYALKALLGGGGKIAIIDYPEVE 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 195 SYRgheEREMGFRHIIADEfPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYNIGaGNSGIG--QALAEAGKADSI 272
Cdd:cd06322  135 SVV---LRVNGFKEAIKKY-PNIEIVAEQPGDGRREEALAATEDMLQANPDLDGIFAIG-DPAALGalTAIESAGKEDKI 209
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 504341065 273 IFVGHELTEHSKRLLL-SGVMDAVIDQNPRVEAREALSMLDCAVRGKPI 320
Cdd:cd06322  210 KVIGFDGNPEAIKAIAkGGKIKADIAQQPDKIGQETVEAIVKYLAGETV 258
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
119-329 1.23e-16

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: 78.57  E-value: 1.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 119 GVGVIALDHPTVREAMRSLASSGVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGR--GSKGKIALFaGSLSY 196
Cdd:cd06317   58 AIILDAIDVNGSIPAIKRASEAGIPVIAYDAVIPSDFQAAQVGVDNLEGGKEIGKYAADYIKAelGGQAKIGVV-GALSS 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 197 RGHEEREMGFRHIIADEfPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYNIGAGNS-GIGQALAEAGKADSIIFV 275
Cdd:cd06317  137 LIQNQRQKGFEEALKAN-PGVEIVATVDGQNVQEKALSAAENLLTANPDLDAIYATGEPALlGAVAAVRSQGRQGKIKVF 215
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504341065 276 GHELTEHSKRLLL-SGVMDAVIDQNPRVEAREALSMLDCAVRGKPIdyhPPRLQV 329
Cdd:cd06317  216 GWDLTKQAIFLGIdEGVLQAVVQQDPEKMGYEAVKAAVKAIKGEDV---EKTIDV 267
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
128-321 3.23e-16

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: 77.29  E-value: 3.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 128 PTVREAMRSlassGVPIVT---------LVSDILHVPrtgYIGIDNRAAGRLAGYLLGRFLGRGskGKIALFAGSLSYRG 198
Cdd:cd19970   74 PVLKKAVDA----GIAVINidnrldadaLKEGGINVP---FVGPDNRQGAYLAGDYLAKKLGKG--GKVAIIEGIPGADN 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 199 HEEREMGFRHIIADEfpALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYnigAGNS----GIGQALAEAGKADSIIF 274
Cdd:cd19970  145 AQQRKAGFLKAFEEA--GMKIVASQSANWEIDEANTVAANLLTAHPDIRGIL---CANDnmalGAIKAVDAAGKAGKVLV 219
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 504341065 275 VGHELTEHSKRLLLSGVMDAVIDQNPRVEAREALSMLDCAVRGKPID 321
Cdd:cd19970  220 VGFDNIPAVRPLLKDGKMLATIDQHPAKQAVYGIEYALKMLNGEEVP 266
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
117-321 1.51e-15

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: 75.31  E-value: 1.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 117 TMGVGVIAL---DHPTVREAMRSLASSGVPIV---TLVSDILHVprTGYIGIDNRAAGRLAG-YLLGRFlgrGSKGKIAL 189
Cdd:cd19971   53 NQGVDAIFLnpvDSEGIRPALEAAKEAGIPVInvdTPVKDTDLV--DSTIASDNYNAGKLCGeDMVKKL---PEGAKIAV 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 190 ----FAGSLSyrgheEREMGFRHIIADeFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYnigAGN--SGIG--Q 261
Cdd:cd19971  128 ldhpTAESCV-----DRIDGFLDAIKK-NPKFEVVAQQDGKGQLEVAMPIMEDILQAHPDLDAVF---ALNdpSALGalA 198
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 262 ALAEAGKADSIIFVGHELTEHSKRLLLSGVMDAVIDQNPRVEAREALSMLDCAVRGKPID 321
Cdd:cd19971  199 ALKAAGKLGDILVYGVDGSPDAKAAIKDGKMTATAAQSPIEIGKKAVETAYKILNGEKVE 258
PBP1_ABC_sugar_binding-like cd06316
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
100-274 4.27e-15

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


Pssm-ID: 380539 [Multi-domain]  Cd Length: 294  Bit Score: 74.58  E-value: 4.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 100 GFNPDTLAGTLQELRgeTMGVGVI---ALDHPTVREAMRSLASSGVPIVTlvsdILHVPrTGY---------IGIDNRAA 167
Cdd:cd06316   39 NFDPAKQITDLETLI--ALKPDIIisiPVDPVATAAAYKKVADAGIKLVF----MDNVP-DGLeagkdyvsvVSSDNRGN 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 168 GRLAGYLLGRFLGrgSKGKIALFAGSLSYRGHEEREMGFRHIIADEFPALEIVELREIrDDRERAFEEAAALLKRHPDLA 247
Cdd:cd06316  112 GQIAAELLAEAIG--GKGKVGIIYHDADFYATNQRDKAFKDTLKEKYPDIKIVAEQGF-ADPNDAEEVASAMLTANPDID 188
                        170       180
                 ....*....|....*....|....*...
gi 504341065 248 GIYNIGAGNS-GIGQALAEAGKADSIIF 274
Cdd:cd06316  189 GIYVSWDTPAlGVISALRAAGRSDIKIT 216
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
122-321 7.68e-15

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: 73.48  E-value: 7.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 122 VIALDHPTVREAMRSLASSGVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGRgsKGKIALFAGSLSYRGHEE 201
Cdd:cd06323   61 INPTDSDAVSPAVEEANEAGIPVITVDRSVTGGKVVSHIASDNVAGGEMAAEYIAKKLGG--KGKVVELQGIPGTSAARE 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 202 REMGFrHIIADEFPALEIVElREIRD-DRERAFEEAAALLKRHPDLAGIYnigAGNS----GIGQALAEAGKADsIIFVG 276
Cdd:cd06323  139 RGKGF-HNAIAKYPKINVVA-SQTADfDRTKGLNVMENLLQAHPDIDAVF---AHNDemalGAIQALKAAGRKD-VIVVG 212
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 504341065 277 HELTEHSKRLLLSGVMDAVIDQNPRVEAREALSMLDCAVRGKPID 321
Cdd:cd06323  213 FDGTPDAVKAVKDGKLAATVAQQPEEMGAKAVETADKYLKGEKVP 257
HTH_LacI cd01392
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ...
7-46 2.49e-14

Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; HTH-DNA binding domain of the LacI (lactose operon repressor) family of bacterial transcriptional regulators and their putative homologs found in plants. The LacI family has more than 500 members distributed among almost all bacterial species. The monomeric proteins of the LacI family contain common structural features that include a small DNA-binding domain with a helix-turn-helix motif in the N-terminus, a regulatory ligand-binding domain which exhibits the type I periplasmic binding protein fold in the C-terminus for oligomerization and for effector binding, and an approximately 18-amino acid linker connecting these two functional domains. In LacI-like transcriptional regulators, the ligands are monosaccharides including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars, with a few exceptions. When the C-terminal domain of the LacI family repressor binds its ligand, it undergoes a conformational change which affects the DNA-binding affinity of the repressor. In Escherichia coli, LacI represses transcription by binding with high affinity to the lac operon at a specific operator DNA sequence until it interacts with the physiological inducer allolactose or a non-degradable analog IPTG (isopropyl-beta-D-thiogalactopyranoside). Induction of the repressor lowers its affinity for the operator sequence, thereby allowing transcription of the lac operon structural genes (lacZ, lacY, and LacA). The lac repressor occurs as a tetramer made up of two functional dimers. Thus, two DNA binding domains of a dimer are required to bind the inverted repeat sequences of the operator DNA binding sites.


