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Conserved domains on  [gi|535980227|gb|ERA80022|]
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autoinducer 2-binding protein lsrB [Escherichia coli HVH 157 (4-3406229)]

Protein Classification

autoinducer 2 ABC transporter substrate-binding protein( domain architecture ID 11487778)

autoinducer 2 ABC transporter substrate-binding protein LsrB serves as the primary receptor for the import of the quorum-sensing signal autoinducer 2 (AI-2) into the cell

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK15408 PRK15408
autoinducer 2 ABC transporter substrate-binding protein LsrB;
6-340 0e+00

autoinducer 2 ABC transporter substrate-binding protein LsrB;


:

Pssm-ID: 237961  Cd Length: 336  Bit Score: 653.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227   6 IKKIAVISTLSLAAFTLNAYAAERIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGY 85
Cdd:PRK15408   2 KKKIALVSALGIALISMTVQAAERIAFIPKLVGVGFFTSGGNGAKEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  86 NAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYYINQGTPAQLGGMLVDMAANQVKKEKAKVAFFYSSPTVT 165
Cdd:PRK15408  82 NAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYYINQGTPEQLGSMLVEMAAKQVGKDKAKVAFFYSSPTVT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 166 DQNQWVKEAKDKIAKDHPGWEVVTTQFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAENLKNTSVAIVGF 245
Cdd:PRK15408 162 DQNQWVKEAKAKIAKEHPGWEIVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRDKVAIVGF 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 246 STPNVMRPYVERGTVKEFGLWDVVQQGKISVYVADALLKKGDMNTGDKLDIPGVGQVEVSPNSVQGYSYEAKGNGIVLLP 325
Cdd:PRK15408 242 STPNVMRPYVKRGTVKEFGLWDVVQQGKISVYVANELLKKGKLNVGDSLDVPGIGKVEVSPNSVQGYDYEAKGNGIVLLP 321

                        330
                 ....*....|....*
gi 535980227 326 ERVVFTKENIDKYDF 340
Cdd:PRK15408 322 ERVVFTKENIDKYDF 336
 
Name Accession Description Interval E-value
PRK15408 PRK15408
autoinducer 2 ABC transporter substrate-binding protein LsrB;
6-340 0e+00

autoinducer 2 ABC transporter substrate-binding protein LsrB;


Pssm-ID: 237961  Cd Length: 336  Bit Score: 653.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227   6 IKKIAVISTLSLAAFTLNAYAAERIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGY 85
Cdd:PRK15408   2 KKKIALVSALGIALISMTVQAAERIAFIPKLVGVGFFTSGGNGAKEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  86 NAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYYINQGTPAQLGGMLVDMAANQVKKEKAKVAFFYSSPTVT 165
Cdd:PRK15408  82 NAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYYINQGTPEQLGSMLVEMAAKQVGKDKAKVAFFYSSPTVT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 166 DQNQWVKEAKDKIAKDHPGWEVVTTQFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAENLKNTSVAIVGF 245
Cdd:PRK15408 162 DQNQWVKEAKAKIAKEHPGWEIVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRDKVAIVGF 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 246 STPNVMRPYVERGTVKEFGLWDVVQQGKISVYVADALLKKGDMNTGDKLDIPGVGQVEVSPNSVQGYSYEAKGNGIVLLP 325
Cdd:PRK15408 242 STPNVMRPYVKRGTVKEFGLWDVVQQGKISVYVANELLKKGKLNVGDSLDVPGIGKVEVSPNSVQGYDYEAKGNGIVLLP 321

                        330
                 ....*....|....*
gi 535980227 326 ERVVFTKENIDKYDF 340
Cdd:PRK15408 322 ERVVFTKENIDKYDF 336
PBP1_LsrB_Quorum_Sensing cd20003
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ...
 29-336 1.24e-158

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: 445.57  E-value: 1.24e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQR 108
Cdd:cd20003    1 TIAMIPKLVGVPYFTAAGQGAQEAAKELGVDVTYDGPTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 109 GVKVLTWDSDTKPECRSYYINQGTPAQLGGMLVDMAANQvKKEKAKVAFFYSSPTVTDQNQWVKEAKDKIAKDHPGWEVV 188
Cdd:cd20003   81 GIKVVTWDSDVNPDARDFFVNQATPEGIGKTLVDMVAEQ-TGEKGKVAIVTSSPTATNQNAWIKAMKAYIAEKYPDMKIV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 189 TTQFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAENLKNT-SVAIVGFSTPNVMRPYVERGTVKEFGLWD 267
Cdd:cd20003  160 TTQYGQEDPAKSLQVAENILKAYPDLKAIIAPDSVALPGAAEAVEQLGRTgKVAVTGLSTPNVMRPYVKDGTVKSVVLWD 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 535980227 268 VVQQGKISVYVADALLKKGDMNTGDKLDIPGVGQVEVSPnsvqgysyeaKGNGIVLLPERVVFTKENID 336
Cdd:cd20003  240 VVDLGYLAVYVARALADGTLLKVGDFFVAGRLGTFTVVP----------KGNGIILLGEPLIFTKENID 298
RhaS TIGR02637
rhamnose ABC transporter, rhamnose-binding protein; This sugar-binding component of ABC ...
 30-340 4.33e-74

rhamnose ABC transporter, rhamnose-binding protein; This sugar-binding component of ABC transporter complexes is found in rhamnose catabolism operon contexts. Mutation of this gene in Rhizobium leguminosarum abolishes rhamnose transport and prevents growth on rhamnose as a carbon source.


Pssm-ID: 131685  Cd Length: 302  Bit Score: 230.90  E-value: 4.33e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227   30 IAFIPKLVGVGFFTSGGNGALEAGKELG-VDVTYDGPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQR 108
Cdd:TIGR02637   1 IGLVVKSLGNPFFEAANKGAEEAAKELGsVYIIYTGPTGTTAEGQIEVVNSLIAQKVDAIAISANDPDALVPALKKAMKR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  109 GVKVLTWDSDTKPECRSYYINQGTPAQLGGMLVDMAANQVkKEKAKVAFFYSSPTVTDQNQWVKEAKDKIAK-DHPGWEV 187
Cdd:TIGR02637  81 GIKVVTWDSGVAPEGRNLFLNQASADLIGRTQVQLAAEQI-GNGGEIAILSAASTATNQNAWIEIMKKELKDpKYPKVKL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  188 VTTQFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAENLKNT-SVAIVGFSTPNVMRPYVERGTVKEFGLW 266
Cdd:TIGR02637 160 VATVYGDDDAQKSYQEAQGLLKSYPNLKGIIAPTTVGIKAAAQAVSDAKLIgKVKLTGLGLPSEMAKYVKNGTVKAFALW 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 535980227  267 DVVQQGKISVYVADALL-KKGDMNTGDKLDIPGVGQVEVSPNsvqgysyeakGNGIVLLPerVVFTKENIDKYDF 340
Cdd:TIGR02637 240 NPIDLGYSAAYTAYRLSsGEITGKPGETFKAGRMGEYTIGDN----------GVAALGPP--FVFDADNIDQFSK 302
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 30-284 3.47e-57

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: 185.98  E-value: 3.47e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227   30 IAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRG 109
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  110 VKVLTWDSDTKPECRSYYINQgTPAQLGGMLVDMAANQVKKeKAKVAFFYSSPTVTDQNQWVKEAKDKIAKDHPGWEVVT 189
Cdd:pfam13407  81 IPVVTFDSDAPSSPRLAYVGF-DNEAAGEAAGELLAEALGG-KGKVAILSGSPGDPNANERIDGFKKVLKEKYPGIKVVA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  190 TQFGYN-DATKSLQTAEGIIKAYAD-LDAIIAPDANALPAAAQAAENL-KNTSVAIVGFSTPNVMRPYVERGTVKEFGLW 266
Cdd:pfam13407 159 EVEGTNwDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAgLAGKVVVTGFDATPEALEAIKDGTIDATVLQ 238

                         250
                  ....*....|....*...
gi 535980227  267 DVVQQGKISVYVADALLK 284
Cdd:pfam13407 239 DPYGQGYAAVELAAALLK 256
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 7-287 1.06e-52

