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Conserved domains on  [gi|1401077077|gb|PYU41715|]
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sugar ABC transporter substrate-binding protein [Acidobacteria bacterium]

Protein Classification

HTH_LacI and PBP1_ABC_sugar_binding_like domain-containing protein( domain architecture ID 11545747)

HTH_LacI and PBP1_ABC_sugar_binding_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 67-323 9.15e-52

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: 172.88  E-value: 9.15e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  67 VGVCIPREIHFFYDQLWSGVLDEARRVAQLGLQFLNrpvhalGEGDTAVFKE----LVQCGVDGIILTAGNPKALTPLID 142
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGP------AEADAAEQVAqiedAIAQGVDAIIVAPVDPTALAPVLK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 143 EAEANGIRVVCVSTDAPESRRSSIVCVEPSLNGSLAGELMGKLVPRASKVAVVAGMLTAEDHRKKTDGFSEAFPRHCTGG 222
Cdd:pfam13407  75 KAKDAGIPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLKEKYPGI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 223 KIAGIIEG-HEDEDESFQKTFDLLRRVPN-LAGLY-VNTVNCLPVCRALGARGLAGKVKLITTDLFAEMSPYFQKGTITA 299
Cdd:pfam13407 155 KVVAEVEGtNWDPEKAQQQMEALLTAYPNpLDGIIsPNDGMAGGAAQALEAAGLAGKVVVTGFDATPEALEAIKDGTIDA 234

                         250       260
                  ....*....|....*....|....
gi 1401077077 300 SIYQQPHRQGQIAVRVMADNLTNK 323
Cdd:pfam13407 235 TVLQDPYGQGYAAVELAAALLKGK 258
HTH_LacI cd01392
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ...
 11-59 7.47e-18

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


:

Pssm-ID: 143331 [Multi-domain]  Cd Length: 52  Bit Score: 76.29  E-value: 7.47e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1401077077  11 IAHMANVSIGTVDRALHGRGGIKESTRQRILQVARQIGYTPNLAARALS 59
Cdd:cd01392     3 IARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLR 51
 
Name Accession Description Interval E-value
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 67-323 9.15e-52

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: 172.88  E-value: 9.15e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  67 VGVCIPREIHFFYDQLWSGVLDEARRVAQLGLQFLNrpvhalGEGDTAVFKE----LVQCGVDGIILTAGNPKALTPLID 142
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGP------AEADAAEQVAqiedAIAQGVDAIIVAPVDPTALAPVLK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 143 EAEANGIRVVCVSTDAPESRRSSIVCVEPSLNGSLAGELMGKLVPRASKVAVVAGMLTAEDHRKKTDGFSEAFPRHCTGG 222
Cdd:pfam13407  75 KAKDAGIPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLKEKYPGI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 223 KIAGIIEG-HEDEDESFQKTFDLLRRVPN-LAGLY-VNTVNCLPVCRALGARGLAGKVKLITTDLFAEMSPYFQKGTITA 299
Cdd:pfam13407 155 KVVAEVEGtNWDPEKAQQQMEALLTAYPNpLDGIIsPNDGMAGGAAQALEAAGLAGKVVVTGFDATPEALEAIKDGTIDA 234

                         250       260
                  ....*....|....*....|....
gi 1401077077 300 SIYQQPHRQGQIAVRVMADNLTNK 323
Cdd:pfam13407 235 TVLQDPYGQGYAAVELAAALLKGK 258
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 54-342 2.32e-44

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: 155.08  E-value: 2.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  54 AARALSVAKASARVGVCIPREIHFFYDQLWSGVLDEArrvAQLGLQFLNRPvhalGEGDTA----VFKELVQCGVDGIIL 129
Cdd:COG1879    23 AAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAA---KELGVELIVVD----AEGDAAkqisQIEDLIAQGVDAIIV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 130 TAGNPKALTPLIDEAEANGIRVVCVSTDAPESRRSSIVCVEPSLNGSLAGELMGKLVPRASKVAVVAGMLTAEDHRKKTD 209
Cdd:COG1879    96 SPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGGKGKVAILTGSPGAPAANERTD 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 210 GFSEAFPRHcTGGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLY-VNTVNCLPVCRALGARGLAGKVKLITTDLFAEM 288
Cdd:COG1879   176 GFKEALKEY-PGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFaANDGMALGAAQALKAAGRKGDVKVVGFDGSPEA 254

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1401077077 289 SPYFQKGTITASIYQQPHRQGQIAVRVMADNLTNKIhFPPAVHLSPGVVMSSNL 342
Cdd:COG1879   255 LQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKE-VPKEILTPPVLVTKENV 307
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
 66-339 1.82e-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: 141.16  E-value: 1.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  66 RVGVCIPREIHFFYDQLWSGVLDEARRVAQLGLQFLNRPVHALGEGDTAVFKELVQCGVDGIILTAGNPKALTPLIDEAE 145
Cdd:cd06307     1 RFGFLLPSPENPFYELLRRAIEAAAAALRDRRVRLRIHFVDSLDPEALAAALRRLAAGCDGVALVAPDHPLVRAAIDELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 146 ANGIRVVCVSTDAPESRRSSIVCVEPSLNGSLAGELMGK-LVPRASKVAVVAGMLTAEDHRKKTDGFSEAFPRHCTGGKI 224
Cdd:cd06307    81 ARGIPVVTLVSDLPGSRRLAYVGIDNRAAGRTAAWLMGRfLGRRPGKVLVILGSHRFRGHEEREAGFRSVLRERFPDLTV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 225 AGIIEGHEDEDESFQKTFDLLRRVPNLAGLYVNTVNCLPVCRALGARGLAGKVKLITTDLFAEMSPYFQKGTITASIYQQ 304
Cdd:cd06307   161 LEVLEGLDDDELAYELLRELLARHPDLVGIYNAGGGNEGIARALREAGRARRVVFIGHELTPETRRLLRDGTIDAVIDQD 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1401077077 305 PHRQGQIAVRVMADNLTNKIHFPPAVHLSPGVVMS 339
Cdd:cd06307   241 PELQARRAIEVLLAHLGGKGPAPPQPPIPIEIITR 275
HTH_LacI cd01392
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ...
 11-59 7.47e-18

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


Pssm-ID: 143331 [Multi-domain]  Cd Length: 52  Bit Score: 76.29  E-value: 7.47e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1401077077  11 IAHMANVSIGTVDRALHGRGGIKESTRQRILQVARQIGYTPNLAARALS 59
Cdd:cd01392     3 IARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLR 51
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
8-73 6.60e-15

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 68.77  E-value: 6.60e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1401077077    8 IHLIAHMANVSIGTVDRALHGRGGIKESTRQRILQVARQIGYTPNLAARALSVAKASArVGVCIPR 73
Cdd:smart00354   3 IKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKT-IGLIVPD 67
PRK10014 PRK10014
DNA-binding transcriptional repressor MalI; Provisional
 1-155 9.10e-14

DNA-binding transcriptional repressor MalI; Provisional


Pssm-ID: 182193 [Multi-domain]  Cd Length: 342  Bit Score: 71.28  E-value: 9.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077   1 MTKPRSGIHLIAHMANVSIGTVDRALHGRGGIKESTRQRILQVARQIGYTPNLAARALSvAKASARVGVcIPREIHF-FY 79
Cdd:PRK10014    2 ATAKKITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALR-GGQSGVIGL-IVRDLSApFY 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1401077077  80 DQLWSGvLDEARRvAQLGLQFLNRPVHAlGEGDTAVFKELVQCGVDGIILtAGNPKALTPLIDEAEANGIRVVCVS 155
Cdd:PRK10014   80 AELTAG-LTEALE-AQGRMVFLLQGGKD-GEQLAQRFSTLLNQGVDGVVI-AGAAGSSDDLREMAEEKGIPVVFAS 151
LacI pfam00356
Bacterial regulatory proteins, lacI family;
8-52 4.85e-10

Bacterial regulatory proteins, lacI family;


Pssm-ID: 306791 [Multi-domain]  Cd Length: 46  Bit Score: 54.57  E-value: 4.85e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1401077077   8 IHLIAHMANVSIGTVDRALHGRGGIKESTRQRILQVARQIGYTPN 52
Cdd:pfam00356   2 IKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
PRK10401 PRK10401
HTH-type transcriptional regulator GalS;
8-71 5.57e-05

HTH-type transcriptional regulator GalS;


Pssm-ID: 236681 [Multi-domain]  Cd Length: 346  Bit Score: 44.77  E-value: 5.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1401077077   8 IHLIAHMANVSIGTVDRALHGRGGIKESTRQRILQVARQIGYTPNLAARALSvAKASARVGVCI 71
Cdd:PRK10401    4 IRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALA-TQVSDTIGVVV 66
 
Name Accession Description Interval E-value
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 67-323 9.15e-52

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: 172.88  E-value: 9.15e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  67 VGVCIPREIHFFYDQLWSGVLDEARRVAQLGLQFLNrpvhalGEGDTAVFKE----LVQCGVDGIILTAGNPKALTPLID 142
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGP------AEADAAEQVAqiedAIAQGVDAIIVAPVDPTALAPVLK 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 143 EAEANGIRVVCVSTDAPESRRSSIVCVEPSLNGSLAGELMGKLVPRASKVAVVAGMLTAEDHRKKTDGFSEAFPRHCTGG 222
Cdd:pfam13407  75 KAKDAGIPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLKEKYPGI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 223 KIAGIIEG-HEDEDESFQKTFDLLRRVPN-LAGLY-VNTVNCLPVCRALGARGLAGKVKLITTDLFAEMSPYFQKGTITA 299
Cdd:pfam13407 155 KVVAEVEGtNWDPEKAQQQMEALLTAYPNpLDGIIsPNDGMAGGAAQALEAAGLAGKVVVTGFDATPEALEAIKDGTIDA 234

                         250       260
                  ....*....|....*....|....
gi 1401077077 300 SIYQQPHRQGQIAVRVMADNLTNK 323
Cdd:pfam13407 235 TVLQDPYGQGYAAVELAAALLKGK 258
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 54-342 2.32e-44