Pssm-ID: 143331 [Multi-domain]  Cd Length: 52  Bit Score: 66.28  E-value: 2.49e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 504341065   7 DIAREAGVSSATVDRVLNNRSGVKDRTREIVMNAARRLGY 46
Cdd:cd01392    2 DIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGY 41
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
64-276 3.40e-14

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: 71.63  E-value: 3.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  64 FVLPAGTNTFVANLLRQLQTQATARPDLDVRVHSIEgfNPDTLAGTLQELRgeTMGVGVIAL---DHPTVREAMRSLASS 140
Cdd:cd06311    4 ISIPSADHGWTAGVAYYAEKQAKELADLEYKLVTSS--NANEQVSQLEDLI--AQKVDAIVIlpqDSEELTVAAQKAKDA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 141 GVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGrgSKGKIALFAGSLSYRGHEEREMGFRHIIAdEFPALEIV 220
Cdd:cd06311   80 GIPVVNFDRGLNVLIYDLYVAGDNPGMGVVSAEYIGKKLG--GKGNVVVLEVPSSGSVNEERVAGFKEVIK-GNPGIKIL 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504341065 221 ELREIRDDRERAFEEAAALLKRHPDLAGIYNIGAGNS-GIGQALAEAGKADSIIFVG 276
Cdd:cd06311  157 AMQAGDWTREDGLKVAQDILTKNKKIDAVWAADDDMAiGVLQAIKEAGRTDIKVMTG 213
PBP1_LsrB_Quorum_Sensing-like cd06302
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ...
128-320 5.00e-14

periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs; Periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that 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 LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.


Pssm-ID: 380525 [Multi-domain]  Cd Length: 296  Bit Score: 71.50  E-value: 5.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 128 PTVREAMrslaSSGVPIVTLVSDILHVPRTGYIgidNRAAGRLAGYLLGRFLGR--GSKGKIALFAGSLSYRGHEEREMG 205
Cdd:cd06302   72 PVLKKAK----DAGIKVITWDSDAPPSARDYFV---NQADDEGLGEALVDSLAKeiGGKGKVAILSGSLTATNLNAWIKA 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 206 FRHIIADEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYNI-GAGNSGIGQALAEAGKADSIIFVGHELTEHSK 284
Cdd:cd06302  145 MKEYLKSKYPDIELVDTYYTDDDQQKAYTQAQNLIQAYPDLKGIIGVsTTAPPAAAQAVEEAGKTGKVAVTGIGLPNTAR 224
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 504341065 285 RLLLSGVMDAVIDQNPRVEAREALSMLDCAVRGKPI 320
Cdd:cd06302  225 PYLKDGSVKEGVLWDPAKLGYLTVYAAYQLLKGKGF 260
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
4-46 7.73e-14

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 65.69  E-value: 7.73e-14
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 504341065     4 TLIDIAREAGVSSATVDRVLNNRSGVKDRTREIVMNAARRLGY 46
Cdd:smart00354   2 TIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGY 44
PBP1_LsrB_Quorum_Sensing-like cd20002
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
162-301 2.40e-13

ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that 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 LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.


Pssm-ID: 380657  Cd Length: 295  Bit Score: 69.27  E-value: 2.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 162 IDNRAAGRLAGYLLGRFLGrgSKGKIALFAGSLSYRGHEER-EMGFRHIiADEFPALEIVELR-EIRDDRERAFEEAAAL 239
Cdd:cd20002  102 IDNEKFGEAQMELLAKEMG--GKGEYAIFVGSLTVPLHNLWaDAAVEYQ-KEKYPNMKQVTDRiPGGEDVDVSRQTTLEL 178
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504341065 240 LKRHPDLAGIYNIG-AGNSGIGQALAEAGKADSIIFVGHELTEHSKRLLLSGVMDAVIDQNPR 301
Cdd:cd20002  179 LKAYPDLKGIISFGsLGPIGAGQALREKGLKGKVAVVGTVIPSQAAAYLKEGSITEGYLWDPA 241
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
64-267 2.41e-13

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: 69.08  E-value: 2.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  64 FVLPAGTNTFVANLLRQLQTQATARpDLDVRVHSIEGfNPDTLAGTLQELRGetMGV-GVIALDHPTVREAMRSLASSGV 142
Cdd:cd06267    4 LIVPDISNPFFAELLRGIEDAARER-GYSLLLCNTDE-DPEREREYLRLLLS--RRVdGIILAPSSLDDELLEELLAAGI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 143 PIVtLVSDILHVPRTGYIGIDNRAAGRLAG-YLLGRflgrGSKgKIALFAGSLSYRGHEEREMGFRHIIADEFPALEIVE 221
Cdd:cd06267   80 PVV-LIDRRLDGLGVDSVVVDNYAGAYLATeHLIEL----GHR-RIAFIGGPLDLSTSRERLEGYRDALAEAGLPVDPEL 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 504341065 222 LREIRDDRERAFEEAAALLKRHPDLAGIYnigAGN--SGIG--QALAEAG 267
Cdd:cd06267  154 VVEGDFSEESGYEAARELLALPPRPTAIF---AANdlMAIGalRALRELG 200
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
119-312 5.09e-13

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: 68.12  E-value: 5.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 119 GVGVIALDhptvreamRSLASSGVPIVTLVSDilhvprtgyigidNRAAGRLAGYLLGRFLGrgSKGKIALFAGSLSYRG 198
Cdd:cd19967   80 GIPVFLID--------REINAEGVAVAQIVSD-------------NYQGAVLLAQYFVKLMG--EKGLYVELLGKESDTN 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 199 HEEREMGFrHIIADEFPALEIVElREIRD-DRERAFEEAAALLKRHPDLAGIYnigAGNS----GIGQALAEAGKADSII 273
Cdd:cd19967  137 AQLRSQGF-HSVIDQYPELKMVA-QQSADwDRTEAFEKMESILQANPDIKGVI---CGNDemalGAIAALKAAGRAGDVI 211
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 504341065 274 FVGHELTEHSKRLLLSGVMDAVIDQNPRVEAREALSMLD 312
Cdd:cd19967  212 IVGFDGSNDVRDAIKEGKISATVLQPAKLIARLAVEQAD 250
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
64-300 5.28e-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: 68.16  E-value: 5.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  64 FVLPAGTNTFVANLLRQLQTQATARpdldvrvhSIEGFNPDTLAGTLQELRGE----TMGVGVIALDhPTVREAMRSL-- 137
Cdd:cd06319    4 YSVYDLDNPFWQIMERGVQAAAEEL--------GYEFVTYDQKNSANEQVTNAndliAQGVDGIIIS-PTNSSAAPTVld 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 138 --ASSGVPIVtlVSDI--LHVPRTGYIGIDNRAAGRLAG-YLLGRFLGRGSK-GKIALFAGSLSYRGHEEREMGFRHIIA 211
Cdd:cd06319   75 laNEAKIPVV--IADIgtGGGDYVSYIISDNYDGGYQAGeYLAEALKENGWGgGSVGIIAIPQSRVNGQARTAGFEDALE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 212 DEfpALEIVELREIRDDR-ERAFEEAAALLKRHPDLAGIYnigAGNS----GIGQALAEAGKADSIIFVGHELTEHSKRL 286
Cdd:cd06319  153 EA--GVEEVALRQTPNSTvEETYSAAQDLLAANPDIKGIF---AQNDqmaqGALQAIEEAGRTGDILVVGFDGDPEALDL 227
                        250
                 ....*....|....
gi 504341065 287 LLSGVMDAVIDQNP 300
Cdd:cd06319  228 IKDGKLDGTVAQQP 241
PBP1_LuxPQ_Quorum_Sensing cd06303
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi ...
122-276 6.70e-13

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: 68.55  E-value: 6.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 122 VIALDHPTVREAMRSLASSGVP------IVTLVSDILHVPRTGYIGIDNRAAGR-LAGYLLGRFLGrgsKGKIALFAGSL 194
Cdd:cd06303   93 IFTLDALRHRRFVEILLDSGKPklilqnITTPLRDWDNHQPLLYVGFDHAEGSRmLAKHFIKIFPE---EGKYAILYLTE 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 195 SYRGHEeREMGFRHIIAdEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYnigAGNSGIG----QALAEAGKAD 270
Cdd:cd06303  170 GYVSDQ-RGDTFIDEVA-RHSNLELVSAYYTDFDRESAREAARALLARHPDLDFIY---ACSTDIAlgaiDALQELGRET 244

