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Conserved domains on  [gi|499969044|ref|WP_011649762|]
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MULTISPECIES: substrate-binding domain-containing protein [Rhizobium]

Protein Classification

type 1 periplasmic-binding domain-containing protein( domain architecture ID 70)

type 1 periplasmic-binding domain-containing protein such as the ligand binding domains of the LacI family of transcriptional regulators, the ABC transporter substrate-binding proteins, the family C GPCRs, membrane bound guanylyl cyclases including the family of natriuretic peptide receptors (NPRs), and the N-terminal LIVBP-like domains of the ionotropic glutamate receptors (iGluRs); contains the Venus flytrap-like domain which undergoes transition from an open to a closed conformational state upon ligand binding

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Periplasmic_Binding_Protein_type1 super family cl10011
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
 40-310 4.43e-80

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.


The actual alignment was detected with superfamily member cd06305:

Pssm-ID: 471960 [Multi-domain]  Cd Length: 273  Bit Score: 245.67  E-value: 4.43e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISAGDFFQAYQAGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKG 119
Cdd:cd06305    1 TIAVVRNGTSGDWDQQALQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 120 IKVVAFDVNLNNPKIPQVEQSDHELASLALEQVVKDNGNSFNAGYVYVAGFAPLDRRNEVWDKFKSDNKGV-VEKARFGN 198
Cdd:cd06305   81 IPVVTFDTDSQVPGVNNITQDDYALGTLSLGQLVKDLNGEGNIAVFNVFGVPPLDKRYDIYKAVLKANPGIkKIVAELGD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 199 VSDTTATSTADQAKAVLTANPD--ISVVFAPYDEFARGVKLAANDLGiASKLKIYSADVSTADIQEIIEEGSPWVATVAT 276
Cdd:cd06305  161 VTPNTAADAQTQVEALLKKYPEggIDAIWAAWDEPAKGAVQALEEAG-RTDIKVYGVDISNQDLELMADEGSPWVATAAQ 239

                        250       260       270
                 ....*....|....*....|....*....|....
gi 499969044 277 NPAVVGAVSIRAAALEIAGQTVPHQITVKPTLLT 310
Cdd:cd06305  240 DPALIGTVAVRNVARKLAGEDLPDKYSLVPVLIT 273
 
Name Accession Description Interval E-value
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
 40-310 4.43e-80

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: 245.67  E-value: 4.43e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISAGDFFQAYQAGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKG 119
Cdd:cd06305    1 TIAVVRNGTSGDWDQQALQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 120 IKVVAFDVNLNNPKIPQVEQSDHELASLALEQVVKDNGNSFNAGYVYVAGFAPLDRRNEVWDKFKSDNKGV-VEKARFGN 198
Cdd:cd06305   81 IPVVTFDTDSQVPGVNNITQDDYALGTLSLGQLVKDLNGEGNIAVFNVFGVPPLDKRYDIYKAVLKANPGIkKIVAELGD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 199 VSDTTATSTADQAKAVLTANPD--ISVVFAPYDEFARGVKLAANDLGiASKLKIYSADVSTADIQEIIEEGSPWVATVAT 276
Cdd:cd06305  161 VTPNTAADAQTQVEALLKKYPEggIDAIWAAWDEPAKGAVQALEEAG-RTDIKVYGVDISNQDLELMADEGSPWVATAAQ 239

                        250       260       270
                 ....*....|....*....|....*....|....
gi 499969044 277 NPAVVGAVSIRAAALEIAGQTVPHQITVKPTLLT 310
Cdd:cd06305  240 DPALIGTVAVRNVARKLAGEDLPDKYSLVPVLIT 273
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 2-314 1.59e-43

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: 152.39  E-value: 1.59e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044   2 KSLARLALSAAVIPFIFIQGAKADGLSGAPApfdkGGVKVALISYISAGDFFQAYQAGAEAQAKALDIDLRIFPGRQDAA 81
Cdd:COG1879    1 KRLALLAAVLALALALAACGSAAAEAAAAAA----KGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  82 EQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNLNNPK-IPQVEQSDHELASLALEQVVKDNGNSF 160
Cdd:COG1879   77 KQISQIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDrVAYVGSDNYAAGRLAAEYLAKALGGKG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 161 NAGYVY-VAGFAPLDRRNEVWDKFKSDNKGVVEKARFgnVSDTTATSTADQAKAVLTANPDISVVFAPYDEFARGVKLAA 239
Cdd:COG1879  157 KVAILTgSPGAPAANERTDGFKEALKEYPGIKVVAEQ--YADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQAL 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499969044 240 NDLGIASKLKIYSADVSTADIQEIIEegSPWVATVATNPAVVGAVSIRAAALEIAGQTVPHQITVKPTLLTQESL 314
Cdd:COG1879  235 KAAGRKGDVKVVGFDGSPEALQAIKD--GTIDATVAQDPYLQGYLAVDAALKLLKGKEVPKEILTPPVLVTKENV 307
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 41-297 5.09e-30

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: 115.10  E-value: 5.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044   41 VALISYISAGDFFQAYQAGAEAQAKALDIDLRI-FPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKG 119
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVvGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  120 IKVVAFDV-NLNNPKIPQVEQSDHELASLALEQVVKDNGNSFNagYVYVAGFAP----LDRRNEVWDKFKSDNKGVVEKA 194
Cdd:pfam13407  81 IPVVTFDSdAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGK--VAILSGSPGdpnaNERIDGFKKVLKEKYPGIKVVA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  195 RFGNVSDTTATSTaDQAKAVLTANPD-ISVVFAPYDEFARGVKLAANDLGIASKLKIYSADVSTADIQEIIEEGSPwvAT 273
Cdd:pfam13407 159 EVEGTNWDPEKAQ-QQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGKVVVTGFDATPEALEAIKDGTID--AT 235

                         250       260
                  ....*....|....*....|....
gi 499969044  274 VATNPAVVGAVSIRAAALEIAGQT 297
Cdd:pfam13407 236 VLQDPYGQGYAAVELAAALLKGKK 259
PRK09701 PRK09701
D-allose transporter substrate-binding protein;
52-287 1.17e-07

D-allose transporter substrate-binding protein;


Pssm-ID: 182037 [Multi-domain]  Cd Length: 311  Bit Score: 52.57  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  52 FFQAYQAGAEAQAKALDIDLRIF--PGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFD--V 127
Cdd:PRK09701  38 FWVDMKKGIEDEAKTLGVSVDIFasPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDekI 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 128 NLNNPKipqvEQSDHELASLALEQV-VKDNGNSF-------NAGYVYV----AGFAP-LDRRNEVWDKFKSDNKgvvEKA 194
Cdd:PRK09701 118 DMDNLK----KAGGNVEAFVTTDNVaVGAKGASFiidklgaEGGEVAIiegkAGNASgEARRNGATEAFKKASQ---IKL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 195 RFGNVSDTTATSTADQAKAVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADvSTADIQEIIEEGSpWVATV 274
Cdd:PRK09701 191 VASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTD-GIPEARKMVEAGQ-MTATV 268

                        250
                 ....*....|...
gi 499969044 275 ATNPAVVGAVSIR 287
Cdd:PRK09701 269 AQNPADIGATGLK 281
 
Name Accession Description Interval E-value
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
 40-310 4.43e-80

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: 245.67  E-value: 4.43e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISAGDFFQAYQAGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKG 119
Cdd:cd06305    1 TIAVVRNGTSGDWDQQALQGAVAEAEKLGGTVIVFDANGDDARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 120 IKVVAFDVNLNNPKIPQVEQSDHELASLALEQVVKDNGNSFNAGYVYVAGFAPLDRRNEVWDKFKSDNKGV-VEKARFGN 198
Cdd:cd06305   81 IPVVTFDTDSQVPGVNNITQDDYALGTLSLGQLVKDLNGEGNIAVFNVFGVPPLDKRYDIYKAVLKANPGIkKIVAELGD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 199 VSDTTATSTADQAKAVLTANPD--ISVVFAPYDEFARGVKLAANDLGiASKLKIYSADVSTADIQEIIEEGSPWVATVAT 276
Cdd:cd06305  161 VTPNTAADAQTQVEALLKKYPEggIDAIWAAWDEPAKGAVQALEEAG-RTDIKVYGVDISNQDLELMADEGSPWVATAAQ 239

                        250       260       270
                 ....*....|....*....|....*....|....
gi 499969044 277 NPAVVGAVSIRAAALEIAGQTVPHQITVKPTLLT 310
Cdd:cd06305  240 DPALIGTVAVRNVARKLAGEDLPDKYSLVPVLIT 273
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
 2-314 1.59e-43

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: 152.39  E-value: 1.59e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044   2 KSLARLALSAAVIPFIFIQGAKADGLSGAPApfdkGGVKVALISYISAGDFFQAYQAGAEAQAKALDIDLRIFPGRQDAA 81
Cdd:COG1879    1 KRLALLAAVLALALALAACGSAAAEAAAAAA----KGKTIGFVVKTLGNPFFVAVRKGAEAAAKELGVELIVVDAEGDAA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  82 EQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNLNNPK-IPQVEQSDHELASLALEQVVKDNGNSF 160
Cdd:COG1879   77 KQISQIEDLIAQGVDAIIVSPVDPDALAPALKKAKAAGIPVVTVDSDVDGSDrVAYVGSDNYAAGRLAAEYLAKALGGKG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 161 NAGYVY-VAGFAPLDRRNEVWDKFKSDNKGVVEKARFgnVSDTTATSTADQAKAVLTANPDISVVFAPYDEFARGVKLAA 239
Cdd:COG1879  157 KVAILTgSPGAPAANERTDGFKEALKEYPGIKVVAEQ--YADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQAL 234

