NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|491069032|ref|WP_004930660|]
View 

MULTISPECIES: substrate-binding domain-containing protein [Acinetobacter]

Protein Classification

LacI family DNA-binding transcriptional regulator( domain architecture ID 11265724)

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PBP1_LacI-like cd06287
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
69-339 1.52e-160

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: 449.56  E-value: 1.52e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  69 TIALISTIPSAISGGASKLGFMMEVANVAAIYALEHDLYILLVPFIdHNNFDGNLMNVDGVILLEPCLNDPIVKKLLQYK 148
Cdd:cd06287    1 AIALISSMPFAIAGGASRLGFMMEVAAAAAEEALEHDLALVLVPPL-HHVSMLDALDVDGAIVVEPTVEDPILARLRQRG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 149 IPLVCIGTPGQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNASLKAEEIYSQYCQQYAMTEVVYKVEEH 228
Cdd:cd06287   80 VPVVSIGRAPGTDEPVPYVDLQSAATARLLLEHLHGAGARQVALLTGSSRRNSSLESEAAYLRFAQEYGTTPVVYKVPES 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 229 LGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTRYNGIRALTSNPPLTAVDLHLDDVAKI 308
Cdd:cd06287  160 EGERAGYEAAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPEDLMVVTRYDGIRARTADPPLTAVDLHLDRVART 239
                        250       260       270
                 ....*....|....*....|....*....|.
gi 491069032 309 AIDLLITQLNEdiETGSLRVMPAPEIIKRTS 339
Cdd:cd06287  240 AIDLLFASLSG--EERSVEVGPAPELVVRAS 268
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
10-75 1.09e-23

helix_turn _helix lactose operon repressor;


:

Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 92.65  E-value: 1.09e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491069032    10 ITISDVALAAQVSRTTVSHALNGKGEVNPDTRKKIQEIAEQLGYRPNRFAKALRSGGTKTIALIST 75
Cdd:smart00354   1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVP 66
 
Name Accession Description Interval E-value
PBP1_LacI-like cd06287
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
69-339 1.52e-160

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: 449.56  E-value: 1.52e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  69 TIALISTIPSAISGGASKLGFMMEVANVAAIYALEHDLYILLVPFIdHNNFDGNLMNVDGVILLEPCLNDPIVKKLLQYK 148
Cdd:cd06287    1 AIALISSMPFAIAGGASRLGFMMEVAAAAAEEALEHDLALVLVPPL-HHVSMLDALDVDGAIVVEPTVEDPILARLRQRG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 149 IPLVCIGTPGQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNASLKAEEIYSQYCQQYAMTEVVYKVEEH 228
Cdd:cd06287   80 VPVVSIGRAPGTDEPVPYVDLQSAATARLLLEHLHGAGARQVALLTGSSRRNSSLESEAAYLRFAQEYGTTPVVYKVPES 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 229 LGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTRYNGIRALTSNPPLTAVDLHLDDVAKI 308
Cdd:cd06287  160 EGERAGYEAAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPEDLMVVTRYDGIRARTADPPLTAVDLHLDRVART 239
                        250       260       270
                 ....*....|....*....|....*....|.
gi 491069032 309 AIDLLITQLNEdiETGSLRVMPAPEIIKRTS 339
Cdd:cd06287  240 AIDLLFASLSG--EERSVEVGPAPELVVRAS 268
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
7-340 2.94e-77

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 240.49  E-value: 2.94e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032   7 KKTITISDVALAAQVSRTTVSHALNGKGEVNPDTRKKIQEIAEQLGYRPNRFAKALRSGGTKTIALIstIPS-------- 78
Cdd:COG1609    1 RKRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVV--VPDlsnpffae 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  79 ---AISGGASKLGFMMEVANVAAIYALEHDLYILLvpfIDHnnfdgnlmNVDGVILLEPCLNDPIVKKLLQYKIPLVCIG 155
Cdd:COG1609   79 llrGIEEAARERGYQLLLANSDEDPEREREALRLL---LSR--------RVDGLILAGSRLDDARLERLAEAGIPVVLID 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 156 TPGQDNkEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNASLKAEEIYSQYCQQYAMT-EVVYKVEEHLGEMGG 234
Cdd:COG1609  148 RPLPDP-GVPSVGVDNRAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPpDPELVVEGDFSAESG 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 235 KSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTRYNGIRALTSNPPLTAVDLHLDDVAKIAIDLLI 314
Cdd:COG1609  227 YEAARRLLARGPRPTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLL 306
                        330       340
                 ....*....|....*....|....*.
gi 491069032 315 TQLNEDIETGSLRVMPaPEIIKRTSS 340
Cdd:COG1609  307 DRIEGPDAPPERVLLP-PELVVREST 331
lacI PRK09526
lac repressor; Reviewed
6-345 2.55e-32

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 123.57  E-value: 2.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032   6 NKKTITISDVALAAQVSRTTVSHALNGKGEVNPDTRKKIQEIAEQLGYRPNRFAKALRSGGTKTIALIST---------I 76
Cdd:PRK09526   2 KSKPVTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTslalhapsqI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  77 PSAISGGASKLGF--MMEVANVAAIYALEHDLYILLVpfidhnnfdgnlMNVDGVILLEPcLNDPIVKKLLQYKIPLVCI 154
Cdd:PRK09526  82 AAAIKSRADQLGYsvVISMVERSGVEACQAAVNELLA------------QRVSGVIINVP-LEDADAEKIVADCADVPCL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 155 GTPGQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITG-QSKRNASLKAEEiYSQYCQQYAMTEVVyKVEEHLGEMG 233
Cdd:PRK09526 149 FLDVSPQSPVNSVSFDPEDGTRLGVEHLVELGHQRIALLAGpESSVSARLRLAG-WLEYLTDYQLQPIA-VREGDWSAMS 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 234 GKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTRYNGIRALTSNPPLTAVDLHLDDVAKIAIDLL 313
Cdd:PRK09526 227 GYQQTLQMLREGPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRL 306
                        330       340       350
                 ....*....|....*....|....*....|..
gi 491069032 314 ITQLNEDIETGSLRvMPAPEIIKRTSSVQISS 345
Cdd:PRK09526 307 LALSQGQAVKGSQL-LPTSLVVRKSTAPPNTQ 337
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
10-75 1.09e-23

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 92.65  E-value: 1.09e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491069032    10 ITISDVALAAQVSRTTVSHALNGKGEVNPDTRKKIQEIAEQLGYRPNRFAKALRSGGTKTIALIST 75
Cdd:smart00354   1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVP 66
HTH_LacI cd01392
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ...
14-64 2.21e-21

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: 85.92  E-value: 2.21e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491069032  14 DVALAAQVSRTTVSHALNGKGEVNPDTRKKIQEIAEQLGYRPNRFAKALRS 64
Cdd:cd01392    2 DIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
181-340 1.23e-17

Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional regulatory proteins. It is related to bacterial periplasmic binding proteins, although this domain is unlikely to be found in the periplasm. This domain acts as a sensor binding small molecule ligands that the DNA-binding domain responds to. This domain recognizes Sugars, sugar phosphates, sugar acids and purines (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433159 [Multi-domain]  Cd Length: 160  Bit Score: 78.92  E-value: 1.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  181 HLVEEGAHQIALITGQSKRNASLkAEEI---YSQYCQQYAMTEVVYKVEEhLGEMGGKSAIAEIMKQYPKTDAILVMIDT 257
Cdd:pfam13377   1 HLAELGHRRIALIGPEGDRDDPY-SDLRergFREAARELGLDVEPTLYAG-DDEAEAAAARERLRWLGALPTAVFVANDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  258 FATGVMQYLTEKGISVPKQMKVVTrYNG--IRALTSnPPLTAVDLHLDDVAKIAIDLLITQLNEDIETGSLRVMPaPEII 335
Cdd:pfam13377  79 VALGVLQALREAGLRVPEDLSVIG-FDDspLAALVS-PPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLP-PELV 155

                  ....*
gi 491069032  336 KRTSS 340
Cdd:pfam13377 156 EREST 160
LacI pfam00356
Bacterial regulatory proteins, lacI family;
11-56 5.04e-13

Bacterial regulatory proteins, lacI family;


Pssm-ID: 306791 [Multi-domain]  Cd Length: 46  Bit Score: 62.65  E-value: 5.04e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 491069032   11 TISDVALAAQVSRTTVSHALNGKGEVNPDTRKKIQEIAEQLGYRPN 56
Cdd:pfam00356   1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
 
Name Accession Description Interval E-value
PBP1_LacI-like cd06287
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
69-339 1.52e-160

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: 449.56  E-value: 1.52e-160
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  69 TIALISTIPSAISGGASKLGFMMEVANVAAIYALEHDLYILLVPFIdHNNFDGNLMNVDGVILLEPCLNDPIVKKLLQYK 148
Cdd:cd06287    1 AIALISSMPFAIAGGASRLGFMMEVAAAAAEEALEHDLALVLVPPL-HHVSMLDALDVDGAIVVEPTVEDPILARLRQRG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 149 IPLVCIGTPGQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNASLKAEEIYSQYCQQYAMTEVVYKVEEH 228
Cdd:cd06287   80 VPVVSIGRAPGTDEPVPYVDLQSAATARLLLEHLHGAGARQVALLTGSSRRNSSLESEAAYLRFAQEYGTTPVVYKVPES 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 229 LGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTRYNGIRALTSNPPLTAVDLHLDDVAKI 308
Cdd:cd06287  160 EGERAGYEAAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRSVPEDLMVVTRYDGIRARTADPPLTAVDLHLDRVART 239
                        250       260       270
                 ....*....|....*....|....*....|.
gi 491069032 309 AIDLLITQLNEdiETGSLRVMPAPEIIKRTS 339
Cdd:cd06287  240 AIDLLFASLSG--EERSVEVGPAPELVVRAS 268
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
7-340 2.94e-77

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 240.49  E-value: 2.94e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032   7 KKTITISDVALAAQVSRTTVSHALNGKGEVNPDTRKKIQEIAEQLGYRPNRFAKALRSGGTKTIALIstIPS-------- 78
Cdd:COG1609    1 RKRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVV--VPDlsnpffae 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  79 ---AISGGASKLGFMMEVANVAAIYALEHDLYILLvpfIDHnnfdgnlmNVDGVILLEPCLNDPIVKKLLQYKIPLVCIG 155
Cdd:COG1609   79 llrGIEEAARERGYQLLLANSDEDPEREREALRLL---LSR--------RVDGLILAGSRLDDARLERLAEAGIPVVLID 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 156 TPGQDNkEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNASLKAEEIYSQYCQQYAMT-EVVYKVEEHLGEMGG 234
Cdd:COG1609  148 RPLPDP-GVPSVGVDNRAGARLATEHLIELGHRRIAFIGGPADSSSARERLAGYREALAEAGLPpDPELVVEGDFSAESG 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 235 KSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTRYNGIRALTSNPPLTAVDLHLDDVAKIAIDLLI 314
Cdd:COG1609  227 YEAARRLLARGPRPTAIFCANDLMALGALRALREAGLRVPEDVSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLL 306
                        330       340
                 ....*....|....*....|....*.
gi 491069032 315 TQLNEDIETGSLRVMPaPEIIKRTSS 340
Cdd:COG1609  307 DRIEGPDAPPERVLLP-PELVVREST 331
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
69-335 5.43e-35