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: 155.08  E-value: 2.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  54 AARALSVAKASARVGVCIPREIHFFYDQLWSGVLDEArrvAQLGLQFLNRPvhalGEGDTA----VFKELVQCGVDGIIL 129
Cdd:COG1879    23 AAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAA---KELGVELIVVD----AEGDAAkqisQIEDLIAQGVDAIIV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 130 TAGNPKALTPLIDEAEANGIRVVCVSTDAPESRRSSIVCVEPSLNGSLAGELMGKLVPRASKVAVVAGMLTAEDHRKKTD 209
Cdd:COG1879    96 SPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGGKGKVAILTGSPGAPAANERTD 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 210 GFSEAFPRHcTGGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLY-VNTVNCLPVCRALGARGLAGKVKLITTDLFAEM 288
Cdd:COG1879   176 GFKEALKEY-PGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFaANDGMALGAAQALKAAGRKGDVKVVGFDGSPEA 254

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1401077077 289 SPYFQKGTITASIYQQPHRQGQIAVRVMADNLTNKIhFPPAVHLSPGVVMSSNL 342
Cdd:COG1879   255 LQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKE-VPKEILTPPVLVTKENV 307
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
 66-339 1.82e-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: 141.16  E-value: 1.82e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  66 RVGVCIPREIHFFYDQLWSGVLDEARRVAQLGLQFLNRPVHALGEGDTAVFKELVQCGVDGIILTAGNPKALTPLIDEAE 145
Cdd:cd06307     1 RFGFLLPSPENPFYELLRRAIEAAAAALRDRRVRLRIHFVDSLDPEALAAALRRLAAGCDGVALVAPDHPLVRAAIDELA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 146 ANGIRVVCVSTDAPESRRSSIVCVEPSLNGSLAGELMGK-LVPRASKVAVVAGMLTAEDHRKKTDGFSEAFPRHCTGGKI 224
Cdd:cd06307    81 ARGIPVVTLVSDLPGSRRLAYVGIDNRAAGRTAAWLMGRfLGRRPGKVLVILGSHRFRGHEEREAGFRSVLRERFPDLTV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 225 AGIIEGHEDEDESFQKTFDLLRRVPNLAGLYVNTVNCLPVCRALGARGLAGKVKLITTDLFAEMSPYFQKGTITASIYQQ 304
Cdd:cd06307   161 LEVLEGLDDDELAYELLRELLARHPDLVGIYNAGGGNEGIARALREAGRARRVVFIGHELTPETRRLLRDGTIDAVIDQD 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1401077077 305 PHRQGQIAVRVMADNLTNKIHFPPAVHLSPGVVMS 339
Cdd:cd06307   241 PELQARRAIEVLLAHLGGKGPAPPQPPIPIEIITR 275
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
 66-323 5.23e-34

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: 126.53  E-value: 5.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  66 RVGVCIPREIHFFYDQLWSGVLDEArrvAQLGLQFlnrpVHALGEGDTA----VFKELVQCGVDGIILTAGNPKALTPLI 141
Cdd:cd01536     1 KIGVVVKDLTNPFWVAVKKGAEAAA---KELGVEL----VVLDAQGDVAkqisQIEDLIAQGVDAIIIAPVDSEALVPAV 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 142 DEAEANGIRVVCVSTDAPE-SRRSSIVCVEPSLNGSLAGELMGKLVPRASKVAVVAGMLTAEDHRKKTDGFSEAFPRHCt 220
Cdd:cd01536    74 KKANAAGIPVVAVDTDIDGgGDVVAFVGTDNYEAGKLAGEYLAEALGGKGKVAILEGPPGSSTAIDRTKGFKEALKKYP- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 221 GGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLY-VNTVNCLPVCRALGARGLAGKVKLITTDLFAEMSPYFQKGTITA 299
Cdd:cd01536   153 DIEIVAEQPANWDRAKALTVTENLLQANPDIDAVFaANDDMALGAAEALKAAGRTGDIKIVGVDGTPEALKAIKDGELDA 232

                         250       260
                  ....*....|....*....|....
gi 1401077077 300 SIYQQPHRQGQIAVRVMADNLTNK 323
Cdd:cd01536   233 TVAQDPYLQGYLAVEAAVKLLNGE 256
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
 115-331 1.17e-33

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: 125.77  E-value: 1.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 115 VFKELVQCGVDGIILTAGNPKALTPLIDEAEANGIRVVCVSTDAPESRRSSIVCVEPSLNGSLAGELMGKLVPRASKVAV 194
Cdd:cd06314    48 LIEDLIARGVDGIAISPNDPEAVTPVINKAADKGIPVITFDSDAPDSKRLAYIGTDNYEAGREAGELMKKALPGGGKVAI 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 195 VAGMLTAEDHRKKTDGFSEAFPRHcTGGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLY-VNTVNCLPVCRALGARGL 273
Cdd:cd06314   128 ITGGLGADNLNERIQGFKDALKGS-PGIEIVDPLSDNDDIAKAVQNVEDILKANPDLDAIFgVGAYNGPAIAAALKDAGK 206

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1401077077 274 AGKVKLITTDLFAEMSPYFQKGTITASIYQQPHRQGQIAVRVMADNLTNKIHFPPAVH 331
Cdd:cd06314   207 VGKVKIVGFDTLPETLQGIKDGVIAATVGQRPYEMGYLSVKLLYKLLKGGKPVPDVID 264
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
3-337 5.32e-33

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 125.31  E-value: 5.32e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077   3 KPRSGIHLIAHMANVSIGTVDRALHGRGGIKESTRQRILQVARQIGYTPNLAARALsVAKASARVGVCIPREIHFFYDQL 82
Cdd:COG1609     1 RKRVTIKDVARLAGVSVATVSRVLNGPPRVSEETRERVLAAAEELGYRPNAAARSL-RTGRTRTIGVVVPDLSNPFFAEL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  83 WSGVLDEARrvaQLGLQFLNRPVHALGEGDTAVFKELVQCGVDGIILTAGNPKAltPLIDEAEANGIRVVCVSTDAPESR 162
Cdd:COG1609    80 LRGIEEAAR---ERGYQLLLANSDEDPEREREALRLLLSRRVDGLILAGSRLDD--ARLERLAEAGIPVVLIDRPLPDPG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 163 RSSIVcvepsLNGSLAGELMGK-LVPR-ASKVAVVAGMLTAEDHRKKTDGFSEAFPRHCTGGKIAGIIEGHEDEDESFQK 240
Cdd:COG1609   155 VPSVG-----VDNRAGARLATEhLIELgHRRIAFIGGPADSSSARERLAGYREALAEAGLPPDPELVVEGDFSAESGYEA 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 241 TFDLLRRVPNLAGLYV-NTVNCLPVCRALGARGLA--GKVKLIT---TDLFAEMSPyfqkgTITaSIYQQPHRQGQIAVR 314
Cdd:COG1609   230 ARRLLARGPRPTAIFCaNDLMALGALRALREAGLRvpEDVSVVGfddIPLARYLTP-----PLT-TVRQPIEEMGRRAAE 303

                         330       340
                  ....*....|....*....|...
gi 1401077077 315 VMADNLTNKIHFPPAVHLSPGVV 337
Cdd:COG1609   304 LLLDRIEGPDAPPERVLLPPELV 326
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
 125-336 1.44e-29

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: 114.74  E-value: 1.44e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 125 DGIILTAGNPKALTPLIDEAEANGIRVVCVSTDAPESRRSSIVCVEPSLNGSLAGELMGKLVPRASKVAVVAGMLTaEDH 204
Cdd:cd19969    58 DGIAVSAIDPEALTPTINKAVDAGIPVVTFDSDAPESKRISYVGTDNYEAGYAAAEKLAELLGGKGKVAVLTGPGQ-PNH 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 205 RKKTDGFSEAFPRHcTGGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLYVNTVNCLP-VCRALGARGLAGKVKLITTD 283
Cdd:cd19969   137 EERVEGFKEAFAEY-PGIEVVAVGDDNDDPEKAAQNTSALLQAHPDLVGIFGVDASGGVgAAQAVREAGKTGKVKIVAFD 215

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1401077077 284 LFAEMSPYFQKGTITASIYQQPHRQGQIAVRVMADNLTNKIHFPPAVHLSPGV 336
Cdd:cd19969   216 DDPETLDLIKDGVIDASIAQRPWMMGYWSLQFLYDLANGLVKDAWQTAGVNPL 268
PBP1_LsrB_Quorum_Sensing-like cd06302
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ...
 90-330 4.50e-25

periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs; Periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.


Pssm-ID: 380525 [Multi-domain]  Cd Length: 296  Bit Score: 103.09  E-value: 4.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  90 ARRVA-QLGLQFLNR-PVHALGEGDTAVFKELVQCGVDGIILTAGNPKALTPLIDEAEANGIRVVCVSTDAPESRRSsiV 167
Cdd:cd06302    21 AKKAAkELGVEVVYTgPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDAGIKVITWDSDAPPSARD--Y 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 168 CVEPSLNGSLA---GELMGKLVPRASKVAVVAGMLTAEDHRKKTDGFSEAFPRHCTGGKIAGIIEGHEDEDESFQKTFDL 244
Cdd:cd06302    99 FVNQADDEGLGealVDSLAKEIGGKGKVAILSGSLTATNLNAWIKAMKEYLKSKYPDIELVDTYYTDDDQQKAYTQAQNL 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 245 LRRVPNLAGLY-VNTVNCLPVCRALGARGLAGKVKLITTDLFAEMSPYFQKGTITASIYQQPHRQGQIAVrVMADNLTNK 323
Cdd:cd06302   179 IQAYPDLKGIIgVSTTAPPAAAQAVEEAGKTGKVAVTGIGLPNTARPYLKDGSVKEGVLWDPAKLGYLTV-YAAYQLLKG 257


                  ....*..
gi 1401077077 324 IHFPPAV 330
Cdd:cd06302   258 KGFTEDS 264
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 110-314 9.30e-24

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


Pssm-ID: 380661 [Multi-domain]  Cd Length: 274  Bit Score: 98.82  E-value: 9.30e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 110 EGDTAVFKELVQCGVDGIILTAGNPKALTPLIDEAEANGIRVVCVSTDAPESRRSSIVCVEPSLNGSLAGELMGKLVPRA 189
Cdd:cd20006    46 DGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERAKKAGIPVITIDSPVNSKKADSFVATDNYEAGKKAGEKLASLLGEK 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 190 SKVAVVAGMLTAEDHRKKTDGFSEAFPRHcTGGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLYV-NTVNCLPVCRAL 268
Cdd:cd20006   126 GKVAIVSFVKGSSTAIEREEGFKQALAEY-PNIKIVETEYCDSDEEKAYEITKELLSKYPDINGIVAlNEQSTLGAARAL 204