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499969044 240 NDLGIASKLKIYSADVSTADIQEIIEegSPWVATVATNPAVVGAVSIRAAALEIAGQTVPHQITVKPTLLTQESL 314
Cdd:COG1879  235 KAAGRKGDVKVVGFDGSPEALQAIKD--GTIDATVAQDPYLQGYLAVDAALKLLKGKEVPKEILTPPVLVTKENV 307
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
 40-308 8.26e-35

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: 128.07  E-value: 8.26e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISAGDFFQAYQAGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKG 119
Cdd:cd01536    1 KIGVVVKDLTNPFWVAVKKGAEAAAKELGVELVVLDAQGDVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 120 IKVVAFDVNLNNP--KIPQVEQSDHELASLALEQVVKDNGNSFNAGYVY-VAGFAPLDRRNEVWDKFKSDNKGVVEkarf 196
Cdd:cd01536   81 IPVVAVDTDIDGGgdVVAFVGTDNYEAGKLAGEYLAEALGGKGKVAILEgPPGSSTAIDRTKGFKEALKKYPDIEI---- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 197 gnVSDTTATSTADQAKAV----LTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADVsTADIQEIIEEGsPWVA 272
Cdd:cd01536  157 --VAEQPANWDRAKALTVtenlLQANPDIDAVFAANDDMALGAAEALKAAGRTGDIKIVGVDG-TPEALKAIKDG-ELDA 232

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 499969044 273 TVATNPAVVGAVSIRAAALEIAGQTVPHQITVKPTL 308
Cdd:cd01536  233 TVAQDPYLQGYLAVEAAVKLLNGEKVPKEILTPVTL 268
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
 41-297 5.09e-30

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: 115.10  E-value: 5.09e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044   41 VALISYISAGDFFQAYQAGAEAQAKALDIDLRI-FPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKG 119
Cdd:pfam13407   1 IGVVPKSTGNPFFQAAEEGAEEAAKELGGEVIVvGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  120 IKVVAFDV-NLNNPKIPQVEQSDHELASLALEQVVKDNGNSFNagYVYVAGFAP----LDRRNEVWDKFKSDNKGVVEKA 194
Cdd:pfam13407  81 IPVVTFDSdAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGK--VAILSGSPGdpnaNERIDGFKKVLKEKYPGIKVVA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  195 RFGNVSDTTATSTaDQAKAVLTANPD-ISVVFAPYDEFARGVKLAANDLGIASKLKIYSADVSTADIQEIIEEGSPwvAT 273
Cdd:pfam13407 159 EVEGTNWDPEKAQ-QQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGKVVVTGFDATPEALEAIKDGTID--AT 235

                         250       260
                  ....*....|....*....|....
gi 499969044  274 VATNPAVVGAVSIRAAALEIAGQT 297
Cdd:pfam13407 236 VLQDPYGQGYAAVELAAALLKGKK 259
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 52-310 5.73e-22

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: 93.50  E-value: 5.73e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  52 FFQAYQAGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNLNN 131
Cdd:cd06322   13 FFVDIKDAMKKEAAELGVKVVVADANGDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEAGIPVFTVDVKADG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 132 PKIPQVEQSDHELAS-LALEQVVKD-NGNSFNAGYV-YVAGFAPLDRRNEVWDKFKSDNKGVVEKARFGNVSDTTATSTA 208
Cdd:cd06322   93 AKVVTHVGTDNYAGGkLAGEYALKAlLGGGGKIAIIdYPEVESVVLRVNGFKEAIKKYPNIEIVAEQPGDGRREEALAAT 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 209 dqaKAVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADVSTADIQEIIEEGSpWVATVATNPAVVGAVSIRA 288
Cdd:cd06322  173 ---EDMLQANPDLDGIFAIGDPAALGALTAIESAGKEDKIKVIGFDGNPEAIKAIAKGGK-IKADIAQQPDKIGQETVEA 248

                        250       260
                 ....*....|....*....|..
gi 499969044 289 AALEIAGQTVPHQITVKPTLLT 310
Cdd:cd06322  249 IVKYLAGETVEKEILIPPKLYT 270
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 40-310 2.72e-20

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: 88.83  E-value: 2.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISAGDFFQAYQAGAEAQAKALDIDLRIFPGRQDAAEQREQILQA-INLGVSGIVIDHGLPESLGDVVQQALDK 118
Cdd:cd20007    1 TIALVPGVTGDPFYITMQCGAEAAAKELGVELDVQGPPTFDPTLQTPIVNAvIAKKPDALLIAPTDPQALIAPLKRAADA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 119 GIKVVAFDVNLNNPKIP-QVEQSDHELA-SLALEQVVKDNGNSfnaGYVYVAGFAP-----LDRRNEVWDKFKSDNKGVV 191
Cdd:cd20007   81 GIKVVTVDTTLGDPSFVlSQIASDNVAGgALAAEALAELIGGK---GKVLVINSTPgvsttDARVKGFAEEMKKYPGIKV 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 192 EKARFgnvSDTTATSTADQAKAVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADVSTADIQEiIEEGSpWV 271
Cdd:cd20007  158 LGVQY---SENDPAKAASIVAAALQANPDLAGIFGTNTFSAEGAAAALRNAGKTGKVKVVGFDASPAQVEQ-LKAGT-ID 232

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 499969044 272 ATVATNPAVVGAVSIRAAALEIAGQTVPHQITVKPTLLT 310
Cdd:cd20007  233 ALIAQKPAEIGYLAVEQAVAALTGKPVPKDILTPFVVIT 271
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 41-316 3.37e-20

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: 88.97  E-value: 3.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  41 VALISYISAGDFFQAYQAGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGI 120
Cdd:cd06317    2 IALVQINQQAQFFNQINQGAQAAAKDLGVDLVVFNANDDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 121 KVVAFDVNLNNPKIPQ---VEQSD--HELASLALEQVVKDNGNSFNAGYV-YVAGFAPLDRRNEVWDKFKSDNKGVVEKA 194
Cdd:cd06317   82 PVIAYDAVIPSDFQAAqvgVDNLEggKEIGKYAADYIKAELGGQAKIGVVgALSSLIQNQRQKGFEEALKANPGVEIVAT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 195 RFGNVSDTTATSTADQakaVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADVSTADIQEIIEEGspWV-AT 273
Cdd:cd06317  162 VDGQNVQEKALSAAEN---LLTANPDLDAIYATGEPALLGAVAAVRSQGRQGKIKVFGWDLTKQAIFLGIDEG--VLqAV 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 499969044 274 VATNPAVVGAVSIRAAALEIAGQTVPHQITVKPTLLTQESLRA 316
Cdd:cd06317  237 VQQDPEKMGYEAVKAAVKAIKGEDVEKTIDVPPTIVTKENVDQ 279
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 40-302 3.42e-19

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


Pssm-ID: 380660 [Multi-domain]  Cd Length: 274  Bit Score: 86.14  E-value: 3.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISAGDFFQAYQAGAEAQAKALDIDLrIFPG---RQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQAL 116
Cdd:cd20005    1 YIAVISKGFQHQFWKAVKKGAEQAAKELGVKI-TFEGpdtESDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 117 DKGIKVVAFDVNLNNPKIPQVEQSDHELA-SLALEQVVKDNGNSfnaGYVYV-----AGFAPLDRRNEVWDKFKSDNKGV 190
Cdd:cd20005   80 EKGIPVVTFDSGVPSDLPLATVATDNYAAgALAADHLAELIGGK---GKVAIvahdaTSETGIDRRDGFKDEIKEKYPDI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 191 veKARFGNVSDTTATSTADQAKAVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADvSTADIQEIIEEGSpW 270
Cdd:cd20005  157 --KVVNVQYGVGDHAKAADIAKAILQANPDLKGIYATNEGAAIGVANALKEMGKLGKIKVVGFD-SGEAQIDAIKNGV-I 232

                        250       260       270
                 ....*....|....*....|....*....|..
gi 499969044 271 VATVATNPAVVGAVSIRAAALEIAGQTVPHQI 302
Cdd:cd20005  233 AGSVTQNPYGMGYKTVKAAVKALKGEEVEKLI 264
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
 61-299 1.15e-18

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: 84.52  E-value: 1.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  61 EAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNLNNPKIPQ-VEQ 139
Cdd:cd06308   23 AEAAKYPNVELIVTDAQGDAAKQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAYDAGIPVIVLDRKVSGDDYTAfIGA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 140 SDHELASLALEQVVKDNGNSFNagYVYVAGF----APLDRRNEVWDKFKSDNKGVVEKARFGNVSDTTAtstADQAKAVL 215
Cdd:cd06308  103 DNVEIGRQAGEYIAELLNGKGN--VVEIQGLpgssPAIDRHKGFLEAIAKYPGIKIVASQDGDWLRDKA---IKVMEDLL 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 216 TANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADVSTADIQEIIEEGSpWVATVaTNPaVVGAVSIRAAALEIAG 295
Cdd:cd06308  178 QAHPDIDAVYAHNDEMALGAYQALKKAGREKEIKIIGVDGLPEAGEKAVKDGI-LAATF-LYP-TGGKEAIEAALKILNG 254


                 ....
gi 499969044 296 QTVP 299
Cdd:cd06308  255 EKVP 258
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 40-311 1.56e-18