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: 128.40  E-value: 5.43e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  69 TIALIstIPSaISGGasklgFMMEVANVAAIYALEHDLYILLvpFIDHNNFDGNL--------MNVDGVILLEPCLNDPI 140
Cdd:cd06267    1 TIGLI--VPD-ISNP-----FFAELLRGIEDAARERGYSLLL--CNTDEDPEREReylrlllsRRVDGIILAPSSLDDEL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 141 VKKLLQYKIPLVCIGTPGqDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNASLKAEEIYSQYCQQYAMTE 220
Cdd:cd06267   71 LEELLAAGIPVVLIDRRL-DGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIGGPLDLSTSRERLEGYRDALAEAGLPV 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 221 V-VYKVEEHLGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTrYNGIR-ALTSNPPLTAV 298
Cdd:cd06267  150 DpELVVEGDFSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRVPEDISVVG-FDDIPlAALLTPPLTTV 228
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 491069032 299 DLHLDDVAKIAIDLLITQLNEDIETGSLRVMPaPEII 335
Cdd:cd06267  229 RQPAYEMGRAAAELLLERIEGEEEPPRRIVLP-TELV 264
lacI PRK09526
lac repressor; Reviewed
6-345 2.55e-32

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 123.57  E-value: 2.55e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032   6 NKKTITISDVALAAQVSRTTVSHALNGKGEVNPDTRKKIQEIAEQLGYRPNRFAKALRSGGTKTIALIST---------I 76
Cdd:PRK09526   2 KSKPVTLYDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTslalhapsqI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  77 PSAISGGASKLGF--MMEVANVAAIYALEHDLYILLVpfidhnnfdgnlMNVDGVILLEPcLNDPIVKKLLQYKIPLVCI 154
Cdd:PRK09526  82 AAAIKSRADQLGYsvVISMVERSGVEACQAAVNELLA------------QRVSGVIINVP-LEDADAEKIVADCADVPCL 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 155 GTPGQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITG-QSKRNASLKAEEiYSQYCQQYAMTEVVyKVEEHLGEMG 233
Cdd:PRK09526 149 FLDVSPQSPVNSVSFDPEDGTRLGVEHLVELGHQRIALLAGpESSVSARLRLAG-WLEYLTDYQLQPIA-VREGDWSAMS 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 234 GKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTRYNGIRALTSNPPLTAVDLHLDDVAKIAIDLL 313
Cdd:PRK09526 227 GYQQTLQMLREGPVPSAILVANDQMALGVLRALHESGLRVPGQISVIGYDDTEDSSYFIPPLTTIKQDFRLLGKEAVDRL 306
                        330       340       350
                 ....*....|....*....|....*....|..
gi 491069032 314 ITQLNEDIETGSLRvMPAPEIIKRTSSVQISS 345
Cdd:PRK09526 307 LALSQGQAVKGSQL-LPTSLVVRKSTAPPNTQ 337
PRK10014 PRK10014
DNA-binding transcriptional repressor MalI; Provisional
5-337 1.54e-31

DNA-binding transcriptional repressor MalI; Provisional


Pssm-ID: 182193 [Multi-domain]  Cd Length: 342  Bit Score: 121.36  E-value: 1.54e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032   5 VNKKtITISDVALAAQVSRTTVSHALNGKGEVNPDTRKKIQEIAEQLGYRPNRFAKALRSGGTKTIALIS---TIPsais 81
Cdd:PRK10014   3 TAKK-ITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVrdlSAP---- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  82 ggasklgFMMEVAnvAAIY-ALEHDLYILlvpFIDHNNFDGNLM----------NVDGVILLEPCLN-DPIVKKLLQYKI 149
Cdd:PRK10014  78 -------FYAELT--AGLTeALEAQGRMV---FLLQGGKDGEQLaqrfstllnqGVDGVVIAGAAGSsDDLREMAEEKGI 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 150 PLVCIGTpGQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSkrnASLKAEEIYSQYCQ---QYAM---TEVVY 223
Cdd:PRK10014 146 PVVFASR-ASYLDDVDTVRPDNMQAAQLLTEHLIRNGHQRIAWLGGQS---SSLTRAERVGGYCAtllKFGLpfhSEWVL 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 224 KVEEHlgEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMkvVTRYNGIR------------ALTs 291
Cdd:PRK10014 222 ECTSS--QKQAAEAITALLRHNPTISAVVCYNETIAMGAWFGLLRAGRQSGESG--VDRYFEQQvalaaftdvpeaELD- 296
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 491069032 292 NPPLTAVDLHLDDVAKIAIDLLITQLNEDiETGSLRVMPAPEIIKR 337
Cdd:PRK10014 297 DPPLTWASTPAREIGRTLADRMMQRITHE-ETHSRNLIIPPRLIAR 341
PBP1_MalR-like cd06294
ligand-binding domain of maltose transcription regulator MalR which is a member of the ...
126-321 1.65e-31

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: 119.61  E-value: 1.65e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 126 VDGVILLEPCLNDPIVKKLLQYKIPLVCIGTPgQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNASLKA 205
Cdd:cd06294   61 VDGFILLYSKEDDPLIEYLKEEGFPFVVIGKP-LDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIGGDKNLVVSIDR 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 206 EEIYSQYCQQ--YAMTEVVYKVEEHLGEmGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTRY 283
Cdd:cd06294  140 LQGYKQALKEagLPLDDDYILLLDFSEE-DGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRVPEDVSIISFN 218
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 491069032 284 NGIRALTSNPPLTAVDLHLDDVAKIAIDLLITQLNEDI 321
Cdd:cd06294  219 NSPLAELASPPLTSVDINPYELGREAAKLLINLLEGPE 256
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
125-339 4.77e-30

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: 115.31  E-value: 4.77e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 125 NVDGVILlepCLNDPIVKKLLQYKIPLVCIGTpgQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNASLK 204
Cdd:cd06291   55 KVDGIIL---GSHSLDIEEYKKLNIPIVSIDR--YLSEGIPSVSSDNYQGGRLAAEHLIEKGCKKILHIGGPSNNSPANE 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 205 AEEIYSQYCQQYAMTEVVYKVEEHLGEMG-GKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTrY 283
Cdd:cd06291  130 RYRGFEDALKEAGIEYEIIEIDENDFSEEdAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRVPEDVQIIG-F 208
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491069032 284 NGIR-ALTSNPPLTAVDLHLDDVAKIAIDLLITQLNEDIETGSLRVMPaPEIIKRTS 339
Cdd:cd06291  209 DGIEiSELLYPELTTIRQPIEEMAKEAVELLLKLIEGEEIEESRIVLP-VELIERET 264
PBP1_GalR cd01544
ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory ...
100-339 3.33e-26

ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand-binding domain of DNA transcription repressor GalR which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalR is a dimeric protein like GalS and is exclusively involved in the regulation of galactose permease, the low-affinity galactose transporter. GalS is involved in regulating expression of the high-affinity galactose transporter encoded by the mgl operon. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are structurally homologous to the periplasmic sugar binding of ABC-type transport systems.


Pssm-ID: 380486 [Multi-domain]  Cd Length: 269  Bit Score: 105.30  E-value: 3.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 100 YALEHDLYILLVpFIDHNNFDGNLMNVDGVILLEPcLNDPIVKKLLQYKIPLVCIGTPGqDNKEVPYVDLQSEQTAIKLL 179
Cdd:cd01544   29 EAKKLGYEIKTI-FRDDEDLESLLEKVDGIIAIGK-FSKEEIEKLKKLNPNIVFVDSNP-DPDGFDSVVPDFEQAVRQAL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 180 EHLVEEGaHQ-IALITGQSKRNASLKAEE-----IYSQYCQQYAMTEVVYKVEEHLGEMGGKSAIAEIMKQYPKTDAILV 253
Cdd:cd01544  106 DYLIELG-HRrIGFIGGKEYTSDDGEEIEdprlrAFREYMKEKGLYNEEYIYIGEFSVESGYEAMKELLKEGDLPTAFFV 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 254 MIDTFATGVMQYLTEKGISVPKQMKVVTrYNGI-RALTSNPPLTAVDLHLDDVAKIAIDLLITQLNEDIETgSLRVMPAP 332
Cdd:cd01544  185 ASDPMAIGALRALQEAGIKVPEDISIIS-FNDIeVAKYVTPPLTTVHIPTEEMGRTAVRLLLERINGGRTI-PKKVLLPT 262

                 ....*..
gi 491069032 333 EIIKRTS 339
Cdd:cd01544  263 KLIERES 269
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
10-75 1.09e-23

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 92.65  E-value: 1.09e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491069032    10 ITISDVALAAQVSRTTVSHALNGKGEVNPDTRKKIQEIAEQLGYRPNRFAKALRSGGTKTIALIST 75
Cdd:smart00354   1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVP 66
PBP1_AglR-like cd20010
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ...
69-335 3.54e-23

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


Pssm-ID: 380665 [Multi-domain]  Cd Length: 269  Bit Score: 96.85  E-value: 3.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  69 TIALISTIPSAISGGASklgFMMEVANVAAIYAlEHDLYILLVPFIDHNN--------FDGNLmnVDGVILLEPCLNDPI 140
Cdd:cd20010    1 AIGLVLPLDPGDLGDPF---FLEFLAGLSEALA-ERGLDLLLAPAPSGEDelatyrrlVERGR--VDGFILARTRVNDPR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 141 VKKLLQYKIPLVCIGtPGQDNKEVPYVDLQSEQTAIKLLEHLVEEGaHQ-IALITGQSKRNASLKAEEIYSQYCQQYAMT 219
Cdd:cd20010   75 IAYLLERGIPFVVHG-RSESGAPYAWVDIDNEGAFRRATRRLLALG-HRrIALLNGPEELNFAHQRRDGYRAALAEAGLP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 220 -EVVYKVEEHLGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTRYNGIRALTS-NPPLTA 297
Cdd:cd20010  153 vDPALVREGPLTEEGGYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLSPGKDVSVIGHDDLLPALEYfSPPLTT 232
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 491069032 298 VDLHLDDVAKIAIDLLITQLNEDiETGSLRVMPAPEII 335
Cdd:cd20010  233 TRSSLRDAGRRLAEMLLALIDGE-PAAELQELWPPELI 269
PRK10423 PRK10423
transcriptional repressor RbsR; Provisional
14-339 5.17e-23

transcriptional repressor RbsR; Provisional


Pssm-ID: 182448 [Multi-domain]  Cd Length: 327  Bit Score: 97.46  E-value: 5.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  14 DVALAAQVSRTTVSHALNGKGEVNPDTRKKIQEIAEQLGYRPNRFAKALRSGGTKTIALISTipsaisggASKLGFMMEV 93
Cdd:PRK10423   3 DVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLIT--------ASTNPFYSEL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  94 anvaaIYALEHDLY------ILLVPFIDHNNFDGNL-----MNVDGVILLEPCLNDPIVKKLLQY-KIPLV--------C 153
Cdd:PRK10423  75 -----VRGVERSCFergyslVLCNTEGDEQRMNRNLetlmqKRVDGLLLLCTETHQPSREIMQRYpSVPTVmmdwapfdG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 154 IGTPGQDNKevpyvdLQSEQTAIKlleHLVEEGAHQIALITG-QSKRNASLKAEEiYSQYCQQYAMT-EVVYKVEEHLGE 231
Cdd:PRK10423 150 DSDLIQDNS------LLGGDLATQ---YLIDKGYTRIACITGpLDKTPARLRLEG-YRAAMKRAGLNiPDGYEVTGDFEF 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 232 MGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTrYNGI---RALTsnPPLTAVDLHLDDVAKI 308
Cdd:PRK10423 220 NGGFDAMQQLLALPLRPQAVFTGNDAMAVGVYQALYQAGLSVPQDIAVIG-YDDIelaRYMT--PPLTTIHQPKDELGEL 296
                        330       340       350
                 ....*....|....*....|....*....|.
gi 491069032 309 AIDLLITQLnEDIETGSLRVMPAPEIIKRTS 339
Cdd:PRK10423 297 AIDVLIHRM-AQPTLQQQRLQLTPELMERGS 326
PBP1_CcpA-like cd19975
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
124-339 1.92e-22

ligand-binding domain of putative DNA transcription regulators highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.


