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Conserved domains on  [gi|490184078|ref|WP_004082691|]
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MULTISPECIES: sugar-binding protein [Thermotoga]

Protein Classification

sugar-binding protein( domain architecture ID 10156885)

periplasmic sugar-binding protein such as Thermotoga maritima glucose-binding protein (TmGBP) and its close homologs from other bacteria is a member of the type 1 periplasmic binding protein superfamily and consists of two domains connected by a three-stranded hinge. TmGBP is specific for glucose and its binding pocket is buried at the interface between the two domains

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
21-303 1.84e-125

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: 359.97  E-value: 1.84e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSV-HPYWSQVEQGVKAAGKALGVDTKFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEM 99
Cdd:cd06314    1 TFALVPKGLnNPFWDLAEAGAEKAAKELGVNVEFVGPQKSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSE-IEIVDIL 178
Cdd:cd06314   81 GIPVITFDSDAPDSKRLAYIGTDNYEAGREAGELMKKALPGGGKVAIITGGLGADNLNERIQGFKDALKGSPgIEIVDPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 179 NDEEDGARAVSLAEAALNAHPDLDAFFGVYAYNGPAQALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRPYM 258
Cdd:cd06314  161 SDNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKVGKVKIVGFDTLPETLQGIKDGVIAATVGQRPYE 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 490184078 259 MGYLSVTVLYLMNKIGvqntlmmlpkvkvdGKVDYVIDTGVDVVT 303
Cdd:cd06314  241 MGYLSVKLLYKLLKGG--------------KPVPDVIDTGVDVVT 271
 
Name Accession Description Interval E-value
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
21-303 1.84e-125

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: 359.97  E-value: 1.84e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSV-HPYWSQVEQGVKAAGKALGVDTKFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEM 99
Cdd:cd06314    1 TFALVPKGLnNPFWDLAEAGAEKAAKELGVNVEFVGPQKSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSE-IEIVDIL 178
Cdd:cd06314   81 GIPVITFDSDAPDSKRLAYIGTDNYEAGREAGELMKKALPGGGKVAIITGGLGADNLNERIQGFKDALKGSPgIEIVDPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 179 NDEEDGARAVSLAEAALNAHPDLDAFFGVYAYNGPAQALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRPYM 258
Cdd:cd06314  161 SDNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKVGKVKIVGFDTLPETLQGIKDGVIAATVGQRPYE 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 490184078 259 MGYLSVTVLYLMNKIGvqntlmmlpkvkvdGKVDYVIDTGVDVVT 303
Cdd:cd06314  241 MGYLSVKLLYKLLKGG--------------KPVPDVIDTGVDVVT 271
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
19-307 2.05e-87

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: 264.48  E-value: 2.05e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  19 ALTIGVIGKSV-HPYWSQVEQGVKAAGKALGVDTKFfVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKAL 97
Cdd:COG1879   33 GKTIGFVVKTLgNPFFVAVRKGAEAAAKELGVELIV-VDAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDALAPALKKAK 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  98 EMGIPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKD-SEIEIVD 176
Cdd:COG1879  112 AAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGGKGKVAILTGSPGAPAANERTDGFKEALKEyPGIKVVA 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 177 ILNDEEDGARAVSLAEAALNAHPDLDAFFGVYAYNGPAQALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRP 256
Cdd:COG1879  192 EQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRKGDVKVVGFDGSPEALQAIKDGTIDATVAQDP 271
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490184078 257 YMMGYLSVTVLYLMnkigvqntlmmlpkvkVDGK-VDYVIDTGVDVVTPENL 307
Cdd:COG1879  272 YLQGYLAVDAALKL----------------LKGKeVPKEILTPPVLVTKENV 307
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
22-268 9.50e-71

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: 220.26  E-value: 9.50e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078   22 IGVIGKSV-HPYWSQVEQGVKAAGKALGVDTKFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMG 100
Cdd:pfam13407   1 IGVVPKSTgNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  101 IPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKD--SEIEIVD-I 177
Cdd:pfam13407  81 IPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLKEkyPGIKVVAeV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  178 LNDEEDGARAVSLAEAALNAHPD-LDAFFGVYAYNGPAQALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRP 256
Cdd:pfam13407 161 EGTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGKVVVTGFDATPEALEAIKDGTIDATVLQDP 240
                         250
                  ....*....|..
gi 490184078  257 YMMGYLSVTVLY 268
Cdd:pfam13407 241 YGQGYAAVELAA 252
PRK09701 PRK09701
D-allose transporter substrate-binding protein;
31-286 5.69e-29

D-allose transporter substrate-binding protein;


Pssm-ID: 182037 [Multi-domain]  Cd Length: 311  Bit Score: 113.04  E-value: 5.69e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  31 PYWSQVEQGVKAAGKALGVDTKFFV-PQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDT- 108
Cdd:PRK09701  37 PFWVDMKKGIEDEAKTLGVSVDIFAsPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEk 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 109 ----DSPDSGRYV--YIGTDNYQAGYT-AGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDA-IKDSEIEIVDILND 180
Cdd:PRK09701 117 idmdNLKKAGGNVeaFVTTDNVAVGAKgASFIIDKLGAEGGEVAIIEGKAGNASGEARRNGATEAfKKASQIKLVASQPA 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 181 EEDGARAVSLAEAALNAHPDLDAFfgvYAYN-----GPAQAlvVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQR 255
Cdd:PRK09701 197 DWDRIKALDVATNVLQRNPNIKAI---YCANdtmamGVAQA--VANAGKTGKVLVVGTDGIPEARKMVEAGQMTATVAQN 271
                        250       260       270
                 ....*....|....*....|....*....|.
gi 490184078 256 PYMMGYLSVTVLYLMNKIGVQNTLMMLPKVK 286
Cdd:PRK09701 272 PADIGATGLKLMVDAEKSGKVIPLDKAPEFK 302
 
Name Accession Description Interval E-value
PBP1_tmGBP cd06314
periplasmic sugar-binding domain of Thermotoga maritima glucose-binding protein (tmGBP) and ...
21-303 1.84e-125

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: 359.97  E-value: 1.84e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSV-HPYWSQVEQGVKAAGKALGVDTKFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEM 99
Cdd:cd06314    1 TFALVPKGLnNPFWDLAEAGAEKAAKELGVNVEFVGPQKSDAAEQVQLIEDLIARGVDGIAISPNDPEAVTPVINKAADK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSE-IEIVDIL 178
Cdd:cd06314   81 GIPVITFDSDAPDSKRLAYIGTDNYEAGREAGELMKKALPGGGKVAIITGGLGADNLNERIQGFKDALKGSPgIEIVDPL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 179 NDEEDGARAVSLAEAALNAHPDLDAFFGVYAYNGPAQALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRPYM 258
Cdd:cd06314  161 SDNDDIAKAVQNVEDILKANPDLDAIFGVGAYNGPAIAAALKDAGKVGKVKIVGFDTLPETLQGIKDGVIAATVGQRPYE 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 490184078 259 MGYLSVTVLYLMNKIGvqntlmmlpkvkvdGKVDYVIDTGVDVVT 303
Cdd:cd06314  241 MGYLSVKLLYKLLKGG--------------KPVPDVIDTGVDVVT 271
PBP1_ABC_sugar_binding-like cd19969
monosaccharide ABC transporter substrate binding protein; Periplasmic sugar-binding domain of ...
22-301 5.53e-93

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: 277.68  E-value: 5.53e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  22 IGVIGKSVHPYWSQVEQGVKAAGKALGVDTKFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGI 101
Cdd:cd19969    3 VMVTFKSGHPYWDDVKEGFEDAGAELGVKTEYTGPATADVNEQITAIEQAIAKNPDGIAVSAIDPEALTPTINKAVDAGI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 102 PVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAmNSLQRIQGFKDAIKDS-EIEIVDILND 180
Cdd:cd19969   83 PVVTFDSDAPESKRISYVGTDNYEAGYAAAEKLAELLGGKGKVAVLTGPGQP-NHEERVEGFKEAFAEYpGIEVVAVGDD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 181 EEDGARAVSLAEAALNAHPDLDAFFGVYAYNGPAQALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRPYMMG 260
Cdd:cd19969  162 NDDPEKAAQNTSALLQAHPDLVGIFGVDASGGVGAAQAVREAGKTGKVKIVAFDDDPETLDLIKDGVIDASIAQRPWMMG 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 490184078 261 YLSVTVLYLMNkigvQNTLMMLPKVKVDGKVDYVIDTGVDV 301
Cdd:cd19969  242 YWSLQFLYDLA----NGLVKDAWQTAGVNPLPPYVDTGITI 278
RbsB COG1879
ABC-type sugar transport system, periplasmic component, contains N-terminal xre family HTH ...
19-307 2.05e-87

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: 264.48  E-value: 2.05e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  19 ALTIGVIGKSV-HPYWSQVEQGVKAAGKALGVDTKFfVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKAL 97
Cdd:COG1879   33 GKTIGFVVKTLgNPFFVAVRKGAEAAAKELGVELIV-VDAEGDAAKQISQIEDLIAQGVDAIIVSPVDPDALAPALKKAK 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  98 EMGIPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKD-SEIEIVD 176
Cdd:COG1879  112 AAGIPVVTVDSDVDGSDRVAYVGSDNYAAGRLAAEYLAKALGGKGKVAILTGSPGAPAANERTDGFKEALKEyPGIKVVA 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 177 ILNDEEDGARAVSLAEAALNAHPDLDAFFGVYAYNGPAQALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRP 256
Cdd:COG1879  192 EQYADWDREKALEVMEDLLQAHPDIDGIFAANDGMALGAAQALKAAGRKGDVKVVGFDGSPEALQAIKDGTIDATVAQDP 271
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 490184078 257 YMMGYLSVTVLYLMnkigvqntlmmlpkvkVDGK-VDYVIDTGVDVVTPENL 307
Cdd:COG1879  272 YLQGYLAVDAALKL----------------LKGKeVPKEILTPPVLVTKENV 307
PBP1_ABC_sugar_binding-like cd01536
periplasmic sugar-binding domain of active transport systems that are members of the type 1 ...
21-268 2.21e-79

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: 242.47  E-value: 2.21e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKS-VHPYWSQVEQGVKAAGKALGVDTKFFVPQKeDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEM 99
Cdd:cd01536    1 KIGVVVKDlTNPFWVAVKKGAEAAAKELGVELVVLDAQG-DVAKQISQIEDLIAQGVDAIIIAPVDSEALVPAVKKANAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTLDTDSPDSGRYV-YIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDS-EIEIVDI 177
Cdd:cd01536   80 GIPVVAVDTDIDGGGDVVaFVGTDNYEAGKLAGEYLAEALGGKGKVAILEGPPGSSTAIDRTKGFKEALKKYpDIEIVAE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 178 LNDEEDGARAVSLAEAALNAHPDLDAFFGVYAYNGPAQALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRPY 257
Cdd:cd01536  160 QPANWDRAKALTVTENLLQANPDIDAVFAANDDMALGAAEALKAAGRTGDIKIVGVDGTPEALKAIKDGELDATVAQDPY 239
                        250
                 ....*....|.
gi 490184078 258 MMGYLSVTVLY 268
Cdd:cd01536  240 LQGYLAVEAAV 250
Peripla_BP_4 pfam13407
Periplasmic binding protein domain; This domain is found in a variety of bacterial periplasmic ...
22-268 9.50e-71

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: 220.26  E-value: 9.50e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078   22 IGVIGKSV-HPYWSQVEQGVKAAGKALGVDTKFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMG 100
Cdd:pfam13407   1 IGVVPKSTgNPFFQAAEEGAEEAAKELGGEVIVVGPAEADAAEQVAQIEDAIAQGVDAIIVAPVDPTALAPVLKKAKDAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  101 IPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKD--SEIEIVD-I 177
Cdd:pfam13407  81 IPVVTFDSDAPSSPRLAYVGFDNEAAGEAAGELLAEALGGKGKVAILSGSPGDPNANERIDGFKKVLKEkyPGIKVVAeV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  178 LNDEEDGARAVSLAEAALNAHPD-LDAFFGVYAYNGPAQALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRP 256
Cdd:pfam13407 161 EGTNWDPEKAQQQMEALLTAYPNpLDGIISPNDGMAGGAAQALEAAGLAGKVVVTGFDATPEALEAIKDGTIDATVLQDP 240
                         250
                  ....*....|..
gi 490184078  257 YMMGYLSVTVLY 268
Cdd:pfam13407 241 YGQGYAAVELAA 252
PBP1_ABC_sugar_binding-like cd20008
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
21-304 7.41e-64

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: 203.23  E-value: 7.41e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSV-HPYWSQVEQGVKAAGKALGVDTKFFVPQKE-DINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALE 98
Cdd:cd20008    1 KIAVIVKDTdSEYWQTVLKGAEKAAKELGVEVTFLGPATEaDIAGQVNLVENAISRKPDAIVLAPNDTAALVPAVEAADA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  99 mGIPVVTLDTdSPDSGRYV-YIGTDNYQAGYTAGLIMKELL----GGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDS--E 171
Cdd:cd20008   81 -GIPVVLVDS-GANTDDYDaFLATDNVAAGALAADELAELLkasgGGKGKVAIISFQAGSQTLVDREEGFRDYIKEKypD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 172 IEIVDILNDEEDGARAVSLAEAALNAHPDLDAFFGVYAYNGPAQALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQAT 251
Cdd:cd20008  159 IEIVDVQYSDGDIAKALNQTTDLLTANPDLVGIFGANNPSAVGVAQALAEAGKAGKIVLVGFDSSPDEVALLKSGVIKAL 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490184078 252 MGQRPYMMGYLsvtvlylmnkiGVQNTLMMLPKVKVDGKvdyVIDTGVDVVTP 304
Cdd:cd20008  239 VVQDPYQMGYE-----------GVKTAVKALKGEEIVEK---NVDTGVTVVTK 277
PBP1_ABC_sugar_binding-like cd19965
monosaccharide ABC transporter substrate binding protein CUT2 family and similar proteins; ...
31-275 2.78e-63

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: 201.73  E-value: 2.78e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  31 PYWSQVEQGVKAAGKALGVDTKFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDTDS 110
Cdd:cd19965   12 PFFQPVKKGMDDACELLGAECQFTGPQTFDVAEQVSLLEAAIASGPDGIATTIVDPEAFDEVIKRALDAGIPVVAFNVDA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 111 PD--SGRYVYIGTDNYQAGYTAGL-IMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDS----EIEIVDILNDEed 183
Cdd:cd19965   92 PGgeNARLAFVGQDLYPAGYVLGKrIAEKFKPGGGHVLLGISTPGQSALEQRLDGIKQALKEYgrgiTYDVIDTGTDL-- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 184 gARAVSLAEAALNAHPDLDAFFGVYAYNGPAQALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRPYMMGYLS 263
Cdd:cd19965  170 -AEALSRIEAYYTAHPDIKAIFATGAFDTAGAGQAIKDLGLKGKVLVGGFDLVPEVLQGIKAGYIDFTIDQQPYLQGFYP 248
                        250
                 ....*....|..
gi 490184078 264 VTVLYLMNKIGV 275
Cdd:cd19965  249 VMQLFLYKKFGL 260
PBP1_ABC_sugar_binding-like cd20005
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
21-303 1.50e-62

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: 199.78  E-value: 1.50e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSV-HPYWSQVEQGVKAAGKALGVDTKFFVPQKE-DINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALE 98
Cdd:cd20005    1 YIAVISKGFqHQFWKAVKKGAEQAAKELGVKITFEGPDTEsDVDKQIEMLDNAIAKKPDAIALAALDTNALLPQLEKAKE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  99 MGIPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKD--SEIEIVD 176
Cdd:cd20005   81 KGIPVVTFDSGVPSDLPLATVATDNYAAGALAADHLAELIGGKGKVAIVAHDATSETGIDRRDGFKDEIKEkyPDIKVVN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 177 ILNDEEDGARAVSLAEAALNAHPDLDaffGVYAYNGPAQ---ALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMG 253
Cdd:cd20005  161 VQYGVGDHAKAADIAKAILQANPDLK---GIYATNEGAAigvANALKEMGKLGKIKVVGFDSGEAQIDAIKNGVIAGSVT 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 490184078 254 QRPYMMGYLSVTVLYlmnkigvqntlmmlpKVKVDGKVDYVIDTGVDVVT 303
Cdd:cd20005  238 QNPYGMGYKTVKAAV---------------KALKGEEVEKLIDTGAKWYD 272
PBP1_LsrB_Quorum_Sensing-like cd06302
periplasmic binding domain of autoinducer-2 (AI-2) receptor LsrB from Salmonella typhimurium ...
21-308 1.66e-62

