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Conserved domains on  [gi|488392037|ref|WP_002461422|]
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MULTISPECIES: LacI family DNA-binding transcriptional regulator [Staphylococcus]

Protein Classification

LacI family DNA-binding transcriptional regulator( domain architecture ID 11265674)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
 60-316 2.75e-84

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: 254.34  E-value: 2.75e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKINVP 139
Cdd:cd01542    1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEITDEHRKALKKLKIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 140 VILVGQEHSGVNSIIHDDYLAGSYVGRQIVEANYKQVYFFGVTEEDKAVGQQRKNGVLDILALNHID-VQVFKTSFQFME 218
Cdd:cd01542   81 VVVLGQEHEGFSCVYHDDYGAGKLLGEYLLKKGHKNIAYIGVDEEDIAVGVARKQGYLDALKEHGIDeVEIVETDFSMES 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 219 AKNDVKlHLQSVHTADAIIGATDTIALAIHSYCSQpHHKLIPHKIY--GFGGDPITQIVTPQINTVMYHYFKAGQQALSQ 296
Cdd:cd01542  161 GYEAAK-ELLKENKPDAIICATDNIALGAIKALRE-LGIKIPEDISvaGFGGYDLSEFVSPSLTTVKFDYEEAGEKAAEL 238

                        250       260
                 ....*....|....*....|
gi 488392037 297 LHRLINHHDAQLLTVIPVEL 316
Cdd:cd01542  239 LLDMIEGEKVPKKQKLPYEL 258
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
3-70 2.49e-27

helix_turn _helix lactose operon repressor;


:

Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 101.51  E-value: 2.49e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488392037     3 NIADIARLAGVSKSTVSRYLNN-GSVSTKTKEKLSKIIKEQDYQPNQFAQSLRARHTKMIGAIIPRMNS 70
Cdd:smart00354   2 TIKDVARLAGVSKATVSRVLNGkGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
 
Name Accession Description Interval E-value
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
 60-316 2.75e-84

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: 254.34  E-value: 2.75e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKINVP 139
Cdd:cd01542    1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEITDEHRKALKKLKIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 140 VILVGQEHSGVNSIIHDDYLAGSYVGRQIVEANYKQVYFFGVTEEDKAVGQQRKNGVLDILALNHID-VQVFKTSFQFME 218
Cdd:cd01542   81 VVVLGQEHEGFSCVYHDDYGAGKLLGEYLLKKGHKNIAYIGVDEEDIAVGVARKQGYLDALKEHGIDeVEIVETDFSMES 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 219 AKNDVKlHLQSVHTADAIIGATDTIALAIHSYCSQpHHKLIPHKIY--GFGGDPITQIVTPQINTVMYHYFKAGQQALSQ 296
Cdd:cd01542  161 GYEAAK-ELLKENKPDAIICATDNIALGAIKALRE-LGIKIPEDISvaGFGGYDLSEFVSPSLTTVKFDYEEAGEKAAEL 238

                        250       260
                 ....*....|....*....|
gi 488392037 297 LHRLINHHDAQLLTVIPVEL 316
Cdd:cd01542  239 LLDMIEGEKVPKKQKLPYEL 258
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
1-316 5.10e-70

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 220.46  E-value: 5.10e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037   1 MKNIADIARLAGVSKSTVSRYLNN-GSVSTKTKEKLSKIIKEQDYQPNQFAQSLRARHTKMIGAIIPRMNSHAVDETIKG 79
Cdd:COG1609    3 RVTIKDVARLAGVSVATVSRVLNGpPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLRG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  80 VAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKINVPVILVGQ--EHSGVNSIIHDD 157
Cdd:COG1609   83 IEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRplPDPGVPSVGVDN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 158 YLAGSYVGRQIVEANYKQVYFFGvTEEDKAVGQQRKNGVLDILALNHIDVQ---VFKTSFQFMEAKNDVKLHLQSVHTAD 234
Cdd:COG1609  163 RAGARLATEHLIELGHRRIAFIG-GPADSSSARERLAGYREALAEAGLPPDpelVVEGDFSAESGYEAARRLLARGPRPT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 235 AIIGATDTIALAIHSYCSQpHHKLIPH--KIYGFGGDPITQIVTPQINTVMYHYFKAGQQALSQLHRLINHHDAQLLTV- 311
Cdd:COG1609  242 AIFCANDLMALGALRALRE-AGLRVPEdvSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERVl 320


                 ....*
gi 488392037 312 IPVEL 316
Cdd:COG1609  321 LPPEL 325
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
3-70 2.49e-27

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 101.51  E-value: 2.49e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488392037     3 NIADIARLAGVSKSTVSRYLNN-GSVSTKTKEKLSKIIKEQDYQPNQFAQSLRARHTKMIGAIIPRMNS 70
Cdd:smart00354   2 TIKDVARLAGVSKATVSRVLNGkGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
PRK10703 PRK10703
HTH-type transcriptional repressor PurR;
1-311 8.69e-25

HTH-type transcriptional repressor PurR;


Pssm-ID: 236739 [Multi-domain]  Cd Length: 341  Bit Score: 102.11  E-value: 8.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037   1 MKNIADIARLAGVSKSTVSRYLNNGS-VSTKTKEKLSKIIKEQDYQPNQFAQSLRARHTKMIGAIIPRMNSHAVDETIKG 79
Cdd:PRK10703   1 MATIKDVAKRAGVSTTTVSHVINKTRfVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  80 VAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKI-NVPVILV--GQEHSGVNSIIHD 156
Cdd:PRK10703  81 VEKNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLLAMLEEYrHIPMVVMdwGEAKADFTDAIID 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 157 DYLAGSYV-GRQIVEANYKQVyffGVT--EEDKAVGQQRKNGVLDILALNHIDVQ---VFKTSFQ---FMEAKNDVklhL 227
Cdd:PRK10703 161 NAFEGGYLaGRYLIERGHRDI---GVIpgPLERNTGAGRLAGFMKAMEEANIKVPeewIVQGDFEpesGYEAMQQI---L 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 228 QSVHTADAIIGATDTIAL-AIhsyCSQPHHKL-IPHKIYGFGGDPI--TQIVTPQINTVmyHYFKA--GQQALSQLHRLI 301
Cdd:PRK10703 235 SQKHRPTAVFCGGDIMAMgAI---CAADEMGLrVPQDISVIGYDNVrnARYFTPALTTI--HQPKDrlGETAFNMLLDRI 309

                        330
                 ....*....|
gi 488392037 302 NHHDAQLLTV 311
Cdd:PRK10703 310 VNKREEPQTI 319
fruct_sucro_rep TIGR02417
D-fructose-responsive transcription factor; Members of this family belong the lacI ...
 4-201 4.54e-21

D-fructose-responsive transcription factor; Members of this family belong the lacI helix-turn-helix family (pfam00356) of DNA-binding transcriptional regulators. All members are from the proteobacteria. Characterized members act as positive and negative transcriptional regulators of fructose and sucrose transport and metabolism. Sucrose is a disaccharide composed of fructose and glucose; D-fructose-1-phosphate rather than an intact sucrose moiety has been shown to act as the inducer. [Regulatory functions, DNA interactions]


Pssm-ID: 131470 [Multi-domain]  Cd Length: 327  Bit Score: 91.74  E-value: 4.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037    4 IADIARLAGVSKSTVSRYLNNGS----VSTKTKEKLSKIIKEQDYQPNQFAQSLRARHTKMIGAIIPRMNSHAVDETIKG 79
Cdd:TIGR02417   2 LSDIAKLAGVSKTTASYVINGKAkeyrISQETVERVMAVVREQGYQPNIHAASLRAGRSRTIGLVIPDLENYSYARIAKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037   80 VAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILmATRITPQHLDV--INKINVPVILVGQ--EHSGVNSIIH 155
Cdd:TIGR02417  82 LEQQCREAGYQLLIACSDDNPDQEKVVIENLLARQVDALIV-ASCMPPEDAYYqkLQNEGLPVVALDRslDDEHFCSVIS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 488392037  156 DDYLAGSYVGRQIVEANYKQVYFFGvTEEDKAVGQQRKNGVLDILA 201
Cdd:TIGR02417 161 DDVDAAAELIERLLSQHADEFWYLG-AQPELSVSRDRLAGFRQALK 205
HTH_LacI cd01392
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ...
 5-55 3.55e-18

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: 76.68  E-value: 3.55e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488392037   5 ADIARLAGVSKSTVSRYLNN-GSVSTKTKEKLSKIIKEQDYQPNQFAQSLRA 55
Cdd:cd01392    1 KDIARAAGVSVATVSRVLNGkPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
LacI pfam00356
Bacterial regulatory proteins, lacI family;
3-47 4.90e-16

Bacterial regulatory proteins, lacI family;


Pssm-ID: 306791 [Multi-domain]  Cd Length: 46  Bit Score: 70.74  E-value: 4.90e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 488392037    3 NIADIARLAGVSKSTVSRYLNN-GSVSTKTKEKLSKIIKEQDYQPN 47
Cdd:pfam00356   1 TIKDVARLAGVSKSTVSRVLNNpGRVSEETRERVEAAMEELNYIPN 46
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 61-302 9.57e-09

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: 55.39  E-value: 9.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037   61 IGAIIPRMNSHAVDETIKGVAHVCKELEYQLLL-NYTGLDLSEEIIALETLSRSKVDGIILMA---TRITPqhldVINKI 136
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVvGPAEADAAEQVAQIEDAIAQGVDAIIVAPvdpTALAP----VLKKA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  137 ---NVPVILVGQEHSGVNSIIH---DDYLAGSYVGRQIVEA---NYKQVYFFGVteEDKAVGQQRKNGVLDILALNHIDV 207
Cdd:pfam13407  77 kdaGIPVVTFDSDAPSSPRLAYvgfDNEAAGEAAGELLAEAlggKGKVAILSGS--PGDPNANERIDGFKKVLKEKYPGI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  208 QVFKTSFQFMEAKNDVKLHLQSV-----HTADAIIGATDTIALAIHSYCSQPHHKLIPhKIYGFGGDP--ITQIVTPQIN 280
Cdd:pfam13407 155 KVVAEVEGTNWDPEKAQQQMEALltaypNPLDGIISPNDGMAGGAAQALEAAGLAGKV-VVTGFDATPeaLEAIKDGTID 233

                         250       260
                  ....*....|....*....|...
gi 488392037  281 -TVMYHYFKAGQQALSQLHRLIN 302
Cdd:pfam13407 234 aTVLQDPYGQGYAAVELAAALLK 256
 
Name Accession Description Interval E-value
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
 60-316 2.75e-84

