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Conserved domains on  [gi|928221397|ref|WP_053860103|]
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sugar ABC transporter substrate-binding protein [Paraburkholderia sp. RCC_158]

Protein Classification

sugar ABC transporter substrate-binding protein( domain architecture ID 14448231)

sugar ABC transporter substrate-binding protein functions as the initial receptor in the active transport of sugar substrates; similar to Caulobacter crescentus myo-inositol binding protein and Agrobacterium vitis ABC transporter solute-binding protein specific for glucosamine and galactosamine

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP1_ABC_sugar_binding-like cd19973
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
37-311 1.58e-158

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: 444.60  E-value: 1.58e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARA 116
Cdd:cd19973    1 TIGLITKTDTNPFFVKMKEGAQKAAKALGIKLMTAAGKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDTPTDPQDATDALFATDNFKAGVLIGKYAKAALNGKPAKIATLDLAPGVSVGVLRHNGFLEGFGV------- 189
Cdd:cd19973   81 AGVLVIALDTPTDPIDAADATFATDNFKAGVLIGEWAKAALGAKDAKIATLDLTPGHTVGVLRHQGFLKGFGIdekdpes 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 190 --KEGDASIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKA 267
Cdd:cd19973  161 neDEDDSQVVGSADTNGDQAKGQTAMENLLQKDPDINLVYTINEPAAAGAYQALKAAGKEKGVLIVSVDGGCPGVKDVKD 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 928221397 268 GSIAATSQQYPLKMASLGVTAGVDYAKTG-KKVTGYQDTGVTLIT 311
Cdd:cd19973  241 GIIGATSQQYPLRMAALGVEAIAAFAKTGgTKGSGFTDTGVTLVT 285
 
Name Accession Description Interval E-value
PBP1_ABC_sugar_binding-like cd19973
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
37-311 1.58e-158

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: 444.60  E-value: 1.58e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARA 116
Cdd:cd19973    1 TIGLITKTDTNPFFVKMKEGAQKAAKALGIKLMTAAGKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDTPTDPQDATDALFATDNFKAGVLIGKYAKAALNGKPAKIATLDLAPGVSVGVLRHNGFLEGFGV------- 189
Cdd:cd19973   81 AGVLVIALDTPTDPIDAADATFATDNFKAGVLIGEWAKAALGAKDAKIATLDLTPGHTVGVLRHQGFLKGFGIdekdpes 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 190 --KEGDASIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKA 267
Cdd:cd19973  161 neDEDDSQVVGSADTNGDQAKGQTAMENLLQKDPDINLVYTINEPAAAGAYQALKAAGKEKGVLIVSVDGGCPGVKDVKD 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 928221397 268 GSIAATSQQYPLKMASLGVTAGVDYAKTG-KKVTGYQDTGVTLIT 311
Cdd:cd19973  241 GIIGATSQQYPLRMAALGVEAIAAFAKTGgTKGSGFTDTGVTLVT 285
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
14-311 5.70e-75

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: 233.28  E-value: 5.70e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  14 IVSMCVAASAVWCTSASQAADQPVVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGrfDGDNASQVTAIENMMTAG 93
Cdd:COG1879   12 LALALAACGSAAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDA--EGDAAKQISQIEDLIAQG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  94 AKAILITPSDTKAIVPSIKKARAAGVMVVALDTPTDPQDAtDALFATDNFKAGVLIGKYAKAALNGKpAKIATLDLAPGV 173
Cdd:COG1879   90 VDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDR-VAYVGSDNYAAGRLAAEYLAKALGGK-GKVAILTGSPGA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 174 SVGVLRHNGFLEGFGvKEGDASIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIV 253
Cdd:COG1879  168 PAANERTDGFKEALK-EYPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRKGDVKVV 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 928221397 254 SIDGGCEGVRNVKAGSIAATSQQYPLKMASLGVTAGVDYAKtGKKVTGYQDTGVTLIT 311
Cdd:COG1879  247 GFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLK-GKEVPKEILTPPVLVT 303
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
38-298 6.65e-47

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: 159.40  E-value: 6.65e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397   38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRfDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAA 117
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPA-EADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  118 GVMVVALDTPTdPQDATDALFATDNFKAGVLIGKYAKAALNGKpAKIATLDLAPGVSVGVLRHNGFLEGFGVKEGDASIV 197
Cdd:pfam13407  80 GIPVVTFDSDA-PSSPRLAYVGFDNEAAGEAAGELLAEALGGK-GKVAILSGSPGDPNANERIDGFKKVLKEKYPGIKVV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  198 CSQDTRG-DQAKGQTAMENCLQKAPD-INVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAATSQ 275
Cdd:pfam13407 158 AEVEGTNwDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGKVVVTGFDATPEALEAIKDGTIDATVL 237
                         250       260
                  ....*....|....*....|...
gi 928221397  276 QYPLKMASLGVTAGVDYAKtGKK 298
Cdd:pfam13407 238 QDPYGQGYAAVELAAALLK-GKK 259
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
13-311 5.46e-39

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 139.45  E-value: 5.46e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  13 KIVSMCVAASAVWCTSASQAADQPVVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITaagrFDGDN--ASQVTAIENMM 90
Cdd:PRK10653   4 KKLATLVSAVALSATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVV----LDSQNnpAKELANVQDLT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  91 TAGAKAILITPSDTKAIVPSIKKARAAGVMVVALDTPTDPQDATDALfATDNFKAGVLIGKYAKAALnGKPAKIATLDLA 170
Cdd:PRK10653  80 VRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRGATKGEVVSHI-ASDNVAGGKMAGDFIAKKL-GEGAKVIQLEGI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 171 PGVSVGVLRHNGFLEGfgVKEGDASIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKsV 250
Cdd:PRK10653 158 AGTSAARERGEGFKQA--VAAHKFNVLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-V 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928221397 251 MIVSIDGGCEGVRNVKAGSIAATSQQYPLKMASLGV-TAgvDYAKTGKKVTGYQDTGVTLIT 311
Cdd:PRK10653 235 MVVGFDGTPDGIKAVNRGKLAATIAQQPDQIGAIGVeTA--DKVLKGEKVEAKIPVDLKLVT 294
 
Name Accession Description Interval E-value
PBP1_ABC_sugar_binding-like cd19973
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
37-311 1.58e-158

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: 444.60  E-value: 1.58e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARA 116
Cdd:cd19973    1 TIGLITKTDTNPFFVKMKEGAQKAAKALGIKLMTAAGKIDGDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDTPTDPQDATDALFATDNFKAGVLIGKYAKAALNGKPAKIATLDLAPGVSVGVLRHNGFLEGFGV------- 189
Cdd:cd19973   81 AGVLVIALDTPTDPIDAADATFATDNFKAGVLIGEWAKAALGAKDAKIATLDLTPGHTVGVLRHQGFLKGFGIdekdpes 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 190 --KEGDASIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKA 267
Cdd:cd19973  161 neDEDDSQVVGSADTNGDQAKGQTAMENLLQKDPDINLVYTINEPAAAGAYQALKAAGKEKGVLIVSVDGGCPGVKDVKD 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 928221397 268 GSIAATSQQYPLKMASLGVTAGVDYAKTG-KKVTGYQDTGVTLIT 311
Cdd:cd19973  241 GIIGATSQQYPLRMAALGVEAIAAFAKTGgTKGSGFTDTGVTLVT 285
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
37-309 2.22e-77

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: 237.85  E-value: 2.22e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGrfDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARA 116
Cdd:cd01536    1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDA--QGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDTPTDPQDATDALFATDNFKAGVLIGKYAKAALNGKpAKIATLDLAPGVSVGVLRHNGFLEGFGvKEGDASI 196
Cdd:cd01536   79 AGIPVVAVDTDIDGGGDVVAFVGTDNYEAGKLAGEYLAEALGGK-GKVAILEGPPGSSTAIDRTKGFKEALK-KYPDIEI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 197 VCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAATSQQ 276
Cdd:cd01536  157 VAEQPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRTGDIKIVGVDGTPEALKAIKDGELDATVAQ 236
                        250       260       270
                 ....*....|....*....|....*....|...
gi 928221397 277 YPLKMASLGVTAGVDYAKtGKKVTGYQDTGVTL 309
Cdd:cd01536  237 DPYLQGYLAVEAAVKLLN-GEKVPKEILTPVTL 268
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
14-311 5.70e-75

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: 233.28  E-value: 5.70e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  14 IVSMCVAASAVWCTSASQAADQPVVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGrfDGDNASQVTAIENMMTAG 93
Cdd:COG1879   12 LALALAACGSAAAEAAAAAAKGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDA--EGDAAKQISQIEDLIAQG 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  94 AKAILITPSDTKAIVPSIKKARAAGVMVVALDTPTDPQDAtDALFATDNFKAGVLIGKYAKAALNGKpAKIATLDLAPGV 173
Cdd:COG1879   90 VDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDR-VAYVGSDNYAAGRLAAEYLAKALGGK-GKVAILTGSPGA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 174 SVGVLRHNGFLEGFGvKEGDASIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIV 253
Cdd:COG1879  168 PAANERTDGFKEALK-EYPGIKVVAEQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRKGDVKVV 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 928221397 254 SIDGGCEGVRNVKAGSIAATSQQYPLKMASLGVTAGVDYAKtGKKVTGYQDTGVTLIT 311
Cdd:COG1879  247 GFDGSPEALQAIKDGTIDATVAQDPYLQGYLAVDAALKLLK-GKEVPKEILTPPVLVT 303
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
37-299 1.45e-55

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: 182.01  E-value: 1.45e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITaagrFDG--DNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKA 114
Cdd:cd19971    1 KFGFSYMTMNNPFFIAINDGIKKAVEANGDELIT----RDPqlDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 115 RAAGVMVVALDTPTDPQDATDALFATDNFKAGVLIGKYAKAALNGKpAKIATLDLaPGVSVGVLRHNGFLEGFGvKEGDA 194
Cdd:cd19971   77 KEAGIPVINVDTPVKDTDLVDSTIASDNYNAGKLCGEDMVKKLPEG-AKIAVLDH-PTAESCVDRIDGFLDAIK-KNPKF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 195 SIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAATS 274
Cdd:cd19971  154 EVVAQQDGKGQLEVAMPIMEDILQAHPDLDAVFALNDPSALGALAALKAAGKLGDILVYGVDGSPDAKAAIKDGKMTATA 233
                        250       260
                 ....*....|....*....|....*
gi 928221397 275 QQYPLKMASLGVTAGVDYAKtGKKV 299
Cdd:cd19971  234 AQSPIEIGKKAVETAYKILN-GEKV 257
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
37-299 2.43e-53

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: 176.31  E-value: 2.43e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGrfDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARA 116
Cdd:cd06322    1 TIGVSLLTLQHPFFVDIKDAMKKEAAELGVKVVVADA--NGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDTPTDpQDATDALFATDNFKAGVLIGKYAKAALNGKPAKIATLDLaPGVSVGVLRHNGFLEGFGvKEGDASI 196
Cdd:cd06322   79 AGIPVFTVDVKAD-GAKVVTHVGTDNYAGGKLAGEYALKALLGGGGKIAIIDY-PEVESVVLRVNGFKEAIK-KYPNIEI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 197 VCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNV-KAGSIAATSQ 275
Cdd:cd06322  156 VAEQPGDGRREEALAATEDMLQANPDLDGIFAIGDPAALGALTAIESAGKEDKIKVIGFDGNPEAIKAIaKGGKIKADIA 235
                        250       260
                 ....*....|....*....|....
gi 928221397 276 QYPLKMASLGVTAGVDYAKtGKKV 299
Cdd:cd06322  236 QQPDKIGQETVEAIVKYLA-GETV 258
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
37-309 3.22e-52

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: 173.59  E-value: 3.22e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASK-DGAKLITAAGRFDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKAR 115
Cdd:cd19970    1 KVALVMKSLANEFFIEMEKGARKHAKEaNGYELLVKGIKQETDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 116 AAGVMVVALDTPTDPQDATDAL-----FATDNFKAGVLIGKYAKAALnGKPAKIATLDLAPGVSVGVLRHNGFLEGFgvK 190
Cdd:cd19970   81 DAGIAVINIDNRLDADALKEGGinvpfVGPDNRQGAYLAGDYLAKKL-GKGGKVAIIEGIPGADNAQQRKAGFLKAF--E 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 191 EGDASIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSI 270
Cdd:cd19970  158 EAGMKIVASQSANWEIDEANTVAANLLTAHPDIRGILCANDNMALGAIKAVDAAGKAGKVLVVGFDNIPAVRPLLKDGKM 237
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 928221397 271 AATSQQYPLKMASLGVTAGVDyAKTGKKVTGYQDTGVTL 309
Cdd:cd19970  238 LATIDQHPAKQAVYGIEYALK-MLNGEEVPGWVKTPVEL 275
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
37-311 7.57e-52

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: 172.98  E-value: 7.57e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRfdGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARA 116
Cdd:cd06318    1 KIGFSQRTLASPYYAALVAAAKAEAKKLGVELVVTDAQ--NDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDTPTDPQDATDALFATDNFKAGVLIGKYAKAALNGKPAKIATLDLAPGVSVGVLRHNGFLEGF----GVKEG 192
Cdd:cd06318   79 AGIPVITVDSALDPSANVATQVGRDNKQNGVLVGKEAAKALGGDPGKIIELSGDKGNEVSRDRRDGFLAGVneyqLRKYG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 193 DASI-VCSQD-TRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSI 270
Cdd:cd06318  159 KSNIkVVAQPyGNWIRSGAVAAMEDLLQAHPDINVVYAENDDMALGAMKALKAAGMLDKVKVAGADGQKEALKLIKDGKY 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 928221397 271 AATSQQYPLKMASLGVTAGVDYAKTGKKVTGYQDTGVTLIT 311
Cdd:cd06318  239 VATGLNDPDLLGKTAVDTAAKVVKGEESFPEFTYTPTALIT 279
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
38-311 1.38e-51