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: 200.16  E-value: 1.66e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSV-HPYWSQVEQGVKAAGKALGVDTKFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEM 99
Cdd:cd06302    1 KIAFVPKVVgIPYFDAAEEGAKKAAKELGVEVVYTGPTQADAAQQVQIVENLIAQGVDAIAVSPNDADALAPVLKKAKDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTLDTDSPDSGRYVYI-GTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDS--EIEIVD 176
Cdd:cd06302   81 GIKVITWDSDAPPSARDYFVnQADDEGLGEALVDSLAKEIGGKGKVAILSGSLTATNLNAWIKAMKEYLKSKypDIELVD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 177 ILNDEEDGARAVSLAEAALNAHPDLDAFFGVYAYNGPAQALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRP 256
Cdd:cd06302  161 TYYTDDDQQKAYTQAQNLIQAYPDLKGIIGVSTTAPPAAAQAVEEAGKTGKVAVTGIGLPNTARPYLKDGSVKEGVLWDP 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 490184078 257 YMMGYLSVTVLYLM----NKIGVQNTLMMLPKVKVDGKVDYVIDTGVDVVTPENLD 308
Cdd:cd06302  241 AKLGYLTVYAAYQLlkgkGFTEDSDDVGTGGKVKVDVAGGEILLGPPLVFTKDNVD 296
PBP1_ABC_sugar_binding-like cd20004
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
21-304 6.52e-59

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: 190.52  E-value: 6.52e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKS-VHPYWSQVEQGVKAAGKALGVDTKFFVPQKE-DINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALE 98
Cdd:cd20004    1 CIAVIPKGtTHDFWKSVKAGAEKAAQELGVEIYWRGPSREdDVEAQIQIIEYFIDQGVDGIVLAPLDRKALVAPVERARA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  99 MGIPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVI-----GTGSLTamnslQRIQGFKDAIK--DSE 171
Cdd:cd20004   81 QGIPVVIIDSDLGGDAVISFVATDNYAAGRLAAKRMAKLLNGKGKVALlrlakGSASTT-----DRERGFLEALKklAPG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 172 IEIVDI--LNDEEDGARAVslAEAALNAHPDLDAFFGVYAYNGPAQALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQ 249
Cdd:cd20004  156 LKVVDDqyAGGTVGEARSS--AENLLNQYPDVDGIFTPNESTTIGALRALRRLGLAGKVKFIGFDASDLLLDALRAGEIS 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 490184078 250 ATMGQRPYMMGYLSVTVLY--LMNKigvqntlmmlpkvkvdgKVDYVIDTGVDVVTP 304
Cdd:cd20004  234 ALVVQDPYRMGYLGVKTAVaaLRGK-----------------PVPKRIDTGVVLVTK 273
PBP1_ABC_sugar_binding-like cd20007
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
17-268 1.53e-58

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: 189.37  E-value: 1.53e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  17 SLALTIGVIGksvHPYWSQVEQGVKAAGKALGVDTKFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKA 96
Cdd:cd20007    1 TIALVPGVTG---DPFYITMQCGAEAAAKELGVELDVQGPPTFDPTLQTPIVNAVIAKKPDALLIAPTDPQALIAPLKRA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  97 LEMGIPVVTLDTDSPD-SGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIK-DSEIEI 174
Cdd:cd20007   78 ADAGIKVVTVDTTLGDpSFVLSQIASDNVAGGALAAEALAELIGGKGKVLVINSTPGVSTTDARVKGFAEEMKkYPGIKV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 175 VDILNDEEDGARAVSLAEAALNAHPDLDAFFGVYAYN--GPAQALvvKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATM 252
Cdd:cd20007  158 LGVQYSENDPAKAASIVAAALQANPDLAGIFGTNTFSaeGAAAAL--RNAGKTGKVKVVGFDASPAQVEQLKAGTIDALI 235
                        250
                 ....*....|....*.
gi 490184078 253 GQRPYMMGYLSVTVLY 268
Cdd:cd20007  236 AQKPAEIGYLAVEQAV 251
PBP1_ABC_sugar_binding-like cd06312
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
30-276 1.53e-58

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: 189.37  E-value: 1.53e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  30 HPYWSQVEQGVKAAGKALGVDTKFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTL--- 106
Cdd:cd06312   12 DPFWSVVKKGAKDAAKDLGVTVQYLGPQNNDIADQARLIEQAIAAKPDGIIVTIPDPDALEPALKRAVAAGIPVIAInsg 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 107 -DTDSPDSGRYVYIGTDNYQAGYTAGLIMKEllGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSEIEiVDILNDEEDGA 185
Cdd:cd06312   92 dDRSKERLGALTYVGQDEYLAGQAAGERALE--AGPKNALCVNHEPGNPGLEARCKGFADAFKGAGIL-VELLDVGGDPT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 186 RAVSLAEAALNAHPDLDAFFGVyaynGPAQAL----VVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRPYMMGY 261
Cdd:cd06312  169 EAQEAIKAYLQADPDTDAVLTL----GPVGADpalkAVKEAGLKGKVKIGTFDLSPETLEAIKDGKILFAIDQQPYLQGY 244
                        250
                 ....*....|....*
gi 490184078 262 LSVTVLYLMNKIGVQ 276
Cdd:cd06312  245 LAVVFLYLYKRYGTL 259
PBP1_ABC_sugar_binding-like cd20006
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
21-304 5.93e-58

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: 187.80  E-value: 5.93e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSVHP---YWSQVEQGVKAAGKALGVDTKFFVPQKE-DINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKA 96
Cdd:cd20006    1 KIALILKSSDPnsdFWQTVKSGAEAAAKEYGVDLEFLGPESEeDIDGQIELIEEAIAQKPDAIVLAASDYDRLVEAVERA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  97 LEMGIPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAI-KDSEIEIV 175
Cdd:cd20006   81 KKAGIPVITIDSPVNSKKADSFVATDNYEAGKKAGEKLASLLGEKGKVAIVSFVKGSSTAIEREEGFKQALaEYPNIKIV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 176 DILNDEEDGARAVSLAEAALNAHPDLDAFFGV--YAYNGPAQAlvVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMG 253
Cdd:cd20006  161 ETEYCDSDEEKAYEITKELLSKYPDINGIVALneQSTLGAARA--LKELGLGGKVKVVGFDSSVEEIQLLEEGIIDALVV 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490184078 254 QRPYMMGYLSvtvlylmnkigVQNTLMMLPKVKVDGKvdyvIDTGVDVVTP 304
Cdd:cd20006  239 QNPFNMGYLS-----------VQAAVDLLNGKKIPKR----IDTGSVVITK 274
PBP1_ABC_sugar_binding-like cd06310
monosaccharide ABC transporter substrate-binding protein such as CUT2; Periplasmic ...
21-268 3.67e-57

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: 186.01  E-value: 3.67e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKS-VHPYWSQVEQGVKAAGKALGVDTKFFVPQKE-DINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALE 98
Cdd:cd06310    1 KIGVVLKGtTSAFWRTVREGAEAAAKDLGVKIIFVGPESEeDVAGQNSLLEELINKKPDAIVVAPLDSEDLVDPLKDAKD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  99 MGIPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDS--EIEIVD 176
Cdd:cd06310   81 KGIPVIVIDSGIKGDAYLSYIATDNYAAGRLAAQKLAEALGGKGKVAVLSLTAGNSTTDQREEGFKEYLKKHpgGIKVLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 177 ILNDEEDGARAVSLAEAALNAHPDLDAFFGVYAYNGPAQALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRP 256
Cdd:cd06310  161 SQYAGSDYAKAANETEDLLGKYPDIDGIFATNEITALGAAVAIKSRKLSGQIKIVGFDSQEELLDALKNGKIDALVVQNP 240
                        250
                 ....*....|..
gi 490184078 257 YMMGYLSVTVLY 268
Cdd:cd06310  241 YEIGYEGIKLAL 252
PBP1_ABC_sugar_binding-like cd06322
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
21-268 1.94e-51

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: 170.92  E-value: 1.94e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGV-IGKSVHPYWSQVEQGVKAAGKALGVDTKFFVPQkEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEM 99
Cdd:cd06322    1 TIGVsLLTLQHPFFVDIKDAMKKEAAELGVKVVVADAN-GDLAKQLSQIEDFIQQGVDAIILAPVDSGGIVPAIEAANEA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTLDTdSPDSGRYV-YIGTDNYQAGYTAGLIMKE-LLGGKGKVVIgTGSLTAMNSLQRIQGFKDAIKDSE-IEIVD 176
Cdd:cd06322   80 GIPVFTVDV-KADGAKVVtHVGTDNYAGGKLAGEYALKaLLGGGGKIAI-IDYPEVESVVLRVNGFKEAIKKYPnIEIVA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 177 ILNDEEDGARAVSLAEAALNAHPDLDAFFgvyAYNGPAqAL----VVKNAGKVGKVKIVCFDTTPDILQYV-KEGVIQAT 251
Cdd:cd06322  158 EQPGDGRREEALAATEDMLQANPDLDGIF---AIGDPA-ALgaltAIESAGKEDKIKVIGFDGNPEAIKAIaKGGKIKAD 233
                        250
                 ....*....|....*..
gi 490184078 252 MGQRPYMMGYLSVTVLY 268
Cdd:cd06322  234 IAQQPDKIGQETVEAIV 250
PBP1_LsrB_Quorum_Sensing cd20003
ligand-binding protein LsrB of ABC transporter periplasmic binding protein; Periplasmic ...
21-270 2.58e-50

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: 169.00  E-value: 2.58e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSV-HPYWSQVEQGVKAAGKALGVDTKFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEM 99
Cdd:cd20003    1 TIAMIPKLVgVPYFTAAGQGAQEAAKELGVDVTYDGPTEASVSKQVEVINNFINQGYDVIAVSANDPDALAPALKKAMKK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTLDTDSPDSGRYVYIGTDNYQA-GYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDS--EIEIVD 176
Cdd:cd20003   81 GIKVVTWDSDVNPDARDFFVNQATPEGiGKTLVDMVAEQTGEKGKVAIVTSSPTATNQNAWIKAMKAYIAEKypDMKIVT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 177 ILNDEEDGARAVSLAEAALNAHPDLDAFFGVYAYNGPAQALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRP 256
Cdd:cd20003  161 TQYGQEDPAKSLQVAENILKAYPDLKAIIAPDSVALPGAAEAVEQLGRTGKVAVTGLSTPNVMRPYVKDGTVKSVVLWDV 240
                        250
                 ....*....|....
gi 490184078 257 YMMGYLSVTVLYLM 270
Cdd:cd20003  241 VDLGYLAVYVARAL 254
PBP1_allose_binding cd06320
periplasmic allose-binding domain of bacterial transport systems that function as a primary ...
22-308 5.11e-50

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: 167.82  E-value: 5.11e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  22 IGVIGKSV-HPYWSQVEQGVKAAGKALGVDTKFFVPQKE-DINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEM 99
Cdd:cd06320    2 IGVVLKTLsNPFWVAMKDGIEAEAKKLGVKVDVQAAPSEtDTQGQLNLLETMLNKGYDAILVSPISDTNLIPPIEKANKK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTLDtDSPDSGRY--------VYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIK-DS 170
Cdd:cd06320   82 GIPVINLD-DAVDADALkkaggkvtSFIGTDNVAAGALAAEYIAEKLPGGGKVAIIEGLPGNAAAEARTKGFKETFKkAP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 171 EIEIVDILNDEEDGARAVSLAEAALNAHPDLDAFfgvYAYN-----GPAQAlvVKNAGKVGKVKIVCFDTTPDILQYVKE 245
Cdd:cd06320  161 GLKLVASQPADWDRTKALDAATAILQAHPDLKGI---YAANdtmalGAVEA--VKAAGKTGKVLVVGTDGIPEAKKSIKA 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490184078 246 GVIQATMGQRPYMMGYLSVtvlylmnkigvqntlMMLPKVKVDGKVDYVIDTGVDVVTPENLD 308
Cdd:cd06320  236 GELTATVAQYPYLEGAMAV---------------EAALRLLQGQKVPAVVATPQALITKDNVD 283
PBP1_sugar_binding cd06307
periplasmic sugar-binding domain of uncharacterized transport systems; Periplasmic ...
24-267 2.53e-46

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


Pssm-ID: 380530 [Multi-domain]  Cd Length: 275  Bit Score: 157.72  E-value: 2.53e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  24 VIGKSVHPYWSQVEQGVKAAGKAL---GVDTKFFVPQKEDINAQLQMLESfIAEGVNGIAIAPSDPTAVIPTIKKALEMG 100
Cdd:cd06307    5 LLPSPENPFYELLRRAIEAAAAALrdrRVRLRIHFVDSLDPEALAAALRR-LAAGCDGVALVAPDHPLVRAAIDELAARG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 101 IPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELLGGK-GKVVIGTGSLTAMNSLQRIQGFKDAIKD--SEIEIVDI 177
Cdd:cd06307   84 IPVVTLVSDLPGSRRLAYVGIDNRAAGRTAAWLMGRFLGRRpGKVLVILGSHRFRGHEEREAGFRSVLRErfPDLTVLEV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 178 LNDEEDGARAVSLAEAALNAHPDLDaffGVYAYNGPAQALV--VKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQR 255
Cdd:cd06307  164 LEGLDDDELAYELLRELLARHPDLV---GIYNAGGGNEGIAraLREAGRARRVVFIGHELTPETRRLLRDGTIDAVIDQD 240
                        250
                 ....*....|..
gi 490184078 256 PYMMGYLSVTVL 267
Cdd:cd06307  241 PELQARRAIEVL 252
PBP1_ABC_sugar_binding-like cd06317
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
32-311 3.23e-46

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: 157.92  E-value: 3.23e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  32 YWSQVEQGVKAAGKALGVDTKFFVPQkEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDTDSP 111
Cdd:cd06317   13 FFNQINQGAQAAAKDLGVDLVVFNAN-DDPSKQNTAVDNYIARGVDAIILDAIDVNGSIPAIKRASEAGIPVIAYDAVIP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 112 DSGRYVYIGTDNYQAG-----YTAGLIMKElLGGKGKVVIgTGSLTAMNSLQRIQGFKDAIKDS-EIEIVDILNDEEDGA 185
Cdd:cd06317   92 SDFQAAQVGVDNLEGGkeigkYAADYIKAE-LGGQAKIGV-VGALSSLIQNQRQKGFEEALKANpGVEIVATVDGQNVQE 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 186 RAVSLAEAALNAHPDLDAffgVYAYNGPA---QALVVKNAGKVGKVKIVCFDTTPD-ILQYVKEGVIQATMGQRPYMMGY 261
Cdd:cd06317  170 KALSAAENLLTANPDLDA---IYATGEPAllgAVAAVRSQGRQGKIKVFGWDLTKQaIFLGIDEGVLQAVVQQDPEKMGY 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 490184078 262 LSVTVLYlmnkigvqntlmmlpKVKVDGKVDYVIDTGVDVVTPENLDEYL 311
Cdd:cd06317  247 EAVKAAV---------------KAIKGEDVEKTIDVPPTIVTKENVDQFR 281
PBP1_ABC_sugar_binding-like cd06319
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
25-307 3.47e-46

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: 157.52  E-value: 3.47e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  25 IGKSVH----PYWSQVEQGVKAAGKALGVDTKFFvPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMG 100
Cdd:cd06319    2 IGYSVYdldnPFWQIMERGVQAAAEELGYEFVTY-DQKNSANEQVTNANDLIAQGVDGIIISPTNSSAAPTVLDLANEAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 101 IPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELLGGKG----KVVIGTGSLTAMNSLQRIQGFKDAIKDSEIEIVD 176
Cdd:cd06319   81 IPVVIADIGTGGGDYVSYIISDNYDGGYQAGEYLAEALKENGwgggSVGIIAIPQSRVNGQARTAGFEDALEEAGVEEVA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 177 IL---NDEEDGARavSLAEAALNAHPDLDAFFGVYAYNGPAQALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMG 253
Cdd:cd06319  161 LRqtpNSTVEETY--SAAQDLLAANPDIKGIFAQNDQMAQGALQAIEEAGRTGDILVVGFDGDPEALDLIKDGKLDGTVA 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490184078 254 QRPYMMGYLSVTvlylmnkigvqntlMMLPKVKVDGKVDYVIDTGVDVVTPENL 307
Cdd:cd06319  239 QQPFGMGARAVE--------------LAIQALNGDNTVEKEIYLPVLLVTSENV 278
PBP1_ABC_sugar_binding-like cd19970
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
21-291 4.56e-45