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1401077077 269 GARGLAGKVKLITTDLFAEMSPYFQKGTITASIYQQPHRQGQIAVR 314
Cdd:cd20006   205 KELGLGGKVKVVGFDSSVEEIQLLEEGIIDALVVQNPFNMGYLSVQ 250
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 82-338 1.05e-23

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


Pssm-ID: 380659 [Multi-domain]  Cd Length: 273  Bit Score: 98.84  E-value: 1.05e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  82 LWSGVLDEARRVAQLglQFLNRpvhalgegdtavfkeLVQCGVDGIILTAGNPKALTPLIDEAEANGIRVVCVSTDAPES 161
Cdd:cd20004    33 YWRGPSREDDVEAQI--QIIEY---------------FIDQGVDGIVLAPLDRKALVAPVERARAQGIPVVIIDSDLGGD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 162 RRSSIVCVEPSLNGSLAGELMGKLVPRASKVAVVagmLTAEDHRKKTD---GFSEAFPRHCTGGKIagIIEGH--EDEDE 236
Cdd:cd20004    96 AVISFVATDNYAAGRLAAKRMAKLLNGKGKVALL---RLAKGSASTTDrerGFLEALKKLAPGLKV--VDDQYagGTVGE 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 237 SFQKTFDLLRRVPNLAGLY-VNTVNCLPVCRALGARGLAGKVKLITTDLFAEMSPYFQKGTITASIYQQPHRQGQIAVRV 315
Cdd:cd20004   171 ARSSAENLLNQYPDVDGIFtPNESTTIGALRALRRLGLAGKVKFIGFDASDLLLDALRAGEISALVVQDPYRMGYLGVKT 250

                         250       260
                  ....*....|....*....|...
gi 1401077077 316 MADNLTNKihfPPAVHLSPGVVM 338
Cdd:cd20004   251 AVAALRGK---PVPKRIDTGVVL 270
PBP1_LsrB_Quorum_Sensing cd20003
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ...
 94-324 6.80e-23

ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.


Pssm-ID: 380658  Cd Length: 298  Bit Score: 96.96  E-value: 6.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  94 AQLGLQFL-NRPVHALGEGDTAVFKELVQCGVDGIILTAGNPKALTPLIDEAEANGIRVVCVSTDA-PESRRSSIVCVEP 171
Cdd:cd20003    26 KELGVDVTyDGPTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKKGIKVVTWDSDVnPDARDFFVNQATP 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 172 SLNGSLAGELMGKLVPRASKVAVVAGMLTAED------HRKKTdgFSEAFPrhctGGKIAGIIEGHEDEDESFQKTFDLL 245
Cdd:cd20003   106 EGIGKTLVDMVAEQTGEKGKVAIVTSSPTATNqnawikAMKAY--IAEKYP----DMKIVTTQYGQEDPAKSLQVAENIL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 246 RRVPNLAGLYVNTVNCLP-VCRALGARGLAGKVKLITTDLFAEMSPYFQKGTITASIYQQPHRQGQIAVRVMADNLTNKI 324
Cdd:cd20003   180 KAYPDLKAIIAPDSVALPgAAEAVEQLGRTGKVAVTGLSTPNVMRPYVKDGTVKSVVLWDVVDLGYLAVYVARALADGTL 259
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
 107-342 1.17e-22

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: 96.18  E-value: 1.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 107 ALGEGDT----AVFKELVQCGVDGIILTAGNPKALTPLIDEAEANGIRVVCVST--DAPESRRS-----SIVCVEPSLNG 175
Cdd:cd06320    37 APSETDTqgqlNLLETMLNKGYDAILVSPISDTNLIPPIEKANKKGIPVINLDDavDADALKKAggkvtSFIGTDNVAAG 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 176 SLAGELMGKLVPRASKVAVVAGMLTAEDHRKKTDGFSEAFPRHcTGGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLY 255
Cdd:cd06320   117 ALAAEYIAEKLPGGGKVAIIEGLPGNAAAEARTKGFKETFKKA-PGLKLVASQPADWDRTKALDAATAILQAHPDLKGIY 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 256 V-NTVNCLPVCRALGARGLAGKVKLITTDLFAEMSPYFQKGTITASIYQQPHRQGQIAVRVMADNLT-NKIhfPPAVHLS 333
Cdd:cd06320   196 AaNDTMALGAVEAVKAAGKTGKVLVVGTDGIPEAKKSIKAGELTATVAQYPYLEGAMAVEAALRLLQgQKV--PAVVATP 273


                  ....*....
gi 1401077077 334 PGVVMSSNL 342
Cdd:cd06320   274 QALITKDNV 282
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 114-313 2.13e-21

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: 92.31  E-value: 2.13e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 114 AVFKELVQCGVDGIILTAGNPKALTPLIDEAEANGIRVVCVST----DAPESRRSSIVCVEPS--LNGSLAGELMGKLVP 187
Cdd:cd19970    49 AIVENLIAQKVDAIVIAPADSKALVPVLKKAVDAGIAVINIDNrldaDALKEGGINVPFVGPDnrQGAYLAGDYLAKKLG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 188 RASKVAVVAGMLTAEDHRKKTDGFSEAFPRHctGGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLY-VNTVNCLPVCR 266
Cdd:cd19970   129 KGGKVAIIEGIPGADNAQQRKAGFLKAFEEA--GMKIVASQSANWEIDEANTVAANLLTAHPDIRGILcANDNMALGAIK 206

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1401077077 267 ALGARGLAGKVKLITTDLFAEMSPYFQKGTITASIYQQPHRQGQIAV 313
Cdd:cd19970   207 AVDAAGKAGKVLVVGFDNIPAVRPLLKDGKMLATIDQHPAKQAVYGI 253
PBP1_ABC_rhamnose cd20000
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ...
 70-297 5.10e-21

rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding protein similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.


Pssm-ID: 380655  Cd Length: 298  Bit Score: 91.93  E-value: 5.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  70 CIPREIHFFYDQLWSGVLDEArrVAQLGLQF-LNRPVHALGEGDTAVFKELVQCGVDGIILTAGNPKALTPLIDEAEANG 148
Cdd:cd20000     4 FLPKSLGNPYFDAARDGAKEA--AKELGGELiFVGPTTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAAG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 149 IRVVCVSTDAPESRRSsiVCVEPSLNGSLAG---ELMGKLVPRASKVAVVAGMLTAEDHRK-----KTDGFSEAFPrhct 220
Cdd:cd20000    82 IKVVTFDSDVAPEARD--LFVNQADADGIGRaqvDMMAELIGGEGEFAILSATPTATNQNAwidamKKELASPEYA---- 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1401077077 221 GGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLYV-NTVNCLPVCRALGARGLAGKVKLITTDLFAEMSPYFQKGTI 297
Cdd:cd20000   156 GMKLVKVAYGDDDAQKSYQEAEALLQAYPDLKGIIApTTVGIAAAARALEDSGLKGKVKVTGLGLPSEMAKYVKDGTV 233
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 76-332 8.08e-21

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


Pssm-ID: 380533 [Multi-domain]  Cd Length: 272  Bit Score: 90.86  E-value: 8.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  76 HFFYDQLWSGVLDEArrvAQLGLQFLNrpVHALGEGDTAV----FKELVQCGVDGIILTAGNPKALTPLIDEAEANGIRV 151
Cdd:cd06310    11 SAFWRTVREGAEAAA---KDLGVKIIF--VGPESEEDVAGqnslLEELINKKPDAIVVAPLDSEDLVDPLKDAKDKGIPV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 152 VCVSTDAPESRRSSIVCVEPSLNGSLAGELMGKLVPRASKVAVVAGMLTAEDHRKKTDGFSEAFPRHCTGGKIAGIIEGH 231
Cdd:cd06310    86 IVIDSGIKGDAYLSYIATDNYAAGRLAAQKLAEALGGKGKVAVLSLTAGNSTTDQREEGFKEYLKKHPGGIKVLASQYAG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 232 EDEDESFQKTFDLLRRVPNLAGLY-VNTVNCLPVCRALGARGLAGKVKLITTDLFAEMSPYFQKGTITASIYQQPHRQGQ 310
Cdd:cd06310   166 SDYAKAANETEDLLGKYPDIDGIFaTNEITALGAAVAIKSRKLSGQIKIVGFDSQEELLDALKNGKIDALVVQNPYEIGY 245

                         250       260
                  ....*....|....*....|..
gi 1401077077 311 IAVRvMADNLTNKIHFPPAVHL 332
Cdd:cd06310   246 EGIK-LALKLLKGEEVPKNIDT 266
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 67-337 1.34e-20

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


Pssm-ID: 380545 [Multi-domain]  Cd Length: 270  Bit Score: 90.03  E-value: 1.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  67 VGVCIPREIHFFYDQLWSGVLDEArrvAQLGLQflnrPVHALGEGDTAV----FKELVQCGVDGIILTAGNPKALTPLID 142
Cdd:cd06322     2 IGVSLLTLQHPFFVDIKDAMKKEA---AELGVK----VVVADANGDLAKqlsqIEDFIQQGVDAIILAPVDSGGIVPAIE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 143 EAEANGIRVVCVSTDAPESRRSSIVCVEPSLNGSLAGELMGK-LVPRASKVAVVaGMLTAEDHRKKTDGFSEAFPRHcTG 221
Cdd:cd06322    75 AANEAGIPVFTVDVKADGAKVVTHVGTDNYAGGKLAGEYALKaLLGGGGKIAII-DYPEVESVVLRVNGFKEAIKKY-PN 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 222 GKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLY-VNTVNCLPVCRALGARGLAGKVKLITTDLFAE-MSPYFQKGTITA 299
Cdd:cd06322   153 IEIVAEQPGDGRREEALAATEDMLQANPDLDGIFaIGDPAALGALTAIESAGKEDKIKVIGFDGNPEaIKAIAKGGKIKA 232

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1401077077 300 SIYQQPHRQGQIAVRVMADNLTNKiHFPPAVHLSPGVV 337
Cdd:cd06322   233 DIAQQPDKIGQETVEAIVKYLAGE-TVEKEILIPPKLY 269
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
 66-338 2.78e-19