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: 254.34  E-value: 2.75e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKINVP 139
Cdd:cd01542    1 LIGVIVPRLDSYSTSRVLEGIDEVLKENGYQPLIANTNLDEEREIEYLETLARQKVDGIILFATEITDEHRKALKKLKIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 140 VILVGQEHSGVNSIIHDDYLAGSYVGRQIVEANYKQVYFFGVTEEDKAVGQQRKNGVLDILALNHID-VQVFKTSFQFME 218
Cdd:cd01542   81 VVVLGQEHEGFSCVYHDDYGAGKLLGEYLLKKGHKNIAYIGVDEEDIAVGVARKQGYLDALKEHGIDeVEIVETDFSMES 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 219 AKNDVKlHLQSVHTADAIIGATDTIALAIHSYCSQpHHKLIPHKIY--GFGGDPITQIVTPQINTVMYHYFKAGQQALSQ 296
Cdd:cd01542  161 GYEAAK-ELLKENKPDAIICATDNIALGAIKALRE-LGIKIPEDISvaGFGGYDLSEFVSPSLTTVKFDYEEAGEKAAEL 238

                        250       260
                 ....*....|....*....|
gi 488392037 297 LHRLINHHDAQLLTVIPVEL 316
Cdd:cd01542  239 LLDMIEGEKVPKKQKLPYEL 258
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
1-316 5.10e-70

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 220.46  E-value: 5.10e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037   1 MKNIADIARLAGVSKSTVSRYLNN-GSVSTKTKEKLSKIIKEQDYQPNQFAQSLRARHTKMIGAIIPRMNSHAVDETIKG 79
Cdd:COG1609    3 RVTIKDVARLAGVSVATVSRVLNGpPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVPDLSNPFFAELLRG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  80 VAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKINVPVILVGQ--EHSGVNSIIHDD 157
Cdd:COG1609   83 IEEAARERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDDARLERLAEAGIPVVLIDRplPDPGVPSVGVDN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 158 YLAGSYVGRQIVEANYKQVYFFGvTEEDKAVGQQRKNGVLDILALNHIDVQ---VFKTSFQFMEAKNDVKLHLQSVHTAD 234
Cdd:COG1609  163 RAGARLATEHLIELGHRRIAFIG-GPADSSSARERLAGYREALAEAGLPPDpelVVEGDFSAESGYEAARRLLARGPRPT 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 235 AIIGATDTIALAIHSYCSQpHHKLIPH--KIYGFGGDPITQIVTPQINTVMYHYFKAGQQALSQLHRLINHHDAQLLTV- 311
Cdd:COG1609  242 AIFCANDLMALGALRALRE-AGLRVPEdvSVVGFDDIPLARYLTPPLTTVRQPIEEMGRRAAELLLDRIEGPDAPPERVl 320


                 ....*
gi 488392037 312 IPVEL 316
Cdd:COG1609  321 LPPEL 325
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
 60-316 1.98e-31

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: 118.39  E-value: 1.98e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKINVP 139
Cdd:cd06267    1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDDELLEELLAAGIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 140 VILVGQ--EHSGVNSIIHDDYLAGSYVGRQIVEANYKQVYFFGvTEEDKAVGQQRKNGVLDILALNHIDVQ---VFKTSF 214
Cdd:cd06267   81 VVLIDRrlDGLGVDSVVVDNYAGAYLATEHLIELGHRRIAFIG-GPLDLSTSRERLEGYRDALAEAGLPVDpelVVEGDF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 215 QFMEAKNDVKLHLQSVHTADAIIGATDTIALAIHSYCSQpHHKLIPHKIY--GFGGDPITQIVTPQINTVMYHYFKAGQQ 292
Cdd:cd06267  160 SEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRE-LGLRVPEDISvvGFDDIPLAALLTPPLTTVRQPAYEMGRA 238

                        250       260
                 ....*....|....*....|....*
gi 488392037 293 ALSQLHRLINHHDAQL-LTVIPVEL 316
Cdd:cd06267  239 AAELLLERIEGEEEPPrRIVLPTEL 263
PBP1_CcpA-like cd19975
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
 61-316 3.56e-31

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: 117.66  E-value: 3.56e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  61 IGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKINVPV 140
Cdd:cd19975    2 IGVIIPDISNSFFAEILKGIEDEARENGYSVILCNTGSDEEREKKYLQLLKEKRVDGIIFASGTLTEENKQLLKNMNIPV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 141 ILVGQEHSGVN--SIIHDDYLAGSYVGRQIVEANYKQVYFFGVTEEDKAVGQQRKNGVLDILALNHIDV---QVFKTSFQ 215
Cdd:cd19975   82 VLVSTESEDPDipSVKIDDYQAAYDATNYLIKKGHRKIAMISGPLDDPNAGYPRYEGYKKALKDAGLPIkenLIVEGDFS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 216 FMEAKNDVKLHLQSVHTADAIIGATDTIALAIHSYCSQphHKL-IPH--KIYGFGGDPITQIVTPQINTVMYHYFKAGQQ 292
Cdd:cd19975  162 FKSGYQAMKRLLKNKKLPTAVFAASDEMALGVISAAYD--HGIrVPEdiSVIGFDNTEIAEMSIPPLTTVSQPFYEMGKK 239

                        250       260
                 ....*....|....*....|....*
gi 488392037 293 ALSQLHRLINHHDAQLL-TVIPVEL 316
Cdd:cd19975  240 AVELLLDLIKNEKKEEKsIVLPHQI 264
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
3-70 2.49e-27

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 101.51  E-value: 2.49e-27
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488392037     3 NIADIARLAGVSKSTVSRYLNN-GSVSTKTKEKLSKIIKEQDYQPNQFAQSLRARHTKMIGAIIPRMNS 70
Cdd:smart00354   2 TIKDVARLAGVSKATVSRVLNGkGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVPDITN 70
PRK10703 PRK10703
HTH-type transcriptional repressor PurR;
1-311 8.69e-25

HTH-type transcriptional repressor PurR;


Pssm-ID: 236739 [Multi-domain]  Cd Length: 341  Bit Score: 102.11  E-value: 8.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037   1 MKNIADIARLAGVSKSTVSRYLNNGS-VSTKTKEKLSKIIKEQDYQPNQFAQSLRARHTKMIGAIIPRMNSHAVDETIKG 79
Cdd:PRK10703   1 MATIKDVAKRAGVSTTTVSHVINKTRfVAEETRNAVWAAIKELHYSPSAVARSLKVNHTKSIGLLATSSEAPYFAEIIEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  80 VAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKI-NVPVILV--GQEHSGVNSIIHD 156
Cdd:PRK10703  81 VEKNCYQKGYTLILCNAWNNLEKQRAYLSMLAQKRVDGLLVMCSEYPEPLLAMLEEYrHIPMVVMdwGEAKADFTDAIID 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 157 DYLAGSYV-GRQIVEANYKQVyffGVT--EEDKAVGQQRKNGVLDILALNHIDVQ---VFKTSFQ---FMEAKNDVklhL 227
Cdd:PRK10703 161 NAFEGGYLaGRYLIERGHRDI---GVIpgPLERNTGAGRLAGFMKAMEEANIKVPeewIVQGDFEpesGYEAMQQI---L 234

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 228 QSVHTADAIIGATDTIAL-AIhsyCSQPHHKL-IPHKIYGFGGDPI--TQIVTPQINTVmyHYFKA--GQQALSQLHRLI 301
Cdd:PRK10703 235 SQKHRPTAVFCGGDIMAMgAI---CAADEMGLrVPQDISVIGYDNVrnARYFTPALTTI--HQPKDrlGETAFNMLLDRI 309

                        330
                 ....*....|
gi 488392037 302 NHHDAQLLTV 311
Cdd:PRK10703 310 VNKREEPQTI 319
PRK10423 PRK10423
transcriptional repressor RbsR; Provisional
 1-314 3.54e-23

transcriptional repressor RbsR; Provisional


Pssm-ID: 182448 [Multi-domain]  Cd Length: 327  Bit Score: 97.46  E-value: 3.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037   1 MKniaDIARLAGVSKSTVSRYLNNGS-VSTKTKEKLSKIIKEQDYQPNQFAQSLRARHTKMIGAIIPRMNSHAVDETIKG 79
Cdd:PRK10423   1 MK---DVARLAGVSTSTVSHVINKDRfVSEAITAKVEAAIKELNYAPSALARSLKLNQTRTIGMLITASTNPFYSELVRG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  80 VAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRitpQHL---DVINKI-NVPVILVG-QEHSGVNSII 154
Cdd:PRK10423  78 VERSCFERGYSLVLCNTEGDEQRMNRNLETLMQKRVDGLLLLCTE---THQpsrEIMQRYpSVPTVMMDwAPFDGDSDLI 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 155 HDD-YLAGSYVGRQIVEANYKQVYFFgVTEEDKAVGQQRKNGVLDILALNHIDVQ---VFKTSFQFMEAKNDVKLHLQSV 230
Cdd:PRK10423 155 QDNsLLGGDLATQYLIDKGYTRIACI-TGPLDKTPARLRLEGYRAAMKRAGLNIPdgyEVTGDFEFNGGFDAMQQLLALP 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 231 HTADAIIGATDtiALAIHSYcsqphHKL------IPHKIYGFGGDPI--TQIVTPQINTVmyHYFK--AGQQALSQL-HR 299
Cdd:PRK10423 234 LRPQAVFTGND--AMAVGVY-----QALyqaglsVPQDIAVIGYDDIelARYMTPPLTTI--HQPKdeLGELAIDVLiHR 304

                        330
                 ....*....|....*.
gi 488392037 300 LIN-HHDAQLLTVIPV 314
Cdd:PRK10423 305 MAQpTLQQQRLQLTPE 320
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
 60-316 3.81e-22

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: 93.35  E-value: 3.81e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDvinKINVP 139
Cdd:cd06291    1 TIGLIVPDISNPFFAELAKYIEKELFKKGYKMILCNSNEDEEKEKEYLEMLKRNKVDGIILGSHSLDIEEYK---KLNIP 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 140 VILVGQEHS-GVNSIIHDDYLAGSYVGRQIVEANYKQVYFFGvTEEDKAVGQQRKNGVLDILALNHIDVQVFKTSFQFM- 217
Cdd:cd06291   78 IVSIDRYLSeGIPSVSSDNYQGGRLAAEHLIEKGCKKILHIG-GPSNNSPANERYRGFEDALKEAGIEYEIIEIDENDFs 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 218 --EAKNDVKLHLQSVHTADAIIGATDTIALAIHSYCSQpHHKLIPH--KIYGFGGDPITQIVTPQINTVMYHYFKAGQQA 293
Cdd:cd06291  157 eeDAYELAKELLEKYPDIDGIFASNDLLAIGVLKALQK-LGIRVPEdvQIIGFDGIEISELLYPELTTIRQPIEEMAKEA 235

                        250       260
                 ....*....|....*....|....
gi 488392037 294 LSQLHRLINHHDAQ-LLTVIPVEL 316
Cdd:cd06291  236 VELLLKLIEGEEIEeSRIVLPVEL 259
fruct_sucro_rep TIGR02417
D-fructose-responsive transcription factor; Members of this family belong the lacI ...
 4-201 4.54e-21