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


Pssm-ID: 380661 [Multi-domain]  Cd Length: 274  Bit Score: 84.19  E-value: 1.56e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISA--GDFFQAYQAGAEAQAKALDIDLRIF--PGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQA 115
Cdd:cd20006    1 KIALILKSSDpnSDFWQTVKSGAEAAAKEYGVDLEFLgpESEEDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 116 LDKGIKVVAFDVNLNNPKIPQVEQSDHELASLALEQVVKDNGNSfnAGYVYVAGFAP-----LDRRNEVWDKFKSDNKGV 190
Cdd:cd20006   81 KKAGIPVITIDSPVNSKKADSFVATDNYEAGKKAGEKLASLLGE--KGKVAIVSFVKgsstaIEREEGFKQALAEYPNIK 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 191 VEKARFGNVSDTTAtstADQAKAVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADVSTADIQeIIEEGspw 270
Cdd:cd20006  159 IVETEYCDSDEEKA---YEITKELLSKYPDINGIVALNEQSTLGAARALKELGLGGKVKVVGFDSSVEEIQ-LLEEG--- 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 499969044 271 V--ATVATNPAVVGAVSIRAAALEIAGQTVPHQITVKPTLLTQ 311
Cdd:cd20006  232 IidALVVQNPFNMGYLSVQAAVDLLNGKKIPKRIDTGSVVITK 274
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 52-314 1.01e-17

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: 82.02  E-value: 1.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  52 FFQAYQAGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNLNN 131
Cdd:cd06319   13 FWQIMERGVQAAAEELGYEFVTYDQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAKIPVVIADIGTGG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 132 -----------------------PKIPQVEQSDHELASLALEQvVKDNGNSFNAGYVYVAGFApldrrnevwdkfksDNK 188
Cdd:cd06319   93 gdyvsyiisdnydggyqageylaEALKENGWGGGSVGIIAIPQ-SRVNGQARTAGFEDALEEA--------------GVE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 189 GVVEKArfgnVSDTTATSTADQAKAVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADVSTADIqEIIEEGS 268
Cdd:cd06319  158 EVALRQ----TPNSTVEETYSAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRTGDILVVGFDGDPEAL-DLIKDGK 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 499969044 269 pWVATVATNPAVVGAVSIRAAALEIAG-QTVPHQITVKPTLLTQESL 314
Cdd:cd06319  233 -LDGTVAQQPFGMGARAVELAIQALNGdNTVEKEIYLPVLLVTSENV 278
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
 52-310 9.78e-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 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: 78.87  E-value: 9.78e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  52 FFQAYQAGAEAQAKALDIDLRIF--PGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNL 129
Cdd:cd06321   13 FFVAMVRGAEEAAAEINPGAKVTvvDARYDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKDAGIIVVAVDVAA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 130 NNpkIPQVEQSDHELA-SLALEQVVKD----------NGNSFNAGYVYVAGFapldrrNEVWDKFkSDNKGVVEKArfgn 198
Cdd:cd06321   93 EG--ADATVTTDNVQAgYLACEYLVEQlggkgkvaiiDGPPVSAVIDRVNGC------KEALAEY-PGIKLVDDQN---- 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 199 vSDTTATSTADQAKAVLTANPDISVVFAPYDEFARGVKLAANDLGiASKLKIYSADVSTADIQEIIEEGSPWVATVATNP 278
Cdd:cd06321  160 -GKGSRAGGLSVMTRMLTAHPDVDGVFAINDPGAIGALLAAQQAG-RDDIVITSVDGSPEAVAALKREGSPFIATAAQDP 237

                        250       260       270
                 ....*....|....*....|....*....|...
gi 499969044 279 AVVGAVSIRAAALEIAGQTVPHQ-ITVKPTLLT 310
Cdd:cd06321  238 YDMARKAVELALKILNGQEPAPElVLIPSTLVT 270
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 51-308 1.18e-16

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: 78.78  E-value: 1.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  51 DFFQAYQAGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNLN 130
Cdd:cd19971   12 PFFIAINDGIKKAVEANGDELITRDPQLDQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAGIPVINVDTPVK 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 131 NPkipqveqsdhelaSLALEQVVKDNgnsFNAGYV-------------------YVAGFAPLDRRNEVWDKFKsDNKGVV 191
Cdd:cd19971   92 DT-------------DLVDSTIASDN---YNAGKLcgedmvkklpegakiavldHPTAESCVDRIDGFLDAIK-KNPKFE 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 192 EKARFGNVSDT-TATSTAdqaKAVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADVStADIQEIIEEGSpW 270
Cdd:cd19971  155 VVAQQDGKGQLeVAMPIM---EDILQAHPDLDAVFALNDPSALGALAALKAAGKLGDILVYGVDGS-PDAKAAIKDGK-M 229

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 499969044 271 VATVATNPAVVGAVSIRAAALEIAGQTVPHQITVKPTL 308
Cdd:cd19971  230 TATAAQSPIEIGKKAVETAYKILNGEKVEKEIVVPTFL 267
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 40-310 6.69e-15

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: 73.92  E-value: 6.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISAGDFFQAYQAGAEAQAKALDIDLrIFPGRQ---DAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQAL 116
Cdd:cd06310    1 KIGVVLKGTTSAFWRTVREGAEAAAKDLGVKI-IFVGPEseeDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 117 DKGIKVVAFDVNLNnPKIPQ--VEQSDHELASLALEQVVKDNGNSfnaGYVYVAGFAP-----LDRRNEVWDKFKSDNKG 189
Cdd:cd06310   80 DKGIPVIVIDSGIK-GDAYLsyIATDNYAAGRLAAQKLAEALGGK---GKVAVLSLTAgnsttDQREEGFKEYLKKHPGG 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 190 VVEKARfgNVSDTTATSTADQAKAVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADvSTADIQEIIEEGSp 269
Cdd:cd06310  156 IKVLAS--QYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGQIKIVGFD-SQEELLDALKNGK- 231

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 499969044 270 WVATVATNPAVVGAVSIRAAALEIAGQTVPHQITVKPTLLT 310
Cdd:cd06310  232 IDALVVQNPYEIGYEGIKLALKLLKGEEVPKNIDTGAELIT 272
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
 40-314 9.50e-15

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: 73.45  E-value: 9.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISAGDFFQAYQAGAEAQAKALDIDLRIF--PGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALD 117
Cdd:cd06320    1 KIGVVLKTLSNPFWVAMKDGIEAEAKKLGVKVDVQaaPSETDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 118 KGIKVVafdvNLNNPKIPQVEQ-----------SDH-ELASLALEQVVKDNGNSfnaGYVYV----AG-FAPLDRRNEVW 180
Cdd:cd06320   81 KGIPVI----NLDDAVDADALKkaggkvtsfigTDNvAAGALAAEYIAEKLPGG---GKVAIieglPGnAAAEARTKGFK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 181 DKFKSDNKGVVEKARFGNVSDTTAtstADQAKAVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADvSTADI 260
Cdd:cd06320  154 ETFKKAPGLKLVASQPADWDRTKA---LDAATAILQAHPDLKGIYAANDTMALGAVEAVKAAGKTGKVLVVGTD-GIPEA 229

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 499969044 261 QEIIEEGSpWVATVATNPAVVGAVSIRAAALEIAGQTVPHQITVKPTLLTQESL 314
Cdd:cd06320  230 KKSIKAGE-LTATVAQYPYLEGAMAVEAALRLLQGQKVPAVVATPQALITKDNV 282
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 40-308 9.88e-15

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: 73.44  E-value: 9.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISAGDFFQAYQAGAE-AQAKALDIDLRIFPGRQ--DAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQAL 116
Cdd:cd19970    1 KVALVMKSLANEFFIEMEKGARkHAKEANGYELLVKGIKQetDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 117 DKGIKVVAFDVNL-------NNPKIPQVEQSDHELASLALEQVVKDNGNSFNAGYVY-VAGFAPLDRRNEVWDKFKSDNK 188
Cdd:cd19970   81 DAGIAVINIDNRLdadalkeGGINVPFVGPDNRQGAYLAGDYLAKKLGKGGKVAIIEgIPGADNAQQRKAGFLKAFEEAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 189 GVVekarfgnVSDTTATSTADQAKAV----LTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADvSTADIQEII 264
Cdd:cd19970  161 MKI-------VASQSANWEIDEANTVaanlLTAHPDIRGILCANDNMALGAIKAVDAAGKAGKVLVVGFD-NIPAVRPLL 232

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 499969044 265 EEGSpWVATVATNPAVVGAVSIRAAALEIAGQTVPHQITVKPTL 308
Cdd:cd19970  233 KDGK-MLATIDQHPAKQAVYGIEYALKMLNGEEVPGWVKTPVEL 275
PBP1_ABC_sugar_binding-like cd06316
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 40-314 1.32e-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: 73.04  E-value: 1.32e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISAGDFFQAYQAGAEAQAKALDID-LRIFPGRQDAAEQREQILQAINLGVSGIV---IDhglPESLGDVVQQA 115
Cdd:cd06316    1 KVAIAMHTTGSDWSRLQVAGIKDTFEELGIEvVAVTDANFDPAKQITDLETLIALKPDIIIsipVD---PVATAAAYKKV 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 116 LDKGIKVVAFDVNLNNPKIPQ-----VEQSDHELASLALEQVVKDNGNSFNAGYVYVAG--FAPLDRRNEVWDKFKSDNK 188
Cdd:cd06316   78 ADAGIKLVFMDNVPDGLEAGKdyvsvVSSDNRGNGQIAAELLAEAIGGKGKVGIIYHDAdfYATNQRDKAFKDTLKEKYP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 189 G--VVEKARFGNVSDTtatstADQAKAVLTANPDISVVFAPYDEFARGVKLAANDLGiASKLKIYSADVSTaDIQEIIEE 266
Cdd:cd06316  158 DikIVAEQGFADPNDA-----EEVASAMLTANPDIDGIYVSWDTPALGVISALRAAG-RSDIKITTVDLGT-EIALDMAK 230