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: 171.65  E-value: 1.38e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAA 117
Cdd:cd20004    2 IAVIPKGTTHDFWKSVKAGAEKAAQELGVEIYWRGPSREDDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARAQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 118 GVMVVALDTPTDpQDATDALFATDNFKAGVLIGKYAKAALNGKPaKIATLDLAPGVSVGVLRHNGFLEgfGVKEGDASIV 197
Cdd:cd20004   82 GIPVVIIDSDLG-GDAVISFVATDNYAAGRLAAKRMAKLLNGKG-KVALLRLAKGSASTTDRERGFLE--ALKKLAPGLK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 198 CSQDTRGDQAKGQT--AMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAATSQ 275
Cdd:cd20004  158 VVDDQYAGGTVGEArsSAENLLNQYPDVDGIFTPNESTTIGALRALRRLGLAGKVKFIGFDASDLLLDALRAGEISALVV 237
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 928221397 276 QYPLKMASLGVTAGVDYAKtGKKVTGYQDTGVTLIT 311
Cdd:cd20004  238 QDPYRMGYLGVKTAVAALR-GKPVPKRIDTGVVLVT 272
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
40-311 3.89e-49

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: 165.48  E-value: 3.89e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  40 LITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKArAAGV 119
Cdd:cd20008    4 VIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLGPATEADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAA-DAGI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 120 MVVALDTPTDPqDATDALFATDNFKAGVLIGKYAKAALN---GKPAKIATLDLAPGVSVGVLRHNGFLEGFGVKEGDASI 196
Cdd:cd20008   83 PVVLVDSGANT-DDYDAFLATDNVAAGALAADELAELLKasgGGKGKVAIISFQAGSQTLVDREEGFRDYIKEKYPDIEI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 197 VCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAATSQQ 276
Cdd:cd20008  162 VDVQYSDGDIAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAGKAGKIVLVGFDSSPDEVALLKSGVIKALVVQ 241
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 928221397 277 YPLKMASLGVTAGVDYAKTGKKVTGYQDTGVTLIT 311
Cdd:cd20008  242 DPYQMGYEGVKTAVKALKGEEIVEKNVDTGVTVVT 276
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
37-311 3.95e-49

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: 165.16  E-value: 3.95e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRfdGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARA 116
Cdd:cd06323    1 TIGLSVSTLNNPFFVSLKDGAQAEAKELGVELVVLDAQ--NDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDTPTDPQDATdALFATDNFKAGVLIGKYAKAALNGKpAKIATLDLAPGVSVGVLRHNGFLEGFGvKEGDASI 196
Cdd:cd06323   79 AGIPVITVDRSVTGGKVV-SHIASDNVAGGEMAAEYIAKKLGGK-GKVVELQGIPGTSAARERGKGFHNAIA-KYPKINV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 197 VCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKdKSVMIVSIDGGCEGVRNVKAGSIAATSQQ 276
Cdd:cd06323  156 VASQTADFDRTKGLNVMENLLQAHPDIDAVFAHNDEMALGAIQALKAAGR-KDVIVVGFDGTPDAVKAVKDGKLAATVAQ 234
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 928221397 277 YPLKMASLGVTAGVDYAKtGKKVTGYQDTGVTLIT 311
Cdd:cd06323  235 QPEEMGAKAVETADKYLK-GEKVPKKIPVPLKLVT 268
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
37-310 4.29e-49

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: 165.03  E-value: 4.29e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASK-DGAKLITAAGrfDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKAR 115
Cdd:cd06308    1 VIGFSQCSLNDPWRAAMNEEIKAEAAKyPNVELIVTDA--QGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 116 AAGVMVVALDTPTDPQDATdALFATDNFKAGVLIGKYAKAALNGKpAKIATLDLAPGVSVGVLRHNGFLEGFGvKEGDAS 195
Cdd:cd06308   79 DAGIPVIVLDRKVSGDDYT-AFIGADNVEIGRQAGEYIAELLNGK-GNVVEIQGLPGSSPAIDRHKGFLEAIA-KYPGIK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 196 IVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCE-GVRNVKAGSIAATS 274
Cdd:cd06308  156 IVASQDGDWLRDKAIKVMEDLLQAHPDIDAVYAHNDEMALGAYQALKKAGREKEIKIIGVDGLPEaGEKAVKDGILAATF 235
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 928221397 275 qQYPLkMASLGVTAGVDYAKtGKKVTGYQDTGVTLI 310
Cdd:cd06308  236 -LYPT-GGKEAIEAALKILN-GEKVPKEIVLPTPLI 268
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
37-299 5.03e-49

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: 165.15  E-value: 5.03e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKD--GAKLITAAGRFDgdNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKA 114
Cdd:cd06321    1 VIGVTVQDLGNPFFVAMVRGAEEAAAEInpGAKVTVVDARYD--LAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 115 RAAGVMVVALDTPTDPQDATdalFATDNFKAGVLIGKYAKAALNGKpAKIATLDlAPGVSVGVLRHNGFLEGFGvKEGDA 194
Cdd:cd06321   79 KDAGIIVVAVDVAAEGADAT---VTTDNVQAGYLACEYLVEQLGGK-GKVAIID-GPPVSAVIDRVNGCKEALA-EYPGI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 195 SIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDkSVMIVSIDGGCEGVRNVK--AGSIAA 272
Cdd:cd06321  153 KLVDDQNGKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAGRD-DIVITSVDGSPEAVAALKreGSPFIA 231
                        250       260
                 ....*....|....*....|....*..
gi 928221397 273 TSQQYPLKMASLGVTAGVDYaKTGKKV 299
Cdd:cd06321  232 TAAQDPYDMARKAVELALKI-LNGQEP 257
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
37-311 1.11e-47

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: 161.74  E-value: 1.11e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARA 116
Cdd:cd06310    1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKIIFVGPESEEDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDTPTDPqDATDALFATDNFKAGVLIGKYAKAALNGKpAKIATLDLAPGVSVGVLRHNGFLEGFGVKEGDASI 196
Cdd:cd06310   81 KGIPVIVIDSGIKG-DAYLSYIATDNYAAGRLAAQKLAEALGGK-GKVAVLSLTAGNSTTDQREEGFKEYLKKHPGGIKV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 197 VCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAATSQQ 276
Cdd:cd06310  159 LASQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGQIKIVGFDSQEELLDALKNGKIDALVVQ 238
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 928221397 277 YPLKMASLGVTAGVDYAKtGKKVTGYQDTGVTLIT 311
Cdd:cd06310  239 NPYEIGYEGIKLALKLLK-GEEVPKNIDTGAELIT 272
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
38-298 6.65e-47

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: 159.40  E-value: 6.65e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397   38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRfDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAA 117
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVVGPA-EADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  118 GVMVVALDTPTdPQDATDALFATDNFKAGVLIGKYAKAALNGKpAKIATLDLAPGVSVGVLRHNGFLEGFGVKEGDASIV 197
Cdd:pfam13407  80 GIPVVTFDSDA-PSSPRLAYVGFDNEAAGEAAGELLAEALGGK-GKVAILSGSPGDPNANERIDGFKKVLKEKYPGIKVV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  198 CSQDTRG-DQAKGQTAMENCLQKAPD-INVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAATSQ 275
Cdd:pfam13407 158 AEVEGTNwDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGKVVVTGFDATPEALEAIKDGTIDATVL 237
                         250       260
                  ....*....|....*....|...
gi 928221397  276 QYPLKMASLGVTAGVDYAKtGKK 298
Cdd:pfam13407 238 QDPYGQGYAAVELAAALLK-GKK 259
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
40-311 3.18e-45

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: 155.05  E-value: 3.18e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  40 LITKTDTNPFFVKMKQGAEAAASKDGAKLItaagrFDG----DNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKAR 115
Cdd:cd06314    4 LVPKGLNNPFWDLAEAGAEKAAKELGVNVE-----FVGpqksDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 116 AAGVMVVALDTPTdPQDATDALFATDNFKAGVLIGKYAKAALnGKPAKIATLDLAPGVSVGVLRHNGFLEGFGvKEGDAS 195
Cdd:cd06314   79 DKGIPVITFDSDA-PDSKRLAYIGTDNYEAGREAGELMKKAL-PGGGKVAIITGGLGADNLNERIQGFKDALK-GSPGIE 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 196 IVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAATSQ 275
Cdd:cd06314  156 IVDPLSDNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKVGKVKIVGFDTLPETLQGIKDGVIAATVG 235
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 928221397 276 QYPLKMASLGVTAGVDYAKTGKKVTGYQDTGVTLIT 311
Cdd:cd06314  236 QRPYEMGYLSVKLLYKLLKGGKPVPDVIDTGVDVVT 271
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
37-303 3.87e-45

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: 155.45  E-value: 3.87e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGrfDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARA 116
Cdd:cd06309    1 TVGFSQAGSESPWRVANTKSIKEAAKKRGYELVYTDA--NQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDTPTDPQDATD--ALFATDNFKAGVLIGKYAKAALNGKPAKIATLDLAPGVSVGVLRHNGFLEGFGvKEGDA 194
Cdd:cd06309   79 AGIPVILVDRTIDGEDGSLyvTFIGSDFVEEGRRAAEWLVKNYKGGKGNVVELQGTAGSSVAIDRSKGFREVIK-KHPNI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 195 SIVCSQDTRGDQAKGQTAMENCLQKAP-DINVVYTINEPAAAGAYRALKAAGKD--KSVMIVSIDGGCEGVRNVKAGSIA 271
Cdd:cd06309  158 KIVASQSGNFTREKGQKVMENLLQAGPgDIDVIYAHNDDMALGAIQALKEAGLKpgKDVLVVGIDGQKDALEAIKAGELN 237
                        250       260       270
                 ....*....|....*....|....*....|..
gi 928221397 272 ATSQQYPLkMASLGVTAGVDYAKtGKKVTGYQ 303
Cdd:cd06309  238 ATVECNPL-FGPTAFDTIAKLLA-GEKVPKLI 267
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
38-311 4.76e-44

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: 152.01  E-value: 4.76e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRfDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAA 117
Cdd:cd20007    2 IALVPGVTGDPFYITMQCGAEAAAKELGVELDVQGPP-TFDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRAADA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 118 GVMVVALDTPTDPQDATDALFATDNFKAGVLIGKYAKAALNGKpAKIATLDLAPGVSVGVLRHNGFLEGFGvKEGDASIV 197
Cdd:cd20007   81 GIKVVTVDTTLGDPSFVLSQIASDNVAGGALAAEALAELIGGK-GKVLVINSTPGVSTTDARVKGFAEEMK-KYPGIKVL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 198 CSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAATSQQY 277
Cdd:cd20007  159 GVQYSENDPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAGKTGKVKVVGFDASPAQVEQLKAGTIDALIAQK 238
                        250       260       270
                 ....*....|....*....|....*....|....
gi 928221397 278 PLKMASLGVTAGVDYAkTGKKVTGYQDTGVTLIT 311
Cdd:cd20007  239 PAEIGYLAVEQAVAAL-TGKPVPKDILTPFVVIT 271
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
38-311 1.85e-42

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: 148.56  E-value: 1.85e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAA 117
Cdd:cd06320    2 IGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVQAAPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANKK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 118 GVMVVALDTPTDPQDATDALFA------TDNFKAGVLIGKYAKAALNGKpAKIATLDLAPGVSVGVLRHNGFLEGFGvKE 191
Cdd:cd06320   82 GIPVINLDDAVDADALKKAGGKvtsfigTDNVAAGALAAEYIAEKLPGG-GKVAIIEGLPGNAAAEARTKGFKETFK-KA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 192 GDASIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIA 271
Cdd:cd06320  160 PGLKLVASQPADWDRTKALDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAGKTGKVLVVGTDGIPEAKKSIKAGELT 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 928221397 272 ATSQQYPLKMASLGVTAGVDYAKtGKKVTGYQDTGVTLIT 311
Cdd:cd06320  240 ATVAQYPYLEGAMAVEAALRLLQ-GQKVPAVVATPQALIT 278
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
37-311 1.16e-40

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: 143.51  E-value: 1.16e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNP--FFVKMKQGAEAAASKDGAKLITAAGRFDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKA 114
Cdd:cd20006    1 KIALILKSSDPNsdFWQTVKSGAEAAAKEYGVDLEFLGPESEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 115 RAAGVMVVALDTPTDPQDAtDALFATDNFKAGVLIGKYAKAALNGKPaKIATLDLAPGVSVGVLRHNGFLEGFGvKEGDA 194
Cdd:cd20006   81 KKAGIPVITIDSPVNSKKA-DSFVATDNYEAGKKAGEKLASLLGEKG-KVAIVSFVKGSSTAIEREEGFKQALA-EYPNI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 195 SIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAATS 274
Cdd:cd20006  158 KIVETEYCDSDEEKAYEITKELLSKYPDINGIVALNEQSTLGAARALKELGLGGKVKVVGFDSSVEEIQLLEEGIIDALV 237
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 928221397 275 QQYPLKMASLGVTAGVDYAKtGKKVTGYQDTGVTLIT 311
Cdd:cd20006  238 VQNPFNMGYLSVQAAVDLLN-GKKIPKRIDTGSVVIT 273
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
38-311 1.12e-39