D-fructose-responsive transcription factor; Members of this family belong the lacI helix-turn-helix family (pfam00356) of DNA-binding transcriptional regulators. All members are from the proteobacteria. Characterized members act as positive and negative transcriptional regulators of fructose and sucrose transport and metabolism. Sucrose is a disaccharide composed of fructose and glucose; D-fructose-1-phosphate rather than an intact sucrose moiety has been shown to act as the inducer. [Regulatory functions, DNA interactions]


Pssm-ID: 131470 [Multi-domain]  Cd Length: 327  Bit Score: 91.74  E-value: 4.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037    4 IADIARLAGVSKSTVSRYLNNGS----VSTKTKEKLSKIIKEQDYQPNQFAQSLRARHTKMIGAIIPRMNSHAVDETIKG 79
Cdd:TIGR02417   2 LSDIAKLAGVSKTTASYVINGKAkeyrISQETVERVMAVVREQGYQPNIHAASLRAGRSRTIGLVIPDLENYSYARIAKE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037   80 VAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILmATRITPQHLDV--INKINVPVILVGQ--EHSGVNSIIH 155
Cdd:TIGR02417  82 LEQQCREAGYQLLIACSDDNPDQEKVVIENLLARQVDALIV-ASCMPPEDAYYqkLQNEGLPVVALDRslDDEHFCSVIS 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 488392037  156 DDYLAGSYVGRQIVEANYKQVYFFGvTEEDKAVGQQRKNGVLDILA 201
Cdd:TIGR02417 161 DDVDAAAELIERLLSQHADEFWYLG-AQPELSVSRDRLAGFRQALK 205
PRK11303 PRK11303
catabolite repressor/activator;
1-237 9.49e-21

catabolite repressor/activator;


Pssm-ID: 236897 [Multi-domain]  Cd Length: 328  Bit Score: 90.71  E-value: 9.49e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037   1 MKnIADIARLAGVSKSTVSrYLNNGS-----VSTKTKEKLSKIIKEQDYQPNQFAQSLRARHTKMIGAIIPRMnshavdE 75
Cdd:PRK11303   1 MK-LDEIARLAGVSRTTAS-YVINGKakqyrVSDKTVEKVMAVVREHNYHPNAVAAGLRAGRTRSIGLIIPDL------E 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  76 TIKgVAHVCKELE-------YQLLLNYTGLDLSEEIIALETLSRSKVDGIILmATRITPQH---LDVINKiNVPVILV-- 143
Cdd:PRK11303  73 NTS-YARIAKYLErqarqrgYQLLIACSDDQPDNEMRCAEHLLQRQVDALIV-STSLPPEHpfyQRLQND-GLPIIALdr 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 144 --GQEHsgVNSIIHDDYLAGSYVGRQIVEANYKQVYFFGVTEEdKAVGQQRKNGVLDILALNHIDVQV-FKTSFQFMEAK 220
Cdd:PRK11303 150 alDREH--FTSVVSDDQDDAEMLAESLLKFPAESILLLGALPE-LSVSFEREQGFRQALKDDPREVHYlYANSFEREAGA 226

                        250
                 ....*....|....*..
gi 488392037 221 NDVKLHLQSVHTADAII 237
Cdd:PRK11303 227 QLFEKWLETHPMPDALF 243
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
 60-293 4.09e-19

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: 85.24  E-value: 4.09e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKINVP 139
Cdd:cd01575    1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEELIRALLSRRPAGLILTGTEHTPATRKLLRAAGIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 140 VI------------LVGQEHsgvnsiihddYLAGSYVGRQIVEANYKQVYFFGVTEEDKAVGQQRKNGVLDILA---LNH 204
Cdd:cd01575   81 VVetwdlpddpidmAVGFSN----------FAAGRAMARHLIERGYRRIAFVGARLDGDSRARQRLEGFRDALAeagLPL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 205 IDVQVFKTSFQF---MEAKNDVklhLQSVHTADAIIGATDTIALAIHSYCSQpHHKLIPHK--IYGFGGDPITQIVTPQI 279
Cdd:cd01575  151 PLVLLVELPSSFalgREALAEL---LARHPDLDAIFCSNDDLALGALFECQR-RGIRVPGDiaIAGFGDLDIAAALPPAL 226

                        250
                 ....*....|....
gi 488392037 280 NTVMYHYFKAGQQA 293
Cdd:cd01575  227 TTVRVPRYEIGRKA 240
PRK14987 PRK14987
HTH-type transcriptional regulator GntR;
4-283 1.04e-18

HTH-type transcriptional regulator GntR;


Pssm-ID: 184949 [Multi-domain]  Cd Length: 331  Bit Score: 85.08  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037   4 IADIARLAGVSKSTVSRYLNN-GSVSTKTKEKLSKIIKEQDYQPNQFAQSLRARHTKMIGAIIPRMNSHAVDETIKGVAH 82
Cdd:PRK14987   8 LQDVADRVGVTKMTVSRFLRNpEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTNQVFAEVLRGIES 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  83 VCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKINVPVILVGQEHSGVNSII--HDDYLA 160
Cdd:PRK14987  88 VTDAHGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERTHTPRTLKMIEVAGIPVVELMDSQSPCLDIAvgFDNFEA 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 161 GSYVGRQIVEANYKQVYFFGVTEEDKAVGQQR--KNGVLDIlALNHIDVQVFKTSfQFMEAKNDVKLHLQSVHTADAIIG 238
Cdd:PRK14987 168 ARQMTTAIIARGHRHIAYLGARLDERTIIKQKgyEQAMLDA-GLVPYSVMVEQSS-SYSSGIELIRQARREYPQLDGVFC 245

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 488392037 239 ATDTIALAIHSYCSQPHHKlIPHK--IYGFGGDPITQIVTPQINTVM 283
Cdd:PRK14987 246 TNDDLAVGAAFECQRLGLK-VPDDmaIAGFHGHDIGQVMEPRLASVL 291
HTH_LacI cd01392
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ...
 5-55 3.55e-18

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: 76.68  E-value: 3.55e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488392037   5 ADIARLAGVSKSTVSRYLNN-GSVSTKTKEKLSKIIKEQDYQPNQFAQSLRA 55
Cdd:cd01392    1 KDIARAAGVSVATVSRVLNGkPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
 60-316 7.25e-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: 81.43  E-value: 7.25e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKiNVP 139
Cdd:cd06284    1 TILVLVPNISNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPEREDDLLDMLRSRRVDGVILLSGRLDAELLSELSK-RYP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 140 VILVG--QEHSGVNSIIHDDYLAGSYVGRQIVEANYKQVYFFGvTEEDKAVGQQRKNGVLDILALNHIDVQ---VFKTSF 214
Cdd:cd06284   80 IVQCCeyIPDSGVPSVSIDNEAAAYDATEYLISLGHRRIAHIN-GPLDNVYARERLEGYRRALAEAGLPVDedlIIEGDF 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 215 QFMEAKNDVKLHLQSVHTADAIIGATDTIALAIHSYCSqpHHKL-IPHKI--YGFGGDPITQIVTPQINTVMYHYFKAGQ 291
Cdd:cd06284  159 SFEAGYAAARALLALPERPTAIFCASDELAIGAIKALR--RAGLrVPEDVsvIGFDDIEFAEMFSPSLTTIRQPRYEIGE 236

                        250       260
                 ....*....|....*....|....*.
gi 488392037 292 QALSQLHRLINHHDAQLLTVI-PVEL 316
Cdd:cd06284  237 TAAELLLEKIEGEGVPPEHIIlPHEL 262
PBP1_CcpB-like cd06286
ligand-binding domain of a novel transcription factor implicated in catabolite repression in ...
 60-303 1.23e-17

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: 81.05  E-value: 1.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIIlMATRITPqhLDVINKINV- 138
Cdd:cd06286    1 TIGVVVPYIDHPYFSQLINGIAEAAFKKGYQVLLLQTNYDKEKELRALELLKTKQIDGLI-ITSREND--WEVIEPYAKy 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 139 -PVILVGQ-EHSGVNSIIHDDYLAGSYVGRQIVEANYKQV-YFFGVTEEDKAVGQQRKNGVLDILALNHIDVQ---VFKT 212
Cdd:cd06286   78 gPIVLCEEtDSPDIPSVYIDRYEAYLEALEYLKEKGHRKIgYCLGRPESSSASTQARLKAYQDVLGEHGLSLReewIFTN 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 213 SFQFMEAKNDVKLHLQSVHTADAIIGATDTIALAIHSYCsQPHHKLIPHKIY--GFGGDPITQIvtPQINTVMYHYFKAG 290
Cdd:cd06286  158 CHTIEDGYKLAKKLLALKERPDAIFTNSDEVAAGIIAEA-QKNGIRVPEDLAviGFDNQPISEL--LNLTTIDQPLEEMG 234

                        250
                 ....*....|...
gi 488392037 291 QQALSQLHRLINH 303
Cdd:cd06286  235 KEAFELLLSQLES 247
PBP1_CcpA cd06298
ligand-binding domain of the catabolite control protein A (CcpA), which functions as the major ...
 61-282 5.08e-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: 5.08e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  61 IGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKINVPV 140
Cdd:cd06298    2 VGVIIPDISNLYYAELARGIDDIATMYKYNIILSNSDNNVDKELDLLNTMLSKQVDGIIFMGDELTEEIREEFKRSPVPV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 141 ILVGQEHSG--VNSIIHDDYLAGSYVGRQIVEANYKQVYFFGVTEEDKAVGQQRKNGVLDILALNHIDVQ---VFKTSFQ 215
Cdd:cd06298   82 VLAGTVDSDheIPSVNIDYEQAAYDATKSLIDKGHKKIAFVSGPLKEYINNDKKLQGYKRALEEAGLEFNeplIFEGDYD 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488392037 216 FMEAKNDVKlHLQSVHTADAIIGATDTIALAIHSYcSQPHHKLIPH--KIYGFGGDPITQIVTPQINTV 282
Cdd:cd06298  162 YDSGYELYE-ELLESGEPDAAIVVRDEIAVGLLNA-AQDRGLKVPEdlEIIGFDNTRYATMSRPQLTSI 228
PBP1_LacI-like cd06273
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 60-316 6.55e-17

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: 79.09  E-value: 6.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKINVP 139
Cdd:cd06273    1 TIGAIVPTLDNAIFARAIQALQQTLAEAGYTLLLATSEYDPARELEQVRALIERGVDGLILVGSDHDPELFELLEQRQVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 140 VILVG--QEHSGVNSIIHDDYLAGSYVGRQIVEANYKQV-YFFGVTEE-DKAvgQQRKNGVLDILA---LNHIDVQVFKT 212
Cdd:cd06273   81 YVLTWsyDEDSPHPSIGFDNRAAAARAAQHLLDLGHRRIaVISGPTAGnDRA--RARLAGIRDALAergLELPEERVVEA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 213 SFQFMEAKNDVKLHLQSVHTADAIIGATDTIALAIHSYCSqpHHKL-IPHK--IYGFGGDPITQIVTPQINTVMYHYFKA 289
Cdd:cd06273  159 PYSIEEGREALRRLLARPPRPTAIICGNDVLALGALAECR--RLGIsVPEDlsITGFDDLELAAHLSPPLTTVRVPAREI 236