Pssm-ID: 380630 [Multi-domain]  Cd Length: 269  Bit Score: 94.93  E-value: 1.92e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 124 MNVDGVILLEPCLNDPIVKKLLQYKIPLVCIGTpGQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITG-QSKRNAS 202
Cdd:cd19975   54 KRVDGIIFASGTLTEENKQLLKNMNIPVVLVST-ESEDPDIPSVKIDDYQAAYDATNYLIKKGHRKIAMISGpLDDPNAG 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 203 LKaeeIYSQYCQqyAMTEVVYKVEEHL---GEM---GGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQ 276
Cdd:cd19975  133 YP---RYEGYKK--ALKDAGLPIKENLiveGDFsfkSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYDHGIRVPED 207
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491069032 277 MKVVTrYNGIR-ALTSNPPLTAVDLHLDDVAKIAIDLLITQLNEDIETGSLRVMPApEIIKRTS 339
Cdd:cd19975  208 ISVIG-FDNTEiAEMSIPPLTTVSQPFYEMGKKAVELLLDLIKNEKKEEKSIVLPH-QIIERES 269
HTH_LacI cd01392
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ...
14-64 2.21e-21

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: 85.92  E-value: 2.21e-21
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 491069032  14 DVALAAQVSRTTVSHALNGKGEVNPDTRKKIQEIAEQLGYRPNRFAKALRS 64
Cdd:cd01392    2 DIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
PBP1_AglR_RafR-like cd06292
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ...
125-340 3.52e-21

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


Pssm-ID: 380515 [Multi-domain]  Cd Length: 273  Bit Score: 91.56  E-value: 3.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 125 NVDGVILLEPCLNDPIVKKLLQYKIPLVCIGtPGQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSkrnASLK 204
Cdd:cd06292   59 RVDGFVLASTRHDDPRVRYLHEAGVPFVAFG-RANPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIGGPE---GSVP 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 205 AEEIYSQYCQqyAMTEV------VYKVEEHLGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMK 278
Cdd:cd06292  135 SDDRLAGYRA--ALEEAglpfdpGLVVEGENTEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGLRVGRDVS 212
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491069032 279 VVTrYNGIRALT-SNPPLTAVDLHLDDVAKIAIDLLITQL--NEDIETGSLRvmpAPEIIKRTSS 340
Cdd:cd06292  213 VVG-FDDSPLAAfTHPPLTTVRQPIDEIGRAVVDLLLAAIegNPSEPREILL---QPELVVRESS 273
PBP1_CelR cd06295
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ...
67-339 7.84e-21

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


Pssm-ID: 380518 [Multi-domain]  Cd Length: 273  Bit Score: 90.39  E-value: 7.84e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  67 TKTIALIstIPSAISGGASKLG-FMMEVanVAAI-YAL-EHDLYILLVPFIDHNNFDGNLMN---VDGVILLEPCLNDPI 140
Cdd:cd06295    3 SRTIAVV--VPMDPHGDQSITDpFFLEL--LGGIsEALtDRGYDMLLSTQDEDANQLARLLDsgrADGLIVLGQGLDHDA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 141 VKKLLQYKIPLVCIGTPGQDnkeVPYVDLQSE--QTAIKLLEHLVEEGAHQIALITGQSKRNASLKaeeiYSQYCQqyAM 218
Cdd:cd06295   79 LRELAQQGLPMVVWGAPEDG---QSYCSVGSDnvKGGALATEHLIEIGRRRIAFLGDPPHPEVADR----LQGYRD--AL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 219 TE------VVYKVEEHLGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTrYNGIR-ALTS 291
Cdd:cd06295  150 AEagleadPSLLLSCDFTEESGYAAMRALLDSGTAFDAIFAASDLIAMGAIRALRERGISVPGDVAVVG-YDDIPlAAYF 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 491069032 292 NPPLTAVDLHLDDVAKIAIDLLITQLNEDIETGSLrvMPApEIIKRTS 339
Cdd:cd06295  229 RPPLTTVRQDLALAGRLLVEKLLALIAGEPVTSSM--LPV-ELVVRES 273
PRK10703 PRK10703
HTH-type transcriptional repressor PurR;
11-339 8.65e-21

HTH-type transcriptional repressor PurR;


Pssm-ID: 236739 [Multi-domain]  Cd Length: 341  Bit Score: 91.71  E-value: 8.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  11 TISDVALAAQVSRTTVSHALNGKGEVNPDTRKKIQEIAEQLGYRPNRFAKALRSGGTKTIALISTipsaisggASKLGFM 90
Cdd:PRK10703   3 TIKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLAT--------SSEAPYF 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  91 MEVanvaaIYALEHDLY---ILLVPFIDHNNFDG-----NLM---NVDGVILLEPCLNDPIVKKLLQYK-IPLVCIGTPG 158
Cdd:PRK10703  75 AEI-----IEAVEKNCYqkgYTLILCNAWNNLEKqraylSMLaqkRVDGLLVMCSEYPEPLLAMLEEYRhIPMVVMDWGE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 159 QDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNAslkAEEIYSQYCQqyAMTEVVYKV-EEHLGE-----M 232
Cdd:PRK10703 150 AKADFTDAIIDNAFEGGYLAGRYLIERGHRDIGVIPGPLERNT---GAGRLAGFMK--AMEEANIKVpEEWIVQgdfepE 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 233 GGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTrYNGIR-ALTSNPPLTAVDLHLDDVAKIAID 311
Cdd:PRK10703 225 SGYEAMQQILSQKHRPTAVFCGGDIMAMGAICAADEMGLRVPQDISVIG-YDNVRnARYFTPALTTIHQPKDRLGETAFN 303
                        330       340       350
                 ....*....|....*....|....*....|.
gi 491069032 312 LL---ITQLNEDIETGSLRvmpaPEIIKRTS 339
Cdd:PRK10703 304 MLldrIVNKREEPQTIEVH----PRLVERRS 330
PBP1_LacI-like cd06279
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ...
87-299 2.69e-20

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: 89.19  E-value: 2.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  87 LGFMMEVANVAAiyalEHDLYILLVPFIDHNNFDGNLMN--VDGVILLEPCLNDPIVKKLLQYKIPLVCIGTPGQDNkeV 164
Cdd:cd06279   20 AQFLRGVAEVCE----EEGLGLLLLPATDEGSAAAAVRNaaVDGFIVYGLSDDDPAVAALRRRGLPLVVVDGPAPPG--I 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 165 PYVDLQSEQTAIKLLEHLVEEGAHQIALIT---GQSKRNASLKAEEIYSQY----------CQQyAMTE--------VVY 223
Cdd:cd06279   94 PSVGIDDRAAARAAARHLLDLGHRRIAILSlrlDRGRERGPVSAERLAAATnsvarerlagYRD-ALEEagldlddvPVV 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491069032 224 KVEEHlGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTrYNGIR-ALTSNPPLTAVD 299
Cdd:cd06279  173 EAPGN-TEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARERGLRVPEDLSVTG-FDDIPeAAAADPGLTTVR 247
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
124-330 4.75e-20

ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of TreR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380484 [Multi-domain]  Cd Length: 259  Bit Score: 87.94  E-value: 4.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 124 MNVDGVILLEPCLNDPIVKKLLQYKIPLVCIGtpgQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALI--------TG 195
Cdd:cd01542   54 QKVDGIILFATEITDEHRKALKKLKIPVVVLG---QEHEGFSCVYHDDYGAGKLLGEYLLKKGHKNIAYIgvdeediaVG 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 196 QSKRNAslkaeeiYSQYCQQYAMTEVVYkVEEHLGEMGGKSAIAEIMKQYpKTDAILVMIDTFATGVMQYLTEKGISVPK 275
Cdd:cd01542  131 VARKQG-------YLDALKEHGIDEVEI-VETDFSMESGYEAAKELLKEN-KPDAIICATDNIALGAIKALRELGIKIPE 201
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491069032 276 QMKVVtrynGI----RALTSNPPLTAVDLHLDDVAKIAIDLLITQLNEDiETGSLRVMP 330
Cdd:cd01542  202 DISVA----GFggydLSEFVSPSLTTVKFDYEEAGEKAAELLLDMIEGE-KVPKKQKLP 255
PBP1_DegA_Like cd19976
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
69-339 5.03e-20

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: 88.07  E-value: 5.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  69 TIALI---------STIPSAISGGASKLGFMMEVANVAAIYALEHdLYILLvpFIDHNnfdgnlmnVDGVILLEPCLNDP 139
Cdd:cd19976    1 TIGLIvpdisnpffSELVRGIEDTLNELGYNIILCNTYNDFEREK-KYIQE--LKERN--------VDGIIIASSNISDE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 140 IVKKLLQ-YKIPLVCIGTPGQDNkEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQskrNASLKAEEIYSQYCQqyAM 218
Cdd:cd19976   70 AIIKLLKeEKIPVVVLDRYIEDN-DSDSVGVDDYRGGYEATKYLIELGHTRIGCIVGP---PSTYNEHERIEGYKN--AL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 219 TEVVYKVEEHLGEM------GGKSAIAEIMKQYPKTdAILVMIDTFATGVMQYLTEKGISVPKQMKVVTRYNGIRALTSN 292
Cdd:cd19976  144 QDHNLPIDESWIYSgessleGGYKAAEELLKSKNPT-AIFAGNDLIAMGVYRAALELGLKIPEDLSVIGFDNIILSEYIT 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 491069032 293 PPLTAVDLHLDDVAKIAIDLLITQLNEDIETGSLRVMPaPEIIKRTS 339
Cdd:cd19976  223 PALTTIAQPIFEMGQEAAKLLLKIIKNPAKKKEEIVLP-PELIKRDS 268
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
125-335 1.39e-19

periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its close homologs; This group includes the ligand-binding domain of putative repressor of the endoglucanase operon from Paenibacillus polymyxa and its close homologs from other bacteria. This group belongs to the LacI-GalR family repressors and are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding.