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: 140.96  E-value: 1.12e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRfdGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAA 117
Cdd:cd06319    2 IGYSVYDLDNPFWQIMERGVQAAAEELGYEFVTYDQK--NSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 118 GVMVVALDTPTDPQDaTDALFATDNFKAGVLIGKYAKAALNGK---PAKIATLDLAPGVSVGVLRHNGFLEGFGvKEGDA 194
Cdd:cd06319   80 KIPVVIADIGTGGGD-YVSYIISDNYDGGYQAGEYLAEALKENgwgGGSVGIIAIPQSRVNGQARTAGFEDALE-EAGVE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 195 SIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAATS 274
Cdd:cd06319  158 EVALRQTPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRTGDILVVGFDGDPEALDLIKDGKLDGTV 237
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 928221397 275 QQYPLKMASLGVTAGVDYAKTGKKVTGYQDTGVTLIT 311
Cdd:cd06319  238 AQQPFGMGARAVELAIQALNGDNTVEKEIYLPVLLVT 274
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
13-311 5.46e-39

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 139.45  E-value: 5.46e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  13 KIVSMCVAASAVWCTSASQAADQPVVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITaagrFDGDN--ASQVTAIENMM 90
Cdd:PRK10653   4 KKLATLVSAVALSATVSANAMAKDTIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVV----LDSQNnpAKELANVQDLT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  91 TAGAKAILITPSDTKAIVPSIKKARAAGVMVVALDTPTDPQDATDALfATDNFKAGVLIGKYAKAALnGKPAKIATLDLA 170
Cdd:PRK10653  80 VRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRGATKGEVVSHI-ASDNVAGGKMAGDFIAKKL-GEGAKVIQLEGI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 171 PGVSVGVLRHNGFLEGfgVKEGDASIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKsV 250
Cdd:PRK10653 158 AGTSAARERGEGFKQA--VAAHKFNVLASQPADFDRTKGLNVMQNLLTAHPDVQAVFAQNDEMALGALRALQTAGKSD-V 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928221397 251 MIVSIDGGCEGVRNVKAGSIAATSQQYPLKMASLGV-TAgvDYAKTGKKVTGYQDTGVTLIT 311
Cdd:PRK10653 235 MVVGFDGTPDGIKAVNRGKLAATIAQQPDQIGAIGVeTA--DKVLKGEKVEAKIPVDLKLVT 294
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
38-311 1.04e-37

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: 135.97  E-value: 1.04e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGrfDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAA 117
Cdd:cd06317    2 IALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNA--NDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 118 GVMVVALDTPTdPQDATDALFATDNFKAGVLIGKYAK---AALNGKPAKIATLDlAPGVSVGVLRHNGFLEgfGVKEG-D 193
Cdd:cd06317   80 GIPVIAYDAVI-PSDFQAAQVGVDNLEGGKEIGKYAAdyiKAELGGQAKIGVVG-ALSSLIQNQRQKGFEE--ALKANpG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 194 ASIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGV-RNVKAGSIAA 272
Cdd:cd06317  156 VEIVATVDGQNVQEKALSAAENLLTANPDLDAIYATGEPALLGAVAAVRSQGRQGKIKVFGWDLTKQAIfLGIDEGVLQA 235
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 928221397 273 TSQQYPLKMASLGVTAGVDYAKtGKKVTGYQDTGVTLIT 311
Cdd:cd06317  236 VVQQDPEKMGYEAVKAAVKAIK-GEDVEKTIDVPPTIVT 273
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
48-304 1.47e-37

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: 135.21  E-value: 1.47e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  48 PFFVKMKQGAEAAASKDGAKLITAagrfDGDNAS--QVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAAGVMVVALD 125
Cdd:cd19968   12 PFFVYMHEQAVDEAAKLGVKLVVL----DAQNSSskQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKAGIPVVTVD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 126 TPTDPQDATdALFATDNFKAGVLIGKYAKAALNGKpAKIATLDLAPGVSVGVLRHNGFLEGFGvKEGDASIVCSQDTRGD 205
Cdd:cd19968   88 RRAEGAAPV-PHVGADNVAGGREVAKFVVDKLPNG-AKVIELTGTPGSSPAIDRTKGFHEELA-AGPKIKVVFEQTGNFE 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 206 QAKGQTAMENCLQKAP-DINVVYTINEPAAAGAYRALKAAG-KDKSVMIVSIDGGCEGVRNVKAGSIAATSQQYPLKMAS 283
Cdd:cd19968  165 RDEGLTVMENILTSLPgPPDAIICANDDMALGAIEAMRAAGlDLKKVKVIGFDAVPDALQAIKDGELYATVEQPPGGQAR 244
                        250       260
                 ....*....|....*....|.
gi 928221397 284 LGVTAGVDYAKTGKKVTGYQD 304
Cdd:cd19968  245 TALRILVDYLKDKKAPKKVNL 265
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
38-311 1.84e-37

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: 135.14  E-value: 1.84e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGrfDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAA 117
Cdd:cd19967    2 VAVIVSTPNNPFFVVEAEGAKEKAKELGYEVTVFDH--QNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 118 GVMVVALDTPTDPQDATDALFATDNFKAGVLIGKYAkAALNGKPAKIATLDLAPGVSVGVLRHNGFLEgfgVKEG--DAS 195
Cdd:cd19967   80 GIPVFLIDREINAEGVAVAQIVSDNYQGAVLLAQYF-VKLMGEKGLYVELLGKESDTNAQLRSQGFHS---VIDQypELK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 196 IVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAATSQ 275
Cdd:cd19967  156 MVAQQSADWDRTEAFEKMESILQANPDIKGVICGNDEMALGAIAALKAAGRAGDVIIVGFDGSNDVRDAIKEGKISATVL 235
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 928221397 276 QYPLKMASLGVTAGVDYAKTGKK-VTGYQDTGVTLIT 311
Cdd:cd19967  236 QPAKLIARLAVEQADQYLKGGSTgKEEKQLFDCVLIT 272
PRK09701 PRK09701
D-allose transporter substrate-binding protein;
13-299 2.03e-36

D-allose transporter substrate-binding protein;


Pssm-ID: 182037 [Multi-domain]  Cd Length: 311  Bit Score: 133.46  E-value: 2.03e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  13 KIVSMCVAASAVwCTSASQAADQPVVgliTKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDNASQVTAIENMMTA 92
Cdd:PRK09701   6 KYFSGTLVGLML-STSAFAAAEYAVV---LKTLSNPFWVDMKKGIEDEAKTLGVSVDIFASPSEGDFQSQLQLFEDLSNK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  93 GAKAILITPSDTKAIVPSIKKARAAGVMVVALDTPTDPQD------ATDALFATDNFKAGVLIGKYAKAALNGKPAKIAT 166
Cdd:PRK09701  82 NYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEKIDMDNlkkaggNVEAFVTTDNVAVGAKGASFIIDKLGAEGGEVAI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 167 LDLAPGVSVGVLRHNGFLEGFgVKEGDASIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGK 246
Cdd:PRK09701 162 IEGKAGNASGEARRNGATEAF-KKASQIKLVASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGK 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 928221397 247 DKSVMIVSIDGGCEGVRNVKAGSIAATSQQYPLKMASLGVTAGVDYAKTGKKV 299
Cdd:PRK09701 241 TGKVLVVGTDGIPEARKMVEAGQMTATVAQNPADIGATGLKLMVDAEKSGKVI 293
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
38-311 8.35e-36

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: 130.83  E-value: 8.35e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAA 117
Cdd:cd20005    2 IAVISKGFQHQFWKAVKKGAEQAAKELGVKITFEGPDTESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKEK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 118 GVMVVALDTPTDPqDATDALFATDNFKAGVLIGKYAkAALNGKPAKIATLDLAPGVSVGVLRHNGFLEGFGVKEGDASIV 197
Cdd:cd20005   82 GIPVVTFDSGVPS-DLPLATVATDNYAAGALAADHL-AELIGGKGKVAIVAHDATSETGIDRRDGFKDEIKEKYPDIKVV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 198 CSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAATSQQY 277
Cdd:cd20005  160 NVQYGVGDHAKAADIAKAILQANPDLKGIYATNEGAAIGVANALKEMGKLGKIKVVGFDSGEAQIDAIKNGVIAGSVTQN 239
                        250       260       270
                 ....*....|....*....|....*....|....
gi 928221397 278 PLKMASLGVTAGVDYAKtGKKVTGYQDTGVTLIT 311
Cdd:cd20005  240 PYGMGYKTVKAAVKALK-GEEVEKLIDTGAKWYD 272
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
49-311 2.78e-35

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


Pssm-ID: 380627 [Multi-domain]  Cd Length: 269  Bit Score: 129.10  E-value: 2.78e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  49 FFVKMKQGAEAAASKDGAKLITAAGRfdGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAAGVMVVALDTpt 128
Cdd:cd19972   13 FFNQIKQSVEAEAKKKGYKVITVDAK--GDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAGIPVIAVDR-- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 129 DPQDAT-DALFATDNFKAGVLIGKYAKAALNGKpAKIATLDLAPGVSVGVLRHNGFLEGFGvKEGDASIVCSQDTRGDQA 207
Cdd:cd19972   89 NPEDAPgDTFIATDSVAAAKELGEWVIKQTGGK-GEIAILHGQLGTTPEVDRTKGFQEALA-EAPGIKVVAEQTADWDQD 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 208 KGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAATSQQYPLKMASLGVT 287
Cdd:cd19972  167 EGFKVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGLDHKIWVVGFDGDVAGLKAVKDGVLDATMTQQTQKMGRLAVD 246
                        250       260
                 ....*....|....*....|....
gi 928221397 288 AGVDYaKTGKKVTGYQDTGVTLIT 311
Cdd:cd19972  247 SAIDL-LNGKAVPKEQLQDAVLTT 269
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
78-310 1.71e-28

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: 110.92  E-value: 1.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  78 DNAS-QVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAAGVMVVALDTPTDPQDAtDALFATDNFKAGVLIGKYAKAA 156
Cdd:cd06311   39 SNANeQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAGIPVVNFDRGLNVLIY-DLYVAGDNPGMGVVSAEYIGKK 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 157 LNGKpAKIATLDLAPGVSVGVLRHNGFLEGFGVKEGDaSIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAG 236
Cdd:cd06311  118 LGGK-GNVVVLEVPSSGSVNEERVAGFKEVIKGNPGI-KILAMQAGDWTREDGLKVAQDILTKNKKIDAVWAADDDMAIG 195
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928221397 237 AYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGS-IAATSQQYPLKMASLGVTAGVDYAKTGKKVTGYQDTGVTLI 310
Cdd:cd06311  196 VLQAIKEAGRTDIKVMTGGGGSQEYFKRIMDGDpIWPASATYSPAMIADAIKLAVLILKGGKTVEKEVIIPSTLV 270
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
38-298 4.87e-28

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: 110.05  E-value: 4.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRFDGdnASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAA 117
Cdd:cd06313    2 IGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDV--STQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 118 GVMVVALDTPTDPQDATdALFATDNFKAGVLIGKYAKAALNGKpAKIATLDLAPGVSVGVLRHNGFLEgFGVKEGDASIV 197
Cdd:cd06313   80 GIPLVGVNALIENEDLT-AYVGSDDVVAGELEGQAVADRLGGK-GNVVILEGPIGQSAQIDRGKGIEN-VLKKYPDIKVL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 198 CSQDTRGDQAKGQTAMENCLQKAPD-INVVYTINEPAAAGAYRALKAAGKDKsVMIVSIDGGCEGVRNVKAGSIAATSQQ 276
Cdd:cd06313  157 AEQTANWSRDEAMSLMENWLQAYGDeIDGIIAQNDDMALGALQAVKAAGRDD-IPVVGIDGIEDALQAVKSGELIATVLQ 235
                        250       260
                 ....*....|....*....|..
gi 928221397 277 YPLKMASLGVTAGVDYAKTGKK 298
Cdd:cd06313  236 DAEAQGKGAVEVAVDAVKGEGV 257
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
36-311 8.29e-28

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: 109.24  E-value: 8.29e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  36 PVVGLITKTDTNPFFVKMKQGAEAAASK-DGAKLITAAGrfDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKA 114
Cdd:cd06301    1 IKIGVSMQNFSDEFLTYLRDAIEAYAKEyPGVKLVIVDA--QSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 115 RAAGVMVVALDTPTDPQDATDALFATDNFKAGVLIGKYAKAALNGKpAKIATLDLAPGVSVGVLRHNGFLEGFGvKEGDA 194
Cdd:cd06301   79 ADAGIPLVYVNREPDSKPKGVAFVGSDDIESGELQMEYLAKLLGGK-GNIAILDGVLGHEAQILRTEGNKDVLA-KYPGM 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 195 SIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAATS 274
Cdd:cd06301  157 KIVAEQTANWSREKAMDIVENWLQSGDKIDAIVANNDEMAIGAILALEAAGKKDDILVAGIDATPDALKAMKAGRLDATV 236
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 928221397 275 QQYPLKMASLGVTAGVDYAKtGKKVTGYQDTGVTLIT 311
Cdd:cd06301  237 FQDAAGQGETAVDVAVKAAK-GEEVESDIWIPFELVT 272
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
45-277 3.48e-26