                        250       260
                 ....*....|....*....|....*..
gi 488392037 290 GQQALSQLHRLINHHDAQLLTVIPVEL 316
Cdd:cd06273  237 GELAARYLLALLEGGPPPKSVELETEL 263
PBP1_MalR-like cd06294
ligand-binding domain of maltose transcription regulator MalR which is a member of the ...
 61-316 9.73e-17

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: 78.39  E-value: 9.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  61 IGAIIPRMNSHAVD-----ETIKGVAHVCKELEYQLLLNyTGLDLSEEIIALETLSRSK-VDGIILMATRITPQHLDVIN 134
Cdd:cd06294    2 IGLVLPSSAEELFQnpffsEVLRGISQVANENGYSLLLA-TGNTEEELLEEVKRMVRGRrVDGFILLYSKEDDPLIEYLK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 135 KINVPVILVGQ--EHSGVNSIIHDDYLAGSYVGRQIVEANYKQVYFFGvTEEDKAVGQQRKNGVLDILALNHI---DVQV 209
Cdd:cd06294   81 EEGFPFVVIGKplDDNDVLYVDNDNVQAGYEATEYLIDKGHKRIAFIG-GDKNLVVSIDRLQGYKQALKEAGLpldDDYI 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 210 FKTSFQFMEAKNDVKLHLQSVHTADAIIGATDTIALAIHSYCSQpHHKLIPHK--IYGFGGDPITQIVTPQINTVMYHYF 287
Cdd:cd06294  160 LLLDFSEEDGYDALQELLSKPPPPTAIVATDDLLALGVLRYLQE-LGLRVPEDvsIISFNNSPLAELASPPLTSVDINPY 238

                        250       260       270
                 ....*....|....*....|....*....|
gi 488392037 288 KAGQQALSQLHRLINHHDAQL-LTVIPVEL 316
Cdd:cd06294  239 ELGREAAKLLINLLEGPESLPkNVIVPHEL 268
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 60-316 3.59e-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: 76.88  E-value: 3.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKINVP 139
Cdd:cd06285    1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTGDDPERELAALDSLLSRRVDGLIITPARDDAPDLQELAARGVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 140 VILVGQ--EHSGVNSIIHDDYLAGSYVGRQIVEANYKQVYFfgVTEEDKA-VGQQRKNGVLDILA---LNHIDVQVFKTS 213
Cdd:cd06285   81 VVLVDRriGDTALPSVTVDNELGGRLATRHLLELGHRRIAV--VAGPLNAsTGRDRLRGYRRALAeagLPVPDERIVPGG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 214 FQFMEAKNDVKLHLQSVHTADAIIGATDTIALAIHSYCSqpHHKL-IPHKI--YGFGGDPITQIVTPQINTVMYHYFKAG 290
Cdd:cd06285  159 FTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAAR--DLGLrVPEDLsvVGFDDIPLAAFLPPPLTTVRQPKYEMG 236

                        250       260
                 ....*....|....*....|....*..
gi 488392037 291 QQALSQLHRLINHHDAQL-LTVIPVEL 316
Cdd:cd06285  237 RRAAELLLQLIEGGGRPPrSITLPPEL 263
LacI pfam00356
Bacterial regulatory proteins, lacI family;
3-47 4.90e-16

Bacterial regulatory proteins, lacI family;


Pssm-ID: 306791 [Multi-domain]  Cd Length: 46  Bit Score: 70.74  E-value: 4.90e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 488392037    3 NIADIARLAGVSKSTVSRYLNN-GSVSTKTKEKLSKIIKEQDYQPN 47
Cdd:pfam00356   1 TIKDVARLAGVSKSTVSRVLNNpGRVSEETRERVEAAMEELNYIPN 46
PBP1_RegR_EndR_KdgR-like cd06283
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ...
 60-316 5.65e-16

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: 76.44  E-value: 5.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKINVP 139
Cdd:cd06283    1 LIGVIVADITNPFSSLLLKGIEDVCREAGYQLLICNSNNDPEKERDYIESLLSQRVDGLILQPTGNNNDAYLELAQKGLP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 140 VILVGQEHSGVN--SIIHDDYLAGSYVGRQIVEANYKQVYFFgvTEEDKAVG--QQRKNGVLDILALNHIDVQVFKTSfq 215
Cdd:cd06283   81 VVLVDRQIEPLNwdTVVTDNYDATYEATEHLKEQGYERIVFV--TEPIKGIStrRERLQGFLDALARYNIEGDVYVIE-- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 216 fMEAKNDVKLHLQSVHTAD-----AIIGATDT----IALAIHSYcsqphHKLIPHK--IYGFGGDPITQIVTPQINTVMY 284
Cdd:cd06283  157 -IEDTEDLQQALAAFLSQHdggktAIFAANGVvllrVLRALKAL-----GIRIPDDvgLCGFDDWDWADLIGPGITTIRQ 230

                        250       260       270
                 ....*....|....*....|....*....|...
gi 488392037 285 HYFKAGQQALSQLHRLINHHDAQL-LTVIPVEL 316
Cdd:cd06283  231 PTYEIGKAAAEILLERIEGDSGEPkEIELPSEL 263
PBP1_LacI-like cd06282
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 61-297 1.09e-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: 380505 [Multi-domain]  Cd Length: 267  Bit Score: 75.40  E-value: 1.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  61 IGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRI-TPQHLDVINKINVP 139
Cdd:cd06282    2 IGVLIPSLNNPVFAEAAQGIQRAARAAGYSLLIATTDYDPARELDAVETLLEQRVDGLILTVGDAqGSEALELLEEEGVP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 140 VILV--GQEHSGVNSIIHDDYLAGSYVGRQIVEANYKQVYFFGV--TEEDKAvgQQRKNGVLDILA---LNHID-VQVfk 211
Cdd:cd06282   82 YVLLfnQTENSSHPFVSVDNRLASYDVAEYLIALGHRRIAMVAGdfSASDRA--RLRYQGYRDALKeagLKPIPiVEV-- 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 212 tSFQFMEAKNDVKLHLQSVHTADAIIGATDTIALAIHSYCSQpHHKLIPHKI--YGFGGDPITQIVTPQINTVMYHYFKA 289
Cdd:cd06282  158 -DFPTNGLEEALTSLLSGPNPPTALFCSNDLLALSVISALRR-LGIRVPDDVsvIGFDGIAIGELLTPTLATVVQPSRDM 235


                 ....*...
gi 488392037 290 GQQALSQL 297
Cdd:cd06282  236 GRAAADLL 243
PBP1_DegA_Like cd19976
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
 60-303 2.61e-15

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: 74.59  E-value: 2.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVI-NKINV 138
Cdd:cd19976    1 TIGLIVPDISNPFFSELVRGIEDTLNELGYNIILCNTYNDFEREKKYIQELKERNVDGIIIASSNISDEAIIKLlKEEKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 139 PVILVGQ--EHSGVNSIIHDDYlAGSYVGRQ-IVEANYKQVYFfgVTEEDKAVG-QQRKNG---VLDILALNHIDVQVFK 211
Cdd:cd19976   81 PVVVLDRyiEDNDSDSVGVDDY-RGGYEATKyLIELGHTRIGC--IVGPPSTYNeHERIEGyknALQDHNLPIDESWIYS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 212 TSFQFMEAKNDVKLHLQSvHTADAIIGATDTIALAIHSYCSQPHHKlIPH--KIYGFGGDPITQIVTPQINTVMYHYFKA 289
Cdd:cd19976  158 GESSLEGGYKAAEELLKS-KNPTAIFAGNDLIAMGVYRAALELGLK-IPEdlSVIGFDNIILSEYITPALTTIAQPIFEM 235

                        250
                 ....*....|....
gi 488392037 290 GQQALSQLHRLINH 303
Cdd:cd19976  236 GQEAAKLLLKIIKN 249
lacI PRK09526
lac repressor; Reviewed
 1-156 2.28e-14

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 72.72  E-value: 2.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037   1 MKNIA--DIARLAGVSKSTVSRYLNNGS-VSTKTKEKLSKIIKEQDYQPNQFAQSLRARHTKMIGAIIPRMNSHAVDETI 77
Cdd:PRK09526   3 SKPVTlyDVARYAGVSYQTVSRVLNQAShVSAKTREKVEAAMAELNYVPNRVAQQLAGKQSLTIGLATTSLALHAPSQIA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  78 KGVAHVCKELEYQLLLNYTGLDLSEEI-IALETLSRSKVDGIIL-------MATRITPQHLDvinkinVPVI-LVGQEHS 148
Cdd:PRK09526  83 AAIKSRADQLGYSVVISMVERSGVEACqAAVNELLAQRVSGVIInvpledaDAEKIVADCAD------VPCLfLDVSPQS 156


                 ....*...
gi 488392037 149 GVNSIIHD 156
Cdd:PRK09526 157 PVNSVSFD 164
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 60-246 3.49e-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: 380501 [Multi-domain]  Cd Length: 266  Bit Score: 68.33  E-value: 3.49e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIiALETLSRSKVDGIILMATRITPQHLDVINKINVP 139
Cdd:cd06278    1 LVGVVVGDLSNPFYAELLEELSRALQARGLRPLLFNVDDEDDVDD-ALRQLLQYRVDGVIVTSATLSSELAEECARRGIP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 140 VILVG--QEHSGVNSIIHDDYLAGSYVGRQIVEANYKQVYFFGvTEEDKAVGQQRKNGVLDILA-LNHIDVQVFKTSFQF 216
Cdd:cd06278   80 VVLFNrvVEDPGVDSVSCDNRAGGRLAADLLLAAGHRRIAFLG-GPEGTSTSRERERGFRAALAeLGLPPPAVEAGDYSY 158

                        170       180       190
                 ....*....|....*....|....*....|
gi 488392037 217 MEAKNDVKLHLQSVHTADAIIGATDTIALA 246
Cdd:cd06278  159 EGGYEAARRLLAAPDRPDAIFCANDLMALG 188
PRK10401 PRK10401
HTH-type transcriptional regulator GalS;
1-130 1.15e-12

HTH-type transcriptional regulator GalS;


Pssm-ID: 236681 [Multi-domain]  Cd Length: 346  Bit Score: 67.49  E-value: 1.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037   1 MKNIADIARLAGVSKSTVSRYLNNGS-VSTKTKEKLSKIIKEQDYQPNQFAQSLRARHTKMIGAIIPRMNSHAVDETIKG 79
Cdd:PRK10401   1 MITIRDVARQAGVSVATVSRVLNNSAlVSADTREAVMKAVSELGYRPNANAQALATQVSDTIGVVVMDVSDAFFGALVKA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488392037  80 VAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHL 130
Cdd:PRK10401  81 VDLVAQQHQKYVLIGNSYHEAEKERHAIEVLIRQRCNALIVHSKALSDDEL 131
PRK10014 PRK10014
DNA-binding transcriptional repressor MalI; Provisional
 3-180 1.68e-12