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: 175.88  E-value: 1.06e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227   7 KKIAVISTLSLAAFTLNAYAAE------------RIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDgPTEPSVSGQV 74
Cdd:COG1879    1 KRLALLAAVLALALALAACGSAaaeaaaaaakgkTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVV-DAEGDAAKQI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  75 QLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYYINQgTPAQLGGMLVDMAANQVkKEKAK 154
Cdd:COG1879   80 SQIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGS-DNYAAGRLAAEYLAKAL-GGKGK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 155 VAFFYSSPTVTDQNQWVKEAKDKIAKdHPGWEVVTTQFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAEN 234
Cdd:COG1879  158 VAILTGSPGAPAANERTDGFKEALKE-YPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKA 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 535980227 235 L-KNTSVAIVGFSTPNVMRPYVERGTVKEFGLWDVVQQGKISVYVADALLKKGD 287
Cdd:COG1879  237 AgRKGDVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKE 290
 
Name Accession Description Interval E-value
PRK15408 PRK15408
autoinducer 2 ABC transporter substrate-binding protein LsrB;
6-340 0e+00

autoinducer 2 ABC transporter substrate-binding protein LsrB;


Pssm-ID: 237961  Cd Length: 336  Bit Score: 653.02  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227   6 IKKIAVISTLSLAAFTLNAYAAERIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGY 85
Cdd:PRK15408   2 KKKIALVSALGIALISMTVQAAERIAFIPKLVGVGFFTSGGNGAKEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  86 NAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYYINQGTPAQLGGMLVDMAANQVKKEKAKVAFFYSSPTVT 165
Cdd:PRK15408  82 NAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYYINQGTPEQLGSMLVEMAAKQVGKDKAKVAFFYSSPTVT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 166 DQNQWVKEAKDKIAKDHPGWEVVTTQFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAENLKNTSVAIVGF 245
Cdd:PRK15408 162 DQNQWVKEAKAKIAKEHPGWEIVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDANALPAAAQAAENLKRDKVAIVGF 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 246 STPNVMRPYVERGTVKEFGLWDVVQQGKISVYVADALLKKGDMNTGDKLDIPGVGQVEVSPNSVQGYSYEAKGNGIVLLP 325
Cdd:PRK15408 242 STPNVMRPYVKRGTVKEFGLWDVVQQGKISVYVANELLKKGKLNVGDSLDVPGIGKVEVSPNSVQGYDYEAKGNGIVLLP 321

                        330
                 ....*....|....*
gi 535980227 326 ERVVFTKENIDKYDF 340
Cdd:PRK15408 322 ERVVFTKENIDKYDF 336
PBP1_LsrB_Quorum_Sensing cd20003
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ...
 29-336 1.24e-158

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: 445.57  E-value: 1.24e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQR 108
Cdd:cd20003    1 TIAMIPKLVGVPYFTAAGQGAQEAAKELGVDVTYDGPTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 109 GVKVLTWDSDTKPECRSYYINQGTPAQLGGMLVDMAANQvKKEKAKVAFFYSSPTVTDQNQWVKEAKDKIAKDHPGWEVV 188
Cdd:cd20003   81 GIKVVTWDSDVNPDARDFFVNQATPEGIGKTLVDMVAEQ-TGEKGKVAIVTSSPTATNQNAWIKAMKAYIAEKYPDMKIV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 189 TTQFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAENLKNT-SVAIVGFSTPNVMRPYVERGTVKEFGLWD 267
Cdd:cd20003  160 TTQYGQEDPAKSLQVAENILKAYPDLKAIIAPDSVALPGAAEAVEQLGRTgKVAVTGLSTPNVMRPYVKDGTVKSVVLWD 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 535980227 268 VVQQGKISVYVADALLKKGDMNTGDKLDIPGVGQVEVSPnsvqgysyeaKGNGIVLLPERVVFTKENID 336
Cdd:cd20003  240 VVDLGYLAVYVARALADGTLLKVGDFFVAGRLGTFTVVP----------KGNGIILLGEPLIFTKENID 298
PBP1_LsrB_Quorum_Sensing-like cd06302
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ...
 29-336 1.85e-108

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: 318.42  E-value: 1.85e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQR 108
Cdd:cd06302    1 KIAFVPKVVGIPYFDAAEEGAKKAAKELGVEVVYTGPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 109 GVKVLTWDSDTKPECRSYYINQGTPAQLGGMLVDMAANQVkKEKAKVAFFYSSPTVTDQNQWVKEAKDKIAKDHPGWEVV 188
Cdd:cd06302   81 GIKVITWDSDAPPSARDYFVNQADDEGLGEALVDSLAKEI-GGKGKVAILSGSLTATNLNAWIKAMKEYLKSKYPDIELV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 189 TTQFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAENL-KNTSVAIVGFSTPNVMRPYVERGTVKEFGLWD 267
Cdd:cd06302  160 DTYYTDDDQQKAYTQAQNLIQAYPDLKGIIGVSTTAPPAAAQAVEEAgKTGKVAVTGIGLPNTARPYLKDGSVKEGVLWD 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 535980227 268 VVQQGKISVYVADALLkKGDMNTGDKLDIPGVGQVEVSPNsvqgysyeakgNGIVLLPERVVFTKENID 336
Cdd:cd06302  240 PAKLGYLTVYAAYQLL-KGKGFTEDSDDVGTGGKVKVDVA-----------GGEILLGPPLVFTKDNVD 296
PBP1_ABC_rhamnose cd20000
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ...
 29-336 5.29e-80

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: 246.01  E-value: 5.29e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQR 108
Cdd:cd20000    1 RIAFLPKSLGNPYFDAARDGAKEAAKELGGELIFVGPTTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 109 GVKVLTWDSDTKPECRSYYINQGTPAQLGGMLVDMAANQVkKEKAKVAFFYSSPTVTDQNQWVKEAKDKIAKD-HPGWEV 187
Cdd:cd20000   81 GIKVVTFDSDVAPEARDLFVNQADADGIGRAQVDMMAELI-GGEGEFAILSATPTATNQNAWIDAMKKELASPeYAGMKL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 188 VTTQFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAENLKNT-SVAIVGFSTPNVMRPYVERGTVKEFGLW 266
Cdd:cd20000  160 VKVAYGDDDAQKSYQEAEALLQAYPDLKGIIAPTTVGIAAAARALEDSGLKgKVKVTGLGLPSEMAKYVKDGTVPAFALW 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 535980227 267 DVVQQGKISVYVADALLKKG-DMNTGDKLDIPGVGqvevspnsvqgySYEAKGNGIVLLPERVVFTKENID 336
Cdd:cd20000  240 NPIDLGYLAAYAAAALAQGEiTGKEGETFTAGRLG------------EYTVGEGGEVVLGPPFVFTADNID 298
RhaS TIGR02637
rhamnose ABC transporter, rhamnose-binding protein; This sugar-binding component of ABC ...
 30-340 4.33e-74

rhamnose ABC transporter, rhamnose-binding protein; This sugar-binding component of ABC transporter complexes is found in rhamnose catabolism operon contexts. Mutation of this gene in Rhizobium leguminosarum abolishes rhamnose transport and prevents growth on rhamnose as a carbon source.


Pssm-ID: 131685  Cd Length: 302  Bit Score: 230.90  E-value: 4.33e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227   30 IAFIPKLVGVGFFTSGGNGALEAGKELG-VDVTYDGPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQR 108
Cdd:TIGR02637   1 IGLVVKSLGNPFFEAANKGAEEAAKELGsVYIIYTGPTGTTAEGQIEVVNSLIAQKVDAIAISANDPDALVPALKKAMKR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  109 GVKVLTWDSDTKPECRSYYINQGTPAQLGGMLVDMAANQVkKEKAKVAFFYSSPTVTDQNQWVKEAKDKIAK-DHPGWEV 187
Cdd:TIGR02637  81 GIKVVTWDSGVAPEGRNLFLNQASADLIGRTQVQLAAEQI-GNGGEIAILSAASTATNQNAWIEIMKKELKDpKYPKVKL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  188 VTTQFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAENLKNT-SVAIVGFSTPNVMRPYVERGTVKEFGLW 266
Cdd:TIGR02637 160 VATVYGDDDAQKSYQEAQGLLKSYPNLKGIIAPTTVGIKAAAQAVSDAKLIgKVKLTGLGLPSEMAKYVKNGTVKAFALW 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 535980227  267 DVVQQGKISVYVADALL-KKGDMNTGDKLDIPGVGQVEVSPNsvqgysyeakGNGIVLLPerVVFTKENIDKYDF 340
Cdd:TIGR02637 240 NPIDLGYSAAYTAYRLSsGEITGKPGETFKAGRMGEYTIGDN----------GVAALGPP--FVFDADNIDQFSK 302
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 30-284 3.47e-57