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


Pssm-ID: 380529 [Multi-domain]  Cd Length: 269  Bit Score: 86.48  E-value: 2.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  66 RVGVCIPreiHFfYDQLWS----GVLDEARRvaqLGLQFlnRPVHALGEGDTAV----FKELVQCGVDGIILTAGNPKAL 137
Cdd:cd06306     1 KICVLFP---HL-KDSYWVgvnyGIVDEAKR---LGVKL--TVYEAGGYTNLSKqisqLEDCVASGADAILLGAISFDGL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 138 TPLIDEAEANGIRVVC----VSTDAPESRrssiVCVEPSLNGSLAGELMGKLVP-RASKVAVVAGMLTAEDHRKKTDGFS 212
Cdd:cd06306    72 DPKVAEAAAAGIPVIDlvngIDSPKVAAR----VLVDFYDMGYLAGEYLVEHHPgKPVKVAWFPGPAGAGWAEDREKGFK 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 213 EAFprhcTGG--KIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLYVNTVNCLPVCRALGARGLAGKVKLITTDLFAEMSP 290
Cdd:cd06306   148 EAL----AGSnvEIVATKYGDTGKAVQLNLVEDALQAHPDIDYIVGNAVAAEAAVGALREAGLTGKVKVVSTYLTPGVYR 223

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1401077077 291 YFQKGTITASIYQQPHRQGQIAVRVMADNLTNKihfPPAVHLSPGVVM 338
Cdd:cd06306   224 GIKRGKILAAPSDQPVLQGRIAVDQAVRALEGK---PVPKHVGPPILV 268
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 113-338 3.60e-19

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: 86.14  E-value: 3.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 113 TAVFKELVQCGVDGIILTAGNPKALTPLIDEAEANGIRVVCVST--DAPESRRSSIVcvepSLN---GSLAGELMGKLVP 187
Cdd:cd20007    46 TPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADAGIKVVTVDTtlGDPSFVLSQIA----SDNvagGALAAEALAELIG 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 188 RASKVAVVA---GMLTAEDHRKktdGFSEAFPRHcTGGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLY-VNTVNCLP 263
Cdd:cd20007   122 GKGKVLVINstpGVSTTDARVK---GFAEEMKKY-PGIKVLGVQYSENDPAKAASIVAAALQANPDLAGIFgTNTFSAEG 197

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1401077077 264 VCRALGARGLAGKVKLITTDLFAEMSPYFQKGTITASIYQQPHRQGQIAVRVMADNLTNKIhfPPAVHLSPGVVM 338
Cdd:cd20007   198 AAAALRNAGKTGKVKVVGFDASPAQVEQLKAGTIDALIAQKPAEIGYLAVEQAVAALTGKP--VPKDILTPFVVI 270
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 123-338 6.38e-19

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: 85.36  E-value: 6.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 123 GVDGIILTAGNPKALTPLIDEAEAnGIRVVCVSTDAPESRRSSIVCVEPSLNGSLAGELMGKLVPRAS----KVAVVAGM 198
Cdd:cd20008    57 KPDAIVLAPNDTAALVPAVEAADA-GIPVVLVDSGANTDDYDAFLATDNVAAGALAADELAELLKASGggkgKVAIISFQ 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 199 LTAEDHRKKTDGFSEAFPRHCTGGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLY-VNTVNCLPVCRALGARGLAGKV 277
Cdd:cd20008   136 AGSQTLVDREEGFRDYIKEKYPDIEIVDVQYSDGDIAKALNQTTDLLTANPDLVGIFgANNPSAVGVAQALAEAGKAGKI 215

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1401077077 278 KLITTDLFAEMSPYFQKGTITASIYQQPHRQGQIAVrVMADNLTNKIHFPPAVhLSPGVVM 338
Cdd:cd20008   216 VLVGFDSSPDEVALLKSGVIKALVVQDPYQMGYEGV-KTAVKALKGEEIVEKN-VDTGVTV 274
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 78-316 1.87e-18

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: 84.33  E-value: 1.87e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  78 FYDQLWSGVLDEArrvAQLGLQFLNRPVHAlgegDTAvfkELVQ-------CGVDGIILTAGNPKALTPLIDEAEANGIR 150
Cdd:cd06319    13 FWQIMERGVQAAA---EELGYEFVTYDQKN----SAN---EQVTnandliaQGVDGIIISPTNSSAAPTVLDLANEAKIP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 151 VVCVSTDAPESRRSSIVCVEPSLNGSLAGELMGKLV----PRASKVAVVAGMLTAEDHRKKTDGFSEAFpRHCTGGKIAG 226
Cdd:cd06319    83 VVIADIGTGGGDYVSYIISDNYDGGYQAGEYLAEALkengWGGGSVGIIAIPQSRVNGQARTAGFEDAL-EEAGVEEVAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 227 IIEGHEDEDESFQKTFDLLRRVPNLAGLYV-NTVNCLPVCRALGARGLAGKVKLITTDLFAEMSPYFQKGTITASIYQQP 305
Cdd:cd06319   162 RQTPNSTVEETYSAAQDLLAANPDIKGIFAqNDQMAQGALQAIEEAGRTGDILVVGFDGDPEALDLIKDGKLDGTVAQQP 241

                         250
                  ....*....|.
gi 1401077077 306 HRQGQIAVRVM 316
Cdd:cd06319   242 FGMGARAVELA 252
HTH_LacI cd01392
Helix-turn-helix (HTH) DNA binding domain of the LacI family of transcriptional regulators; ...
 11-59 7.47e-18

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


Pssm-ID: 143331 [Multi-domain]  Cd Length: 52  Bit Score: 76.29  E-value: 7.47e-18
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1401077077  11 IAHMANVSIGTVDRALHGRGGIKESTRQRILQVARQIGYTPNLAARALS 59
Cdd:cd01392     3 IARAAGVSVATVSRVLNGKPRVSEETRERVLAAAEELGYRPNAAARSLR 51
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 123-318 4.26e-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: 380660 [Multi-domain]  Cd Length: 274  Bit Score: 77.28  E-value: 4.26e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 123 GVDGIILTAGNPKALTPLIDEAEANGIRVVCVSTDAPESrrsSIVCVEPSLN---GSLAGELMGKLVPRASKVAVVAGML 199
Cdd:cd20005    57 KPDAIALAALDTNALLPQLEKAKEKGIPVVTFDSGVPSD---LPLATVATDNyaaGALAADHLAELIGGKGKVAIVAHDA 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 200 TAEDHRKKTDGFSEAFPRHCTGGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLY-VNTVNCLPVCRALGARGLAGKVK 278
Cdd:cd20005   134 TSETGIDRRDGFKDEIKEKYPDIKVVNVQYGVGDHAKAADIAKAILQANPDLKGIYaTNEGAAIGVANALKEMGKLGKIK 213

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1401077077 279 LITTDLFAEMSPYFQKGTITASIYQQPHRQGQIAVRVMAD 318
Cdd:cd20005   214 VVGFDSGEAQIDAIKNGVIAGSVTQNPYGMGYKTVKAAVK 253
HTH_LACI smart00354
helix_turn _helix lactose operon repressor;
8-73 6.60e-15

helix_turn _helix lactose operon repressor;


Pssm-ID: 197675 [Multi-domain]  Cd Length: 70  Bit Score: 68.77  E-value: 6.60e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1401077077    8 IHLIAHMANVSIGTVDRALHGRGGIKESTRQRILQVARQIGYTPNLAARALSVAKASArVGVCIPR 73
Cdd:smart00354   3 IKDVARLAGVSKATVSRVLNGKGRVSEETREKVLAAMEELGYIPNRVARSLKGKKTKT-IGLIVPD 67
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
 118-341 9.43e-15

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


Pssm-ID: 380541 [Multi-domain]  Cd Length: 282  Bit Score: 73.60  E-value: 9.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 118 ELVQCGVDGIILTAGNPKALTPLIDEAEANGIRVVCV-STDAPESRRSSIVCVEPSLNGSLAGELMGKLVPRAS-KVAVV 195
Cdd:cd06318    50 DLITRGVDVLILNPVDPEGLTPAVKAAKAAGIPVITVdSALDPSANVATQVGRDNKQNGVLVGKEAAKALGGDPgKIIEL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 196 AGMLTAEDHRKKTDGFSEAF--PRHCTGGK----IAGIIEGHEDEDESFQKTFDLLRRVPNLAGLYV-NTVNCLPVCRAL 268
Cdd:cd06318   130 SGDKGNEVSRDRRDGFLAGVneYQLRKYGKsnikVVAQPYGNWIRSGAVAAMEDLLQAHPDINVVYAeNDDMALGAMKAL 209

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1401077077 269 GARGLAGKVKLITTDLFAEMSPYFQKGTITASIYQQPHRQGQIAVRVMADNLTNKIHFPPAVHLSPGVVMSSN 341
Cdd:cd06318   210 KAAGMLDKVKVAGADGQKEALKLIKDGKYVATGLNDPDLLGKTAVDTAAKVVKGEESFPEFTYTPTALITKDN 282
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 67-337 1.04e-14

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: 73.24  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  67 VGVCIPREIHFFYDQLWSGVLDEArrvAQLGLQFLNrpVHALGEGDTAV--FKELVQCGVDGIILTAGNPKALTPLIDEA 144
Cdd:cd19972     2 IGLAVANLQADFFNQIKQSVEAEA---KKKGYKVIT--VDAKGDSATQVnqIQDLITQNIDALIYIPAGATAAAVPVKAA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 145 EANGIRVVCVSTDAPESRRSSIVCVEpSLNGSLA-GELMGKLVPRASKVAVVAGML--TAEDHRKKtdGFSEAFPRhCTG 221
Cdd:cd19972    77 RAAGIPVIAVDRNPEDAPGDTFIATD-SVAAAKElGEWVIKQTGGKGEIAILHGQLgtTPEVDRTK--GFQEALAE-APG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 222 GKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLYVNTVnclpvCRALGAR------GLAGKVKLITTDLFAEMSPYFQKG 295
Cdd:cd19972   153 IKVVAEQTADWDQDEGFKVAQDMLQANPNITVFFGQSD-----AMALGAAqavkvaGLDHKIWVVGFDGDVAGLKAVKDG 227

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1401077077 296 TITASIYQQPHRQGQIAVRVMADNLTNKIhfPPAVHLSPGVV 337
Cdd:cd19972   228 VLDATMTQQTQKMGRLAVDSAIDLLNGKA--VPKEQLQDAVL 267
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
 123-313 2.86e-14