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 499969044 267 GSPWVATVATNPAVVGAVSIRAAALEIAGQTVPHQITVKPTLLTQESL 314
Cdd:cd06316  231 GGNVKGIGAQRPYDQGVAEALAAALALLGKEVPPFIGVPPLAVTKDNL 278
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
 52-312 2.18e-14

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: 72.44  E-value: 2.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  52 FFQAYQAGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFD--VNL 129
Cdd:cd06318   13 YYAALVAAAKAEAKKLGVELVVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAAGIPVITVDsaLDP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 130 NNPKIPQVEQSDHELASLALEQVVKDNGN--------SFNAGyvyvaGFAPLDRR--------NEVWDKFKSDNKGVVEK 193
Cdd:cd06318   93 SANVATQVGRDNKQNGVLVGKEAAKALGGdpgkiielSGDKG-----NEVSRDRRdgflagvnEYQLRKYGKSNIKVVAQ 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 194 ARFGNVSDTTATSTADqakaVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADVSTADIQeIIEEGSpWVAT 273
Cdd:cd06318  168 PYGNWIRSGAVAAMED----LLQAHPDINVVYAENDDMALGAMKALKAAGMLDKVKVAGADGQKEALK-LIKDGK-YVAT 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 499969044 274 VATNPAVVGAVSIRAAALEIAGQ-TVPHQITVKPTLLTQE 312
Cdd:cd06318  242 GLNDPDLLGKTAVDTAAKVVKGEeSFPEFTYTPTALITKD 281
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
 40-267 3.45e-14

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


Pssm-ID: 380620 [Multi-domain]  Cd Length: 272  Bit Score: 71.53  E-value: 3.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISAGDFFQAYQAGAEAQAKALDIDLR-IFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDK 118
Cdd:cd19965    1 KFVFVTHVTTNPFFQPVKKGMDDACELLGAECQfTGPQTFDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 119 GIKVVAFDVNL---NNPKIPQVEQ----SDHELASLALEQVVKDNGNSfnAGYVYVAGFAPLDRRNE-VWDKFKSDNKGV 190
Cdd:cd19965   81 GIPVVAFNVDApggENARLAFVGQdlypAGYVLGKRIAEKFKPGGGHV--LLGISTPGQSALEQRLDgIKQALKEYGRGI 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499969044 191 VEKarfgnVSDTTATS--TADQAKAVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADVsTADIQEIIEEG 267
Cdd:cd19965  159 TYD-----VIDTGTDLaeALSRIEAYYTAHPDIKAIFATGAFDTAGAGQAIKDLGLKGKVLVGGFDL-VPEVLQGIKAG 231
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
 51-310 4.22e-14

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: 71.46  E-value: 4.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  51 DFFQAYQAGAEAQAKALDIDLR-IFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNL 129
Cdd:cd06314   12 PFWDLAEAGAEKAAKELGVNVEfVGPQKSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADKGIPVITFDSDA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 130 NNPK-IPQVEQSDHELASLALEQVVKDNGNsfNAGYVYVAGFAP----LDRRNEVWDKFKSDNKGVVEKARFGNVSDTTA 204
Cdd:cd06314   92 PDSKrLAYIGTDNYEAGREAGELMKKALPG--GGKVAIITGGLGadnlNERIQGFKDALKGSPGIEIVDPLSDNDDIAKA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 205 TStadQAKAVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADvSTADIQEIIEEGSPwVATVATNPAVVGAV 284
Cdd:cd06314  170 VQ---NVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKVGKVKIVGFD-TLPETLQGIKDGVI-AATVGQRPYEMGYL 244

                        250       260
                 ....*....|....*....|....*..
gi 499969044 285 SIRA-AALEIAGQTVPHQITVKPTLLT 310
Cdd:cd06314  245 SVKLlYKLLKGGKPVPDVIDTGVDVVT 271
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
 52-304 4.45e-13

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: 68.48  E-value: 4.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  52 FFQAYQAGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNLNN 131
Cdd:cd06323   13 FFVSLKDGAQAEAKELGVELVVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAGIPVITVDRSVTG 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 132 PKIPQVEQSDH----ELASLALEQVVKDNGNSfnAGYVYVAGFAPLDRRNEVWDKFKSDNKGVVEKAR-FGNVSDTTATS 206
Cdd:cd06323   93 GKVVSHIASDNvaggEMAAEYIAKKLGGKGKV--VELQGIPGTSAARERGKGFHNAIAKYPKINVVASqTADFDRTKGLN 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 207 TADQakaVLTANPDISVVFAPYDEFARGvklAANDLGIASKLKIYSADV-STADIQEIIEEGSpWVATVATNPAVVGAVS 285
Cdd:cd06323  171 VMEN---LLQAHPDIDAVFAHNDEMALG---AIQALKAAGRKDVIVVGFdGTPDAVKAVKDGK-LAATVAQQPEEMGAKA 243

                        250
                 ....*....|....*....
gi 499969044 286 IRAAALEIAGQTVPHQITV 304
Cdd:cd06323  244 VETADKYLKGEKVPKKIPV 262
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
 52-309 2.26e-12

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: 66.45  E-value: 2.26e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  52 FFQAYQAGAEAQAKALDIDLRIFP--GRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNL 129
Cdd:cd06306   13 YWVGVNYGIVDEAKRLGVKLTVYEagGYTNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGIPVIDLVNGI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 130 NNPKI-PQVEQSDHELASLALEQVVKDNGNsfNAGYVYV------AGFAPlDRRNEVWDKFKSDNKGVVEKARfgnvsdt 202
Cdd:cd06306   93 DSPKVaARVLVDFYDMGYLAGEYLVEHHPG--KPVKVAWfpgpagAGWAE-DREKGFKEALAGSNVEIVATKY------- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 203 TATSTADQAKAV---LTANPDISVVfAPYDEFARGVKLAANDLGIASKLKIYSADVsTADIQEIIEEGSPwVATVATNPA 279
Cdd:cd06306  163 GDTGKAVQLNLVedaLQAHPDIDYI-VGNAVAAEAAVGALREAGLTGKVKVVSTYL-TPGVYRGIKRGKI-LAAPSDQPV 239

                        250       260       270
                 ....*....|....*....|....*....|
gi 499969044 280 VVGAVSIRAAALEIAGQTVPHQITVKPTLL 309
Cdd:cd06306  240 LQGRIAVDQAVRALEGKPVPKHVGPPILVV 269
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 40-300 5.59e-12

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: 65.33  E-value: 5.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISAGDFFQAYQAGAEAQAKALDIDLRIF--PGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQAlD 117
Cdd:cd20008    1 KIAVIVKDTDSEYWQTVLKGAEKAAKELGVEVTFLgpATEADIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAA-D 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 118 KGIKVVAFDVNLNNPKIPQVEQSDH----ELASLALEQVVKDNGNsfNAGYVYVAGFAP-----LDRRNEVWDKFKSDNK 188
Cdd:cd20008   80 AGIPVVLVDSGANTDDYDAFLATDNvaagALAADELAELLKASGG--GKGKVAIISFQAgsqtlVDREEGFRDYIKEKYP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 189 GVVEKARFGNVSDTTAtsTADQAKAVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADvSTADIQEIIEEGS 268
Cdd:cd20008  158 DIEIVDVQYSDGDIAK--ALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAGKAGKIVLVGFD-SSPDEVALLKSGV 234

                        250       260       270
                 ....*....|....*....|....*....|..
gi 499969044 269 pWVATVATNPAVVGAVSIRAAALEIAGQTVPH 300
Cdd:cd20008  235 -IKALVVQDPYQMGYEGVKTAVKALKGEEIVE 265
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 40-263 2.77e-11

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


Pssm-ID: 380535 [Multi-domain]  Cd Length: 272  Bit Score: 63.02  E-value: 2.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISAGD-FFQAYQAGAEAQAKALDIDLRI-FPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALD 117
Cdd:cd06312    1 TIYVISHGSPSDpFWSVVKKGAKDAAKDLGVTVQYlGPQNNDIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 118 KGIKVVAFDV-----NLNNPKIPQVEQSDHELASLALEQVVKD---NGNSFNAgyvyVAGFAPLDRR-NEVWDKFKSDNK 188
Cdd:cd06312   81 AGIPVIAINSgddrsKERLGALTYVGQDEYLAGQAAGERALEAgpkNALCVNH----EPGNPGLEARcKGFADAFKGAGI 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499969044 189 GVVEkarfgnVSDTTATSTADQA-KAVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADVSTADIQEI 263
Cdd:cd06312  157 LVEL------LDVGGDPTEAQEAiKAYLQADPDTDAVLTLGPVGADPALKAVKEAGLKGKVKIGTFDLSPETLEAI 226
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
 40-312 4.35e-11