                 ....*.
gi 504341065 271 SIIFVG 276
Cdd:cd06303  245 DIMING 250
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
128-300 8.01e-13

monosaccharide ABC transporter substrate binding protein CUT2 family 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: 380620 [Multi-domain]  Cd Length: 272  Bit Score: 67.68  E-value: 8.01e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 128 PTVREAMrslaSSGVPIVTLVSDILHVP--RTGYIGIDNRAAGRLAGYLLGRFLGRGSkGKIALFagsLSYRGH---EER 202
Cdd:cd19965   72 EVIKRAL----DAGIPVVAFNVDAPGGEnaRLAFVGQDLYPAGYVLGKRIAEKFKPGG-GHVLLG---ISTPGQsalEQR 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 203 EMGFRHIIaDEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYNIGA-GNSGIGQALAEAGKADSIIFVGHELTE 281
Cdd:cd19965  144 LDGIKQAL-KEYGRGITYDVIDTGTDLAEALSRIEAYYTAHPDIKAIFATGAfDTAGAGQAIKDLGLKGKVLVGGFDLVP 222
                        170
                 ....*....|....*....
gi 504341065 282 HSKRLLLSGVMDAVIDQNP 300
Cdd:cd19965  223 EVLQGIKAGYIDFTIDQQP 241
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
124-323 9.51e-13

TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria; TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor respiratory system upon trimethylamine N-oxide (TMAO) electron-acceptor binding in bacteria. The Tor respiratory system is consists of three proteins (TorC, TorA, and TorD) and is induced in the presence of TMAO. The TMAO control is tightly regulated by three proteins: TorS, TorT, and TorR. Thus, the disruption of any of these proteins can abolish the Tor respiratory induction. TorT shares homology with the sugar-binding domain of the type 1 periplasmic binding proteins. The members of TorT-like family bind TMAO or related compounds and are predicted to be involved in signal transduction and/or substrate transport.


Pssm-ID: 380529 [Multi-domain]  Cd Length: 269  Bit Score: 67.22  E-value: 9.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 124 ALDHPTVREAMRSLASSGVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGrGSKGKIALFAGSLSYRGHEERE 203
Cdd:cd06306   65 AISFDGLDPKVAEAAAAGIPVIDLVNGIDSPKVAARVLVDFYDMGYLAGEYLVEHHP-GKPVKVAWFPGPAGAGWAEDRE 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 204 MGFRHIIADefPALEIVELREIRDDRERAFEEAAALLKRHPDLAgiYNIGAGNSGIG--QALAEAGKADSIIFVGHELTE 281
Cdd:cd06306  144 KGFKEALAG--SNVEIVATKYGDTGKAVQLNLVEDALQAHPDID--YIVGNAVAAEAavGALREAGLTGKVKVVSTYLTP 219
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 504341065 282 HSKRLLLSGVMDAVIDQNPRVEAREALSMldcAVR---GKPIDYH 323
Cdd:cd06306  220 GVYRGIKRGKILAAPSDQPVLQGRIAVDQ---AVRaleGKPVPKH 261
PRK09701 PRK09701
D-allose transporter substrate-binding protein;
158-320 1.05e-12

D-allose transporter substrate-binding protein;


Pssm-ID: 182037 [Multi-domain]  Cd Length: 311  Bit Score: 67.59  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 158 GYIGIDNRAAGRL-AGYLLGRFLGRGskGKIALFAGSLSYRGHEEREMGFRHIIADEfPALEIVELREIRDDRERAFEEA 236
Cdd:PRK09701 131 AFVTTDNVAVGAKgASFIIDKLGAEG--GEVAIIEGKAGNASGEARRNGATEAFKKA-SQIKLVASQPADWDRIKALDVA 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 237 AALLKRHPDLAGIYnigAGNS----GIGQALAEAGKADSIIFVGHELTEHSKRLLLSGVMDAVIDQNPRVEAREALSMLD 312
Cdd:PRK09701 208 TNVLQRNPNIKAIY---CANDtmamGVAQAVANAGKTGKVLVVGTDGIPEARKMVEAGQMTATVAQNPADIGATGLKLMV 284

                 ....*...
gi 504341065 313 CAVRGKPI 320
Cdd:PRK09701 285 DAEKSGKV 292
LacI pfam00356
Bacterial regulatory proteins, lacI family;
4-46 1.30e-12

Bacterial regulatory proteins, lacI family;


Pssm-ID: 306791 [Multi-domain]  Cd Length: 46  Bit Score: 61.50  E-value: 1.30e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 504341065    4 TLIDIAREAGVSSATVDRVLNNRSGVKDRTREIVMNAARRLGY 46
Cdd:pfam00356   1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNY 43
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
102-323 1.27e-11

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


Pssm-ID: 380621 [Multi-domain]  Cd Length: 278  Bit Score: 64.27  E-value: 1.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 102 NPDTLAgtlqelrgeTMGVGVIALDHPTVREAmrslASSGVPIVTLVSDI----LHVPRTGYIGIDNRAAG-RLAGYLLG 176
Cdd:cd19966   56 KPDGIA---------IMGHPGDGAYTPLIEAA----KKAGIIVTSFNTDLpkleYGDCGLGYVGADLYAAGyTLAKELVK 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 177 RF-LGRGSKGKIALFAGSLSYRGheEREMGfrhiIADEFPALEI-VELREIRDDRERAFEEA---AALLKRHPDLAGIYN 251
Cdd:cd19966  123 RGgLKTGDRVFVPGLLPGQPYRV--LRTKG----VIDALKEAGIkVDYLEISLEPNKPAEGIpvmTGYLAANPDVKAIVG 196
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504341065 252 IGAGNSG-IGQALAEAG-KADSIIFVGHELTEHSKRLLLSGVMDAVIDQNPRVEAREALSMLDCAVRGKPIDYH 323
Cdd:cd19966  197 DGGGLTAnVAKYLKAAGkKPGEIPVAGFDLSPATVQAIKSGYVNATIDQQPYLQGYLPVLQIYLTKKYGFSGLD 270
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
141-328 1.78e-11

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: 63.61  E-value: 1.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 141 GVPIVTLVSDILHVPRTGYIGIDNRAAGrlagYLLGRFLGR--GSKGKIALFAGSLSYRGHEEREMGFRHIIAdEFPALE 218
Cdd:cd19972   80 GIPVIAVDRNPEDAPGDTFIATDSVAAA----KELGEWVIKqtGGKGEIAILHGQLGTTPEVDRTKGFQEALA-EAPGIK 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 219 IVELREIRDDRERAFEEAAALLKRHPDLAGIynIGAGNS---GIGQALAEAGKADSIIFVGHELTEHSKRLLLSGVMDAV 295
Cdd:cd19972  155 VVAEQTADWDQDEGFKVAQDMLQANPNITVF--FGQSDAmalGAAQAVKVAGLDHKIWVVGFDGDVAGLKAVKDGVLDAT 232
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 504341065 296 IDQNP----RVEAREALSMLDcavrGKPIdyhpPRLQ 328
Cdd:cd19972  233 MTQQTqkmgRLAVDSAIDLLN----GKAV----PKEQ 261
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
138-316 1.99e-11

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: 63.40  E-value: 1.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 138 ASSGVPIVTLVSDILHVPR-TGYIGIDNRAAGRLAGYLLGRFLGrgSKGKIALFAGSLSYRGHEEREMGFRHIIAdEFPA 216
Cdd:cd06301   79 ADAGIPLVYVNREPDSKPKgVAFVGSDDIESGELQMEYLAKLLG--GKGNIAILDGVLGHEAQILRTEGNKDVLA-KYPG 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 217 LEIVELREIRDDRERAFEEAAALLKRHPDLAGIYnigAGNS--GIG--QALAEAGKADSIIFVGHELTEHSKRLLLSGVM 292
Cdd:cd06301  156 MKIVAEQTANWSREKAMDIVENWLQSGDKIDAIV---ANNDemAIGaiLALEAAGKKDDILVAGIDATPDALKAMKAGRL 232
                        170       180
                 ....*....|....*....|....
gi 504341065 293 DAVIDQNPRVEAREAlsmLDCAVR 316
Cdd:cd06301  233 DATVFQDAAGQGETA---VDVAVK 253
PBP1_LsrB_Quorum_Sensing-like cd20001
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
163-295 8.61e-11

ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that 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 LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.