DNA-binding transcriptional repressor MalI; Provisional


Pssm-ID: 182193 [Multi-domain]  Cd Length: 342  Bit Score: 67.04  E-value: 1.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037   3 NIADIARLAGVSKSTVSRYLN-NGSVSTKTKEKLSKIIKEQDYQPNQFAQSLRARHTKMIGAIIPRMNSHAVDETIKGVA 81
Cdd:PRK10014   8 TIHDVALAAGVSVSTVSLVLSgKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSAPFYAELTAGLT 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  82 HVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILM-ATRITPQHLDVINKINVPVILVGQEHS--GVNSIIHDDY 158
Cdd:PRK10014  88 EALEAQGRMVFLLQGGKDGEQLAQRFSTLLNQGVDGVVIAgAAGSSDDLREMAEEKGIPVVFASRASYldDVDTVRPDNM 167

                        170       180
                 ....*....|....*....|..
gi 488392037 159 LAGSYVGRQIVEANYKQVYFFG 180
Cdd:PRK10014 168 QAAQLLTEHLIRNGHQRIAWLG 189
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
 61-316 5.30e-12

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: 64.89  E-value: 5.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  61 IGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATR---ITPqHLDVINKI- 136
Cdd:cd01541    2 IGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKEREILESLLDQNVDGLIIEPTKsalPNP-NLDLYEELq 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 137 --NVPVILVGQEHS--GVNSIIHDDYLAGSYVGRQIVEANYKQVyfFGVTEEDKAVGQQRKNGVLDILALNHIDVQ---V 209
Cdd:cd01541   81 kkGIPVVFINSYYPelDAPSVSLDDEKGGYLATKHLIDLGHRRI--AGIFKSDDLQGVERYQGFIKALREAGLPIDddrI 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 210 FK---TSFQFMEAKNDVKLHLQSVHTADAIIGATDTIALAIHSYCSQpHHKLIPHK--IYGFGGDPITQIVTPQINTVMY 284
Cdd:cd01541  159 LWystEDLEDRFFAEELREFLRRLSRCTAIVCYNDEIALRLIQALRE-AGLRVPEDlsVVGFDDSYLASLSEPPLTSVVH 237

                        250       260       270
                 ....*....|....*....|....*....|..
gi 488392037 285 HYFKAGQQALSQLHRLINHHDAQLLTVIPVEL 316
Cdd:cd01541  238 PKEELGRKAAELLLRMIEEGRKPESVIFPPEL 269
PBP1_SalR cd01545
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ...
 60-316 6.85e-12

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: 64.50  E-value: 6.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLL---LNYTGLDLSEEIIALetLSRSKVDGIILmatriTPQH------L 130
Cdd:cd01545    1 LIGLLYDNPSASYVSALQVGALRACREAGYHLVvepCDSDDEDLADRLRRF--LSRSRPDGVIL-----TPPLsddpalL 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 131 DVINKINVPVILV--GQEHSGVNSIIHDDYLAGSYVGRQIVEANYKQVYFFGVtEEDKAVGQQRKNGVLDILALNHIDVQ 208
Cdd:cd01545   74 DALDELGIPYVRIapGTDDDRSPSVRIDDRAAAREMTRHLIALGHRRIGFIAG-PPDHGASAERLEGFRDALAEAGLPLD 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 209 V---------FKTSFQFMEAkndvkLhLQSVHTADAIIGATDTIALAIHSYCSQphHKL-IPHK--IYGFGGDPITQIVT 276
Cdd:cd01545  153 PdlvvqgdftFESGLEAAEA-----L-LDLPDRPTAIFASNDEMAAGVLAAAHR--LGLrVPDDlsVAGFDDSPIARLVW 224

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 488392037 277 PQINTV------MyhyfkaGQQALSQLHRLINHHDAQLLT-VIPVEL 316
Cdd:cd01545  225 PPLTTVrqpiaeM------ARRAVELLIAAIRGAPAGPEReTLPHEL 265
PBP1_CcpA_TTHA0807 cd06297
ligand-binding domain of TTHA0807, a CcpA regulator, from Thermus thermophilus HB8 and its ...
 61-302 1.23e-11

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: 64.02  E-value: 1.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  61 IGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLnYTGLDLSEEIIALETLSRSK-VDGIILMATRITPQHLDVINKINVP 139
Cdd:cd06297    2 ISLLVPEVMTPFYMRLLTGVERALDENRYDLAI-FPLLSEYRLEKYLRNSTLAYqCDGLVMASLDLTELFEEVIVPTEKP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 140 VILVGQEHSGVNSIIHDDYLAGSYVGRQIVEANYKQVYFFGVTEED---KAVGQQRKNGVLDILALNHIDVQ---VFKTS 213
Cdd:cd06297   81 VVLIDANSMGYDCVYVDNVKGGFMATEYLAGLGEREYVFFGIEEDTvftETVFREREQGFLEALNKAGRPISssrMFRID 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 214 FQFMEAKNDVKLHLQSVHTADAIIGATDTIALAIHSyCSQPHHKLIPHKIY--GFGGDPITQivTPQINTVMYHYFKAGQ 291
Cdd:cd06297  161 NSSKKAECLARELLKKADNPAAFFAAADLVALGLIR-AAQSLGLRVGEDVAviGFDGQPWAA--SPGLTTVRQPVEEMGE 237

                        250
                 ....*....|.
gi 488392037 292 QALSQLHRLIN 302
Cdd:cd06297  238 AAAKLLLKRLN 248
PBP1_sucrose_transcription_regulator cd06288
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ...
 60-316 1.54e-10

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: 60.64  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNS--HAVDeTIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIIL--MATRITPQHLDvinK 135
Cdd:cd06288    1 TIGLITDDIATtpFAGD-IIRGAQDAAEEHGYLLLLANTGGDPELEAEAIRELLSRRVDGIIYasMHHREVTLPPE---L 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 136 INVPVILVGQ--EHSGVNSIIHDDYLAGSYVGRQIVEANYKQVYFFGVTEEDKAVgQQRKNGVLDILALNHIDVQ---VF 210
Cdd:cd06288   77 TDIPLVLLNCfdDDPSLPSVVPDDEQGGYLATRHLIEAGHRRIAFIGGPEDSLAT-RLRLAGYRAALAEAGIPYDpslVV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 211 KTSFQFMEAKNDVKLHLQSVHTADAIIGATDTIALAIHSYCSQphHKL-IPH--KIYGFGGDPITQIVTPQINTVMYHYF 287
Cdd:cd06288  156 HGDWGRESGYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAE--LGLrVPEdlSVVGFDNQELAAYLRPPLTTVALPYY 233

                        250       260       270
                 ....*....|....*....|....*....|
gi 488392037 288 KAGQQALSQLHRLINHHDAQ-LLTVIPVEL 316
Cdd:cd06288  234 EMGRRAAELLLDGIEGEPPEpGVIRVPCPL 263
PBP1_PurR cd06275
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ...
 60-316 2.42e-10

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: 59.96  E-value: 2.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKI-NV 138
Cdd:cd06275    1 TIGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAELLAALrSI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 139 PVILV--GQEHSGVNSIIhDDYLAGSYV-GRQIVEANYKQVYFFGVTEEdKAVGQQRKNGVLDILALNHIDVQ---VFKT 212
Cdd:cd06275   81 PVVVLdrEIAGDNADAVL-DDSFQGGYLaTRHLIELGHRRIGCITGPLE-HSVSRERLAGFRRALAEAGIEVPpswIVEG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 213 SFQF---MEAKNDVklhLQSVHTADAIIGATDTIAL-AIHSycSQPHHKLIPH--KIYGFGGDPITQIVTPQINTVMYHY 286
Cdd:cd06275  159 DFEPeggYEAMQRL---LSQPPRPTAVFACNDMMALgALRA--AQEQGLRVPQdiSIIGYDDIELARYFSPALTTIHQPK 233

                        250       260       270
                 ....*....|....*....|....*....|.
gi 488392037 287 FKAGQQALSQL-HRLINHHDAQLLTVIPVEL 316
Cdd:cd06275  234 DELGELAVELLlDRIENKREEPQSIVLEPEL 264
PBP1_GalS-like cd06270
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ...
 60-305 2.90e-10

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: 59.84  E-value: 2.90e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKINVP 139
Cdd:cd06270    1 TIGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEEREAIEFLLDRRCDAIILHSRALSDEELILIAEKIPP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 140 VILVGQ---EHSGvNSIIHDDYLAGSYVGRQIVEANYKQVYFFGVtEEDKAVGQQRKNGVLDILALNHIDVQ---VFKTS 213
Cdd:cd06270   81 LVVINRyipGLAD-RCVWLDNEQGGRLAAEHLLDLGHRRIACITG-PLDIPDARERLAGYRDALAEAGIPLDpslIIEGD 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 214 FQFMEAKNDVKLHLQSVHTADAIIGATDTIALAIHSYCSQpHHKLIPHKI--YGFGGDPITQIVTPQINTVMYHYFKAGQ 291
Cdd:cd06270  159 FTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHE-AGIKVPEDVsvIGFDDVPLARYLSPKLTTVHYPIEEMAQ 237

                        250
                 ....*....|....
gi 488392037 292 QALSQLHRLINHHD 305
Cdd:cd06270  238 AAAELALNLAYGEP 251
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 61-316 3.20e-10

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: 59.94  E-value: 3.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  61 IGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMAtrITPQHL-DVINKIN-- 137
Cdd:COG1879   36 IGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAAKQISQIEDLIAQGVDAIIVSP--VDPDALaPALKKAKaa 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 138 -VPVILVgqeHSGVNS------IIHDDYLAGSYVGRQIVEA-NYKQVYFFGVTEEDKAVGQQRKNGVLDILAlNHIDVQV 209
Cdd:COG1879  114 gIPVVTV---DSDVDGsdrvayVGSDNYAAGRLAAEYLAKAlGGKGKVAILTGSPGAPAANERTDGFKEALK-EYPGIKV 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 210 FKTS---FQFMEAKNDVKLHLQSVHTADAIIGATDTIALAIHSYCSQpHHKLIPHKIYGFGGDP--ITQIVTPQIN-TVM 283
Cdd:COG1879  190 VAEQyadWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKA-AGRKGDVKVVGFDGSPeaLQAIKDGTIDaTVA 268

                        250       260       270
                 ....*....|....*....|....*....|...
gi 488392037 284 YHYFKAGQQALSQLHRLINHHDAQLLTVIPVEL 316
Cdd:COG1879  269 QDPYLQGYLAVDAALKLLKGKEVPKEILTPPVL 301
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
 61-316 1.21e-09