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: 105.01  E-value: 3.48e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  45 DTNPFFVKMKQGAEAAASKDGAKL-ITAAGRFDGdnASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAAGVMVVA 123
Cdd:cd06312   10 PSDPFWSVVKKGAKDAAKDLGVTVqYLGPQNNDI--ADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAAGIPVIA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 124 LDT-PTDPQDATDALF--ATDNFKAGVLIGKYAKAAlngKPAKIATLDLAPGVSVGVLRHNGFLEGFGVKEGDASIVcsq 200
Cdd:cd06312   88 INSgDDRSKERLGALTyvGQDEYLAGQAAGERALEA---GPKNALCVNHEPGNPGLEARCKGFADAFKGAGILVELL--- 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928221397 201 DTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAAT--SQQY 277
Cdd:cd06312  162 DVGGDPTEAQEAIKAYLQADPDTDAVLTLGPVGADPALKAVKEAGLKGKVKIGTFDLSPETLEAIKDGKILFAidQQPY 240
PBP1_ABC_sugar_binding-like cd19996
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
37-251 5.69e-26

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: 105.02  E-value: 5.69e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASK---DGAKLITAAGrfDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKK 113
Cdd:cd19996    1 TIGFSNAGLGNSWRVQMIAEFEAEAAKlkkLIKELIYTDA--QGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 114 ARAAGVMVVALDTPTDPQDATDALfATDNFKAGVLIGKYAKAALNGKpAKIATLDLAPGVSVGVLRHNGFLEGFGvKEGD 193
Cdd:cd19996   79 AAAAGIPVVLFDSGVGSDKYTAFV-GVDDAAFGRVGAEWLVKQLGGK-GNIIALRGIAGVSVSEDRWAGAKEVFK-EYPG 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 928221397 194 ASIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVM 251
Cdd:cd19996  156 IKIVGEVYADWDYAKAKQAVESLLAAYPDIDGVWSDGGAMTLGAIEAFEEAGRPLVPM 213
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
48-309 1.39e-25

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: 103.57  E-value: 1.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  48 PFFVKMKQGAEAAASKDGAKlITAAGRFDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAAGVMVVALDTp 127
Cdd:cd19969   12 PYWDDVKEGFEDAGAELGVK-TEYTGPATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIPVVTFDS- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 128 TDPQDATDALFATDNFKAGVLIGKYAKAALNGKpAKIATLDLaPGVSVGVLRHNGFLEGFGvKEGDASIVCSQDTRGDQA 207
Cdd:cd19969   90 DAPESKRISYVGTDNYEAGYAAAEKLAELLGGK-GKVAVLTG-PGQPNHEERVEGFKEAFA-EYPGIEVVAVGDDNDDPE 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 208 KGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAATSQQYPLKM------ 281
Cdd:cd19969  167 KAAQNTSALLQAHPDLVGIFGVDASGGVGAAQAVREAGKTGKVKIVAFDDDPETLDLIKDGVIDASIAQRPWMMgywslq 246
                        250       260       270
                 ....*....|....*....|....*....|..
gi 928221397 282 ----ASLGVTAGVDYAKTGKKVTGYQDTGVTL 309
Cdd:cd19969  247 flydLANGLVKDAWQTAGVNPLPPYVDTGITI 278
PBP1_ABC_xylose_binding-like cd19992
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
37-305 5.31e-25

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: 101.89  E-value: 5.31e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGrfDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARA 116
Cdd:cd19992    1 KIGVSFPTQQEERWQKDKEYMEEEAKELGVELIFQVA--DNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDTPtdPQDATDALFAT-DNFKAGVLIGKYA-KAALNGkpaKIATLDLAPGVSVGVLRHNGFLEGFG--VKEG 192
Cdd:cd19992   79 AGVPVISYDRL--ILNADVDLYVGrDNYKVGQLQAEYAlEAVPKG---NYVILSGDPGDNNAQLITAGAMDVLQpaIDSG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 193 DASIVCSQDTRG---DQAKGQtaMENCLQKA-PDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAG 268
Cdd:cd19992  154 DIKIVLDQYVKGwspDEAMKL--VENALTANnNNIDAVLAPNDGMAGGAIQALKAQGLAGKVFVTGQDAELAALKRIVEG 231
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 928221397 269 SIAATSQQYPLKMASLGVTAGVDYAKtGKKVTGYQDT 305
Cdd:cd19992  232 TQTMTVWKDLKELARAAADAAVKLAK-GEKPQTTDET 267
XylF COG4213
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ...
34-273 1.33e-23

ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism];


Pssm-ID: 443359 [Multi-domain]  Cd Length: 310  Bit Score: 98.67  E-value: 1.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  34 DQPVVGLI--TKTDTNpfFVKMKQGAEAAASKDGAKLITAAGrfDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSI 111
Cdd:COG4213    1 GKIKIGVSlpTKTSER--WIRDGDNFKAALKELGYEVDVQNA--NGDVATQLSQIENMITKGADVLVIAPIDGTALAAVL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 112 KKARAAGVMVVA-----LDTPTDpqdatdaLFAT-DNFKAGVLIGKYAKAALNGKP-AKIATLDLAPGVSVGVLRHNGFL 184
Cdd:COG4213   77 EKAKAAGIPVIAydrliLNSDVD-------YYVSfDNVKVGELQGQYLVDGLPLKGkGNIELFGGSPTDNNATLFFEGAM 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 185 EGFG--VKEGDASIVCSQDTRG-DQAKGQTAMENCLQKAP-DINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCE 260
Cdd:COG4213  150 SVLQpyIDSGKLVVVSGQWTLGwDPETAQKRMENLLTANGnKVDAVLAPNDGLAGGIIQALKAQGLAGKVVVTGQDAELA 229
                        250
                 ....*....|...
gi 928221397 261 GVRNVKAGSIAAT 273
Cdd:COG4213  230 AVQRILAGTQYMT 242
PBP1_ABC_xylose_binding-like cd19995
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
76-308 1.56e-22

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: 380650 [Multi-domain]  Cd Length: 294  Bit Score: 95.43  E-value: 1.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  76 DGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAAGVMVVALDTPTdPQDATDALFATDNFKAGVLIGKYAKA 155
Cdd:cd19995   41 NGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYDRLI-LGGPADYYVSFDNVAVGEAQAQSLVD 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 156 AL---NGKPAKIATLDLAPGVSVGVLRHNGFLEGF--GVKEGDASIVCSQDTRG-DQAKGQTAMENCLQKAP-DINVVYT 228
Cdd:cd19995  120 HLkaiGKKGVNIVMINGSPTDNNAGLFKKGAHEVLdpLGDSGELKLVCEYDTPDwDPANAQTAMEQALTKLGnNIDGVLS 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 229 INEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAATSQQYPLKMASLGVTAGVDYAKTGK----KVTGYQD 304
Cdd:cd19995  200 ANDGLAGGAIAALKAQGLAGKVPVTGQDATVAGLQRILAGDQYMTVYKPIKKEAAAAAKVAVALLKGETppsdLVTGTVT 279

                 ....
gi 928221397 305 TGVT 308
Cdd:cd19995  280 NGGD 283
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
48-301 2.10e-22

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: 94.57  E-value: 2.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  48 PFFVKMKQGAEAAASKDGAKLI--TAAGrfDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAAGVMVVALD 125
Cdd:cd06306   12 SYWVGVNYGIVDEAKRLGVKLTvyEAGG--YTNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGIPVIDLV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 126 TPTDPQDATDALFAtDNFKAGVLIGKYAKAALNGKPAKIATLDLAPGVSVGVLRHNGFLEgfGVKEGDASIVCSQdtRGD 205
Cdd:cd06306   90 NGIDSPKVAARVLV-DFYDMGYLAGEYLVEHHPGKPVKVAWFPGPAGAGWAEDREKGFKE--ALAGSNVEIVATK--YGD 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 206 QAK--GQTAMENCLQKAPDINvVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAATSQQYPLKMAS 283
Cdd:cd06306  165 TGKavQLNLVEDALQAHPDID-YIVGNAVAAEAAVGALREAGLTGKVKVVSTYLTPGVYRGIKRGKILAAPSDQPVLQGR 243
                        250
                 ....*....|....*...
gi 928221397 284 LGVTAGVDYAKtGKKVTG 301
Cdd:cd06306  244 IAVDQAVRALE-GKPVPK 260
PBP1_LsrB_Quorum_Sensing-like cd06302
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ...
38-308 6.25e-22

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: 93.85  E-value: 6.25e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAaGRFDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAA 117
Cdd:cd06302    2 IAFVPKVVGIPYFDAAEEGAKKAAKELGVEVVYT-GPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 118 GVMVVALDTPTDPQDATDALFATDNFKAGVLIGKYAkAALNGKPAKIATLDLAPGVSVGVLRHNGFLEGFGVKEGDASIV 197
Cdd:cd06302   81 GIKVITWDSDAPPSARDYFVNQADDEGLGEALVDSL-AKEIGGKGKVAILSGSLTATNLNAWIKAMKEYLKSKYPDIELV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 198 CSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIdggceGVRN-----VKAGSIAA 272
Cdd:cd06302  160 DTYYTDDDQQKAYTQAQNLIQAYPDLKGIIGVSTTAPPAAAQAVEEAGKTGKVAVTGI-----GLPNtarpyLKDGSVKE 234
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 928221397 273 TSQQYPLKMASLGVTAGVDYAKTGKKVTGYQDTGVT 308
Cdd:cd06302  235 GVLWDPAKLGYLTVYAAYQLLKGKGFTEDSDDVGTG 270
PBP1_ABC_sugar_binding-like cd06300
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ...
52-275 2.04e-21

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: 92.39  E-value: 2.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  52 KMKQGAEAAASKDGAKLITAAGRfDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAAGVMVVALDTPTdpq 131
Cdd:cd06300   20 SLKADAAQSGQKGLVKELIVANS-NGDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFDGAV--- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 132 DATDALFATDNFK-AGVLIGKYAKAALNGKpAKIATLDLAPGVSVGVLRHNGFLEGFGvKEGDASIVCSQDTRGDQAKGQ 210
Cdd:cd06300   96 TSPDAYNVSNDQVeWGRLGAKWLFEALGGK-GNVLVVRGIAGAPASADRHAGVKEALA-EYPGIKVVGEVFGGWDEATAQ 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928221397 211 TAMENCLQKAPDINVVYTiNEPAAAGAYRALKAAGKDK-SVMIVSIDGGCEGVRNVKA---GSIAATSQ 275
Cdd:cd06300  174 TAMLDFLATHPQVDGVWT-QGGEDTGVLQAFQQAGRPPvPIVGGDENGFAKQWWKHPKkglTGAAVWPP 241
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
38-311 9.50e-21

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: 90.05  E-value: 9.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGrfDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAA 117
Cdd:cd06305    2 IAVVRNGTSGDWDQQALQGAVAEAEKLGGTVIVFDA--NGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 118 GVMVVALDTPTDPQDATDAlfATDNFKAGVLIGKYAKAALNGKpAKIATLDLApGVSVGVLRH----NGFLEGFGVKEGD 193
Cdd:cd06305   80 GIPVVTFDTDSQVPGVNNI--TQDDYALGTLSLGQLVKDLNGE-GNIAVFNVF-GVPPLDKRYdiykAVLKANPGIKKIV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 194 ASI-VCSQDTRGDQakgQTAMENCLQKAPD--INVVY-TINEPaAAGAYRALKAAGKDKsVMIVSIDGGCEGVRNV-KAG 268
Cdd:cd06305  156 AELgDVTPNTAADA---QTQVEALLKKYPEggIDAIWaAWDEP-AKGAVQALEEAGRTD-IKVYGVDISNQDLELMaDEG 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 928221397 269 SI-AATSQQYPLKMASLGVTAGVDYAkTGKKVTGYQDTGVTLIT 311
Cdd:cd06305  231 SPwVATAAQDPALIGTVAVRNVARKL-AGEDLPDKYSLVPVLIT 273
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
41-278 3.62e-20

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: 88.48  E-value: 3.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  41 ITKTDTNPFFVKMKQGAEAAASKDGAKlITAAGRFDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAAGVM 120
Cdd:cd19965    5 VTHVTTNPFFQPVKKGMDDACELLGAE-CQFTGPQTFDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAGIP 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 121 VVALDTpTDPQDATDAL--FATDNFKAGVLIGKYAKAALNGKPAKIATLDLAPGVSVGVLRHNG---FLEGFGVKEGDAS 195
Cdd:cd19965   84 VVAFNV-DAPGGENARLafVGQDLYPAGYVLGKRIAEKFKPGGGHVLLGISTPGQSALEQRLDGikqALKEYGRGITYDV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 196 IvcsqDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAATSQ 275
Cdd:cd19965  163 I----DTGTDLAEALSRIEAYYTAHPDIKAIFATGAFDTAGAGQAIKDLGLKGKVLVGGFDLVPEVLQGIKAGYIDFTID 238

                 ...
gi 928221397 276 QYP 278
Cdd:cd19965  239 QQP 241
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
36-255 1.32e-19

Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the periplasmic binding proteins, and the LacI family transcriptional regulators. The periplasmic binding proteins are the primary receptors for chemotaxis and transport of many sugar based solutes. The LacI family of proteins consist of transcriptional regulators related to the lac repressor. In this case, generally the sugar binding domain binds a sugar which changes the DNA binding activity of the repressor domain (pfam00356).