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: 62.67  E-value: 4.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISAGDFFQAYQAGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKG 119
Cdd:cd06313    1 KIGFTVYGLSSEFITNLVEAMKAVAKELNVDLVVLDGNGDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 120 IKVVAFDVNLNNPKI-PQVEQSDHELASLALEQVVKDNGNSFNagYVYVAG----FAPLDRR---NEVWDKfKSDNKGVV 191
Cdd:cd06313   81 IPLVGVNALIENEDLtAYVGSDDVVAGELEGQAVADRLGGKGN--VVILEGpigqSAQIDRGkgiENVLKK-YPDIKVLA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 192 EKArfGNVSDTTATSTadqAKAVLTANPD-ISVVFAPYDEFARGVKLAANDLGIaSKLKIYSADVSTADIQEIIEEGspW 270
Cdd:cd06313  158 EQT--ANWSRDEAMSL---MENWLQAYGDeIDGIIAQNDDMALGALQAVKAAGR-DDIPVVGIDGIEDALQAVKSGE--L 229

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 499969044 271 VATVATNPAVVGAVSIRAAALEIAGQTVPHQITVKPTLLTQE 312
Cdd:cd06313  230 IATVLQDAEAQGKGAVEVAVDAVKGEGVEKKYYIPFVLVTKD 271
PBP1_ABC_sugar_binding-like cd19998
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 40-336 6.55e-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: 380653 [Multi-domain]  Cd Length: 302  Bit Score: 62.31  E-value: 6.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISAGDFFQAYQAGAEAQAKALDI----DLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQA 115
Cdd:cd19998    1 KIALSNSYSGNDWRQEMINIAKAAAKQPPYadkvELKVVSSGTDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 116 LDKGIKVVAFDVNLNNPKIPQVEQSDHELASLALEQVVKDNGNS----FNAGyvyVAGFAPLDRRNEVWDK-FKSDNKGV 190
Cdd:cd19998   81 CDAGIVVVAFDNVVDEPCAYNVNTDQAKAGEQTAQWLVDKLGGKgnilMVRG---VPGTSVDRDRYEGAKEvFKKYPDIK 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 191 VEKARFGNVSDTTA-TSTADqakaVLTANPDISVVFAPYDEFarGVKLAANDLGI--------ASKL-KIYSADVSTADI 260
Cdd:cd19998  158 VVAEYYGNWDDGTAqKAVAD----ALAAHPDVDGVWTQGGET--GVIKALQAAGHplvpvggeAENGfRKAMLEPLANGL 231

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499969044 261 QEIIEEGSPWvatvatnpavVGAVSIRAAALEIAGQTVPHQITVKPTLLTQESLRAAGVKTIEELAEKIPAFSTSD 336
Cdd:cd19998  232 PGISAGSPPA----------LSAVALKLAVAVLEGEKEPKTIELPLPWVTTDDVKLCQGGFPDLPKNGFTVNDFPS 297
PBP1_ABC_sugar_binding-like cd19997
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 58-316 1.97e-10

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: 61.15  E-value: 1.97e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  58 AGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNLNNPKIPQV 137
Cdd:cd19997   24 AAKKAKADGLIADYIVVNADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQACDAGIKVVVFDSGVTEPCAYIL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 138 EQSDHELASLALEQVVKDNGNSFNAGYVY-VAGFAP----LDRRNEVWDKFkSDNKGVVEKarFGNVSDTTATStadQAK 212
Cdd:cd19997  104 NNDFEDYGAASVEYVADRLGGKGNVLEVRgVAGTSPdeeiYAGQVEALKKY-PDLKVVAEV--YGNWTQSVAQK---AVT 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 213 AVLTANPDISVVFAPydefargvklAANDLGIASKLKIYSADV----------STADIQEIIEEGSPWVATVATNPAvVG 282
Cdd:cd19997  178 GILPSLPEVDAVITQ----------GGDGYGAAQAFEAAGRPLpiiiggnrgeFLKWWQEEYAKNGYETVSVSTDPG-QG 246

                        250       260       270
                 ....*....|....*....|....*....|....
gi 499969044 283 AVSIRAAALEIAGQTVPHQITVKPTLLTQESLRA 316
Cdd:cd19997  247 SAAFWVALDILNGKDVPKEMILPVVTITEDDLDA 280
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
 43-282 7.69e-10

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: 58.89  E-value: 7.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  43 LISYISAGDFFQAYQAGAEAQAKALDIDLRI-FPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIK 121
Cdd:cd19969    4 MVTFKSGHPYWDDVKEGFEDAGAELGVKTEYtGPATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGIP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 122 VVAFDVNLNNPK-IPQVEQSDHELASLALEQVVKDNGNSFNAGYVYVAGFAPLDRRNEVWDKFKSDNKG--VVEKARfGN 198
Cdd:cd19969   84 VVTFDSDAPESKrISYVGTDNYEAGYAAAEKLAELLGGKGKVAVLTGPGQPNHEERVEGFKEAFAEYPGieVVAVGD-DN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 199 VSDTTAtstADQAKAVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADVSTADIQeIIEEGSPwVATVATNP 278
Cdd:cd19969  163 DDPEKA---AQNTSALLQAHPDLVGIFGVDASGGVGAAQAVREAGKTGKVKIVAFDDDPETLD-LIKDGVI-DASIAQRP 237


                 ....
gi 499969044 279 AVVG 282
Cdd:cd19969  238 WMMG 241
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
 44-310 8.16e-10

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: 58.78  E-value: 8.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  44 ISYISAG---DFFQAYQAGAEAQAKALDIDLrIFPGRQ---DAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALD 117
Cdd:cd20004    2 IAVIPKGtthDFWKSVKAGAEKAAQELGVEI-YWRGPSredDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 118 KGIKVVAFDVNLNNPKIPQVEQSDHE----LASLALEQVVKDNGNSfnAGYVYVAGFAPLDRRNEVW-DKFKSDNKGV-V 191
Cdd:cd20004   81 QGIPVVIIDSDLGGDAVISFVATDNYaagrLAAKRMAKLLNGKGKV--ALLRLAKGSASTTDRERGFlEALKKLAPGLkV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 192 EKARFGNVSDTTATSTadqAKAVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADvSTADIQEIIEEGSpWV 271
Cdd:cd20004  159 VDDQYAGGTVGEARSS---AENLLNQYPDVDGIFTPNESTTIGALRALRRLGLAGKVKFIGFD-ASDLLLDALRAGE-IS 233

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 499969044 272 ATVATNPAVVGAVSIRAAALEIAGQTVPHQITVKPTLLT 310
Cdd:cd20004  234 ALVVQDPYRMGYLGVKTAVAALRGKPVPKRIDTGVVLVT 272
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
 60-308 1.10e-09

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: 58.53  E-value: 1.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  60 AEAQAKAL-DIDLRIFPGrQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNLNNPK-IPQV 137
Cdd:cd06311   21 AEKQAKELaDLEYKLVTS-SNANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAGIPVVNFDRGLNVLIyDLYV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 138 EQSDHELASLALEQVVKDNGNSFNAGYVYVAGFAPLDrrNEVWDKFKsdnKGVVEKARFGNVSDTTATSTADQAKAV--- 214
Cdd:cd06311  100 AGDNPGMGVVSAEYIGKKLGGKGNVVVLEVPSSGSVN--EERVAGFK---EVIKGNPGIKILAMQAGDWTREDGLKVaqd 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 215 -LTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADVSTADIQEIIEEGSPWVATVATNPAVVGAVSIRAAALEI 293
Cdd:cd06311  175 iLTKNKKIDAVWAADDDMAIGVLQAIKEAGRTDIKVMTGGGGSQEYFKRIMDGDPIWPASATYSPAMIADAIKLAVLILK 254

                        250
                 ....*....|....*
gi 499969044 294 AGQTVPHQITVKPTL 308
Cdd:cd06311  255 GGKTVEKEVIIPSTL 269
PBP1_LsrB_Quorum_Sensing-like cd06302
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ...
 40-227 1.54e-09

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: 58.02  E-value: 1.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISAGDFFQAYQAGAEAQAKALDIDLrIF--PGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALD 117
Cdd:cd06302    1 KIAFVPKVVGIPYFDAAEEGAKKAAKELGVEV-VYtgPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 118 KGIKVVAFDVNLNNPK----IPQVeqSDHELASLALEQVVKDNGNSfnAGYVYVAGFAPLDRRNEVWDKFKSDNKGVVEK 193
Cdd:cd06302   80 AGIKVITWDSDAPPSArdyfVNQA--DDEGLGEALVDSLAKEIGGK--GKVAILSGSLTATNLNAWIKAMKEYLKSKYPD 155

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 499969044 194 ARFGNV--SDTTATSTADQAKAVLTANPDISVVFAP 227
Cdd:cd06302  156 IELVDTyyTDDDQQKAYTQAQNLIQAYPDLKGIIGV 191
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
 52-296 2.54e-09

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: 57.33  E-value: 2.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  52 FFQAYQAGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFD--VNL 129
Cdd:cd19967   13 FFVVEAEGAKEKAKELGYEVTVFDHQNDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAGIPVFLIDreINA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 130 NNPKIPQVEQSDHELASLALEQVVKDNGNSFNagYVYVAGfapLDRRNEVWDKFKSDNKGVVEKARFGNVSDTTATSTAD 209
Cdd:cd19967   93 EGVAVAQIVSDNYQGAVLLAQYFVKLMGEKGL--YVELLG---KESDTNAQLRSQGFHSVIDQYPELKMVAQQSADWDRT 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 210 QAK----AVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADvSTADIQEIIEEGSpWVATVATNPAVvgavs 285
Cdd:cd19967  168 EAFekmeSILQANPDIKGVICGNDEMALGAIAALKAAGRAGDVIIVGFD-GSNDVRDAIKEGK-ISATVLQPAKL----- 240