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: 57.96  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  61 IGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMA---TRITPqhldVINKIN 137
Cdd:cd01536    2 IGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPvdsEALVP----AVKKAN 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 138 ---VPVILVGQE---HSGVNSII-HDDYLAGSYVGRQIVEA-----NYkqVYFFGVteEDKAVGQQRKNGVLDILAlNHI 205
Cdd:cd01536   78 aagIPVVAVDTDidgGGDVVAFVgTDNYEAGKLAGEYLAEAlggkgKV--AILEGP--PGSSTAIDRTKGFKEALK-KYP 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 206 DVQVFKT---------SFQFMEAKndvklhLQSVHTADAIIGATDTIALAIHSYCSQpHHKLIPHKIYGFGGDP--ITQI 274
Cdd:cd01536  153 DIEIVAEqpanwdrakALTVTENL------LQANPDIDAVFAANDDMALGAAEALKA-AGRTGDIKIVGVDGTPeaLKAI 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 488392037 275 VTPQIN-TVMYHYFKAGQQALSQLHRLINHHDAQLLTVIPVEL 316
Cdd:cd01536  226 KDGELDaTVAQDPYLQGYLAVEAAVKLLNGEKVPKEILTPVTL 268
PBP1_LacI-like cd06290
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 60-316 2.87e-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: 380513 [Multi-domain]  Cd Length: 267  Bit Score: 56.85  E-value: 2.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITP-QHLDVINKInv 138
Cdd:cd06290    1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGDEeLLKLLAEGI-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 139 PVILVGQEHSGVN-SIIHDDYLAGSYVGrqiveANY-------KQVYFFGVteEDKAVGQQRKNGVLDILALNHIDV-QV 209
Cdd:cd06290   79 PVVLVDRELEGLNlPVVNVDNEQGGYNA-----TNHlidlghrRIVHISGP--EDHPDAQERYAGYRRALEDAGLEVdPR 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 210 FKTSFQFME--AKNDVKLHLQSVHTADAIIGATDTIAL----AIHSycsqpHHKLIPH--KIYGFGGDPITQIVTPQINT 281
Cdd:cd06290  152 LIVEGDFTEesGYEAMKKLLKRGGPFTAIFAANDLMALgamkALRE-----AGIRVPDdvSVIGFDDLPFSKYTTPPLTT 226

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 488392037 282 VMYHYFKAGQQALSQLHRLINH-HDAQLLTVIPVEL 316
Cdd:cd06290  227 VRQPLYEMGKTAAEILLELIEGkGRPPRRIILPTEL 262
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
 60-316 3.05e-09

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: 56.77  E-value: 3.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKINVP 139
Cdd:cd19977    1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVILCNTDEDPEKEKKYIEMLRAKQVDGIIIAPTGGNEDLIEKLVKSGIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 140 VILVGQEHSG--VNSIIHDDYLAGSYVGRQIVEANYKQVYFFGVTEEDKAvGQQRKNGVLDILALNHIDV--QVFKTSFQ 215
Cdd:cd19977   81 VVFVDRYIPGldVDTVVVDNFKGAYQATEHLIELGHKRIAFITYPLELST-RQERLEGYKAALADHGLPVdeELIKHVDR 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 216 FMEAKNDVKLHLQSVHTADAIIGATDTIALAIHSYCSQpHHKLIPHKI--YGFGGDPITQIVTPQINTVMYHYFKAGQQA 293
Cdd:cd19977  160 QDDVRKAISELLKLEKPPDAIFAANNLITLEVLKAIKE-LGLRIPDDIalIGFDDIPWADLFNPPLTVIAQPTYEIGRKA 238

                        250       260
                 ....*....|....*....|....*
gi 488392037 294 LSQLHRLINHHDAQL--LTVIPVEL 316
Cdd:cd19977  239 AELLLDRIENKPKGPprQIVLPTEL 263
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
 60-316 3.55e-09

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: 56.50  E-value: 3.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKINVP 139
Cdd:cd06280    1 TIGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANTDEDPEKEKRYLDSLLSKQVDGIILAPSAGPSRELKRLLKHGIP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 140 VILVGQEHSG--VNSIIHDDYLAGSYVGRQIVEANYKQVYFFgVTEEDKAVGQQRKNGVLDILALNHIDVQ---VFKTSF 214
Cdd:cd06280   81 IVLIDREVEGleLDLVAGDNREGAYKAVKHLIELGHRRIGLI-TGPLEISTTRERLAGYREALAEAGIPVDeslIFEGDS 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 215 QFMEAKNDVKLHLQSVHTADAIIGATDTiaLAIHSYCSQPHHKL-IPHKI--YGFGGDPITQIVTPQINTVMYHYFKAGQ 291
Cdd:cd06280  160 TIEGGYEAVKALLDLPPRPTAIFATNNL--MAVGALRALRERGLeIPQDIsvVGFDDSDWFEIVDPPLTVVAQPAYEIGR 237

                        250       260
                 ....*....|....*....|....*.
gi 488392037 292 QALSQLHRLINHHD-AQLLTVIPVEL 316
Cdd:cd06280  238 IAAQLLLERIEGQGeEPRRIVLPTEL 263
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 61-302 9.57e-09

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: 55.39  E-value: 9.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037   61 IGAIIPRMNSHAVDETIKGVAHVCKELEYQLLL-NYTGLDLSEEIIALETLSRSKVDGIILMA---TRITPqhldVINKI 136
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVvGPAEADAAEQVAQIEDAIAQGVDAIIVAPvdpTALAP----VLKKA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  137 ---NVPVILVGQEHSGVNSIIH---DDYLAGSYVGRQIVEA---NYKQVYFFGVteEDKAVGQQRKNGVLDILALNHIDV 207
Cdd:pfam13407  77 kdaGIPVVTFDSDAPSSPRLAYvgfDNEAAGEAAGELLAEAlggKGKVAILSGS--PGDPNANERIDGFKKVLKEKYPGI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  208 QVFKTSFQFMEAKNDVKLHLQSV-----HTADAIIGATDTIALAIHSYCSQPHHKLIPhKIYGFGGDP--ITQIVTPQIN 280
Cdd:pfam13407 155 KVVAEVEGTNWDPEKAQQQMEALltaypNPLDGIISPNDGMAGGAAQALEAAGLAGKV-VVTGFDATPeaLEAIKDGTID 233

                         250       260
                  ....*....|....*....|...
gi 488392037  281 -TVMYHYFKAGQQALSQLHRLIN 302
Cdd:pfam13407 234 aTVLQDPYGQGYAAVELAAALLK 256
PRK10727 PRK10727
HTH-type transcriptional regulator GalR;
1-130 3.33e-08

HTH-type transcriptional regulator GalR;


Pssm-ID: 182681 [Multi-domain]  Cd Length: 343  Bit Score: 53.99  E-value: 3.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037   1 MKNIADIARLAGVSKSTVSRYLNNG-SVSTKTKEKLSKIIKEQDYQPNQFAQSLRARHTKMIGAIIPRMNSHAVDETIKG 79
Cdd:PRK10727   1 MATIKDVARLAGVSVATVSRVINNSpKASEASRLAVHSAMESLSYHPNANARALAQQSTETVGLVVGDVSDPFFGAMVKA 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488392037  80 VAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHL 130
Cdd:PRK10727  81 VEQVAYHTGNFLLIGNGYHNEQKERQAIEQLIRHRCAALVVHAKMIPDAEL 131
PBP1_LacI cd01574
ligand-binding domain of DNA transcription repressor LacI specific for lactose, a member of ...
 60-170 2.61e-07

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: 51.04  E-value: 2.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLL-NYTGLDLSEEIIALETLSRSKVDGIILMA-TRITPQHLDVINKiN 137
Cdd:cd01574    1 TIGVIATGLSLYGPASTLAGIERAARERGYSVSIaTVDEDDPASVREALDRLLSQRVDGIIVIApDEAVLEALRRLPP-G 79

                         90       100       110
                 ....*....|....*....|....*....|....
gi 488392037 138 VPVILVG-QEHSGVNSIIHDDYLAgsyvGRQIVE 170
Cdd:cd01574   80 LPVVIVGsGPSPGVPTVSIDQEEG----ARLATR 109
PBP1_AglR_RafR-like cd06292
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ...
 60-316 4.24e-07

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: 50.34  E-value: 4.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIP----RMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINK 135
Cdd:cd06292    1 LIGYVVPelpgGFSDPFFDEFLAALGHAAAARGYDVLLFTASGDEDEIDYYRDLVRSRRVDGFVLASTRHDDPRVRYLHE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 136 INVPVILVGQ--EHSGVNSIIHDDYLAGSYVGRQIVEANYKQVYFFGvTEEDKAVGQQRKNGVLDILALNHIDVQ----- 208
Cdd:cd06292   81 AGVPFVAFGRanPDLDFPWVDVDGAAGMRQAVRHLIALGHRRIGLIG-GPEGSVPSDDRLAGYRAALEEAGLPFDpglvv 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 209 --VFKTSFQFMEAKNdvkLhLQSVHTADAIIGATDTIALAIHSYCSQpHHKLIPHK--IYGFGGDPITQIVTPQINTVMY 284
Cdd:cd06292  160 egENTEEGGYAAAAR---L-LDLGPPPTAIVCVSDLLALGAMRAARE-RGLRVGRDvsVVGFDDSPLAAFTHPPLTTVRQ 234

                        250       260       270
                 ....*....|....*....|....*....|...
gi 488392037 285 HYFKAGQQALSQLHRLINH-HDAQLLTVIPVEL 316
Cdd:cd06292  235 PIDEIGRAVVDLLLAAIEGnPSEPREILLQPEL 267
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
 76-296 8.58e-07

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


Pssm-ID: 380620 [Multi-domain]  Cd Length: 272  Bit Score: 49.58  E-value: 8.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  76 TIKGVAHVCKEL--EYQLLLNYTGlDLSEEIIALETLSRSKVDGIILmaTRITPQHLD-VINKI---NVPVILV-----G 144
Cdd:cd19965   17 VKKGMDDACELLgaECQFTGPQTF-DVAEQVSLLEAAIASGPDGIAT--TIVDPEAFDeVIKRAldaGIPVVAFnvdapG 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 145 QEHSGVNSIIHDDYLAGSYVGRQIVEANYKQ--VYFFGVTEEDKAVGQQRKNGVLDILALNH--IDVQVFKTSFQFMEAK 220
Cdd:cd19965   94 GENARLAFVGQDLYPAGYVLGKRIAEKFKPGggHVLLGISTPGQSALEQRLDGIKQALKEYGrgITYDVIDTGTDLAEAL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 221 NDVKLHLQSvHTADAIIGATDTIAlaiHSYCSQPHHKL-IPHKIYGFGGDpitqiVTPQINTVM---YHYFKAGQQALSQ 296
Cdd:cd19965  174 SRIEAYYTA-HPDIKAIFATGAFD---TAGAGQAIKDLgLKGKVLVGGFD-----LVPEVLQGIkagYIDFTIDQQPYLQ 244
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
 61-301 1.44e-06