Pssm-ID: 380656  Cd Length: 296  Bit Score: 61.91  E-value: 8.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 163 DNRAAGRLAGYLLGRflGRGSKGKIALFAGSLSYRGHEEREMGFRHIIADEFPALEIVELR-EIRDDRERAFEEAAALLK 241
Cdd:cd20001  103 DNAAYGAFIMDKLAE--AMGGKGKYVTFVGSLTSTSHMEWANAAVAYQKANYPDMLLVTDRvETNDDSETAYEKAKELLK 180
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504341065 242 RHPDLAGIYNIGAGNS-GIGQALAEAGKADSIIFVGHELTEHSKRLLLSGVMDAV 295
Cdd:cd20001  181 TYPDLKGIVGCSSSDVpGAARAVEELGLQGKIAVVGTGLPSVAGEYLEDGTIDYI 235
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
121-268 1.93e-10

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: 60.61  E-value: 1.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 121 GVIALDHPTVREamrSLASSGVPIVTLVSDI-LHVPrtgYIGIDNRAAGRLAGYLLgrfLGRGSKgKIALFAGSLSYRGH 199
Cdd:cd06291   58 GIILGSHSLDIE---EYKKLNIPIVSIDRYLsEGIP---SVSSDNYQGGRLAAEHL---IEKGCK-KILHIGGPSNNSPA 127
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504341065 200 EEREMGFRHIIADEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYnigAGN----SGIGQALAEAGK 268
Cdd:cd06291  128 NERYRGFEDALKEAGIEYEIIEIDENDFSEEDAYELAKELLEKYPDIDGIF---ASNdllaIGVLKALQKLGI 197
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
70-324 3.25e-10

periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group includes periplasmic D-threitol-binding protein ThpA and xylitol/L-sorbitol-binding protein XypA, which are part of sugar ABC-type transport systems. Both ThpA and XypA share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.


Pssm-ID: 380536 [Multi-domain]  Cd Length: 277  Bit Score: 59.98  E-value: 3.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  70 TNTFVANLLRQLQTQATArpdLDVRVHSIEG-FNPDTLAGTLQELrgETMGVGVIALD-------HPTVREAMrslaSSG 141
Cdd:cd06313   10 SSEFITNLVEAMKAVAKE---LNVDLVVLDGnGDVSTQINQVDTL--IAQGVDAIIVVpvdadalAPAVEKAK----EAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 142 VPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLgrGSKGKIALFAGSLSYRGHEEREMGFRHIIAdEFPALEIVE 221
Cdd:cd06313   81 IPLVGVNALIENEDLTAYVGSDDVVAGELEGQAVADRL--GGKGNVVILEGPIGQSAQIDRGKGIENVLK-KYPDIKVLA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 222 LREIRDDRERAFEEAAALLKRHPDlaGIYNIGAGNS--GIG--QALAEAGKADsIIFVGHELTEHSKRLLLSGVMDAVID 297
Cdd:cd06313  158 EQTANWSRDEAMSLMENWLQAYGD--EIDGIIAQNDdmALGalQAVKAAGRDD-IPVVGIDGIEDALQAVKSGELIATVL 234
                        250       260
                 ....*....|....*....|....*..
gi 504341065 298 QNPRVEAREALSMLDCAVRGKPIDYHP 324
Cdd:cd06313  235 QDAEAQGKGAVEVAVDAVKGEGVEKKY 261
PRK10401 PRK10401
HTH-type transcriptional regulator GalS;
4-56 3.39e-10

HTH-type transcriptional regulator GalS;


Pssm-ID: 236681 [Multi-domain]  Cd Length: 346  Bit Score: 60.56  E-value: 3.39e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504341065   4 TLIDIAREAGVSSATVDRVLNNRSGVKDRTREIVMNAARRLGYlSPAAhNASA 56
Cdd:PRK10401   3 TIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGY-RPNA-NAQA 53
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
119-310 4.23e-10

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: 59.61  E-value: 4.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 119 GVGVIALD-------HPTVREAMrslaSSGVPIVTLvsDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGrgSKGKIALFA 191
Cdd:cd06321   57 GVDLILLNaadsagiEPAIKRAK----DAGIIVVAV--DVAAEGADATVTTDNVQAGYLACEYLVEQLG--GKGKVAIID 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 192 GSlSYRGHEEREMGFRHIIAdEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYNIGAGnSGIGQALA--EAGKA 269
Cdd:cd06321  129 GP-PVSAVIDRVNGCKEALA-EYPGIKLVDDQNGKGSRAGGLSVMTRMLTAHPDVDGVFAINDP-GAIGALLAaqQAGRD 205
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 504341065 270 DSII--FVGHEltEHSKRLLLSGVM-DAVIDQNPRVEAREALSM 310
Cdd:cd06321  206 DIVItsVDGSP--EAVAALKREGSPfIATAAQDPYDMARKAVEL 247
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
84-311 6.14e-10

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: 380535 [Multi-domain]  Cd Length: 272  Bit Score: 59.17  E-value: 6.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  84 QATARPDLDVRVHSIEGFNPDTLAGTLQELRGEtmGVGVIAL---DHPTVREAMRSLASSGVPIVTLVS-DILHVPRTG- 158
Cdd:cd06312   24 DAAKDLGVTVQYLGPQNNDIADQARLIEQAIAA--KPDGIIVtipDPDALEPALKRAVAAGIPVIAINSgDDRSKERLGa 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 159 --YIGIDNRAAGRLAGYllgRFLGRGSKGkiALF----AGSLsyrGHEEREMGFrhiiADEFPALEI-VELREIRDDRER 231
Cdd:cd06312  102 ltYVGQDEYLAGQAAGE---RALEAGPKN--ALCvnhePGNP---GLEARCKGF----ADAFKGAGIlVELLDVGGDPTE 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 232 AFEEAAALLKRHPDLAGIYNIGA-GNSGIGQALAEAGKADSIIFVGHELTEHSKRLLLSGVMDAVIDQNPRVEAREALSM 310
Cdd:cd06312  170 AQEAIKAYLQADPDTDAVLTLGPvGADPALKAVKEAGLKGKVKIGTFDLSPETLEAIKDGKILFAIDQQPYLQGYLAVVF 249

                 .
gi 504341065 311 L 311
Cdd:cd06312  250 L 250
PBP1_LsrB_Quorum_Sensing cd20003
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ...
117-320 6.87e-10

ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that 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 LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.


Pssm-ID: 380658  Cd Length: 298  Bit Score: 59.21  E-value: 6.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 117 TMGVGVI---ALDHPTVREAMRSLASSGVPIVTLVSDILHVPRTGYIgidNRAAGRLAGYLLGRFLGR--GSKGKIALFA 191
Cdd:cd20003   54 NQGYDVIavsANDPDALAPALKKAMKKGIKVVTWDSDVNPDARDFFV---NQATPEGIGKTLVDMVAEqtGEKGKVAIVT 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 192 GSLSYRGHEE--REMgfRHIIADEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYNIGAGNS-GIGQALAEAGK 268
Cdd:cd20003  131 SSPTATNQNAwiKAM--KAYIAEKYPDMKIVTTQYGQEDPAKSLQVAENILKAYPDLKAIIAPDSVALpGAAEAVEQLGR 208
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504341065 269 ADSIIFVGHELTEHSKRLLLSGVMDAVIDQNPRVEAREALSMLDCAVRGKPI 320
Cdd:cd20003  209 TGKVAVTGLSTPNVMRPYVKDGTVKSVVLWDVVDLGYLAVYVARALADGTLL 260
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
117-319 2.40e-09

periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The periplasmic binding protein (PBP) IbpA mediates the uptake of myo-inositol by an ABC transporter that consists of the PBP IbpA, the transmembrane permease IatP, and the ABC IatA. IbpA shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily, which consists of two domains connected by a three-stranded hinge.