                        250
                 ....*....|.
gi 499969044 286 IRAAALEIAGQ 296
Cdd:cd19967  241 IARLAVEQADQ 251
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 51-310 4.53e-09

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: 56.68  E-value: 4.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  51 DFFQAYQAGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNLN 130
Cdd:cd19972   12 DFFNQIKQSVEAEAKKKGYKVITVDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAGIPVIAVDRNPE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 131 NPKIPQVEQSDHELASLAL-EQVVKDNGNSFNAGYVY-VAGFAPLDRRNEVWDKFKSDNKGVVEKARfgNVSDTTATSTA 208
Cdd:cd19972   92 DAPGDTFIATDSVAAAKELgEWVIKQTGGKGEIAILHgQLGTTPEVDRTKGFQEALAEAPGIKVVAE--QTADWDQDEGF 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 209 DQAKAVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADVSTADIQEiIEEGSpWVATVATNPAVVGAVSIRA 288
Cdd:cd19972  170 KVAQDMLQANPNITVFFGQSDAMALGAAQAVKVAGLDHKIWVVGFDGDVAGLKA-VKDGV-LDATMTQQTQKMGRLAVDS 247

                        250       260
                 ....*....|....*....|..
gi 499969044 289 AALEIAGQTVPHQITVKPTLLT 310
Cdd:cd19972  248 AIDLLNGKAVPKEQLQDAVLTT 269
PBP1_ABC_sugar_binding-like cd19973
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
 41-290 1.30e-08

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: 55.17  E-value: 1.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  41 VALISYISAGDFFQAYQAGAEAQAKALDIDLRIFPGRQ--DAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDK 118
Cdd:cd19973    2 IGLITKTDTNPFFVKMKEGAQKAAKALGIKLMTAAGKIdgDNATQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARDA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 119 GIKVVAfdvnLNNPKIPQvEQSDHELASlaleqvvkDNgnsFNAGYVY----VAGFAPLDRRNEVWDKFKSDNKGV---- 190
Cdd:cd19973   82 GVLVIA----LDTPTDPI-DAADATFAT--------DN---FKAGVLIgewaKAALGAKDAKIATLDLTPGHTVGVlrhq 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 191 ----------VEKARFGNVSDT----TATSTADQAKA------VLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKI 250
Cdd:cd19973  146 gflkgfgideKDPESNEDEDDSqvvgSADTNGDQAKGqtamenLLQKDPDINLVYTINEPAAAGAYQALKAAGKEKGVLI 225

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 499969044 251 YSADVSTADIQEiIEEGSpWVATVATNPAVVGAVSIRAAA 290
Cdd:cd19973  226 VSVDGGCPGVKD-VKDGI-IGATSQQYPLRMAALGVEAIA 263
PBP1_ABC_xylose_binding-like cd01538
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ...
 61-265 1.79e-08

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: 54.74  E-value: 1.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  61 EAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNLNNPKIPQVEQS 140
Cdd:cd01538   22 VEQLEEKGAKVLVQSADGDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEGIKVIAYDRLILNADVDYYISF 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 141 DHELASLALEQVVKDNGNSFNagYVYVAGfAPLDRRNevwDKFKSDNKGVVE---KARFGNVSDTTATSTADQAKA---- 213
Cdd:cd01538  102 DNEKVGELQAQALLDAKPEGN--YVLIGG-SPTDNNA---KLFRDGQMKVLQpaiDSGKIKVVGDQWVDDWLPANAqqim 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 499969044 214 --VLTAN-PDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADVSTADIQEIIE 265
Cdd:cd01538  176 enALTANgNNVDAVVASNDGTAGGAIAALKAQGLSGGVPVSGQDADLAAIKRILA 230
PBP1_ABC_xylose_binding-like cd19992
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
 61-298 6.72e-08

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: 52.97  E-value: 6.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  61 EAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNLNNPKI------ 134
Cdd:cd19992   22 EEEAKELGVELIFQVADNDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAGVPVISYDRLILNADVdlyvgr 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 135 --PQVEQSdheLASLALEQVVKDNgnsfnagYVYVAGfaplDRRNEVWDKFKSDNKGVVEKAR-FGN---VSDTTATS-T 207
Cdd:cd19992  102 dnYKVGQL---QAEYALEAVPKGN-------YVILSG----DPGDNNAQLITAGAMDVLQPAIdSGDikiVLDQYVKGwS 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 208 ADQAKA----VLTA-NPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADVSTADIQEIIeEGSPwVATVATNPAVVG 282
Cdd:cd19992  168 PDEAMKlvenALTAnNNNIDAVLAPNDGMAGGAIQALKAQGLAGKVFVTGQDAELAALKRIV-EGTQ-TMTVWKDLKELA 245

                        250
                 ....*....|....*.
gi 499969044 283 AVSIRAAALEIAGQTV 298
Cdd:cd19992  246 RAAADAAVKLAKGEKP 261
PBP1_ABC_sugar_binding-like cd19999
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 57-298 1.07e-07

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: 52.70  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  57 QAGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNLNNPKIPQ 136
Cdd:cd19999   23 EVAAEYKEEGVISDLIVQNADADATGQISQIRNMINEGVDAILIDPVSATALNPVIEKAQAAGILVVSFDQPVSSPDAIN 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 137 VEQSDHELASLALEQVVKDNGNSFNAGYVY-VAGFAPLDRRNEVWDKFKSDNKG--VVEKArFGNVSDTTATSTADQaka 213
Cdd:cd19999  103 VVIDQYKWAAIQAQWLAEQLGGKGNIVAINgVAGNPANEARVKAADDVFAKYPGikVLASV-PGGWDQATAQQVMAT--- 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 214 VLTANPDISVVFAPyDEFARGVKLAANDLGiaSKLKIYSADVSTADIQEIIE-EGSPWVATVATNPAVVGAVSIRAAALE 292
Cdd:cd19999  179 LLATYPDIDGVLTQ-DGMAEGVLRAFQAAG--KDPPVMTGDYRKGFLRKWKElDLPDFESIGVVNPPGIGATALRIAVRL 255


                 ....*.
gi 499969044 293 IAGQTV 298
Cdd:cd19999  256 LQGKEL 261
PRK09701 PRK09701
D-allose transporter substrate-binding protein;
52-287 1.17e-07

D-allose transporter substrate-binding protein;


Pssm-ID: 182037 [Multi-domain]  Cd Length: 311  Bit Score: 52.57  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  52 FFQAYQAGAEAQAKALDIDLRIF--PGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFD--V 127
Cdd:PRK09701  38 FWVDMKKGIEDEAKTLGVSVDIFasPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDekI 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 128 NLNNPKipqvEQSDHELASLALEQV-VKDNGNSF-------NAGYVYV----AGFAP-LDRRNEVWDKFKSDNKgvvEKA 194
Cdd:PRK09701 118 DMDNLK----KAGGNVEAFVTTDNVaVGAKGASFiidklgaEGGEVAIiegkAGNASgEARRNGATEAFKKASQ---IKL 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 195 RFGNVSDTTATSTADQAKAVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADvSTADIQEIIEEGSpWVATV 274
Cdd:PRK09701 191 VASQPADWDRIKALDVATNVLQRNPNIKAIYCANDTMAMGVAQAVANAGKTGKVLVVGTD-GIPEARKMVEAGQ-MTATV 268

                        250
                 ....*....|...
gi 499969044 275 ATNPAVVGAVSIR 287
Cdd:PRK09701 269 AQNPADIGATGLK 281
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
 51-304 1.33e-07

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: 52.23  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  51 DFFQAYQAGA--EAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVN 128
Cdd:cd06301   12 DEFLTYLRDAieAYAKEYPGVKLVIVDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADAGIPLVYVNRE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 129 LNNPKIPQ--VEQSDHELASLALEQVVKDNGNSFNAGYVY-VAGFAPLDRRNEvwdkfksDNKGVVEKARFGNVSDT-TA 204
Cdd:cd06301   92 PDSKPKGVafVGSDDIESGELQMEYLAKLLGGKGNIAILDgVLGHEAQILRTE-------GNKDVLAKYPGMKIVAEqTA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 205 TSTADQAKAV----LTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADvSTADIQEIIEEGSpWVATVATNPAV 280
Cdd:cd06301  165 NWSREKAMDIvenwLQSGDKIDAIVANNDEMAIGAILALEAAGKKDDILVAGID-ATPDALKAMKAGR-LDATVFQDAAG 242

                        250       260
                 ....*....|....*....|....
gi 499969044 281 VGAVSIRAAALEIAGQTVPHQITV 304
Cdd:cd06301  243 QGETAVDVAVKAAKGEEVESDIWI 266
PBP1_LsrB_Quorum_Sensing cd20003
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ...
 40-250 1.42e-07

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: 52.28  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISAGDFFQAYQAGAEAQAKALDIDLrIF--PGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALD 117
Cdd:cd20003    1 TIAMIPKLVGVPYFTAAGQGAQEAAKELGVDV-TYdgPTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 118 KGIKVVAFDVNLnNPKIPQ--VEQSDHE-LASLALEQVVKDNGNSFNAGYVYVAGFAPLDRR--NEVWDKFKSDNKGV-V 191
Cdd:cd20003   80 KGIKVVTWDSDV-NPDARDffVNQATPEgIGKTLVDMVAEQTGEKGKVAIVTSSPTATNQNAwiKAMKAYIAEKYPDMkI 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 499969044 192 EKARFGNVSDTTATStadQAKAVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKI 250
Cdd:cd20003  159 VTTQYGQEDPAKSLQ---VAENILKAYPDLKAIIAPDSVALPGAAEAVEQLGRTGKVAV 214
PBP1_ABC_sugar_binding-like cd06300
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ...
 53-221 1.92e-07