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: 71.92  E-value: 2.86e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 123 GVDGIILTAGNPKALTPLIDEAEANGIRVVCVSTDAP--ESRRSSIVCVEPSLNG-SLAGELMGKLVPRASKVAV---VA 196
Cdd:cd19965    56 GPDGIATTIVDPEAFDEVIKRALDAGIPVVAFNVDAPggENARLAFVGQDLYPAGyVLGKRIAEKFKPGGGHVLLgisTP 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 197 GMLTAEdHRKktDGFSEAFPRHCTGGKIAGIIEGHeDEDESFQKTFDLLRRVPNLAGLY-VNTVNCLPVCRALGARGLAG 275
Cdd:cd19965   136 GQSALE-QRL--DGIKQALKEYGRGITYDVIDTGT-DLAEALSRIEAYYTAHPDIKAIFaTGAFDTAGAGQAIKDLGLKG 211

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1401077077 276 KVKLITTDLFAEMSPYFQKGTITASIYQQPHRQGQIAV 313
Cdd:cd19965   212 KVLVGGFDLVPEVLQGIKAGYIDFTIDQQPYLQGFYPV 249
PRK10014 PRK10014
DNA-binding transcriptional repressor MalI; Provisional
 1-155 9.10e-14

DNA-binding transcriptional repressor MalI; Provisional


Pssm-ID: 182193 [Multi-domain]  Cd Length: 342  Bit Score: 71.28  E-value: 9.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077   1 MTKPRSGIHLIAHMANVSIGTVDRALHGRGGIKESTRQRILQVARQIGYTPNLAARALSvAKASARVGVcIPREIHF-FY 79
Cdd:PRK10014    2 ATAKKITIHDVALAAGVSVSTVSLVLSGKGRISTATGERVNQAIEELGFVRNRQASALR-GGQSGVIGL-IVRDLSApFY 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1401077077  80 DQLWSGvLDEARRvAQLGLQFLNRPVHAlGEGDTAVFKELVQCGVDGIILtAGNPKALTPLIDEAEANGIRVVCVS 155
Cdd:PRK10014   80 AELTAG-LTEALE-AQGRMVFLLQGGKD-GEQLAQRFSTLLNQGVDGVVI-AGAAGSSDDLREMAEEKGIPVVFAS 151
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
 109-323 7.98e-13

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: 67.96  E-value: 7.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 109 GEGDTAVF----KELVQCGVDGIILTAGNPKALTPLIDEAEANGIRVVCVSTDAPESRRSSIVCVEPSLNGSLAGELMGK 184
Cdd:cd06308    38 AQGDAAKQiadiEDLIAQGVDLLIVSPNEADALTPVVKKAYDAGIPVIVLDRKVSGDDYTAFIGADNVEIGRQAGEYIAE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 185 LVPRASKVAVVAGMLTAEDHRKKTDGFSEAFpRHCTGGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLYV-NTVNCLP 263
Cdd:cd06308   118 LLNGKGNVVEIQGLPGSSPAIDRHKGFLEAI-AKYPGIKIVASQDGDWLRDKAIKVMEDLLQAHPDIDAVYAhNDEMALG 196

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1401077077 264 VCRALGARGLAGKVKLITTD-LFAEMSPYFQKGTITASIYQQPHrqGQIAVRVMADNLTNK 323
Cdd:cd06308   197 AYQALKKAGREKEIKIIGVDgLPEAGEKAVKDGILAATFLYPTG--GKEAIEAALKILNGE 255
PBP1_ABC_sugar_binding-like cd06300
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ...
 117-342 2.54e-12

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


Pssm-ID: 380523 [Multi-domain]  Cd Length: 302  Bit Score: 66.58  E-value: 2.54e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 117 KELVQCGVDGIILTAGNPKALTPLIDEAEANGIRVVCVS--TDAPEsrrSSIVCVEPSLNGSLAGELMGKLVPRASKVAV 194
Cdd:cd06300    54 RNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFDgaVTSPD---AYNVSNDQVEWGRLGAKWLFEALGGKGNVLV 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 195 VAGM--LTAEDHRKKtdGFSEAFPRhCTGGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLYVNTVNCLPVCRALGARG 272
Cdd:cd06300   131 VRGIagAPASADRHA--GVKEALAE-YPGIKVVGEVFGGWDEATAQTAMLDFLATHPQVDGVWTQGGEDTGVLQAFQQAG 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1401077077 273 LAgKVKLITTD-----LFAEMSPYFQKGTITASiyqQPHRQGQIAVRVMADNLTNKIHFPPAVHLSPGVVMSSNL 342
Cdd:cd06300   208 RP-PVPIVGGDengfaKQWWKHPKKGLTGAAVW---PPPAIGAAGLEVALRLLEGQGPKPQSVLLPPPLITNDDA 278
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 111-337 4.44e-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: 4.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 111 GDTAVFKELVQ----CGVDGIILTAGNPKALTPLIDEAEANGIRVVCVST--DAPESRRSSIVCV--EPSLNGSLAGElm 182
Cdd:cd06312    41 NDIADQARLIEqaiaAKPDGIIVTIPDPDALEPALKRAVAAGIPVIAINSgdDRSKERLGALTYVgqDEYLAGQAAGE-- 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 183 gKLVPRASKVAVVAgmLTAEDH---RKKTDGFSEAFprhcTGGKIAGI-IEGHEDEDESFQKTFDLLRRVPNLAGLYVNT 258
Cdd:cd06312   119 -RALEAGPKNALCV--NHEPGNpglEARCKGFADAF----KGAGILVElLDVGGDPTEAQEAIKAYLQADPDTDAVLTLG 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 259 VNCL-PVCRALGARGLAGKVKLITTDLFAEMSPYFQKGTITASIYQQPHRQGQIAVRVMADNLTNKIhFPPAVHLS--PG 335
Cdd:cd06312   192 PVGAdPALKAVKEAGLKGKVKIGTFDLSPETLEAIKDGKILFAIDQQPYLQGYLAVVFLYLYKRYGT-LPPPEPILtgPG 270


                  ..
gi 1401077077 336 VV 337
Cdd:cd06312   271 FV 272
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 119-346 6.51e-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: 380540 [Multi-domain]  Cd Length: 281  Bit Score: 65.48  E-value: 6.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 119 LVQCGVDGIILTAGNPKALTPLIDEAEANGIRVVCVSTDAPESRRSSIVCVEPslngSLAGELMGKLVPR--------AS 190
Cdd:cd06317    51 YIARGVDAIILDAIDVNGSIPAIKRASEAGIPVIAYDAVIPSDFQAAQVGVDN----LEGGKEIGKYAADyikaelggQA 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 191 KVAVVaGMLTAEDHRKKTDGFSEAFpRHCTGGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLY-VNTVNCLPVCRALG 269
Cdd:cd06317   127 KIGVV-GALSSLIQNQRQKGFEEAL-KANPGVEIVATVDGQNVQEKALSAAENLLTANPDLDAIYaTGEPALLGAVAAVR 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 270 ARGLAGKVKLITTDLFAEMspYFQK---GTITASIYQQPHRQGQIAVRVmADNLTNKIHFPPAVHLSPGVVMSSNLHLFR 346
Cdd:cd06317   205 SQGRQGKIKVFGWDLTKQA--IFLGideGVLQAVVQQDPEKMGYEAVKA-AVKAIKGEDVEKTIDVPPTIVTKENVDQFR 281
PBP1_ABC_sugar_binding-like cd06316
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 119-342 1.09e-11

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: 64.95  E-value: 1.09e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 119 LVQCGVDGIILTAGNPKALTPLIDEAEANGIRVVcVSTDAPESRR-----SSIVCVEPSLNGSLAGELMGKLVPRASKVA 193
Cdd:cd06316    52 LIALKPDIIISIPVDPVATAAAYKKVADAGIKLV-FMDNVPDGLEagkdyVSVVSSDNRGNGQIAAELLAEAIGGKGKVG 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 194 VV--AGMLTAEDHRKKtdGFSEAFPRHCTGGKIAGIiEGHEDEDESFQKTFDLLRRVPNLAGLYVN-TVNCLPVCRALGA 270
Cdd:cd06316   131 IIyhDADFYATNQRDK--AFKDTLKEKYPDIKIVAE-QGFADPNDAEEVASAMLTANPDIDGIYVSwDTPALGVISALRA 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1401077077 271 RGLAgKVKLITTDLFAEMSPYFQKGTITASI-YQQPHRQGQIAVRVMADNLTNKIhFPPAVHLSPGVVMSSNL 342
Cdd:cd06316   208 AGRS-DIKITTVDLGTEIALDMAKGGNVKGIgAQRPYDQGVAEALAAALALLGKE-VPPFIGVPPLAVTKDNL 278
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 118-323 1.30e-11

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


Pssm-ID: 380626 [Multi-domain]  Cd Length: 267  Bit Score: 64.14  E-value: 1.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 118 ELVQCGVDGIILTAGNPKALTPLIDEAEANGIRVVCVstDAPESRRSSIVCVEPSLN---GSLAGELMGKLVPRASKVAV 194
Cdd:cd19971    50 DMINQGVDAIFLNPVDSEGIRPALEAAKEAGIPVINV--DTPVKDTDLVDSTIASDNynaGKLCGEDMVKKLPEGAKIAV 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 195 VAgMLTAEDHRKKTDGFSEAFPRHcTGGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLY-VNTVNCLPVCRALGARGL 273
Cdd:cd19971   128 LD-HPTAESCVDRIDGFLDAIKKN-PKFEVVAQQDGKGQLEVAMPIMEDILQAHPDLDAVFaLNDPSALGALAALKAAGK 205

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1401077077 274 AGKVKLITTDLFAEMSPYFQKGTITASIYQQPHRQGQIAVRVMADNLTNK 323
Cdd:cd19971   206 LGDILVYGVDGSPDAKAAIKDGKMTATAAQSPIEIGKKAVETAYKILNGE 255
PBP1_LsrB_Quorum_Sensing-like cd20002
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
 123-309 2.15e-10

ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.