Pssm-ID: 380623 [Multi-domain]  Cd Length: 271  Bit Score: 57.40  E-value: 2.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 117 TMGVGVIALDHPTVRE---AMRSLASSGVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGRGskGKIALFAGS 193
Cdd:cd19968   53 AQGVDGIIVSPIDVKAlvpAIEAAIKAGIPVVTVDRRAEGAAPVPHVGADNVAGGREVAKFVVDKLPNG--AKVIELTGT 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 194 LSYRGHEEREMGFRHIIAdEFPALEIVELRE---IRDDRERAFEEAAALLKRHPDLagiynIGAGNS----GIGQALAEA 266
Cdd:cd19968  131 PGSSPAIDRTKGFHEELA-AGPKIKVVFEQTgnfERDEGLTVMENILTSLPGPPDA-----IICANDdmalGAIEAMRAA 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504341065 267 G-KADSIIFVGHELTEHSKRLLLSGVMDAVIDQNPRVEAREALSMLDCAVRGKP 319
Cdd:cd19968  205 GlDLKKVKVIGFDAVPDALQAIKDGELYATVEQPPGGQARTALRILVDYLKDKK 258
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
141-321 1.51e-08

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: 54.92  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 141 GVPIVTLVSDILHVP---RTGYIGIDNRAAGRLAGYLLGRFLGRGsKGKIALFAGSLSYRGHEEREMGFRHIIAdEFPAL 217
Cdd:cd06309   80 GIPVILVDRTIDGEDgslYVTFIGSDFVEEGRRAAEWLVKNYKGG-KGNVVELQGTAGSSVAIDRSKGFREVIK-KHPNI 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 218 EIVELREIRDDRERAFEEAAALLKRHP-DLAGIYnigAGNS----GIGQALAEAGKAD--SIIFVGHELTEHSKRLLLSG 290
Cdd:cd06309  158 KIVASQSGNFTREKGQKVMENLLQAGPgDIDVIY---AHNDdmalGAIQALKEAGLKPgkDVLVVGIDGQKDALEAIKAG 234
                        170       180       190
                 ....*....|....*....|....*....|.
gi 504341065 291 VMDAVIDQNPRVeAREALSMLDCAVRGKPID 321
Cdd:cd06309  235 ELNATVECNPLF-GPTAFDTIAKLLAGEKVP 264
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
121-250 1.92e-08

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: 54.46  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 121 GVIALDHPTVREAMRSLASSGVPIVTLVSDIlHVPRTGYIGIDNRAAGRLAGyllGRFLGRGSKgKIALFAGSLSYRGHE 200
Cdd:cd06278   57 GVIVTSATLSSELAEECARRGIPVVLFNRVV-EDPGVDSVSCDNRAGGRLAA---DLLLAAGHR-RIAFLGGPEGTSTSR 131
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 504341065 201 EREMGFRHIIADEfpALEIVELREIRDDRERAFEEAAALLKRHPDLAGIY 250
Cdd:cd06278  132 ERERGFRAALAEL--GLPPPAVEAGDYSYEGGYEAARRLLAAPDRPDAIF 179
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
132-294 2.55e-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: 2.55e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 132 EAMRSLASSGVPIVTLVSDI-------LHVPRTGY------IGIDNRAAGR-LAGYLL--GRFLGRGSKGKIALFAGSLS 195
Cdd:cd06324   73 ELLELAEQAKIPVFLINNDLtdeeralLGKPREKFkywlgsIVPDNEQAGYlLAKALIkaARKKSDDGKIRVLAISGDKS 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 196 YRGHEEREMGFRHIIAdEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYnigAGNSGIG----QALAEAGKA-- 269
Cdd:cd06324  153 TPASILREQGLRDALA-EHPDVTLLQIVYANWSEDEAYQKTEKLLQRYPDIDIVW---AANDAMAlgaiDALEEAGLKpg 228
                        170       180
                 ....*....|....*....|....*
gi 504341065 270 DSIIFVGHELTEHSKRLLLSGVMDA 294
Cdd:cd06324  229 KDVLVGGIDWSPEALQAVKDGELTA 253
PBP1_ABC_rhamnose cd20000
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ...
103-319 4.33e-08

rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding protein similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that 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 LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.


Pssm-ID: 380655  Cd Length: 298  Bit Score: 53.80  E-value: 4.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 103 PDTLAGTLQELRGETM---GVGVIAL---DHPTVREAMRSLASSGVPIVTLVSDILHVPRTGYIgidNRAAGRLAGYLLG 176
Cdd:cd20000   37 PTTATAEAQIPFINTLiqqGVDAIAIsanDPDALAPALKKARAAGIKVVTFDSDVAPEARDLFV---NQADADGIGRAQV 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 177 RFLGR--GSKGKIALFAGSLSYRGHEE--REMGfRHIIADEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIynI 252
Cdd:cd20000  114 DMMAEliGGEGEFAILSATPTATNQNAwiDAMK-KELASPEYAGMKLVKVAYGDDDAQKSYQEAEALLQAYPDLKGI--I 190
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504341065 253 GAGNSGI---GQALAEAGKADSIIFVGHELTEHSKRLLLSGVMDAVIDQNPR----VEAREALSMLDCAVRGKP 319
Cdd:cd20000  191 APTTVGIaaaARALEDSGLKGKVKVTGLGLPSEMAKYVKDGTVPAFALWNPIdlgyLAAYAAAALAQGEITGKE 264
PRK10936 PRK10936
TMAO reductase system periplasmic protein TorT; Provisional
137-336 4.53e-08

TMAO reductase system periplasmic protein TorT; Provisional


Pssm-ID: 236801 [Multi-domain]  Cd Length: 343  Bit Score: 53.80  E-value: 4.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 137 LASSGVPIVTLVSDIlHVPR-TGYIGIDNRAAGRLAG-YLLGRFLGRGSKGKIALFAGSLSYRGHEEREMGFRHIIADEf 214
Cdd:PRK10936 124 LQAANIPVIALVNGI-DSPQvTTRVGVSWYQMGYQAGrYLAQWHPKGSKPLNVALLPGPEGAGGSKAVEQGFRAAIAGS- 201
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 215 pALEIVELREIRDDRERAFEEAAALLKRHPDLAgiYNIG---AGNSGIGQaLAEAGKADSIIFVGHELTEHSKRLLLSG- 290
Cdd:PRK10936 202 -DVRIVDIAYGDNDKELQRNLLQELLERHPDID--YIAGsavAAEAAIGE-LRGRNLTDKIKLVSFYLSHQVYRGLKRGk 277
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 504341065 291 VMDAVIDQnPRVEAREAlsmLDCAVR---GKPIDYH-PPRLQVIFRENIP 336
Cdd:PRK10936 278 VLAAPSDQ-MVLQGRLA---IDQAVRqleGAPVPGDvGPKILVLTPKNLD 323
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
64-267 1.00e-07

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: 52.23  E-value: 1.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  64 FVLPAGTNTFVANLLRQLQTQATARpDLDVRVHSIEGfNPDTLAGTLQELRGetMGV-GVIALDHPTVREAMRSLASSGV 142
Cdd:cd06285    4 VLVSDLSNPFYAELVEGIEDAARER-GYTVLLADTGD-DPERELAALDSLLS--RRVdGLIITPARDDAPDLQELAARGV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 143 PIVtLVSDILHVPRTGYIGIDNRAAGRLAG-YLLGrfLG-RgskgKIALFAGSLSYRGHEEREMGFRHIIADEFPALEIV 220
Cdd:cd06285   80 PVV-LVDRRIGDTALPSVTVDNELGGRLATrHLLE--LGhR----RIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDE 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504341065 221 ELREIRDDRERAFEEAAALLKRHPDLAGIYnigAGNS----GIGQALAEAG 267
Cdd:cd06285  153 RIVPGGFTIEAGREAAYRLLSRPERPTAVF---AANDlmaiGVLRAARDLG 200
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
117-317 1.91e-07

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: 51.64  E-value: 1.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 117 TMGVGVIAL---DHPTVREAMRSLASSGVPIVTLVSDILHVPR-TGYIGIDNRAAGRLAGYLLGRFLGrGSKGKIALFAG 192
Cdd:cd06318   53 TRGVDVLILnpvDPEGLTPAVKAAKAAGIPVITVDSALDPSANvATQVGRDNKQNGVLVGKEAAKALG-GDPGKIIELSG 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 193 SLSYRGHEEREMGFRHIIADE------FPALEIVE---LREIRDDRERAFEEaaaLLKRHPDLAGIYniGAGNS---GIG 260
Cdd:cd06318  132 DKGNEVSRDRRDGFLAGVNEYqlrkygKSNIKVVAqpyGNWIRSGAVAAMED---LLQAHPDINVVY--AENDDmalGAM 206
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504341065 261 QALAEAGKADSIIFVGHELTEHSKRLLLSGVMDAVIDQNPRVEAREALSMLDCAVRG 317
Cdd:cd06318  207 KALKAAGMLDKVKVAGADGQKEALKLIKDGKYVATGLNDPDLLGKTAVDTAAKVVKG 263
PRK10339 PRK10339
DNA-binding transcriptional repressor EbgR; Provisional
3-64 6.85e-07