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: 185.98  E-value: 3.47e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227   30 IAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRG 109
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  110 VKVLTWDSDTKPECRSYYINQgTPAQLGGMLVDMAANQVKKeKAKVAFFYSSPTVTDQNQWVKEAKDKIAKDHPGWEVVT 189
Cdd:pfam13407  81 IPVVTFDSDAPSSPRLAYVGF-DNEAAGEAAGELLAEALGG-KGKVAILSGSPGDPNANERIDGFKKVLKEKYPGIKVVA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  190 TQFGYN-DATKSLQTAEGIIKAYAD-LDAIIAPDANALPAAAQAAENL-KNTSVAIVGFSTPNVMRPYVERGTVKEFGLW 266
Cdd:pfam13407 159 EVEGTNwDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAgLAGKVVVTGFDATPEALEAIKDGTIDATVLQ 238

                         250
                  ....*....|....*...
gi 535980227  267 DVVQQGKISVYVADALLK 284
Cdd:pfam13407 239 DPYGQGYAAVELAAALLK 256
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 7-287 1.06e-52

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: 175.88  E-value: 1.06e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227   7 KKIAVISTLSLAAFTLNAYAAE------------RIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDgPTEPSVSGQV 74
Cdd:COG1879    1 KRLALLAAVLALALALAACGSAaaeaaaaaakgkTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVV-DAEGDAAKQI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  75 QLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYYINQgTPAQLGGMLVDMAANQVkKEKAK 154
Cdd:COG1879   80 SQIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDRVAYVGS-DNYAAGRLAAEYLAKAL-GGKGK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 155 VAFFYSSPTVTDQNQWVKEAKDKIAKdHPGWEVVTTQFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAEN 234
Cdd:COG1879  158 VAILTGSPGAPAANERTDGFKEALKE-YPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKA 236

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 535980227 235 L-KNTSVAIVGFSTPNVMRPYVERGTVKEFGLWDVVQQGKISVYVADALLKKGD 287
Cdd:COG1879  237 AgRKGDVKVVGFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLKGKE 290
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
 29-287 1.88e-40

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: 142.71  E-value: 1.88e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGPtEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQR 108
Cdd:cd01536    1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDA-QGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 109 GVKVLTWDSD-TKPECRSYYInqGTPAQLGG-MLVDMAANQVKKeKAKVAFFYSSPTVTDQNQWVKEAKDKIAKdHPGWE 186
Cdd:cd01536   80 GIPVVAVDTDiDGGGDVVAFV--GTDNYEAGkLAGEYLAEALGG-KGKVAILEGPPGSSTAIDRTKGFKEALKK-YPDIE 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 187 VVTTQFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAENL-KNTSVAIVGFSTPNVMRPYVERGTVKEFGL 265
Cdd:cd01536  156 IVAEQPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAgRTGDIKIVGVDGTPEALKAIKDGELDATVA 235

                        250       260
                 ....*....|....*....|..
gi 535980227 266 WDVVQQGKISVYVADALLKKGD 287
Cdd:cd01536  236 QDPYLQGYLAVEAAVKLLNGEK 257
PBP1_LsrB_Quorum_Sensing-like cd20002
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
 30-336 1.90e-40

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: 143.61  E-value: 1.90e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  30 IAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRG 109
Cdd:cd20002    2 IVTVVKLAGIPWFNRMEQGVKKAGKEFGVNAYQVGPADADPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREKG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 110 VKVLTWDSDTKPEcRSYYINQGTPAQLGGMLVDMAAnQVKKEKAKVAFFYSSPTVTDQNQWVKEAKDKIAKDHPGWEVVT 189
Cdd:cd20002   82 IVVITHESPGQKG-ADWDVELIDNEKFGEAQMELLA-KEMGGKGEYAIFVGSLTVPLHNLWADAAVEYQKEKYPNMKQVT 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 190 TQF-GYNDATKSLQTAEGIIKAYADLDAIIA--PDANALPAAAQAAENLKNtSVAIVGFSTPNVMRPYVERGTVKEFGLW 266
Cdd:cd20002  160 DRIpGGEDVDVSRQTTLELLKAYPDLKGIISfgSLGPIGAGQALREKGLKG-KVAVVGTVIPSQAAAYLKEGSITEGYLW 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 267 DVVQQGKISVYVADALLKKGDMNTGDKLDIPGVGQVEVSpnsvqgysyeakgNGIVLLPERVVFTKENID 336
Cdd:cd20002  239 DPADAGYAMVYIAKMLLDGKRKEIGDGFEIPGKGTPDID-------------GNVIIFDAPLEITKENAD 295
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
 29-297 3.44e-39

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: 139.64  E-value: 3.44e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQR 108
Cdd:cd06314    1 TFALVPKGLNNPFWDLAEAGAEKAAKELGVNVEFVGPQKSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 109 GVKVLTWDSDTKPECRSYYInqGTPAQLGGMLVDMAANQVKKEKAKVAFFYSSPTVTDQNQWVKEAKDKIAKdHPGWEVV 188
Cdd:cd06314   81 GIPVITFDSDAPDSKRLAYI--GTDNYEAGREAGELMKKALPGGGKVAIITGGLGADNLNERIQGFKDALKG-SPGIEIV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 189 TTQFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAENLKNTS-VAIVGFSTPNVMRPYVERGTVKefGLwd 267
Cdd:cd06314  158 DPLSDNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKVGkVKIVGFDTLPETLQGIKDGVIA--AT-- 233

                        250       260       270
                 ....*....|....*....|....*....|....
gi 535980227 268 VVQQ----GKISVYVADALLKKGDMnTGDKLDIP 297
Cdd:cd06314  234 VGQRpyemGYLSVKLLYKLLKGGKP-VPDVIDTG 266
PBP1_LsrB_Quorum_Sensing-like cd20001
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
 29-336 1.95e-36

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: 133.17  E-value: 1.95e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQR 108
Cdd:cd20001    1 TIAVVVKVTGIAWFDRMETGVEQFAKDTGVNVYQIGPATADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 109 GVKVLTWDSDTKPECrSYYINQGTPAQLGGMLVDMAANQVkKEKAKVAFFYSSPTVTDQNQWVKEAKDKIAKDHPGWEVV 188
Cdd:cd20001   81 GIVVITHEASNLKNV-DYDVEAFDNAAYGAFIMDKLAEAM-GGKGKYVTFVGSLTSTSHMEWANAAVAYQKANYPDMLLV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 189 T-TQFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAENLKNT-SVAIVGFSTPNVMRPYVERGTVKEFGLW 266
Cdd:cd20001  159 TdRVETNDDSETAYEKAKELLKTYPDLKGIVGCSSSDVPGAARAVEELGLQgKIAVVGTGLPSVAGEYLEDGTIDYIQFW 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 535980227 267 DVVQQGKISVYVADALLKKGDMNTGDKLDIPGVGQVEV-SPNSVQgysyeakGNGIvllperVVFTKENID 336
Cdd:cd20001  239 DPADAGYAMNALAVMVLEGEKITDGTDLGVPGYEKVTVgKGKVLY-------GNAW------LIVTKDNVD 296
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 29-284 1.15e-27

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: 109.24  E-value: 1.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGP-TEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQ 107
Cdd:cd20004    1 CIAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWRGPsREDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 108 RGVKVLTWDSDTKPECRSYYInqGTPAQLGGMLvdmAANQVKKE---KAKVAFFYSSPTV--TDQnqwvKEA--KDKIAK 180
Cdd:cd20004   81 QGIPVVIIDSDLGGDAVISFV--ATDNYAAGRL---AAKRMAKLlngKGKVALLRLAKGSasTTD----RERgfLEALKK 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 181 DHPGWEVVTTQFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAENLK-NTSVAIVGFSTPNVMRPYVERGT 259
Cdd:cd20004  152 LAPGLKVVDDQYAGGTVGEARSSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGlAGKVKFIGFDASDLLLDALRAGE 231

                        250       260
                 ....*....|....*....|....*....
gi 535980227 260 VkeFGLwdVVQQ----GKISVYVADALLK 284
Cdd:cd20004  232 I--SAL--VVQDpyrmGYLGVKTAVAALR 256
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 29-261 2.71e-27

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: 108.09  E-value: 2.71e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGP-TEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQ 107
Cdd:cd20008    1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLGPaTEADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAADA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 108 rGVKVLTWDS--DTKPECRSYYINQGTPAQLGGmlvDMAANQVKK---EKAKVAFFYSSPTVTDQNQWVKEAKDKIAKDH 182
Cdd:cd20008   81 -GIPVVLVDSgaNTDDYDAFLATDNVAAGALAA---DELAELLKAsggGKGKVAIISFQAGSQTLVDREEGFRDYIKEKY 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 183 PGWEVVTTQFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALP-AAAQAAENLKNTSVAIVGFSTPNVMRPYVERGTVK 261
Cdd:cd20008  157 PDIEIVDVQYSDGDIAKALNQTTDLLTANPDLVGIFGANNPSAVgVAQALAEAGKAGKIVLVGFDSSPDEVALLKSGVIK 236
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 29-288 2.39e-25