Pssm-ID: 395423 [Multi-domain]  Cd Length: 281  Bit Score: 87.18  E-value: 1.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397   36 PVVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDNASQvtAIENMMTAGAKAILITPSDTKAivPSI-KKA 114
Cdd:pfam00532   2 LKLGALVPQLDEPFFQDLVKGITKAAKDHGFDVFLLAVGDGEDTLTN--AIDLLLASGADGIIITTPAPSG--DDItAKA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  115 RAAGVMVVAL-DTPTDPQDATDALFatDNFKAGVLIGKYAKAALNGKPakIATLDLAPGVSVGVLRHNGFLE-----GFG 188
Cdd:pfam00532  78 EGYGIPVIAAdDAFDNPDGVPCVMP--DDTQAGYESTQYLIAEGHKRP--IAVMAGPASALTARERVQGFMAalaaaGRE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 928221397  189 VKEGDASIVCSqdtrgDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSI 255
Cdd:pfam00532 154 VKIYHVATGDN-----DIPDAALAANAMLVSHPTIDAIVAMNDEAAMGAVRALLKQGRVKIPDIVGI 215
PBP1_ABC_xylose_binding-like cd19993
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
59-314 1.61e-19

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: 380648 [Multi-domain]  Cd Length: 287  Bit Score: 86.76  E-value: 1.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  59 AAASKDGAKLITAAGRfdGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAAGVMVVALDTPTDPQDATDALF 138
Cdd:cd19993   23 KALEKAGAKYISADAQ--SSAEKQLDDIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVIAYDRLIENPIAFYISF 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 139 atDNFKAGVLigkYAKAALNGKP-AKIATLDLAPGVSVGVLRHNGFLEGFG--VKEGDASIVCSQDTRG-DQAKGQTAME 214
Cdd:cd19993  101 --DNVEVGRM---QARGVLKAKPeGNYVFIKGSPTDPNADFLRAGQMEVLQpaIDSGKIKIVGEQYTDGwKPANAQKNME 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 215 NCL-QKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAATSQQYPLKMASLGVTAGVDYA 293
Cdd:cd19993  176 QILtANNNKVDAVVASNDGTAGGAVAALAAQGLAGKVPVSGQDADKAALNRIALGTQTVTVWKDARELGKEAAEIAVELA 255
                        250       260
                 ....*....|....*....|.
gi 928221397 294 KtGKKVTGYqdTGVTLITDKP 314
Cdd:cd19993  256 K-GTKIEAI--KGAALTNDGP 273
PBP1_ABC_sugar_binding-like cd19999
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
75-251 2.97e-19

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: 86.59  E-value: 2.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  75 FDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAAGVMVVALDTPTDPQDATDAlfATDNFKAGVLIGKYAK 154
Cdd:cd19999   42 ADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAGILVVSFDQPVSSPDAINV--VIDQYKWAAIQAQWLA 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 155 AALNGKpAKIATLDLAPGVSVGVLRHNGFLEGFGvKEGDASIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTiNEPAA 234
Cdd:cd19999  120 EQLGGK-GNIVAINGVAGNPANEARVKAADDVFA-KYPGIKVLASVPGGWDQATAQQVMATLLATYPDIDGVLT-QDGMA 196
                        170
                 ....*....|....*..
gi 928221397 235 AGAYRALKAAGKDKSVM 251
Cdd:cd19999  197 EGVLRAFQAAGKDPPVM 213
PBP1_arabinose_binding cd01540
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ...
37-311 5.47e-18

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: 82.72  E-value: 5.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDNAsqVTAIENMMTAGAKAILITPSDTKAIVPSIKKARA 116
Cdd:cd01540    1 KIGFIVKQPDQPWFQDEWKGAKKAAKELGFEVIKIDAKMDGEKV--LSAIDNLIAQGAQGIVICTPDQKLGPAIAAKAKA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDTP-TDPQDATDALFATDNFKA-----GVLIGKYAKAALNGKPAKIATLDLA-PGVSVGVLRHNGFLEGFGV 189
Cdd:cd01540   79 AGIPVIAVDDQlVDADPMKIVPFVGIDAYKigeavGEWLAKEMKKRGWDDVKEVGVLAITmDTLSVCVDRTDGAKDALKA 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 190 KEGDASIVCSQDTRG-DQAKGQTAMENCLQKAPDIN--VVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVK 266
Cdd:cd01540  159 AGFPEDQIFQAPYKGtDTEGAFNAANAVITAHPEVKhwLVVGCNDEGVLGAVRALEQAGFDAEDIIGVGIGGYLAADEEF 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 928221397 267 AGSIA---ATSQQYPLKMASLGVTAGVDYAKTGKKVTGYQDTGVTLIT 311
Cdd:cd01540  239 KKQPTgfkASLYISPDKHGYIAAEELYNWITDGKPPPAETLTDGVIVT 286
PBP1_ABC_sugar_binding-like cd19998
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
47-251 7.74e-18

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: 82.34  E-value: 7.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  47 NPFFVKMKQGAEA-AASKDGAKLITAAGRFDGDNAS-QVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAAGVMVVAL 124
Cdd:cd19998   11 NDWRQEMINIAKAaAKQPPYADKVELKVVSSGTDVQaQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 125 DTPTDPQDATDAlfATDNFKAGVLIGKYAKAALNGKpAKIATLDLAPGVSVGVLRHNGFLEGFGvKEGDASIVCSQDTRG 204
Cdd:cd19998   91 DNVVDEPCAYNV--NTDQAKAGEQTAQWLVDKLGGK-GNILMVRGVPGTSVDRDRYEGAKEVFK-KYPDIKVVAEYYGNW 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 928221397 205 DQAKGQTAMENCLQKAPDINVVYTinEPAAAGAYRALKAAGKDKSVM 251
Cdd:cd19998  167 DDGTAQKAVADALAAHPDVDGVWT--QGGETGVIKALQAAGHPLVPV 211
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
38-273 1.25e-17

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


Pssm-ID: 380547 [Multi-domain]  Cd Length: 317  Bit Score: 81.88  E-value: 1.25e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTD-TNPFFVKMKQGAEAAASKDGAKL-ITAAGRfdgDNASQVTAIENMMTAGAK-AILITPSDTKAIVPSIKKA 114
Cdd:cd06324    2 VVFINPGKeDEPFWQNVTRFMQAAAKDLGIELeVLYANR---NRFKMLELAEELLARPPKpDYLILVNEKGVAPELLELA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 115 RAAGVMVVALDTPTDPQDATDAL------------FATDNFKAGVLIGKY----AKAALNGKPAKIATLDLAPGVSVGVL 178
Cdd:cd06324   79 EQAKIPVFLINNDLTDEERALLGkprekfkywlgsIVPDNEQAGYLLAKAlikaARKKSDDGKIRVLAISGDKSTPASIL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 179 RHNGFLEGFgVKEGDASIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKD--KSVMIVSID 256
Cdd:cd06324  159 REQGLRDAL-AEHPDVTLLQIVYANWSEDEAYQKTEKLLQRYPDIDIVWAANDAMALGAIDALEEAGLKpgKDVLVGGID 237
                        250
                 ....*....|....*..
gi 928221397 257 GGCEGVRNVKAGSIAAT 273
Cdd:cd06324  238 WSPEALQAVKDGELTAS 254
PBP1_LsrB_Quorum_Sensing cd20003
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ...
37-253 6.70e-17

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: 79.63  E-value: 6.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAaGRFDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARA 116
Cdd:cd20003    1 TIAMIPKLVGVPYFTAAGQGAQEAAKELGVDVTYD-GPTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDTPTDPqDATDaLF---ATDNFKAGVLIGKYAKaaLNGKPAKIATLDLAPGVSVgvlrHNGFLEG----FGV 189
Cdd:cd20003   80 KGIKVVTWDSDVNP-DARD-FFvnqATPEGIGKTLVDMVAE--QTGEKGKVAIVTSSPTATN----QNAWIKAmkayIAE 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 928221397 190 KEGDASIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIV 253
Cdd:cd20003  152 KYPDMKIVTTQYGQEDPAKSLQVAENILKAYPDLKAIIAPDSVALPGAAEAVEQLGRTGKVAVT 215
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
37-257 1.26e-16

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


Pssm-ID: 380508 [Multi-domain]  Cd Length: 269  Bit Score: 78.42  E-value: 1.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRfdGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSikKARA 116
Cdd:cd06285    1 TIGVLVSDLSNPFYAELVEGIEDAARERGYTVLLADTG--DDPERELAALDSLLSRRVDGLIITPARDDAPDLQ--ELAA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDTPTDPQDAtdALFATDNFKAGVLIGKYAkAALnGKpAKIATLDLAPGVSVGVLRHNGF---LEGFGVKEGD 193
Cdd:cd06285   77 RGVPVVLVDRRIGDTAL--PSVTVDNELGGRLATRHL-LEL-GH-RRIAVVAGPLNASTGRDRLRGYrraLAEAGLPVPD 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928221397 194 ASIVcsqDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAG----KDKSVmiVSIDG 257
Cdd:cd06285  152 ERIV---PGGFTIEAGREAAYRLLSRPERPTAVFAANDLMAIGVLRAARDLGlrvpEDLSV--VGFDD 214
PBP1_ABC_rhamnose cd20000
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ...
38-131 2.67e-16

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: 78.07  E-value: 2.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLItAAGRFDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAA 117
Cdd:cd20000    2 IAFLPKSLGNPYFDAARDGAKEAAKELGGELI-FVGPTTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAA 80
                         90
                 ....*....|....
gi 928221397 118 GVMVVALDTPTDPQ 131
Cdd:cd20000   81 GIKVVTFDSDVAPE 94
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
37-257 6.40e-16

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 77.16  E-value: 6.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGrfDGDNASQVTAIENMMTAGAKAILITPSDTKAivPSIKKARA 116
Cdd:COG1609   63 TIGVVVPDLSNPFFAELLRGIEEAARERGYQLLLANS--DEDPEREREALRLLLSRRVDGLILAGSRLDD--ARLERLAE 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDTPTDpqDATDALFATDNFKAGVLIGKYAkAALNGKpaKIATLDLAPGVSVGVLRHNGFLEGF---GVKEGD 193
Cdd:COG1609  139 AGIPVVLIDRPLP--DPGVPSVGVDNRAGARLATEHL-IELGHR--RIAFIGGPADSSSARERLAGYREALaeaGLPPDP 213
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 928221397 194 ASIVCSQDTRGDqakGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKD--KSVMIVSIDG 257
Cdd:COG1609  214 ELVVEGDFSAES---GYEAARRLLARGPRPTAIFCANDLMALGALRALREAGLRvpEDVSVVGFDD 276
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
37-257 6.60e-16

ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily; Ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 periplasmic-binding fold protein superfamily. In most cases, ligands are monosaccharide including lactose, ribose, fructose, xylose, arabinose, galactose/glucose, and other sugars. The LacI family of proteins consists of transcriptional regulators related to the lac repressor. In this case, the domain sugar binding changes the DNA binding activity of the repressor domain.


Pssm-ID: 380491 [Multi-domain]  Cd Length: 264  Bit Score: 76.40  E-value: 6.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGrfDGDNASQVTAIENMMTAGAKAILITPSDTKAivPSIKKARA 116
Cdd:cd06267    1 TIGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNT--DEDPEREREYLRLLLSRRVDGIILAPSSLDD--ELLEELLA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDTPTDPQDAtDALfATDNFKAGVLIGKYAkAALNGKpaKIATLDLAPGVSVGVLRHNGF---LEGFGVKEGD 193
Cdd:cd06267   77 AGIPVVLIDRRLDGLGV-DSV-VVDNYAGAYLATEHL-IELGHR--RIAFIGGPLDLSTSRERLEGYrdaLAEAGLPVDP 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 928221397 194 ASIVCSQDTRGDqakGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKD--KSVMIVSIDG 257
Cdd:cd06267  152 ELVVEGDFSEES---GYEAARELLALPPRPTAIFAANDLMAIGALRALRELGLRvpEDISVVGFDD 214
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
44-278 2.33e-15

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: 75.05  E-value: 2.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  44 TDTNPFFVKMKQGAEAAASKDGAKLITaagRF-DGDNASQVTAIENMMTAGAKAILIT-PSDTKAIVPSIKKARAAGVMV 121
Cdd:cd19966    9 APGDPFWTVVYNGAKDAAADLGVDLDY---VFsSWDPEKMVEQFKEAIAAKPDGIAIMgHPGDGAYTPLIEAAKKAGIIV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 122 VALDTPtDP----QDATDALFATDNFKAGVLIGKYA-KAALNGKPAKIATLDLAPGVSVGVLRHNGFLEGF---GVKegd 193
Cdd:cd19966   86 TSFNTD-LPkleyGDCGLGYVGADLYAAGYTLAKELvKRGGLKTGDRVFVPGLLPGQPYRVLRTKGVIDALkeaGIK--- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 194 ASIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKS-VMIVSIDGGCEGVRNVKAGSIAA 272
Cdd:cd19966  162 VDYLEISLEPNKPAEGIPVMTGYLAANPDVKAIVGDGGGLTANVAKYLKAAGKKPGeIPVAGFDLSPATVQAIKSGYVNA 241

                 ....*.
gi 928221397 273 TSQQYP 278
Cdd:cd19966  242 TIDQQP 247
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
38-268 1.09e-14