DNA-binding transcriptional repressor EbgR; Provisional


Pssm-ID: 182389 [Multi-domain]  Cd Length: 327  Bit Score: 50.14  E-value: 6.85e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504341065   3 STLIDIAREAGVSSATVDRVLNNRS--GVKDRTREIVMNAARRLGYLSPAAHNASAEGRVRLDF 64
Cdd:PRK10339   2 ATLKDIAIEAGVSLATVSRVLNDDPtlNVKEETKHRILEIAEKLEYKTSSARKLQTGAVNQHHI 65
PRK10423 PRK10423
transcriptional repressor RbsR; Provisional
7-267 7.21e-07

transcriptional repressor RbsR; Provisional


Pssm-ID: 182448 [Multi-domain]  Cd Length: 327  Bit Score: 50.08  E-value: 7.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065   7 DIAREAGVSSATVDRVLNNRSGVKDRTREIVMNAARRLGYlSPAAHNASAE-GRVR-LDFVLPAGTNTFVANLLRQLQTQ 84
Cdd:PRK10423   3 DVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNY-APSALARSLKlNQTRtIGMLITASTNPFYSELVRGVERS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  85 ATAR----------PDLDVRVHSIEgfnpdtlagTLQELRGEtmgvGVIAL---DHPTVREAMRSLASsgVPIVTL---- 147
Cdd:PRK10423  82 CFERgyslvlcnteGDEQRMNRNLE---------TLMQKRVD----GLLLLcteTHQPSREIMQRYPS--VPTVMMdwap 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 148 ---VSDILHvprtgyigiDNRAagrLAGYLLGRFL-GRGSKgKIALFAGSLSYRGHEEREMGFRHIIADEfpALEIVELR 223
Cdd:PRK10423 147 fdgDSDLIQ---------DNSL---LGGDLATQYLiDKGYT-RIACITGPLDKTPARLRLEGYRAAMKRA--GLNIPDGY 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 504341065 224 EIRDDRERA--FEEAAALLKRHPDLAGIYnigAGNS----GIGQALAEAG 267
Cdd:PRK10423 212 EVTGDFEFNggFDAMQQLLALPLRPQAVF---TGNDamavGVYQALYQAG 258
PBP1_ABC_sugar_binding-like cd06300
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ...
124-269 7.73e-07

periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.


Pssm-ID: 380523 [Multi-domain]  Cd Length: 302  Bit Score: 50.01  E-value: 7.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 124 ALDhPTVREAMRSlassGVPIVTlVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGrgSKGKIALFAGSLSYRGHEERE 203
Cdd:cd06300   73 ALN-AVIEQAADA----GIPVVA-FDGAVTSPDAYNVSNDQVEWGRLGAKWLFEALG--GKGNVLVVRGIAGAPASADRH 144
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504341065 204 MGFRHIIAdEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYNIGAGNSGIGQALAEAGKA 269
Cdd:cd06300  145 AGVKEALA-EYPGIKVVGEVFGGWDEATAQTAMLDFLATHPQVDGVWTQGGEDTGVLQAFQQAGRP 209
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
64-311 9.51e-07

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: 49.43  E-value: 9.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065   64 FVLPAGTNTFVANLLRQLqTQATARPDLDVRVhsIEGF-NPDTLAGTLQELRGETMGVGVIALDHPTVREAMRSLASSGV 142
Cdd:pfam00532   6 ALVPQLDEPFFQDLVKGI-TKAAKDHGFDVFL--LAVGdGEDTLTNAIDLLLASGADGIIITTPAPSGDDITAKAEGYGI 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  143 PIVTLVsdilhvpRTGYIGID---NRAAGRLAGYLLGRFL-GRGSKGKIALFAGSLSYRGHEEREMGFRHIIADEFPALE 218
Cdd:pfam00532  83 PVIAAD-------DAFDNPDGvpcVMPDDTQAGYESTQYLiAEGHKRPIAVMAGPASALTARERVQGFMAALAAAGREVK 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  219 IVELREIRDDRERAFEEAAALLKRHPDLAGIYnigAGNS----GIGQALAEAG--KADSIIFVGHE-------LTEHSKR 285
Cdd:pfam00532 156 IYHVATGDNDIPDAALAANAMLVSHPTIDAIV---AMNDeaamGAVRALLKQGrvKIPDIVGIGINsvvgfdgLSKAQDT 232
                         250       260
                  ....*....|....*....|....*.
gi 504341065  286 LLLSGVMdAVIDQNPRVEAREALSML 311
Cdd:pfam00532 233 GLYLSPL-TVIQLPRQLLGIKASDMV 257
lacI PRK09526
lac repressor; Reviewed
3-46 1.17e-06

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 49.61  E-value: 1.17e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 504341065   3 STLIDIAREAGVSSATVDRVLNNRSGVKDRTREIVMNAARRLGY 46
Cdd:PRK09526   6 VTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNY 49
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
64-207 1.52e-06

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: 48.69  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  64 FVLPAGTNTFVANLLRQLQTQATARpDLDVRVHSIEGfNPDTLAGTLQELRGeTMGVGVIALDhPTVREAMRSLASSGVP 143
Cdd:cd06284    4 VLVPNISNPFYSEILRGIEDAAAEA-GYDVLLGDTDS-DPEREDDLLDMLRS-RRVDGVILLS-GRLDAELLSELSKRYP 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504341065 144 IVtLVSDILHVPRTGYIGIDNRAAGRLAG-YLLGrfLGRgskGKIALFAGSLSYRGHEEREMGFR 207
Cdd:cd06284   80 IV-QCCEYIPDSGVPSVSIDNEAAAYDATeYLIS--LGH---RRIAHINGPLDNVYARERLEGYR 138
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
119-330 3.98e-06

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 47.78  E-value: 3.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 119 GVGVIaLDHPT----VREAMRSLASSGVPIVTLVSDILHVPRTGYIGIDNRAAGRLAGYLLGRFLGRGSKgKIAL--FAG 192
Cdd:PRK10653  82 GTKIL-LINPTdsdaVGNAVKMANQANIPVITLDRGATKGEVVSHIASDNVAGGKMAGDFIAKKLGEGAK-VIQLegIAG 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 193 SLSYRgheEREMGFRHIIADEfpALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYnigAGNS----GIGQALAEAGK 268
Cdd:PRK10653 160 TSAAR---ERGEGFKQAVAAH--KFNVLASQPADFDRTKGLNVMQNLLTAHPDVQAVF---AQNDemalGALRALQTAGK 231
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504341065 269 ADsIIFVGHELTEHSKRLLLSGVMDAVIDQNPRVEAREALSMLDCAVRGKPID-YHPPRLQVI 330
Cdd:PRK10653 232 SD-VMVVGFDGTPDGIKAVNRGKLAATIAQQPDQIGAIGVETADKVLKGEKVEaKIPVDLKLV 293
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
129-249 1.10e-05

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: 46.40  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 129 TVREAMRSLASSGVPIVTLVSDILHVPrTGYIGIDNRAAGRLAGyllGRFLGRGSKgKIALFAGSLSYRGHEEREMGFRH 208
Cdd:cd06289   67 TTAELLRRLKAWGIPVVLALRDVPGSD-LDYVGIDNRLGAQLAT---EHLIALGHR-RIAFLGGLSDSSTRRERLAGFRA 141
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 504341065 209 IIAD---EFPALEIVELREirdDRERAFEEAAALLKRHPDLAGI 249
Cdd:cd06289  142 ALAEaglPLDESLIVPGPA---TREAGAEAARELLDAAPPPTAV 182
PRK11303 PRK11303
catabolite repressor/activator;
4-302 1.14e-05

catabolite repressor/activator;