Pssm-ID: 380657  Cd Length: 295  Bit Score: 60.79  E-value: 2.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 123 GVDGIILTAGNPKALTPLIDEAEANGIRVVcvSTDAPeSRRSSIVCVEPSLN---GSLAGELMGKLVPRASKVAVVAGML 199
Cdd:cd20002    56 GVDAILVVPNDAKVLEPVFKKAREKGIVVI--THESP-GQKGADWDVELIDNekfGEAQMELLAKEMGGKGEYAIFVGSL 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 200 TAEDHRKKTDGFSEAFPRHCTGGK-IAGIIEGHEDEDESFQKTFDLLRRVPNLAG-LYVNTVNCLPVCRALGARGLAGKV 277
Cdd:cd20002   133 TVPLHNLWADAAVEYQKEKYPNMKqVTDRIPGGEDVDVSRQTTLELLKAYPDLKGiISFGSLGPIGAGQALREKGLKGKV 212

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1401077077 278 KLITTDLFAEMSPYFQKGTITASIYQQPHRQG 309
Cdd:cd20002   213 AVVGTVIPSQAAAYLKEGSITEGYLWDPADAG 244
PBP1_LsrB_Quorum_Sensing-like cd20001
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
 123-299 3.02e-10

ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; Ligand-binding protein LsrB-like of a transport system, similar to periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium and its close homologs from other bacteria. The members of this group are homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transporters of many sugar based solutes in bacteria and archaea and that are a member of the type 1 periplasmic binding protein superfamily. LsrB, which is part of the ABC transporter complex LsrABCD, binds a chemically distinct form of the AI-2 signal that lacks boron, in contrast to the Vibrio harveyi AI-2 signaling molecule that has an unusual furanosyl borate diester. Hence, many bacteria coordinate their gene expression according to the local density of their population by producing species specific AI-2. This process of quorum sensing allows LsrB to function as a periplasmic AI-2 binding protein in interspecies signaling.


Pssm-ID: 380656  Cd Length: 296  Bit Score: 60.37  E-value: 3.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 123 GVDGIILTAGNPKALTPLIDEAEANGIRVVC------VSTDAPesrrssivcVEPSLN---GSLAGELMGKLVPRASKVA 193
Cdd:cd20001    56 GVDAICVVPNDPEALEPVLKKARDAGIVVITheasnlKNVDYD---------VEAFDNaayGAFIMDKLAEAMGGKGKYV 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 194 VVAGMLTAEDHRKKTDG----FSEAFPrhcTGGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLYVNTVNCLP-VCRAL 268
Cdd:cd20001   127 TFVGSLTSTSHMEWANAavayQKANYP---DMLLVTDRVETNDDSETAYEKAKELLKTYPDLKGIVGCSSSDVPgAARAV 203

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1401077077 269 GARGLAGKVKLITTDLFAEMSPYFQKGTITA 299
Cdd:cd20001   204 EELGLQGKIAVVGTGLPSVAGEYLEDGTIDY 234
LacI pfam00356
Bacterial regulatory proteins, lacI family;
8-52 4.85e-10

Bacterial regulatory proteins, lacI family;


Pssm-ID: 306791 [Multi-domain]  Cd Length: 46  Bit Score: 54.57  E-value: 4.85e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1401077077   8 IHLIAHMANVSIGTVDRALHGRGGIKESTRQRILQVARQIGYTPN 52
Cdd:pfam00356   2 IKDVARLAGVSKSTVSRVLNNPGRVSEETRERVEAAMEELNYIPN 46
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
 66-330 1.15e-09

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


Pssm-ID: 380528 [Multi-domain]  Cd Length: 273  Bit Score: 58.46  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  66 RVGVCIPREIHFFYDQLWSGVLDEARRvaqLGLQflnrPVHALGEGDTAVFKELVQC----GVDGIILTAGNPKALTPLI 141
Cdd:cd06305     1 TIAVVRNGTSGDWDQQALQGAVAEAEK---LGGT----VIVFDANGDDARMADQIQQaitqKVDAIIISHGDADALDPKL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 142 DEAEANGIRVVCVSTDAPESRrssiVCVEPSLNGSLAGELMGKLVPR---ASKVAVV-AGMLTAEDHRKKT-DGFSEAFP 216
Cdd:cd06305    74 KKALDAGIPVVTFDTDSQVPG----VNNITQDDYALGTLSLGQLVKDlngEGNIAVFnVFGVPPLDKRYDIyKAVLKANP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 217 rhctGGKIAGIIEGHEDED---ESFQKTFDLLRRVPNlaglyvNTVN---------CLPVCRALGARGLAgKVKLITTDL 284
Cdd:cd06305   150 ----GIKKIVAELGDVTPNtaaDAQTQVEALLKKYPE------GGIDaiwaawdepAKGAVQALEEAGRT-DIKVYGVDI 218

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1401077077 285 FAEMSPYFQK--GTITASIYQQPHRQGQIAVRVMA-----DNLTNKIHFPPAV 330
Cdd:cd06305   219 SNQDLELMADegSPWVATAAQDPALIGTVAVRNVArklagEDLPDKYSLVPVL 271
Periplasmic_Binding_Protein_type1 cd01391
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
 78-322 2.37e-09

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


Pssm-ID: 380477 [Multi-domain]  Cd Length: 280  Bit Score: 57.66  E-value: 2.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  78 FYDQLWSGVLDEARrvaQLGLQFLNRPVHALGEGDTAVFKELVQCGVDGIIltaGNPKALTPLIDEAEANGIRVVCVSTD 157
Cdd:cd01391    16 FGIQRVEAIFHTAD---KLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVI---GPGSSSVAIVIQNLAQLFDIPQLALD 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 158 A------PESRRSSIVCVEPSLNgsLAGELMGKLVPR--ASKVAVVAGMLTAEDhRKKTDGFSEAFPRhctggkiAGIIE 229
Cdd:cd01391    90 AtsqdlsDKTLYKYFLSVVFSDT--LGARLGLDIVKRknWTYVAAIHGEGLNSG-ELRMAGFKELAKQ-------EGICI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 230 GHEDEDESF--QKTFDLLRRVPNlAGLYVNTVNC------LPVCRALGARGLAGKVKLITTDLFAEMS--PYFQKGTITA 299
Cdd:cd01391   160 VASDKADWNagEKGFDRALRKLR-EGLKARVIVCandmtaRGVLSAMRRLGLVGDVSVIGSDGWADRDevGYEVEANGLT 238

                         250       260
                  ....*....|....*....|...
gi 1401077077 300 SIYQQPHRQGQIAVRVMADNLTN 322
Cdd:cd01391   239 TIKQQKMGFGITAIKAMADGSQN 261
lacI PRK09526
lac repressor; Reviewed
 11-328 1.14e-08

lac repressor; Reviewed


Pssm-ID: 181929 [Multi-domain]  Cd Length: 342  Bit Score: 56.16  E-value: 1.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  11 IAHMANVSIGTVDRALHGRGGIKESTRQRILQVARQIGYTPNLAARALsVAKASARVG-VCIPREIHfFYDQLWSGVlde 89
Cdd:PRK09526   11 VARYAGVSYQTVSRVLNQASHVSAKTREKVEAAMAELNYVPNRVAQQL-AGKQSLTIGlATTSLALH-APSQIAAAI--- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  90 ARRVAQLGLQ----FLNRPVhalGEGDTAVFKELVQCGVDGIILTagnpkalTPLiDEAEANGIRVVCVST-----DAPE 160
Cdd:PRK09526   86 KSRADQLGYSvvisMVERSG---VEACQAAVNELLAQRVSGVIIN-------VPL-EDADAEKIVADCADVpclflDVSP 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 161 SrrSSIVCV--EPSLNGSLAGELMGKLVPRasKVAVVAGMLTAEDHRKKTDGFSEAFPRHctGGKIAGIIEGHEDEDESF 238
Cdd:PRK09526  155 Q--SPVNSVsfDPEDGTRLGVEHLVELGHQ--RIALLAGPESSVSARLRLAGWLEYLTDY--QLQPIAVREGDWSAMSGY 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 239 QKTFDLLRRVPNLAGLYV-NTVNCLPVCRALGARGLA--GKVKLITTDLFAEmSPYFQKGTITasIYQQPHRQGQIAVRV 315
Cdd:PRK09526  229 QQTLQMLREGPVPSAILVaNDQMALGVLRALHESGLRvpGQISVIGYDDTED-SSYFIPPLTT--IKQDFRLLGKEAVDR 305

                         330
                  ....*....|...
gi 1401077077 316 MADNLTNKIHFPP 328
Cdd:PRK09526  306 LLALSQGQAVKGS 318
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
 117-315 1.54e-08

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: 54.93  E-value: 1.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 117 KELVQCGVDGIILTAGNPKALTPLIDEAEANGIRVVCVSTDAPESRRSSIVCVEPSLN-GSLAGELMGKLVPRASKVAVV 195
Cdd:cd06301    51 ENFIAQGVDAIIVNPVDTDASAPAVDAAADAGIPLVYVNREPDSKPKGVAFVGSDDIEsGELQMEYLAKLLGGKGNIAIL 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 196 AGMLTAEDHRKKTDGFSEAFPRHcTGGKIAGIIEGHEDEDESFQKTFDLLRrvpnlAGLYVNTVNCLPVCRALGA----- 270
Cdd:cd06301   131 DGVLGHEAQILRTEGNKDVLAKY-PGMKIVAEQTANWSREKAMDIVENWLQ-----SGDKIDAIVANNDEMAIGAilale 204

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1401077077 271 -RGLAGKVKLITTDLFAEMSPYFQKGTITASIYQQPHRQGQIAVRV 315
Cdd:cd06301   205 aAGKKDDILVAGIDATPDALKAMKAGRLDATVFQDAAGQGETAVDV 250
PBP1_ABC_sugar_binding-like cd19999
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 123-283 3.88e-08

monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.