Pssm-ID: 380632 [Multi-domain]  Cd Length: 264  Bit Score: 86.81  E-value: 1.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 125 NVDGVILLEPCLNDPIVKKLLQYKIPLVCIG-TPgqDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNASL 203
Cdd:cd19977   55 QVDGIIIAPTGGNEDLIEKLVKSGIPVVFVDrYI--PGLDVDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLELSTRQ 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 204 KAEEIYSQYCQQYAM---TEVVYKVEEhlgEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVV 280
Cdd:cd19977  133 ERLEGYKAALADHGLpvdEELIKHVDR---QDDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRIPDDIALI 209
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491069032 281 TrYNGIRALT-SNPPLTAVDLHLDDVAKIAIDLLITQLNEDIETGSLRVMPAPEII 335
Cdd:cd19977  210 G-FDDIPWADlFNPPLTVIAQPTYEIGRKAAELLLDRIENKPKGPPRQIVLPTELI 264
PBP1_LacI cd01574
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ...
79-339 2.60e-19

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: 86.10  E-value: 2.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  79 AISGGASKLGFMMEVANVAAiYALEHDLYILLVPfIDHNNFD------GNLM--NVDGVILLEPclnDPIVKKLLQYK-- 148
Cdd:cd01574    4 VIATGLSLYGPASTLAGIER-AARERGYSVSIAT-VDEDDPAsvrealDRLLsqRVDGIIVIAP---DEAVLEALRRLpp 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 149 -IPLVCIGTPGQDNkeVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNASLKAEEIYSQYCQQyAMTEVVYKVEE 227
Cdd:cd01574   79 gLPVVIVGSGPSPG--VPTVSIDQEEGARLATRHLLELGHRRIAHIAGPLDWVDARARLRGWREALEE-AGLPPPPVVEG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 228 HLGEMGGKSAIAEIMKQYPKTdAILVMIDTFATGVMQYLTEKGISVPKQMKVV-------TRYngiraltSNPPLTAVDL 300
Cdd:cd01574  156 DWSAASGYRAGRRLLDDGPVT-AVFAANDQMALGALRALHERGLRVPEDVSVVgfddipeAAY-------FVPPLTTVRQ 227
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 491069032 301 HLDDVAKIAIDLLITQLNEDIETGSLRVMPaPEIIKRTS 339
Cdd:cd01574  228 DFAELGRRAVELLLALIEGPAPPPESVLLP-PELVVRES 265
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
74-339 2.00e-18

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: 83.74  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  74 STIPSAISGGASKLGFMMEVANVAAIYALEHDLYILLvpfidhnnFDGNlmnVDGVILLEPCLNDPIVKKLlQYKIPLVC 153
Cdd:cd06284   15 SEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDML--------RSRR---VDGVILLSGRLDAELLSEL-SKRYPIVQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 154 IGTPgQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNASLKAEEIYSQYCQQYAMTEV-VYKVEEHLGEM 232
Cdd:cd06284   83 CCEY-IPDSGVPSVSIDNEAAAYDATEYLISLGHRRIAHINGPLDNVYARERLEGYRRALAEAGLPVDeDLIIEGDFSFE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 233 GGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTrYNGIR-ALTSNPPLTAVDLHLDDVAKIAID 311
Cdd:cd06284  162 AGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGLRVPEDVSVIG-FDDIEfAEMFSPSLTTIRQPRYEIGETAAE 240
                        250       260
                 ....*....|....*....|....*...
gi 491069032 312 LLITQLNEDIETGSLRVMPApEIIKRTS 339
Cdd:cd06284  241 LLLEKIEGEGVPPEHIILPH-ELIVRES 267
PBP1_AglR_RafR-like cd06271
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ...
88-335 2.04e-18

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


Pssm-ID: 380495 [Multi-domain]  Cd Length: 264  Bit Score: 83.63  E-value: 2.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  88 GFMMEVANVAAIYALEHDLYILLVPFIDHNNFDG--NLM---NVDGVILLEPCLNDPIVKKLLQYKIPLVCIGTPGQDnK 162
Cdd:cd06271   15 GTVSE*VSGITEEAGTTGYHLLVWPFEEAES*VPirDLVetgSADGVILSEIEPNDPRVQFLTKQNFPFVAHGRSD*P-I 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 163 EVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNASLKAEEIYSQYCQQYAMTEVVYKVEEHLgeMGGKSAIAEIM 242
Cdd:cd06271   94 GHAWVDIDNEAGAYEAVERLAGLGHRRIAFIVPPARYSPHDRRLQGYVRA*RDAGLTGYPLDADTTL--EAGRAAAQRLL 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 243 KQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTRYN--GIRALTSnPPLTAVDLHLDDVAKIAIDLLITQLNeD 320
Cdd:cd06271  172 ALSPRPTAIVTMNDSATIGLVAGLQAAGLKIGEDVSIIGKDSapFLGAMIT-PPLTTVHAPIAEAGRELAKALLARID-G 249
                        250
                 ....*....|....*
gi 491069032 321 IETGSLRVMPAPEII 335
Cdd:cd06271  250 EDPETLQVLVQPSLS 264
PBP1_PurR cd06275
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ...
126-339 1.11e-17

ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli; Ligand-binding domain of purine repressor, PurR, which functions as the master regulatory protein of de novo purine nucleotide biosynthesis in Escherichia coli. This dimeric PurR belongs to the LacI-GalR family of transcription regulators and is activated to bind to DNA operator sites by initially binding either of high affinity corepressors, hypoxanthine or guanine. PurR is composed of two functional domains: aan N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the purine transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380499 [Multi-domain]  Cd Length: 269  Bit Score: 81.53  E-value: 1.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 126 VDGVILLEPCLNDPIVKKLLQYK-IPLVCIGTPGQ-DNKEVPYVDlqSEQTAIKLLEHLVEEGAHQIALITGQSKRNASL 203
Cdd:cd06275   56 VDGLLLMCSEMTDDDAELLAALRsIPVVVLDREIAgDNADAVLDD--SFQGGYLATRHLIELGHRRIGCITGPLEHSVSR 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 204 KAEEIYSQYCQQyAMTEVV--YKVEEHLGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVT 281
Cdd:cd06275  134 ERLAGFRRALAE-AGIEVPpsWIVEGDFEPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGLRVPQDISIIG 212
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 491069032 282 rYNGIR-ALTSNPPLTAVDLHLDDVAKIAIDLLITQLNEDIETGSLRVMPaPEIIKRTS 339
Cdd:cd06275  213 -YDDIElARYFSPALTTIHQPKDELGELAVELLLDRIENKREEPQSIVLE-PELIERES 269
PBP1_GalS-like cd06270
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ...
126-337 1.18e-17

ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism; Ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory proteins involved in galactose transport and metabolism. Transcription of the galactose regulon genes is regulated by Gal iso-repressor (GalS) and Gal repressor (GalR) in different ways, but both repressors recognize the same DNA binding site in the absence of D-galactose. GalS is a dimeric protein like GalR,and its major role is in regulating expression of the high-affinity galactose transporter encoded by the mgl operon, whereas GalR is the exclusive regulator of galactose permease, the low-affinity galactose transporter. GalS and GalR are members of the LacI-GalR family of transcription regulators and both contain the type 1 periplasmic binding protein-like fold. Hence, they are homologous to the periplasmic sugar binding of ABC-type transport systems.


Pssm-ID: 380494 [Multi-domain]  Cd Length: 266  Bit Score: 81.41  E-value: 1.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 126 VDGVILLEPCLNDPIVKKLLQYKIPLVCIgtpgqdNKEVP-----YVDLQSEQTAIKLLEHLVEEGAHQIALITGqskRN 200
Cdd:cd06270   56 CDAIILHSRALSDEELILIAEKIPPLVVI------NRYIPgladrCVWLDNEQGGRLAAEHLLDLGHRRIACITG---PL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 201 ASLKAEEIYSQYCQqyAMTEVVYKVEEHL------GEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVP 274
Cdd:cd06270  127 DIPDARERLAGYRD--ALAEAGIPLDPSLiiegdfTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGIKVP 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491069032 275 KQMKVVtrynGIR----ALTSNPPLTAVDLHLDDVAKIAIDLLITQLNEDIETGSLRVMpaPEIIKR 337
Cdd:cd06270  205 EDVSVI----GFDdvplARYLSPKLTTVHYPIEEMAQAAAELALNLAYGEPLPISHEFT--PTLIER 265
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
181-340 1.23e-17

Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional regulatory proteins. It is related to bacterial periplasmic binding proteins, although this domain is unlikely to be found in the periplasm. This domain acts as a sensor binding small molecule ligands that the DNA-binding domain responds to. This domain recognizes Sugars, sugar phosphates, sugar acids and purines (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1. https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 433159 [Multi-domain]  Cd Length: 160  Bit Score: 78.92  E-value: 1.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  181 HLVEEGAHQIALITGQSKRNASLkAEEI---YSQYCQQYAMTEVVYKVEEhLGEMGGKSAIAEIMKQYPKTDAILVMIDT 257
Cdd:pfam13377   1 HLAELGHRRIALIGPEGDRDDPY-SDLRergFREAARELGLDVEPTLYAG-DDEAEAAAARERLRWLGALPTAVFVANDE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  258 FATGVMQYLTEKGISVPKQMKVVTrYNG--IRALTSnPPLTAVDLHLDDVAKIAIDLLITQLNEDIETGSLRVMPaPEII 335
Cdd:pfam13377  79 VALGVLQALREAGLRVPEDLSVIG-FDDspLAALVS-PPLTTVRVDAEELGRAAAELLLDLLNGEPAPPERVLLP-PELV 155

                  ....*
gi 491069032  336 KRTSS 340
Cdd:pfam13377 156 EREST 160
PBP1_SalR cd01545
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ...
124-339 1.60e-17

ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of bacterial transcription regulators. The SalR binds to glucose based compound Salicin which is chemically related to aspirin. The ligand-binding of SalR is structurally homologous to the periplasmic sugar-binding domain of ABC-transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380487 [Multi-domain]  Cd Length: 270  Bit Score: 81.06  E-value: 1.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 124 MNVDGVILLEPCLNDPIVKKLLQ-YKIPLVCIGtPGQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNAS 202
Cdd:cd01545   55 SRPDGVILTPPLSDDPALLDALDeLGIPYVRIA-PGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAGPPDHGAS 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 203 lkaEEIYSQYCQqyAMTEVVYKVEEHL---GEM---GGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQ 276
Cdd:cd01545  134 ---AERLEGFRD--ALAEAGLPLDPDLvvqGDFtfeSGLEAAEALLDLPDRPTAIFASNDEMAAGVLAAAHRLGLRVPDD 208
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491069032 277 MKVVtrynG-----IRALTSnPPLTAVDLHLDDVAKIAIDLLITQLNEDiETGSLRVMPAPEIIKRTS 339
Cdd:cd01545  209 LSVA----GfddspIARLVW-PPLTTVRQPIAEMARRAVELLIAAIRGA-PAGPERETLPHELVIRES 270
PBP1_CcpA cd06298
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ...
121-339 7.36e-17

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: 79.26  E-value: 7.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 121 GNLMN--VDGVILLEPCLNDPIVKKLLQYKIPLVCIGTPgQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGqSK 198
Cdd:cd06298   49 NTMLSkqVDGIIFMGDELTEEIREEFKRSPVPVVLAGTV-DSDHEIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSG-PL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 199 RNASLKAEEIysqycQQY--AMTEVVYKVEEHLGEMGGKS-----AIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGI 271
Cdd:cd06298  127 KEYINNDKKL-----QGYkrALEEAGLEFNEPLIFEGDYDydsgyELYEELLESGEPDAAIVVRDEIAVGLLNAAQDRGL 201
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491069032 272 SVPKQMKVVTRYNGIRALTSNPPLTAVDLHLDDVAKIAIDLLiTQLNEDIETGSLRVMPAPEIIKRTS 339
Cdd:cd06298  202 KVPEDLEIIGFDNTRYATMSRPQLTSINQPLYDIGAVAMRLL-TKLMNKEEVEETIVKLPHSIIWRQS 268
PBP1_CcpB-like cd06286
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ...
126-337 1.01e-16

ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species; This group includes the ligand-binding domain of a novel transcription factor implicated in catabolite repression in Bacillus and Clostridium species. Catabolite control protein B (CcpB) is 30% identical in sequence to CcpA which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. Like CcpA, the DNA-binding protein CcpB exerts its catabolite-repressing effect by a mechanism dependent on the presence of HPr(Ser-P), the small phosphocarrier proteins of the phosphoenolpyruvate-sugar phosphotransferase system, but with a less significant degree.