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: 51.94  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  53 FQAYQAGAEAQAKALDIDLRIFPGrqDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNLNNP 132
Cdd:cd06300   21 LKADAAQSGQKGLVKELIVANSNG--DATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFDGAVTSP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 133 KIPQVEQSDHELASLALEQVVKDNGNSFNAGYVY-VAGFAPLDRRNEVWDKFKSDNKGV-VEKARFGNVSDTTAtstADQ 210
Cdd:cd06300   99 DAYNVSNDQVEWGRLGAKWLFEALGGKGNVLVVRgIAGAPASADRHAGVKEALAEYPGIkVVGEVFGGWDEATA---QTA 175

                        170
                 ....*....|.
gi 499969044 211 AKAVLTANPDI 221
Cdd:cd06300  176 MLDFLATHPQV 186
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
 52-310 2.99e-07

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


Pssm-ID: 380623 [Multi-domain]  Cd Length: 271  Bit Score: 51.23  E-value: 2.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  52 FFQAYQAGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNLN- 130
Cdd:cd19968   13 FFVYMHEQAVDEAAKLGVKLVVLDAQNSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKAGIPVVTVDRRAEg 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 131 NPKIPQVEQSDHELASLALEQVVKDNGnsfNAGYVYVAGFAP-----LDRRNEVWDKFKSDNKgvvekarFGNVSDTTAT 205
Cdd:cd19968   93 AAPVPHVGADNVAGGREVAKFVVDKLP---NGAKVIELTGTPgsspaIDRTKGFHEELAAGPK-------IKVVFEQTGN 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 206 STADQAKAV----LTANP-DISVVFAPYDEFARGVKLAANDLGI-ASKLKIYSADvSTADIQEIIEEGSpWVATVATNPA 279
Cdd:cd19968  163 FERDEGLTVmeniLTSLPgPPDAIICANDDMALGAIEAMRAAGLdLKKVKVIGFD-AVPDALQAIKDGE-LYATVEQPPG 240

                        250       260       270
                 ....*....|....*....|....*....|.
gi 499969044 280 VVGAVSIRAAALEIAGQTVPHQITVKPTLLT 310
Cdd:cd19968  241 GQARTALRILVDYLKDKKAPKKVNLKPKLIT 271
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
 46-126 4.92e-07

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: 50.71  E-value: 4.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  46 YISAGDFFQAY--QAGAEAqakaldiDLRIFPGrqDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVV 123
Cdd:cd19994   14 WIKDGENLKSEleEAGYTV-------DLQYADD--DVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAGIPVI 84


                 ...
gi 499969044 124 AFD 126
Cdd:cd19994   85 AYD 87
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
 48-312 2.18e-06

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


Pssm-ID: 380532 [Multi-domain]  Cd Length: 285  Bit Score: 48.37  E-value: 2.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  48 SAGDFFQAYQAGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDV 127
Cdd:cd06309    9 SESPWRVANTKSIKEAAKKRGYELVYTDANQDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAGIPVILVDR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 128 NLNnpkipqVEQSDHELASLAL------EQVVKDNGNSFNAGYVYVA------GFAP-LDRRNEVWDKFKSDNKGVVEKA 194
Cdd:cd06309   89 TID------GEDGSLYVTFIGSdfveegRRAAEWLVKNYKGGKGNVVelqgtaGSSVaIDRSKGFREVIKKHPNIKIVAS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 195 RFGNVSDTTATstaDQAKAVLTANP-DISVVFAPYDEFARGVKLAANDLGI--ASKLKIYSADVSTADIQEIIeEGSpWV 271
Cdd:cd06309  163 QSGNFTREKGQ---KVMENLLQAGPgDIDVIYAHNDDMALGAIQALKEAGLkpGKDVLVVGIDGQKDALEAIK-AGE-LN 237

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 499969044 272 ATVATNPAvVGAVSIRAAALEIAGQTVPHQITVKPTLLTQE 312
Cdd:cd06309  238 ATVECNPL-FGPTAFDTIAKLLAGEKVPKLIIVEERLFDKD 277
XylF COG4213
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ...
 46-243 3.47e-06

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


Pssm-ID: 443359 [Multi-domain]  Cd Length: 310  Bit Score: 48.21  E-value: 3.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  46 YISAGDFFqayqagaEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAF 125
Cdd:COG4213   17 WIRDGDNF-------KAALKELGYEVDVQNANGDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAKAAGIPVIAY 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 126 DVNLNNPKIP--------QVEQSdheLASLALEQV-VKDNGNsfnagYVYVAGfAPLDR-----RNEVWD----KFKSdn 187
Cdd:COG4213   90 DRLILNSDVDyyvsfdnvKVGEL---QGQYLVDGLpLKGKGN-----IELFGG-SPTDNnatlfFEGAMSvlqpYIDS-- 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499969044 188 kGVVEKarfgnVSD--------TTATSTADQAkavLTANP-DISVVFAPYDEFARGV--KLAANDLG 243
Cdd:COG4213  159 -GKLVV-----VSGqwtlgwdpETAQKRMENL---LTANGnKVDAVLAPNDGLAGGIiqALKAQGLA 216
PBP1_ABC_xylose_binding-like cd19995
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
 61-303 5.60e-06

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: 47.28  E-value: 5.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  61 EAQAKAL--DIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNLNNPKI---- 134
Cdd:cd19995   23 EKAMKKLcpDCKVIYQNANGDASTQQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYDRLILGGPAdyyv 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 135 ----PQVEQSDHELASLALEQVVKDNGN--------SFNAGYVYVAGFapldrrNEVWDK-FKSDNKGVVEKARFGNVSD 201
Cdd:cd19995  103 sfdnVAVGEAQAQSLVDHLKAIGKKGVNivmingspTDNNAGLFKKGA------HEVLDPlGDSGELKLVCEYDTPDWDP 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 202 TTATSTADQAkavLTANPD-ISVVFAPYDEFARGVKLAANDLGIASKLKIYSADVSTADIQEIIeEGSPWVaTVATNPAV 280
Cdd:cd19995  177 ANAQTAMEQA---LTKLGNnIDGVLSANDGLAGGAIAALKAQGLAGKVPVTGQDATVAGLQRIL-AGDQYM-TVYKPIKK 251

                        250       260
                 ....*....|....*....|...
gi 499969044 281 VGAVSIRAAALEIAGQTVPHQIT 303
Cdd:cd19995  252 EAAAAAKVAVALLKGETPPSDLV 274
PBP1_ABC_sugar_binding-like cd19996
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
 60-312 7.36e-06

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


Pssm-ID: 380651 [Multi-domain]  Cd Length: 302  Bit Score: 46.85  E-value: 7.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  60 AEAQAKALDI---DLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNLNNPKIP- 135
Cdd:cd19996   21 FEAEAAKLKKlikELIYTDAQGDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAAAAGIPVVLFDSGVGSDKYTa 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 136 QVEQSDHELASLALEQVVKDNGNSfnaGYVYV----AGFAP-LDRRN---EVWDKfksdNKGVVEkarfgnVSDTTATST 207
Cdd:cd19996  101 FVGVDDAAFGRVGAEWLVKQLGGK---GNIIAlrgiAGVSVsEDRWAgakEVFKE----YPGIKI------VGEVYADWD 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 208 ADQAKAV----LTANPDISVVFAPYDEFARGVKLAANDLGiaskLKIYSadVSTADIQEIIE-----EGSPWVATvaTNP 278
Cdd:cd19996  168 YAKAKQAveslLAAYPDIDGVWSDGGAMTLGAIEAFEEAG----RPLVP--MTGEDNNGFLKawkelPGFKSIAP--SYP 239

                        250       260       270
                 ....*....|....*....|....*....|....
gi 499969044 279 AVVGAVSIRAAALEIAGQTVPHQITVKPTLLTQE 312
Cdd:cd19996  240 PWLGATALDAALAALEGEPVPKYVYIPLPVITDE 273
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
 40-129 1.28e-05

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: 46.16  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISAGDFFQAY-QAGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVI-DHGLPESLGDVVQQALD 117
Cdd:cd19966    1 KIYFIPGGAPGDPFWTVvYNGAKDAAADLGVDLDYVFSSWDPEKMVEQFKEAIAAKPDGIAImGHPGDGAYTPLIEAAKK 80

                         90
                 ....*....|..
gi 499969044 118 KGIKVVAFDVNL 129
Cdd:cd19966   81 AGIIVTSFNTDL 92
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
1-311 4.23e-05

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 44.70  E-value: 4.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044   1 MKSLARLaLSAAVIPFIFIQGAKADGlsgapapfdkggvKVALISYISAGDFFQAYQAGAEAQAKALDIDLRIFPGRQDA 80
Cdd:PRK10653   3 MKKLATL-VSAVALSATVSANAMAKD-------------TIALVVSTLNNPFFVSLKDGAQKEADKLGYNLVVLDSQNNP 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  81 AEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNLNNPKIPQVEQSDHELAS-LALEQVVKDNGNs 159
Cdd:PRK10653  69 AKELANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRGATKGEVVSHIASDNVAGGkMAGDFIAKKLGE- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 160 fNAGYVYVAGFAPLDRRNEVWDKFKSdnkgVVEKARFgnvsDTTATSTAD--QAKAV------LTANPDISVVFAPYDEF 231
Cdd:PRK10653 148 -GAKVIQLEGIAGTSAARERGEGFKQ----AVAAHKF----NVLASQPADfdRTKGLnvmqnlLTAHPDVQAVFAQNDEM 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 232 ARGVKLAANDLGiASKLKIYSADvSTADIQEIIEEGSpWVATVATNPAVVGAVSIRAAALEIAGQTVPHQITVKPTLLTQ 311
Cdd:PRK10653 219 ALGALRALQTAG-KSDVMVVGFD-GTPDGIKAVNRGK-LAATIAQQPDQIGAIGVETADKVLKGEKVEAKIPVDLKLVTK 295
Periplasmic_Binding_Protein_type1 cd01391
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
 52-290 7.45e-05