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: 102.70  E-value: 2.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQR 108
Cdd:cd20007    1 TIALVPGVTGDPFYITMQCGAEAAAKELGVELDVQGPPTFDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 109 GVKVLTWDSD-TKPECRSYYInqGTPAQLGGMLVDMAANQVKKEKAKVAFFYSSPTVTDQNQWVKEAKDKIAKdHPGWEV 187
Cdd:cd20007   81 GIKVVTVDTTlGDPSFVLSQI--ASDNVAGGALAAEALAELIGGKGKVLVINSTPGVSTTDARVKGFAEEMKK-YPGIKV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 188 VTTQFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAENL-KNTSVAIVGFSTPNVMRPYVERGTVKEFGLW 266
Cdd:cd20007  158 LGVQYSENDPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAgKTGKVKVVGFDASPAQVEQLKAGTIDALIAQ 237

                        250       260
                 ....*....|....*....|..
gi 535980227 267 DVVQQGKISVYVADALLKKGDM 288
Cdd:cd20007  238 KPAEIGYLAVEQAVAALTGKPV 259
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 29-286 1.10e-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: 101.14  E-value: 1.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVG--FFTSGGNGALEAGKELGVDVTYDGPT-EPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRA 105
Cdd:cd20006    1 KIALILKSSDPNsdFWQTVKSGAEAAAKEYGVDLEFLGPEsEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 106 MQRGVKVLTWDSDTKPECRSYYInqGTP-AQLGGMLVDMAANQVkKEKAKVAFFYSSPTVTDQNQWVKEAKDKIAKdHPG 184
Cdd:cd20006   81 KKAGIPVITIDSPVNSKKADSFV--ATDnYEAGKKAGEKLASLL-GEKGKVAIVSFVKGSSTAIEREEGFKQALAE-YPN 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 185 WEVVTTQFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAENLKNT-SVAIVGFSTPNVMRPYVERGTVKEF 263
Cdd:cd20006  157 IKIVETEYCDSDEEKAYEITKELLSKYPDINGIVALNEQSTLGAARALKELGLGgKVKVVGFDSSVEEIQLLEEGIIDAL 236

                        250       260
                 ....*....|....*....|....*...
gi 535980227 264 glwdVVQQ----GKISV-YVADALLKKG 286
Cdd:cd20006  237 ----VVQNpfnmGYLSVqAAVDLLNGKK 260
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 29-258 8.74e-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: 380660 [Multi-domain]  Cd Length: 274  Bit Score: 98.47  E-value: 8.74e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGP-TEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQ 107
Cdd:cd20005    1 YIAVISKGFQHQFWKAVKKGAEQAAKELGVKITFEGPdTESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 108 RGVKVLTWDSDTkpECRSYYINQGTP-AQLGGMLVDMAANQVkKEKAKVAFFYSSPTVTDQNQWVKEAKDKIAKDHPGWE 186
Cdd:cd20005   81 KGIPVVTFDSGV--PSDLPLATVATDnYAAGALAADHLAELI-GGKGKVAIVAHDATSETGIDRRDGFKDEIKEKYPDIK 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 535980227 187 VVTTQFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAENLKNT-SVAIVGFSTPNVMRPYVERG 258
Cdd:cd20005  158 VVNVQYGVGDHAKAADIAKAILQANPDLKGIYATNEGAAIGVANALKEMGKLgKIKVVGFDSGEAQIDAIKNG 230
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 29-290 2.67e-22

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


Pssm-ID: 380533 [Multi-domain]  Cd Length: 272  Bit Score: 94.33  E-value: 2.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGP-TEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQ 107
Cdd:cd06310    1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFVGPeSEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 108 RGVKVLTWDSDTKPEcrsyyINQGTPA----QLGGMLVDMAANQVKKeKAKVAFFYSSPTVTDQNQWVKEAKDKIAKDHP 183
Cdd:cd06310   81 KGIPVIVIDSGIKGD-----AYLSYIAtdnyAAGRLAAQKLAEALGG-KGKVAVLSLTAGNSTTDQREEGFKEYLKKHPG 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 184 GWEVVTTQFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAENLKNT-SVAIVGFSTPNVMRPYVERGTVKe 262
Cdd:cd06310  155 GIKVLASQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSgQIKIVGFDSQEELLDALKNGKID- 233

                        250       260       270
                 ....*....|....*....|....*....|..
gi 535980227 263 fGLwdVVQQ----GKISVYVADALLKKGDMNT 290
Cdd:cd06310  234 -AL--VVQNpyeiGYEGIKLALKLLKGEEVPK 262
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
 32-260 4.15e-22

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: 93.94  E-value: 4.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  32 FIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVK 111
Cdd:cd19969    4 MVTFKSGHPYWDDVKEGFEDAGAELGVKTEYTGPATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 112 VLTWDSDTKPECRSYYINQGTPAQlGGMLVDMAANQVkKEKAKVAFFYSSPTvTDQNQWVKEAKDKIAKdHPGWEVVTTQ 191
Cdd:cd19969   84 VVTFDSDAPESKRISYVGTDNYEA-GYAAAEKLAELL-GGKGKVAVLTGPGQ-PNHEERVEGFKEAFAE-YPGIEVVAVG 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 192 FGYNDATKSLQTAEGIIKAYADLDAIIAPDANALP-AAAQAAENLKNTSVAIVGFSTPNVMRPYVERGTV 260
Cdd:cd19969  160 DDNDDPEKAAQNTSALLQAHPDLVGIFGVDASGGVgAAQAVREAGKTGKVKIVAFDDDPETLDLIKDGVI 229
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 29-219 7.65e-21

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: 90.51  E-value: 7.65e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGPTEPSvSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQR 108
Cdd:cd06317    1 TIALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDP-SKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 109 GVKVLTWDSDTKPECRSYYINqGTPAQLGGMLVDMAANQVKKE---KAKVAFFYSSPTVTdQNQWVKEAKDKIaKDHPGW 185
Cdd:cd06317   80 GIPVIAYDAVIPSDFQAAQVG-VDNLEGGKEIGKYAADYIKAElggQAKIGVVGALSSLI-QNQRQKGFEEAL-KANPGV 156

                        170       180       190
                 ....*....|....*....|....*....|....
gi 535980227 186 EVVTTQFGYNDATKSLQTAEGIIKAYADLDAIIA 219
Cdd:cd06317  157 EIVATVDGQNVQEKALSAAENLLTANPDLDAIYA 190
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
 29-219 9.83e-21

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: 90.40  E-value: 9.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYD-GPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQ 107
Cdd:cd06320    1 KIGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVQaAPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 108 RGVKVLTWDSDTKPECRSYYINQGTP------AQLGGMLVDMAANQVKKeKAKVAFFYSSPTVTDQNQWVKEAKDKIAKD 181
Cdd:cd06320   81 KGIPVINLDDAVDADALKKAGGKVTSfigtdnVAAGALAAEYIAEKLPG-GGKVAIIEGLPGNAAAEARTKGFKETFKKA 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 535980227 182 hPGWEVVTTQFGYNDATKSLQTAEGIIKAYADLDAIIA 219
Cdd:cd06320  160 -PGLKLVASQPADWDRTKALDAATAILQAHPDLKGIYA 196
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 41-219 1.15e-18

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: 84.25  E-value: 1.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  41 FFTSGGNGALEAGKELGVDVTYDGPtEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDTK 120
Cdd:cd06322   13 FFVDIKDAMKKEAAELGVKVVVADA-NGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAGIPVFTVDVKAD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 121 PECRSYYInqGTPAQLGGMlvdMAANQVKK----EKAKVAFFySSPTVTDQNQWVKEAKDKIAKdHPGWEVVTTQFGYND 196
Cdd:cd06322   92 GAKVVTHV--GTDNYAGGK---LAGEYALKallgGGGKIAII-DYPEVESVVLRVNGFKEAIKK-YPNIEIVAEQPGDGR 164

                        170       180
                 ....*....|....*....|...
gi 535980227 197 ATKSLQTAEGIIKAYADLDAIIA 219
Cdd:cd06322  165 REEALAATEDMLQANPDLDGIFA 187
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
 41-287 1.27e-17