Pssm-ID: 380509 [Multi-domain]  Cd Length: 262  Bit Score: 78.74  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 126 VDGVILLEPCLNDPIVKKLLQYKiPLVCIGTPgqDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNAS--- 202
Cdd:cd06286   56 IDGLIITSRENDWEVIEPYAKYG-PIVLCEET--DSPDIPSVYIDRYEAYLEALEYLKEKGHRKIGYCLGRPESSSAstq 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 203 --LKAeeiYSQYCQQYAMT-------EVVYKVEEhlgemgGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISV 273
Cdd:cd06286  133 arLKA---YQDVLGEHGLSlreewifTNCHTIED------GYKLAKKLLALKERPDAIFTNSDEVAAGIIAEAQKNGIRV 203
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491069032 274 PKQMKVVTRYNGIraLTSNPPLTAVDLHLDDVAKIAIDLLITQLNEDIETgslRVMPAPEIIKR 337
Cdd:cd06286  204 PEDLAVIGFDNQP--ISELLNLTTIDQPLEEMGKEAFELLLSQLESKEPT---KKELPSKLIER 262
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
126-340 2.74e-16

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: 77.65  E-value: 2.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 126 VDGVILLEPCLNDPIVKKLLQYKIPLVCIGTPGqDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNASLKA 205
Cdd:cd06285   56 VDGLIITPARDDAPDLQELAARGVPVVLVDRRI-GDTALPSVTVDNELGGRLATRHLLELGHRRIAVVAGPLNASTGRDR 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 206 EEIYSQYCQQYAMTEV-VYKVEEHLGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTrYN 284
Cdd:cd06285  135 LRGYRRALAEAGLPVPdERIVPGGFTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGLRVPEDLSVVG-FD 213
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491069032 285 GIR-ALTSNPPLTAVDLHLDDVAKIAIDLLITQLNEDIETGSLRVMPaPEIIKRTSS 340
Cdd:cd06285  214 DIPlAAFLPPPLTTVRQPKYEMGRRAAELLLQLIEGGGRPPRSITLP-PELVVREST 269
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
125-339 4.25e-16

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: 77.19  E-value: 4.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 125 NVDGVILLEPCLNDPIVKKLLQYKIPLVCIGtPGQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNASLK 204
Cdd:cd06278   54 RVDGVIVTSATLSSELAEECARRGIPVVLFN-RVVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLGGPEGTSTSRE 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 205 AEEIYSQYCQQYAMTEVVYkVEEHLGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYL-TEKGISVPKQMKVVTrY 283
Cdd:cd06278  133 RERGFRAALAELGLPPPAV-EAGDYSYEGGYEAARRLLAAPDRPDAIFCANDLMALGALDAArQEGGLVVPEDISVVG-F 210
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 491069032 284 NGIrALTSNPP--LTAVDLHLDDVAKIAIDLLITQLNEDIETGSLRVMPaPEIIKRTS 339
Cdd:cd06278  211 DDI-PMAAWPSydLTTVRQPIEEMAEAAVDLLLERIENPETPPERRVLP-GELVERGS 266
PBP1_CatR-like cd06296
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ...
125-340 3.76e-15

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: 74.24  E-value: 3.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 125 NVDGVILLEPCLNDPIVKKLLQYKIPLVCIGTPGQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKrnaSLK 204
Cdd:cd06296   55 GSAGVVLVTSDPTSRQLRLLRSAGIPFVLIDPVGEPDPDLPSVGATNWAGGRLATEHLLDLGHRRIAVITGPPR---SVS 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 205 AEEIYSQYcqQYAMTEV---VYKVEEHLGEMGGKSAIAEIMKQY----PKTdAILVMIDTFATGVMQYLTEKGISVPKQM 277
Cdd:cd06296  132 GRARLAGY--RAALAEAgiaVDPDLVREGDFTYEAGYRAARELLelpdPPT-AVFAGNDEQALGVYRAARALGLRVPDDL 208
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491069032 278 KVVTRYNGIRALTSNPPLTAVDLHLDDVAKIAIDLLItQLNEDIETGSLRVMPAPEIIKRTSS 340
Cdd:cd06296  209 SVIGFDDTPPARWTSPPLTTVHQPLREMGAVAVRLLL-RLLEGGPPDARRIELATELVVRGST 270
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
124-337 6.34e-15

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: 73.75  E-value: 6.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 124 MNVDGVILLePCLNDP--IVKKLLQYKIPLVCIGTPgQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSkrnA 201
Cdd:cd06289   54 QGVDGLILS-PAAGTTaeLLRRLKAWGIPVVLALRD-VPGSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLGGLS---D 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 202 SLKAEEIYSQYCQqyAMTE------VVYKVEEHLGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPK 275
Cdd:cd06289  129 SSTRRERLAGFRA--ALAEaglpldESLIVPGPATREAGAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEPGR 206
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491069032 276 QMKVVtrynGIRALT----SNPPLTAVDLHLDDVAKIAIDLLITQLNEDIETGSlRVMPAPEIIKR 337
Cdd:cd06289  207 DIAVV----GFDDVPeaalWTPPLTTVSVHPREIGRRAARLLLRRIEGPDTPPE-RIIIEPRLVVR 267
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
124-339 7.08e-15

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: 73.68  E-value: 7.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 124 MNVDGVILLEPCLNDPIVKKLLQYKIPLVCIGtpgqDNKEVPyVDLQ---SEQTAIKLL-EHLVEEGAHQIALITGQSKR 199
Cdd:cd01575   54 RRPAGLILTGTEHTPATRKLLRAAGIPVVETW----DLPDDP-IDMAvgfSNFAAGRAMaRHLIERGYRRIAFVGARLDG 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 200 NasLKAEEIYSQYCQqyAMTE------VVYKVEEHLGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISV 273
Cdd:cd01575  129 D--SRARQRLEGFRD--ALAEaglplpLVLLVELPSSFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRGIRV 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491069032 274 PKQMKVVTrYNGIR-ALTSNPPLTAVDLHLDDVAKIAIDLLITQLNEDIETGSLRVMPaPEIIKRTS 339
Cdd:cd01575  205 PGDIAIAG-FGDLDiAAALPPALTTVRVPRYEIGRKAAELLLARLEGEEPEPRVVDLG-FELVRRES 269
PBP1_LacI-like cd19974
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
125-339 8.78e-15

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


Pssm-ID: 380629 [Multi-domain]  Cd Length: 270  Bit Score: 73.35  E-value: 8.78e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 125 NVDGVILLEPClNDPIVKKLLQYKIPLVCIGTPGQDNkEVPYVDLQSEQTAIKLLEHLVEEGAHQIALItgqSKRNASLK 204
Cdd:cd19974   58 KVDGIIILGEI-SKEYLEKLKELGIPVVLVDHYDEEL-NADSVLSDNYYGAYKLTSYLIEKGHKKIGFV---GDINYTSS 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 205 AEEIYSQYCQqyAMTE----------VVYKVEEHLGEMGGKSAIAEIMKqyPktDAILVMIDTFATGVMQYLTEKGISVP 274
Cdd:cd19974  133 FMDRYLGYRK--ALLEaglppekeewLLEDRDDGYGLTEEIELPLKLML--P--TAFVCANDSIAIQLIKALKEKGYRVP 206
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 491069032 275 KQMKVVTRYNGIRALTSNPPLTAVDLHLDDVAKIAIDLLITQLnEDIETGSLRVMPAPEIIKRTS 339
Cdd:cd19974  207 EDISVVGFDNIELAELSTPPLTTVEVDKEAMGRRAVEQLLWRI-ENPDRPFEKILVSGKLIERDS 270
PRK11303 PRK11303
catabolite repressor/activator;
11-281 9.35e-15

catabolite repressor/activator;


Pssm-ID: 236897 [Multi-domain]  Cd Length: 328  Bit Score: 74.14  E-value: 9.35e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  11 TISDVALAAQVSRTTVSHALNGKGE---VNPDTRKKIQEIAEQLGYRPNRFAKALRSGGTKTIALIstIP---------- 77
Cdd:PRK11303   2 KLDEIARLAGVSRTTASYVINGKAKqyrVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLI--IPdlentsyari 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  78 -SAISGGASKLGFM-------------MEVAnvaaiyalEHdlyiLLVPFIDhnnfdgnlmnvdgVILLEPCL--NDPIV 141
Cdd:PRK11303  80 aKYLERQARQRGYQlliacsddqpdneMRCA--------EH----LLQRQVD-------------ALIVSTSLppEHPFY 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 142 KKLLQYKIPLVCIGTPgQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNASLKAEEIYSQYCQQYAmTEV 221
Cdd:PRK11303 135 QRLQNDGLPIIALDRA-LDREHFTSVVSDDQDDAEMLAESLLKFPAESILLLGALPELSVSFEREQGFRQALKDDP-REV 212
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 222 VYKVEEHLGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVT 281
Cdd:PRK11303 213 HYLYANSFEREAGAQLFEKWLETHPMPDALFTTSYTLLQGVLDVLLERPGELPSDLAIAT 272
PBP1_LacI-like cd06290
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
125-339 1.04e-14

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


Pssm-ID: 380513 [Multi-domain]  Cd Length: 267  Bit Score: 73.03  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 125 NVDGVILLEpCLNDPIVKKLLQYKIPLVCIGTPGQDNKeVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGqskRNASLK 204
Cdd:cd06290   55 KVDGIIVVG-GFGDEELLKLLAEGIPVVLVDRELEGLN-LPVVNVDNEQGGYNATNHLIDLGHRRIVHISG---PEDHPD 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 205 AEEIYSQYCQqyAMTEVVYKVEEHL------GEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMK 278
Cdd:cd06290  130 AQERYAGYRR--ALEDAGLEVDPRLivegdfTEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAGIRVPDDVS 207
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 491069032 279 VV-------TRYngiraltSNPPLTAVDLHLDDVAKIAIDLLITQLNEDIETGSLRVMPApEIIKRTS 339
Cdd:cd06290  208 VIgfddlpfSKY-------TTPPLTTVRQPLYEMGKTAAEILLELIEGKGRPPRRIILPT-ELVIRES 267
PBP1_sucrose_transcription_regulator cd06288
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ...
69-339 7.77e-14