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: 154.71  E-value: 4.56e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSV-HPYWSQVEQG-VKAAGKALGVDTKFFVPQKE-DINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKAL 97
Cdd:cd19970    1 KVALVMKSLaNEFFIEMEKGaRKHAKEANGYELLVKGIKQEtDIEQQIAIVENLIAQKVDAIVIAPADSKALVPVLKKAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  98 EMGIPVVTLDTD-----SPDSGRYV-YIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSE 171
Cdd:cd19970   81 DAGIAVINIDNRldadaLKEGGINVpFVGPDNRQGAYLAGDYLAKKLGKGGKVAIIEGIPGADNAQQRKAGFLKAFEEAG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 172 IEIVDILNDEEDGARAVSLAEAALNAHPDLDaffGVYAYN-----GPAQAlvVKNAGKVGKVKIVCFDTTPDILQYVKEG 246
Cdd:cd19970  161 MKIVASQSANWEIDEANTVAANLLTAHPDIR---GILCANdnmalGAIKA--VDAAGKAGKVLVVGFDNIPAVRPLLKDG 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 490184078 247 VIQATMGQRPYMMGYLsvtvlylmnkiGVQNTLMMLPKVKVDGKV 291
Cdd:cd19970  236 KMLATIDQHPAKQAVY-----------GIEYALKMLNGEEVPGWV 269
PBP1_ABC_sugar_binding-like cd19971
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
31-268 7.53e-44

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: 151.20  E-value: 7.53e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  31 PYWSQVEQGVKAAGKALGVDTKFFVPQKeDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDTDS 110
Cdd:cd19971   12 PFFIAINDGIKKAVEANGDELITRDPQL-DQNKQNEQIEDMINQGVDAIFLNPVDSEGIRPALEAAKEAGIPVINVDTPV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 111 PDSgRYV--YIGTDNYQAGYTAGLIMKELLGGKGKVVIGTgSLTAMNSLQRIQGFKDAIKDS-EIEIVDILNDEEDGARA 187
Cdd:cd19971   91 KDT-DLVdsTIASDNYNAGKLCGEDMVKKLPEGAKIAVLD-HPTAESCVDRIDGFLDAIKKNpKFEVVAQQDGKGQLEVA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 188 VSLAEAALNAHPDLDAFFGVyayNGPAqAL----VVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRPYMMGYLS 263
Cdd:cd19971  169 MPIMEDILQAHPDLDAVFAL---NDPS-ALgalaALKAAGKLGDILVYGVDGSPDAKAAIKDGKMTATAAQSPIEIGKKA 244

                 ....*
gi 490184078 264 VTVLY 268
Cdd:cd19971  245 VETAY 249
PBP1_ribose_binding cd06323
periplasmic sugar-binding domain of the thermophilic Thermoanaerobacter tengcongensis ribose ...
31-279 8.94e-41

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: 143.20  E-value: 8.94e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  31 PYWSQVEQGVKAAGKALGVDTkFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDTDS 110
Cdd:cd06323   12 PFFVSLKDGAQAEAKELGVEL-VVLDAQNDPAKQLSQVEDLIVRKVDALLINPTDSDAVSPAVEEANEAGIPVITVDRSV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 111 PDSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDS-EIEIVDILNDEEDGARAVS 189
Cdd:cd06323   91 TGGKVVSHIASDNVAGGEMAAEYIAKKLGGKGKVVELQGIPGTSAARERGKGFHNAIAKYpKINVVASQTADFDRTKGLN 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 190 LAEAALNAHPDLDAffgVYAYN-----GPAQALvvKNAGKvGKVKIVCFDTTPDILQYVKEGVIQATMGQRPYMMGYLSV 264
Cdd:cd06323  171 VMENLLQAHPDIDA---VFAHNdemalGAIQAL--KAAGR-KDVIVVGFDGTPDAVKAVKDGKLAATVAQQPEEMGAKAV 244
                        250
                 ....*....|....*.
gi 490184078 265 -TVLYLMNKIGVQNTL 279
Cdd:cd06323  245 eTADKYLKGEKVPKKI 260
PBP1_ABC_sugar_binding-like cd06321
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
21-268 1.82e-40

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: 142.43  E-value: 1.82e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSV-HPYWSQVEQGVKAAGKALGVDTKFFVPQKE-DINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALE 98
Cdd:cd06321    1 VIGVTVQDLgNPFFVAMVRGAEEAAAEINPGAKVTVVDARyDLAKQFSQIDDFIAQGVDLILLNAADSAGIEPAIKRAKD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  99 MGIPVVTLDTdsPDSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGS-LTAMnsLQRIQGFKDAI-KDSEIEIVD 176
Cdd:cd06321   81 AGIIVVAVDV--AAEGADATVTTDNVQAGYLACEYLVEQLGGKGKVAIIDGPpVSAV--IDRVNGCKEALaEYPGIKLVD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 177 ILNDEEDGARAVSLAEAALNAHPDLDAFFGVyayNGPaQA----LVVKNAGKVGkVKIVCFDTTPDILQYVK--EGVIQA 250
Cdd:cd06321  157 DQNGKGSRAGGLSVMTRMLTAHPDVDGVFAI---NDP-GAigalLAAQQAGRDD-IVITSVDGSPEAVAALKreGSPFIA 231
                        250
                 ....*....|....*...
gi 490184078 251 TMGQRPYMMGYLSVTVLY 268
Cdd:cd06321  232 TAAQDPYDMARKAVELAL 249
PBP1_sensor_kinase-like cd06308
periplasmic binding domain of two-component sensor kinase signaling systems; Periplasmic ...
24-251 2.65e-39

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: 139.22  E-value: 2.65e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  24 VIGKSV----HPYWSQVEQGVKA-AGKALGVdtKFFVPQKEDINA-QLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKAL 97
Cdd:cd06308    1 VIGFSQcslnDPWRAAMNEEIKAeAAKYPNV--ELIVTDAQGDAAkQIADIEDLIAQGVDLLIVSPNEADALTPVVKKAY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  98 EMGIPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAI-KDSEIEIVD 176
Cdd:cd06308   79 DAGIPVIVLDRKVSGDDYTAFIGADNVEIGRQAGEYIAELLNGKGNVVEIQGLPGSSPAIDRHKGFLEAIaKYPGIKIVA 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490184078 177 ILNDEEDGARAVSLAEAALNAHPDLDAffgVYAYNGP---AQALVVKNAGKVGKVKIVCFDTTPDIL-QYVKEGVIQAT 251
Cdd:cd06308  159 SQDGDWLRDKAIKVMEDLLQAHPDIDA---VYAHNDEmalGAYQALKKAGREKEIKIIGVDGLPEAGeKAVKDGILAAT 234
PBP1_LsrB_Quorum_Sensing-like cd20001
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
21-270 5.48e-38

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


Pssm-ID: 380656  Cd Length: 296  Bit Score: 136.64  E-value: 5.48e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGK-SVHPYWSQVEQGVKAAGKALGVDTKFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEM 99
Cdd:cd20001    1 TIAVVVKvTGIAWFDRMETGVEQFAKDTGVNVYQIGPATADAAQQVQIIEDLIAQGVDAICVVPNDPEALEPVLKKARDA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTLDTDSPDSGRYVYIGTDNyqAGYTAgLIMKEL---LGGKGKVVIGTGSLTAMNSLQRIQGFKDAIK---DSEIE 173
Cdd:cd20001   81 GIVVITHEASNLKNVDYDVEAFDN--AAYGA-FIMDKLaeaMGGKGKYVTFVGSLTSTSHMEWANAAVAYQKanyPDMLL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 174 IVDILNDEEDGARAVSLAEAALNAHPDLDAFFGVYAYNGPAQALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMG 253
Cdd:cd20001  158 VTDRVETNDDSETAYEKAKELLKTYPDLKGIVGCSSSDVPGAARAVEELGLQGKIAVVGTGLPSVAGEYLEDGTIDYIQF 237
                        250
                 ....*....|....*..
gi 490184078 254 QRPYMMGYLSVTVLYLM 270
Cdd:cd20001  238 WDPADAGYAMNALAVMV 254
PBP1_ABC_rhamnose cd20000
rhamnose ABC transporter substrate-binding protein; Rhamnose ABC transporter substrate-binding ...
21-264 3.41e-37

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: 134.69  E-value: 3.41e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSV-HPYWSQVEQGVKAAGKALGVDTKFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEM 99
Cdd:cd20000    1 RIAFLPKSLgNPYFDAARDGAKEAAKELGGELIFVGPTTATAEAQIPFINTLIQQGVDAIAISANDPDALAPALKKARAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTLDTDSPDSGRYVYIG-TDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSE---IEIV 175
Cdd:cd20000   81 GIKVVTFDSDVAPEARDLFVNqADADGIGRAQVDMMAELIGGEGEFAILSATPTATNQNAWIDAMKKELASPEyagMKLV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 176 DILNDEEDGARAVSLAEAALNAHPDLDaffGVYAYNG---PAQALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATM 252
Cdd:cd20000  161 KVAYGDDDAQKSYQEAEALLQAYPDLK---GIIAPTTvgiAAAARALEDSGLKGKVKVTGLGLPSEMAKYVKDGTVPAFA 237
                        250
                 ....*....|..
gi 490184078 253 GQRPYMMGYLSV 264
Cdd:cd20000  238 LWNPIDLGYLAA 249
PBP1_ABC_sugar_binding-like cd19972
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
32-272 3.60e-37

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: 133.72  E-value: 3.60e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  32 YWSQVEQGVKAAGKALGVDTKFfVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDTDSP 111
Cdd:cd19972   13 FFNQIKQSVEAEAKKKGYKVIT-VDAKGDSATQVNQIQDLITQNIDALIYIPAGATAAAVPVKAARAAGIPVIAVDRNPE 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 112 DSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDS-EIEIVDILNDEEDGARAVSL 190
Cdd:cd19972   92 DAPGDTFIATDSVAAAKELGEWVIKQTGGKGEIAILHGQLGTTPEVDRTKGFQEALAEApGIKVVAEQTADWDQDEGFKV 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 191 AEAALNAHPDLDAFFG---VYAYnGPAQAlvVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRPYMMGYLSV-TV 266
Cdd:cd19972  172 AQDMLQANPNITVFFGqsdAMAL-GAAQA--VKVAGLDHKIWVVGFDGDVAGLKAVKDGVLDATMTQQTQKMGRLAVdSA 248

                 ....*.
gi 490184078 267 LYLMNK 272
Cdd:cd19972  249 IDLLNG 254
PBP1_TmRBP-like cd19967
D-ribose ABC transporter substrate-binding protein such as Thermoanaerobacter tengcongensis ...
31-265 3.91e-37

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


Pssm-ID: 380622 [Multi-domain]  Cd Length: 272  Bit Score: 133.99  E-value: 3.91e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  31 PYWSQVEQGVKAAGKALGVDTKFFVPQkEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDTDS 110
Cdd:cd19967   12 PFFVVEAEGAKEKAKELGYEVTVFDHQ-NDTAKEAELFDTAIASGAKAIILDPADADASIAAVKKAKDAGIPVFLIDREI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 111 PDSGRYV-YIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKD-SEIEIVDILNDEEDGARAV 188
Cdd:cd19967   91 NAEGVAVaQIVSDNYQGAVLLAQYFVKLMGEKGLYVELLGKESDTNAQLRSQGFHSVIDQyPELKMVAQQSADWDRTEAF 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 189 SLAEAALNAHPDLDaffGVYAYN-----GPAQALvvKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRPYMMGYLS 263
Cdd:cd19967  171 EKMESILQANPDIK---GVICGNdemalGAIAAL--KAAGRAGDVIIVGFDGSNDVRDAIKEGKISATVLQPAKLIARLA 245

                 ..
gi 490184078 264 VT 265
Cdd:cd19967  246 VE 247
PBP1_ABC_sugar_binding-like cd19966
monosaccharide ABC transporter substrate binding protein CUT2 family and simialr proteins; ...
31-274 2.02e-34

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: 126.67  E-value: 2.02e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  31 PYWSQVEQGVKAAGKALGVDTKFFVPqKEDINAQLQMLESFIAEGVNGIAIAPSDPT-AVIPTIKKALEMGIPVVTLDTD 109
Cdd:cd19966   13 PFWTVVYNGAKDAAADLGVDLDYVFS-SWDPEKMVEQFKEAIAAKPDGIAIMGHPGDgAYTPLIEAAKKAGIIVTSFNTD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 110 SPD----SGRYVYIGTDNYQAGYTAGlimKELLGGKGkvvIGTGSLTAMNSL--------QRIQGFKDAIKDSEI--EIV 175
Cdd:cd19966   92 LPKleygDCGLGYVGADLYAAGYTLA---KELVKRGG---LKTGDRVFVPGLlpgqpyrvLRTKGVIDALKEAGIkvDYL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 176 DILNDEEDGARAVSLAEAALNAHPDLDAFFGVYAYNGPAQALVVKNAG-KVGKVKIVCFDTTPDILQYVKEGVIQATMGQ 254
Cdd:cd19966  166 EISLEPNKPAEGIPVMTGYLAANPDVKAIVGDGGGLTANVAKYLKAAGkKPGEIPVAGFDLSPATVQAIKSGYVNATIDQ 245
                        250       260
                 ....*....|....*....|
gi 490184078 255 RPYMMGYLSVTVLYLMNKIG 274
Cdd:cd19966  246 QPYLQGYLPVLQIYLTKKYG 265
PBP1_rhizopine_binding-like cd06301
periplasmic binding proteins specific to rhizopines; Periplasmic binding proteins specific to ...
34-272 6.15e-34

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: 125.42  E-value: 6.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  34 SQVEQGVKAAGKA-LGVDTKFfVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDTDSPD 112
Cdd:cd06301   16 TYLRDAIEAYAKEyPGVKLVI-VDAQSDAAKQLSQVENFIAQGVDAIIVNPVDTDASAPAVDAAADAGIPLVYVNREPDS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 113 SGRY-VYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSE-IEIVDILNDEEDGARAVSL 190
Cdd:cd06301   95 KPKGvAFVGSDDIESGELQMEYLAKLLGGKGNIAILDGVLGHEAQILRTEGNKDVLAKYPgMKIVAEQTANWSREKAMDI 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 191 AEAALNAHPDLDAffgVYAYN-----GPAQALvvKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRPYMMGYLSVT 265
Cdd:cd06301  175 VENWLQSGDKIDA---IVANNdemaiGAILAL--EAAGKKDDILVAGIDATPDALKAMKAGRLDATVFQDAAGQGETAVD 249

                 ....*..
gi 490184078 266 VLYLMNK 272
Cdd:cd06301  250 VAVKAAK 256
PBP1_TorT-like cd06306
TorT-like proteins, a periplasmic binding protein family that activates induction of the Tor ...
31-264 5.03e-33

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: 122.69  E-value: 5.03e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  31 PYWSQVEQGVKAAGKALGVDTKFFVPQK-EDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTL--D 107
Cdd:cd06306   12 SYWVGVNYGIVDEAKRLGVKLTVYEAGGyTNLSKQISQLEDCVASGADAILLGAISFDGLDPKVAEAAAAGIPVIDLvnG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 108 TDSPD-SGRyvyIGTDNYQAGYTAGLIMKELL-GGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSEIEIVDILNDEEDGA 185
Cdd:cd06306   92 IDSPKvAAR---VLVDFYDMGYLAGEYLVEHHpGKPVKVAWFPGPAGAGWAEDREKGFKEALAGSNVEIVATKYGDTGKA 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490184078 186 RAVSLAEAALNAHPDLDAFFGVyAYNGPAQALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRPYMMGYLSV 264
Cdd:cd06306  169 VQLNLVEDALQAHPDIDYIVGN-AVAAEAAVGALREAGLTGKVKVVSTYLTPGVYRGIKRGKILAAPSDQPVLQGRIAV 246
PBP1_ABC_D-talitol-like cd06318
periplasmic D-talitol-binding protein of an ABC transport system and similar proteins; ...
24-306 3.09e-32

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: 120.98  E-value: 3.09e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  24 VIGKS----VHPYWSQVEQGVKAAGKALGVDTkFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEM 99
Cdd:cd06318    1 KIGFSqrtlASPYYAALVAAAKAEAKKLGVEL-VVTDAQNDLTKQISDVEDLITRGVDVLILNPVDPEGLTPAVKAAKAA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTLDTDSPDSGRYV-YIGTDNYQAGYTAGLIMKELLGGK-GKVVIGTGSLTAMNSLQRIQGFKDAI--------KD 169
Cdd:cd06318   80 GIPVITVDSALDPSANVAtQVGRDNKQNGVLVGKEAAKALGGDpGKIIELSGDKGNEVSRDRRDGFLAGVneyqlrkyGK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 170 SEIEIVDILNDEEDGARAVSLAEAALNAHPDLDaffGVYAYN-----GPAQALvvKNAGKVGKVKIVCFDTTPDILQYVK 244
Cdd:cd06318  160 SNIKVVAQPYGNWIRSGAVAAMEDLLQAHPDIN---VVYAENddmalGAMKAL--KAAGMLDKVKVAGADGQKEALKLIK 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490184078 245 EGVIQATMGQRPYMMGYLSVTVLylmnkigvqntlmmLPKVKVDGKVDYVIDTGVDVVTPEN 306
Cdd:cd06318  235 DGKYVATGLNDPDLLGKTAVDTA--------------AKVVKGEESFPEFTYTPTALITKDN 282
PBP1_ABC_sugar_binding-like cd19973
monosaccharide ABC transporter substrate-binding protein; Periplasmic sugar-binding domain of ...
21-303 3.83e-32