Pssm-ID: 380654 [Multi-domain]  Cd Length: 313  Bit Score: 54.24  E-value: 3.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 123 GVDGIILTAGNPKALTPLIDEAEANGIRVvcVSTDAPESRRSSI-VCVEPSLNGS-----LAGELMGKlvprASKVAV-- 194
Cdd:cd19999    60 GVDAILIDPVSATALNPVIEKAQAAGILV--VSFDQPVSSPDAInVVIDQYKWAAiqaqwLAEQLGGK----GNIVAIng 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 195 VAGMlTAEDHRKKtdGFSEAFPRHcTGGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLYVNTVNCLPVCRALGARGLa 274
Cdd:cd19999   134 VAGN-PANEARVK--AADDVFAKY-PGIKVLASVPGGWDQATAQQVMATLLATYPDIDGVLTQDGMAEGVLRAFQAAGK- 208


                  ....*....
gi 1401077077 275 gKVKLITTD 283
Cdd:cd19999   209 -DPPVMTGD 216
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
 117-313 6.57e-08

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: 53.07  E-value: 6.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 117 KELVQCGVDGIILTAGNPKALTPLIDEAEANGIRVVCVSTDAPESRRSSIVCVEPSLNGSLAGELMGKLVPRASKVAVVA 196
Cdd:cd06323    49 EDLIVRKVDALLINPTDSDAVSPAVEEANEAGIPVITVDRSVTGGKVVSHIASDNVAGGEMAAEYIAKKLGGKGKVVELQ 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 197 GMLTAEDHRKKTDGFSEAFPRHcTGGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLYV-NTVNCLPVCRALGARGLAg 275
Cdd:cd06323   129 GIPGTSAARERGKGFHNAIAKY-PKINVVASQTADFDRTKGLNVMENLLQAHPDIDAVFAhNDEMALGAIQALKAAGRK- 206

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1401077077 276 KVKLITTDLFAEMSPYFQKGTITASIYQQPHRQGQIAV 313
Cdd:cd06323   207 DVIVVGFDGTPDAVKAVKDGKLAATVAQQPEEMGAKAV 244
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 67-249 1.06e-07

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


Pssm-ID: 380501 [Multi-domain]  Cd Length: 266  Bit Score: 52.54  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  67 VGVCIPReihfFYDQLWSGVLDE-ARRVAQLGLQFLnrpVHALGEGDTA--VFKELVQCGVDGIILTAGNPKAltPLIDE 143
Cdd:cd06278     2 VGVVVGD----LSNPFYAELLEElSRALQARGLRPL---LFNVDDEDDVddALRQLLQYRVDGVIVTSATLSS--ELAEE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 144 AEANGIRVVCVSTDAPESRRSSIVCvepslNGSLAGELMGKLVPRA--SKVAVVAGMLTAEDHRKKTDGFSEAFPRHctG 221
Cdd:cd06278    73 CARRGIPVVLFNRVVEDPGVDSVSC-----DNRAGGRLAADLLLAAghRRIAFLGGPEGTSTSRERERGFRAALAEL--G 145

                         170       180
                  ....*....|....*....|....*...
gi 1401077077 222 GKIAGIIEGHEDEDESFQKTFDLLRRVP 249
Cdd:cd06278   146 LPPPAVEAGDYSYEGGYEAARRLLAAPD 173
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
 123-323 1.23e-07

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: 52.39  E-value: 1.23e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 123 GVDGIILTAGNPKALTPLIDEAEANGIRVVCVSTDAPESRRSSIVCVEPSLNGSLAGELMGKLVPRASKVAVVAGMLTAE 202
Cdd:cd19968    55 GVDGIIVSPIDVKALVPAIEAAIKAGIPVVTVDRRAEGAAPVPHVGADNVAGGREVAKFVVDKLPNGAKVIELTGTPGSS 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 203 DHRKKTDGFSEAFPRhctGGKIAGIIE--GHEDEDESFQKTFDLLRRVPNlaglYVNTVNCLPVCRALGA------RGL- 273
Cdd:cd19968   135 PAIDRTKGFHEELAA---GPKIKVVFEqtGNFERDEGLTVMENILTSLPG----PPDAIICANDDMALGAieamraAGLd 207

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1401077077 274 AGKVKLITTDLFAEMSPYFQKGTITASIYQQPHRQGQIAVRVMADNLTNK 323
Cdd:cd19968   208 LKKVKVIGFDAVPDALQAIKDGELYATVEQPPGGQARTALRILVDYLKDK 257
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 117-337 1.81e-07

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


Pssm-ID: 380544 [Multi-domain]  Cd Length: 270  Bit Score: 51.91  E-value: 1.81e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 117 KELVQCGVDGIILTAGNPKALTPLIDEAEANGIRVVCVstDAPESRRSSIVCVEPSLNGSLAGELMGKLVPRASKVAVVA 196
Cdd:cd06321    51 DDFIAQGVDLILLNAADSAGIEPAIKRAKDAGIIVVAV--DVAAEGADATVTTDNVQAGYLACEYLVEQLGGKGKVAIID 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 197 GM-LTAEDHRkkTDGFSEAFPRHcTGGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLYvnTVNCLPVCRALGARGLAG 275
Cdd:cd06321   129 GPpVSAVIDR--VNGCKEALAEY-PGIKLVDDQNGKGSRAGGLSVMTRMLTAHPDVDGVF--AINDPGAIGALLAAQQAG 203

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1401077077 276 K--VKLITTDLFAEMSPYFQK--GTITASIYQQPHRQGQIAVRVMADNLTNKIHFPPAVHLSPGVV 337
Cdd:cd06321   204 RddIVITSVDGSPEAVAALKRegSPFIATAAQDPYDMARKAVELALKILNGQEPAPELVLIPSTLV 269
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
 67-337 5.22e-07

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: 50.21  E-value: 5.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  67 VGVCIPREIHFFYDQLWSGVLDEARrvaQLGLQFLNRPVHALGEGDTAVFKELVQCGVDGIILTAGNPKalTPLIDEAEA 146
Cdd:cd06267     2 IGLIVPDISNPFFAELLRGIEDAAR---ERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLD--DELLEELLA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 147 NGIRVVCVSTDAPESRRSSIVCvepslNGSLAGELMGK-LVPR-ASKVAVVAGMLTAEDHRKKTDGFSEAFPRHCTGGKI 224
Cdd:cd06267    77 AGIPVVLIDRRLDGLGVDSVVV-----DNYAGAYLATEhLIELgHRRIAFIGGPLDLSTSRERLEGYRDALAEAGLPVDP 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 225 AGIIEGHEDEDESFQKTFDLLRRVPNLAGLYV-NTVNCLPVCRALGARGLA--GKVKLIT---TDLFAEMSPyfqkgTIT 298
Cdd:cd06267   152 ELVVEGDFSEESGYEAARELLALPPRPTAIFAaNDLMAIGALRALRELGLRvpEDISVVGfddIPLAALLTP-----PLT 226

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1401077077 299 aSIYQQPHRQGQIAVRVMADNLTNKIHFPPAVHLSPGVV 337
Cdd:cd06267   227 -TVRQPAYEMGRAAAELLLERIEGEEEPPRRIVLPTELV 264
PRK09701 PRK09701
D-allose transporter substrate-binding protein;
59-328 6.58e-07

D-allose transporter substrate-binding protein;


Pssm-ID: 182037 [Multi-domain]  Cd Length: 311  Bit Score: 50.26  E-value: 6.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  59 SVAKASARVGVCIPREIHFFYDQLWSGVLDEARRVAqLGLQFLNRPVHALGEGDTAVFKELVQCGVDGIILTAGNPKALT 138
Cdd:PRK09701   19 TSAFAAAEYAVVLKTLSNPFWVDMKKGIEDEAKTLG-VSVDIFASPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 139 PLIDEAEANGIRVVCVSTDAP-ESRRSSIVCVEP-------SLNGSLAGELMGKLVPRASKVAVV---AGMLTAEDHRKk 207
Cdd:PRK09701   98 MPVARAWKKGIYLVNLDEKIDmDNLKKAGGNVEAfvttdnvAVGAKGASFIIDKLGAEGGEVAIIegkAGNASGEARRN- 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 208 tdGFSEAFPRhctGGKIAGIIEGHEDEDESfqKTFDL----LRRVPNLAGLYV-NTVNCLPVCRALGARGLAGKVKLITT 282
Cdd:PRK09701  177 --GATEAFKK---ASQIKLVASQPADWDRI--KALDVatnvLQRNPNIKAIYCaNDTMAMGVAQAVANAGKTGKVLVVGT 249

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1401077077 283 DLFAEMSPYFQKGTITASIYQQPHRQGQIAVRVMADNLTNKIHFPP 328
Cdd:PRK09701  250 DGIPEARKMVEAGQMTATVAQNPADIGATGLKLMVDAEKSGKVIPL 295
PRK10936 PRK10936
TMAO reductase system periplasmic protein TorT; Provisional
 53-346 2.51e-06

TMAO reductase system periplasmic protein TorT; Provisional


Pssm-ID: 236801 [Multi-domain]  Cd Length: 343  Bit Score: 48.79  E-value: 2.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  53 LAARALSVAKASARVGVCIPreiHFfYDQLWSGV----LDEARRvaqLGLQFlnRPVHALGEGDTAVFKE-LVQC---GV 124
Cdd:PRK10936   35 LQYSPLLKAKKAWKLCALYP---HL-KDSYWLSVnygmVEEAKR---LGVDL--KVLEAGGYYNLAKQQQqLEQCvawGA 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 125 DGIILTAGNPKALTPLIdEAEANGIRVVCV----STDAPESRrssiVCVEPSLNGSLAGELMGKLVPRASKVAVVAgMLT 200
Cdd:PRK10936  106 DAILLGAVTPDGLNPDL-ELQAANIPVIALvngiDSPQVTTR----VGVSWYQMGYQAGRYLAQWHPKGSKPLNVA-LLP 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 201 AEDHRKKTD----GFSEAFprhcTGGKIAGIIEGHEDEDESFQKTF--DLLRRVPN---LAGlyvNTVNCLPVCRALGAR 271
Cdd:PRK10936  180 GPEGAGGSKaveqGFRAAI----AGSDVRIVDIAYGDNDKELQRNLlqELLERHPDidyIAG---SAVAAEAAIGELRGR 252

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 272 GLAGKVKLITTDLfaemSP--Y--FQKGTITASIYQQPHRQGQIAVRVMADNLTNKihfPPAVHLSPGVVM--SSNLHLF 345
Cdd:PRK10936  253 NLTDKIKLVSFYL----SHqvYrgLKRGKVLAAPSDQMVLQGRLAIDQAVRQLEGA---PVPGDVGPKILVltPKNLDSE 325


                  .
gi 1401077077 346 R 346
Cdd:PRK10936  326 D 326
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
 116-328 3.19e-06

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: 48.09  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 116 FKELVQCGVDGIIlTAGNP--KALTPLIDEAEANGIRVVCVSTDAPESRRSSIVCVEPSLNGSLAGELMGK-LVPRA--- 189
Cdd:cd19966    49 FKEAIAAKPDGIA-IMGHPgdGAYTPLIEAAKKAGIIVTSFNTDLPKLEYGDCGLGYVGADLYAAGYTLAKeLVKRGglk 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 190 --SKVAVVAGMLTAEDHRKKTDGFSEAFprhctggKIAGI---IEGHEDED----ESFQKTFDLLRRVPNLAGLYVNTVN 260
Cdd:cd19966   128 tgDRVFVPGLLPGQPYRVLRTKGVIDAL-------KEAGIkvdYLEISLEPnkpaEGIPVMTGYLAANPDVKAIVGDGGG 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 261 CL-PVCRALGARGL-AGKVKLITTDLFAEMSPYFQKGTITASIYQQPHRQGQIAVRVMAdnLTNKIHFPP 328
Cdd:cd19966   201 LTaNVAKYLKAAGKkPGEIPVAGFDLSPATVQAIKSGYVNATIDQQPYLQGYLPVLQIY--LTKKYGFSG 268
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
 109-328 3.91e-06

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: 47.65  E-value: 3.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 109 GEGDTAV----FKELVQCGVDGIILTAGNPKALTPLIDEAEANGIRVVCVSTDAPESRRSSIVCVEPSLNGSLAGELMGK 184
Cdd:cd06313    37 GNGDVSTqinqVDTLIAQGVDAIIVVPVDADALAPAVEKAKEAGIPLVGVNALIENEDLTAYVGSDDVVAGELEGQAVAD 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 185 LVPRASKVAVVAGML--TAEDHRKKtdGFSEAFPRHctgGKIAGIIE--GHEDEDESFQKTFDLLrrvpNLAGLYVNTVN 260
Cdd:cd06313   117 RLGGKGNVVILEGPIgqSAQIDRGK--GIENVLKKY---PDIKVLAEqtANWSRDEAMSLMENWL----QAYGDEIDGII 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 261 C------LPVCRALGARGLaGKVKLITTDLFAEMSPYFQKGTITASIYQQPHRQGQIAVRVMADNLTNK-------IHFP 327
Cdd:cd06313   188 AqnddmaLGALQAVKAAGR-DDIPVVGIDGIEDALQAVKSGELIATVLQDAEAQGKGAVEVAVDAVKGEgvekkyyIPFV 266


                  .
gi 1401077077 328 P 328
Cdd:cd06313   267 L 267
PBP1_ABC_sugar_binding-like cd19996
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 119-269 4.24e-06

monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.