Pssm-ID: 236897 [Multi-domain]  Cd Length: 328  Bit Score: 46.41  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065   4 TLIDIAREAGVSSATVDRVLNNRSG---VKDRTREIVMNAARRLGYLSPAAHNASAEGRVR-LDFVLPAGTNTFVANLLR 79
Cdd:PRK11303   2 KLDEIARLAGVSRTTASYVINGKAKqyrVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRsIGLIIPDLENTSYARIAK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  80 QLQTQATARpdldvrvhsieGF---------NPDTLAGTLQELRGETMGVGVIALDHPTVREAMRSLASSGVPIVTL--V 148
Cdd:PRK11303  82 YLERQARQR-----------GYqlliacsddQPDNEMRCAEHLLQRQVDALIVSTSLPPEHPFYQRLQNDGLPIIALdrA 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 149 SDILHVprTGYIGIDNRAAGRLAGYLLGR------FLGrgskgkiALFAGSLSYrgheEREMGFRHIIADefpaleivel 222
Cdd:PRK11303 151 LDREHF--TSVVSDDQDDAEMLAESLLKFpaesilLLG-------ALPELSVSF----EREQGFRQALKD---------- 207
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 223 reirDDRERAFEEAAAllkrhpdlagiYNIGAGNSGIGQALAEAGKADSII---FVgheltehskrlLLSGVMDAVIDQN 299
Cdd:PRK11303 208 ----DPREVHYLYANS-----------FEREAGAQLFEKWLETHPMPDALFttsYT-----------LLQGVLDVLLERP 261

                 ...
gi 504341065 300 PRV 302
Cdd:PRK11303 262 GEL 264
PBP1_LacI-like cd06299
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ...
121-267 2.81e-05

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: 44.96  E-value: 2.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 121 GVIALDHPTVREAMRSLASSGVPIVTLVSDILHVPRTGYIGIDNRAAGRLA-GYLLGrfLGRGSkgkIALFAGSLSYRGH 199
Cdd:cd06299   58 GIIAVPTGENSEGLQALIAQGLPVVFVDREVEGLGGVPVVTSDNRPGAREAvEYLVS--LGHRR---IGYISGPLSTSTG 132
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504341065 200 EEREMGFRHIIADEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYnigAGNS----GIGQALAEAG 267
Cdd:cd06299  133 RERLAAFRAALTAAGIPIDEELVAFGDFRQDSGAAAAHRLLSRGDPPTALI---AGDSlmalGAIQALRELG 201
PBP1_LacI cd01574
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ...
65-207 9.05e-05

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: 43.34  E-value: 9.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  65 VLPAGTNTF-VANLLRQLQTQATARpDLDVRVHSIEGFNPDTLAGTLQELRGetMGV-GVIAL-DHPTVREAMRSLASsG 141
Cdd:cd01574    4 VIATGLSLYgPASTLAGIERAARER-GYSVSIATVDEDDPASVREALDRLLS--QRVdGIIVIaPDEAVLEALRRLPP-G 79
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504341065 142 VPIVTLVSDilHVPRTGYIGIDNRAAGRLA-GYLLGrfLGRGSkgkIALFAGSLSYRGHEEREMGFR 207
Cdd:cd01574   80 LPVVIVGSG--PSPGVPTVSIDQEEGARLAtRHLLE--LGHRR---IAHIAGPLDWVDARARLRGWR 139
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
116-267 1.01e-04

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


Pssm-ID: 380516 [Multi-domain]  Cd Length: 270  Bit Score: 43.41  E-value: 1.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 116 ETMGV-GVIALDHPTVREAMRSLASSGVPIVTLVSDILHvPRTGYIGIDNRAAGRLAGYLLgrfLGRGSKgKIALFAGSL 194
Cdd:cd06293   52 ESQRVrGLIVTPSDDDLSHLARLRARGTAVVLLDRPAPG-PAGCSVSVDDVQGGALAVDHL---LELGHR-RIAFVSGPL 126
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504341065 195 SYRGHEEREMGFRHII--ADEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYnigAGNS----GIGQALAEAG 267
Cdd:cd06293  127 RTRQVAERLAGARAAVaeAGLDPDEVVRELSAPDANAELGRAAAAQLLAMPPRPTAVF---AANDllalGLLAGLRRAG 202
PBP1_CcpA cd06298
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ...
65-247 1.52e-04

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: 42.66  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  65 VLPAGTNTFVANLLRQLQTQATARpDLDVRVHSIEgFNPDTLAGTLQELRGEtmGV-GVIALDHPTVREAMRSLASSGVP 143
Cdd:cd06298    5 IIPDISNLYYAELARGIDDIATMY-KYNIILSNSD-NNVDKELDLLNTMLSK--QVdGIIFMGDELTEEIREEFKRSPVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 144 IVtLVSDILHVPRTGYIGIDNRAAGRLAgylLGRFLGRGSKgKIALFAGSLS-YRGHEEREMGFRHIIAD---EFPALEI 219
Cdd:cd06298   81 VV-LAGTVDSDHEIPSVNIDYEQAAYDA---TKSLIDKGHK-KIAFVSGPLKeYINNDKKLQGYKRALEEaglEFNEPLI 155
                        170       180
                 ....*....|....*....|....*....
gi 504341065 220 VELREIRDDRERAFEEaaaLLKR-HPDLA 247
Cdd:cd06298  156 FEGDYDYDSGYELYEE---LLESgEPDAA 181
PRK10727 PRK10727
HTH-type transcriptional regulator GalR;
3-56 1.58e-04

HTH-type transcriptional regulator GalR;


Pssm-ID: 182681 [Multi-domain]  Cd Length: 343  Bit Score: 42.82  E-value: 1.58e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504341065   3 STLIDIAREAGVSSATVDRVLNNRSGVKDRTREIVMNAARRLGYlSPAAhNASA 56
Cdd:PRK10727   2 ATIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSY-HPNA-NARA 53
PRK14987 PRK14987
HTH-type transcriptional regulator GntR;
2-169 1.96e-04

HTH-type transcriptional regulator GntR;


Pssm-ID: 184949 [Multi-domain]  Cd Length: 331  Bit Score: 42.71  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065   2 RSTLIDIAREAGVSSATVDRVLNNRSGVKDRTREIVMNAARRLGYLSPAAHNASAEGRVR-LDFVLPAGTNTFVANLLRQ 80
Cdd:PRK14987   5 RPVLQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRaIGVLLPSLTNQVFAEVLRG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  81 LQTQATARPDLDVRVHSieGFNPDtlagtLQELRGETMGV----GVIALDHPTVREAMRSLASSGVPIVTL---VSDILH 153
Cdd:PRK14987  85 IESVTDAHGYQTMLAHY--GYKPE-----MEQERLESMLSwnidGLILTERTHTPRTLKMIEVAGIPVVELmdsQSPCLD 157
                        170
                 ....*....|....*.
gi 504341065 154 VPrtgyIGIDNRAAGR 169
Cdd:PRK14987 158 IA----VGFDNFEAAR 169
PBP1_sucrose_transcription_regulator cd06288
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ...
100-267 2.47e-04

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: 42.15  E-value: 2.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 100 GFNPDTLAGTLQELRGetMGV-GVI-ALDHPTVREAMRSLAssGVPIVTL--VSDILHVPrtgYIGIDNRAAGRLAGYLL 175
Cdd:cd06288   39 GGDPELEAEAIRELLS--RRVdGIIyASMHHREVTLPPELT--DIPLVLLncFDDDPSLP---SVVPDDEQGGYLATRHL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 176 grfLGRGSKgKIALFAGSLSYRGHEEREMGFRHIIADE--FPALEIVELREirDDRERAFEEAAALLKRHPDLAGIYnig 253
Cdd:cd06288  112 ---IEAGHR-RIAFIGGPEDSLATRLRLAGYRAALAEAgiPYDPSLVVHGD--WGRESGYEAAKRLLSAPDRPTAIF--- 182
                        170
                 ....*....|....*...
gi 504341065 254 AGNS----GIGQALAEAG 267
Cdd:cd06288  183 CGNDrmamGVYQAAAELG 200
PBP1_XylR cd01543
ligand-binding domain of DNA transcription repressor specific for xylose (XylR); ...
101-244 3.09e-04