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: 121.04  E-value: 3.83e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKS-VHPYWSQVEQGVKAAGKALGVDTKFFVPQKEDINA-QLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALE 98
Cdd:cd19973    1 TIGLITKTdTNPFFVKMKEGAQKAAKALGIKLMTAAGKIDGDNAtQVTAIENMIAAGAKGILITPSDTKAIVPAVKKARD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  99 MGIPVVTLDT--DSPDSGRYVYiGTDNYQAGYTAGLIMKELLGGKgKVVIGTGSLTAMNSL--QRIQGF--------KDA 166
Cdd:cd19973   81 AGVLVIALDTptDPIDAADATF-ATDNFKAGVLIGEWAKAALGAK-DAKIATLDLTPGHTVgvLRHQGFlkgfgideKDP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 167 IK-----DSEIEIVDILNDEEDGARAVslAEAALNAHPDLDAffgVYAYNGPA-----QALvvKNAGKVGKVKIVCFDTT 236
Cdd:cd19973  159 ESnededDSQVVGSADTNGDQAKGQTA--MENLLQKDPDINL---VYTINEPAaagayQAL--KAAGKEKGVLIVSVDGG 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490184078 237 PDILQYVKEGVIQATMGQRPYMMGYLSVTVLYLMNKIGVQntlmmlpkvkvdgKVDYVIDTGVDVVT 303
Cdd:cd19973  232 CPGVKDVKDGIIGATSQQYPLRMAALGVEAIAAFAKTGGT-------------KGSGFTDTGVTLVT 285
PBP1_galactofuranose_YtfQ-like cd06309
periplasmic binding domain of ABC-type galactofuranose YtfQ-like transport systems; ...
38-251 4.70e-32

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: 120.79  E-value: 4.70e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  38 QGVKAAGKALGVDTKFFVPQkEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLD--TDSPDSGR 115
Cdd:cd06309   19 KSIKEAAKKRGYELVYTDAN-QDQEKQINDIRDLIAQGVDAILISPIDATGWDPVLKEAKDAGIPVILVDrtIDGEDGSL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 116 YV-YIGTDNYQAGYTAGLIM-KELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIK-DSEIEIVDILNDEEDGARAVSLAE 192
Cdd:cd06309   98 YVtFIGSDFVEEGRRAAEWLvKNYKGGKGNVVELQGTAGSSVAIDRSKGFREVIKkHPNIKIVASQSGNFTREKGQKVME 177
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490184078 193 AALNAHP-DLDAffgVYAYN-----GPAQALvvKNAGKV--GKVKIVCFDTTPDILQYVKEGVIQAT 251
Cdd:cd06309  178 NLLQAGPgDIDV---IYAHNddmalGAIQAL--KEAGLKpgKDVLVVGIDGQKDALEAIKAGELNAT 239
PBP1_ABC_IbpA-like cd19968
periplasmic sugar-binding protein IbpA of an ABC transporter and similar proteins; The ...
24-273 2.97e-30

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: 115.56  E-value: 2.97e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  24 VIGKSVH----PYWSQVEQGVKAAGKALGVDTKFFVPQkEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEM 99
Cdd:cd19968    1 KIGFSFPnlsfPFFVYMHEQAVDEAAKLGVKLVVLDAQ-NSSSKQASDLENAIAQGVDGIIVSPIDVKALVPAIEAAIKA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSE-IEIVDIL 178
Cdd:cd19968   80 GIPVVTVDRRAEGAAPVPHVGADNVAGGREVAKFVVDKLPNGAKVIELTGTPGSSPAIDRTKGFHEELAAGPkIKVVFEQ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 179 NDEEDGARAVSLAEAALNAHP-DLDAffgVYAYN-----GPAQAlvVKNAG-KVGKVKIVCFDTTPDILQYVKEGVIQAT 251
Cdd:cd19968  160 TGNFERDEGLTVMENILTSLPgPPDA---IICANddmalGAIEA--MRAAGlDLKKVKVIGFDAVPDALQAIKDGELYAT 234
                        250       260
                 ....*....|....*....|...
gi 490184078 252 MGQRPymmGYLSVTVL-YLMNKI 273
Cdd:cd19968  235 VEQPP---GGQARTALrILVDYL 254
PRK09701 PRK09701
D-allose transporter substrate-binding protein;
31-286 5.69e-29

D-allose transporter substrate-binding protein;


Pssm-ID: 182037 [Multi-domain]  Cd Length: 311  Bit Score: 113.04  E-value: 5.69e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  31 PYWSQVEQGVKAAGKALGVDTKFFV-PQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDT- 108
Cdd:PRK09701  37 PFWVDMKKGIEDEAKTLGVSVDIFAsPSEGDFQSQLQLFEDLSNKNYKGIAFAPLSSVNLVMPVARAWKKGIYLVNLDEk 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 109 ----DSPDSGRYV--YIGTDNYQAGYT-AGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDA-IKDSEIEIVDILND 180
Cdd:PRK09701 117 idmdNLKKAGGNVeaFVTTDNVAVGAKgASFIIDKLGAEGGEVAIIEGKAGNASGEARRNGATEAfKKASQIKLVASQPA 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 181 EEDGARAVSLAEAALNAHPDLDAFfgvYAYN-----GPAQAlvVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQR 255
Cdd:PRK09701 197 DWDRIKALDVATNVLQRNPNIKAI---YCANdtmamGVAQA--VANAGKTGKVLVVGTDGIPEARKMVEAGQMTATVAQN 271
                        250       260       270
                 ....*....|....*....|....*....|.
gi 490184078 256 PYMMGYLSVTVLYLMNKIGVQNTLMMLPKVK 286
Cdd:PRK09701 272 PADIGATGLKLMVDAEKSGKVIPLDKAPEFK 302
PBP1_ABC_ThpA_XypA cd06313
periplasmic sugar-binding proteins (ThpA and XypA) of ABC-type transport systems; This group ...
38-311 6.22e-28

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


Pssm-ID: 380536 [Multi-domain]  Cd Length: 277  Bit Score: 109.67  E-value: 6.22e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  38 QGVKAAGKALGVDTKFFVPQkEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDTDSPDSGRYV 117
Cdd:cd06313   19 EAMKAVAKELNVDLVVLDGN-GDVSTQINQVDTLIAQGVDAIIVVPVDADALAPAVEKAKEAGIPLVGVNALIENEDLTA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 118 YIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAI-KDSEIEIVDILNDEEDGARAVSLAEAALN 196
Cdd:cd06313   98 YVGSDDVVAGELEGQAVADRLGGKGNVVILEGPIGQSAQIDRGKGIENVLkKYPDIKVLAEQTANWSRDEAMSLMENWLQ 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 197 AHPD-LDaffGVYAYN-----GPAQAlvVKNAGKvGKVKIVCFDTTPDILQYVKEGVIQATMGQRPYMMGYLSVTVLYLM 270
Cdd:cd06313  178 AYGDeID---GIIAQNddmalGALQA--VKAAGR-DDIPVVGIDGIEDALQAVKSGELIATVLQDAEAQGKGAVEVAVDA 251
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 490184078 271 NKIGvqntlmmlpKVKVDGKVDYVidtgvdVVTPENLDEYL 311
Cdd:cd06313  252 VKGE---------GVEKKYYIPFV------LVTKDNVDDYL 277
PRK15408 PRK15408
autoinducer 2 ABC transporter substrate-binding protein LsrB;
38-319 3.38e-25

autoinducer 2 ABC transporter substrate-binding protein LsrB;


Pssm-ID: 237961  Cd Length: 336  Bit Score: 103.34  E-value: 3.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  38 QGVKAAGKALGVDTKFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDTDSPDSGRYV 117
Cdd:PRK15408  43 NGAKEAGKELGVDVTYDGPTEPSVSGQVQLINNFVNQGYNAIIVSAVSPDGLCPALKRAMQRGVKVLTWDSDTKPECRSY 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 118 YI--GTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDS--EIEIVDILNDEEDGARAVSLAEA 193
Cdd:PRK15408 123 YInqGTPEQLGSMLVEMAAKQVGKDKAKVAFFYSSPTVTDQNQWVKEAKAKIAKEhpGWEIVTTQFGYNDATKSLQTAEG 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 194 ALNAHPDLDAFFGVYAYNGPAQALVVKNAgKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRPYMMGYLSVTvlylmnki 273
Cdd:PRK15408 203 ILKAYPDLDAIIAPDANALPAAAQAAENL-KRDKVAIVGFSTPNVMRPYVKRGTVKEFGLWDVVQQGKISVY-------- 273
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 490184078 274 gVQNTLMMLPKVKVDGKVDyVIDTGVDVVTPENLDEYLKKMEELGI 319
Cdd:PRK15408 274 -VANELLKKGKLNVGDSLD-VPGIGKVEVSPNSVQGYDYEAKGNGI 317
PBP1_methylthioribose_binding-like cd06305
similar to methylthioribose-binding protein of ABC-type transport systems that belong to a ...
21-264 3.89e-25

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: 101.99  E-value: 3.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGK-SVHPYWSQVEQGVKAAGKALGVDTKFFVPQKEDiNAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEM 99
Cdd:cd06305    1 TIAVVRNgTSGDWDQQALQGAVAEAEKLGGTVIVFDANGDD-ARMADQIQQAITQKVDAIIISHGDADALDPKLKKALDA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTLDTDSPDSGrYVYIGTDNYQAGYTAGLIMKELLGGKGKV-VIGTGSLTAMNSLQRI-QGFKDAIKDSEIeIVDI 177
Cdd:cd06305   80 GIPVVTFDTDSQVPG-VNNITQDDYALGTLSLGQLVKDLNGEGNIaVFNVFGVPPLDKRYDIyKAVLKANPGIKK-IVAE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 178 LNDEEDGARAVSLA--EAALNAHPD--LDAFFGvyAYNGPA----QALvvKNAGKvGKVKIVCFDTTPDILQYVKE--GV 247
Cdd:cd06305  158 LGDVTPNTAADAQTqvEALLKKYPEggIDAIWA--AWDEPAkgavQAL--EEAGR-TDIKVYGVDISNQDLELMADegSP 232
                        250
                 ....*....|....*..
gi 490184078 248 IQATMGQRPYMMGYLSV 264
Cdd:cd06305  233 WVATAAQDPALIGTVAV 249
PBP1_LsrB_Quorum_Sensing-like cd20002
ligand-binding protein LsrB-like of ABC transporter periplasmic binding protein; ...
21-308 4.69e-25

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: 102.01  E-value: 4.69e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSVH-PYWSQVEQGVKAAGKALGVDTKFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEM 99
Cdd:cd20002    1 TIVTVVKLAGiPWFNRMEQGVKKAGKEFGVNAYQVGPADADPAQQVRIIEDLIAQGVDAILVVPNDAKVLEPVFKKAREK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTldTDSPDSGRYVY----IGTDNYqagytAGLIMKEL---LGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSE- 171
Cdd:cd20002   81 GIVVIT--HESPGQKGADWdvelIDNEKF-----GEAQMELLakeMGGKGEYAIFVGSLTVPLHNLWADAAVEYQKEKYp 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 172 --IEIVDILNDEEDGARAVSLAEAALNAHPDLDAFFGVYAYNGPAQALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQ 249
Cdd:cd20002  154 nmKQVTDRIPGGEDVDVSRQTTLELLKAYPDLKGIISFGSLGPIGAGQALREKGLKGKVAVVGTVIPSQAAAYLKEGSIT 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490184078 250 ATMGQRPYMMGYLSVTVL-YLMN----KIGVQNTLMMLPKVKVDGKVdyVIDTGVDVVTPENLD 308
Cdd:cd20002  234 EGYLWDPADAGYAMVYIAkMLLDgkrkEIGDGFEIPGKGTPDIDGNV--IIFDAPLEITKENAD 295
PBP1_ABC_sugar_binding-like cd06324
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; This group ...
21-320 1.20e-24

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


Pssm-ID: 380547 [Multi-domain]  Cd Length: 317  Bit Score: 101.53  E-value: 1.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVI--GKSVHPYWSQVEQGVKAAGKALGVDTKFFvpqkediNAQ---LQMLESfiaegVNGIAIAPSDPTAVI----- 90
Cdd:cd06324    1 RVVFInpGKEDEPFWQNVTRFMQAAAKDLGIELEVL-------YANrnrFKMLEL-----AEELLARPPKPDYLIlvnek 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  91 ----PTIKKALEMGIPVVTLDTDSPDS---------GRYVY----IGTDNYQAGYtagLIMKELL--------GGKGKVV 145
Cdd:cd06324   69 gvapELLELAEQAKIPVFLINNDLTDEerallgkprEKFKYwlgsIVPDNEQAGY---LLAKALIkaarkksdDGKIRVL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 146 IGTGSLTAMNSLQRIQGFKDAIKD-SEIEIVDILNDEEDGARAVSLAEAALNAHPDLDaffGVYAYN-----GPAQALvv 219
Cdd:cd06324  146 AISGDKSTPASILREQGLRDALAEhPDVTLLQIVYANWSEDEAYQKTEKLLQRYPDID---IVWAANdamalGAIDAL-- 220
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 220 KNAGKV-GK-VKIVCFDTTPDILQYVKEGVIQATMGqRPYMMGYLSVTVLYlmnkigvqntlmmlpkvKVDGKVDYVIDT 297
Cdd:cd06324  221 EEAGLKpGKdVLVGGIDWSPEALQAVKDGELTASVG-GHFLEGAWALVLLY-----------------DYHHGIDFAAGT 282
                        330       340
                 ....*....|....*....|....*...
gi 490184078 298 GV-----DVVTPENLDEYLKKMEELGIP 320
Cdd:cd06324  283 SVqlkpmLAITRDNVAQYLKLFGDDNWP 310
PBP1_ABC_sugar_binding-like cd19999
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
21-245 1.32e-23

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: 98.53  E-value: 1.32e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSVHPYW-SQVEQGVKAAGKAL---GVDTKFFVPQKE-DINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKK 95
Cdd:cd19999    1 VIGVSNGYVGNEWrAQMIADFEEVAAEYkeeGVISDLIVQNADaDATGQISQIRNMINEGVDAILIDPVSATALNPVIEK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  96 ALEMGIPVVTLDT--DSPDSgryVYIGTDNYQ--AGYTAGLImkELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKD-S 170
Cdd:cd19999   81 AQAAGILVVSFDQpvSSPDA---INVVIDQYKwaAIQAQWLA--EQLGGKGNIVAINGVAGNPANEARVKAADDVFAKyP 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490184078 171 EIEIVDILNDEEDGARAVSLAEAALNAHPDLDaffGVYAYNGPAQALV--VKNAGKvgKVKIVCFDTTPDILQYVKE 245
Cdd:cd19999  156 GIKVLASVPGGWDQATAQQVMATLLATYPDID---GVLTQDGMAEGVLraFQAAGK--DPPVMTGDYRKGFLRKWKE 227
PBP1_ABC_sugar_binding-like cd19996
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
59-224 3.65e-23

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: 96.93  E-value: 3.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  59 EDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDtDSPDSGRYV-YIGTDNYQAGYTAGLIMKEL 137
Cdd:cd19996   42 GDTQKQIADIQDLIAQGVDAIIVSPNSPTALLPAIEKAAAAGIPVVLFD-SGVGSDKYTaFVGVDDAAFGRVGAEWLVKQ 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 138 LGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKD-SEIEIVDILNDEEDGARAVSLAEAALNAHPDLDAFFGVYAYNGPAQA 216
Cdd:cd19996  121 LGGKGNIIALRGIAGVSVSEDRWAGAKEVFKEyPGIKIVGEVYADWDYAKAKQAVESLLAAYPDIDGVWSDGGAMTLGAI 200

                 ....*...
gi 490184078 217 LVVKNAGK 224
Cdd:cd19996  201 EAFEEAGR 208
PBP1_ABC_sugar_binding-like cd06300
periplasmic sugar-binding component of uncharacterized ABC-type transport systems that are ...
59-245 5.37e-23

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: 96.62  E-value: 5.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  59 EDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLD--TDSPdsgrYVYIGTDNY-QAGYTAGLIMK 135
Cdd:cd06300   44 GDATEQIAQIRNLIDQGVDAIIINPSSPTALNAVIEQAADAGIPVVAFDgaVTSP----DAYNVSNDQvEWGRLGAKWLF 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 136 ELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDS-EIEIVDILNDEEDGARAVSLAEAALNAHPDLDaffGVYAYNGPA 214
Cdd:cd06300  120 EALGGKGNVLVVRGIAGAPASADRHAGVKEALAEYpGIKVVGEVFGGWDEATAQTAMLDFLATHPQVD---GVWTQGGED 196
                        170       180       190
                 ....*....|....*....|....*....|...
gi 490184078 215 QALV--VKNAGKVgKVKIVCFDTTPDILQYVKE 245
Cdd:cd06300  197 TGVLqaFQQAGRP-PVPIVGGDENGFAKQWWKH 228
PurR COG1609
DNA-binding transcriptional regulator, LacI/PurR family [Transcription];
21-267 4.14e-22