Pssm-ID: 380651 [Multi-domain]  Cd Length: 302  Bit Score: 48.01  E-value: 4.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 119 LVQCGVDGIILTAGNPKALTPLIDEAEANGIRVVcVSTDAPESRRS-SIVCVEPSLNGSLAGELMGKLVPRASKVAV--- 194
Cdd:cd19996    54 LIAQGVDAIIVSPNSPTALLPAIEKAAAAGIPVV-LFDSGVGSDKYtAFVGVDDAAFGRVGAEWLVKQLGGKGNIIAlrg 132

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1401077077 195 VAGMLTAEDHRKktdGFSEAFPRHcTGGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLYVN----TVNCLPVCRALG 269
Cdd:cd19996   133 IAGVSVSEDRWA---GAKEVFKEY-PGIKIVGEVYADWDYAKAKQAVESLLAAYPDIDGVWSDggamTLGAIEAFEEAG 207
PRK10401 PRK10401
HTH-type transcriptional regulator GalS;
8-71 5.57e-05

HTH-type transcriptional regulator GalS;


Pssm-ID: 236681 [Multi-domain]  Cd Length: 346  Bit Score: 44.77  E-value: 5.57e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1401077077   8 IHLIAHMANVSIGTVDRALHGRGGIKESTRQRILQVARQIGYTPNLAARALSvAKASARVGVCI 71
Cdd:PRK10401    4 IRDVARQAGVSVATVSRVLNNSALVSADTREAVMKAVSELGYRPNANAQALA-TQVSDTIGVVV 66
PBP1_SalR cd01545
ligand-binding domain of DNA transcription repressor SalR, a member of the LacI-GalR family of ...
 76-170 2.79e-04

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


Pssm-ID: 380487 [Multi-domain]  Cd Length: 270  Bit Score: 42.16  E-value: 2.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  76 HFFYDQLWSGVLDEARrvaQLGLQFLNRPVHALGEGDTAVFKELVQ-CGVDGIILT---AGNPkaltPLIDEAEANGIRV 151
Cdd:cd01545    11 ASYVSALQVGALRACR---EAGYHLVVEPCDSDDEDLADRLRRFLSrSRPDGVILTpplSDDP----ALLDALDELGIPY 83

                          90
                  ....*....|....*....
gi 1401077077 152 VCVSTDAPESRRSSIVCVE 170
Cdd:cd01545    84 VRIAPGTDDDRSPSVRIDD 102
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 95-301 1.23e-03

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: 40.28  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  95 QLGLQFlnRPVHAlgEGDTAVFKELVQ------CGVDGIILTagNPKALTP-LIDEAEANGIRVVCVSTDAPESRRSSIV 167
Cdd:cd06324    28 DLGIEL--EVLYA--NRNRFKMLELAEellarpPKPDYLILV--NEKGVAPeLLELAEQAKIPVFLINNDLTDEERALLG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 168 cvEPSLN-----GSL------AGELMGK-LVPRASK--------VAVVAGMLT--AEDHRKKtdGFSEAFPRHcTGGKIA 225
Cdd:cd06324   102 --KPREKfkywlGSIvpdneqAGYLLAKaLIKAARKksddgkirVLAISGDKStpASILREQ--GLRDALAEH-PDVTLL 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1401077077 226 GIIEGHEDEDESFQKTFDLLRRVPNLAGLYV-NTVNCLPVCRALGARGL-AGK-VKLITTDLFAEMSPYFQKGTITASI 301
Cdd:cd06324   177 QIVYANWSEDEAYQKTEKLLQRYPDIDIVWAaNDAMALGAIDALEEAGLkPGKdVLVGGIDWSPEALQAVKDGELTASV 255
PBP1_ABC_sugar_binding-like cd19998
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 119-342 1.62e-03

monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are members of the pentose/hexose sugar-binding protein family of the type 1 periplasmic binding protein superfamily, which consists of two alpha/beta globular domains connected by a three-stranded hinge. This Venus flytrap-like domain undergoes transition from an open to a closed conformational state upon ligand binding. Members of this group are predicted to be involved in the transport of sugar-containing molecules across cellular and organellar membranes; however their substrate specificity is not known in detail.


Pssm-ID: 380653 [Multi-domain]  Cd Length: 302  Bit Score: 39.96  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 119 LVQCGVDGIILTAGNPKALTPLIDEAEANGIRVV---------C---VSTDAPESrrssivcvepslnGSLAGELMGKLV 186
Cdd:cd19998    55 MIAAGYDAILIYAISPTALNPVIKRACDAGIVVVafdnvvdepCaynVNTDQAKA-------------GEQTAQWLVDKL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 187 PRASKVAVVAGMLTAEDHRKKTDGFSEAFPRHcTGGKIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLYVNtVNCLPVCR 266
Cdd:cd19998   122 GGKGNILMVRGVPGTSVDRDRYEGAKEVFKKY-PDIKVVAEYYGNWDDGTAQKAVADALAAHPDVDGVWTQ-GGETGVIK 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 267 ALGARGLagKVKLITTD-------LFAEMSPYFQKGtitaSIYQQPHRQGQIAVRVMADNLTNKiHFPPAVHLSPGVVMS 339
Cdd:cd19998   200 ALQAAGH--PLVPVGGEaengfrkAMLEPLANGLPG----ISAGSPPALSAVALKLAVAVLEGE-KEPKTIELPLPWVTT 272


                  ...
gi 1401077077 340 SNL 342
Cdd:cd19998   273 DDV 275
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 67-273 2.32e-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: 39.13  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077  67 VGVCIPREIHFFYDQLWSGVLDEARRvaqLGLQFLNRPVHALGEGDTAVFKELVQCGVDGIILTagNPKALTPLIDEAEA 146
Cdd:cd06285     2 IGVLVSDLSNPFYAELVEGIEDAARE---RGYTVLLADTGDDPERELAALDSLLSRRVDGLIIT--PARDDAPDLQELAA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 147 NGIRVVCVSTDAPESRRSSIVCvepslNGSLAGELMGK----LVPRasKVAVVAGMLTAEDHRKKTDGFSEAFPRHCTGG 222
Cdd:cd06285    77 RGVPVVLVDRRIGDTALPSVTV-----DNELGGRLATRhlleLGHR--RIAVVAGPLNASTGRDRLRGYRRALAEAGLPV 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1401077077 223 KIAGIIEGHEDEDESFQKTFDLLRRVPNLAGLY-VNTVNCLPVCRALGARGL 273
Cdd:cd06285   150 PDERIVPGGFTIEAGREAAYRLLSRPERPTAVFaANDLMAIGVLRAARDLGL 201
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
 119-219 5.60e-03

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: 37.97  E-value: 5.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077 119 LVQCGVDGIILTAGNPKALTPLIDEAEANGIRVVCVSTDAPESRRSSIVC------VEpslNGSLAGELMGK-LVPRASK 191
Cdd:cd06309    51 LIAQGVDAILISPIDATGWDPVLKEAKDAGIPVILVDRTIDGEDGSLYVTfigsdfVE---EGRRAAEWLVKnYKGGKGN 127

                          90       100
                  ....*....|....*....|....*...
gi 1401077077 192 VAVVAGMLTAEDHRKKTDGFSEAFPRHC 219
Cdd:cd06309   128 VVELQGTAGSSVAIDRSKGFREVIKKHP 155
PRK10339 PRK10339
DNA-binding transcriptional repressor EbgR; Provisional
 11-62 5.67e-03

DNA-binding transcriptional repressor EbgR; Provisional


Pssm-ID: 182389 [Multi-domain]  Cd Length: 327  Bit Score: 38.20  E-value: 5.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1401077077  11 IAHMANVSIGTVDRALHGRG--GIKESTRQRILQVARQIGYTPNLAARALSVAK 62
Cdd:PRK10339    7 IAIEAGVSLATVSRVLNDDPtlNVKEETKHRILEIAEKLEYKTSSARKLQTGAV 60
PRK14987 PRK14987
HTH-type transcriptional regulator GntR;
1-152 8.29e-03

HTH-type transcriptional regulator GntR;


Pssm-ID: 184949 [Multi-domain]  Cd Length: 331  Bit Score: 37.70  E-value: 8.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1401077077   1 MTKPRSGIHLIAHMANVSIGTVDRALHGRGGIKESTRQRILQVARQIGYTPNLAARALSVAKASArVGVCIPReihfFYD 80
Cdd:PRK14987    1 MKKKRPVLQDVADRVGVTKMTVSRFLRNPEQVSVALRGKIAAALDELGYIPNRAPDILSNATSRA-IGVLLPS----LTN 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1401077077  81 QLWSGVLDEARRVAQL-GLQFLNRPVHALGEGDTAVFKELVQCGVDGIILTAGN--PKALTPLideaEANGIRVV 152
Cdd:PRK14987   76 QVFAEVLRGIESVTDAhGYQTMLAHYGYKPEMEQERLESMLSWNIDGLILTERThtPRTLKMI----EVAGIPVV 146
 
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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