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: 41.80  E-value: 3.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 101 FNPDTLAGTLQELRGETmGVGVIA--LDHPTVREAMRSlassGVPIVtLVSDILHVPRTGYIGIDNRAAGRLAG-Yllgr 177
Cdd:cd01543   34 LEPPGYEELLDLLKGWK-GDGIIArlDDPELAEALRRL----GIPVV-NVSGSRPEPGFPRVTTDNEAIGRMAAeH---- 103
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504341065 178 FLGRGSKgKIAlFAGSLSYRGHEEREMGFRHIIADEFPALEIVE--LREIRDDRERAFEEAAALLKRHP 244
Cdd:cd01543  104 LLERGFR-HFA-FCGFRNAAWSRERGEGFREALREAGYECHVYEspPSGSSRSWEEEREELADWLKSLP 170
PBP1_CatR-like cd06296
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ...
61-245 4.03e-04

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: 41.49  E-value: 4.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065  61 RLDFVLPAGTNTFVANLLRQLQTQATARpdlDVRVHSIEGFNPDTLAGTLQELRGETMGVGVIALDHPTVREAMRSLASS 140
Cdd:cd06296    1 LIDLVLPQLDSPYALEVLRGVERAAAAA---GLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQLRLLRSA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 141 GVPIVTLvsDILHVPRTG--YIGIDNRAAGRLAGYLLgrfLGRGSKgKIALFAGSLSYRGHEEREMGFRHIIADEFPALE 218
Cdd:cd06296   78 GIPFVLI--DPVGEPDPDlpSVGATNWAGGRLATEHL---LDLGHR-RIAVITGPPRSVSGRARLAGYRAALAEAGIAVD 151
                        170       180
                 ....*....|....*....|....*..
gi 504341065 219 IVELREIRDDRERAFEEAAALLkRHPD 245
Cdd:cd06296  152 PDLVREGDFTYEAGYRAARELL-ELPD 177
PBP1_MalR-like cd06294
ligand-binding domain of maltose transcription regulator MalR which is a member of the ...
137-249 1.15e-03

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: 39.87  E-value: 1.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 137 LASSGVPIVTLVSDiLHVPRTGYIGIDNRAAGRLA-GYLLGRflgrGSKgKIALFAGSLSYRGHEEREMGFRHIIAD--- 212
Cdd:cd06294   79 LKEEGFPFVVIGKP-LDDNDVLYVDNDNVQAGYEAtEYLIDK----GHK-RIAFIGGDKNLVVSIDRLQGYKQALKEagl 152
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 504341065 213 EFPALEIVELREIRDDRERAFEEaaaLLKRHPDLAGI 249
Cdd:cd06294  153 PLDDDYILLLDFSEEDGYDALQE---LLSKPPPPTAI 186
PBP1_LacI-like cd06279
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ...
103-245 2.07e-03

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: 39.50  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 103 PDTLAGTLQELRGETMGVGVIALDHPTVREAMRSLASSGVPIVTLvsDILHVPRTGYIGIDNRAAGRLAGYLLgrfLGRG 182
Cdd:cd06279   41 PATDEGSAAAAVRNAAVDGFIVYGLSDDDPAVAALRRRGLPLVVV--DGPAPPGIPSVGIDDRAAARAAARHL---LDLG 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 183 SKgKIALFAGSLSYRGHE-----------------EREMGFRHIIADEFPALEIVELREIRDDRERAFEEAA-ALLKRHP 244
Cdd:cd06279  116 HR-RIAILSLRLDRGRERgpvsaerlaaatnsvarERLAGYRDALEEAGLDLDDVPVVEAPGNTEEAGRAAArALLALDP 194

                 .
gi 504341065 245 D 245
Cdd:cd06279  195 R 195
PRK15408 PRK15408
autoinducer 2 ABC transporter substrate-binding protein LsrB;
128-276 3.60e-03

autoinducer 2 ABC transporter substrate-binding protein LsrB;


Pssm-ID: 237961  Cd Length: 336  Bit Score: 38.62  E-value: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 128 PTVREAMRSlassGVPIVTLVSDILHVPRTGYIgidNRAAGRLAGYLLGRFLGR---GSKGKIALFAGSLSYRGHEEREM 204
Cdd:PRK15408  96 PALKRAMQR----GVKVLTWDSDTKPECRSYYI---NQGTPEQLGSMLVEMAAKqvgKDKAKVAFFYSSPTVTDQNQWVK 168
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504341065 205 GFRHIIADEFPALEIVELREIRDDRERAFEEAAALLKRHPDLAGIYNIGAGN-SGIGQAlAEAGKADSIIFVG 276
Cdd:PRK15408 169 EAKAKIAKEHPGWEIVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANAlPAAAQA-AENLKRDKVAIVG 240
PBP1_LacI-like cd06287
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
121-269 4.05e-03

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: 38.56  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 121 GVIALDhPTVREA-MRSLASSGVPIVTLVSDILhvPRTGYIGIDNRAAgRLAGYLLGRFLGRGSKgKIALFAGSLSYRGH 199
Cdd:cd06287   59 GAIVVE-PTVEDPiLARLRQRGVPVVSIGRAPG--TDEPVPYVDLQSA-ATARLLLEHLHGAGAR-QVALLTGSSRRNSS 133
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504341065 200 EEREMGFRHIIADEFPALEIVELREIRDDRErAFEEAAALLKRHPDLAGIYN-IGAGNSGIGQALAEAGKA 269
Cdd:cd06287  134 LESEAAYLRFAQEYGTTPVVYKVPESEGERA-GYEAAAALLAAHPDIDAVCVpVDAFAVGAMRAARDSGRS 203
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
131-250 5.32e-03

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: 37.86  E-value: 5.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 131 REAMRSLASSGVPIVTLVS------DILhvprtgyIGIDNRAAGRLAGYLLgrfLGRGSKgKIALFAGSLS--YRGHeER 202
Cdd:cd01575   68 PATRKLLRAAGIPVVETWDlpddpiDMA-------VGFSNFAAGRAMARHL---IERGYR-RIAFVGARLDgdSRAR-QR 135
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504341065 203 EMGFRHIIADEFPALEivelREIRDDRERAFEEAAA----LLKRHPDLAGIY 250
Cdd:cd01575  136 LEGFRDALAEAGLPLP----LVLLVELPSSFALGREalaeLLARHPDLDAIF 183
PBP1_DegA_Like cd19976
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
137-281 7.96e-03

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: 37.61  E-value: 7.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 137 LASSGVPIVTLVSDI-LHVPrtGYIGIDNRAAGRLAG-YLLgrflgrgSKG--KIALFAGSLSYRGHEEREMGFRHIIAD 212
Cdd:cd19976   75 LKEEKIPVVVLDRYIeDNDS--DSVGVDDYRGGYEATkYLI-------ELGhtRIGCIVGPPSTYNEHERIEGYKNALQD 145
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504341065 213 EFPALEIVELREIRDDRERAFEEAAALLKRHPDLAgiynIGAGNS----GIGQALAEAGKA---D-SII-FVGHELTE 281
Cdd:cd19976  146 HNLPIDESWIYSGESSLEGGYKAAEELLKSKNPTA----IFAGNDliamGVYRAALELGLKipeDlSVIgFDNIILSE 219
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
117-270 9.54e-03

similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Proteins similar to methylthioribose-binding protein of ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. The sugar-binding domain of the periplasmic proteins in this group is also homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR), DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380528 [Multi-domain]  Cd Length: 273  Bit Score: 37.28  E-value: 9.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 117 TMGVGVIALDH---PTVREAMRSLASSGVPIVTLVSDIlHVPRTGYIGIDNRAAGRL-AGYLLGRFlgrGSKGKIALFAG 192
Cdd:cd06305   53 TQKVDAIIISHgdaDALDPKLKKALDAGIPVVTFDTDS-QVPGVNNITQDDYALGTLsLGQLVKDL---NGEGNIAVFNV 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504341065 193 SlSYRGHEEREMGFRHIIAdEFPALEIVELRE---IRDDRERAFEEAAALLKRHPDlAGI------YNIGAgnSGIGQAL 263
Cdd:cd06305  129 F-GVPPLDKRYDIYKAVLK-ANPGIKKIVAELgdvTPNTAADAQTQVEALLKKYPE-GGIdaiwaaWDEPA--KGAVQAL 203

                 ....*..
gi 504341065 264 AEAGKAD 270
Cdd:cd06305  204 EEAGRTD 210
 
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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