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


Pssm-ID: 441217 [Multi-domain]  Cd Length: 335  Bit Score: 94.88  E-value: 4.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSV-HPYWSQVEQGVKAAGKALGVDTkFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAviPTIKKALEM 99
Cdd:COG1609   63 TIGVVVPDLsNPFFAELLRGIEEAARERGYQL-LLANSDEDPEREREALRLLLSRRVDGLILAGSRLDD--ARLERLAEA 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTLDTDSPDSGrYVYIGTDNYQAGYTAgliMKELLgGKGKVVIG--TGSLTAMNSLQRIQGFKDAIKDSEIEIVDI 177
Cdd:COG1609  140 GIPVVLIDRPLPDPG-VPSVGVDNRAGARLA---TEHLI-ELGHRRIAfiGGPADSSSARERLAGYREALAEAGLPPDPE 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 178 L-----NDEEDGARAvslAEAALNAHPDLDAFF--------GVYayngpaQALvvKNAG-KVGK-VKIVCFDTTPdILQY 242
Cdd:COG1609  215 LvvegdFSAESGYEA---ARRLLARGPRPTAIFcandlmalGAL------RAL--REAGlRVPEdVSVVGFDDIP-LARY 282
                        250       260
                 ....*....|....*....|....*
gi 490184078 243 VKEGViqATMGQRPYMMGYLSVTVL 267
Cdd:COG1609  283 LTPPL--TTVRQPIEEMGRRAAELL 305
PBP1_ABC_sugar_binding-like cd06316
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
33-313 1.06e-21

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


Pssm-ID: 380539 [Multi-domain]  Cd Length: 294  Bit Score: 93.07  E-value: 1.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  33 WSQ-VEQGVKAAGKALGV------DTKFfvpqkeDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVT 105
Cdd:cd06316   13 WSRlQVAGIKDTFEELGIevvavtDANF------DPAKQITDLETLIALKPDIIISIPVDPVATAAAYKKVADAGIKLVF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 106 LDTdSPD----SGRYV-YIGTDNYQAGYTAGLIMKELLGGKGKV-VIGTGS-LTAMNslQRIQGFKDAIKDS--EIEIVD 176
Cdd:cd06316   87 MDN-VPDgleaGKDYVsVVSSDNRGNGQIAAELLAEAIGGKGKVgIIYHDAdFYATN--QRDKAFKDTLKEKypDIKIVA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 177 IlNDEEDGARAVSLAEAALNAHPDLDAFFGVYAynGPAQALV--VKNAGKvGKVKIVCFDTTPDILQY-VKEGVIQATMG 253
Cdd:cd06316  164 E-QGFADPNDAEEVASAMLTANPDIDGIYVSWD--TPALGVIsaLRAAGR-SDIKITTVDLGTEIALDmAKGGNVKGIGA 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490184078 254 QRPYMMGYLS--VTVLYLMNKigvqntlMMLPKVKVDGKvdyvidtgvdVVTPENLDEYLKK 313
Cdd:cd06316  240 QRPYDQGVAEalAAALALLGK-------EVPPFIGVPPL----------AVTKDNLLEAWKQ 284
PBP1_LacI_sugar_binding-like cd06267
ligand binding domain of the LacI transcriptional regulator family belonging to the type 1 ...
21-283 3.93e-21

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: 90.65  E-value: 3.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVI-GKSVHPYWSQVEQGVKAAGKALGVDTkFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAviPTIKKALEM 99
Cdd:cd06267    1 TIGLIvPDISNPFFAELLRGIEDAARERGYSL-LLCNTDEDPEREREYLRLLLSRRVDGIILAPSSLDD--ELLEELLAA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTLDTDSPDSGRYvYIGTDNYQAGYTAgliMKELLG-GKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSEIEIVDIL 178
Cdd:cd06267   78 GIPVVLIDRRLDGLGVD-SVVVDNYAGAYLA---TEHLIElGHRRIAFIGGPLDLSTSRERLEGYRDALAEAGLPVDPEL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 179 -----NDEEDGARAvslAEAALNAHPDLDAFF--------GVYayngpaQALvvKNAG-KVGK-VKIVCFD-------TT 236
Cdd:cd06267  154 vvegdFSEESGYEA---ARELLALPPRPTAIFaandlmaiGAL------RAL--RELGlRVPEdISVVGFDdiplaalLT 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 490184078 237 PDIlqyvkegviqATMGQRPYMMGYLSVTVLY-LMNKIGVQNTLMMLP 283
Cdd:cd06267  223 PPL----------TTVRQPAYEMGRAAAELLLeRIEGEEEPPRRIVLP 260
PBP1_Qymf-like cd06291
ligand binding domain of the lacI-like transcription regulator from a novel metal-reducing ...
21-283 1.99e-19

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


Pssm-ID: 380514 [Multi-domain]  Cd Length: 264  Bit Score: 86.03  E-value: 1.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSV-HPYWSQVEQGVKAAGKALGVDTkFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSdptavIPTIKKALEM 99
Cdd:cd06291    1 TIGLIVPDIsNPFFAELAKYIEKELFKKGYKM-ILCNSNEDEEKEKEYLEMLKRNKVDGIILGSH-----SLDIEEYKKL 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTLDTDSPDSgrYVYIGTDNYQAGYTAGlimKELLG-GKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSEIEIVDIL 178
Cdd:cd06291   75 NIPIVSIDRYLSEG--IPSVSSDNYQGGRLAA---EHLIEkGCKKILHIGGPSNNSPANERYRGFEDALKEAGIEYEIIE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 179 NDEEDG--ARAVSLAEAALNAHPDLDAFFgvyAYNGPAQALVVKNAGKVGK-----VKIVCFDTTPdILQYVKEGViqAT 251
Cdd:cd06291  150 IDENDFseEDAYELAKELLEKYPDIDGIF---ASNDLLAIGVLKALQKLGIrvpedVQIIGFDGIE-ISELLYPEL--TT 223
                        250       260       270
                 ....*....|....*....|....*....|...
gi 490184078 252 MGQRPYMMGYLSVTVLY-LMNKIGVQNTLMMLP 283
Cdd:cd06291  224 IRQPIEEMAKEAVELLLkLIEGEEIEESRIVLP 256
PBP1_ABC_xylose_binding-like cd19992
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
22-264 3.36e-19

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


Pssm-ID: 380647 [Multi-domain]  Cd Length: 284  Bit Score: 85.71  E-value: 3.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  22 IGV-IGKSVHPYWSQVEQGVKAAGKALGVDTKFFVPQkEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMG 100
Cdd:cd19992    2 IGVsFPTQQEERWQKDKEYMEEEAKELGVELIFQVAD-NDAKTQASQVENLLAQGIDVLIIAPVDAGAAANIVDKAKAAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 101 IPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKElLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKD----SEIEIV- 175
Cdd:cd19992   81 VPVISYDRLILNADVDLYVGRDNYKVGQLQAEYALE-AVPKGNYVILSGDPGDNNAQLITAGAMDVLQPaidsGDIKIVl 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 176 DILNDEEDGARAVSLAEAALNA-HPDLDAFFgvyAYN-----GPAQALvvKNAGKVGKVKIVCFDTTPDILQYVKEGVIQ 249
Cdd:cd19992  160 DQYVKGWSPDEAMKLVENALTAnNNNIDAVL---APNdgmagGAIQAL--KAQGLAGKVFVTGQDAELAALKRIVEGTQT 234
                        250
                 ....*....|....*
gi 490184078 250 ATMGQRPYMMGYLSV 264
Cdd:cd19992  235 MTVWKDLKELARAAA 249
PRK10936 PRK10936
TMAO reductase system periplasmic protein TorT; Provisional
32-272 7.77e-19

TMAO reductase system periplasmic protein TorT; Provisional


Pssm-ID: 236801 [Multi-domain]  Cd Length: 343  Bit Score: 85.77  E-value: 7.77e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  32 YWSQVEQGVKAAGKALGVDTKFFvpqkE-----DINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKAlEMGIPVVTL 106
Cdd:PRK10936  60 YWLSVNYGMVEEAKRLGVDLKVL----EaggyyNLAKQQQQLEQCVAWGADAILLGAVTPDGLNPDLELQ-AANIPVIAL 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 107 --DTDSPD-SGRyvyIGTDNYQAGYTAGLIMKELL-GGKGKVVIG--TGSLTAMNSLQRIQGFKDAIKDSEIEIVDIL-- 178
Cdd:PRK10936 135 vnGIDSPQvTTR---VGVSWYQMGYQAGRYLAQWHpKGSKPLNVAllPGPEGAGGSKAVEQGFRAAIAGSDVRIVDIAyg 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 179 -NDEEDGARavsLAEAALNAHPDLDAFFGvyayNGPA---QALVVKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQ 254
Cdd:PRK10936 212 dNDKELQRN---LLQELLERHPDIDYIAG----SAVAaeaAIGELRGRNLTDKIKLVSFYLSHQVYRGLKRGKVLAAPSD 284
                        250       260
                 ....*....|....*....|
gi 490184078 255 RPYMMGYLSV--TVLYLMNK 272
Cdd:PRK10936 285 QMVLQGRLAIdqAVRQLEGA 304
PBP1_ABC_sugar_binding-like cd06311
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
32-205 8.39e-19

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: 84.34  E-value: 8.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  32 YWSQveqgvKAAGKALGVDTKFFVPqkEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDTDSP 111
Cdd:cd06311   19 YYAE-----KQAKELADLEYKLVTS--SNANEQVSQLEDLIAQKVDAIVILPQDSEELTVAAQKAKDAGIPVVNFDRGLN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 112 DSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDS-EIEIVDILNDEEDGARAVSL 190
Cdd:cd06311   92 VLIYDLYVAGDNPGMGVVSAEYIGKKLGGKGNVVVLEVPSSGSVNEERVAGFKEVIKGNpGIKILAMQAGDWTREDGLKV 171
                        170
                 ....*....|....*
gi 490184078 191 AEAALNAHPDLDAFF 205
Cdd:cd06311  172 AQDILTKNKKIDAVW 186
PRK10653 PRK10653
ribose ABC transporter substrate-binding protein RbsB;
56-264 2.08e-18

ribose ABC transporter substrate-binding protein RbsB;


Pssm-ID: 182620 [Multi-domain]  Cd Length: 295  Bit Score: 83.60  E-value: 2.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  56 PQKEdinaqLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDTDSpDSGRYV-YIGTDNYQAGYTAGLIM 134
Cdd:PRK10653  68 PAKE-----LANVQDLTVRGTKILLINPTDSDAVGNAVKMANQANIPVITLDRGA-TKGEVVsHIASDNVAGGKMAGDFI 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 135 KELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSEIEIVDILNDEEDGARAVSLAEAALNAHPDLDAffgVYAYN--- 211
Cdd:PRK10653 142 AKKLGEGAKVIQLEGIAGTSAARERGEGFKQAVAAHKFNVLASQPADFDRTKGLNVMQNLLTAHPDVQA---VFAQNdem 218
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 490184078 212 --GPAQALvvKNAGKvGKVKIVCFDTTPDILQYVKEGVIQATMGQRPYMMGYLSV 264
Cdd:PRK10653 219 alGALRAL--QTAGK-SDVMVVGFDGTPDGIKAVNRGKLAATIAQQPDQIGAIGV 270
PBP1_LacI-like cd06280
ligand-binding domain of an uncharacterized transcription regulator from Staphylococcus ...
21-239 3.18e-17

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


Pssm-ID: 380503 [Multi-domain]  Cd Length: 266  Bit Score: 80.00  E-value: 3.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVI-GKSVHPYWSQVEQGVKAAGKALGVDTkFFVPQKEDINAQLQMLESFIAEGVNGIAIAPS-DPTaviPTIKKALE 98
Cdd:cd06280    1 TIGLIvPDITNPFFTTIARGIEDAAEKHGYQV-ILANTDEDPEKEKRYLDSLLSKQVDGIILAPSaGPS---RELKRLLK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  99 MGIPVVTLDTDSPDSGRYVyIGTDNYQAGYTAgliMKELLG-GKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSEIEIVDI 177
Cdd:cd06280   77 HGIPIVLIDREVEGLELDL-VAGDNREGAYKA---VKHLIElGHRRIGLITGPLEISTTRERLAGYREALAEAGIPVDES 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490184078 178 L-----NDEEDGARAVslaEAALNAHPDLDAFFGV--YAYNGPAQALvvKNAGKVGK--VKIVCFDTTPDI 239
Cdd:cd06280  153 LifegdSTIEGGYEAV---KALLDLPPRPTAIFATnnLMAVGALRAL--RERGLEIPqdISVVGFDDSDWF 218
PBP1_ABC_sugar_binding-like cd19998
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
34-224 8.46e-17

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: 79.25  E-value: 8.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  34 SQVEQGVKAAGKALGVDTK--FFVPQKE-DINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDT-- 108
Cdd:cd19998   15 QEMINIAKAAAKQPPYADKveLKVVSSGtDVQAQISAIDNMIAAGYDAILIYAISPTALNPVIKRACDAGIVVVAFDNvv 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 109 DSPDsgryVY-IGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDS-EIEIVDILNDEEDGAR 186
Cdd:cd19998   95 DEPC----AYnVNTDQAKAGEQTAQWLVDKLGGKGNILMVRGVPGTSVDRDRYEGAKEVFKKYpDIKVVAEYYGNWDDGT 170
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 490184078 187 AVSLAEAALNAHPDLDAFFGVYAYNGPAQALvvKNAGK 224
Cdd:cd19998  171 AQKAVADALAAHPDVDGVWTQGGETGVIKAL--QAAGH 206
PBP1_EndR-like cd19977
periplasmic ligand-binding domain of putative repressor of the endoglucanase operon and its ...
21-237 5.09e-16

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


Pssm-ID: 380632 [Multi-domain]  Cd Length: 264  Bit Score: 76.41  E-value: 5.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSV-HPYWSQVEQGVKAAGKALGVDTKF----FVPQKEdinaqLQMLESFIAEGVNGIAIAPSDPTAviPTIKK 95
Cdd:cd19977    1 TIGLIVADIlNPFFTSVVRGIEDEAYKNGYHVILcntdEDPEKE-----KKYIEMLRAKQVDGIIIAPTGGNE--DLIEK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  96 ALEMGIPVVTLDTDSPDSGrYVYIGTDNYQAGYTAgliMKELLG-GKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSEI-- 172
Cdd:cd19977   74 LVKSGIPVVFVDRYIPGLD-VDTVVVDNFKGAYQA---TEHLIElGHKRIAFITYPLELSTRQERLEGYKAALADHGLpv 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490184078 173 --EIVDILNDEEDGARAVSlaeAALNAHPDLDAFFgvYAYNGPAQALV--VKNAGKV--GKVKIVCFDTTP 237
Cdd:cd19977  150 deELIKHVDRQDDVRKAIS---ELLKLEKPPDAIF--AANNLITLEVLkaIKELGLRipDDIALIGFDDIP 215
PBP1_ABC_sugar_binding-like cd19997
monosaccharide ABC transporter substrate binding protein such as CUT2; Periplasmic ...
35-319 2.00e-15

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


Pssm-ID: 380652 [Multi-domain]  Cd Length: 305  Bit Score: 75.40  E-value: 2.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  35 QVEQGVKAAGKAL---GVDTKF-FVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLD--T 108
Cdd:cd19997   16 QMVDAFEEAAKKAkadGLIADYiVVNADGSATTQISQIQNLILQGVDAIVIDAASPTALNGAIQQACDAGIKVVVFDsgV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 109 DSPDsgryVYIGTDNYQ--AGYTAGLIMkELLGGKGKV-----VIGTGSLTAMNslqriQGFKDAIKDSE-IEIVDILND 180
Cdd:cd19997   96 TEPC----AYILNNDFEdyGAASVEYVA-DRLGGKGNVlevrgVAGTSPDEEIY-----AGQVEALKKYPdLKVVAEVYG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 181 EEDGARAVSLAEAALNAHPDLDAFF--GVYAYnGPAQALvvKNAGKvgKVKIVCFDTTPDILQYVKEGVIQAtmgqrpym 258
Cdd:cd19997  166 NWTQSVAQKAVTGILPSLPEVDAVItqGGDGY-GAAQAF--EAAGR--PLPIIIGGNRGEFLKWWQEEYAKN-------- 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490184078 259 mGYLSVTVLYL--MNKIGVQNTLMMLpkvkvDGK-VDYVIDTGVDVVTPENLDEYLKKMEELGI 319
Cdd:cd19997  233 -GYETVSVSTDpgQGSAAFWVALDIL-----NGKdVPKEMILPVVTITEDDLDAWLAVTPDGIV 290
PBP1_LacI-like cd06285
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
21-283 2.50e-15

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


Pssm-ID: 380508 [Multi-domain]  Cd Length: 269  Bit Score: 74.57  E-value: 2.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSV-HPYWSQVEQGVKAAGKALGVDTkFFVPQKEDINAQLQMLESFIAEGVNGIAIAP-SDPTAVIPTIKKAle 98
Cdd:cd06285    1 TIGVLVSDLsNPFYAELVEGIEDAARERGYTV-LLADTGDDPERELAALDSLLSRRVDGLIITPaRDDAPDLQELAAR-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  99 mGIPVVTLDTDSPDsGRYVYIGTDNYQAGYTAgliMKELLG-GKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSEIEIVDI 177
Cdd:cd06285   78 -GVPVVLVDRRIGD-TALPSVTVDNELGGRLA---TRHLLElGHRRIAVVAGPLNASTGRDRLRGYRRALAEAGLPVPDE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 178 L-----NDEEDGARAVS--LAEA----ALNAHPDLDAfFGVYayngpaQALvvKNAG-KVGK-VKIVCFDTTPdILQYVK 244
Cdd:cd06285  153 RivpggFTIEAGREAAYrlLSRPerptAVFAANDLMA-IGVL------RAA--RDLGlRVPEdLSVVGFDDIP-LAAFLP 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 490184078 245 EGViqATMGQRPYMMGYLSV-TVLYLMNKIGVQNTLMMLP 283
Cdd:cd06285  223 PPL--TTVRQPKYEMGRRAAeLLLQLIEGGGRPPRSITLP 260
Peripla_BP_1 pfam00532
Periplasmic binding proteins and sugar binding domain of LacI family; This family includes the ...
19-230 2.97e-15

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


Pssm-ID: 395423 [Multi-domain]  Cd Length: 281  Bit Score: 74.47  E-value: 2.97e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078   19 ALTIGVIGKSV-HPYWSQVEQGVKAAGKALGVDTkFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAviPTI-KKA 96
Cdd:pfam00532   1 TLKLGALVPQLdEPFFQDLVKGITKAAKDHGFDV-FLLAVGDGEDTLTNAIDLLLASGADGIIITTPAPSG--DDItAKA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078   97 LEMGIPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGtGSLTAMNSLQRIQGFKDAIKDS--EIEI 174
Cdd:pfam00532  78 EGYGIPVIAADDAFDNPDGVPCVMPDDTQAGYESTQYLIAEGHKRPIAVMA-GPASALTARERVQGFMAALAAAgrEVKI 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 490184078  175 VDIL---NDEEDGAravSLAEAALNAHPDLDAffgVYAYNGPAQALVVKNAGKVGKVKI 230
Cdd:pfam00532 157 YHVAtgdNDIPDAA---LAANAMLVSHPTIDA---IVAMNDEAAMGAVRALLKQGRVKI 209
XylF COG4213
ABC-type xylose transport system, periplasmic component [Carbohydrate transport and metabolism] ...
33-246 9.27e-15

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


Pssm-ID: 443359 [Multi-domain]  Cd Length: 310  Bit Score: 73.63  E-value: 9.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  33 WSQVEQGVKAAGKALGVDTKFFVPQkEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDTDSPD 112
Cdd:COG4213   17 WIRDGDNFKAALKELGYEVDVQNAN-GDVATQLSQIENMITKGADVLVIAPIDGTALAAVLEKAKAAGIPVIAYDRLILN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 113 SGRYVYIGTDNYQAGYTAGLIMKELLG--GKGKVVIGTGSLTAMNSLQRIQGFKDA----IKDSEIEIV---DILNdeED 183
Cdd:COG4213   96 SDVDYYVSFDNVKVGELQGQYLVDGLPlkGKGNIELFGGSPTDNNATLFFEGAMSVlqpyIDSGKLVVVsgqWTLG--WD 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490184078 184 GARAVSLAEAALNAHP-DLDAffgVYAYN-----GPAQALvvKNAGKVGKVKIVCFDTTPDILQYVKEG 246
Cdd:COG4213  174 PETAQKRMENLLTANGnKVDA---VLAPNdglagGIIQAL--KAQGLAGKVVVTGQDAELAAVQRILAG 237
PBP1_LacI-like cd06299
ligand-binding domain of DNA-binding regulatory protein from Corynebacterium glutamicum ...
21-283 2.25e-14

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


Pssm-ID: 380522 [Multi-domain]  Cd Length: 268  Bit Score: 71.93  E-value: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSV-HPYWSQVEQGVKAAGKALGVDTKFFVPQkEDINAQLQMLESFIAEGVNGIAIAPSDptAVIPTIKKALEM 99
Cdd:cd06299    1 TIGLLVPDIrNPFFAELASGIEDEARAHGYSVILGNSD-EDPEREDESLEMLLSQRVDGIIAVPTG--ENSEGLQALIAQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTLDTDSPDSGRYVYIGTDNYQAGYTAglimKELLGGKGKVVIG--TGSLTAMNSLQRIQGFKDAIKDSEIEIvDI 177
Cdd:cd06299   78 GLPVVFVDREVEGLGGVPVVTSDNRPGAREA----VEYLVSLGHRRIGyiSGPLSTSTGRERLAAFRAALTAAGIPI-DE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 178 LNDEEDGARAVSLAEAA---LNAHPDLDAFFGVYAYNGPAQALVVKNAG-KVGK-VKIVCFDTTPdILQYVKEGViqATM 252
Cdd:cd06299  153 ELVAFGDFRQDSGAAAAhrlLSRGDPPTALIAGDSLMALGAIQALRELGlRIGDdVSLISFDDVP-WFELLSPPL--TVI 229
                        250       260       270
                 ....*....|....*....|....*....|.
gi 490184078 253 GQRPYMMGYLSVTVLYLMNKIGVQNTLMMLP 283
Cdd:cd06299  230 AQPVERIGRRAVELLLALIENGGRATSIRVP 260
PBP1_arabinose_binding cd01540
periplasmic L-arabinose-binding protein (ABP), a member of a family of pentose/hexose ...
22-211 1.48e-13

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: 70.01  E-value: 1.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  22 IGVIGKSVHPYWSQVEQ-GVKAAGKALGVDTKFfVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMG 100
Cdd:cd01540    2 IGFIVKQPDQPWFQDEWkGAKKAAKELGFEVIK-IDAKMDGEKVLSAIDNLIAQGAQGIVICTPDQKLGPAIAAKAKAAG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 101 IPVVTLD---TDSpDSGRYV-YIGTDNYQAGYTAGLIMKELLGGKGKVV---IGTGSLTaMNSL----QRIQGFKDAIKD 169
Cdd:cd01540   81 IPVIAVDdqlVDA-DPMKIVpFVGIDAYKIGEAVGEWLAKEMKKRGWDDvkeVGVLAIT-MDTLsvcvDRTDGAKDALKA 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 490184078 170 ---SEIEIVDILNDEEDGARAVSLAEAALNAHPDLDAFFgVYAYN 211
Cdd:cd01540  159 agfPEDQIFQAPYKGTDTEGAFNAANAVITAHPEVKHWL-VVGCN 202
PBP1_MalI-like cd06289
ligand-binding domain of MalI, a transcription regulator of the maltose system of Escherichia ...
21-209 2.75e-13

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


Pssm-ID: 380512 [Multi-domain]  Cd Length: 268  Bit Score: 68.75  E-value: 2.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIgksVH----PYWSQ----VEQGVKAAGKALgvdtkFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSD--PTAVI 90
Cdd:cd06289    1 TVGLI---VPdlsnPFFAEllagIEEALEEAGYLV-----FLANTGEDPERQRRFLRRMLEQGVDGLILSPAAgtTAELL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  91 PTIKKAlemGIPVVTLDTDSPDSGrYVYIGTDNYQAGYTAG--LIMkelLGGKGKVVIGtGSLTAMNSLQRIQGFKDAIK 168
Cdd:cd06289   73 RRLKAW---GIPVVLALRDVPGSD-LDYVGIDNRLGAQLATehLIA---LGHRRIAFLG-GLSDSSTRRERLAGFRAALA 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 490184078 169 DSEIEIVDILN-----DEEDGARAVslaEAALNAHPDLDAF--------FGVYA 209
Cdd:cd06289  145 EAGLPLDESLIvpgpaTREAGAEAA---RELLDAAPPPTAVvcfndlvaLGAML 195
Periplasmic_Binding_Protein_type1 cd01391
Type 1 periplasmic binding fold superfamily; Type 1 periplasmic binding fold superfamily. This ...
22-295 2.01e-12

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


Pssm-ID: 380477 [Multi-domain]  Cd Length: 280  Bit Score: 66.52  E-value: 2.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  22 IGVIGKSVH----PYWSQVEQGVKAAGKALGVDTKFFVPQKEDiNAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKAL 97
Cdd:cd01391    2 IGVVTSSLHqireQFGIQRVEAIFHTADKLGASVEIRDSCWHG-SVALEQSIEFIRDNIAGVIGPGSSSVAIVIQNLAQL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  98 EmGIPVVTLDTDSPDSGR------YVYIGTDNYQAGYTAGLIMKELlgGKGKVVIGTGSLTAMNSLqRIQGFKDAIKDSE 171
Cdd:cd01391   81 F-DIPQLALDATSQDLSDktlykyFLSVVFSDTLGARLGLDIVKRK--NWTYVAAIHGEGLNSGEL-RMAGFKELAKQEG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 172 IEIVDI-LNDEEDGARAVSLAEAALNAHPDLDAFFGVYAYNGPAQALVVKNAGKVGKVKIVCFDTTPDI--LQYVKEGVI 248
Cdd:cd01391  157 ICIVASdKADWNAGEKGFDRALRKLREGLKARVIVCANDMTARGVLSAMRRLGLVGDVSVIGSDGWADRdeVGYEVEANG 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 490184078 249 QATMGQRPYMMGylsVTVLYLMNKIGVQNTLMMLPKVKVDGKVDYVI 295
Cdd:cd01391  237 LTTIKQQKMGFG---ITAIKAMADGSQNMHEEVWFDEKGDALGRYIL 280
PBP1_ABC_xylose_binding-like cd19993
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
33-251 7.64e-12

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


Pssm-ID: 380648 [Multi-domain]  Cd Length: 287  Bit Score: 64.81  E-value: 7.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  33 WSQVEQGVKAAGKALGVDtkfFVPQKEDINAQLQM--LESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDTdS 110
Cdd:cd19993   14 WKTDEAAMKKALEKAGAK---YISADAQSSAEKQLddIESLISQGAKALIVLAQDGDAILPAVEKAAAEGIPVIAYDR-L 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 111 PDSGRYVYIGTDNYQAG-YTAGLIMKelLGGKGKVVIGTGSLTAMNSLQRIQG----FKDAIKDSEIEIV-DILNDEEDG 184
Cdd:cd19993   90 IENPIAFYISFDNVEVGrMQARGVLK--AKPEGNYVFIKGSPTDPNADFLRAGqmevLQPAIDSGKIKIVgEQYTDGWKP 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490184078 185 ARAVSLAEAALNAHP-DLDAffgVYAYN-----GPAQALvvKNAGKVGKVKIVCFDTTPDILQYVKEGVIQAT 251
Cdd:cd19993  168 ANAQKNMEQILTANNnKVDA---VVASNdgtagGAVAAL--AAQGLAGKVPVSGQDADKAALNRIALGTQTVT 235
PBP1_DegA_Like cd19976
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
21-176 1.46e-11

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


Pssm-ID: 380631 [Multi-domain]  Cd Length: 268  Bit Score: 63.81  E-value: 1.46e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSV-HPYWSQVEQGVKAAGKALGVDTkFFVPQKEDINAQLQMLESFIAEGVNGIAIAPS--DPTAVIPTIKKAl 97
Cdd:cd19976    1 TIGLIVPDIsNPFFSELVRGIEDTLNELGYNI-ILCNTYNDFEREKKYIQELKERNVDGIIIASSniSDEAIIKLLKEE- 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490184078  98 emGIPVVTLDTDSPDSGRYvYIGTDNYQAGYTAGLIMKELlgGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSEIEIVD 176
Cdd:cd19976   79 --KIPVVVLDRYIEDNDSD-SVGVDDYRGGYEATKYLIEL--GHTRIGCIVGPPSTYNEHERIEGYKNALQDHNLPIDE 152
PBP1_ChvE cd19994
periplasmic sugar binding protein ChvE that interacts with a bacterial two-component signaling ...
33-246 3.32e-11

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: 63.03  E-value: 3.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  33 WSQVEQGVKAAGKALG--VDTKFFvpqKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLD--- 107
Cdd:cd19994   14 WIKDGENLKSELEEAGytVDLQYA---DDDVATQNSQIENMINKGAKVLVIAPVDGSALGDVLEEAKDAGIPVIAYDrli 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 108 TDSPDSGRYVyiGTDNYQAGYTAGLIMKELLGGKG-----KVVIGTGSLT----------AMNSLQ-RIQGFKDAIKDSE 171
Cdd:cd19994   91 MNTDAVDYYV--TFDNEKVGELQGQYLVDKLGLKDgkgpfNIELFAGSPDdnnaqlffkgAMEVLQpYIDDGTLVVRSGQ 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 172 IEIVDILNDEEDGARAVSLAEAALNAHP----DLDAFFGvyAYNGPAQAL--VVKNAGKVGKVKIVCF--DTTPDILQYV 243
Cdd:cd19994  169 TTFEQVATPDWDTETAQARMETLLSAYYtggkKLDAVLS--PNDGIARGVieALKAAGYDTGPWPVVTgqDAEDASVKSI 246

                 ...
gi 490184078 244 KEG 246
Cdd:cd19994  247 LDG 249
PBP1_LacI-like cd06284
ligand-binding domain of an uncharacterized transcription regulator from Actinobacillus ...
30-283 5.06e-11

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


Pssm-ID: 380507 [Multi-domain]  Cd Length: 267  Bit Score: 62.17  E-value: 5.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  30 HPYWSQVEQGVKAAGKALGVDTKFF--VPQKEDINAQLQMLESFIAEGVngIAIAPSDPTAVIptikKALEMGIPVVTLD 107
Cdd:cd06284   11 NPFYSEILRGIEDAAAEAGYDVLLGdtDSDPEREDDLLDMLRSRRVDGV--ILLSGRLDAELL----SELSKRYPIVQCC 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 108 TDSPDSGRYvYIGTDNYQAGYTAgliMKELLG-GKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSEIEIVDIL-----NDE 181
Cdd:cd06284   85 EYIPDSGVP-SVSIDNEAAAYDA---TEYLISlGHRRIAHINGPLDNVYARERLEGYRRALAEAGLPVDEDLiiegdFSF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 182 EDGARAvslAEAALNAHPDLDAFFG---VYAyngpAQAL-VVKNAG-KVGK-VKIVCFDTTpDILQYVKEGViqATMGQR 255
Cdd:cd06284  161 EAGYAA---ARALLALPERPTAIFCasdELA----IGAIkALRRAGlRVPEdVSVIGFDDI-EFAEMFSPSL--TTIRQP 230
                        250       260
                 ....*....|....*....|....*....
gi 490184078 256 PYMMGYLSVTVLY-LMNKIGVQNTLMMLP 283
Cdd:cd06284  231 RYEIGETAAELLLeKIEGEGVPPEHIILP 259
PBP1_LacI-like cd06278
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
55-205 5.69e-11

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


Pssm-ID: 380501 [Multi-domain]  Cd Length: 266  Bit Score: 61.78  E-value: 5.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  55 VPQKEDINAQLQMLESFIAEGVngIAIAPSDPTAVIptiKKALEMGIPVVTLDTDSPDSGRYvYIGTDNYQAGYTAGlim 134
Cdd:cd06278   37 VDDEDDVDDALRQLLQYRVDGV--IVTSATLSSELA---EECARRGIPVVLFNRVVEDPGVD-SVSCDNRAGGRLAA--- 107
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490184078 135 kELL--GGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSEIEIVDIL---NDEEDGARAvslAEAALNAHPDLDAFF 205
Cdd:cd06278  108 -DLLlaAGHRRIAFLGGPEGTSTSRERERGFRAALAELGLPPPAVEagdYSYEGGYEA---ARRLLAAPDRPDAIF 179
PBP1_LacI-like cd06290
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
21-283 5.69e-11

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


Pssm-ID: 380513 [Multi-domain]  Cd Length: 267  Bit Score: 61.86  E-value: 5.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSV-HPYWSQVEQGVKAAGKALGVdTKFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTaviPTIKKALEM 99
Cdd:cd06290    1 TIGVLVPDIdSPFYSEILNGIEEVLAESGY-TLIVSTSHWNADRELEILRLLLARKVDGIIVVGGFGD---EELLKLLAE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTLDTDSPDsGRYVYIGTDNYQAGYTAG--LIMKellgGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSEIEIVDI 177
Cdd:cd06290   77 GIPVVLVDRELEG-LNLPVVNVDNEQGGYNATnhLIDL----GHRRIVHISGPEDHPDAQERYAGYRRALEDAGLEVDPR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 178 LN-----DEEDGARAVslaEAALNAHPDLDAFFGV---YAYnGPAQALvvKNAG-KV-GKVKIVCFDTTPdILQYVKEGV 247
Cdd:cd06290  152 LIvegdfTEESGYEAM---KKLLKRGGPFTAIFAAndlMAL-GAMKAL--REAGiRVpDDVSVIGFDDLP-FSKYTTPPL 224
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 490184078 248 iqATMGQRPYMMGYLSV-TVLYLMNKIGVQNTLMMLP 283
Cdd:cd06290  225 --TTVRQPLYEMGKTAAeILLELIEGKGRPPRRIILP 259
PBP1_LacI-like cd06293
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
21-205 1.23e-10

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


Pssm-ID: 380516 [Multi-domain]  Cd Length: 270  Bit Score: 61.13  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSV-HPYWSQVEQGVKAAGKALGVdTKFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPtaVIPTIKKALEM 99
Cdd:cd06293    1 TIGLVVPDVsNPFFAEVARGVEDAARERGY-AVVLCNSGRDPERERRYLEMLESQRVRGLIVTPSDD--DLSHLARLRAR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTLDTDSP-DSGRYVYIgtDNYQAGYtagLIMKELLG-GKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSEIEIVDI 177
Cdd:cd06293   78 GTAVVLLDRPAPgPAGCSVSV--DDVQGGA---LAVDHLLElGHRRIAFVSGPLRTRQVAERLAGARAAVAEAGLDPDEV 152
                        170       180       190
                 ....*....|....*....|....*....|..
gi 490184078 178 LNDEEDGARAVSLAEAA----LNAHPDLDAFF 205
Cdd:cd06293  153 VRELSAPDANAELGRAAaaqlLAMPPRPTAVF 184
PBP1_RegR_EndR_KdgR-like cd06283
ligand-binding domain of DNA transcription repressor RegR and other putative regulators such ...
21-273 1.36e-10

ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR; Ligand-binding domain of DNA transcription repressor RegR and other putative regulators such as KdgR and EndR, all of which are members of the LacI-GalR family of bacterial transcription regulators. RegR regulates bacterial competence and the expression of virulence factors, including hyaluronidase. 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: 380506 [Multi-domain]  Cd Length: 266  Bit Score: 60.64  E-value: 1.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIgksV----HPYWSQVEQGVKAAGKALGVDTKFFV----PQKEdinaqLQMLESFIAEGVNGIAIAPSDPTAviPT 92
Cdd:cd06283    1 LIGVI---VaditNPFSSLLLKGIEDVCREAGYQLLICNsnndPEKE-----RDYIESLLSQRVDGLILQPTGNNN--DA 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  93 IKKALEMGIPVVTLDTDSPDSgRYVYIGTDNYQAGYTAGLIMKEllggKG--KVVIGTGSLTAMNS-LQRIQGFKDAIKD 169
Cdd:cd06283   71 YLELAQKGLPVVLVDRQIEPL-NWDTVVTDNYDATYEATEHLKE----QGyeRIVFVTEPIKGISTrRERLQGFLDALAR 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 170 SEIEI-VDILNDEEDGARAVSLAEAALNAHPDLDAFFGVyayNGPAQALVVKNAGKVG-----KVKIVCFDtTPDILQYV 243
Cdd:cd06283  146 YNIEGdVYVIEIEDTEDLQQALAAFLSQHDGGKTAIFAA---NGVVLLRVLRALKALGiripdDVGLCGFD-DWDWADLI 221
                        250       260       270
                 ....*....|....*....|....*....|
gi 490184078 244 KEGViqATMGQRPYMMGYLSVTVlyLMNKI 273
Cdd:cd06283  222 GPGI--TTIRQPTYEIGKAAAEI--LLERI 247
PBP1_GGBP cd01539
periplasmic glucose/galactose-binding protein (GGBP) involved in chemotaxis towards, and ...
31-260 1.82e-10

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: 60.68  E-value: 1.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  31 PYWSQVEQGVKAAGKALGVDTKFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDTDS 110
Cdd:cd01539   13 TFISSVRKALEKAAKAGGKIELEIYDAQNDQSTQNDQIDTMIAKGVDLLVVNLVDRTAAQTIIDKAKAANIPVIFFNREP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 111 PDS-----GRYVYIGTDNYQAGYTAGLIMKELLG--------GKGKV--VIGTGSLTAMNSLQRIQGFKDAIKDSEI--E 173
Cdd:cd01539   93 SREdlksyDKAYYVGTDAEESGIMQGEIIADYWKanpeidknGDGKIqyVMLKGEPGHQDAIARTKYSVKTLNDAGIktE 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 174 IVDILNDEEDGARAVSLAEAALNAHPD-LDAffgVYAYN-----GPAQALV---VKNAGKVGKVKIVCFDTTPDILQYVK 244
Cdd:cd01539  173 QLAEDTANWDRAQAKDKMDAWLSKYGDkIEL---VIANNddmalGAIEALKaagYNTGDGDKYIPVFGVDATPEALEAIK 249
                        250
                 ....*....|....*.
gi 490184078 245 EGVIQATMGQRPYMMG 260
Cdd:cd01539  250 EGKMLGTVLNDAKAQA 265
PBP1_GalS-like cd06270
ligand binding domain of DNA transcription iso-repressor GalS, which is one of two regulatory ...
21-211 4.13e-10

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


Pssm-ID: 380494 [Multi-domain]  Cd Length: 266  Bit Score: 59.46  E-value: 4.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSVH-PYWS----QVEQGVKAAGKALGVDTKFFVPQKEdinaqLQMLESFIAEGVNGIAIAPSDPTAVIptIKK 95
Cdd:cd06270    1 TIGLVVPDLSgPFFGsllkGAERVARAHGKQLLITSGHHDAEEE-----REAIEFLLDRRCDAIILHSRALSDEE--LIL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  96 ALEMGIPVVTLDTDSP-DSGRYVYIgtDNYQAGYTAgliMKELLG-GKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSEIE 173
Cdd:cd06270   74 IAEKIPPLVVINRYIPgLADRCVWL--DNEQGGRLA---AEHLLDlGHRRIACITGPLDIPDARERLAGYRDALAEAGIP 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 490184078 174 IVDIL-----NDEEDGARAvslAEAALNAHPDLDAFFgvyAYN 211
Cdd:cd06270  149 LDPSLiiegdFTIEGGYAA---AKQLLARGLPFTALF---AYN 185
PBP1_GntR cd01575
ligand-binding domain of DNA transcription repressor GntR specific for gluconate, a member of ...
66-205 1.07e-09

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


Pssm-ID: 380489 [Multi-domain]  Cd Length: 269  Bit Score: 58.28  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  66 QMLESFIAEGVNGIAIAPSDPTAviPTIKKALEMGIPVV-TLDTDSPDSGRYVyiGTDNYQAGYTAGlimkELLGGKGK- 143
Cdd:cd01575   46 ELIRALLSRRPAGLILTGTEHTP--ATRKLLRAAGIPVVeTWDLPDDPIDMAV--GFSNFAAGRAMA----RHLIERGYr 117
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490184078 144 --VVIGTGSLTAMNSLQRIQGFKDAIKDSEIEIVDILNDE-----EDGARAVslaEAALNAHPDLDAFF 205
Cdd:cd01575  118 riAFVGARLDGDSRARQRLEGFRDALAEAGLPLPLVLLVElpssfALGREAL---AELLARHPDLDAIF 183
PBP1_ABC_xylose_binding-like cd19995
periplasmic xylose-like sugar-binding component of the ABC-type transport systems; Periplasmic ...
64-306 1.23e-09

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: 58.07  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  64 QLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELLGGKGK 143
Cdd:cd19995   47 QQQQAEAAITQGAKVLVVDPVDSNAAAGIVAKAAQAGVPVIAYDRLILGGPADYYVSFDNVAVGEAQAQSLVDHLKAIGK 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 144 ----VVIGTGSLTAMNSLQRIQG----FKDAIKDSEIEIV---DILNDEEDGARavSLAEAALNAHPD-LDAFFGvyAYN 211
Cdd:cd19995  127 kgvnIVMINGSPTDNNAGLFKKGahevLDPLGDSGELKLVceyDTPDWDPANAQ--TAMEQALTKLGNnIDGVLS--AND 202
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 212 GPAQALV--VKNAGKVGKVKIVCFDTTPDILQYVKEGVIQATMGQRPYMMGYLSVTV-LYLMNKIGVqntlmmlPKVKVD 288
Cdd:cd19995  203 GLAGGAIaaLKAQGLAGKVPVTGQDATVAGLQRILAGDQYMTVYKPIKKEAAAAAKVaVALLKGETP-------PSDLVT 275
                        250
                 ....*....|....*...
gi 490184078 289 GKVDYVIDTGVDVVTPEN 306
Cdd:cd19995  276 GTVTNGGDKVPAVLLPPV 293
PBP1_ABC_sugar_binding-like cd06315
periplasmic sugar-binding domain of uncharacterized ABC-type transport systems; Periplasmic ...
36-177 1.48e-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: 380538  Cd Length: 278  Bit Score: 57.74  E-value: 1.48e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  36 VEQGVKAAGKALGVDTKFFvPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDTDS----- 110
Cdd:cd06315   18 VGRGVKEAAAALGWKVDVL-DGGGTVTGRLAALNQALALKPDGIILGGDDAVELQEPLKKAVKAGIPVVGWHAAAspgpi 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490184078 111 PDSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGTGSLTAMnSLQRIQGFKDAIKDSE----IEIVDI 177
Cdd:cd06315   97 PELGLFTNITTDPREVAETAAALVIAQSGGKAGVVIFTDSRYAI-ATAKANAMKKAIEACSgckvLEYVDI 166
PBP1_CatR-like cd06296
ligand-binding domain of a LacI-like transcriptional regulator, CatR which is involved in ...
31-210 2.55e-09

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


Pssm-ID: 380519 [Multi-domain]  Cd Length: 270  Bit Score: 56.90  E-value: 2.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  31 PYWSQVEQGVKAAGKALGVDTKFFVPQKEDINAQlQMLESFIAEGVNGIAIAPSDPTAviPTIKKALEMGIPVVTLDTDS 110
Cdd:cd06296   12 PYALEVLRGVERAAAAAGLDLVVTATRAGRAPVD-DWVRRAVARGSAGVVLVTSDPTS--RQLRLLRSAGIPFVLIDPVG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 111 PDSGRYVYIGTDNYQAGYTAGlimkELLGGKGKVVIG--TGSLTAMNSLQRIQGFKDAIKDSEIEIVDILNDE-----ED 183
Cdd:cd06296   89 EPDPDLPSVGATNWAGGRLAT----EHLLDLGHRRIAviTGPPRSVSGRARLAGYRAALAEAGIAVDPDLVREgdftyEA 164
                        170       180       190
                 ....*....|....*....|....*....|...
gi 490184078 184 GARAV----SLAE--AALNAHPDLDAfFGVYAY 210
Cdd:cd06296  165 GYRAArellELPDppTAVFAGNDEQA-LGVYRA 196
PBP1_LacI-like cd06279
ligand-binding domain of an uncharacterized transcription regulator from Corynebacterium ...
91-205 8.95e-09

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


Pssm-ID: 380502 [Multi-domain]  Cd Length: 284  Bit Score: 55.68  E-value: 8.95e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  91 PTIKKALEMGIPVVTLDTDSPDSgrYVYIGTDNYQAGYTAGLIMKELlgGKGKVVIGTGSLTAMNS-------------- 156
Cdd:cd06279   70 PAVAALRRRGLPLVVVDGPAPPG--IPSVGIDDRAAARAAARHLLDL--GHRRIAILSLRLDRGRErgpvsaerlaaatn 145
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 490184078 157 ---LQRIQGFKDAIKDSEIEIVDIL------NDEEDGARAvslAEAALNAHPDLDAFF 205
Cdd:cd06279  146 svaRERLAGYRDALEEAGLDLDDVPvveapgNTEEAGRAA---ARALLALDPRPTAIL 200
PBP1_ABC_xylose_binding cd19991
D-xylose binding periplasmic protein; Periplasmic xylose-binding component of the ABC-type ...
59-225 1.44e-08

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: 54.93  E-value: 1.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  59 EDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDTDSPDSGRYVYIGTDNYQAGYT-AGLIMKEl 137
Cdd:cd19991   39 GDDEKQISQAEELIEQGVDVLVVVPNNGEALAPIVKEAKKAGVPVLAYDRLILNADVDLYVSFDNEKVGELqAEALVKA- 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 138 lGGKGKVVIGTGSLTAMNSLQRIQGFKDAIK---DS-EIEIV-DILNDEEDGARAVSLAEAALNAH-PDLDAffgVYAYN 211
Cdd:cd19991  118 -KPKGNYVLLGGSPTDNNAKLFREGQMKVLQpliDSgDIKVVgDQWVDDWDPEEALKIMENALTANnNKIDA---VIASN 193
                        170       180
                 ....*....|....*....|
gi 490184078 212 -----GPAQALVVKN-AGKV 225
Cdd:cd19991  194 dgtagGAIQALAEQGlAGKV 213
PBP1_MalR-like cd06294
ligand-binding domain of maltose transcription regulator MalR which is a member of the ...
91-291 2.47e-08

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


Pssm-ID: 380517 [Multi-domain]  Cd Length: 269  Bit Score: 54.13  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  91 PTIKKALEMGIPVVTLDTdSPDSGRYVYIGTDNYQAGYTAglimKELLGGKGKVVIG--TGSLTAMNSLQRIQGFKDAIK 168
Cdd:cd06294   74 PLIEYLKEEGFPFVVIGK-PLDDNDVLYVDNDNVQAGYEA----TEYLIDKGHKRIAfiGGDKNLVVSIDRLQGYKQALK 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 169 DSEIEIVD--ILNDEEDGARAVSLAEAALNAHPDLDAF--------FGVYAYngpAQALVVKNAGKVGkvkIVCFDTTPd 238
Cdd:cd06294  149 EAGLPLDDdyILLLDFSEEDGYDALQELLSKPPPPTAIvatddllaLGVLRY---LQELGLRVPEDVS---IISFNNSP- 221
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 490184078 239 ILQYVKEGviQATMGQRPYMMGYLSVTVlyLMNKIgvQNTLMMLPKVKVDGKV 291
Cdd:cd06294  222 LAELASPP--LTSVDINPYELGREAAKL--LINLL--EGPESLPKNVIVPHEL 268
PBP1_ABC_xylose_binding-like cd01538
periplasmic xylose-like sugar-binding component of the ABC-type transport systems that belong ...
31-230 3.81e-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: 53.58  E-value: 3.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  31 PYWSQVEQGVKAAGKALGVDTKFFVPQkEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEMGIPVVTLDTDS 110
Cdd:cd01538   12 ARWQTDRDIMVEQLEEKGAKVLVQSAD-GDKAKQASQIENLLTQGADVLVLAPVDGQALSPVVAEAKAEGIKVIAYDRLI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 111 PDSGRYVYIGTDNYQAGYTAGLIMKELLGGKGKVVIGtGSLTAMNSLQRIQG----FKDAIKDSEIEIV-DILNDEEDGA 185
Cdd:cd01538   91 LNADVDYYISFDNEKVGELQAQALLDAKPEGNYVLIG-GSPTDNNAKLFRDGqmkvLQPAIDSGKIKVVgDQWVDDWLPA 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 490184078 186 RAVSLAEAALNAH-PDLDAffgVYAYN-----GPAQALvvKNAGKVGKVKI 230
Cdd:cd01538  170 NAQQIMENALTANgNNVDA---VVASNdgtagGAIAAL--KAQGLSGGVPV 215
PBP1_CcpA-like cd19975
ligand-binding domain of putative DNA transcription regulators highly similar to that of the ...
98-268 3.89e-08

ligand-binding domain of putative DNA transcription regulators highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation; This group includes the ligand-binding domain of uncharacterized DNA transcription repressors highly similar to that of the catabolite control protein A (CcpA), which functions as the major transcriptional regulator of carbon catabolite repression/regulation (CCR), a process in which enzymes necessary for the metabolism of alternative sugars are inhibited in the presence of glucose. In gram-positive bacteria, CCR is controlled by HPr, a phosphoenolpyruvate:sugar phsophotrasnferase system (PTS) and a transcriptional regulator CcpA. Moreover, CcpA can regulate sporulation and antibiotic resistance as well as play a role in virulence development of certain pathogens such as the group A streptococcus. The ligand binding domain of CcpA is a member of the LacI-GalR family of bacterial transcription regulators.


Pssm-ID: 380630 [Multi-domain]  Cd Length: 269  Bit Score: 53.71  E-value: 3.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  98 EMGIPVVTLDTDSPDSGRYvYIGTDNYQAGYTAgliMKELLG-GKGKVVIGTGSLTAMNS-LQRIQGFKDAIKDSEIEIV 175
Cdd:cd19975   76 NMNIPVVLVSTESEDPDIP-SVKIDDYQAAYDA---TNYLIKkGHRKIAMISGPLDDPNAgYPRYEGYKKALKDAGLPIK 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 176 DILNDE-----EDGARAVslaEAALNAHPDLDAFFgvyAYN-----GPAQALVVKNAGKVGKVKIVCFDTTPdILQYVKE 245
Cdd:cd19975  152 ENLIVEgdfsfKSGYQAM---KRLLKNKKLPTAVF---AASdemalGVISAAYDHGIRVPEDISVIGFDNTE-IAEMSIP 224
                        170       180
                 ....*....|....*....|...
gi 490184078 246 GViqATMGQRPYMMGYLSVTVLY 268
Cdd:cd19975  225 PL--TTVSQPFYEMGKKAVELLL 245
PBP1_LacI-like cd06282
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
21-184 4.72e-08

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: 380505 [Multi-domain]  Cd Length: 267  Bit Score: 53.44  E-value: 4.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSV-HPYWSQVEQGVKAAGKALGVdtKFFVPQKE-DINAQLQMLESFIAEGVNGIAIAPSDPTAViPTIKKALE 98
Cdd:cd06282    1 TIGVLIPSLnNPVFAEAAQGIQRAARAAGY--SLLIATTDyDPARELDAVETLLEQRVDGLILTVGDAQGS-EALELLEE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  99 MGIPVVTLDTDSPDSGR-YVYIgtDNYQAGYTAGlimkELLGGKGKVVIG--TGSLTAMN-SLQRIQGFKDAIKDSE--- 171
Cdd:cd06282   78 EGVPYVLLFNQTENSSHpFVSV--DNRLASYDVA----EYLIALGHRRIAmvAGDFSASDrARLRYQGYRDALKEAGlkp 151
                        170
                 ....*....|....*.
gi 490184078 172 ---IEIVDILNDEEDG 184
Cdd:cd06282  152 ipiVEVDFPTNGLEEA 167
PBP1_FruR cd06274
ligand binding domain of DNA transcription repressor specific for fructose (FruR) and its ...
64-205 5.25e-08

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


Pssm-ID: 380498 [Multi-domain]  Cd Length: 264  Bit Score: 52.98  E-value: 5.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  64 QLQMLESFIAEGVNGIAIAPS-DPTAVIPTIKKAlemGIPVVTLDTDSPDSgRYVYIGTDNYQAGYTagLIMKELLGGKG 142
Cdd:cd06274   44 ERRLVENLIARQVDGLIVAPStPPDDIYYLCQAA---GLPVVFLDRPFSGS-DAPSVVSDNRAGARA--LTEKLLAAGPG 117
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490184078 143 KVV-IGtGSLTAMNSLQRIQGFKDAIKDSEIEIVD--ILNDEEDGARAVSLAEAALNAHPDL-DAFF 205
Cdd:cd06274  118 EIYfLG-GRPELPSTAERIRGFRAALAEAGITEGDdwILAEGYDRESGYQLMAELLARLGGLpQALF 183
PBP1_PurR cd06275
ligand-binding domain of purine repressor, PurR, which functions as the master regulatory ...
21-205 6.52e-07

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


Pssm-ID: 380499 [Multi-domain]  Cd Length: 269  Bit Score: 49.95  E-value: 6.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIG-VIGKSVHPYWSQVEQGVKAAGKALGVdTKFFVPQKEDINAQLQMLESFIAEGVNGIAIAPSDPTAVIPTIKKALEm 99
Cdd:cd06275    1 TIGlLVTSSENPFFAEVVRGVEDACFRAGY-SLILCNSDNDPEKQRAYLDMLAEKRVDGLLLMCSEMTDDDAELLAALR- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 100 GIPVVTLDTDSPDSGRYVyIGTDNYQAGYTAGlimKELLgGKGKVVIG--TGSLTAMNSLQRIQGFKDAIKDSEIE---- 173
Cdd:cd06275   79 SIPVVVLDREIAGDNADA-VLDDSFQGGYLAT---RHLI-ELGHRRIGciTGPLEHSVSRERLAGFRRALAEAGIEvpps 153
                        170       180       190
                 ....*....|....*....|....*....|...
gi 490184078 174 -IVDILNDEEDGARAvslAEAALNAHPDLDAFF 205
Cdd:cd06275  154 wIVEGDFEPEGGYEA---MQRLLSQPPRPTAVF 183
PBP1_LacI-like cd19974
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
21-237 6.93e-07

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


Pssm-ID: 380629 [Multi-domain]  Cd Length: 270  Bit Score: 49.86  E-value: 6.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSVHP----YWSQVEQGVKAAGKALGVDTKFFVPQKEDINaQLQMLESFIAEGVNGIAIApsdptAVIPT--IK 94
Cdd:cd19974    1 NIAVLIPERFFgdnsFYGKIYQGIEKELSELGYNLVLEIISDEDEE-ELNLPSIISEEKVDGIIIL-----GEISKeyLE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  95 KALEMGIPVVTLDTDSPDsGRYVYIGTDNYQAGYTAgliMKELLgGKGKVVIG-TGSLTAMNSLQ-RIQGFKDAIKDSEI 172
Cdd:cd19974   75 KLKELGIPVVLVDHYDEE-LNADSVLSDNYYGAYKL---TSYLI-EKGHKKIGfVGDINYTSSFMdRYLGYRKALLEAGL 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490184078 173 EIVD---ILNDEEDGARAVSLAEAALNAH-PdlDAFFGV---YAYNgpaqalVVKNAGKVGK-----VKIVCFDTTP 237
Cdd:cd19974  150 PPEKeewLLEDRDDGYGLTEEIELPLKLMlP--TAFVCAndsIAIQ------LIKALKEKGYrvpedISVVGFDNIE 218
PBP1_sucrose_transcription_regulator cd06288
ligand-binding domain of DNA-binding regulatory proteins specific to sucrose that are members ...
58-267 1.11e-06

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


Pssm-ID: 380511 [Multi-domain]  Cd Length: 268  Bit Score: 49.08  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  58 KEDINAQLQMLESFiaeGVNGIAIAPSDPTAVIPTIKKAlemGIPVVTLDTDSPDSgRYVYIGTDNYQAGYTAGlimkEL 137
Cdd:cd06288   42 PELEAEAIRELLSR---RVDGIIYASMHHREVTLPPELT---DIPLVLLNCFDDDP-SLPSVVPDDEQGGYLAT----RH 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078 138 LGGKG--KVVIGTGSLTAMNSLQRIQGFKDAIKDSEIEIVDIL-----NDEEDGARAvslAEAALNAHPDLDAFF----- 205
Cdd:cd06288  111 LIEAGhrRIAFIGGPEDSLATRLRLAGYRAALAEAGIPYDPSLvvhgdWGRESGYEA---AKRLLSAPDRPTAIFcgndr 187
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490184078 206 ---GVYAYngpAQALvvknaG-KVGK-VKIVCFDTTpDILQYVKEGViqATMgQRPY-MMGYLSVTVL 267
Cdd:cd06288  188 mamGVYQA---AAEL-----GlRVPEdLSVVGFDNQ-ELAAYLRPPL--TTV-ALPYyEMGRRAAELL 243
PBP1_AraR cd01541
ligand-binding domain of DNA transcription repressor specific for arabinose (AraR) which is a ...
21-176 1.56e-06

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


Pssm-ID: 380483 [Multi-domain]  Cd Length: 274  Bit Score: 48.71  E-value: 1.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSVHPY-WSQVEQGVKAAGKALGVDTKFFVPQkEDINAQLQMLESFIAEGVNGIAIAPS---DPTAVIPTIKKA 96
Cdd:cd01541    1 TIGVITTYIDDYiFPSIIQGIESVLSENGYSLLLALTN-NDVEKEREILESLLDQNVDGLIIEPTksaLPNPNLDLYEEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  97 LEMGIPVVTLDTdSPDSGRYVYIGTDNYQAGYTAGlimKELLgGKGKVVIgtGSLTAMNSLQ---RIQGFKDAIKDSEIE 173
Cdd:cd01541   80 QKKGIPVVFINS-YYPELDAPSVSLDDEKGGYLAT---KHLI-DLGHRRI--AGIFKSDDLQgveRYQGFIKALREAGLP 152

                 ...
gi 490184078 174 IVD 176
Cdd:cd01541  153 IDD 155
PBP1_ABC_unchar_transporter cd06325
type 1 periplasmic ligand-binding domain of uncharacterized ABC-type transport systems ...
21-141 3.86e-06

type 1 periplasmic ligand-binding domain of uncharacterized ABC-type transport systems predicted to be involved in uptake of amino acids, peptides, or inorganic ions; This group includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type transport systems that are predicted to be involved in the uptake of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); its ligand specificity has not been determined experimentally.


Pssm-ID: 380548  Cd Length: 282  Bit Score: 47.50  E-value: 3.86e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVIGKSVHPYWSQVEQGVKAAGKALGVDTKFF-VPQKEDINaqlQMLESFIAEGVNGIaIAPSDPTAV--IPTI-KKA 96
Cdd:cd06325  133 RVGVLYNPGEPNSVAQLEELEAAAKKLGLELVEVpVSSPADIE---QAFASLAGKVADAL-YVPTDNTVAsaRPRIaALA 208
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 490184078  97 LEMGIPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELLGGK 141
Cdd:cd06325  209 LKARIPVIYSDREFVEAGALMSYGPDYYDLGRQAARYVDRILKGA 253
PBP1_repressor_sugar_binding-like cd01537
Ligand-binding domain of the LacI-GalR family of transcription regulators and the ...
22-183 8.37e-06

Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems; Ligand-binding domain of the LacI-GalR family of transcription regulators and the sugar-binding domain of ABC-type transport systems, all of which contain the type 1 periplasmic binding protein-like fold. Their specific ligands include 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 general the sugar binding domain in this family binds a sugar, which in turn changes the DNA binding activity of the repressor domain. The core structure of the periplasmic binding proteins is classified into two types and they differ in number and order of beta strands in each domain: type 1, which has six beta strands, and type 2, which has five beta strands. These two distinct structural arrangements may have originated from a common ancestor.


Pssm-ID: 380479 [Multi-domain]  Cd Length: 265  Bit Score: 46.47  E-value: 8.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  22 IGV-IGKSVHPYWSQVEQGVKAAGKALGVDTKFFVPQK--EDINAQLQMLesfIAEGVNGIAIAPSDPTAVIpTIKKALE 98
Cdd:cd01537    2 IGVtIYSYDDNFMSVIRKAIEQDAKQPGVQLLMNDSQNdqEKQNDQIDVL---LAKRVKGLAINLVDPAAAG-VAEKARG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  99 MGIPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELlgGKGKVVIGTGSLTAMNSLQRIQGFKDAIKDSEIEIVDIL 178
Cdd:cd01537   78 QNVPVVFFDKEPSRYDKAYYVITDSKEGGIIQGDLLAKH--GHIQIVLLKGPLGHPDAEARLAGVIKELNDKGIKTEQLQ 155

                 ....*
gi 490184078 179 NDEED 183
Cdd:cd01537  156 LDTGD 160
PBP1_LacI-like cd06273
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
21-200 5.27e-05

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


Pssm-ID: 380497 [Multi-domain]  Cd Length: 268  Bit Score: 44.04  E-value: 5.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVI---------GKSVHpywsQVEQGVKAAGKALGVDTKFFVPQKEdinaqLQMLESFIAEGVNGIAIAPSD-PTAVI 90
Cdd:cd06273    1 TIGAIvptldnaifARAIQ----ALQQTLAEAGYTLLLATSEYDPARE-----LEQVRALIERGVDGLILVGSDhDPELF 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  91 PTIKKAlemGIPVVTLDTDSPDSgRYVYIGTDNYQAGYtagLIMKELLG-GKGKVVIGTGSlTAMN--SLQRIQGFKDAI 167
Cdd:cd06273   72 ELLEQR---QVPYVLTWSYDEDS-PHPSIGFDNRAAAA---RAAQHLLDlGHRRIAVISGP-TAGNdrARARLAGIRDAL 143
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 490184078 168 KDSEIEIVDILNDE-----EDGARAvslAEAALNAHPD 200
Cdd:cd06273  144 AERGLELPEERVVEapysiEEGREA---LRRLLARPPR 178
PBP1_RafR-like cd20009
Ligand-binding domain of DNA transcription repressor specific for raffinose (RafR) and similar ...
97-205 1.94e-04

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


Pssm-ID: 380664 [Multi-domain]  Cd Length: 266  Bit Score: 42.14  E-value: 1.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  97 LEMGIPVVT-----LDTDSPdsgryvYIGTDNYQAGY--TAGLIMKellgGKGKVVIGTGSLTAMNSLQRIQGFKDAIKD 169
Cdd:cd20009   77 LERGFPFVThgrteLSTPHA------YFDFDNEAFAYeaVRRLAAR----GRRRIALVAPPRELTYAQHRLRGFRRALAE 146
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490184078 170 S--EIEIVDILNDEEDGARAVSLAEAALNAHPDLDAFF 205
Cdd:cd20009  147 AglEVEPLLIVTLDSSAEAIRAAARRLLRQPPRPDGII 184
COG2984 COG2984
ABC-type uncharacterized transport system, periplasmic component [General function prediction ...
21-141 2.41e-04

ABC-type uncharacterized transport system, periplasmic component [General function prediction only];


Pssm-ID: 442223  Cd Length: 284  Bit Score: 42.20  E-value: 2.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  21 TIGVI-GKSVHPYWSQVEQgVKAAGKALGVDTKFF-VPQKEDINAQLQMLesfiAEGVNGIaIAPSDPTAV--IPTI-KK 95
Cdd:COG2984  134 RIGVLyNPSEANSVAQVEE-LKKAAKKLGLELVEAtVTSSNEIQQALQSL----AGKVDAI-YVPTDNTVVsaLEAIaKV 207
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 490184078  96 ALEMGIPVVTLDTDSPDSGRYVYIGTDNYQAGYTAGLIMKELLGGK 141
Cdd:COG2984  208 AARAKIPVFGGDDSSVKAGALAGYGIDYYELGRQAAEMALRILKGE 253
PBP1_TreR-like cd01542
ligand-binding domain of DNA transcription repressor specific for trehalose (TreR) which is a ...
60-178 2.92e-04

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


Pssm-ID: 380484 [Multi-domain]  Cd Length: 259  Bit Score: 41.71  E-value: 2.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  60 DINAQLQMLESFIAEGVNGIAIAPsdpTAVIPTIKKALE-MGIPVVTLDTDSPDsgrYVYIGTDNYQAGYTAGLIMKELl 138
Cdd:cd01542   40 DEEREIEYLETLARQKVDGIILFA---TEITDEHRKALKkLKIPVVVLGQEHEG---FSCVYHDDYGAGKLLGEYLLKK- 112
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 490184078 139 GGKGKVVIG-------TGsltamnsLQRIQGFKDAIKDSEIEIVDIL 178
Cdd:cd01542  113 GHKNIAYIGvdeediaVG-------VARKQGYLDALKEHGIDEVEIV 152
PBP1_LacI-like cd06281
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
59-166 5.00e-04

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: 380504 [Multi-domain]  Cd Length: 270  Bit Score: 41.07  E-value: 5.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  59 EDINAQLQMLESFIAEGVNGIAIAPSDPTAviPTIKKALE-MGIPVVTLDTDSPDSGRYVyiGTDNYQAGYTAgliMKEL 137
Cdd:cd06281   39 NDEERELELLSLFQRRRVDGLILTPGDEDD--PELAAALArLDIPVVLIDRDLPGDIDSV--LVDHRSGVRQA---TEYL 111
                         90       100       110
                 ....*....|....*....|....*....|
gi 490184078 138 LG-GKGKVVIGTGSLTAMNSLQRIQGFKDA 166
Cdd:cd06281  112 LSlGHRRIALLTGGPDIRPGRERIAGFKAA 141
PBP1_LacI-like cd06287
ligand-binding domain of uncharacterized DNA-binding regulatory proteins that are members of ...
85-203 9.10e-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: 37.02  E-value: 9.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490184078  85 DPTAVIPTIKKALEMGIPVVTL------DTDSPdsgrYVYIgtdnyQAGYTAgLIMKELLGGKGKVVIG--TGSLTAMNS 156
Cdd:cd06287   64 EPTVEDPILARLRQRGVPVVSIgrapgtDEPVP----YVDL-----QSAATA-RLLLEHLHGAGARQVAllTGSSRRNSS 133
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 490184078 157 LQRIQGFKDAIKDSEIEIVDILNDEEDGARA-VSLAEAALNAHPDLDA 203
Cdd:cd06287  134 LESEAAYLRFAQEYGTTPVVYKVPESEGERAgYEAAAALLAAHPDIDA 181
 
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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