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: 48.78  E-value: 1.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  61 IGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKI-NVP 139
Cdd:cd01537    2 IGVTIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNDQEKQNDQIDVLLAKRVKGLAINLVDPAAAGVAEKARGqNVP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 140 VILVGQEHSG---VNSIIHDDYLAGSYVGRQIVEANYKQvyfFGVT--EEDKAVGQQRKNGVLDILALNHIDVQ---VFK 211
Cdd:cd01537   82 VVFFDKEPSRydkAYYVITDSKEGGIIQGDLLAKHGHIQ---IVLLkgPLGHPDAEARLAGVIKELNDKGIKTEqlqLDT 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 212 TSFQFMEAKNDVKLHLQSVHTADAIIGATDTIALAihSYCS-QPHHKLIPHKIYGFGGD--PITQIVTPQINTVMYHYFK 288
Cdd:cd01537  159 GDWDTASGKDKMDQWLSGPNKPTAVIANNDAMAMG--AVEAlKEHGLRVPSDISVFGYDalPEALKSGPLLTTILQDANN 236

                        250
                 ....*....|...
gi 488392037 289 AGQQALSQLHRLI 301
Cdd:cd01537  237 LGKTTFDLLLNLA 249
PBP1_CelR cd06295
ligand binding domain of a transcription regulator of cellulose genes, CelR, which is highly ...
 80-316 1.89e-06

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: 48.40  E-value: 1.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  80 VAHVCKEL---EYQLLLNYTGLDLSEEiiaLETLSRSKVDGIILMATRITPQHLDVINKINVPVILVG-----QEHSGVN 151
Cdd:cd06295   29 LGGISEALtdrGYDMLLSTQDEDANQL---ARLLDSGRADGLIVLGQGLDHDALRELAQQGLPMVVWGapedgQSYCSVG 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 152 SiihDDYLAGSYVGRQIVEANYKQVYFFGVTEEdkAVGQQRKNGVLDILA---LNHIDVQVFKTSFQFMEAKNDVKLHLQ 228
Cdd:cd06295  106 S---DNVKGGALATEHLIEIGRRRIAFLGDPPH--PEVADRLQGYRDALAeagLEADPSLLLSCDFTEESGYAAMRALLD 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 229 SVHTADAIIGATDTIALAIHSYCSQpHHKLIPHK--IYGFGGDPITQIVTPQINTVMYHYFKAGQQALSQLHRLINHHDA 306
Cdd:cd06295  181 SGTAFDAIFAASDLIAMGAIRALRE-RGISVPGDvaVVGYDDIPLAAYFRPPLTTVRQDLALAGRLLVEKLLALIAGEPV 259

                        250
                 ....*....|
gi 488392037 307 QLLTViPVEL 316
Cdd:cd06295  260 TSSML-PVEL 268
PBP1_FruR cd06274
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ...
 60-209 2.65e-06

ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs; Ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its close homologs, all of which are members of the LacI-GalR family of bacterial transcription regulators. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to members of the type 1 periplasmic binding protein superfamily. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor


Pssm-ID: 380498 [Multi-domain]  Cd Length: 264  Bit Score: 47.97  E-value: 2.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHavdetikGVAHVCKELE-------YQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDV 132
Cdd:cd06274    1 TIGLIVPDLANR-------FFARLAEALErlarergLQLLIACSDDDPEQERRLVENLIARQVDGLIVAPSTPPDDIYYL 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488392037 133 INKINVPVILVGQEHSGVN--SIIHDDYLAGSYVGRQIVEANYKQVYFFGVTEEDKAVgQQRKNGVLDILALNHIDVQV 209
Cdd:cd06274   74 CQAAGLPVVFLDRPFSGSDapSVVSDNRAGARALTEKLLAAGPGEIYFLGGRPELPST-AERIRGFRAALAEAGITEGD 151
PBP1_LacI-like cd06277
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 73-302 3.36e-06

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: 47.62  E-value: 3.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  73 VDETIKGVAHVCKELEYQLLLN--YTGLDLSEEIIALETlsrSKVDGIILMATRITPQHLDVINKINVPVILVGQ--EHS 148
Cdd:cd06277   21 FSELIDGIEREARKYGYNLLISsvDIGDDFDEILKELTD---DQSSGIILLGTELEEKQIKLFQDVSIPVVVVDNyfEDL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 149 GVNSIIHDD----YLAGSYvgrqIVEANYKQVYFFGvTEEDKAVGQQRKNGVLDILALNHI-----DVQVFKTSFQfmEA 219
Cdd:cd06277   98 NFDCVVIDNedgaYEAVKY----LVELGHTRIGYLA-SSYRIKNFEERRRGFRKAMRELGLsedpePEFVVSVGPE--GA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 220 KNDVKLHL-QSVHTADAIIGATDTIAL-AIHSYcsQPHHKLIPHKIYGFGGDPIT--QIVTPQINTVMYHYFKAGQQALS 295
Cdd:cd06277  171 YKDMKALLdTGPKLPTAFFAENDIIALgCIKAL--QEAGIRVPEDVSVIGFDDIPvsAMVDPPLTTIHVPKEQMGKLAVR 248


                 ....*..
gi 488392037 296 QLHRLIN 302
Cdd:cd06277  249 RLIEKIK 255
PBP1_LacI-like cd06281
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 60-146 3.90e-06

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: 47.62  E-value: 3.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRIT-PQHLDVINKINV 138
Cdd:cd06281    1 TVGCLVSDISNPLYARIVKAAEARLRAAGYTLLLASTGNDEERELELLSLFQRRRVDGLILTPGDEDdPELAAALARLDI 80


                 ....*...
gi 488392037 139 PVILVGQE 146
Cdd:cd06281   81 PVVLIDRD 88
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
 61-248 4.43e-06

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: 47.51  E-value: 4.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037   61 IGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIIL--MATR---ITPQHldviNK 135
Cdd:pfam00532   4 LGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTNAIDLLLASGADGIIIttPAPSgddITAKA----EG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  136 INVPVIL---VGQEHSGVNSIIHDDYLAGSYVGRQIVEANYKQ-VYFFGVTEEDKAVGqQRKNGVLDILALNHIDVQvfk 211
Cdd:pfam00532  80 YGIPVIAaddAFDNPDGVPCVMPDDTQAGYESTQYLIAEGHKRpIAVMAGPASALTAR-ERVQGFMAALAAAGREVK--- 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 488392037  212 tSFQFMEAKNDVKL-------HLQSVHTADAIIGATDTIALAIH 248
Cdd:pfam00532 156 -IYHVATGDNDIPDaalaanaMLVSHPTIDAIVAMNDEAAMGAV 198
PBP1_CatR-like cd06296
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ...
 61-316 5.99e-06

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: 46.89  E-value: 5.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  61 IGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKINVPV 140
Cdd:cd06296    2 IDLVLPQLDSPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDDWVRRAVARGSAGVVLVTSDPTSRQLRLLRSAGIPF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 141 ILV---GQEHSGVNSIIHDDYLAGSYVGRQIVEANYKQVYFFGvTEEDKAVGQQRKNGVLDILALNHIDVQ---VFKTSF 214
Cdd:cd06296   82 VLIdpvGEPDPDLPSVGATNWAGGRLATEHLLDLGHRRIAVIT-GPPRSVSGRARLAGYRAALAEAGIAVDpdlVREGDF 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 215 QFMEAKNDVKLHLQSVHTADAIIGATDTIALAIHSYCSQpHHKLIPHK--IYGFGGDPITQIVTPQINTVMYHYFKAGQQ 292
Cdd:cd06296  161 TYEAGYRAARELLELPDPPTAVFAGNDEQALGVYRAARA-LGLRVPDDlsVIGFDDTPPARWTSPPLTTVHQPLREMGAV 239

                        250       260
                 ....*....|....*....|....
gi 488392037 293 ALSQLHRLINHHDaqlLTVIPVEL 316
Cdd:cd06296  240 AVRLLLRLLEGGP---PDARRIEL 260
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 78-316 1.23e-05

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


Pssm-ID: 380542 [Multi-domain]  Cd Length: 278  Bit Score: 45.81  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  78 KGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATR--ITPQHLDVINKINVPVIL--VGQEHSGVNSI 153
Cdd:cd06319   19 RGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNssAAPTVLDLANEAKIPVVIadIGTGGGDYVSY 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 154 IHDD-----YLAGSYVGRQIvEANYKQVYFFGV--TEEDKAVGQQRKNGVLDILA---LNHIDVQVFKTS-----FQFME 218
Cdd:cd06319   99 IISDnydggYQAGEYLAEAL-KENGWGGGSVGIiaIPQSRVNGQARTAGFEDALEeagVEEVALRQTPNStveetYSAAQ 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 219 ----AKNDVK-LHLQsvhTADAIIGATDTIALAIHSycsqphHKLIphkIYGFGGDPITQIVTPQ---INTVMYHYFKAG 290
Cdd:cd06319  178 dllaANPDIKgIFAQ---NDQMAQGALQAIEEAGRT------GDIL---VVGFDGDPEALDLIKDgklDGTVAQQPFGMG 245

                        250       260
                 ....*....|....*....|....*..
gi 488392037 291 QQALSQLHRLINHHDAQLLTV-IPVEL 316
Cdd:cd06319  246 ARAVELAIQALNGDNTVEKEIyLPVLL 272
PBP1_AglR_RafR-like cd06271
ligand-binding domain of DNA transcription repressors specific for raffinose (RafR) and ...
 66-312 1.29e-05

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: 45.88  E-value: 1.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  66 PRMNSHAVDETIKGVAHVCKELEYQLLLnyTGLDLSEEIIALETLSRS-KVDGIILMATRITPQHLDVINKINVPVILVG 144
Cdd:cd06271   10 ETELNGTVSE*VSGITEEAGTTGYHLLV--WPFEEAES*VPIRDLVETgSADGVILSEIEPNDPRVQFLTKQNFPFVAHG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 145 QEHSGVNSIIHD-DYLAGSY--VGRqIVEANYKQVYFFGvTEEDKAVGQQRKNGVLDIL---ALNHIDVQVFKTsfqfME 218
Cdd:cd06271   88 RSD*PIGHAWVDiDNEAGAYeaVER-LAGLGHRRIAFIV-PPARYSPHDRRLQGYVRA*rdaGLTGYPLDADTT----LE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 219 AKNDVKLHL-QSVHTADAIIGATDTIALAIHSyCSQPHHKLIPH--KIYGFGGDPITQ-IVTPQINTVMYHYFKAGQQAL 294
Cdd:cd06271  162 AGRAAAQRLlALSPRPTAIVTMNDSATIGLVA-GLQAAGLKIGEdvSIIGKDSAPFLGaMITPPLTTVHAPIAEAGRELA 240

                        250
                 ....*....|....*...
gi 488392037 295 SQLHRLINHHDAQLLTVI 312
Cdd:cd06271  241 KALLARIDGEDPETLQVL 258
Peripla_BP_3 pfam13377
Periplasmic binding protein-like domain; This domain is found in a variety of transcriptional ...
 176-316 1.76e-05

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: 44.25  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  176 VYFFGVTEEDKAVGQQRKNGVLDILALNHIDVQVF-KTSFQFMEAKNDVKLHLQSVHTADAIIGATDTIALAIHSYCSQp 254
Cdd:pfam13377  11 ALIGPEGDRDDPYSDLRERGFREAARELGLDVEPTlYAGDDEAEAAAARERLRWLGALPTAVFVANDEVALGVLQALRE- 89