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: 70.65  E-value: 7.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  69 TIALIS----TIPSAIS--GGASKlgfmmevanvaaiYALEHDlYILLVpfIDHNNFDGNL---------MNVDGVILLE 133
Cdd:cd06288    1 TIGLITddiaTTPFAGDiiRGAQD-------------AAEEHG-YLLLL--ANTGGDPELEaeairellsRRVDGIIYAS 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 134 P---CLNDPIVKkllqYKIPLVCIGTPGQDNKeVPYV---DLQSEQTAIkllEHLVEEGAHQIALITGQSKRNASLKAEE 207
Cdd:cd06288   65 MhhrEVTLPPEL----TDIPLVLLNCFDDDPS-LPSVvpdDEQGGYLAT---RHLIEAGHRRIAFIGGPEDSLATRLRLA 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 208 IYSQycqqyAMTEVVYKVEEHLGEMG------GKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVt 281
Cdd:cd06288  137 GYRA-----ALAEAGIPYDPSLVVHGdwgresGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGLRVPEDLSVV- 210
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491069032 282 rynG------IRALTsnPPLTAVDLHLDDVAKIAIDLLITQLNEDIETGSLRVMPAPeIIKRTS 339
Cdd:cd06288  211 ---GfdnqelAAYLR--PPLTTVALPYYEMGRRAAELLLDGIEGEPPEPGVIRVPCP-LIERES 268
PBP1_LacI-like cd06299
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ...
126-339 2.60e-13

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: 69.23  E-value: 2.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 126 VDGVILLEPCLNDPIVKKLLQYKIPLVCIGTPGQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNASLKA 205
Cdd:cd06299   56 VDGIIAVPTGENSEGLQALIAQGLPVVFVDREVEGLGGVPVVTSDNRPGAREAVEYLVSLGHRRIGYISGPLSTSTGRER 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 206 EEIYSQycqqyAMTEVVYKVEEHLGEMG------GKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKV 279
Cdd:cd06299  136 LAAFRA-----ALTAAGIPIDEELVAFGdfrqdsGAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRIGDDVSL 210
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 280 VTRYNGIRALTSNPPLTAVDLHLDDVAKIAIDLLITQLNEDIETGSLRVmpAPEIIKRTS 339
Cdd:cd06299  211 ISFDDVPWFELLSPPLTVIAQPVERIGRRAVELLLALIENGGRATSIRV--PTELIPRES 268
PRK10339 PRK10339
DNA-binding transcriptional repressor EbgR; Provisional
11-314 2.68e-13

DNA-binding transcriptional repressor EbgR; Provisional


Pssm-ID: 182389 [Multi-domain]  Cd Length: 327  Bit Score: 69.79  E-value: 2.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  11 TISDVALAAQVSRTTVSHALNGKG--EVNPDTRKKIQEIAEQLGYRPNRFAKALRSGGTKT--IALISTIPSAisggask 86
Cdd:PRK10339   3 TLKDIAIEAGVSLATVSRVLNDDPtlNVKEETKHRILEIAEKLEYKTSSARKLQTGAVNQHhiLAIYSYQQEL------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  87 lgfmmEVAN---VAAIYALE---HDLYILLVPFIDHNnFDGNLMNVDGVILLEPclNDPIVKKLLQYKIPLVCIGTPGQD 160
Cdd:PRK10339  76 -----EINDpyyLAIRHGIEtqcEKLGIELTNCYEHS-GLPDIKNVTGILIVGK--PTPALRAAASALTDNICFIDFHEP 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 161 NKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNASLKAEEIYSQYCQqyaMTEVVYKVEEHLGEMGGKSA--I 238
Cdd:PRK10339 148 GSGYDAVDIDLARISKEIIDFYINQGVNRIGFIGGEDEPGKADIREVAFAEYGR---LKQVVREEDIWRGGFSSSSGyeL 224
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491069032 239 AEIM---KQYPKtdAILVMIDTFATGVMQYLTEKGISVPKQMKVVTRYNGIRALTSNPPLTAVDLHLDDVAKIAIDLLI 314
Cdd:PRK10339 225 AKQMlarEDYPK--ALFVASDSIAIGVLRAIHERGLNIPQDISLISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNLLY 301
PBP1_LacI-like cd06273
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
126-339 4.07e-13

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


Pssm-ID: 380497 [Multi-domain]  Cd Length: 268  Bit Score: 68.30  E-value: 4.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 126 VDGVILLEPClNDPIVKKLL-QYKIPLVCIGTPGQDNKeVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRN---- 200
Cdd:cd06273   56 VDGLILVGSD-HDPELFELLeQRQVPYVLTWSYDEDSP-HPSIGFDNRAAAARAAQHLLDLGHRRIAVISGPTAGNdrar 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 201 --------------ASLKAEEIYsqycqqyamtEVVYKVEEhlgemgGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYL 266
Cdd:cd06273  134 arlagirdalaergLELPEERVV----------EAPYSIEE------GREALRRLLARPPRPTAIICGNDVLALGALAEC 197
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491069032 267 TEKGISVPKQMKvVTRYNGIR-ALTSNPPLTAVDLHLDDVAKIAIDLLITQLNEDIETGSLRVmpAPEIIKRTS 339
Cdd:cd06273  198 RRLGISVPEDLS-ITGFDDLElAAHLSPPLTTVRVPAREIGELAARYLLALLEGGPPPKSVEL--ETELIVRES 268
LacI pfam00356
Bacterial regulatory proteins, lacI family;
11-56 5.04e-13

Bacterial regulatory proteins, lacI family;


Pssm-ID: 306791 [Multi-domain]  Cd Length: 46  Bit Score: 62.65  E-value: 5.04e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 491069032   11 TISDVALAAQVSRTTVSHALNGKGEVNPDTRKKIQEIAEQLGYRPN 56
Cdd:pfam00356   1 TIKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
PBP1_hexuronate_repressor-like cd06272
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ...
124-337 5.87e-13

ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and close homologs, all members of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon from Bacillus species and its close homologs from other bacteria, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380496 [Multi-domain]  Cd Length: 266  Bit Score: 68.17  E-value: 5.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 124 MNVDGVILLEPCLNDPIVKKLLQYKIPLVCIGTPGqdnKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALI-TGQSKRNAS 202
Cdd:cd06272   55 NRFDGVIVFGISDSDIEYLNKNKPKIPIVLYNRES---PKYSTVNVDNEKAGRLAVLLLIQKGHKSIAYIgNPNSNRNQT 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 203 LKAEEiYSQYCQQ--YAMTEVVYKVEEhLGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVV 280
Cdd:cd06272  132 LRGKG-FIETCEKhgIHLSDSIIDSRG-LSIEGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGISIPEDISIV 209
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491069032 281 TRYNGIRALTSNPPLTAVDLHLDDVAKIAIDLLItQLNEDIETGSLRVMPAPEIIKR 337
Cdd:cd06272  210 SYDNIPQEARSDPPLTVVGVPIEKIAEESLRLIL-KLIEGRENEIQQLILYPELIFR 265
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
125-337 2.61e-12

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


Pssm-ID: 380503 [Multi-domain]  Cd Length: 266  Bit Score: 66.13  E-value: 2.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 125 NVDGVILLEPCLNDPIVKKLLQYKIPLVCIGTpGQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGqsKRNASLK 204
Cdd:cd06280   55 QVDGIILAPSAGPSRELKRLLKHGIPIVLIDR-EVEGLELDLVAGDNREGAYKAVKHLIELGHRRIGLITG--PLEISTT 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 205 AEEI--YSQYCQQYAMTEVVYKVEE-HLGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVT 281
Cdd:cd06280  132 RERLagYREALAEAGIPVDESLIFEgDSTIEGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEIPQDISVVG 211
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 491069032 282 RYNGIRALTSNPPLTAVDLHLDDVAKIAIDLLITQLNEDIETGSLRVMPaPEIIKR 337
Cdd:cd06280  212 FDDSDWFEIVDPPLTVVAQPAYEIGRIAAQLLLERIEGQGEEPRRIVLP-TELIIR 266
PRK10401 PRK10401
HTH-type transcriptional regulator GalS;
10-312 7.47e-12

HTH-type transcriptional regulator GalS;


Pssm-ID: 236681 [Multi-domain]  Cd Length: 346  Bit Score: 65.57  E-value: 7.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  10 ITISDVALAAQVSRTTVSHALNGKGEVNPDTRKKIQEIAEQLGYRPNRFAKALRSGGTKTIALIstipsaisggasklgf 89
Cdd:PRK10401   2 ITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVV---------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  90 MMEVAN------VAAI--YALEHDLYILLVPFIDHNNFDGNLMNV------DGVILLEPCLNDPIVKKLLQYKIPLVCIG 155
Cdd:PRK10401  66 VMDVSDaffgalVKAVdlVAQQHQKYVLIGNSYHEAEKERHAIEVlirqrcNALIVHSKALSDDELAQFMDQIPGMVLIN 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 156 --TPGQDNKEVPYVDLQSEQTAIKLlehLVEEGAHQIALITGQSKRNASLKAEEIYSQYCQQYAMTEVVYKVEEHLGEM- 232
Cdd:PRK10401 146 rvVPGYAHRCVCLDNVSGARMATRM---LLNNGHQRIGYLSSSHGIEDDAMRRAGWMSALKEQGIIPPESWIGTGTPDMq 222
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 233 GGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVV-------TRYngiraltSNPPLTAVDLHLDDV 305
Cdd:PRK10401 223 GGEAAMVELLGRNLQLTAVFAYNDNMAAGALTALKDNGIAIPLHLSIIgfddipiARY-------TDPQLTTVRYPIASM 295

                 ....*..
gi 491069032 306 AKIAIDL 312
Cdd:PRK10401 296 AKLATEL 302
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
124-339 1.95e-11

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


Pssm-ID: 380516 [Multi-domain]  Cd Length: 270  Bit Score: 63.44  E-value: 1.95e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 124 MNVDGVILLEPCLNDPIVKKLLQYKIPLVCIGTPGQDnKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSK----- 198
Cdd:cd06293   54 QRVRGLIVTPSDDDLSHLARLRARGTAVVLLDRPAPG-PAGCSVSVDDVQGGALAVDHLLELGHRRIAFVSGPLRtrqva 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 199 -RNASLKAeeiysqycqqyAMTEVVYKVEEHLGE--------MGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEK 269
Cdd:cd06293  133 eRLAGARA-----------AVAEAGLDPDEVVRElsapdanaELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRA 201
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491069032 270 GISVPKQMKVVTrYNGIR-ALTSNPPLTAVDLHLDDVAKIAIDLLItqlnEDIETGSL---RVMPAPEIIKRTS 339
Cdd:cd06293  202 GLRVPDDVSVVG-YDDLPfAAAANPPLTTVRQPSYELGRAAADLLL----DEIEGPGHpheHVVFQPELVVRSS 270
PBP1_LacI-like cd06281
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
126-339 5.14e-11

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


Pssm-ID: 380504 [Multi-domain]  Cd Length: 270  Bit Score: 62.26  E-value: 5.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 126 VDGVILLEPCLNDPIVKKLL-QYKIPLVCIgtpgqdNKEVPyVDLQSEQT-----AIKLLEHLVEEGAHQIALITGQSKR 199
Cdd:cd06281   56 VDGLILTPGDEDDPELAAALaRLDIPVVLI------DRDLP-GDIDSVLVdhrsgVRQATEYLLSLGHRRIALLTGGPDI 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 200 NASLKAEEIYSQycqqyAMTEVVYKVEEHLGEMG------GKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISV 273
Cdd:cd06281  129 RPGRERIAGFKA-----AFAAAGLPPDPDLVRLGsfsadsGFREAMALLRQPRPPTAIIALGTQLLAGVLRAVRAAGLRI 203
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491069032 274 PKQMKVVTRYNGIRALTSNPPLTAVDLHLDDVAKIAIDLLITQLNEDIETGSLRVMPAPEIIKRTS 339
Cdd:cd06281  204 PGDLSVVSIGDSDLAELHDPPITAIRWDLDAVGRAAAELLLDRIEGPPAGPPRRIVVPTELILRDS 269
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
69-339 5.73e-11

ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators; Ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a member of the LacI-GalR family of bacterial transcription regulators. The ligand-binding domain of AraR is structurally homologous to the periplasmic sugar-binding domain of ABC-type transporters and both domains contain the type 1 periplasmic binding protein-like fold. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the type 1 periplasmic binding proteins. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380483 [Multi-domain]  Cd Length: 274  Bit Score: 62.19  E-value: 5.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  69 TIALIST-----I-PSAISGGASKL---GFMMEVANVAAIYALEhdlYILLVPFIDHNnfdgnlmnVDGVILlEPC---- 135
Cdd:cd01541    1 TIGVITTyiddyIfPSIIQGIESVLsenGYSLLLALTNNDVEKE---REILESLLDQN--------VDGLII-EPTksal 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 136 --LNDPIVKKLLQYKIPLVCIGT--PGQDnkeVPYVDLQSEQTAIKLLEHLVEEGAHQIALI------TGQSKRNASLKA 205
Cdd:cd01541   69 pnPNLDLYEELQKKGIPVVFINSyyPELD---APSVSLDDEKGGYLATKHLIDLGHRRIAGIfksddlQGVERYQGFIKA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 206 eeiYSQYCQQYAMTEVV-YKVEEhLGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTRYN 284
Cdd:cd01541  146 ---LREAGLPIDDDRILwYSTED-LEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALREAGLRVPEDLSVVGFDD 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 491069032 285 GIRALTSNPPLTAVDLHLDDVAKIAIDLLITQLNEDiETGSLRVMPaPEIIKRTS 339
Cdd:cd01541  222 SYLASLSEPPLTSVVHPKEELGRKAAELLLRMIEEG-RKPESVIFP-PELIERES 274
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
126-330 6.60e-11

Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems; Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems, all of which contain the type 1 periplasmic binding protein-like fold. Their specific ligands include lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor; in general the sugar binding domain in this family binds a sugar, which in turn changes the DNA binding activity of the repressor domain. The core structure of the periplasmic binding proteins is classified into two types and they differ in number and order of beta strands in each domain: type 1, which has six beta strands, and type 2, which has five beta strands. These two distinct structural arrangements may have originated from a common ancestor.


Pssm-ID: 380479 [Multi-domain]  Cd Length: 265  Bit Score: 61.88  E-value: 6.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 126 VDGVILLEPCLNDPIVKKLLQYK-IPLVCIGTPGQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRN-ASL 203
Cdd:cd01537   56 VKGLAINLVDPAAAGVAEKARGQnVPVVFFDKEPSRYDKAYYVITDSKEGGIIQGDLLAKHGHIQIVLLKGPLGHPdAEA 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 204 KAEEIYSQYCQQYAMTEVVYKVEEHLGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTRY 283
Cdd:cd01537  136 RLAGVIKELNDKGIKTEQLQLDTGDWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMGAVEALKEHGLRVPSDISVFGYD 215
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 491069032 284 NGIRALTSNPPLTAVDLHLDDVAKIAIDLLITQL-NEDIETGSLRVMP 330
Cdd:cd01537  216 ALPEALKSGPLLTTILQDANNLGKTTFDLLLNLAdNWKIDNKVVRVPY 263
PBP1_LacI-like cd06277
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
73-339 5.42e-09

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


Pssm-ID: 380500 [Multi-domain]  Cd Length: 275  Bit Score: 56.48  E-value: 5.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  73 ISTIPSAISGGASKLGFMMEVANVAAIYALEHDLYILlvpfidhnnfdgNLMNVDGVILLEPCLNDPIVKKLLQYKIPLV 152
Cdd:cd06277   21 FSELIDGIEREARKYGYNLLISSVDIGDDFDEILKEL------------TDDQSSGIILLGTELEEKQIKLFQDVSIPVV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 153 CIGTPGQDNKeVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNASLKAEEIYSQycqqyAMTE---VVYKVEEHL 229
Cdd:cd06277   89 VVDNYFEDLN-FDCVVIDNEDGAYEAVKYLVELGHTRIGYLASSYRIKNFEERRRGFRK-----AMRElglSEDPEPEFV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 230 GEMGGKSAIAEIMKQYPKTD----AILVMIDTFATGVMQYLTEKGISVPKQMKVVTRYNGIRALTSNPPLTAVDLHLDDV 305
Cdd:cd06277  163 VSVGPEGAYKDMKALLDTGPklptAFFAENDIIALGCIKALQEAGIRVPEDVSVIGFDDIPVSAMVDPPLTTIHVPKEQM 242
                        250       260       270
                 ....*....|....*....|....*....|....
gi 491069032 306 AKIAIDLLITQLNEDiETGSLRVMPAPEIIKRTS 339
Cdd:cd06277  243 GKLAVRRLIEKIKDP-DGGTLKILVSTKLVERGS 275
PRK11041 PRK11041
DNA-binding transcriptional regulator CytR; Provisional
36-340 1.64e-08

DNA-binding transcriptional regulator CytR; Provisional


Pssm-ID: 182923 [Multi-domain]  Cd Length: 309  Bit Score: 55.00  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  36 VNPDTRKKIQEIAEQLGYRPNRFAKALRSGGTKTIALI---------STIPSAISGGASKLGFMMEVANVAAIYALEHDl 106
Cdd:PRK11041   4 VSQATRQRVEQAVLEVGYSPQSLGRNLKRNESRTILVIvpdicdpffSEIIRGIEVTAAEHGYLVLIGDCAHQNQQEKT- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 107 yillvpFIdhnnfdgNLM---NVDGVILLEPCLndPI-VKKLLQYKIPLVCIGTPGQDNKEVPYVDLQSEQTAIKLLEHL 182
Cdd:PRK11041  83 ------FV-------NLIitkQIDGMLLLGSRL--PFdASKEEQRNLPPMVMANEFAPELELPTVHIDNLTAAFEAVNYL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 183 VEEGAHQIALITGqskrnaslkAEEI-YSQYCQQ-Y--AMTEVVYKVEEHL---GEM---GGKSAIAEIMKQYPKTDAIL 252
Cdd:PRK11041 148 HELGHKRIACIAG---------PEEMpLCHYRLQgYvqALRRCGITVDPQYiarGDFtfeAGAKALKQLLDLPQPPTAVF 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 253 VMIDTFATGVMQYLTEKGISVPKQMKVVTRYNGIRALTSNPPLTAVDLHLDDVAKIAIDLLITQLN-EDIETGSlRVMPA 331
Cdd:PRK11041 219 CHSDVMALGALSQAKRMGLRVPQDLSIIGFDDIDLAQYCDPPLTTVAQPRYEIGREAMLLLLEQLQgHHVSSGS-RLLDC 297

                 ....*....
gi 491069032 332 pEIIKRTSS 340
Cdd:PRK11041 298 -ELIIRGST 305
PBP1_LacI-like cd06282
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
126-340 2.49e-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: 380505 [Multi-domain]  Cd Length: 267  Bit Score: 54.21  E-value: 2.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 126 VDGVIL-LEPCLNDPIVKKLLQYKIPLVCIGTPgQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQskRNASLK 204
Cdd:cd06282   56 VDGLILtVGDAQGSEALELLEEEGVPYVLLFNQ-TENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAGD--FSASDR 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 205 AEEIYSQYCQqyAMTEVVYK----VEEHLGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVV 280
Cdd:cd06282  133 ARLRYQGYRD--ALKEAGLKpipiVEVDFPTNGLEEALTSLLSGPNPPTALFCSNDLLALSVISALRRLGIRVPDDVSVI 210
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491069032 281 TrYNGIR-ALTSNPPLTAVDLHLDDVAKIAIDLLITQLNEDIETGSLRVmpaPEIIKRTSS 340
Cdd:cd06282  211 G-FDGIAiGELLTPTLATVVQPSRDMGRAAADLLLAEIEGESPPTSIRL---PHHLREGGS 267
PBP1_RafR-like cd20009
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ...
127-335 4.65e-08

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


Pssm-ID: 380664 [Multi-domain]  Cd Length: 266  Bit Score: 53.31  E-value: 4.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 127 DGVIL--LEPclNDPIVKKLLQYKIPLVCIG-TpgQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNASL 203
Cdd:cd20009   59 DGIIIshTEP--QDPRVRYLLERGFPFVTHGrT--ELSTPHAYFDFDNEAFAYEAVRRLAARGRRRIALVAPPRELTYAQ 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 204 KAEEIYSQYCQQYAMTEVVykVEEHLGEMG---GKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVV 280
Cdd:cd20009  135 HRLRGFRRALAEAGLEVEP--LLIVTLDSSaeaIRAAARRLLRQPPRPDGIICASEIAALGALAGLEDAGLVVGRDVDVV 212
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 491069032 281 TRYN-GIRALTsNPPLTAVDLHLDDVAKIAIDLLITQL-NEDIETgsLRVMPAPEII 335
Cdd:cd20009  213 AKETsPILDYF-RPPIDTLYEDIEEAGRFLAEALLRRIeGEPAEP--LQTLERPELI 266
PRK14987 PRK14987
HTH-type transcriptional regulator GntR;
5-317 4.78e-08

HTH-type transcriptional regulator GntR;


Pssm-ID: 184949 [Multi-domain]  Cd Length: 331  Bit Score: 53.88  E-value: 4.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032   5 VNKKTITISDVALAAQVSRTTVSHALNGKGEVNPDTRKKIQEIAEQLGYRPNRFAKALRSGGTKTIALIstIPSAISGGA 84
Cdd:PRK14987   1 MKKKRPVLQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVL--LPSLTNQVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  85 SKLGFMMEVANVAAIYA--LEHDLYillVPFIDHNNFDGNL-MNVDGVILLEPCLNDPIVKKLLQYKIPLVCIgtpgQDN 161
Cdd:PRK14987  79 AEVLRGIESVTDAHGYQtmLAHYGY---KPEMEQERLESMLsWNIDGLILTERTHTPRTLKMIEVAGIPVVEL----MDS 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 162 KEvPYVDL----QSEQTAIKLLEHLVEEGAHQIALITGQSKRNASLKaEEIYSQYCQQYAMTEVVYKVEEHLGEMGGKSA 237
Cdd:PRK14987 152 QS-PCLDIavgfDNFEAARQMTTAIIARGHRHIAYLGARLDERTIIK-QKGYEQAMLDAGLVPYSVMVEQSSSYSSGIEL 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 238 IAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKVVTRYNGIRALTSNPPLTAVDLHLDDVAKIAIDLLITQL 317
Cdd:PRK14987 230 IRQARREYPQLDGVFCTNDDLAVGAAFECQRLGLKVPDDMAIAGFHGHDIGQVMEPRLASVLTPRERMGSIGAERLLARI 309
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
126-336 1.04e-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: 52.51  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  126 VDGVILLEPCLNDP-IVKKLLQYKIPLVCIGTPGQDNKEVPYVDLQSEQTAIKLLEHLVEEGaHQ--IALITGQSKRNAS 202
Cdd:pfam00532  58 ADGIIITTPAPSGDdITAKAEGYGIPVIAADDAFDNPDGVPCVMPDDTQAGYESTQYLIAEG-HKrpIAVMAGPASALTA 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  203 LKAEEIYSQYCQQYAMTEVVYKVEEHLGEM-GGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKG-ISVPKQmkVV 280
Cdd:pfam00532 137 RERVQGFMAALAAAGREVKIYHVATGDNDIpDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGrVKIPDI--VG 214
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491069032  281 TRYN---GIRALTS-------NPPLTAVDLHLDDVAKIAIDLLITQLNEDIETGSLRVMPAPEIIK 336
Cdd:pfam00532 215 IGINsvvGFDGLSKaqdtglyLSPLTVIQLPRQLLGIKASDMVYQWIPKFREHPRVLLIPRDFFKE 280
PRK10727 PRK10727
HTH-type transcriptional regulator GalR;
11-297 1.66e-07