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: 73.43  E-value: 1.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAgrFDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAA 117
Cdd:cd19994    2 IGISLPTKSEERWIKDGENLKSELEEAGYTVDLQY--ADDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 118 GVMVVALDTPTDPQDATDALFATDNFKAGVLIGKYAKAALNGKPAK-IATLDLAPGVS------------VGVLRhnGFL 184
Cdd:cd19994   80 GIPVIAYDRLIMNTDAVDYYVTFDNEKVGELQGQYLVDKLGLKDGKgPFNIELFAGSPddnnaqlffkgaMEVLQ--PYI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 185 E--GFGVKEGDASI--VCSQDTrgDQAKGQTAMENCLQKAP----DINVVYTINEPAAAGAYRALKAAGKDKSVMIVsID 256
Cdd:cd19994  158 DdgTLVVRSGQTTFeqVATPDW--DTETAQARMETLLSAYYtggkKLDAVLSPNDGIARGVIEALKAAGYDTGPWPV-VT 234
                        250
                 ....*....|....*
gi 928221397 257 G-GCE--GVRNVKAG 268
Cdd:cd19994  235 GqDAEdaSVKSILDG 249
PBP1_ABC_sugar_binding-like cd06316
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
38-302 1.54e-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: 380539 [Multi-domain]  Cd Length: 294  Bit Score: 72.66  E-value: 1.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLI-TAAGRFDGdnASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARA 116
Cdd:cd06316    2 VAIAMHTTGSDWSRLQVAGIKDTFEELGIEVVaVTDANFDP--AKQITDLETLIALKPDIIISIPVDPVATAAAYKKVAD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDTPTDPQDATD---ALFATDNFKAGVLIGKYAKAALNGKpAKIATLDLAPGVSVGVLRHNGFLEGFGVKEGD 193
Cdd:cd06316   80 AGIKLVFMDNVPDGLEAGKdyvSVVSSDNRGNGQIAAELLAEAIGGK-GKVGIIYHDADFYATNQRDKAFKDTLKEKYPD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 194 ASIVCSQDTRGDQAKGQTAMEnCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKsVMIVSIDGGCEGVRN-VKAGSIAA 272
Cdd:cd06316  159 IKIVAEQGFADPNDAEEVASA-MLTANPDIDGIYVSWDTPALGVISALRAAGRSD-IKITTVDLGTEIALDmAKGGNVKG 236
                        250       260       270
                 ....*....|....*....|....*....|
gi 928221397 273 TSQQYPLKMASLGVTAGVdYAKTGKKVTGY 302
Cdd:cd06316  237 IGAQRPYDQGVAEALAAA-LALLGKEVPPF 265
PBP1_ABC_xylose_binding-like cd01538
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ...
37-268 2.20e-14

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: 72.07  E-value: 2.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGrfDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARA 116
Cdd:cd01538    1 KIGVSLPNLREARWQTDRDIMVEQLEEKGAKVLVQSA--DGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDTPTdpQDATDALFAT-DNFKAGVLigkYAKAALNGKPAK-IATLDLAPGVSVGVLRHNG---FLEGFgVKE 191
Cdd:cd01538   79 EGIKVIAYDRLI--LNADVDYYISfDNEKVGEL---QAQALLDAKPEGnYVLIGGSPTDNNAKLFRDGqmkVLQPA-IDS 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 928221397 192 GDASIVCSQDTRG-DQAKGQTAMENCLQKA-PDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAG 268
Cdd:cd01538  153 GKIKVVGDQWVDDwLPANAQQIMENALTANgNNVDAVVASNDGTAGGAIAALKAQGLSGGVPVSGQDADLAAIKRILAG 231
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
38-256 3.26e-14

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


Pssm-ID: 380503 [Multi-domain]  Cd Length: 266  Bit Score: 71.52  E-value: 3.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGrfDGDNASQVTAIENMMTAGAKAILITPS-DTKAivpSIKKARA 116
Cdd:cd06280    2 IGLIVPDITNPFFTTIARGIEDAAEKHGYQVILANT--DEDPEKEKRYLDSLLSKQVDGIILAPSaGPSR---ELKRLLK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDTPTDPQDATdaLFATDNFKAGVligKYAKAALNGKPAKIATLDLAPGVSVGVLRHNGF---LEGFGVKEGD 193
Cdd:cd06280   77 HGIPIVLIDREVEGLELD--LVAGDNREGAY---KAVKHLIELGHRRIGLITGPLEISTTRERLAGYreaLAEAGIPVDE 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928221397 194 ASIVCSQDTRgdqAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKD--KSVMIVSID 256
Cdd:cd06280  152 SLIFEGDSTI---EGGYEAVKALLDLPPRPTAIFATNNLMAVGALRALRERGLEipQDISVVGFD 213
PBP1_ABC_xylose_binding cd19991
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ...
58-273 5.69e-14

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: 71.11  E-value: 5.69e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  58 EAAASKDGAK-LITAAgrfDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAAGVMVVALDTPTDPQDAtDA 136
Cdd:cd19991   22 VKKAKELGAEvIVQSA---NGDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYDRLILNADV-DL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 137 LFATDNFKAGVLigkYAKAALNGKP-AKIATLDLAPGVSVGVLRHNGFLEGFG--VKEGDASIVCSQDTRGDQA-KGQTA 212
Cdd:cd19991   98 YVSFDNEKVGEL---QAEALVKAKPkGNYVLLGGSPTDNNAKLFREGQMKVLQplIDSGDIKVVGDQWVDDWDPeEALKI 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 928221397 213 MENCLQKA-PDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAAT 273
Cdd:cd19991  175 MENALTANnNKIDAVIASNDGTAGGAIQALAEQGLAGKVAVSGQDADLAACQRIVEGTQTMT 236
PBP1_LsrB_Quorum_Sensing-like cd20001
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
38-160 1.06e-12

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: 67.30  E-value: 1.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKlITAAGRFDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAA 117
Cdd:cd20001    2 IAVVVKVTGIAWFDRMETGVEQFAKDTGVN-VYQIGPATADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDA 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 928221397 118 GVMVVALDTPTdpQDATDA-LFATDNFKAGVLIGKYAKAALNGK 160
Cdd:cd20001   81 GIVVITHEASN--LKNVDYdVEAFDNAAYGAFIMDKLAEAMGGK 122
Periplasmic_Binding_Protein_type1 cd01391
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
37-306 2.49e-12

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


Pssm-ID: 380477 [Multi-domain]  Cd Length: 280  Bit Score: 66.14  E-value: 2.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKT---DTNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDnaSQVTAIENMMTAGAKAILITPSDTKAIVPSIKk 113
Cdd:cd01391    1 IIGVVTSSlhqIREQFGIQRVEAIFHTADKLGASVEIRDSCWHGS--VALEQSIEFIRDNIAGVIGPGSSSVAIVIQNL- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 114 ARAAGVMVVALDT----PTDPQDATDALFAT-DNFKAGVLIGKYAKAALNGKPAKIATldlaPGVSVGVLRHNGFLEGFg 188
Cdd:cd01391   78 AQLFDIPQLALDAtsqdLSDKTLYKYFLSVVfSDTLGARLGLDIVKRKNWTYVAAIHG----EGLNSGELRMAGFKELA- 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 189 vKEGDASIVCSQ--DTRGDQaKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCE--GVRN 264
Cdd:cd01391  153 -KQEGICIVASDkaDWNAGE-KGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLVGDVSVIGSDGWADrdEVGY 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 928221397 265 VKAGSIAATSQQYPLKMASLGVTAGVDYAKTGKKVTGYQDTG 306
Cdd:cd01391  231 EVEANGLTTIKQQKMGFGITAIKAMADGSQNMHEEVWFDEKG 272
PBP1_LsrB_Quorum_Sensing-like cd20002
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
38-272 4.34e-12

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: 65.80  E-value: 4.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKlITAAGRFDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAA 117
Cdd:cd20002    2 IVTVVKLAGIPWFNRMEQGVKKAGKEFGVN-AYQVGPADADPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 118 GVMVVALDTPTDPQDATDALFAtDNFKAG-VLIGKYAKAAlnGKPAKIAtldlapgVSVGVLR---HNGFLEGF------ 187
Cdd:cd20002   81 GIVVITHESPGQKGADWDVELI-DNEKFGeAQMELLAKEM--GGKGEYA-------IFVGSLTvplHNLWADAAveyqke 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 188 ---GVKEGDASIVCSQDTrgDQAKgQTAMEnCLQKAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRN 264
Cdd:cd20002  151 kypNMKQVTDRIPGGEDV--DVSR-QTTLE-LLKAYPDLKGIISFGSLGPIGAGQALREKGLKGKVAVVGTVIPSQAAAY 226

                 ....*...
gi 928221397 265 VKAGSIAA 272
Cdd:cd20002  227 LKEGSITE 234
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
38-253 1.40e-11

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: 64.12  E-value: 1.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAA-GRFDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARA 116
Cdd:cd06307    2 FGFLLPSPENPFYELLRRAIEAAAAALRDRRVRLRiHFVDSLDPEALAAALRRLAAGCDGVALVAPDHPLVRAAIDELAA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDtpTD-PQDATDALFATDNFKAGV----LIGKYAKaalnGKPAKIATLDLAPGVSVGVLRHNGFLEGFGVKE 191
Cdd:cd06307   82 RGIPVVTLV--SDlPGSRRLAYVGIDNRAAGRtaawLMGRFLG----RRPGKVLVILGSHRFRGHEEREAGFRSVLRERF 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928221397 192 GDASIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTInepaAAGAY---RALKAAGKDKSVMIV 253
Cdd:cd06307  156 PDLTVLEVLEGLDDDELAYELLRELLARHPDLVGIYNA----GGGNEgiaRALREAGRARRVVFI 216
PBP1_GGBP cd01539
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ...
36-282 8.62e-11

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


Pssm-ID: 380481 [Multi-domain]  Cd Length: 302  Bit Score: 61.83  E-value: 8.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  36 PVVGLITKTDTNPFFVKMKQGAEAAASKDG-AKLITaagrFDGDN--ASQVTAIENMMTAGAKAILITPSDTKAIVPSIK 112
Cdd:cd01539    1 IKIGVFIYNYDDTFISSVRKALEKAAKAGGkIELEI----YDAQNdqSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIID 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 113 KARAAGVMVVALDTPTDPQDA---TDALFA-TDNFKAGVLIGKYAKAALNGKPAkiatLDL-------------APGVSV 175
Cdd:cd01539   77 KAKAANIPVIFFNREPSREDLksyDKAYYVgTDAEESGIMQGEIIADYWKANPE----IDKngdgkiqyvmlkgEPGHQD 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 176 GVLRHNGFLEGFGVKEGDASIVCSQDTRGDQAKGQTAMENCLQKAPD-INVVYTINEPAAAGAYRALKAAG-----KDKS 249
Cdd:cd01539  153 AIARTKYSVKTLNDAGIKTEQLAEDTANWDRAQAKDKMDAWLSKYGDkIELVIANNDDMALGAIEALKAAGyntgdGDKY 232
                        250       260       270
                 ....*....|....*....|....*....|...
gi 928221397 250 VMIVSIDGGCEGVRNVKAGSIAATSQQYPLKMA 282
Cdd:cd01539  233 IPVFGVDATPEALEAIKEGKMLGTVLNDAKAQA 265
PBP1_ABC_sugar_binding-like cd19997
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
53-261 8.98e-11

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: 61.92  E-value: 8.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  53 MKQGAEAAASKDGAK-LITAAGRFDGDN--ASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAAGVMVVALDTPTD 129
Cdd:cd19997   17 MVDAFEEAAKKAKADgLIADYIVVNADGsaTTQISQIQNLILQGVDAIVIDAASPTALNGAIQQACDAGIKVVVFDSGVT 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 130 PQDATDALFATDNFkaGVLIGKYAKAALNGKPAKIATLDLApGVSVGVLRHNGFLEGFGvKEGDASIVCSQDTRGDQAKG 209
Cdd:cd19997   97 EPCAYILNNDFEDY--GAASVEYVADRLGGKGNVLEVRGVA-GTSPDEEIYAGQVEALK-KYPDLKVVAEVYGNWTQSVA 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 928221397 210 QTAMENCLQKAPDINVVYTINEpAAAGAYRALKAAGKDKSVMIvsidGGCEG 261
Cdd:cd19997  173 QKAVTGILPSLPEVDAVITQGG-DGYGAAQAFEAAGRPLPIII----GGNRG 219
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
37-245 1.55e-10

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


Pssm-ID: 380516 [Multi-domain]  Cd Length: 270  Bit Score: 60.75  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGrfDGDNASQVTAIENMMTAGAKAILITPSDTKaiVPSIKKARA 116
Cdd:cd06293    1 TIGLVVPDVSNPFFAEVARGVEDAARERGYAVVLCNS--GRDPERERRYLEMLESQRVRGLIVTPSDDD--LSHLARLRA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDTPTDPQDATDAlfATDNFKAGVL-------IGKYAKAALNGkPAKIatldlapgVSVGvLRHNGFLEGFGV 189
Cdd:cd06293   77 RGTAVVLLDRPAPGPAGCSV--SVDDVQGGALavdhlleLGHRRIAFVSG-PLRT--------RQVA-ERLAGARAAVAE 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 928221397 190 KEGDASIVCSQDTRGDQ--AKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAG 245
Cdd:cd06293  145 AGLDPDEVVRELSAPDAnaELGRAAAAQLLAMPPRPTAVFAANDLLALGLLAGLRRAG 202
PBP1_sucrose_transcription_regulator cd06288
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ...
37-251 1.55e-10

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


Pssm-ID: 380511 [Multi-domain]  Cd Length: 268  Bit Score: 60.64  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLIT-KTDTNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDNASQvtAIENMMTAGAKAILITPSDTKAIVPSIKKAR 115
Cdd:cd06288    1 TIGLITdDIATTPFAGDIIRGAQDAAEEHGYLLLLANTGGDPELEAE--AIRELLSRRVDGIIYASMHHREVTLPPELTD 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 116 AAGVMVVALDTptDPQDATdalFATDNFKAG-----VLIGKYAK--AALNGKPAKIATldlapgvsvgVLRHNGF---LE 185
Cdd:cd06288   79 IPLVLLNCFDD--DPSLPS---VVPDDEQGGylatrHLIEAGHRriAFIGGPEDSLAT----------RLRLAGYraaLA 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 186 GFGVKEGDASIVCSQDTRGDqakGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAG----KDKSVM 251
Cdd:cd06288  144 EAGIPYDPSLVVHGDWGRES---GYEAAKRLLSAPDRPTAIFCGNDRMAMGVYQAAAELGlrvpEDLSVV 210
PBP1_LacI-like cd06299
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ...
37-256 1.99e-08

ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum produces significant amounts of L-glutamate directly from cheap sugar and ammonia; This group includes the ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum which has a unique ability to produce significant amounts of L-glutamate directly from cheap sugar and ammonia. This regulatory protein is a member of the LacI-GalR family of bacterial transcription repressors. The LacI-GalR family repressors are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380522 [Multi-domain]  Cd Length: 268  Bit Score: 54.59  E-value: 1.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGrfDGDNASQVTAIENMMTAGAKAILITPSDTKAivPSIKKARA 116
Cdd:cd06299    1 TIGLLVPDIRNPFFAELASGIEDEARAHGYSVILGNS--DEDPEREDESLEMLLSQRVDGIIAVPTGENS--EGLQALIA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 117 AGVMVVALDTPTDPQDATDALFAtDNFKAgvligkyAKAAL-----NGKpAKIATLDLAPGVSVGVLRHNGFLEGF---G 188
Cdd:cd06299   77 QGLPVVFVDREVEGLGGVPVVTS-DNRPG-------AREAVeylvsLGH-RRIGYISGPLSTSTGRERLAAFRAALtaaG 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 189 VKEGDASIVCSqDTRGDQakGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKD--KSVMIVSID 256
Cdd:cd06299  148 IPIDEELVAFG-DFRQDS--GAAAAHRLLSRGDPPTALIAGDSLMALGAIQALRELGLRigDDVSLISFD 214
PRK15408 PRK15408
autoinducer 2 ABC transporter substrate-binding protein LsrB;
12-245 6.78e-08

autoinducer 2 ABC transporter substrate-binding protein LsrB;


Pssm-ID: 237961  Cd Length: 336  Bit Score: 53.26  E-value: 6.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  12 RKIVSMCVAASAVWCTSASQAADQpvVGLITKTDTNPFFVKMKQGAEAAASKDGAKlITAAGRFDGDNASQVTAIENMMT 91
Cdd:PRK15408   2 KKKIALVSALGIALISMTVQAAER--IAFIPKLVGVGFFTSGGNGAKEAGKELGVD-VTYDGPTEPSVSGQVQLINNFVN 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  92 AGAKAILITPSDTKAIVPSIKKARAAGVMVVALDTPTDPQDATDALFATDNFKAGVLIGKYAKAALNGKPAKIATLDLAP 171
Cdd:PRK15408  79 QGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSYYINQGTPEQLGSMLVEMAAKQVGKDKAKVAFFYSSP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 172 GVSvgvlRHNGFlegfgVKEGDASI---------VCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINE---PAAAGAYR 239
Cdd:PRK15408 159 TVT----DQNQW-----VKEAKAKIakehpgweiVTTQFGYNDATKSLQTAEGILKAYPDLDAIIAPDAnalPAAAQAAE 229

                 ....*.
gi 928221397 240 ALKAAG 245
Cdd:PRK15408 230 NLKRDK 235
PBP1_FruR cd06274
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ...
38-214 1.83e-07

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


Pssm-ID: 380498 [Multi-domain]  Cd Length: 264  Bit Score: 51.44  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDNASQvtAIENMMTAGAKAILITPSdTKAIVPSiKKARAA 117
Cdd:cd06274    2 IGLIVPDLANRFFARLAEALERLARERGLQLLIACSDDDPEQERR--LVENLIARQVDGLIVAPS-TPPDDIY-YLCQAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 118 GVMVVALDTPTDPQDATdaLFATDNFKAG-VLIGKYAKAAlngkPAKIATLDLAPGVSVGVLRHNGFLEGF---GVKEGD 193
Cdd:cd06274   78 GLPVVFLDRPFSGSDAP--SVVSDNRAGArALTEKLLAAG----PGEIYFLGGRPELPSTAERIRGFRAALaeaGITEGD 151
                        170       180
                 ....*....|....*....|.
gi 928221397 194 ASIVCSQDTRgdqAKGQTAME 214
Cdd:cd06274  152 DWILAEGYDR---ESGYQLMA 169
PBP1_LuxPQ_Quorum_Sensing cd06303
periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi ...
74-273 7.63e-07

periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs; Periplasmic binding protein (LuxP) of autoinducer-2 (AI-2) receptor LuxPQ from Vibrio harveyi and its close homologs from other bacteria. The members of this group are highly homologous to a family of periplasmic pentose/hexose sugar-binding proteins that function as the primary receptors for chemotaxis and transport of many sugar based solutes in bacteria and archaea, and that are members of the type 1 periplasmic binding protein superfamily. The Vibrio harveyi AI-2 receptor consists of two polypeptides, LuxP and LuxQ: LuxP is a periplasmic binding protein that binds AI-2 by clamping it between two domains, LuxQ is an integral membrane protein belonging to the two-component sensor kinase family. Unlike AI-2 bound to the LsrB receptor in Salmonella typhimurium, the Vibrio harveyi AI-2 signaling molecule 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 LuxPQ to control light production as well as its motility behavior.


Pssm-ID: 380526 [Multi-domain]  Cd Length: 320  Bit Score: 50.06  E-value: 7.63e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  74 RFDGDNASQVTAIENMMTAGAKAILITPSDTKAiVPSIKKARAAGVMVVALDTPTDPQDATDAL-------FatDNFKAG 146
Cdd:cd06303   69 RPGAEIRLQALQIREMLKSDPDYLIFTLDALRH-RRFVEILLDSGKPKLILQNITTPLRDWDNHqpllyvgF--DHAEGS 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 147 VLIGKYAKAALnGKPAKIATLDLAPGVsVGVLRHNGFLEGFGvKEGDASIVCSQDTRGDQAKGQTAMENCLQKAPDINVV 226
Cdd:cd06303  146 RMLAKHFIKIF-PEEGKYAILYLTEGY-VSDQRGDTFIDEVA-RHSNLELVSAYYTDFDRESAREAARALLARHPDLDFI 222
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 928221397 227 YTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGSIAAT 273
Cdd:cd06303  223 YACSTDIALGAIDALQELGRETDIMINGWGGGSAELDALQKGGLDVT 269
PBP1_PurR cd06275
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ...
38-251 2.79e-06

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


Pssm-ID: 380499 [Multi-domain]  Cd Length: 269  Bit Score: 48.02  E-value: 2.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGrfDGDNASQVTAIENMMtagAKA----ILITPSDTKAIVPSIkk 113
Cdd:cd06275    2 IGLLVTSSENPFFAEVVRGVEDACFRAGYSLILCNS--DNDPEKQRAYLDMLA---EKRvdglLLMCSEMTDDDAELL-- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 114 ARAAGVMVVALDTptDPQDATDALFATDNFKAGVLIGKYAkAALNGKpaKIATLDLAPGVSVGVLRHNGF---LEGFGVK 190
Cdd:cd06275   75 AALRSIPVVVLDR--EIAGDNADAVLDDSFQGGYLATRHL-IELGHR--RIGCITGPLEHSVSRERLAGFrraLAEAGIE 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 928221397 191 EGDASIVcsqDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAG----KDKSVM 251
Cdd:cd06275  150 VPPSWIV---EGDFEPEGGYEAMQRLLSQPPRPTAVFACNDMMALGALRAAQEQGlrvpQDISII 211
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
38-257 3.23e-06

ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus Metalliredigens (strain Qymf) and its close homologs; This group includes the ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing bacterium Alkaliphilus metalliredigens (strain Qymf) and its close homologs. Qymf is a strict anaerobe that could be grown in the presence of borax and its cells are straight rods that produce endospores. This group is a member of the LacI-GalR family repressors that are composed of two functional domains: an N-terminal HTH (helix-turn-helix) domain, which is responsible for the DNA-binding specificity, and a C-terminal ligand-binding domain, which is homologous to the sugar-binding domain of ABC-type transport systems that contain the type 1 periplasmic binding protein-like fold. As also observed in the periplasmic binding proteins, the C-terminal domain of the bacterial transcription repressor undergoes a conformational change upon ligand binding which in turn changes the DNA binding affinity of the repressor.


Pssm-ID: 380514 [Multi-domain]  Cd Length: 264  Bit Score: 47.90  E-value: 3.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLITaaGRFDGDNASQVTAIE----NMMtAGakaiLITPSDTKAIVPSIKK 113
Cdd:cd06291    2 IGLIVPDISNPFFAELAKYIEKELFKKGYKMIL--CNSNEDEEKEKEYLEmlkrNKV-DG----IILGSHSLDIEEYKKL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 114 ARAagvmVVALDTPTDPQDATdalFATDNFKAGVLIGKY-----AK--AALNGKPAKIATLDlapgvsvgvlRHNGF--- 183
Cdd:cd06291   75 NIP----IVSIDRYLSEGIPS---VSSDNYQGGRLAAEHliekgCKkiLHIGGPSNNSPANE----------RYRGFeda 137
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 928221397 184 LEGFGVKEGDASIVCSQDTRGDqakGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKD--KSVMIVSIDG 257
Cdd:cd06291  138 LKEAGIEYEIIEIDENDFSEED---AYELAKELLEKYPDIDGIFASNDLLAIGVLKALQKLGIRvpEDVQIIGFDG 210
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
37-256 3.54e-06

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


Pssm-ID: 380512 [Multi-domain]  Cd Length: 268  Bit Score: 47.56  E-value: 3.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDnaSQVTAIENMMTAGAKAILITPS-DTKAIVPSIKKAR 115
Cdd:cd06289    1 TVGLIVPDLSNPFFAELLAGIEEALEEAGYLVFLANTGEDPE--RQRRFLRRMLEQGVDGLILSPAaGTTAELLRRLKAW 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 116 AAGVMVVALDTPTDPQDatdaLFATDNFKAGVLIGKYakaaLNGKPAK-IATLDLAPGVSVGVLRHNGF---LEGFGVKE 191
Cdd:cd06289   79 GIPVVLALRDVPGSDLD----YVGIDNRLGAQLATEH----LIALGHRrIAFLGGLSDSSTRRERLAGFraaLAEAGLPL 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 928221397 192 GDASIVCSQDTRGDqakGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKD--KSVMIVSID 256
Cdd:cd06289  151 DESLIVPGPATREA---GAEAARELLDAAPPPTAVVCFNDLVALGAMLALRRRGLEpgRDIAVVGFD 214
PBP1_GalS-like cd06270
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ...
38-251 5.70e-06

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


Pssm-ID: 380494 [Multi-domain]  Cd Length: 266  Bit Score: 47.13  E-value: 5.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  38 VGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDNASQvtAIENMMTAGAKAILITP--SDTKAIvpSIKKAR 115
Cdd:cd06270    2 IGLVVPDLSGPFFGSLLKGAERVARAHGKQLLITSGHHDAEEERE--AIEFLLDRRCDAIILHSraLSDEEL--ILIAEK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 116 AAGVMVVALDTPTDPqdatDALFATDNFKAGVLIGKYAkaaLNGKPAKIATLDLAPGVSVGVLRHNGF---LEGFGVKEG 192
Cdd:cd06270   78 IPPLVVINRYIPGLA----DRCVWLDNEQGGRLAAEHL---LDLGHRRIACITGPLDIPDARERLAGYrdaLAEAGIPLD 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928221397 193 DASIVCSQdtrGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAG----KDKSVM 251
Cdd:cd06270  151 PSLIIEGD---FTIEGGYAAAKQLLARGLPFTALFAYNDDMAIGALAALHEAGikvpEDVSVI 210
PBP1_LacI-like cd06290
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
37-245 4.63e-05

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


Pssm-ID: 380513 [Multi-domain]  Cd Length: 267  Bit Score: 44.14  E-value: 4.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDNASQvtAIENMMTAGAKA-ILITPSDTKAIVPSIKKar 115
Cdd:cd06290    1 TIGVLVPDIDSPFYSEILNGIEEVLAESGYTLIVSTSHWNADRELE--ILRLLLARKVDGiIVVGGFGDEELLKLLAE-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 116 aaGVMVVALDTptDPQDATDALFATDNFKAGVLIGKYAkaaLNGKPAKIATLDLAPGVSVGVLRHNGF---LEGFGVKEG 192
Cdd:cd06290   77 --GIPVVLVDR--ELEGLNLPVVNVDNEQGGYNATNHL---IDLGHRRIVHISGPEDHPDAQERYAGYrraLEDAGLEVD 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 928221397 193 DASIVCsqdtrGD--QAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAG 245
Cdd:cd06290  150 PRLIVE-----GDftEESGYEAMKKLLKRGGPFTAIFAANDLMALGAMKALREAG 199
PRK15395 PRK15395
galactose/glucose ABC transporter substrate-binding protein MglB;
12-273 9.46e-05

galactose/glucose ABC transporter substrate-binding protein MglB;


Pssm-ID: 185293 [Multi-domain]  Cd Length: 330  Bit Score: 43.56  E-value: 9.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  12 RKIVSMCVAASAVWCTSASQAADQPVVGLITKTDTNpFFVKMKQG--AEAAASKDGAKLITaagrfDGDNAS--QVTAIE 87
Cdd:PRK15395   2 KKVLTLSALMASMLFGAAAAAADTRIGVTIYKYDDN-FMSVVRKAieKDAKAAPDVQLLMN-----DSQNDQskQNDQID 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  88 NMMTAGAKAILITPSDTKAIVPSIKKARAAGVMVVALDTptDPQDATDALF------ATDNFKAGV----LIGKYAKAA- 156
Cdd:PRK15395  76 VLLAKGVKALAINLVDPAAAPTVIEKARGQDVPVVFFNK--EPSRKALDSYdkayyvGTDSKESGIiqgdLIAKHWKANp 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 157 ---LNgKPAKI--ATLDLAPGVSVGVLRHNgflegFGVKEGDASIVCSQDTRGDQAKGQTAMEN-------CLQKAPDIN 224
Cdd:PRK15395 154 awdLN-KDGKIqyVLLKGEPGHPDAEARTT-----YVIKELNDKGIKTEQLQLDTAMWDTAQAKdkmdawlSGPNANKIE 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 928221397 225 VVYTINEPAAAGAYRALKAAGKDKsVMIVSIDGGCEGVRNVKAGSIAAT 273
Cdd:PRK15395 228 VVIANNDAMAMGAVEALKAHNKSS-IPVFGVDALPEALALVKSGAMAGT 275
xylF PRK10355
D-xylose ABC transporter substrate-binding protein;
60-269 1.06e-04

D-xylose ABC transporter substrate-binding protein;


Pssm-ID: 182403 [Multi-domain]  Cd Length: 330  Bit Score: 43.58  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  60 AASKDGAKLITAAGrfDGDNASQVTAIENMMTAGAKAILITPSDTKAIVPSIKKARAAGVMVVALDTPTDPQDaTDALFA 139
Cdd:PRK10355  50 KAESLGAKVFVQSA--NGNEETQMSQIENMINRGVDVLVIIPYNGQVLSNVIKEAKQEGIKVLAYDRMINNAD-IDFYIS 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 140 TDNFKAGVLigkYAKAALNGKPAkiATLDLAPGVSVGvlrHNGFLEGFG--------VKEGDASIVcsqdtrGDQ----- 206
Cdd:PRK10355 127 FDNEKVGEL---QAKALVDKVPQ--GNYFLMGGSPVD---NNAKLFRAGqmkvlkpyIDSGKIKVV------GDQwvdgw 192
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 928221397 207 --AKGQTAMENCLQ-KAPDINVVYTINEPAAAGAYRALKAAGKDKSVMIVSIDGGCEGVRNVKAGS 269
Cdd:PRK10355 193 lpENALKIMENALTaNNNKIDAVVASNDATAGGAIQALSAQGLSGKVAISGQDADLAAIKRIVAGT 258
PBP1_AglR-like cd20010
Ligand-binding domain of DNA transcription repressor specific for alpha-glucosides (AglR) and ...
37-282 1.97e-04

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


Pssm-ID: 380665 [Multi-domain]  Cd Length: 269  Bit Score: 42.54  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTD----TNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDnasQVTAIENMMTAG-AKAILITpsDTKAIVPSI 111
Cdd:cd20010    1 AIGLVLPLDpgdlGDPFFLEFLAGLSEALAERGLDLLLAPAPSGED---ELATYRRLVERGrVDGFILA--RTRVNDPRI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 112 KKARAAGVMVVALDTPTDPQDAtdALFATDNFKAGV-----LIgkyakaALNGKpaKIATLDLAPGVSVGVLRHNGFLEG 186
Cdd:cd20010   76 AYLLERGIPFVVHGRSESGAPY--AWVDIDNEGAFRratrrLL------ALGHR--RIALLNGPEELNFAHQRRDGYRAA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 187 F---GVKEGDASIVCSQDTRGDqakGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGK--DKSVMIVSIDGgceG 261
Cdd:cd20010  146 LaeaGLPVDPALVREGPLTEEG---GYQAARRLLALPPPPTAIVCGSDLLALGAYRALREAGLspGKDVSVIGHDD---L 219
                        250       260
                 ....*....|....*....|.
gi 928221397 262 VRNVKAGSIAATSQQYPLKMA 282
Cdd:cd20010  220 LPALEYFSPPLTTTRSSLRDA 240
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
141-257 2.03e-04

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


Pssm-ID: 380484 [Multi-domain]  Cd Length: 259  Bit Score: 42.10  E-value: 2.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 141 DNFKAGVLIGKYAkAALNGKpaKIATLDLAPG-VSVGVLRHNGFLEGFgvKEGDASIVCSQDTRGDQAKGQTAMENCLQK 219
Cdd:cd01542   97 DDYGAGKLLGEYL-LKKGHK--NIAYIGVDEEdIAVGVARKQGYLDAL--KEHGIDEVEIVETDFSMESGYEAAKELLKE 171
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 928221397 220 -APDINVVYTINepAAAGAYRALKAAGKD--KSVMIVSIDG 257
Cdd:cd01542  172 nKPDAIICATDN--IALGAIKALRELGIKipEDISVAGFGG 210
PBP1_AglR_RafR-like cd06292
Ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that ...
37-251 2.12e-04

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


Pssm-ID: 380515 [Multi-domain]  Cd Length: 273  Bit Score: 42.25  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLI----TKTDTNPFFVKMKQGAEAAASKDGAKLITAAGrfdGDNASQVTAIENMMTAGAKAILITpSDTKAIVPSIK 112
Cdd:cd06292    1 LIGYVvpelPGGFSDPFFDEFLAALGHAAAARGYDVLLFTA---SGDEDEIDYYRDLVRSRRVDGFVL-ASTRHDDPRVR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 113 KARAAGVMVVALDTPTDPQDATDalFATDNFKAGVLIGKYAKAAlnGKpAKIATLDLAPGVSVGVLRHNGFLEG---FGV 189
Cdd:cd06292   77 YLHEAGVPFVAFGRANPDLDFPW--VDVDGAAGMRQAVRHLIAL--GH-RRIGLIGGPEGSVPSDDRLAGYRAAleeAGL 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 928221397 190 KEGDASIVCSQDtrgDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAG----KDKSVM 251
Cdd:cd06292  152 PFDPGLVVEGEN---TEEGGYAAAARLLDLGPPPTAIVCVSDLLALGAMRAARERGlrvgRDVSVV 214
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
37-245 5.02e-04

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


Pssm-ID: 380489 [Multi-domain]  Cd Length: 269  Bit Score: 40.94  E-value: 5.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDNASQVtaIENMMTAGAKAILITPSD-TKAivpSIKKAR 115
Cdd:cd01575    1 LVAVVVPSLSNSVFAETLQGLSDVLEPAGYQLLLGNTGYSPEREEEL--IRALLSRRPAGLILTGTEhTPA---TRKLLR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 116 AAGVMVV-ALDTPTDPqdaTDALFATDNFKAGVLIGKYAKAAlnG--KPAKIATLDlaPGVSVGVLRHNGFLEGFGVKEG 192
Cdd:cd01575   76 AAGIPVVeTWDLPDDP---IDMAVGFSNFAAGRAMARHLIER--GyrRIAFVGARL--DGDSRARQRLEGFRDALAEAGL 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 928221397 193 DASIVCSQDTRGDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAG 245
Cdd:cd01575  149 PLPLVLLVELPSSFALGREALAELLARHPDLDAIFCSNDDLALGALFECQRRG 201
PBP1_MalR-like cd06294
ligand-binding domain of maltose transcription regulator MalR which is a member of the ...
37-256 7.35e-04

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


Pssm-ID: 380517 [Multi-domain]  Cd Length: 269  Bit Score: 40.64  E-value: 7.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDT-----NPFFVKMKQGAEAAASKDGAKLITAAGRFDGDNASQVtaiENMMTAGA-KAILITPSDTKAivPS 110
Cdd:cd06294    1 TIGLVLPSSAeelfqNPFFSEVLRGISQVANENGYSLLLATGNTEEELLEEV---KRMVRGRRvDGFILLYSKEDD--PL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 111 IKKARAAGVMVVALDTPTDPQDAT--DalfaTDNFKAG-----VLIGKYAKaalngkpaKIATLDLAPGVSVGVLRHNGF 183
Cdd:cd06294   76 IEYLKEEGFPFVVIGKPLDDNDVLyvD----NDNVQAGyeateYLIDKGHK--------RIAFIGGDKNLVVSIDRLQGY 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 928221397 184 ---LEGFGVKEGDASIVCSQDTRGDqakGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKD--KSVMIVSID 256
Cdd:cd06294  144 kqaLKEAGLPLDDDYILLLDFSEED---GYDALQELLSKPPPPTAIVATDDLLALGVLRYLQELGLRvpEDVSIISFN 218
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
46-251 1.43e-03

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


Pssm-ID: 380507 [Multi-domain]  Cd Length: 267  Bit Score: 39.83  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  46 TNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDNasQVTAIENMMTAGAKAILITpsDTKAIVPSIKKARAAGVMVVALD 125
Cdd:cd06284   10 SNPFYSEILRGIEDAAAEAGYDVLLGDTDSDPER--EDDLLDMLRSRRVDGVILL--SGRLDAELLSELSKRYPIVQCCE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 126 TPTDPQDATdalFATDNFKAGVLIGKYakaaL--NGKpAKIATLDLAPGVSVGVLRHNGF---LEGFGVKEgDASIVCSQ 200
Cdd:cd06284   86 YIPDSGVPS---VSIDNEAAAYDATEY----LisLGH-RRIAHINGPLDNVYARERLEGYrraLAEAGLPV-DEDLIIEG 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 928221397 201 DTrgDQAKGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAG----KDKSVM 251
Cdd:cd06284  157 DF--SFEAGYAAARALLALPERPTAIFCASDELAIGAIKALRRAGlrvpEDVSVI 209
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
37-256 4.19e-03

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


Pssm-ID: 380632 [Multi-domain]  Cd Length: 264  Bit Score: 38.28  E-value: 4.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLI---TaagrfDGDNASQVTAIENMMTAGAKAILITPSDTKAivPSIKK 113
Cdd:cd19977    1 TIGLIVADILNPFFTSVVRGIEDEAYKNGYHVIlcnT-----DEDPEKEKKYIEMLRAKQVDGIIIAPTGGNE--DLIEK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 114 ARAAGVMVVALDTpTDPQDATDAlFATDNFKAGV-----LIGKYAKaalngkpaKIATLDLAPGVSVGVLRHNGF---LE 185
Cdd:cd19977   74 LVKSGIPVVFVDR-YIPGLDVDT-VVVDNFKGAYqatehLIELGHK--------RIAFITYPLELSTRQERLEGYkaaLA 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 928221397 186 GFGVKEgDASIVCSQDTRGDqakGQTAMENCLQKAPDINVVYTINEPAAAGAYRALKAAGKD--KSVMIVSID 256
Cdd:cd19977  144 DHGLPV-DEELIKHVDRQDD---VRKAISELLKLEKPPDAIFAANNLITLEVLKAIKELGLRipDDIALIGFD 212
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
37-152 7.21e-03

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


Pssm-ID: 380483 [Multi-domain]  Cd Length: 274  Bit Score: 37.54  E-value: 7.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  37 VVGLITKTDTNPFFVKMKQGAEAAASKDGAKLITAAGRFDGDNASQvtAIENMMTAGAKAILITPsdTKAIVPSI----- 111
Cdd:cd01541    1 TIGVITTYIDDYIFPSIIQGIESVLSENGYSLLLALTNNDVEKERE--ILESLLDQNVDGLIIEP--TKSALPNPnldly 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 928221397 112 KKARAAGVMVVALDTPTDPQDAtdALFATDNFKAGVLIGKY 152
Cdd:cd01541   77 EELQKKGIPVVFINSYYPELDA--PSVSLDDEKGGYLATKH 115
PBP1_CatR-like cd06296
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ...
47-251 7.58e-03

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


Pssm-ID: 380519 [Multi-domain]  Cd Length: 270  Bit Score: 37.64  E-value: 7.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397  47 NPFFVKMKQGAEAAASKDGAKLITAAGRFDGDNASQvtAIENMMTAGAKAILITPSDtkAIVPSIKKARAAGVMVVALDT 126
Cdd:cd06296   11 SPYALEVLRGVERAAAAAGLDLVVTATRAGRAPVDD--WVRRAVARGSAGVVLVTSD--PTSRQLRLLRSAGIPFVLIDP 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 928221397 127 PTDPQDATDALfATDNFKAGVLIGKYAkAALNGKpaKIATLDLAPGVSVGVLRHNGFLEGFgvkeGDASIVCSQDT-RGd 205
Cdd:cd06296   87 VGEPDPDLPSV-GATNWAGGRLATEHL-LDLGHR--RIAVITGPPRSVSGRARLAGYRAAL----AEAGIAVDPDLvRE- 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 928221397 206 qakGQTAMENCLQKAPDI-------NVVYTINEPAAAGAYRALKAAG----KDKSVM 251
Cdd:cd06296  158 ---GDFTYEAGYRAARELlelpdppTAVFAGNDEQALGVYRAARALGlrvpDDLSVI 211
 
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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