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488392037  255 HHKLIPH--KIYGFGGDPITQIVTPQINTVMYHYFKAGQQALSQLHRLINHHDAQL-LTVIPVEL 316
Cdd:pfam13377  90 AGLRVPEdlSVIGFDDSPLAALVSPPLTTVRVDAEELGRAAAELLLDLLNGEPAPPeRVLLPPEL 154
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
 60-306 3.07e-05

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


Pssm-ID: 380512 [Multi-domain]  Cd Length: 268  Bit Score: 44.86  E-value: 3.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILM-ATRITPQHLDVINKINV 138
Cdd:cd06289    1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPERQRRFLRRMLEQGVDGLILSpAAGTTAELLRRLKAWGI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 139 PVILVGQ--EHSGVNSIIHDDYLAGSYVGRQIVEANYKQVYFFGvTEEDKAVGQQRKNGVLDILA-----LNHIDVQVFK 211
Cdd:cd06289   81 PVVLALRdvPGSDLDYVGIDNRLGAQLATEHLIALGHRRIAFLG-GLSDSSTRRERLAGFRAALAeaglpLDESLIVPGP 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 212 TSFQF-MEAKNDVklhLQSVHTADAIIGATDTIALAIHSYCSqpHHKLIPHK---IYGFGGDPITQIVTPQINTVMYHYF 287
Cdd:cd06289  160 ATREAgAEAAREL---LDAAPPPTAVVCFNDLVALGAMLALR--RRGLEPGRdiaVVGFDDVPEAALWTPPLTTVSVHPR 234

                        250
                 ....*....|....*....
gi 488392037 288 KAGQQALSQLHRLINHHDA 306
Cdd:cd06289  235 EIGRRAARLLLRRIEGPDT 253
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 60-180 2.30e-04

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


Pssm-ID: 380516 [Multi-domain]  Cd Length: 270  Bit Score: 41.87  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKINVP 139
Cdd:cd06293    1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDDDLSHLARLRARGTA 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488392037 140 VILVGQ--EHSGVNSIIHDDYLAGSYVGRQIVEANYKQVYFFG 180
Cdd:cd06293   81 VVLLDRpaPGPAGCSVSVDDVQGGALAVDHLLELGHRRIAFVS 123
PBP1_LacI-like cd06279
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ...
 69-316 3.17e-04

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: 41.81  E-value: 3.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  69 NSHAVdETIKGVAHVCKELEYQLLLnytgLDLSEEIIALETLSRSKVDGIILMATRITPQHLDVINKINVPVILVGQEH- 147
Cdd:cd06279   16 DPVAA-QFLRGVAEVCEEEGLGLLL----LPATDEGSAAAAVRNAAVDGFIVYGLSDDDPAVAALRRRGLPLVVVDGPAp 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 148 SGVNSIIHDDYLAGSYVGRQIVEANYKQV-----------YFFGVTEEDKA-----VGQQRKNGVLDILA---LNHIDVQ 208
Cdd:cd06279   91 PGIPSVGIDDRAAARAAARHLLDLGHRRIailslrldrgrERGPVSAERLAaatnsVARERLAGYRDALEeagLDLDDVP 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 209 VFKTSFQ-FMEAKNDVKLHLQSVHTADAIIGATDTIALAIHSYCSQpHHKLIPH--KIYGFGGDPITQIVTPQINTV-MY 284
Cdd:cd06279  171 VVEAPGNtEEAGRAAARALLALDPRPTAILCMSDVLALGALRAARE-RGLRVPEdlSVTGFDDIPEAAAADPGLTTVrQP 249

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 488392037 285 HYFK---AGQQALSQLHRLINHHdaqllTVIPVEL 316
Cdd:cd06279  250 AVEKgraAARLLLGLLPGAPPRP-----VILPTEL 279
PBP1_LacI-like cd19974
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 77-303 3.59e-04

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


Pssm-ID: 380629 [Multi-domain]  Cd Length: 270  Bit Score: 41.38  E-value: 3.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  77 IKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATrITPQHLDVINKINVPVILVGQEHSGVN--SII 154
Cdd:cd19974   21 YQGIEKELSELGYNLVLEIISDEDEEELNLPSIISEEKVDGIIILGE-ISKEYLEKLKELGIPVVLVDHYDEELNadSVL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 155 HDDYLAGSYVGRQIVEANYKQVYFFGVTE-----ED------KAVgqqRKNGVLDILALNHIDVQ--VFKTSFQFMEAkn 221
Cdd:cd19974  100 SDNYYGAYKLTSYLIEKGHKKIGFVGDINytssfMDrylgyrKAL---LEAGLPPEKEEWLLEDRddGYGLTEEIELP-- 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 222 dVKLHLqsvhtADAIIGATDTIALAIHSYCSQpHHKLIPH--KIYGFGGDPITQIVTPQINTVMYHYFKAGQQALSQLHR 299
Cdd:cd19974  175 -LKLML-----PTAFVCANDSIAIQLIKALKE-KGYRVPEdiSVVGFDNIELAELSTPPLTTVEVDKEAMGRRAVEQLLW 247


                 ....
gi 488392037 300 LINH 303
Cdd:cd19974  248 RIEN 251
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 60-270 3.81e-04

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


Pssm-ID: 380545 [Multi-domain]  Cd Length: 270  Bit Score: 41.49  E-value: 3.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  60 MIGAIIPRMNSHAVDETIKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIILMATR---ITPQhLDVINKI 136
Cdd:cd06322    1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDsggIVPA-IEAANEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 137 NVPVILVGQEHSGVNSIIH---DDYLAGSYVGRQIVEANYKQVYFFGVTEEDKAVGQ-QRKNGVLDILA----LNHIDVQ 208
Cdd:cd06322   80 GIPVFTVDVKADGAKVVTHvgtDNYAGGKLAGEYALKALLGGGGKIAIIDYPEVESVvLRVNGFKEAIKkypnIEIVAEQ 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488392037 209 VFKTSFQ-FMEAKNDVklhLQSVHTADAIIGATDTIALAIHSYCSQPhHKLIPHKIYGFGGDP 270
Cdd:cd06322  160 PGDGRREeALAATEDM---LQANPDLDGIFAIGDPAALGALTAIESA-GKEDKIKVIGFDGNP 218
PBP1_hexuronate_repressor-like cd06272
ligand-binding domain of DNA transcription repressor for the hexuronate utilization operon ...
 106-273 1.49e-03

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: 39.66  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 106 ALETLSRSKVDGIILMATRITPQHLDVINKINVPVILVGQEHSGVNSIIHDDYLAGSYVGRQIVEANYKQVYFFGVTEED 185
Cdd:cd06272   48 AKGLFSENRFDGVIVFGISDSDIEYLNKNKPKIPIVLYNRESPKYSTVNVDNEKAGRLAVLLLIQKGHKSIAYIGNPNSN 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 186 KAVgQQRKNGVLDILALNHI---DVQVFKTSFQFMEAKNDVKLHLQSVHTADAIIGATDTIALAIHSYCSQPHHKlIPHK 262
Cdd:cd06272  128 RNQ-TLRGKGFIETCEKHGIhlsDSIIDSRGLSIEGGDNAAKKLLKKKTLPKAIFCNSDDIALGVLRVLKENGIS-IPED 205

                        170
                 ....*....|.
gi 488392037 263 IYGFGGDPITQ 273
Cdd:cd06272  206 ISIVSYDNIPQ 216
PRK10339 PRK10339
DNA-binding transcriptional repressor EbgR; Provisional
 1-316 3.65e-03

DNA-binding transcriptional repressor EbgR; Provisional


Pssm-ID: 182389 [Multi-domain]  Cd Length: 327  Bit Score: 38.59  E-value: 3.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037   1 MKNIADIARLAGVSKSTVSRYLNNG---SVSTKTKEKLSKIIKEQDYQPNQFAQ-SLRARHTKMIGAIIPRMNSHAVDE- 75
Cdd:PRK10339   1 MATLKDIAIEAGVSLATVSRVLNDDptlNVKEETKHRILEIAEKLEYKTSSARKlQTGAVNQHHILAIYSYQQELEINDp 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  76 ---TIK-GVAHVCKELEYQLLLNYTgldlSEEIIALetlsrSKVDGiILMATRITPQHLDVINKINVPVILVG--QEHSG 149
Cdd:PRK10339  81 yylAIRhGIETQCEKLGIELTNCYE----HSGLPDI-----KNVTG-ILIVGKPTPALRAAASALTDNICFIDfhEPGSG 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 150 VNSIIHDDYLAGSYVGRQIVEANYKQVYFFGvTEEDKAVGQQRKNGVLDILALNHI--DVQVFKTSFQFMEAKNDVKLHL 227
Cdd:PRK10339 151 YDAVDIDLARISKEIIDFYINQGVNRIGFIG-GEDEPGKADIREVAFAEYGRLKQVvrEEDIWRGGFSSSSGYELAKQML 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037 228 QSVHTADAIIGATDTIAL----AIHSYCSQphhklIPHKI--YGFGGDPITQIVTPQINTVMYHYFKAGQQALSQL-HRL 300
Cdd:PRK10339 230 AREDYPKALFVASDSIAIgvlrAIHERGLN-----IPQDIslISVNDIPTARFTFPPLSTVRIHSEMMGSQGVNLLyEKA 304

                        330
                 ....*....|....*.
gi 488392037 301 INHHDAQLLTVIPVEL 316
Cdd:PRK10339 305 RDGRALPLLVFVPSKL 320
HTH_IclR pfam09339
IclR helix-turn-helix domain;
4-23 5.77e-03

IclR helix-turn-helix domain;


Pssm-ID: 430539 [Multi-domain]  Cd Length: 52  Bit Score: 34.31  E-value: 5.77e-03
                          10        20
                  ....*....|....*....|
gi 488392037    4 IADIARLAGVSKSTVSRYLN 23
Cdd:pfam09339  21 LTEIARRTGLPKSTAHRLLQ 40
HTH_XRE cd00093
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ...
 4-39 6.69e-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: 34.45  E-value: 6.69e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 488392037   4 IADIARLAGVSKSTVSRYLNNGS-VSTKTKEKLSKII 39
Cdd:cd00093   15 QEELAEKLGVSRSTISRIENGKRnPSLETLEKLAKAL 51
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
 63-186 7.78e-03

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


Pssm-ID: 380528 [Multi-domain]  Cd Length: 273  Bit Score: 37.28  E-value: 7.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488392037  63 AIIPRMNSHAVDET-IKGVAHVCKELEYQLLLNYTGLDLSEEIIALETLSRSKVDGIIL---MATRITPQHLDVINK-IN 137
Cdd:cd06305    3 AVVRNGTSGDWDQQaLQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIIshgDADALDPKLKKALDAgIP 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488392037 138 VPVILVGQEHSGVNSIIHDDYLAGSYVGRQIV-----EANYKQVYFFGVTEEDK 186
Cdd:cd06305   83 VVTFDTDSQVPGVNNITQDDYALGTLSLGQLVkdlngEGNIAVFNVFGVPPLDK 136
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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