HTH-type transcriptional regulator GalR;


Pssm-ID: 182681 [Multi-domain]  Cd Length: 343  Bit Score: 52.45  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  11 TISDVALAAQVSRTTVSHALNGKGEVNPDTRKKIQEIAEQLGYRPNRFAKALRSGGTKTIALI---------STIPSAIS 81
Cdd:PRK10727   3 TIKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVvgdvsdpffGAMVKAVE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  82 GGASKLGFMMEVANVaaiYALEHDLYILLVPFIDHnnfdgnlmNVDGVILLEPCLNDPIVKKLLQYKIPLVCIG--TPGQ 159
Cdd:PRK10727  83 QVAYHTGNFLLIGNG---YHNEQKERQAIEQLIRH--------RCAALVVHAKMIPDAELASLMKQIPGMVLINriLPGF 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 160 DNKEVPYVDLQSEQTAIKlleHLVEEGAHQIALITgqSKRNASlKAEEIYSQYCQqyAMTEVVYKVEEHL------GEMG 233
Cdd:PRK10727 152 ENRCIALDDRYGAWLATR---HLIQQGHTRIGYLC--SNHSIS-DAEDRLQGYYD--ALAESGIPANDRLvtfgepDESG 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 491069032 234 GKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISVPKQMKV-------VTRYNGIRALTSNPPLTA 297
Cdd:PRK10727 224 GEQAMTELLGRGRNFTAVACYNDSMAAGAMGVLNDNGIDVPGEISLigfddvlVSRYVRPRLTTVRYPIVT 294
PBP1_RegR_EndR_KdgR-like cd06283
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ...
74-335 2.90e-07

ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR; Ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR, all of which are members of the LacI-GalR family of bacterial transcription regulators. RegR regulates bacterial competence and the expression of virulence factors, including hyaluronidase. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380506 [Multi-domain]  Cd Length: 266  Bit Score: 51.01  E-value: 2.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  74 STIPSAISGGASKLGFMMEVANVAAIYALEHDlYILLvpFIDhnnfdgnlMNVDGVILlEPC-LNDPIVKKLLQYKIPLV 152
Cdd:cd06283   15 SLLLKGIEDVCREAGYQLLICNSNNDPEKERD-YIES--LLS--------QRVDGLIL-QPTgNNNDAYLELAQKGLPVV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 153 CIGTPgQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQ----SKRNASLKAeeiYSQYCQQYAMTEVVYKVEEH 228
Cdd:cd06283   83 LVDRQ-IEPLNWDTVVTDNYDATYEATEHLKEQGYERIVFVTEPikgiSTRRERLQG---FLDALARYNIEGDVYVIEIE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 229 LGEMgGKSAIAEIMKQYPK-TDAILVMIDTFATGVMQYLTEKGISVPKQMKVV-------TRYNGiraltsnPPLTAVDL 300
Cdd:cd06283  159 DTED-LQQALAAFLSQHDGgKTAIFAANGVVLLRVLRALKALGIRIPDDVGLCgfddwdwADLIG-------PGITTIRQ 230
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 491069032 301 HLDDVAKIAIDLLITQLNEDIETGSLRVMPAPEII 335
Cdd:cd06283  231 PTYEIGKAAAEILLERIEGDSGEPKEIELPSELII 265
PBP1_CcpA_TTHA0807 cd06297
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ...
122-339 8.05e-07

ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its close homologs; Ligand-binding domain of the uncharacterized transcription regulator TTHA0807 from the extremely thermophilic organism Thermus thermophilus HB8 and close homologs from other bacteria. Although its exact biological function is not known, the TTHA0807 belongs to the catabolite control protein A (CcpA)family of regulatory proteins. The CcpA functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.


Pssm-ID: 380520 [Multi-domain]  Cd Length: 268  Bit Score: 49.77  E-value: 8.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 122 NLMNVDGVILLEPCLNDPIVKKLLQYKIPLVCIGtpgQDNKEVPYVDLQSEQTAIKLLEHLVEEGAHQIALITGQSKRNA 201
Cdd:cd06297   52 LAYQCDGLVMASLDLTELFEEVIVPTEKPVVLID---ANSMGYDCVYVDNVKGGFMATEYLAGLGEREYVFFGIEEDTVF 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 202 SlkaEEIYSQYCQQY--AMTEVVYKVEE------HLGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGISV 273
Cdd:cd06297  129 T---ETVFREREQGFleALNKAGRPISSsrmfriDNSSKKAECLARELLKKADNPAAFFAAADLVALGLIRAAQSLGLRV 205
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491069032 274 PKQMKVVTryNGIRALTSNPPLTAVDLHLDDVAKIAIDLLITQLNEDIET-GSLRVMpaPEIIKRTS 339
Cdd:cd06297  206 GEDVAVIG--FDGQPWAASPGLTTVRQPVEEMGEAAAKLLLKRLNEYGGPpRSLKFE--PELIVRES 268
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
125-318 6.38e-06

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: 47.23  E-value: 6.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 125 NVDGVILlepCLND-----PIVKKLLQYKIPLVCIGTPGQDNKEVPYVDLQSEQTAIKLLEHLVEE--GAHQIALITGQS 197
Cdd:COG1879   89 GVDAIIV---SPVDpdalaPALKKAKAAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKAlgGKGKVAILTGSP 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 198 KRNASLKAEEIYSQYCQQYAMTEVVYKVEEHLGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTEKGIsvPKQM 277
Cdd:COG1879  166 GAPAANERTDGFKEALKEYPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGR--KGDV 243
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 491069032 278 KVVTRY--NGIRALTSNPPLTA-VDLHLDDVAKIAIDLLITQLN 318
Cdd:COG1879  244 KVVGFDgsPEALQAIKDGTIDAtVAQDPYLQGYLAVDAALKLLK 287
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
125-281 5.20e-04

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: 41.01  E-value: 5.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 125 NVDGVILlepCLND-----PIVKKLLQYKIPLVCIGTP-----------GQDNKEVpyvdlqSEQTAIKLLEHLVEEGah 188
Cdd:cd01536   55 GVDAIII---APVDsealvPAVKKANAAGIPVVAVDTDidgggdvvafvGTDNYEA------GKLAGEYLAEALGGKG-- 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 189 QIALITGQSKRNASLKAEEIYSQYCQQYAMTEVVYKVEEHLGEMGGKSAIAEIMKQYPKTDAILVMIDTFATGVMQYLTE 268
Cdd:cd01536  124 KVAILEGPPGSSTAIDRTKGFKEALKKYPDIEIVAEQPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKA 203
                        170
                 ....*....|...
gi 491069032 269 KGISvpKQMKVVT 281
Cdd:cd01536  204 AGRT--GDIKIVG 214
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
124-270 6.59e-04

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: 40.74  E-value: 6.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 124 MNVDGVIL---LEPCLNDPIvKKLLQYKIPLVCIGTPGQDNkEVPYVDLQSEQTAIKLLEHLVEE--GAHQIALITGQS- 197
Cdd:cd06305   54 QKVDAIIIshgDADALDPKL-KKALDAGIPVVTFDTDSQVP-GVNNITQDDYALGTLSLGQLVKDlnGEGNIAVFNVFGv 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032 198 ----KRNASLKAEEiysqycqqyAMTEVVYKVEEHLGEMGGKSA------IAEIMKQYPKT--DAILVMIDTFATGVMQY 265
Cdd:cd06305  132 ppldKRYDIYKAVL---------KANPGIKKIVAELGDVTPNTAadaqtqVEALLKKYPEGgiDAIWAAWDEPAKGAVQA 202

                 ....*
gi 491069032 266 LTEKG 270
Cdd:cd06305  203 LEEAG 207
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
125-281 1.10e-03

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: 39.99  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  125 NVDGVILlepCLND-----PIVKKLLQYKIPLVCIGTPGQDNKEVPYVDLQSEQTAIKLLEHLVE--EGAHQIALITG-Q 196
Cdd:pfam13407  55 GVDAIIV---APVDptalaPVLKKAKDAGIPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEalGGKGKVAILSGsP 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491069032  197 SKRNASLKAEEIYSQYCQQYAMTEVVYKVEEHLGEMG-GKSAIAEIMKQYP-KTDAILVMIDTFATGVMQYLTEKGISvp 274
Cdd:pfam13407 132 GDPNANERIDGFKKVLKEKYPGIKVVAEVEGTNWDPEkAQQQMEALLTAYPnPLDGIISPNDGMAGGAAQALEAAGLA-- 209

                  ....*..
gi 491069032  275 KQMKVVT 281
Cdd:pfam13407 210 GKVVVTG 216
HTH_3 pfam01381
Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and ...
6-58 1.46e-03

Helix-turn-helix; This large family of DNA binding helix-turn helix proteins includes Cro and CI. Within the protein Swiss:Q5F9C2, the full protein fold incorporates a helix-turn-helix motif, but the function of this member is unlikely to be that of a DNA-binding regulator, the function of most other members, so is not necessarily characteriztic of the whole family.


Pssm-ID: 460181 [Multi-domain]  Cd Length: 55  Bit Score: 36.36  E-value: 1.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 491069032    6 NKKTITISDVALAAQVSRTTVSHALNGKGEVNPDTrkkIQEIAEQLGYRPNRF 58
Cdd:pfam01381   6 EELGLSQEELAEKLGVSRSTISKIENGKREPSLET---LKKLAEALGVSLDEL 55
HTH_XRE smart00530
Helix-turn-helix XRE-family like proteins;
7-52 4.07e-03

Helix-turn-helix XRE-family like proteins;


Pssm-ID: 197775 [Multi-domain]  Cd Length: 56  Bit Score: 35.19  E-value: 4.07e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 491069032     7 KKTITISDVALAAQVSRTTVSHALNGKGEVNPDTrkkIQEIAEQLG 52
Cdd:smart00530   8 EKGLTQEELAEKLGVSRSTLSRIENGKRKPSLET---LKKLAKALG 50
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
6-58 5.17e-03

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


Pssm-ID: 238045 [Multi-domain]  Cd Length: 58  Bit Score: 34.84  E-value: 5.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 491069032   6 NKKTITISDVALAAQVSRTTVSHALNGKGEVNPDTrkkIQEIAEQLGYRPNRF 58
Cdd:cd00093    9 KEKGLTQEELAEKLGVSRSTISRIENGKRNPSLET---LEKLAKALGVSLDEL 58
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH