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Conserved domains on  [gi|503384779|ref|WP_013619440|]
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substrate-binding domain-containing protein [Phocaeicola salanitronis]

Protein Classification

HTH_LacI and PBP1_sugar_binding domain-containing protein( domain architecture ID 11265738)

HTH_LacI and PBP1_sugar_binding domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
 68-343 4.21e-39

periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic sugar-binding domain of uncharacterized transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes.


:

Pssm-ID: 380530 [Multi-domain]  Cd Length: 275  Bit Score: 140.00  E-value: 4.21e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  68 FACLLPQhSEGEYWSYVENGMKQAIKDFSDFNISLALAYYDQYTLGDFLKSGKKLLEQSpDGLII----SPTIESEtesf 143
Cdd:cd06307    2 FGFLLPS-PENPFYELLRRAIEAAAAALRDRRVRLRIHFVDSLDPEALAAALRRLAAGC-DGVALvapdHPLVRAA---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 144 ISELRTHGIPYIFIDSNIPKLNPLCFYGQHAEQSGYFAARMMSMLMQGAT-ELVIFRqiseGRLGSNQQLHREEGFYTYM 222
Cdd:cd06307   76 IDELAARGIPVVTLVSDLPGSRRLAYVGIDNRAAGRTAAWLMGRFLGRRPgKVLVIL----GSHRFRGHEEREAGFRSVL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 223 KEHRPNLNMFTVNLYAKLPDEDETILDNFFKKYPGIQYGITFNSKAYAIGEYMERHGK-KDFHLMGYDLLQRNVDCLRKG 301
Cdd:cd06307  152 RERFPDLTVLEVLEGLDDDELAYELLRELLARHPDLVGIYNAGGGNEGIARALREAGRaRRVVFIGHELTPETRRLLRDG 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 503384779 302 SIDFIIAQQPTLQGYSSIESLCNHLILKKEIKACNYMPINLL 343
Cdd:cd06307  232 TIDAVIDQDPELQARRAIEVLLAHLGGKGPAPPQPPIPIEII 273
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
8-73 4.87e-21

helix_turn _helix lactose operon repressor;


:

Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 85.72  E-value: 4.87e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503384779     8 IRIKDIAQLAGVSVGTVDRVLHGRSGVSEKSREKVEKILKKLDYQPNMYASALASNKKYVFACLLP 73
Cdd:smart00354   1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVP 66
 
Name Accession Description Interval E-value
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
 68-343 4.21e-39

periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic sugar-binding domain of uncharacterized transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes.


Pssm-ID: 380530 [Multi-domain]  Cd Length: 275  Bit Score: 140.00  E-value: 4.21e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  68 FACLLPQhSEGEYWSYVENGMKQAIKDFSDFNISLALAYYDQYTLGDFLKSGKKLLEQSpDGLII----SPTIESEtesf 143
Cdd:cd06307    2 FGFLLPS-PENPFYELLRRAIEAAAAALRDRRVRLRIHFVDSLDPEALAAALRRLAAGC-DGVALvapdHPLVRAA---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 144 ISELRTHGIPYIFIDSNIPKLNPLCFYGQHAEQSGYFAARMMSMLMQGAT-ELVIFRqiseGRLGSNQQLHREEGFYTYM 222
Cdd:cd06307   76 IDELAARGIPVVTLVSDLPGSRRLAYVGIDNRAAGRTAAWLMGRFLGRRPgKVLVIL----GSHRFRGHEEREAGFRSVL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 223 KEHRPNLNMFTVNLYAKLPDEDETILDNFFKKYPGIQYGITFNSKAYAIGEYMERHGK-KDFHLMGYDLLQRNVDCLRKG 301
Cdd:cd06307  152 RERFPDLTVLEVLEGLDDDELAYELLRELLARHPDLVGIYNAGGGNEGIARALREAGRaRRVVFIGHELTPETRRLLRDG 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 503384779 302 SIDFIIAQQPTLQGYSSIESLCNHLILKKEIKACNYMPINLL 343
Cdd:cd06307  232 TIDAVIDQDPELQARRAIEVLLAHLGGKGPAPPQPPIPIEII 273
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 71-330 5.34e-37

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: 133.97  E-value: 5.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779   71 LLPQHSEGEYWSYVENGMKQAIKDFSDFNISLALAYYDQYTLGDFLKSgkkLLEQSPDGLIISPTIESETESFISELRTH 150
Cdd:pfam13407   3 VVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIED---AIAQGVDAIIVAPVDPTALAPVLKKAKDA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  151 GIPYIFIDSNIPKLNPLCFYGQHAEQSGYFAARMMSMLMQGATELVIFRqiseGRLGSNQQLHREEGFYTYMKEHRPNLN 230
Cdd:pfam13407  80 GIPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILS----GSPGDPNANERIDGFKKVLKEKYPGIK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  231 MFTVNLYAK-LPDEDETILDNFFKKYP-GIQYGITFNSK-AYAIGEYMERHGKKD-FHLMGYDLLQRNVDCLRKGSIDFI 306
Cdd:pfam13407 156 VVAEVEGTNwDPEKAQQQMEALLTAYPnPLDGIISPNDGmAGGAAQALEAAGLAGkVVVTGFDATPEALEAIKDGTIDAT 235

                         250       260
                  ....*....|....*....|....
gi 503384779  307 IAQQPTLQGYSSIESLCNHLILKK 330
Cdd:pfam13407 236 VLQDPYGQGYAAVELAAALLKGKK 259
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
7-225 4.53e-34

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 128.39  E-value: 4.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779   7 RIRIKDIAQLAGVSVGTVDRVLHGRSGVSEKSREKVEKILKKLDYQPNMYASALASNKKYVFACLLPqHSEGEYWSYVEN 86
Cdd:COG1609    3 RVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVP-DLSNPFFAELLR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  87 GMKQAIKDfSDFNISLALAYYDQYTLGDFLKSgkkLLEQSPDGLIISPTieSETESFISELRTHGIPYIFIDSNIPKLNP 166
Cdd:COG1609   82 GIEEAARE-RGYQLLLANSDEDPEREREALRL---LLSRRVDGLILAGS--RLDDARLERLAEAGIPVVLIDRPLPDPGV 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 503384779 167 LCFYGQHaEQSGYFAARMmsMLMQGATELVIFRqiseGRLGSNQQLHREEGFYTYMKEH 225
Cdd:COG1609  156 PSVGVDN-RAGARLATEH--LIELGHRRIAFIG----GPADSSSARERLAGYREALAEA 207
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
8-73 4.87e-21

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 85.72  E-value: 4.87e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503384779     8 IRIKDIAQLAGVSVGTVDRVLHGRSGVSEKSREKVEKILKKLDYQPNMYASALASNKKYVFACLLP 73
Cdd:smart00354   1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVP 66
HTH_LacI cd01392
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ...
 11-62 1.25e-20

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: 84.00  E-value: 1.25e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503384779  11 KDIAQLAGVSVGTVDRVLHGRSGVSEKSREKVEKILKKLDYQPNMYASALAS 62
Cdd:cd01392    1 KDIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
LacI pfam00356
Bacterial regulatory proteins, lacI family;
10-54 1.56e-17

Bacterial regulatory proteins, lacI family;


Pssm-ID: 306791 [Multi-domain]  Cd Length: 46  Bit Score: 75.37  E-value: 1.56e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 503384779   10 IKDIAQLAGVSVGTVDRVLHGRSGVSEKSREKVEKILKKLDYQPN 54
Cdd:pfam00356   2 IKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
PRK10014 PRK10014
DNA-binding transcriptional repressor MalI; Provisional
 7-156 2.02e-11

DNA-binding transcriptional repressor MalI; Provisional


Pssm-ID: 182193 [Multi-domain]  Cd Length: 342  Bit Score: 64.35  E-value: 2.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779   7 RIRIKDIAQLAGVSVGTVDRVLHGRSGVSEKSREKVEKILKKLDYQPNMYASALASNKKYVFACLLPQHSEgEYWSYVEN 86
Cdd:PRK10014   6 KITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSA-PFYAELTA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  87 GMKQAIKDfsdfnislalayyDQYTLgdFL----KSGKK-------LLEQSPDGLIISPTIESETEsFISELRTHGIPYI 155
Cdd:PRK10014  85 GLTEALEA-------------QGRMV--FLlqggKDGEQlaqrfstLLNQGVDGVVIAGAAGSSDD-LREMAEEKGIPVV 148


                 .
gi 503384779 156 F 156
Cdd:PRK10014 149 F 149
PRK10401 PRK10401
HTH-type transcriptional regulator GalS;
8-62 2.04e-11

HTH-type transcriptional regulator GalS;


Pssm-ID: 236681 [Multi-domain]  Cd Length: 346  Bit Score: 64.41  E-value: 2.04e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 503384779   8 IRIKDIAQLAGVSVGTVDRVLHGRSGVSEKSREKVEKILKKLDYQPNMYASALAS 62
Cdd:PRK10401   2 ITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALAT 56
aMBF1 COG1813
Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and ...
 6-47 9.92e-03

Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and HTH domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441418 [Multi-domain]  Cd Length: 70  Bit Score: 34.53  E-value: 9.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 503384779   6 ERIR---------IKDIAQLAGVSVGTVDRVLHGRSGVSEKSREKVEKILK 47
Cdd:COG1813   15 ERIRearearglsQEELAEKLGVSESTIRRIERGEATPSLDTLRKLEKALG 65
 
Name Accession Description Interval E-value
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
 68-343 4.21e-39

periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic sugar-binding domain of uncharacterized transport systems that share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily. The members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes.


Pssm-ID: 380530 [Multi-domain]  Cd Length: 275  Bit Score: 140.00  E-value: 4.21e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  68 FACLLPQhSEGEYWSYVENGMKQAIKDFSDFNISLALAYYDQYTLGDFLKSGKKLLEQSpDGLII----SPTIESEtesf 143
Cdd:cd06307    2 FGFLLPS-PENPFYELLRRAIEAAAAALRDRRVRLRIHFVDSLDPEALAAALRRLAAGC-DGVALvapdHPLVRAA---- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 144 ISELRTHGIPYIFIDSNIPKLNPLCFYGQHAEQSGYFAARMMSMLMQGAT-ELVIFRqiseGRLGSNQQLHREEGFYTYM 222
Cdd:cd06307   76 IDELAARGIPVVTLVSDLPGSRRLAYVGIDNRAAGRTAAWLMGRFLGRRPgKVLVIL----GSHRFRGHEEREAGFRSVL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 223 KEHRPNLNMFTVNLYAKLPDEDETILDNFFKKYPGIQYGITFNSKAYAIGEYMERHGK-KDFHLMGYDLLQRNVDCLRKG 301
Cdd:cd06307  152 RERFPDLTVLEVLEGLDDDELAYELLRELLARHPDLVGIYNAGGGNEGIARALREAGRaRRVVFIGHELTPETRRLLRDG 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 503384779 302 SIDFIIAQQPTLQGYSSIESLCNHLILKKEIKACNYMPINLL 343
Cdd:cd06307  232 TIDAVIDQDPELQARRAIEVLLAHLGGKGPAPPQPPIPIEII 273
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 71-330 5.34e-37

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: 133.97  E-value: 5.34e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779   71 LLPQHSEGEYWSYVENGMKQAIKDFSDFNISLALAYYDQYTLGDFLKSgkkLLEQSPDGLIISPTIESETESFISELRTH 150
Cdd:pfam13407   3 VVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIED---AIAQGVDAIIVAPVDPTALAPVLKKAKDA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  151 GIPYIFIDSNIPKLNPLCFYGQHAEQSGYFAARMMSMLMQGATELVIFRqiseGRLGSNQQLHREEGFYTYMKEHRPNLN 230
Cdd:pfam13407  80 GIPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILS----GSPGDPNANERIDGFKKVLKEKYPGIK 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  231 MFTVNLYAK-LPDEDETILDNFFKKYP-GIQYGITFNSK-AYAIGEYMERHGKKD-FHLMGYDLLQRNVDCLRKGSIDFI 306
Cdd:pfam13407 156 VVAEVEGTNwDPEKAQQQMEALLTAYPnPLDGIISPNDGmAGGAAQALEAAGLAGkVVVTGFDATPEALEAIKDGTIDAT 235

                         250       260
                  ....*....|....*....|....
gi 503384779  307 IAQQPTLQGYSSIESLCNHLILKK 330
Cdd:pfam13407 236 VLQDPYGQGYAAVELAAALLKGKK 259
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
7-225 4.53e-34

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 128.39  E-value: 4.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779   7 RIRIKDIAQLAGVSVGTVDRVLHGRSGVSEKSREKVEKILKKLDYQPNMYASALASNKKYVFACLLPqHSEGEYWSYVEN 86
Cdd:COG1609    3 RVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSLRTGRTRTIGVVVP-DLSNPFFAELLR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  87 GMKQAIKDfSDFNISLALAYYDQYTLGDFLKSgkkLLEQSPDGLIISPTieSETESFISELRTHGIPYIFIDSNIPKLNP 166
Cdd:COG1609   82 GIEEAARE-RGYQLLLANSDEDPEREREALRL---LLSRRVDGLILAGS--RLDDARLERLAEAGIPVVLIDRPLPDPGV 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 503384779 167 LCFYGQHaEQSGYFAARMmsMLMQGATELVIFRqiseGRLGSNQQLHREEGFYTYMKEH 225
Cdd:COG1609  156 PSVGVDN-RAGARLATEH--LIELGHRRIAFIG----GPADSSSARERLAGYREALAEA 207
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 57-348 7.43e-33

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: 124.27  E-value: 7.43e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  57 ASALASNKKYVFAcLLPQHSEGEYWSYVENGMKQAIKDFsDFNISLALAYYDQYTLGDFLKSgkkLLEQSPDGLIISPTI 136
Cdd:COG1879   25 EAAAAAAKGKTIG-FVVKTLGNPFFVAVRKGAEAAAKEL-GVELIVVDAEGDAAKQISQIED---LIAQGVDAIIVSPVD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 137 ESETESFISELRTHGIPYIFIDSNIPKLNPLCFYGQHAEQSGYFAARMMSMLMQGATELVIFrqisEGRLGSNQQLHREE 216
Cdd:COG1879  100 PDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGGKGKVAIL----TGSPGAPAANERTD 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 217 GFYTYMKEHrPNLNMFTVnLYAK-LPDEDETILDNFFKKYPGIQYGITFNSkAYAIG--EYMERHGKK-DFHLMGYDLLQ 292
Cdd:COG1879  176 GFKEALKEY-PGIKVVAE-QYADwDREKALEVMEDLLQAHPDIDGIFAAND-GMALGaaQALKAAGRKgDVKVVGFDGSP 252

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 503384779 293 RNVDCLRKGSIDFIIAQQPTLQGYSSIESLCNHLiLKKEIKACNYMPINLLSIENI 348
Cdd:COG1879  253 EALQAIKDGTIDATVAQDPYLQGYLAVDAALKLL-KGKEVPKEILTPPVLVTKENV 307
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
 71-333 1.76e-21

periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs; Periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and its close homologs from other bacteria. They are members of the type 1 periplasmic binding protein superfamily which consists of two domains connected by a three-stranded hinge. TmGBP is specific for glucose and its binding pocket is buried at the interface of the two domains. TmGBP also exhibits high thermostability and the highest structural similarity to E. coli glucose binding protein (ecGBP).


Pssm-ID: 380537 [Multi-domain]  Cd Length: 271  Bit Score: 92.65  E-value: 1.76e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  71 LLPQHSEGEYWSYVENGMKQAIKDFsdfNISLALAYYDQYTLGDFLKSGKKLLEQSPDGLIISPTIESETESFISELRTH 150
Cdd:cd06314    4 LVPKGLNNPFWDLAEAGAEKAAKEL---GVNVEFVGPQKSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 151 GIPYIFIDSNIPKLNPLCFYGQHAEQSGYFAARMMSMLMQGATELVIFRqiseGRLGSNQQLHREEGFYTYMKEHrpnln 230
Cdd:cd06314   81 GIPVITFDSDAPDSKRLAYIGTDNYEAGREAGELMKKALPGGGKVAIIT----GGLGADNLNERIQGFKDALKGS----- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 231 mFTVNLYAKLPDED-----ETILDNFFKKYPGIQ-YGITFNSKAYAIGEYM-ERHGKKDFHLMGYDLLQRNVDCLRKGSI 303
Cdd:cd06314  152 -PGIEIVDPLSDNDdiakaVQNVEDILKANPDLDaIFGVGAYNGPAIAAALkDAGKVGKVKIVGFDTLPETLQGIKDGVI 230

                        250       260       270
                 ....*....|....*....|....*....|
gi 503384779 304 DFIIAQQPTLQGYSSIESLCNHLILKKEIK 333
Cdd:cd06314  231 AATVGQRPYEMGYLSVKLLYKLLKGGKPVP 260
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
8-73 4.87e-21

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 85.72  E-value: 4.87e-21
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503384779     8 IRIKDIAQLAGVSVGTVDRVLHGRSGVSEKSREKVEKILKKLDYQPNMYASALASNKKYVFACLLP 73
Cdd:smart00354   1 ATIKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKTIGLIVP 66
HTH_LacI cd01392
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ...
 11-62 1.25e-20

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: 84.00  E-value: 1.25e-20
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503384779  11 KDIAQLAGVSVGTVDRVLHGRSGVSEKSREKVEKILKKLDYQPNMYASALAS 62
Cdd:cd01392    1 KDIARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLRT 52
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
 71-326 3.23e-20

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: 88.78  E-value: 3.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  71 LLPQHSEGEYWSYVENGMKQAIKDFsDFNISLALAYYDQYTLGDFLKSgkkLLEQSPDGLIISPTIESETESFISELRTH 150
Cdd:cd01536    4 VVVKDLTNPFWVAVKKGAEAAAKEL-GVELVVLDAQGDVAKQISQIED---LIAQGVDAIIIAPVDSEALVPAVKKANAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 151 GIPYIFIDSNIPKL-NPLCFYGQHAEQSGYFAARMMSMLMQGATELVIFrqisEGRLGSNQQLHREEGFYTYMKEHRPnl 229
Cdd:cd01536   80 GIPVVAVDTDIDGGgDVVAFVGTDNYEAGKLAGEYLAEALGGKGKVAIL----EGPPGSSTAIDRTKGFKEALKKYPD-- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 230 nmftVNLYAKLPDEDE-----TILDNFFKKYPGIQyGITFNSKAYAIG--EYMERHGK-KDFHLMGYDLLQRNVDCLRKG 301
Cdd:cd01536  154 ----IEIVAEQPANWDrakalTVTENLLQANPDID-AVFAANDDMALGaaEALKAAGRtGDIKIVGVDGTPEALKAIKDG 228

                        250       260
                 ....*....|....*....|....*
gi 503384779 302 SIDFIIAQQPTLQGYSSIESLCNHL 326
Cdd:cd01536  229 ELDATVAQDPYLQGYLAVEAAVKLL 253
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 79-326 1.03e-18

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


Pssm-ID: 380659 [Multi-domain]  Cd Length: 273  Bit Score: 84.59  E-value: 1.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  79 EYWSYVENGMKQAIKDFsdfNISLalaYYDQYTLGDFLKSGKKLLE----QSPDGLIISPTIESETESFISELRTHGIPY 154
Cdd:cd20004   12 DFWKSVKAGAEKAAQEL---GVEI---YWRGPSREDDVEAQIQIIEyfidQGVDGIVLAPLDRKALVAPVERARAQGIPV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 155 IFIDSNIPKLNPLCFYGQHAEQSGYFAARMMSMLMQGATELVIFRQISegrlGSNQQLHREEGFYTYMKEHRPNLNMfTV 234
Cdd:cd20004   86 VIIDSDLGGDAVISFVATDNYAAGRLAAKRMAKLLNGKGKVALLRLAK----GSASTTDRERGFLEALKKLAPGLKV-VD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 235 NLYAKlPDEDETILD--NFFKKYPGIQyGI-TFN-SKAYAIGEYMERHGK-KDFHLMGYDLLQRNVDCLRKGSIDFIIAQ 309
Cdd:cd20004  161 DQYAG-GTVGEARSSaeNLLNQYPDVD-GIfTPNeSTTIGALRALRRLGLaGKVKFIGFDASDLLLDALRAGEISALVVQ 238

                        250
                 ....*....|....*..
gi 503384779 310 QPTLQGYSSIESLCNHL 326
Cdd:cd20004  239 DPYRMGYLGVKTAVAAL 255
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 79-343 2.48e-18

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


Pssm-ID: 380533 [Multi-domain]  Cd Length: 272  Bit Score: 83.55  E-value: 2.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  79 EYWSYVENGMKQAIKDFSDFNISLALAyyDQYTLGDFLKSGKKLLEQSPDGLIISPTIESETESFISELRTHGIPYIFID 158
Cdd:cd06310   12 AFWRTVREGAEAAAKDLGVKIIFVGPE--SEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKDKGIPVIVID 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 159 SNIPKLNPLCFYGQHAEQSGYFAARMMSMLMQGATELVIFRqiseGRLGSNQQLHREEGFYTYMKEHrPNLNMFTVNLYA 238
Cdd:cd06310   90 SGIKGDAYLSYIATDNYAAGRLAAQKLAEALGGKGKVAVLS----LTAGNSTTDQREEGFKEYLKKH-PGGIKVLASQYA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 239 KL-PDEDETILDNFFKKYPGIQyGITFNSKAYAIG---EYMERHGKKDFHLMGYDLLQRNVDCLRKGSIDFIIAQQPTLQ 314
Cdd:cd06310  165 GSdYAKAANETEDLLGKYPDID-GIFATNEITALGaavAIKSRKLSGQIKIVGFDSQEELLDALKNGKIDALVVQNPYEI 243

                        250       260
                 ....*....|....*....|....*....
gi 503384779 315 GYSSIESLCNHLiLKKEIKACNYMPINLL 343
Cdd:cd06310  244 GYEGIKLALKLL-KGEEVPKNIDTGAELI 271
LacI pfam00356
Bacterial regulatory proteins, lacI family;
10-54 1.56e-17

Bacterial regulatory proteins, lacI family;


Pssm-ID: 306791 [Multi-domain]  Cd Length: 46  Bit Score: 75.37  E-value: 1.56e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 503384779   10 IKDIAQLAGVSVGTVDRVLHGRSGVSEKSREKVEKILKKLDYQPN 54
Cdd:pfam00356   2 IKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 78-321 1.01e-16

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


Pssm-ID: 380661 [Multi-domain]  Cd Length: 274  Bit Score: 79.18  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  78 GEYWSYVENGMKQAIKDF-SDFNISLALA---YYDQytlgdflksgKKLLEQS----PDGLIISPTIESETESFISELRT 149
Cdd:cd20006   13 SDFWQTVKSGAEAAAKEYgVDLEFLGPESeedIDGQ----------IELIEEAiaqkPDAIVLAASDYDRLVEAVERAKK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 150 HGIPYIFIDSNIPKLNPLCFYGQHAEQSGYFAARMMSMLMQGATELVI--FRQISegrlgSNQQLhREEGFYTYMKEHrP 227
Cdd:cd20006   83 AGIPVITIDSPVNSKKADSFVATDNYEAGKKAGEKLASLLGEKGKVAIvsFVKGS-----STAIE-REEGFKQALAEY-P 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 228 NLNMFTVNLYAKLPDEDETILDNFFKKYPGIQYGITFNSK-----AYAIGeymERHGKKDFHLMGYDLLQRNVDCLRKGS 302
Cdd:cd20006  156 NIKIVETEYCDSDEEKAYEITKELLSKYPDINGIVALNEQstlgaARALK---ELGLGGKVKVVGFDSSVEEIQLLEEGI 232

                        250
                 ....*....|....*....
gi 503384779 303 IDFIIAQQPTLQGYSSIES 321
Cdd:cd20006  233 IDALVVQNPFNMGYLSVQA 251
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
 65-337 9.81e-16

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: 76.16  E-value: 9.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  65 KYVFACllpqHSEGE-YWSYVENGMKQAIKDF---------SDFNISLALAYYDQytlgdflksgkkLLEQSPDGLIIsp 134
Cdd:cd19965    1 KFVFVT----HVTTNpFFQPVKKGMDDACELLgaecqftgpQTFDVAEQVSLLEA------------AIASGPDGIAT-- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 135 TIeSETESF---ISELRTHGIPYIFIDSNIPKL--NPLCFYGQHAEQSGYFAA-RMMSMLMQGATELVIFrqISEGrlGS 208
Cdd:cd19965   63 TI-VDPEAFdevIKRALDAGIPVVAFNVDAPGGenARLAFVGQDLYPAGYVLGkRIAEKFKPGGGHVLLG--ISTP--GQ 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 209 NQQLHREEGFYTYMKEHRPNlnmFTVNLYAKLPDEDETI--LDNFFKKYPGIQYGI-TFNSKAYAIGEYMERHGKKD-FH 284
Cdd:cd19965  138 SALEQRLDGIKQALKEYGRG---ITYDVIDTGTDLAEALsrIEAYYTAHPDIKAIFaTGAFDTAGAGQAIKDLGLKGkVL 214

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 503384779 285 LMGYDLLQRNVDCLRKGSIDFIIAQQPTLQGYSSIESLcnHLILKKEIKACNY 337
Cdd:cd19965  215 VGGFDLVPEVLQGIKAGYIDFTIDQQPYLQGFYPVMQL--FLYKKFGLSPFDI 265
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
 79-322 1.06e-13

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


Pssm-ID: 380624 [Multi-domain]  Cd Length: 278  Bit Score: 70.44  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  79 EYWSYVENGMKQAIKDFsdfNISLALAYYDQYTLGDFLKSGKKLLEQSPDGLIISPTIESETESFISELRTHGIPYIFID 158
Cdd:cd19969   12 PYWDDVKEGFEDAGAEL---GVKTEYTGPATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTFD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 159 SNIPKLNPLCFYGQHAEQSGYFAARMMSMLMQGATELVIFrqisEGRLGSNQQLhREEGFYTYMKEhrpNLNMFTVnlyA 238
Cdd:cd19969   89 SDAPESKRISYVGTDNYEAGYAAAEKLAELLGGKGKVAVL----TGPGQPNHEE-RVEGFKEAFAE---YPGIEVV---A 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 239 KLPDEDET-----ILDNFFKKYPGIQYGITFN-SKAYAIGEYMERHGKK-DFHLMGYDLLQRNVDCLRKGSIDFIIAQQP 311
Cdd:cd19969  158 VGDDNDDPekaaqNTSALLQAHPDLVGIFGVDaSGGVGAAQAVREAGKTgKVKIVAFDDDPETLDLIKDGVIDASIAQRP 237

                        250
                 ....*....|.
gi 503384779 312 TLQGYSSIESL 322
Cdd:cd19969  238 WMMGYWSLQFL 248
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
 80-324 1.35e-12

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


Pssm-ID: 380621 [Multi-domain]  Cd Length: 278  Bit Score: 67.35  E-value: 1.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  80 YWSYVENGMKQAIKDFS-DFNIslalayydQYTLGD---FLKSGKKLLEQSPDGLIIS--PTIESETEsFISELRTHGIP 153
Cdd:cd19966   14 FWTVVYNGAKDAAADLGvDLDY--------VFSSWDpekMVEQFKEAIAAKPDGIAIMghPGDGAYTP-LIEAAKKAGII 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 154 YIFIDSNIPKL----NPLCFYGQHAEQSGYFAARMM---SMLMQGATeLVIFRQISegrlGSNQQLHREEGFYTYMKEHR 226
Cdd:cd19966   85 VTSFNTDLPKLeygdCGLGYVGADLYAAGYTLAKELvkrGGLKTGDR-VFVPGLLP----GQPYRVLRTKGVIDALKEAG 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 227 PNLNMFTVNLYAKLPDEDETILDNFFKKYPGIQYGITFNSKAYA-IGEYMERHGKK--DFHLMGYDLLQRNVDCLRKGSI 303
Cdd:cd19966  160 IKVDYLEISLEPNKPAEGIPVMTGYLAANPDVKAIVGDGGGLTAnVAKYLKAAGKKpgEIPVAGFDLSPATVQAIKSGYV 239

                        250       260
                 ....*....|....*....|.
gi 503384779 304 DFIIAQQPTLQGYSSIESLCN 324
Cdd:cd19966  240 NATIDQQPYLQGYLPVLQIYL 260
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 80-322 3.96e-12

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


Pssm-ID: 380535 [Multi-domain]  Cd Length: 272  Bit Score: 65.72  E-value: 3.96e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  80 YWSYVENGMKQAIKDFsdfNISLALAYYDQYTLGDFLKsgkkLLEQS----PDGLIISPTIESETESFISELRTHGIPYI 155
Cdd:cd06312   14 FWSVVKKGAKDAAKDL---GVTVQYLGPQNNDIADQAR----LIEQAiaakPDGIIVTIPDPDALEPALKRAVAAGIPVI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 156 FIDSNI----PKLNPLCFYGQHAEQSGYFAARmmSMLMQGATELVIFRQIsEGRLGSNQqlhREEGFYTYMKEHRPNLNM 231
Cdd:cd06312   87 AINSGDdrskERLGALTYVGQDEYLAGQAAGE--RALEAGPKNALCVNHE-PGNPGLEA---RCKGFADAFKGAGILVEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 232 FTVNLYaklPDEDETILDNFFKKYPGIQYGITFNSK-AYAIGEYMERHG-KKDFHLMGYDLLQRNVDCLRKGSIDFIIAQ 309
Cdd:cd06312  161 LDVGGD---PTEAQEAIKAYLQADPDTDAVLTLGPVgADPALKAVKEAGlKGKVKIGTFDLSPETLEAIKDGKILFAIDQ 237

                        250
                 ....*....|...
gi 503384779 310 QPTLQGYSSIESL 322
Cdd:cd06312  238 QPYLQGYLAVVFL 250
PRK10014 PRK10014
DNA-binding transcriptional repressor MalI; Provisional
 7-156 2.02e-11

DNA-binding transcriptional repressor MalI; Provisional


Pssm-ID: 182193 [Multi-domain]  Cd Length: 342  Bit Score: 64.35  E-value: 2.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779   7 RIRIKDIAQLAGVSVGTVDRVLHGRSGVSEKSREKVEKILKKLDYQPNMYASALASNKKYVFACLLPQHSEgEYWSYVEN 86
Cdd:PRK10014   6 KITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALRGGQSGVIGLIVRDLSA-PFYAELTA 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  87 GMKQAIKDfsdfnislalayyDQYTLgdFL----KSGKK-------LLEQSPDGLIISPTIESETEsFISELRTHGIPYI 155
Cdd:PRK10014  85 GLTEALEA-------------QGRMV--FLlqggKDGEQlaqrfstLLNQGVDGVVIAGAAGSSDD-LREMAEEKGIPVV 148


                 .
gi 503384779 156 F 156
Cdd:PRK10014 149 F 149
PRK10401 PRK10401
HTH-type transcriptional regulator GalS;
8-62 2.04e-11

HTH-type transcriptional regulator GalS;


Pssm-ID: 236681 [Multi-domain]  Cd Length: 346  Bit Score: 64.41  E-value: 2.04e-11
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 503384779   8 IRIKDIAQLAGVSVGTVDRVLHGRSGVSEKSREKVEKILKKLDYQPNMYASALAS 62
Cdd:PRK10401   2 ITIRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALAT 56
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 71-326 3.42e-11

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


Pssm-ID: 380663 [Multi-domain]  Cd Length: 277  Bit Score: 63.02  E-value: 3.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  71 LLPQHSEGEYWSYVENGMKQAIKDFSDFNISLALAYY----DQYTLGDFLKSGKklleqsPDGLIISPT----IESETES 142
Cdd:cd20008    4 VIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLGPATEadiaGQVNLVENAISRK------PDAIVLAPNdtaaLVPAVEA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 143 FISelrthGIPYIFIDSNIPKLNPLCFYGQHAEQSGYFAARMMSMLMQ--GATELVIFRQISEGRLGSNQQlhREEGFYT 220
Cdd:cd20008   78 ADA-----GIPVVLVDSGANTDDYDAFLATDNVAAGALAADELAELLKasGGGKGKVAIISFQAGSQTLVD--REEGFRD 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 221 YMKEHRPNLNMFTVnLYAklpDEDET----ILDNFFKKYPGIQ--YGITfNSKAYAIGEYMERHGK-KDFHLMGYDLLQR 293
Cdd:cd20008  151 YIKEKYPDIEIVDV-QYS---DGDIAkalnQTTDLLTANPDLVgiFGAN-NPSAVGVAQALAEAGKaGKIVLVGFDSSPD 225

                        250       260       270
                 ....*....|....*....|....*....|...
gi 503384779 294 NVDCLRKGSIDFIIAQQPTLQGYSSIESLCNHL 326
Cdd:cd20008  226 EVALLKSGVIKALVVQDPYQMGYEGVKTAVKAL 258
lacI PRK09526
lac repressor; Reviewed
 11-61 1.42e-10

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 61.93  E-value: 1.42e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 503384779  11 KDIAQLAGVSVGTVDRVLHGRSGVSEKSREKVEKILKKLDYQPNMYASALA 61
Cdd:PRK09526   9 YDVARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQLA 59
PRK10727 PRK10727
HTH-type transcriptional regulator GalR;
10-61 1.65e-10

HTH-type transcriptional regulator GalR;


Pssm-ID: 182681 [Multi-domain]  Cd Length: 343  Bit Score: 61.70  E-value: 1.65e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503384779  10 IKDIAQLAGVSVGTVDRVLHGRSGVSEKSREKVEKILKKLDYQPNMYASALA 61
Cdd:PRK10727   4 IKDVARLAGVSVATVSRVINNSPKASEASRLAVHSAMESLSYHPNANARALA 55
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 122-326 1.09e-09

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


Pssm-ID: 380662 [Multi-domain]  Cd Length: 271  Bit Score: 58.40  E-value: 1.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 122 LLEQSPDGLIISPTiesETESFISELRT---HGIPYIFIDSNIPKLN-PLCFYGQHAEQSGYFAARMMSMLMQGATELVI 197
Cdd:cd20007   52 VIAKKPDALLIAPT---DPQALIAPLKRaadAGIKVVTVDTTLGDPSfVLSQIASDNVAGGALAAEALAELIGGKGKVLV 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 198 frqiSEGRLGSNQQLHREEGFYTYMKEHrPNLNMFTVNLYAKLPDEDETILDNFFKKYP---GIqYGITFNSKAYAIGEY 274
Cdd:cd20007  129 ----INSTPGVSTTDARVKGFAEEMKKY-PGIKVLGVQYSENDPAKAASIVAAALQANPdlaGI-FGTNTFSAEGAAAAL 202

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503384779 275 MERHGKKDFHLMGYDLLQRNVDCLRKGSIDFIIAQQPTLQGYSSIESLCNHL 326
Cdd:cd20007  203 RNAGKTGKVKVVGFDASPAQVEQLKAGTIDALIAQKPAEIGYLAVEQAVAAL 254
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
 120-342 7.26e-09

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


Pssm-ID: 380546 [Multi-domain]  Cd Length: 268  Bit Score: 56.15  E-value: 7.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 120 KKLLEQSPDGLIISPTIESETESFISELRTHGIPYIFIDSNIPKLNPLCFYGQHAEQSGYFAARMMSMLMQGATELVIFr 199
Cdd:cd06323   49 EDLIVRKVDALLINPTDSDAVSPAVEEANEAGIPVITVDRSVTGGKVVSHIASDNVAGGEMAAEYIAKKLGGKGKVVEL- 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 200 qisEGRLGSNQQLHREEGFYTYMKEHrPNLNMFtvnlyAKLP---DEDE--TILDNFFKKYPGIQyGITFNSKAYAIG-- 272
Cdd:cd06323  128 ---QGIPGTSAARERGKGFHNAIAKY-PKINVV-----ASQTadfDRTKglNVMENLLQAHPDID-AVFAHNDEMALGai 197

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 273 EYMERHGKKDFHLMGYDLLQRNVDCLRKGSIDFIIAQQPTLQGYSSIESLCNHLilkKEIKACNYMPINL 342
Cdd:cd06323  198 QALKAAGRKDVIVVGFDGTPDAVKAVKDGKLAATVAQQPEEMGAKAVETADKYL---KGEKVPKKIPVPL 264
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 74-322 9.22e-09

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


Pssm-ID: 380660 [Multi-domain]  Cd Length: 274  Bit Score: 55.71  E-value: 9.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  74 QHsegEYWSYVENGMKQAIKDFSD---FNISLALAYYDQYTlgDFLKSGkklLEQSPDGLIISPTIESETESFISELRTH 150
Cdd:cd20005   10 QH---QFWKAVKKGAEQAAKELGVkitFEGPDTESDVDKQI--EMLDNA---IAKKPDAIALAALDTNALLPQLEKAKEK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 151 GIPYIFIDSNIPKLNPLCFYGQHAEQSGYFAARMMSMLMQGATELVIFRQISEGRLGSNqqlhREEGFYTYMKEHRPnlN 230
Cdd:cd20005   82 GIPVVTFDSGVPSDLPLATVATDNYAAGALAADHLAELIGGKGKVAIVAHDATSETGID----RRDGFKDEIKEKYP--D 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 231 MFTVNLYAKLPDED--ETILDNFFKKYPGIQyGITFNSKAYAIG---EYMERHGKKDFHLMGYDLLQRNVDCLRKGSIDF 305
Cdd:cd20005  156 IKVVNVQYGVGDHAkaADIAKAILQANPDLK-GIYATNEGAAIGvanALKEMGKLGKIKVVGFDSGEAQIDAIKNGVIAG 234

                        250
                 ....*....|....*..
gi 503384779 306 IIAQQPTLQGYSSIESL 322
Cdd:cd20005  235 SVTQNPYGMGYKTVKAA 251
PRK10423 PRK10423
transcriptional repressor RbsR; Provisional
 10-65 4.90e-08

transcriptional repressor RbsR; Provisional


Pssm-ID: 182448 [Multi-domain]  Cd Length: 327  Bit Score: 53.93  E-value: 4.90e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 503384779  10 IKDIAQLAGVSVGTVDRVLHGRSGVSEKSREKVEKILKKLDYQPnmyaSALASNKK 65
Cdd:PRK10423   1 MKDVARLAGVSTSTVSHVINKDRFVSEAITAKVEAAIKELNYAP----SALARSLK 52
PRK11303 PRK11303
catabolite repressor/activator;
12-60 6.44e-08

catabolite repressor/activator;


Pssm-ID: 236897 [Multi-domain]  Cd Length: 328  Bit Score: 53.73  E-value: 6.44e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 503384779  12 DIAQLAGVSVGTVDRVLHGRSG---VSEKSREKVEKILKKLDYQPNMYASAL 60
Cdd:PRK11303   5 EIARLAGVSRTTASYVINGKAKqyrVSDKTVEKVMAVVREHNYHPNAVAAGL 56
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 79-348 1.10e-07

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


Pssm-ID: 380542 [Multi-domain]  Cd Length: 278  Bit Score: 52.36  E-value: 1.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  79 EYWSYVENGMKQAIKDfsdfnISLALAYYDQYTLGDFLKSG-KKLLEQSPDGLIISPTIESETESFISELRTHGIPYIFI 157
Cdd:cd06319   12 PFWQIMERGVQAAAEE-----LGYEFVTYDQKNSANEQVTNaNDLIAQGVDGIIISPTNSSAAPTVLDLANEAKIPVVIA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 158 DSNIPKLNPLCFYGQHAEQSGYFAARMMSMLMQGAT----ELVIFrQISEGRlgSNQQLhREEGFYTYMKE--------- 224
Cdd:cd06319   87 DIGTGGGDYVSYIISDNYDGGYQAGEYLAEALKENGwgggSVGII-AIPQSR--VNGQA-RTAGFEDALEEagveevalr 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 225 HRPNlnmFTVnlyaklpDEDETILDNFFKKYPGIQYGITFNSKAY-AIGEYMERHGKK-DFHLMGYDLLQRNVDCLRKGS 302
Cdd:cd06319  163 QTPN---STV-------EETYSAAQDLLAANPDIKGIFAQNDQMAqGALQAIEEAGRTgDILVVGFDGDPEALDLIKDGK 232

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 503384779 303 IDFIIAQQPTLQGYSSIESLCNHL----ILKKEIkacnYMPINLLSIENI 348
Cdd:cd06319  233 LDGTVAQQPFGMGARAVELAIQALngdnTVEKEI----YLPVLLVTSENV 278
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
 122-260 4.88e-07

periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic binding domain of two-component sensor kinase signaling systems, some of which are fused with a C-terminal histidine kinase A domain (HisK) and/or a signal receiver domain (REC). Members of this group share homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily and are predicted to be involved in sensing of environmental stimuli; their substrate specificities, however, are not known in detail.


Pssm-ID: 380531 [Multi-domain]  Cd Length: 268  Bit Score: 50.62  E-value: 4.88e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 122 LLEQSPDGLIISPTIESETESFISELRTHGIPYIFIDSNIPKLNPLCFYGQHAEQSGYFAARMMSMLMQGATELVIFrqi 201
Cdd:cd06308   52 LIAQGVDLLIVSPNEADALTPVVKKAYDAGIPVIVLDRKVSGDDYTAFIGADNVEIGRQAGEYIAELLNGKGNVVEI--- 128

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503384779 202 sEGRLGSNQQLHREEGFYTYMKEHrPNlnmftVNLYAKLP-----DEDETILDNFFKKYPGIQY 260
Cdd:cd06308  129 -QGLPGSSPAIDRHKGFLEAIAKY-PG-----IKIVASQDgdwlrDKAIKVMEDLLQAHPDIDA 185
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
 122-352 6.70e-07

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


Pssm-ID: 380536 [Multi-domain]  Cd Length: 277  Bit Score: 49.96  E-value: 6.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 122 LLEQSPDGLIISPtIESETES-FISELRTHGIPYIFIDSNIPKLNPLCFYGQHAEQSGYFAARMMSMLMQGATELVIFrq 200
Cdd:cd06313   51 LIAQGVDAIIVVP-VDADALApAVEKAKEAGIPLVGVNALIENEDLTAYVGSDDVVAGELEGQAVADRLGGKGNVVIL-- 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 201 isEGRLGSNQQLHREEGFYTYMKEHrPNlnmftVNLYAKLP-----DEDETILDNFFKKYPGIQYGITFNSKAYAIGEY- 274
Cdd:cd06313  128 --EGPIGQSAQIDRGKGIENVLKKY-PD-----IKVLAEQTanwsrDEAMSLMENWLQAYGDEIDGIIAQNDDMALGALq 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 275 -MERHGKKDFHLMGYDLLQRNVDCLRKGSIDFIIAQQPTLQGYSSIESLCNHLI---LKKEIkacnYMPINLLSIENIDF 350
Cdd:cd06313  200 aVKAAGRDDIPVVGIDGIEDALQAVKSGELIATVLQDAEAQGKGAVEVAVDAVKgegVEKKY----YIPFVLVTKDNVDD 275


                 ..
gi 503384779 351 YL 352
Cdd:cd06313  276 YL 277
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
 79-349 1.92e-06

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


Pssm-ID: 380543 [Multi-domain]  Cd Length: 283  Bit Score: 48.80  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  79 EYWSYVENGMKQAIKDFsDFNISLALAYYDQYTLGDfLKSGKKLLEQSPDGLIISPTIESETESFISELRTHGIPYIFID 158
Cdd:cd06320   12 PFWVAMKDGIEAEAKKL-GVKVDVQAAPSETDTQGQ-LNLLETMLNKGYDAILVSPISDTNLIPPIEKANKKGIPVINLD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 159 SNI-------PKLNPLCFYGQHAEQSGYFAAR-MMSMLMQGATELVIfrqisEGRLGSNQQLHREEGFYTYMKEHrPNLN 230
Cdd:cd06320   90 DAVdadalkkAGGKVTSFIGTDNVAAGALAAEyIAEKLPGGGKVAII-----EGLPGNAAAEARTKGFKETFKKA-PGLK 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 231 mftvnLYAKLP-DED-ETILD---NFFKKYPGIQyGITFNSKAYAIG--EYMERHGKK-DFHLMGYDLLQRNVDCLRKGS 302
Cdd:cd06320  164 -----LVASQPaDWDrTKALDaatAILQAHPDLK-GIYAANDTMALGavEAVKAAGKTgKVLVVGTDGIPEAKKSIKAGE 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 503384779 303 IDFIIAQQPTLQGYSSIEsLCNHLILKKEIKACNYMPINLLSIENID 349
Cdd:cd06320  238 LTATVAQYPYLEGAMAVE-AALRLLQGQKVPAVVATPQALITKDNVD 283
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
 122-352 5.48e-06

periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; Periplasmic binding domain of ABC-type YtfQ-like transport systems. The YtfQ protein from Escherichia coli is up-regulated under glucose-limited conditions and shares homology with a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their ligand specificity is not determined experimentally.


Pssm-ID: 380532 [Multi-domain]  Cd Length: 285  Bit Score: 47.21  E-value: 5.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 122 LLEQSPDGLIISPTIESETESFISELRTHGIPYIFIDSNI---PKLNPLCFYGQHAEQSGYFAARMMS-MLMQGATELVI 197
Cdd:cd06309   51 LIAQGVDAILISPIDATGWDPVLKEAKDAGIPVILVDRTIdgeDGSLYVTFIGSDFVEEGRRAAEWLVkNYKGGKGNVVE 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 198 FrqisEGRLGSNQQLHREEGFYTYMKEHrPNLNMFTVNLYAKLPDEDETILDNFFKKYPG-IQyGITFNSKAYAIG--EY 274
Cdd:cd06309  131 L----QGTAGSSVAIDRSKGFREVIKKH-PNIKIVASQSGNFTREKGQKVMENLLQAGPGdID-VIYAHNDDMALGaiQA 204

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 275 MERHGK---KDFHLMGYDLLQRNVDCLRKGSIDFIIAQQPtLQGYSSIESLcNHLILKKEIKACNYMPINLLSIENIDFY 351
Cdd:cd06309  205 LKEAGLkpgKDVLVVGIDGQKDALEAIKAGELNATVECNP-LFGPTAFDTI-AKLLAGEKVPKLIIVEERLFDKDNAAEE 282


                 .
gi 503384779 352 L 352
Cdd:cd06309  283 L 283
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
 128-289 1.02e-05

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: 46.36  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 128 DGLIISPTIESetesfISELRTHGIPYIFIDSNIPKLNPlCFYGQHaEQSGYFAARMMsmLMQGATELVIFRqiseGRLG 207
Cdd:cd06291   57 DGIILGSHSLD-----IEEYKKLNIPIVSIDRYLSEGIP-SVSSDN-YQGGRLAAEHL--IEKGCKKILHIG----GPSN 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 208 SNQQLHREEGFYTYMKEHRPNLNMFTVNLYAKLPDEDETILDNFFKKYPGIQyGITFNSKAYAIG--EYMERHGKK---D 282
Cdd:cd06291  124 NSPANERYRGFEDALKEAGIEYEIIEIDENDFSEEDAYELAKELLEKYPDID-GIFASNDLLAIGvlKALQKLGIRvpeD 202


                 ....*..
gi 503384779 283 FHLMGYD 289
Cdd:cd06291  203 VQIIGFD 209
PRK10703 PRK10703
HTH-type transcriptional repressor PurR;
10-63 1.35e-05

HTH-type transcriptional repressor PurR;


Pssm-ID: 236739 [Multi-domain]  Cd Length: 341  Bit Score: 46.64  E-value: 1.35e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 503384779  10 IKDIAQLAGVSVGTVDRVLHGRSGVSEKSREKVEKILKKLDYQPNMYASALASN 63
Cdd:PRK10703   4 IKDVAKRAGVSTTTVSHVINKTRFVAEETRNAVWAAIKELHYSPSAVARSLKVN 57
PRK14987 PRK14987
HTH-type transcriptional regulator GntR;
5-165 2.11e-05

HTH-type transcriptional regulator GntR;


Pssm-ID: 184949 [Multi-domain]  Cd Length: 331  Bit Score: 45.79  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779   5 EERIRIKDIAQLAGVSVGTVDRVLHGRSGVSEKSREKVEKILKKLDYQPNMYASALASNKKYVFACLLPQHSEgEYWSYV 84
Cdd:PRK14987   3 KKRPVLQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRAIGVLLPSLTN-QVFAEV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  85 ENGMkQAIKDFSDFNISLALAYYDQYTLGDFLKSgkkLLEQSPDGLIIspTIESETESFISELRTHGIPYI-FIDSNIPK 163
Cdd:PRK14987  82 LRGI-ESVTDAHGYQTMLAHYGYKPEMEQERLES---MLSWNIDGLIL--TERTHTPRTLKMIEVAGIPVVeLMDSQSPC 155


                 ..
gi 503384779 164 LN 165
Cdd:PRK14987 156 LD 157
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
 98-169 2.52e-05

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: 45.24  E-value: 2.52e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503384779  98 FNISLALAYYDQYTLGDFLKSgkkLLEQSPDGLIISPT---IESETESFISELRTHGIPYIFIDSNIPKLNPLCF 169
Cdd:cd01541   30 YSLLLALTNNDVEKEREILES---LLDQNVDGLIIEPTksaLPNPNLDLYEELQKKGIPVVFINSYYPELDAPSV 101
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 73-260 1.00e-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 consists of two domains connected by a three-stranded hinge. The substrate specificity of this group is not known, but it is predicted to be involved in the transport of sugar-containing molecules and chemotaxis.


Pssm-ID: 380547 [Multi-domain]  Cd Length: 317  Bit Score: 43.75  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  73 PQHSEGEYWSYVENGMKQAIKdfsDFNISLAL--AYYDQYTlgdFLKSGKKLLEQS--PDGLIISPtIESETESFISELR 148
Cdd:cd06324    7 PGKEDEPFWQNVTRFMQAAAK---DLGIELEVlyANRNRFK---MLELAEELLARPpkPDYLILVN-EKGVAPELLELAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 149 THGIPYIFIDSNIPK--LNPLCFYGQH-----------AEQSGYfaaRMMSMLMQGAtelvifRQISE----------GR 205
Cdd:cd06324   80 QAKIPVFLINNDLTDeeRALLGKPREKfkywlgsivpdNEQAGY---LLAKALIKAA------RKKSDdgkirvlaisGD 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 503384779 206 LGSNQQLHREEGFYTYMKEHrPNLNMFTVnLYAK-LPDEDETILDNFFKKYPGIQY 260
Cdd:cd06324  151 KSTPASILREQGLRDALAEH-PDVTLLQI-VYANwSEDEAYQKTEKLLQRYPDIDI 204
PBP1_ABC_sugar_binding-like cd06316
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 75-330 1.10e-04

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


Pssm-ID: 380539 [Multi-domain]  Cd Length: 294  Bit Score: 43.38  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  75 HSEGEYWSY-VENGMKQAikdFSDFNISL---ALAYYDQYTLGDFLKSgkkLLEQSPDGLIISPTIESETESFISELRTH 150
Cdd:cd06316    7 HTTGSDWSRlQVAGIKDT---FEELGIEVvavTDANFDPAKQITDLET---LIALKPDIIISIPVDPVATAAAYKKVADA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 151 GIPYIFIDsNIPKLnpLCFYGQHA-------EQSGYFAARMMSMLMQGATEL-VIFRQISegRLGSNQqlhREEGFYTYM 222
Cdd:cd06316   81 GIKLVFMD-NVPDG--LEAGKDYVsvvssdnRGNGQIAAELLAEAIGGKGKVgIIYHDAD--FYATNQ---RDKAFKDTL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 223 KEHRPNLNMFTVNLYAKlPDEDETILDNFFKKYPGIQyGI--TFNSKAYAIGEYMERHGKKDFHLMGYDLLQRN-VDCLR 299
Cdd:cd06316  153 KEKYPDIKIVAEQGFAD-PNDAEEVASAMLTANPDID-GIyvSWDTPALGVISALRAAGRSDIKITTVDLGTEIaLDMAK 230

                        250       260       270
                 ....*....|....*....|....*....|.
gi 503384779 300 KGSIDFIIAQQPTLQGYSSIESLCNHLILKK 330
Cdd:cd06316  231 GGNVKGIGAQRPYDQGVAEALAAALALLGKE 261
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 122-339 1.48e-04

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


Pssm-ID: 380627 [Multi-domain]  Cd Length: 269  Bit Score: 42.81  E-value: 1.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 122 LLEQSPDGLIISPTIESETESFISELRTHGIPYIFIDSNIPKLNPLCFYGQHAEQSGYFAARMMSMLMQGATELVIFrqi 201
Cdd:cd19972   51 LITQNIDALIYIPAGATAAAVPVKAARAAGIPVIAVDRNPEDAPGDTFIATDSVAAAKELGEWVIKQTGGKGEIAIL--- 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 202 sEGRLGSNQQLHREEGFYTYMKEHrPNLNMFtvnlyAKLP---DEDE--TILDNFFKKYPGIQygITF-NSKAYAIGEYM 275
Cdd:cd19972  128 -HGQLGTTPEVDRTKGFQEALAEA-PGIKVV-----AEQTadwDQDEgfKVAQDMLQANPNIT--VFFgQSDAMALGAAQ 198

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503384779 276 ---ERHGKKDFHLMGYDLLQRNVDCLRKGSIDFIIAQQPTLQGYSSIESLCNhLILKKEIKACNYMP 339
Cdd:cd19972  199 avkVAGLDHKIWVVGFDGDVAGLKAVKDGVLDATMTQQTQKMGRLAVDSAID-LLNGKAVPKEQLQD 264
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
 120-225 2.27e-04

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: 42.12  E-value: 2.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 120 KKLLEQSPDGLIISPTieSETESFISELRTHGIPYIFIDSNIPKLNPLCFYGQHaEQSGYFAARMmsMLMQGATELVIfr 199
Cdd:cd06267   49 RLLLSRRVDGIILAPS--SLDDELLEELLAAGIPVVLIDRRLDGLGVDSVVVDN-YAGAYLATEH--LIELGHRRIAF-- 121

                         90       100
                 ....*....|....*....|....*.
gi 503384779 200 qISeGRLGSNQQLHREEGFYTYMKEH 225
Cdd:cd06267  122 -IG-GPLDLSTSRERLEGYRDALAEA 145
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
 120-225 3.33e-04

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: 41.78  E-value: 3.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 120 KKLLEQSPDGLIISPTIESETESFiSELRTHGIPYIFIDSNIPkLNPLCFYGQHAEQSGYFAARmmSMLMQGATELVIFr 199
Cdd:cd06289   49 RRMLEQGVDGLILSPAAGTTAELL-RRLKAWGIPVVLALRDVP-GSDLDYVGIDNRLGAQLATE--HLIALGHRRIAFL- 123

                         90       100
                 ....*....|....*....|....*.
gi 503384779 200 qisEGRLGSNQQLHREEGFYTYMKEH 225
Cdd:cd06289  124 ---GGLSDSSTRRERLAGFRAALAEA 146
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 120-320 9.60e-04

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


Pssm-ID: 380625 [Multi-domain]  Cd Length: 275  Bit Score: 40.31  E-value: 9.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 120 KKLLEQSPDGLIISPTIESETESFISELRTHGIPYIFIDSNI------PKLNPLCFYGQHAEQSGYFAARMMSMLMQGAT 193
Cdd:cd19970   52 ENLIAQKVDAIVIAPADSKALVPVLKKAVDAGIAVINIDNRLdadalkEGGINVPFVGPDNRQGAYLAGDYLAKKLGKGG 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 194 ELVIFrqisEGRLGSNQQLHREEGFYTYMKEHrpNLNMFTVNLYAKLPDEDETILDNFFKKYPGIQyGITFNSKAYAIG- 272
Cdd:cd19970  132 KVAII----EGIPGADNAQQRKAGFLKAFEEA--GMKIVASQSANWEIDEANTVAANLLTAHPDIR-GILCANDNMALGa 204

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 503384779 273 -EYMERHGKKD-FHLMGYDLLQRNVDCLRKGSIDFIIAQQPTLQGYSSIE 320
Cdd:cd19970  205 iKAVDAAGKAGkVLVVGFDNIPAVRPLLKDGKMLATIDQHPAKQAVYGIE 254
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
 122-340 2.02e-03

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


Pssm-ID: 380623 [Multi-domain]  Cd Length: 271  Bit Score: 39.29  E-value: 2.02e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 122 LLEQSPDGLIISPTIESETESFISELRTHGIPYIFIDSNIPKLNPLCFYGQHAEQSGYFAARMMSMLMQGATELVIFrqi 201
Cdd:cd19968   51 AIAQGVDGIIVSPIDVKALVPAIEAAIKAGIPVVTVDRRAEGAAPVPHVGADNVAGGREVAKFVVDKLPNGAKVIEL--- 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 202 sEGRLGSNQQLHREEGFYTYMKEHrPNLNMFTVNLYAKLPDEDETILDNFFKKYPGIQYGITFNSKAYAIG--EYMERHG 279
Cdd:cd19968  128 -TGTPGSSPAIDRTKGFHEELAAG-PKIKVVFEQTGNFERDEGLTVMENILTSLPGPPDAIICANDDMALGaiEAMRAAG 205

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503384779 280 --KKDFHLMGYDLLQRNVDCLRKGSIDFIIAQQPTLQGYSSIESLCNHLILKKEIKACNYMPI 340
Cdd:cd19968  206 ldLKKVKVIGFDAVPDALQAIKDGELYATVEQPPGGQARTALRILVDYLKDKKAPKKVNLKPK 268
PRK10339 PRK10339
DNA-binding transcriptional repressor EbgR; Provisional
 10-69 3.39e-03

DNA-binding transcriptional repressor EbgR; Provisional


Pssm-ID: 182389 [Multi-domain]  Cd Length: 327  Bit Score: 38.97  E-value: 3.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503384779  10 IKDIAQLAGVSVGTVDRVLHGRS--GVSEKSREKVEKILKKLDY--QPNMYASALASNKKYVFA 69
Cdd:PRK10339   4 LKDIAIEAGVSLATVSRVLNDDPtlNVKEETKHRILEIAEKLEYktSSARKLQTGAVNQHHILA 67
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
 122-165 3.78e-03

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: 38.66  E-value: 3.78e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 503384779 122 LLEQSPDGLIISPTieSETESFISELRTHGIPYIFIDSNIPKLN 165
Cdd:cd19977   51 LRAKQVDGIIIAPT--GGNEDLIEKLVKSGIPVVFVDRYIPGLD 92
PBP1_GGBP cd01539
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ...
 80-185 4.64e-03

periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species; Periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and active transport of, glucose and galactose in various bacterial species. GGBP is a member of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic GGBP is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380481 [Multi-domain]  Cd Length: 302  Bit Score: 38.33  E-value: 4.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  80 YWSYVENGMKQAIKDFSDFNISLALAYYDQYTLGDFLKSgkkLLEQSPDGLIISPTIESETESFISELRTHGIPYIFI-- 157
Cdd:cd01539   14 FISSVRKALEKAAKAGGKIELEIYDAQNDQSTQNDQIDT---MIAKGVDLLVVNLVDRTAAQTIIDKAKAANIPVIFFnr 90

                         90       100       110
                 ....*....|....*....|....*....|.
gi 503384779 158 ---DSNIPKLNPLCFYGQHAEQSGYFAARMM 185
Cdd:cd01539   91 epsREDLKSYDKAYYVGTDAEESGIMQGEII 121
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
 79-320 6.62e-03

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


Pssm-ID: 380524 [Multi-domain]  Cd Length: 272  Bit Score: 37.98  E-value: 6.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779  79 EYWSYVENGMKQAIKDFSDFNISLALAYYDQYTLgdfLKSGKKLLEQSPDGLIISPTIESETESFISELRTHGIPYIFID 158
Cdd:cd06301   13 EFLTYLRDAIEAYAKEYPGVKLVIVDAQSDAAKQ---LSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADAGIPLVYVN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 159 SNIPKL-NPLCFYGQHAEQSGYFAARMMSMLMQGATELVIFRqiseGRLGSNQQLHREEGFYTYMKEHrPNLNMFTVNLY 237
Cdd:cd06301   90 REPDSKpKGVAFVGSDDIESGELQMEYLAKLLGGKGNIAILD----GVLGHEAQILRTEGNKDVLAKY-PGMKIVAEQTA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503384779 238 AKLPDEDETILDNFFKKYPGIQyGITFNSKAYAIG--EYMERHGKKD-FHLMGYDLLQRNVDCLRKGSIDFIIAQQPTLQ 314
Cdd:cd06301  165 NWSREKAMDIVENWLQSGDKID-AIVANNDEMAIGaiLALEAAGKKDdILVAGIDATPDALKAMKAGRLDATVFQDAAGQ 243


                 ....*.
gi 503384779 315 GYSSIE 320
Cdd:cd06301  244 GETAVD 249
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 122-183 7.39e-03

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


Pssm-ID: 380508 [Multi-domain]  Cd Length: 269  Bit Score: 37.59  E-value: 7.39e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503384779 122 LLEQSPDGLIISPTieSETESFISELRTHGIPYIFIDSNIPKLnPLCFYGQHAEQSGYFAAR 183
Cdd:cd06285   51 LLSRRVDGLIITPA--RDDAPDLQELAARGVPVVLVDRRIGDT-ALPSVTVDNELGGRLATR 109
aMBF1 COG1813
Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and ...
 6-47 9.92e-03

Archaeal ribosome-binding protein aMBF1, putative translation factor, contains Zn-ribbon and HTH domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 441418 [Multi-domain]  Cd Length: 70  Bit Score: 34.53  E-value: 9.92e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 503384779   6 ERIR---------IKDIAQLAGVSVGTVDRVLHGRSGVSEKSREKVEKILK 47
Cdd:COG1813   15 ERIRearearglsQEELAEKLGVSESTIRRIERGEATPSLDTLRKLEKALG 65
 
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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