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: 81.19  E-value: 1.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  41 FFTSGGNGALEAGKELGVDVT-YDGPTEPSVsgQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDT 119
Cdd:cd06323   13 FFVSLKDGAQAEAKELGVELVvLDAQNDPAK--QLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAGIPVITVDRSV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 120 KPECRSYYInqGTPAQLGGmlvDMAAN---QVKKEKAKVAFFYSSPTVTDQNQWVKEAKDKIAKdHPGWEVVTTQFGYND 196
Cdd:cd06323   91 TGGKVVSHI--ASDNVAGG---EMAAEyiaKKLGGKGKVVELQGIPGTSAARERGKGFHNAIAK-YPKINVVASQTADFD 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 197 ATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAENLKNTSVAIVGF-STPNVMRPyVERGTVKEfglwDVVQQ---- 271
Cdd:cd06323  165 RTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAGRKDVIVVGFdGTPDAVKA-VKDGKLAA----TVAQQpeem 239

                        250
                 ....*....|....*.
gi 535980227 272 GKISVYVADALLKKGD 287
Cdd:cd06323  240 GAKAVETADKYLKGEK 255
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
 40-219 1.92e-17

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: 81.11  E-value: 1.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  40 GFFTSGGNGALEAGKELGVDVTYDgPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDT 119
Cdd:cd06309   12 PWRVANTKSIKEAAKKRGYELVYT-DANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAGIPVILVDRTI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 120 KPECRSYYINQGTP--AQLGGMLVDMAANQVKKEKAKVAFF---YSSPTVTDQNQWVKEAkdkiAKDHPGWEVVTTQFGY 194
Cdd:cd06309   91 DGEDGSLYVTFIGSdfVEEGRRAAEWLVKNYKGGKGNVVELqgtAGSSVAIDRSKGFREV----IKKHPNIKIVASQSGN 166

                        170       180
                 ....*....|....*....|....*.
gi 535980227 195 NDATKSLQTAEGIIKAY-ADLDAIIA 219
Cdd:cd06309  167 FTREKGQKVMENLLQAGpGDIDVIYA 192
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
 48-288 1.87e-16

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: 78.01  E-value: 1.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  48 GALEAGKELGVDVT-YDGPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDTkpecRSY 126
Cdd:cd06306   20 GIVDEAKRLGVKLTvYEAGGYTNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGIPVIDLVNGI----DSP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 127 YIN---QGTPAQLGGMLVDMAANQVKKEKAKVAFFySSPtvtdQNQ-WVKEA----KDKIAKdhPGWEVVTTQFGYNDAT 198
Cdd:cd06306   96 KVAarvLVDFYDMGYLAGEYLVEHHPGKPVKVAWF-PGP----AGAgWAEDRekgfKEALAG--SNVEIVATKYGDTGKA 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 199 KSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAENLKNTSVAIVGFS-TPNVMRpYVERGTVKEFGLWDVVQQGKISVY 277
Cdd:cd06306  169 VQLNLVEDALQAHPDIDYIVGNAVAAEAAVGALREAGLTGKVKVVSTYlTPGVYR-GIKRGKILAAPSDQPVLQGRIAVD 247

                        250
                 ....*....|.
gi 535980227 278 VADALLKKGDM 288
Cdd:cd06306  248 QAVRALEGKPV 258
PBP1_ABC_sugar_binding-like cd19996
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 69-217 1.64e-15

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: 75.74  E-value: 1.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  69 SVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYYINQGtPAQLGGMLVDMAANQV 148
Cdd:cd19996   43 DTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAAAAGIPVVLFDSGVGSDKYTAFVGVD-DAAFGRVGAEWLVKQL 121

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 535980227 149 KKeKAKVAFFYSSPTVTDQNQWVKEAKdKIAKDHPGWEVVTTQFGYNDATKSLQTAEGIIKAYADLDAI 217
Cdd:cd19996  122 GG-KGNIIALRGIAGVSVSEDRWAGAK-EVFKEYPGIKIVGEVYADWDYAKAKQAVESLLAAYPDIDGV 188
PBP1_ABC_sugar_binding-like cd19999
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 70-221 5.64e-14

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: 71.57  E-value: 5.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  70 VSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSD-TKPECRSYYINQGTPAQLGGMLVdmaANQV 148
Cdd:cd19999   46 ATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAGILVVSFDQPvSSPDAINVVIDQYKWAAIQAQWL---AEQL 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 535980227 149 kKEKAKVAFFYSSPTVTDQNQWVKEAKDKIAKdHPGWEVVTTQFGYNDATKSLQTAEGIIKAYADLDAIIAPD 221
Cdd:cd19999  123 -GGKGNIVAINGVAGNPANEARVKAADDVFAK-YPGIKVLASVPGGWDQATAQQVMATLLATYPDIDGVLTQD 193
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 41-219 5.86e-14

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


Pssm-ID: 380535 [Multi-domain]  Cd Length: 272  Bit Score: 70.72  E-value: 5.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  41 FFTSGGNGALEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDS-DT 119
Cdd:cd06312   14 FWSVVKKGAKDAAKDLGVTVQYLGPQNNDIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAAGIPVIAINSgDD 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 120 KPECRSYYINQ-GTPAQLGGMLvdmAANQVKKEKAKVAFFYSS-PTVTDQNQWVKEAKDKIAKDhpGWEVVTTQFGyNDA 197
Cdd:cd06312   94 RSKERLGALTYvGQDEYLAGQA---AGERALEAGPKNALCVNHePGNPGLEARCKGFADAFKGA--GILVELLDVG-GDP 167

                        170       180
                 ....*....|....*....|..
gi 535980227 198 TKSLQTAEGIIKAYADLDAIIA 219
Cdd:cd06312  168 TEAQEAIKAYLQADPDTDAVLT 189
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 29-304 1.50e-13

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


Pssm-ID: 380625 [Multi-domain]  Cd Length: 275  Bit Score: 69.59  E-value: 1.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVGFFTSGGNGALEAGKE-LGVD-VTYDGPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAM 106
Cdd:cd19970    1 KVALVMKSLANEFFIEMEKGARKHAKEaNGYElLVKGIKQETDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 107 QRGVKVLTWDS--DTKpECRSYYIN---QGTPAQLGGMLVDMAANQVKKEKAKVAFFYSSPTVTDQNQWVKEAKDkiAKD 181
Cdd:cd19970   81 DAGIAVINIDNrlDAD-ALKEGGINvpfVGPDNRQGAYLAGDYLAKKLGKGGKVAIIEGIPGADNAQQRKAGFLK--AFE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 182 HPGWEVVTTQFGYNDATKSLQTAEGIIKAYADLDAII-APDANALPAAAQAAENLKNTSVAIVGFSTPNVMRPYVERGTV 260
Cdd:cd19970  158 EAGMKIVASQSANWEIDEANTVAANLLTAHPDIRGILcANDNMALGAIKAVDAAGKAGKVLVVGFDNIPAVRPLLKDGKM 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 535980227 261 kefgLWDVVQQG-KISVYVADALLKkgdMNTGDklDIPGVGQVEV 304
Cdd:cd19970  238 ----LATIDQHPaKQAVYGIEYALK---MLNGE--EVPGWVKTPV 273
PBP1_ABC_sugar_binding-like cd06300
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ...
 70-219 2.09e-13

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: 69.66  E-value: 2.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  70 VSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSD-TKPECRSYYINQGTPAQLGGMLVdmaanqV 148
Cdd:cd06300   46 ATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFDGAvTSPDAYNVSNDQVEWGRLGAKWL------F 119

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 535980227 149 KK--EKAKVAFFY---SSPTVTDQNQWVKEAKDKiakdHPGWEVVTTQFGYNDATKSLQTAEGIIKAYADLDAIIA 219
Cdd:cd06300  120 EAlgGKGNVLVVRgiaGAPASADRHAGVKEALAE----YPGIKVVGEVFGGWDEATAQTAMLDFLATHPQVDGVWT 191
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
 29-220 2.31e-13

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: 69.25  E-value: 2.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIpKLVGVGFFTS-GGNGALEAGKELGVDV-TYDGptEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAM 106
Cdd:cd06305    1 TIAVV-RNGTSGDWDQqALQGAVAEAEKLGGTViVFDA--NGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKAL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 107 QRGVKVLTWDSDTKPecrsYYINQGTpaQLGGMLVDMAANQVKKE---KAKVA---FFYSSPTVTDQNQWvkeakDKIAK 180
Cdd:cd06305   78 DAGIPVVTFDTDSQV----PGVNNIT--QDDYALGTLSLGQLVKDlngEGNIAvfnVFGVPPLDKRYDIY-----KAVLK 146

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 535980227 181 DHPGWEVVTTQFGYNDATKSLQTA---EGIIKAY--ADLDAIIAP 220
Cdd:cd06305  147 ANPGIKKIVAELGDVTPNTAADAQtqvEALLKKYpeGGIDAIWAA 191
PBP1_ABC_sugar_binding-like cd19997
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 69-218 5.37e-13

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: 380652 [Multi-domain]  Cd Length: 305  Bit Score: 68.47  E-value: 5.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  69 SVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECrsYYINQGTPAQLGGMLVDMAANQV 148
Cdd:cd19997   45 SATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQACDAGIKVVVFDSGVTEPC--AYILNNDFEDYGAASVEYVADRL 122

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 535980227 149 KKeKAKVAFFY----SSPtvtdqNQWVKEAKDKIAKDHPGWEVVTTQFGYNDATKSLQTAEGIIKAYADLDAII 218
Cdd:cd19997  123 GG-KGNVLEVRgvagTSP-----DEEIYAGQVEALKKYPDLKVVAEVYGNWTQSVAQKAVTGILPSLPEVDAVI 190
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 41-219 5.44e-13

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


Pssm-ID: 380626 [Multi-domain]  Cd Length: 267  Bit Score: 67.99  E-value: 5.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  41 FFTSGGNGALEAGKELGVD-VTYDGptEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDT 119
Cdd:cd19971   13 FFIAINDGIKKAVEANGDElITRDP--QLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAGIPVINVDTPV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 120 K-PECRSYYInqGTPAQLGGMLVDMAANQVKKEKAKVAFFYsSPTVTDQNQWVKEAKDKIaKDHPGWEVVTTQFGYNDAT 198
Cdd:cd19971   91 KdTDLVDSTI--ASDNYNAGKLCGEDMVKKLPEGAKIAVLD-HPTAESCVDRIDGFLDAI-KKNPKFEVVAQQDGKGQLE 166

                        170       180
                 ....*....|....*....|.
gi 535980227 199 KSLQTAEGIIKAYADLDAIIA 219
Cdd:cd19971  167 VAMPIMEDILQAHPDLDAVFA 187
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
 29-221 7.19e-13

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


Pssm-ID: 380620 [Multi-domain]  Cd Length: 272  Bit Score: 67.68  E-value: 7.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQR 108
Cdd:cd19965    1 KFVFVTHVTTNPFFQPVKKGMDDACELLGAECQFTGPQTFDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 109 GVKVLTW--DSDTKPECRSYYINQG-TPAqlGGMLVDMAANQVKKEKAKVAFFYSSPTVTDQNQWVKEAKDKIAKDHPG- 184
Cdd:cd19965   81 GIPVVAFnvDAPGGENARLAFVGQDlYPA--GYVLGKRIAEKFKPGGGHVLLGISTPGQSALEQRLDGIKQALKEYGRGi 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 535980227 185 -WEVVTTqfgyndaTKSLQTAEGIIKAY----ADLDAIIAPD 221
Cdd:cd19965  159 tYDVIDT-------GTDLAEALSRIEAYytahPDIKAIFATG 193
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
 29-252 1.01e-12

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: 67.41  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVGFFTSGGNGALEAGKELGVD-VTYDGptEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQ 107
Cdd:cd19968    1 KIGFSFPNLSFPFFVYMHEQAVDEAAKLGVKlVVLDA--QNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 108 RGVKVLTWDSdtKPECRSYYINQGTPAQLGGMLVDMAANQVKKEKAKVAFFYSSPTVTDQNQWVKEAKDKIAKdHPGWEV 187
Cdd:cd19968   79 AGIPVVTVDR--RAEGAAPVPHVGADNVAGGREVAKFVVDKLPNGAKVIELTGTPGSSPAIDRTKGFHEELAA-GPKIKV 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 535980227 188 VTTQFGYNDATKSLQTAEGIIKAY-ADLDAIIAP--DANALPAAAQAAENLKNTSVAIVGF-STPNVMR 252
Cdd:cd19968  156 VFEQTGNFERDEGLTVMENILTSLpGPPDAIICAndDMALGAIEAMRAAGLDLKKVKVIGFdAVPDALQ 224
PBP1_ABC_sugar_binding-like cd19998
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 66-219 1.50e-12

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: 67.31  E-value: 1.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  66 TEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECrSYYIN---QGTPAQLGGMLVD 142
Cdd:cd19998   41 SGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAFDNVVDEPC-AYNVNtdqAKAGEQTAQWLVD 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 143 MAanqvkKEKAKVAFFYSSP--TVTDQNQwvkEAKDKIAKDHPGWEVVTTQFG-YNDATKSLQTAEgIIKAYADLDAIIA 219
Cdd:cd19998  120 KL-----GGKGNILMVRGVPgtSVDRDRY---EGAKEVFKKYPDIKVVAEYYGnWDDGTAQKAVAD-ALAAHPDVDGVWT 190
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
 29-219 1.59e-12

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: 66.91  E-value: 1.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVGFFTSGGNGALEAGKELGVDVT-YDGptEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQ 107
Cdd:cd06313    1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVvLDG--NGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 108 RGVKVLTWDSDTKPECRSYYInqGTPAQLGG-MLVDMAANQVkKEKAKVAFFY----SSPTVTDqnqwvKEAKDKIAKDH 182
Cdd:cd06313   79 AGIPLVGVNALIENEDLTAYV--GSDDVVAGeLEGQAVADRL-GGKGNVVILEgpigQSAQIDR-----GKGIENVLKKY 150

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 535980227 183 PGWEVVTTQFGYNDATKSLQTAEGIIKAY-ADLDAIIA 219
Cdd:cd06313  151 PDIKVLAEQTANWSRDEAMSLMENWLQAYgDEIDGIIA 188
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
 41-299 1.09e-11

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


Pssm-ID: 380622 [Multi-domain]  Cd Length: 272  Bit Score: 64.27  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  41 FFTSGGNGALEAGKELGVDVT-YDgpTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDt 119
Cdd:cd19967   13 FFVVEAEGAKEKAKELGYEVTvFD--HQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAGIPVFLIDRE- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 120 kpecrsyyINQGTPAQL--------GGMLVDMAANQVKKEKAKVAFFYSSPTvtDQNQWVK-EAKDKIAKDHPGWEVVTT 190
Cdd:cd19967   90 --------INAEGVAVAqivsdnyqGAVLLAQYFVKLMGEKGLYVELLGKES--DTNAQLRsQGFHSVIDQYPELKMVAQ 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 191 QFGYNDATKSLQTAEGIIKAYADLDAIIAPDANALPAAAQAAENL-KNTSVAIVGFSTPNVMRPYVERGTVKEFGLWDVV 269
Cdd:cd19967  160 QSADWDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAgRAGDVIIVGFDGSNDVRDAIKEGKISATVLQPAK 239

                        250       260       270
                 ....*....|....*....|....*....|
gi 535980227 270 QQGKISVYVADALLKKGDMNTGDKLDIPGV 299
Cdd:cd19967  240 LIARLAVEQADQYLKGGSTGKEEKQLFDCV 269
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
 51-285 1.51e-11

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


Pssm-ID: 380524 [Multi-domain]  Cd Length: 272  Bit Score: 63.79  E-value: 1.51e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  51 EAGKELGVDVTY-DGptEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDTK--PECRSYY 127
Cdd:cd06301   25 YAKEYPGVKLVIvDA--QSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADAGIPLVYVNREPDskPKGVAFV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 128 inqGTPAQLGGMLVDMAANQVKKEKAKVAFFYSSPTVTDQNQWVKEAKDKIAKdHPGWEVVTTQFGYNDATKSLQTAEGI 207
Cdd:cd06301  103 ---GSDDIESGELQMEYLAKLLGGKGNIAILDGVLGHEAQILRTEGNKDVLAK-YPGMKIVAEQTANWSREKAMDIVENW 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 208 IKAYADLDAIIAPDANALPAAAQAAENL-KNTSVAIVGF-STPNVMRpYVERGTVKEFGLWDVVQQGKISVYVADALLKK 285
Cdd:cd06301  179 LQSGDKIDAIVANNDEMAIGAILALEAAgKKDDILVAGIdATPDALK-AMKAGRLDATVFQDAAGQGETAVDVAVKAAKG 257
PRK09701 PRK09701
D-allose transporter substrate-binding protein;
3-116 4.76e-11

D-allose transporter substrate-binding protein;


Pssm-ID: 182037 [Multi-domain]  Cd Length: 311  Bit Score: 62.97  E-value: 4.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227   3 IQSIKKIAVISTLSLAAFTLNAYAAErIAFIPKLVGVGFFTSGGNGALEAGKELGVDV-TYDGPTEPSVSGQVQLINNFV 81
Cdd:PRK09701   1 MNKYLKYFSGTLVGLMLSTSAFAAAE-YAVVLKTLSNPFWVDMKKGIEDEAKTLGVSVdIFASPSEGDFQSQLQLFEDLS 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 535980227  82 NQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWD 116
Cdd:PRK09701  80 NKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLD 114
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
 51-219 6.46e-11

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: 61.79  E-value: 6.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  51 EAGKELGVDVTY-DGptEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDTkpECRSY--Y 127
Cdd:cd06308   24 EAAKYPNVELIVtDA--QGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDAGIPVIVLDRKV--SGDDYtaF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 128 INQ-----GTpaqlggmlvdMAANQVK---KEKAKVAFFY----SSPTVTDQNQWvkeaKDKIAKdHPGWEVVTTQFGYN 195
Cdd:cd06308  100 IGAdnveiGR----------QAGEYIAellNGKGNVVEIQglpgSSPAIDRHKGF----LEAIAK-YPGIKIVASQDGDW 164

                        170       180
                 ....*....|....*....|....
gi 535980227 196 DATKSLQTAEGIIKAYADLDAIIA 219
Cdd:cd06308  165 LRDKAIKVMEDLLQAHPDIDAVYA 188
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
 41-219 1.62e-10

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: 60.89  E-value: 1.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  41 FFTSGGNGALEAGKELGVDVTY-DGptEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDT 119
Cdd:cd06318   13 YYAALVAAAKAEAKKLGVELVVtDA--QNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAGIPVITVDSAL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 120 KPECRSY-YInqGTPAQLGGMLVDM-AANQVKKEKAKVAFFYSSP--TVTDQNQW------VKEAKDKIAkdHPGWEVVT 189
Cdd:cd06318   91 DPSANVAtQV--GRDNKQNGVLVGKeAAKALGGDPGKIIELSGDKgnEVSRDRRDgflagvNEYQLRKYG--KSNIKVVA 166

                        170       180       190
                 ....*....|....*....|....*....|
gi 535980227 190 TQFGYNDATKSLQTAEGIIKAYADLDAIIA 219
Cdd:cd06318  167 QPYGNWIRSGAVAAMEDLLQAHPDINVVYA 196
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 41-219 5.07e-10

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


Pssm-ID: 380544 [Multi-domain]  Cd Length: 270  Bit Score: 59.22  E-value: 5.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  41 FFTSGGNGALEAGKELGVDVTYDG-PTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDT 119
Cdd:cd06321   13 FFVAMVRGAEEAAAEINPGAKVTVvDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKDAGIIVVAVDVAA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 120 KPEcrsyyinQGTPA----QLGGMLVDMAANQVkKEKAKVAFFySSPTVTDQNQWVKEAKDKIAKdHPGWEVVTTQFGYN 195
Cdd:cd06321   93 EGA-------DATVTtdnvQAGYLACEYLVEQL-GGKGKVAII-DGPPVSAVIDRVNGCKEALAE-YPGIKLVDDQNGKG 162

                        170       180
                 ....*....|....*....|....
gi 535980227 196 DATKSLQTAEGIIKAYADLDAIIA 219
Cdd:cd06321  163 SRAGGLSVMTRMLTAHPDVDGVFA 186
PBP1_ABC_sugar_binding-like cd19973
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 41-122 4.79e-09

monosaccharide ABC transporter substrate-binding protein; 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: 380628 [Multi-domain]  Cd Length: 285  Bit Score: 56.71  E-value: 4.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  41 FFTSGGNGALEAGKELGVDV-TYDGPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDT 119
Cdd:cd19973   13 FFVKMKEGAQKAAKALGIKLmTAAGKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARDAGVLVIALDTPT 92


                 ...
gi 535980227 120 KPE 122
Cdd:cd19973   93 DPI 95
PBP1_ABC_sugar_binding-like cd06316
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 47-220 2.12e-07

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


Pssm-ID: 380539 [Multi-domain]  Cd Length: 294  Bit Score: 51.47  E-value: 2.12e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  47 NGALEAGKELGVDV--TYDGPTEPSVsgQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVK-VLTwdsDTKP-- 121
Cdd:cd06316   19 AGIKDTFEELGIEVvaVTDANFDPAK--QITDLETLIALKPDIIISIPVDPVATAAAYKKVADAGIKlVFM---DNVPdg 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 122 -ECRSYYINQGTPAQLG-GMLVDMAANQVKKEKAKVAFFYSSPTVTDQNQWVKEAKDKIAKDHPGWEVVTTQfGYNDATK 199
Cdd:cd06316   94 lEAGKDYVSVVSSDNRGnGQIAAELLAEAIGGKGKVGIIYHDADFYATNQRDKAFKDTLKEKYPDIKIVAEQ-GFADPND 172

                        170       180
                 ....*....|....*....|.
gi 535980227 200 SLQTAEGIIKAYADLDAIIAP 220
Cdd:cd06316  173 AEEVASAMLTANPDIDGIYVS 193
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 49-221 2.17e-07

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


Pssm-ID: 380534 [Multi-domain]  Cd Length: 270  Bit Score: 51.60  E-value: 2.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  49 ALEAGKELGvDVTYDGPTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYYI 128
Cdd:cd06311   21 AEKQAKELA-DLEYKLVTSSNANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAGIPVVNFDRGLNVLIYDLYV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 129 NQGTPaqlgGMLVDMAANQVKK--EKAKVAFFYSSPTVTDQNQWVKEAKDKIaKDHPGWEVVTTQFGYNDATKSLQTAEG 206
Cdd:cd06311  100 AGDNP----GMGVVSAEYIGKKlgGKGNVVVLEVPSSGSVNEERVAGFKEVI-KGNPGIKILAMQAGDWTREDGLKVAQD 174

                        170
                 ....*....|....*
gi 535980227 207 IIKAYADLDAIIAPD 221
Cdd:cd06311  175 ILTKNKKIDAVWAAD 189
PBP1_ABC_xylose_binding-like cd01538
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ...
 51-220 3.10e-06

periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong to a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein (PBP1) superfamily; Periplasmic xylose-like sugar-binding component of the 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 a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380480 [Multi-domain]  Cd Length: 283  Bit Score: 48.19  E-value: 3.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  51 EAGKELGVDVTY---DGptepSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYY 127
Cdd:cd01538   23 EQLEEKGAKVLVqsaDG----DKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEGIKVIAYDRLILNADVDYY 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 128 I---NQgtpaQLGgmlvDMAANQVKKEKAKVAFFYSSPTVTDQNQ-------------WVKEAKDKIAKDH--PGWevvt 189
Cdd:cd01538   99 IsfdNE----KVG----ELQAQALLDAKPEGNYVLIGGSPTDNNAklfrdgqmkvlqpAIDSGKIKVVGDQwvDDW---- 166

                        170       180       190
                 ....*....|....*....|....*....|..
gi 535980227 190 tqfgynDATKSLQTAEGIIKAY-ADLDAIIAP 220
Cdd:cd01538  167 ------LPANAQQIMENALTANgNNVDAVVAS 192
PBP1_ABC_xylose_binding cd19991
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ...
 51-116 1.07e-05

D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the 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 a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380646 [Multi-domain]  Cd Length: 284  Bit Score: 46.46  E-value: 1.07e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 535980227  51 EAGKELGVDVTYDGPTEpSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWD 116
Cdd:cd19991   23 KKAKELGAEVIVQSANG-DDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYD 87
PRK10936 PRK10936
TMAO reductase system periplasmic protein TorT; Provisional
 22-279 1.42e-04

TMAO reductase system periplasmic protein TorT; Provisional


Pssm-ID: 236801 [Multi-domain]  Cd Length: 343  Bit Score: 43.01  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  22 LNAYAAERI-AFIPKL-----VGVGFftsggnGALEAGKELGVDVT------YDGPTEpsvsgQVQLINNFVNQGYNAIV 89
Cdd:PRK10936  41 LKAKKAWKLcALYPHLkdsywLSVNY------GMVEEAKRLGVDLKvleaggYYNLAK-----QQQQLEQCVAWGADAIL 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  90 VSAVSPDGLCPALKRaMQRGVKVLtwdsDTkpecrsyyINQ-GTPAQLGGMLVD---MA-------ANQVKKE--KAKVA 156
Cdd:PRK10936 110 LGAVTPDGLNPDLEL-QAANIPVI----AL--------VNGiDSPQVTTRVGVSwyqMGyqagrylAQWHPKGskPLNVA 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 157 FFysspTVTDQNQWVKEAKDKIAKDHPGWEVVTTQFGYNDATKSLQT--AEGIIKAYADLDAIIAPDANALPAAAQAAEN 234
Cdd:PRK10936 177 LL----PGPEGAGGSKAVEQGFRAAIAGSDVRIVDIAYGDNDKELQRnlLQELLERHPDIDYIAGSAVAAEAAIGELRGR 252

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 535980227 235 LKNTSVAIVGF-STPNVMRPyVERGTVkEFGLWD-VVQQGKISVYVA 279
Cdd:PRK10936 253 NLTDKIKLVSFyLSHQVYRG-LKRGKV-LAAPSDqMVLQGRLAIDQA 297
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
 83-217 7.44e-04

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: 40.62  E-value: 7.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  83 QGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYYInqG--------TPAQL-GGMLVdmaanqvkKEKA 153
Cdd:cd06307   57 AGCDGVALVAPDHPLVRAAIDELAARGIPVVTLVSDLPGSRRLAYV--GidnraagrTAAWLmGRFLG--------RRPG 126

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 535980227 154 KVAFFYSSPTVTDQNQwvKEA--KDKIAKDHPGWEVVTTQFGYNDATKSLQTAEGIIKAYADLDAI 217
Cdd:cd06307  127 KVLVILGSHRFRGHEE--REAgfRSVLRERFPDLTVLEVLEGLDDDELAYELLRELLARHPDLVGI 190
PBP1_ABC_sugar_binding-like cd06315
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 29-181 1.10e-03

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: 380538  Cd Length: 278  Bit Score: 40.02  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVGFFTSGGNGALEAGKELGVDV-TYDGptEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQ 107
Cdd:cd06315    2 TIAYVASDLRNGGVLGVGRGVKEAAAALGWKVdVLDG--GGTVTGRLAALNQALALKPDGIILGGDDAVELQEPLKKAVK 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 535980227 108 RGVKVLTWDSDTKP---ECRSYYINQGT-PAQLGGMLVDMAANQVKKeKAKVAFFyssptvTDQNQWVKEAKDKIAKD 181
Cdd:cd06315   80 AGIPVVGWHAAASPgpiPELGLFTNITTdPREVAETAAALVIAQSGG-KAGVVIF------TDSRYAIATAKANAMKK 150
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
 58-116 1.12e-03

periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling system; Periplasmic aldose-monosaccharides binding protein ChvE that belongs 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 a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380649 [Multi-domain]  Cd Length: 304  Bit Score: 40.31  E-value: 1.12e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 535980227  58 VDVTYdgpTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWD 116
Cdd:cd19994   32 VDLQY---ADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAGIPVIAYD 87
PBP1_arabinose_binding cd01540
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ...
 29-215 1.14e-03

periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily; Periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose sugar-binding proteins of the type 1 periplasmic binding protein superfamily. ABP is only involved in transport contrary to other related sugar-binding proteins such as the glucose/galactose-binding protein (GGBP) and the ribose-binding protein (RBP), both of which are involved in chemotaxis as well as transport. The periplasmic ABP consists of two alpha/beta globular domains connected by a three-stranded hinge, a Venus flytrap-like domain, which undergoes a transition from an open to a closed conformational state upon ligand binding. Moreover, ABP is homologous to the ligand-binding domain of eukaryotic receptors such as metabotropic glutamate receptor (mGluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380482 [Multi-domain]  Cd Length: 294  Bit Score: 40.35  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKLVGVGFFTSGGNGALEAGKELGVDVTY-DGPTEPSVsgQVQLINNFVNQGYNAIVVsaVSPD-GLCPA-LKRA 105
Cdd:cd01540    1 KIGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKiDAKMDGEK--VLSAIDNLIAQGAQGIVI--CTPDqKLGPAiAAKA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 106 MQRGVKVLTWD-----SDTKPEC-----RSYYINQgtpaQLGGMLVDMAANQVKKEKAKVAF----FYSSPTVTDQnqwV 171
Cdd:cd01540   77 KAAGIPVIAVDdqlvdADPMKIVpfvgiDAYKIGE----AVGEWLAKEMKKRGWDDVKEVGVlaitMDTLSVCVDR---T 149

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 535980227 172 KEAKDKI-AKDHPGWEVVTTQFGYNDATKSLQTAEGIIKAYADLD 215
Cdd:cd01540  150 DGAKDALkAAGFPEDQIFQAPYKGTDTEGAFNAANAVITAHPEVK 194
PBP1_ABC_xylose_binding-like cd19992
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
 51-220 1.76e-03

periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic xylose-binding component of the 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 a transition from an open to a closed conformational state upon ligand binding. Moreover, the periplasmic xylose-binding protein is homologous to the ligand-binding domain of eukaryotic receptors such as glutamate receptor (GluR) and DNA-binding transcriptional repressors such as LacI and GalR.


Pssm-ID: 380647 [Multi-domain]  Cd Length: 284  Bit Score: 39.49  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  51 EAGKELGVDVTYDGpTEPSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYYINQ 130
Cdd:cd19992   23 EEAKELGVELIFQV-ADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAGVPVISYDRLILNADVDLYVGR 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 131 GTpAQLGGMLVDMAANQVkkEKAKVAFFYSSPTVTDQNQWVKEAKDKI--AKDHPGWEVVTTQFGYN-DATKSLQTAEGI 207
Cdd:cd19992  102 DN-YKVGQLQAEYALEAV--PKGNYVILSGDPGDNNAQLITAGAMDVLqpAIDSGDIKIVLDQYVKGwSPDEAMKLVENA 178

                        170
                 ....*....|....
gi 535980227 208 IKAYA-DLDAIIAP 220
Cdd:cd19992  179 LTANNnNIDAVLAP 192
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 41-116 2.91e-03

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: 38.88  E-value: 2.91e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 535980227  41 FFTSGGNGALEAGKELGVD-VTYDGPTepSVSGQVQLINNFVNQGYNAIVVSAVSPDGLCPALKRAMQRGVKVLTWD 116
Cdd:cd06319   13 FWQIMERGVQAAAEELGYEfVTYDQKN--SANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAKIPVVIAD 87
PBP1_BmpA_Med_PnrA-like cd06304
periplasmic binding component of a family of basic membrane lipoproteins from Borrelia and ...
 40-213 6.15e-03

periplasmic binding component of a family of basic membrane lipoproteins from Borrelia and various putative lipoproteins from other bacteria; Periplasmic binding component of a family of basic membrane lipoproteins from Borrelia and various putative lipoproteins from other bacteria. These outer membrane proteins include Med, a cell-surface localized protein regulating the competence transcription factor gene comK in Bacillus subtilis, and PnrA, a periplasmic purine nucleoside binding protein of an ATP-binding cassette (ABC) transport system in Treponema pallidum. All contain the type 1 periplasmic sugar-binding protein-like fold.


Pssm-ID: 380527  Cd Length: 262  Bit Score: 37.90  E-value: 6.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  40 GFFTSGGNGALEAGKELGVDVTYdgpTE-PSVSGQVQLINNFVNQGYNAIV---------VSAVSPDglCPALKRAmqrg 109
Cdd:cd06304   14 GWNQAAYEGLKKAAKELGIEVAY---SEnVPPADAERVLRDYASQGYDLIIghgfqfedaAKEVAPE--FPDTKFV---- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227 110 vkVLTWDSDTKPECRSYYINQGTPAQLGGMLvdmAANQVKkeKAKVAFFYSSPtVTDQNQWVKEAKDKIAKDHPGWEVVT 189
Cdd:cd06304   85 --VISGNVTAAPNVASYDFKEEEGGYLAGAL---AALMTK--TGKVGFVGGME-IPPIKRLLAGFEAGAKAVNPDAKVLV 156

                        170       180
                 ....*....|....*....|....*
gi 535980227 190 TQFG-YNDATKSLQTAEGIIKAYAD 213
Cdd:cd06304  157 AYTGsWDDVAKAKEAALAMIAQGAD 181
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
 29-118 7.12e-03

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: 37.69  E-value: 7.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 535980227  29 RIAFIPKL-VGVGFFTSGGNGALEAGKELGVDVTYDGPTEpSVSGQVQLINNFVNQGYNAIVVSAVSPDG-LCPALKRAM 106
Cdd:cd19966    1 KIYFIPGGaPGDPFWTVVYNGAKDAAADLGVDLDYVFSSW-DPEKMVEQFKEAIAAKPDGIAIMGHPGDGaYTPLIEAAK 79

                         90
                 ....*....|..
gi 535980227 107 QRGVKVLTWDSD 118
Cdd:cd19966   80 KAGIIVTSFNTD 91
 
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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