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: 43.80  E-value: 7.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  52 FFQAYQAGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHglPESLGDVVQ-QALDKGIKVVAFDV--- 127
Cdd:cd01391   16 FGIQRVEAIFHTADKLGASVEIRDSCWHGSVALEQSIEFIRDNIAGVIGPG--SSSVAIVIQnLAQLFDIPQLALDAtsq 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 128 NLNNPKIPQVEQS---DHELASLALEQVVKDNGNSFnAGYVYVAGFAPLDRRNEVWDKF--KSDNKGVVEKarfgnVSDT 202
Cdd:cd01391   94 DLSDKTLYKYFLSvvfSDTLGARLGLDIVKRKNWTY-VAAIHGEGLNSGELRMAGFKELakQEGICIVASD-----KADW 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 203 TATSTA-DQAKAVLTANPDISVVFAPYDEFARGVKLAANDLGIASKLKIYSADvSTADIQEI-IEEGSPWVATVATNPAV 280
Cdd:cd01391  168 NAGEKGfDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLVGDVSVIGSD-GWADRDEVgYEVEANGLTTIKQQKMG 246

                        250
                 ....*....|
gi 499969044 281 VGAVSIRAAA 290
Cdd:cd01391  247 FGITAIKAMA 256
PBP1_arabinose_binding cd01540
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ...
 53-312 1.16e-04

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: 43.43  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  53 FQAYQAGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVI---DhglpESLGD-VVQQALDKGIKVVAFDVN 128
Cdd:cd01540   14 FQDEWKGAKKAAKELGFEVIKIDAKMDGEKVLSAIDNLIAQGAQGIVIctpD----QKLGPaIAAKAKAAGIPVIAVDDQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 129 L----NNPKIPQVEQSDHELASL---ALEQVVKDNG--NSFNAGYVYVAgFAPL----DRRNEVWDKFKSdnKGVVEKAR 195
Cdd:cd01540   90 LvdadPMKIVPFVGIDAYKIGEAvgeWLAKEMKKRGwdDVKEVGVLAIT-MDTLsvcvDRTDGAKDALKA--AGFPEDQI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 196 FGNVSDTTATSTA-DQAKAVLTANPDIS--VVFAPYDEfarGVKLAANDLGIASKLKIYSADV----STADIQEIIEEGS 268
Cdd:cd01540  167 FQAPYKGTDTEGAfNAANAVITAHPEVKhwLVVGCNDE---GVLGAVRALEQAGFDAEDIIGVgiggYLAADEEFKKQPT 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 499969044 269 PWVATVATNPAVVGAVSIRAAALEIA-GQTVPHQITVKPTLLTQE 312
Cdd:cd01540  244 GFKASLYISPDKHGYIAAEELYNWITdGKPPPAETLTDGVIVTRD 288
PBP1_ABC_xylose_binding cd19991
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ...
 78-265 2.42e-04

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: 42.22  E-value: 2.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  78 QDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNLNNPKIPQVEQSDHE-LASLALEQVVKdn 156
Cdd:cd19991   39 GDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYDRLILNADVDLYVSFDNEkVGELQAEALVK-- 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 157 gNSFNAGYVYVAGfAPLDR-----RNEVWDKFKSD-NKGVVEKARFGNVSDTTATSTADQAKAVLTAN-PDISVVFAPYD 229
Cdd:cd19991  117 -AKPKGNYVLLGG-SPTDNnaklfREGQMKVLQPLiDSGDIKVVGDQWVDDWDPEEALKIMENALTANnNKIDAVIASND 194

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 499969044 230 EFARGVKLAANDLGIASKLKIYSADVSTADIQEIIE 265
Cdd:cd19991  195 GTAGGAIQALAEQGLAGKVAVSGQDADLAACQRIVE 230
PRK15408 PRK15408
autoinducer 2 ABC transporter substrate-binding protein LsrB;
40-227 4.10e-04

autoinducer 2 ABC transporter substrate-binding protein LsrB;


Pssm-ID: 237961  Cd Length: 336  Bit Score: 41.70  E-value: 4.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISAGDFFQAYQAGAEAQAKALDIDLRI-FPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDK 118
Cdd:PRK15408  25 RIAFIPKLVGVGFFTSGGNGAKEAGKELGVDVTYdGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQR 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 119 GIKVVAFDVNLN--------NPKIPqvEQSDHELASLALEQVVKDNGNsfnagyvyVAGF--APLDRRNEVW-----DKF 183
Cdd:PRK15408 105 GVKVLTWDSDTKpecrsyyiNQGTP--EQLGSMLVEMAAKQVGKDKAK--------VAFFysSPTVTDQNQWvkeakAKI 174

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 499969044 184 KSDNKG-VVEKARFGNVSDTTATSTADqakAVLTANPDISVVFAP 227
Cdd:PRK15408 175 AKEHPGwEIVTTQFGYNDATKSLQTAE---GILKAYPDLDAIIAP 216
PBP1_ABC_rhamnose cd20000
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ...
 52-126 5.03e-04

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: 41.47  E-value: 5.03e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499969044  52 FFQAYQAGAEAQAKALDIDLRIF-PGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFD 126
Cdd:cd20000   13 YFDAARDGAKEAAKELGGELIFVgPTTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAAGIKVVTFD 88
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
 41-244 7.36e-04

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


Pssm-ID: 380491 [Multi-domain]  Cd Length: 264  Bit Score: 40.58  E-value: 7.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  41 VALISYISAGDFFQAYQAGAEAQAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESlgDVVQQALDKGI 120
Cdd:cd06267    2 IGLIVPDISNPFFAELLRGIEDAARERGYSLLLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDD--ELLEELLAAGI 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 121 KVVAFDVNLNNPKIPQVEqSDHELAS-LALEQVVKdngnsfnAGY---VYVAG---FAPLDRRNEVWDKFKSDNKGVVEK 193
Cdd:cd06267   80 PVVLIDRRLDGLGVDSVV-VDNYAGAyLATEHLIE-------LGHrriAFIGGpldLSTSRERLEGYRDALAEAGLPVDP 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 499969044 194 ARFgNVSDTTATSTADQAKAVLTANPDISVVFAPYDEFARGVKLAANDLGI 244
Cdd:cd06267  152 ELV-VEGDFSEESGYEAARELLALPPRPTAIFAANDLMAIGALRALRELGL 201
xylF PRK10355
D-xylose ABC transporter substrate-binding protein;
63-265 1.65e-03

D-xylose ABC transporter substrate-binding protein;


Pssm-ID: 182403 [Multi-domain]  Cd Length: 330  Bit Score: 39.73  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  63 QAKALDIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAFDVNLNNPKIPQVEQSDH 142
Cdd:PRK10355  50 KAESLGAKVFVQSANGNEETQMSQIENMINRGVDVLVIIPYNGQVLSNVIKEAKQEGIKVLAYDRMINNADIDFYISFDN 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044 143 E-LASLALEQVVKD--NGNSFNAGYVYVAGFAPLDRRNEVwdkfkSDNKGVVEKARFGNVSDTTATS-TADQAKAV---- 214
Cdd:PRK10355 130 EkVGELQAKALVDKvpQGNYFLMGGSPVDNNAKLFRAGQM-----KVLKPYIDSGKIKVVGDQWVDGwLPENALKImena 204

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 499969044 215 LTANPD-ISVVFAPYDEFARGVKLAANDLGIASKLKIYSADVSTADIQEIIE 265
Cdd:PRK10355 205 LTANNNkIDAVVASNDATAGGAIQALSAQGLSGKVAISGQDADLAAIKRIVA 256
PBP1_LacI-like cd06287
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
 208-245 2.78e-03

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


Pssm-ID: 380510 [Multi-domain]  Cd Length: 268  Bit Score: 38.94  E-value: 2.78e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 499969044 208 ADQAKAVLTANPDISVVFAPYDEFARGVKLAANDLGIA 245
Cdd:cd06287  166 YEAAAALLAAHPDIDAVCVPVDAFAVGAMRAARDSGRS 203
PBP1_LsrB_Quorum_Sensing-like cd20002
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
 40-126 3.51e-03

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: 38.84  E-value: 3.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499969044  40 KVALISYISAGDFFQAYQAGAEAQAKALDIDL-RIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDK 118
Cdd:cd20002    1 TIVTVVKLAGIPWFNRMEQGVKKAGKEFGVNAyQVGPADADPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREK 80


                 ....*...
gi 499969044 119 GIKVVAFD 126
Cdd:cd20002   81 GIVVITHE 88
PBP1_GGBP cd01539
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ...
 52-125 4.32e-03

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


Pssm-ID: 380481 [Multi-domain]  Cd Length: 302  Bit Score: 38.33  E-value: 4.32e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 499969044  52 FFQAYQAGAEAQAKAL-DIDLRIFPGRQDAAEQREQILQAINLGVSGIVIDHGLPESLGDVVQQALDKGIKVVAF 125
Cdd:cd01539   14 FISSVRKALEKAAKAGgKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAANIPVIFF 88
 
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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